60S acidic ribosomal protein P1-B RLA3_CANAL CaRP1B Q9HFQ6 RLA3_CANAL 41688727 Candida albicans (Yeast) 108 MSTEASVSYAALILADAEQEITSEKLLAITKAAGANVDQVWADVFAKAVEGKNLKELLFSFAAAAPASGAAAGSASGAAAGGEAAAEEAAEEEAAEESDDDMGFGLFD Disordered 1 108 MSTEASVSYAALILADAEQEITSEKLLAITKAAGANVDQVWADVFAKAVEGKNLKELLFSFAAAAPASGAAAGSASGAAAGGEAAAEEAAEEEAAEESDDDMGFGLFD Native Relationship to function unknown Molecular assembly Protein-protein binding Paper 15182941 Abramczyk D, Tchorzewski M, Krokowski D, Boguszewska A, Grankowski N 2004 Biochim Biophys Acta 1672 3 214-23 60S acidic ribosomal protein P2-beta RLA4_YEAST L45 L12EIA YPA1 YL44C YP2beta P2B P02400 RLA4_YEAST 133071 Saccharomyces cerevisiae (Baker's yeast) 110 MKYLAAYLLLVQGGNAAPSAADIKAVVESVGAEVDEARINELLSSLEGKGSLEEIIAEGQKKFATVPTGGASSAAAGAAGAAAGGDAAEEEKEEEAKEESDDDMGFGLFD Disordered - Molten Globule 1 110 MKYLAAYLLLVQGGNAAPSAADIKAVVESVGAEVDEARINELLSSLEGKGSLEEIIAEGQKKFATVPTGGASSAAAGAAGAAAGGDAAEEEKEEEAKEESDDDMGFGLFD Native Function arises via a molten globule to order transition Molecular recognition effectors Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV Nuclear magnetic resonance (NMR) Analytical ultracentrifugation Hydrogen-deuterium exchange Stability at thermal extremes Paper 9236009 Zurdo J, Sanz JM, Gonzalez C, Rico M, Ballesta JP 1997 Biochemistry 36 31 9625-35 10913306 Zurdo J, Gonzalez C, Sanz JM, Rico M, Remacha M, Ballesta JP 2000 Biochemistry 39 30 8935-43 Early E2A DNA-binding protein DNB2_ADE05 Adenovirus ssDNA binding protein P03265 DNB2_ADE05 118736 Human adenovirus C serotype 5 (HAdV-5)(Human adenovirus 5) 529 MASREEEQRETTPERGRGAARRPPTMEDVSSPSPSPPPPRAPPKKRMRRRIESEDEEDSSQDALVPRTPSPRPSTSAADLAIAPKKKKKRPSPKPERPPSPEVIVDSEEEREDVALQMVGFSNPPVLIKHGKGGKRTVRRLNEDDPVARGMRTQEEEEEPSEAESEITVMNPLSVPIVSAWEKGMEAARALMDKYHVDNDLKANFKLLPDQVEALAAVCKTWLNEEHRGLQLTFTSNKTFVTMMGRFLQAYLQSFAEVTYKHHEPTGCALWLHRCAEIEGELKCLHGSIMINKEHVIEMDVTSENGQRALKEQSSKAKIVKNRWGRNVVQISNTDARCCVHDAACPANQFSGKSCGMFFSEGAKAQVAFKQIKAFMQALYPNAQTGHGHLLMPLRCECNSKPGHAPFLGRQLPKLTPFALSNAEDLDADLISDKSVLASVHHPALIVFQCCNPVYRNSRAQGGGPNCDFKISAPDLLNALVMVRSLWSENFTELPRMVVPEFKWSTKHQYRNVSLPVAHSDARQNPFDF Disordered - Extended 401 406 KPGHAP Native 1ADTA 1ADVA 1ADVB 1ANVA Relationship to function unknown Unknown Unknown X-ray crystallography 7.2 ethanol 5 NaCl 1.6 phosphate buffer 100 protein 0.5 Paper 9545375 Dekker J, Kanellopoulos PN, van Oosterhout JA, Stier G, Tucker PA, van der Vliet PC 1998 J Mol Biol 277 4 825-38 8039495 Tucker, P., Tsernoglou, D., Tucker, A., Coenjaerts, F., Leenders, H., Vliet, P. 1994 13 13 2994-3002 4040872 Tsernoglou D, Tsugita A, Tucker AD, van der Vliet PC 1985 FEBS Lett 188 2 248-52 This region is part of the C-terminal portion of the protein which is important in chain formation and DNA replication. Ordered 332 400 SNTDARCCVHDAACPANQFSGKSCGMFFSEGAKAQVAFKQIKAFMQALYPNAQTGHGHLLMPLRCECNS 1ADTA 1ADVA 1ADVB 1ANVA Paper 8039495 Tucker, P., Tsernoglou, D., Tucker, A., Coenjaerts, F., Leenders, H., Vliet, P. 1994 13 13 2994-3002 9545375 Dekker J, Kanellopoulos PN, van Oosterhout JA, Stier G, Tucker PA, van der Vliet PC 1998 J Mol Biol 277 4 825-38 4040872 Tsernoglou D, Tsugita A, Tucker AD, van der Vliet PC 1985 FEBS Lett 188 2 248-52 Ordered 465 529 PNCDFKISAPDLLNALVMVRSLWSENFTELPRMVVPEFKWSTKHQYRNVSLPVAHSDARQNPFDF 1ADTA 1ADVA 1ADVB 1ANVA Paper 8039495 Tucker, P., Tsernoglou, D., Tucker, A., Coenjaerts, F., Leenders, H., Vliet, P. 1994 13 13 2994-3002 9545375 Dekker J, Kanellopoulos PN, van Oosterhout JA, Stier G, Tucker PA, van der Vliet PC 1998 J Mol Biol 277 4 825-38 4040872 Tsernoglou D, Tsugita A, Tucker AD, van der Vliet PC 1985 FEBS Lett 188 2 248-52 Ordered 407 452 FLGRQLPKLTPFALSNAEDLDADLISDKSVLASVHHPALIVFQCCN 1ADTA 1ADVA 1ADVB 1ANVA Paper 8039495 Tucker, P., Tsernoglou, D., Tucker, A., Coenjaerts, F., Leenders, H., Vliet, P. 1994 13 13 2994-3002 9545375 Dekker J, Kanellopoulos PN, van Oosterhout JA, Stier G, Tucker PA, van der Vliet PC 1998 J Mol Biol 277 4 825-38 4040872 Tsernoglou D, Tsugita A, Tucker AD, van der Vliet PC 1985 FEBS Lett 188 2 248-52 Disordered - Extended 453 464 PVYRNSRAQGGG Native 1ADTA 1ADVA 1ADVB 1ANVA Relationship to function unknown Unknown Unknown X-ray crystallography 7.2 ethanol 5 NaCl 1.6 phosphate buffer 100 protein 0.5 Paper 9545375 Dekker J, Kanellopoulos PN, van Oosterhout JA, Stier G, Tucker PA, van der Vliet PC 1998 J Mol Biol 277 4 825-38 8039495 Tucker, P., Tsernoglou, D., Tucker, A., Coenjaerts, F., Leenders, H., Vliet, P. 1994 13 13 2994-3002 4040872 Tsernoglou D, Tsugita A, Tucker AD, van der Vliet PC 1985 FEBS Lett 188 2 248-52 This region is part of the C-terminal portion of the protein which is important for chain formation and DNA replication. Disordered - Extended Flexible Loop 297 331 IEMDVTSENGQRALKEQSSKAKIVKNRWGRNVVQI Native 1ADTA 1ADVA 1ADVB 1ANVA Function arises via a disorder to order transition Molecular recognition effectors DNA unwinding Protein-DNA binding X-ray crystallography 7.2 ethanol 5 NaCl 1.6 phosphate buffer 100 protein 0.5 Paper 9545375 Dekker J, Kanellopoulos PN, van Oosterhout JA, Stier G, Tucker PA, van der Vliet PC 1998 J Mol Biol 277 4 825-38 8039495 Tucker, P., Tsernoglou, D., Tucker, A., Coenjaerts, F., Leenders, H., Vliet, P. 1994 13 13 2994-3002 4040872 Tsernoglou D, Tsugita A, Tucker AD, van der Vliet PC 1985 FEBS Lett 188 2 248-52 This region is known as the flexible loop. It goes from disordered to ordered upon binding to DNA, helps to stabilize the binding complex and plays an important role in DNA replication. Ordered 174 296 SVPIVSAWEKGMEAARALMDKYHVDNDLKANFKLLPDQVEALAAVCKTWLNEEHRGLQLTFTSNKTFVTMMGRFLQAYLQSFAEVTYKHHEPTGCALWLHRCAEIEGELKCLHGSIMINKEHV 1ADTA 1ADVA 1ADVB 1ANVA Paper 4040872 Tsernoglou D, Tsugita A, Tucker AD, van der Vliet PC 1985 FEBS Lett 188 2 248-52 8039495 Tucker, P., Tsernoglou, D., Tucker, A., Coenjaerts, F., Leenders, H., Vliet, P. 1994 13 13 2994-3002 9545375 Dekker J, Kanellopoulos PN, van Oosterhout JA, Stier G, Tucker PA, van der Vliet PC 1998 J Mol Biol 277 4 825-38 Cathelicidin antimicrobial peptide CAMP_HUMAN 18 kDa cationic antimicrobial protein CAP-18 hCAP-18 Antibacterial protein FALL-39 [cleavage product 1] FALL-39 peptide antibiotic [cleavage product 1] Antibacterial protein LL-37 [cleavage product 2] P49913 Hs.51120 CAMP_HUMAN 1706745 Homo sapiens (Human) 170 MKTQRNGHSLGRWSLVLLLLGLVMPLAIIAQVLSYKEAVLRAIDGINQRSSDANLYRLLDLDPRPTMDGDPDTPKPVSFTVKETVCPRTTQQSPEDCDFKKDGLVKRCMGTVTLNQARGSFDISCDKDNKRFALLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES Previous entry DP00004 has been split into polyprotein DP00004 and cleavage product DP00004_C002. Antibacterial protein LL-37 CAMP_HUMAN Cleavage product 2 of Cathelicidin antimicrobial peptide P49913 Hs.51120 CAMP_HUMAN 1706745 Homo sapiens (Human) 37 LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES Disordered - Extended 1 37 LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES Engineered Function arises via a disorder to order transition Unknown Unknown Circular dichroism (CD) spectroscopy, near-UV 298 6 magnesium sulfate salt 84 sodium chloride salt 160 Paper 9452503 Johansson J, Gudmundsson GH, Rottenberg ME, Berndt KD, Agerberth B 1998 J Biol Chem 273 6 3718-24 The disordered region became significantly more disordered below pH 5. At pH of 2, it was completely disordered. At pH of 13, it adopted a helical structure. Previous entry DP00004 has been split into polyprotein DP00004 and cleavage product DP00004_C002. Antitermination protein N REGN_LAMBD Antitermination protein N of bacteriophage lambda Nucleocapsid protein Regulatory protein N PN P03045 REGN_LAMBD 132276 Enterobacteria phage lambda (Bacteriophage lambda) 107 MDAQTRRRERRAEKQAQWKAANPLLVGVSAKPVNLPILSLNRKPKSRVESALNPIDLTVLAEYHKQIESNLQRIERKNQRTWYSKPGERGITCSGRQKIKGKSIPLI Disordered 1 107 MDAQTRRRERRAEKQAQWKAANPLLVGVSAKPVNLPILSLNRKPKSRVESALNPIDLTVLAEYHKQIESNLQRIERKNQRTWYSKPGERGITCSGRQKIKGKSIPLI Native Function arises via a disorder to order transition Protein-genomic RNA binding Nuclear magnetic resonance (NMR) 298 5.5 Varian Inova 500 MHz spectrometer d4-succinate Aldrich 25 NaCl 100 EDTA 0.2 NaN3 0.05 DTT fresh 2 Paper 9659923 Mogridge J, Legault P, Li J, Van Oene MD, Kay LE, Greenblatt J 1998 Mol Cell 1 2 265-75 AV (6-15-2010) PubMed: 9659923 Cytochrome c CYC_HORSE Apocytochrome c P00004 Eca.1571 CYC_HORSE 119388048 Equus caballus (Horse) 104 GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWKEETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE Disordered 1 104 GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWKEETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE Fragment Monomeric Cofactor/heme binding Circular dichroism (CD) spectroscopy, far-UV Cary model 60 spectropolarimeter extinction rate 2330 Analytical ultracentrifugation average V 0.744 Sphinco Model E analytical ultracentrifuge Viscometry 296 Ostwald capillary viscometer outflow time 80 Paper 4344990 Stellwagen E, Rysavy R, Babul G 1972 J Biol Chem 247 24 8074-7 Sent for AV (6-15-2010) PubMed: 4344990 DNA-(apurinic or apyrimidinic site) lyase APEX1_HUMAN Apurinic-apyrimidinic endonuclease 1 AP endonuclease 1 APEX nuclease APEN APE nuclease HAP1 Apurinic/apyrimidinic endonuclease Protein REF-1 EC=4.2.99.18 P27695 Hs.73722 APEX1_HUMAN 113984 Homo sapiens (Human) 318 MPKRGKKGAVAEDGDELRTEPEAKKSKTAAKKNDKEAAGEGPALYEDPPDQKTSPSGKPATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQELPGLSHQYWSAPSDKEGYSGVGLLSRQCPLKVSYGIGDEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQRWDEAFRKFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLPALCDSKIRSKALGSDHCPITLYLAL Disordered - Extended 102 112 NKLPAELQELP Complex Native 1HD7A Relationship to function unknown Unknown Unknown X-ray crystallography 4.6 sodium acetate pH 4.6 0.1 polyethylene glycol 4000 25% (w/v) lead (II) acetate 1 Paper 11286553 Beernink PT, Segelke BW, Hadi MZ, Erzberger JP, Wilson DM 3rd, Rupp B 2001 J Mol Biol 307 4 1023-34 This structure is refered to as 'form II' in Beernink (2001). Disordered - Extended 123 127 SDKEG Complex Native 1HD7A Relationship to function unknown Unknown Unknown X-ray crystallography 4.6 lead (II) acetate 1 polyethylene glycol 4000 25% (w/v) sodium acetate pH 4.6 0.1 Paper 11286553 Beernink PT, Segelke BW, Hadi MZ, Erzberger JP, Wilson DM 3rd, Rupp B 2001 J Mol Biol 307 4 1023-34 This structure is refered to as 'form II' in Beernink (2001). Disordered 100 104 SENKL Complex Engineered Relationship to function unknown Unknown Unknown X-ray crystallography 6.2 1,4- Dioxane 5 percent w/v calcium acetate 292 Kelvin 200 crystals flash cooled 110 Kelvin HEPES pH 7.4 10 MES pH 6.2 100 PEG 8000 16 to 20 percent w/v samarium acetate 7.5-30 mM well solution 3 Paper 11286553 Beernink PT, Segelke BW, Hadi MZ, Erzberger JP, Wilson DM 3rd, Rupp B 2001 J Mol Biol 307 4 1023-34 This structure is refered to as 'form I' in Beernink (2001). The experimental sequence did not contain the N-terminal residues 1-35. Disordered - Extended 1 42 MPKRGKKGAVAEDGDELRTEPEAKKSKTAAKKNDKEAAGEGP Complex Native 1E9NA 1E9NB Relationship to function unknown Unknown Disordered region is not essential for protein function Unknown X-ray crystallography 7.5 HECAMEG 19.5 lead (II) acetate 1 polyethylene glycol 4000 25% (w/v) sodium acetate 0.2 Tris-HCl pH 7.5 0.1 Paper 9351835 Gorman MA, Morera S, Rothwell DG, de La Fortelle E, Mol CD, Tainer JA, Hickson ID, Freemont PS 1997 Embo J 16 21 6548-58 This region is not essential for function (Gorman 1997). This structure is refered to as 'form III' in Beernink (2001) Disordered - Extended 1 43 MPKRGKKGAVAEDGDELRTEPEAKKSKTAAKKNDKEAAGEGPA Complex Native 1HD7A Relationship to function unknown Unknown Unknown Disordered region is not essential for protein function X-ray crystallography 4.6 lead (II) acetate 1 polyethylene glycol 4000 25% (w/v) sodium acetate pH 4.6 0.1 Paper 11286553 Beernink PT, Segelke BW, Hadi MZ, Erzberger JP, Wilson DM 3rd, Rupp B 2001 J Mol Biol 307 4 1023-34 This structure is refered to as 'form II' in Beernink (2001). Disordered - Extended 36 43 EAAGEGPA Complex Engineered Fragment 1BIX_ Relationship to function unknown Unknown Disordered region is not essential for protein function Unknown X-ray crystallography 6.2 1,4- Dioxane 5 percent w/v calcium acetate 292 Kelvin 200 crystals flash cooled 110 Kelvin HEPES pH 7.4 10 MES pH 6.2 100 PEG 8000 16 to 20 percent w/v samarium acetate 7.5-30 mM well solution 3 Paper 9351835 Gorman MA, Morera S, Rothwell DG, de La Fortelle E, Mol CD, Tainer JA, Hickson ID, Freemont PS 1997 Embo J 16 21 6548-58 This structure is refered to as 'form I' in Beernink (2001). The experimental sequence did not contain the N-terminal residues 1-35. For forms I, II and III of this protein referenced in Beernick (2001) , there is relatively high thermal motion in the areas of residues 100-110, 145, 200 and 270. These areas also show large root-mean-square fluctuations. POU domain class 2-associating factor 1 OBF1_MOUSE B-cell-specific coactivator OBF-1 OCT-binding factor 1 B-cell-specific coactivator OCA-B OCA-B B-cell-specific coactivator BOB-1 BOB-1 Q64693 Mm.897 OBF1_MOUSE 2842674 Mus musculus (Mouse) 256 MLWQKSTAPEQAPAPPRPYQGVRVKEPVKELLRRKRGHTSVGAAGPPTAGVLPHQPLATYSTVGPSCLDMEVSASTVTEEGTLCAGWLSQPAPATLHALAPWTPYTEYVSHEAVSCPYSTDMYVQPVCPSYTVVGPSSVLTYASPPLITNVTPRSTATPAVGPQLEGPEHQAPLTYFPWPQPLSTLPTSSLQYQPPAPTLSGPQFVQLPISIPEPVLQDMDDPRRAISSLTIDKLLLEEEESNTYELNHTLSVEGF Disordered 1 256 MLWQKSTAPEQAPAPPRPYQGVRVKEPVKELLRRKRGHTSVGAAGPPTAGVLPHQPLATYSTVGPSCLDMEVSASTVTEEGTLCAGWLSQPAPATLHALAPWTPYTEYVSHEAVSCPYSTDMYVQPVCPSYTVVGPSSVLTYASPPLITNVTPRSTATPAVGPQLEGPEHQAPLTYFPWPQPLSTLPTSSLQYQPPAPTLSGPQFVQLPISIPEPVLQDMDDPRRAISSLTIDKLLLEEEESNTYELNHTLSVEGF Native Function arises via a disorder to order transition Protein-DNA binding Circular dichroism (CD) spectroscopy, far-UV Station 3.1 Daresbury Synchrotron radiation source path length quartz cuvette 0.01 NaCl 50 DTT 5 Small-angle X-ray scattering (SAXS) Nuclear magnetic resonance (NMR) 295 Paper 11380252 Lee L, Stollar E, Chang J, Grossmann JG, O'Brien R, Ladbury J, Carpenter B, Roberts S, Luisi B 2001 Biochemistry 40 22 6580-8 10329190 Chang JF, Phillips K, Lundback T, Gstaiger M, Ladbury JE, Luisi B 1999 J Mol Biol 288 5 941-52 AV (6-15-2010) PubMed: 11380252 Transcription initiation factor IIA small subunit TOA2_YEAST TFIIA 13.5 kDa subunit P32774 TOA2_YEAST 418109 Saccharomyces cerevisiae (Baker's yeast) 122 MAVPGYYELYRRSTIGNSLVDALDTLISDGRIEASLAMRVLETFDKVVAETLKDNTQSKLTVKGNLDTYGFCDDVWTFIVKNCQVTVEDSHRDASQNGSGDSQSVISVDKLRIVACNSKKSE Disordered 90 102 DSHRDASQNGSGDSQ Complex Molecular assembly Transactivation (transcriptional activation) Protein-protein binding X-ray crystallography 103 Paper 8610010 Tan S, Hunziker Y, Sargent DF, Richmond TJ 1996 Nature 381 6578 127-51 Sulfotransferase 1A3/1A4 ST1A3_HUMAN Monoamine-sulfating phenol sulfotransferase Sulfotransferase, monoamine-preferring Catecholamine-sulfating phenol sulfotransferase HAST3 M-PST Thermolabile phenol sulfotransferase Placental estrogen sulfotransferase TL-PST EC=2.8.2.1 P50224 Hs.460558 ST1A3_HUMAN 1711609 Homo sapiens (Human) 295 MELIQDTSRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLINTYPKSGTTWVSQILDMIYQGGDLEKCNRAPIYVRVPFLEVNDPGEPSGLETLKDTPPPRLIKSHLPLALLPQTLLDQKVKVVYVARNPKDVAVSYYHFHRMEKAHPEPGTWDSFLEKFMAGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETMDFMVQHTSFKEMKKNPMTNYTTVPQELMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL Ordered 78 90 RVPFLEVNDPGEP 1CJMA Paper 10543947 Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL 1999 J Mol Biol 293 3 521-30 Disordered - Extended 216 261 PEETMDFMVQHTSFKEMKKNPMTNYTTVPQELMDHSISPFMRKGMA Fragment 1CJMA Function arises via a disorder to order transition Metal sponge Substrate/ligand binding X-ray crystallography 293 PAP at 277 K pre-incubation for 1-2 hours lithium sulfate 0.5 polyethylene glycol 8000 5-7% (w/v) Paper 10543947 Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL 1999 J Mol Biol 293 3 521-30 Disordered 1 7 MELIQDT Fragment 1CJMA Function arises via a disorder to order transition Unknown Substrate/ligand binding X-ray crystallography 293 PAP at 277 K pre-incubation for 1-2 hours lithium sulfate 0.5 polyethylene glycol 8000 5-7% (w/v) Paper 10543947 Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL 1999 J Mol Biol 293 3 521-30 Disordered 64 77 GGDLEKCNRAPIYV Fragment 1CJMA Function arises via a disorder to order transition Unknown Substrate/ligand binding X-ray crystallography 293 lithium sulfate 0.5 PAP at 277 K pre-incubation for 1-2 hours polyethylene glycol 8000 5-7% (w/v) Paper 10543947 Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL 1999 J Mol Biol 293 3 521-30 Disordered 91 93 SGL Fragment 1CJMA Function arises via a disorder to order transition Unknown Substrate/ligand binding X-ray crystallography 293 lithium sulfate 0.5 PAP at 277 K pre-incubation for 1-2 hours polyethylene glycol 8000 5-7% (w/v) Paper 10543947 Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL 1999 J Mol Biol 293 3 521-30 Disordered 294 295 EL Fragment 1CJMA Function arises via a disorder to order transition Unknown Substrate/ligand binding X-ray crystallography 293 lithium sulfate 0.5 PAP at 277 K pre-incubation for 1-2 hours polyethylene glycol 8000 5-7% (w/v) Paper 10543947 Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL 1999 J Mol Biol 293 3 521-30 Disordered 216 224 PEETMDFMV Fragment 1CJMA Function arises via a disorder to order transition Unknown Substrate/ligand binding X-ray crystallography 293 lithium sulfate 0.5 PAP at 277 K pre-incubation for 1-2 hours polyethylene glycol 8000 5-7% (w/v) Paper 10543947 Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL 1999 J Mol Biol 293 3 521-30 Ordered 8 63 SRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLINTYPKSGTTWVSQILDMIYQ 1CJMA Paper 10543947 Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL 1999 J Mol Biol 293 3 521-30 Ordered 94 215 ETLKDTPPPRLIKSHLPLALLPQTLLDQKVKVVYVARNPKDVAVSYYHFHRMEKAHPEPGTWDSFLEKFMAGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSL 1CJMA Paper 10543947 Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL 1999 J Mol Biol 293 3 521-30 Ordered 262 293 GDWKTTFTVAQNERFDADYAEKMAGCSLSFRS 1CJMA Paper 10543947 Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL 1999 J Mol Biol 293 3 521-30 Cystic fibrosis transmembrane conductance regulator CFTR_HUMAN CFTR Channel conductance-controlling ATPase cAMP-dependent chloride channel ATP-binding cassette transporter sub-family C member 7 EC=3.6.3.49 P13569 Hs.489786 CFTR_HUMAN 147744553 Homo sapiens (Human) 1480 MQRSPLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEKLEREWDRELASKKNPKLINALRRCFFWRFMFYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGLGRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVFLSVLPYALIKGIILRKIFTTISFCIVLRMAVTRQFPWAVQTWYDSLGAINKIQDFLQKQEYKTLEYNLTTTEVVMENVTAFWEEGFGELFEKAKQNNNNRKTSNGDDSLFFSNFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPDFSSKLMGCDSFDQFSAERRNSILTETLHRFSLEGDAPVSWTETKKQSFKQTGEFGEKRKNSILNPINSIRKFSIVQKTPLQMNGIEEDSDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSVNQGQNIHRKTTASTRKVSLAPQANLTELDIYSRRLSQETGLEISEEINEEDLKECFFDDMESIPAVTTWNTYLRYITVHKSLIFVLIWCLVIFLAEVAASLVVLWLLGNTPLQDKGNSTHSRNNSYAVIITSTSSYYVFYIYVGVADTLLAMGFFRGLPLVHTLITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFISILTTGEGEGRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFIDMPTEGKPTKSTKPYKNGQLSKVMIIENSHVKKDDIWPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQAISPSDRVKLFPHRNSSKCKSKPQIAALKEETEEEVQDTRL Disordered R8 708 831 IRKFSIVQKTPLQMNGIEEDSDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSVNQGQNIHRKTTASTRKVSLAPQANLTELDIYSRRLSQETGLEISEEINEEDLKE Native Phosphorylation Circular dichroism (CD) spectroscopy, near-UV 295 9 Aviv CD Model 62DS path length quartz cuvette 0.2 bandwidth 1 averaging time 2 protein sample 0.15 Analytical ultracentrifugation 298 9 An-60 Ti rotor Beckman XL-I centrifuge glycine 10 NaCl 0.1 Paper 10792060 Ostedgaard LS, Baldursson O, Vermeer DW, Welsh MJ, Robertson AD 2000 Proc Natl Acad Sci U S A 97 10 5657-62 The sequence contains a mismatch at amino acid 470 when compared to PIR and SwissProt. Additional UniGene IDs, Hs.621460 and Hs.661104 Sent for AV (6-15-2010) PubMed: 10792060 Choriogonadotropin subunit beta CGHB_HUMAN CG-beta Chorionic gonadotrophin chain beta HCG Human chorionic gonadotropin P01233 Hs.172944 CGHB_HUMAN 116184 Homo sapiens (Human) 145 SKEPLRPRCRPINATLAVEKEGCPVCITVNTTICAGYCPTMTRVLQGVLPALPQVVCNYRDVRFESIRLPGCPRGVNPVVSYAVALSCQCALCRRSTTDCGGPKDHPLTCDDPRFQDSSSSKAPPPSLPSPSRLPGPSDTPILPQ Disordered C-terminal 112 145 DPRFQDSSSSKAPPPSLPSPSRLPGPSDTPILPQ Monomeric Native 1HRPB Intraprotein interaction Glycosylation X-ray crystallography 298 Siemens/Xentronics P1000 area detector and synchrotron (film) wavelength 1.54 and 1.48 A resolution 3 Paper 8202136 Lapthorn AJ, Harris DC, Littlejohn A, Lustbader JW, Canfield RE, Machin KJ, Morgan FJ, Isaacs NW 1994 Nature 369 6480 455-61 SwissProt and NCBI have a sequence of 165 amino acids. This includes a 20 amino acid signal region on the N-terminal. Unigene, Hs.446683, Hs.590955, Hs.659014, Hs.681647, Hs.719497 AV (6-15-2010) PubMed: 8202136 Clusterin CLUS_RAT Sulfated glycoprotein 2 SGP-2 Dimeric acid glycoprotein DAG Testosterone repressed prostate message 2 TRPM-2 Clusterin beta chain (cleavage chain 1) Clusterin alpha chain (cleavage chain 2) P05371 Rn.1780 CLUS_RAT 461756 Rattus norvegicus (Rat) 447 MKILLLCVALLLTWDNGMVLGEQEFSDNELQELSTQGSRYVNKEIQNAVQGVKHIKTLIEKTNAERKSLLNSLEEAKKKKEGALDDTRDSEMKLKAFPEVCNETMMALWEECKPCLKHTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRIDSLLESDRQQSQVLDAMQDSFTRASGIIDTLFQDRFFTHEPQDIHHFSPMGFPHKRPHFLYPKSRLVRSLMPLSHYGPLSFHNMFQPFFDMIHQAQQAMDVQLHSPALQFPDVDFLKEGEDDPTVCKEIRHNSTGCLKMKGQCEKCQEILSVDCSTNNPAQANLRQELNDSLQVAERLTQQYNELLHSLQSKMLNTSSLLEQLNDQFTWVSQLANLTQGDDQYLRVSTVTTHSSDSEVPSRVTEVVVKLFDSDPITVVLPEEVSKDNPKFMDTVAEKALQEYRRKSRME Disordered 22 41 EQEFSDNELQELSTQGSRYV Relationship to function unknown Unknown Protein detergent Circular dichroism (CD) spectroscopy, far-UV 298 7 Clusterin protein prepared in PBS 4 Nuclear magnetic resonance (NMR) Sensitivity to proteolysis 310 Clusterin renatured or partially denatured Deionized H2O 200 uL Tris pH 7.3, 10 uL 1 Trypsin 4 ug Paper 11570883 Bailey RW, Dunker AK, Brown CJ, Garner EC, Griswold MD 2001 Biochemistry 40 39 11828-40 This protein has been determined disordered based on numerous experimental results that indicate it contains flexible loops. However, no exact amino acid locations of disorder are known and the domains specified were based on PONDR predictions. Disordered 66 97 RKSLLNSLEEAKKKKEGALDDTRDSEMKLKAF Relationship to function unknown Unknown Protein detergent Circular dichroism (CD) spectroscopy, far-UV 298 7 Clusterin protein prepared in PBS 4 Nuclear magnetic resonance (NMR) Sensitivity to proteolysis 310 Clusterin renatured or partially denatured Deionized H2O 200 uL Tris pH 7.3, 10 uL 1 Trypsin 4 ug Paper 11570883 Bailey RW, Dunker AK, Brown CJ, Garner EC, Griswold MD 2001 Biochemistry 40 39 11828-40 This protein has been determined disordered based on numerous experimental results that indicate it contains flexible loops. However, no exact amino acid locations of disorder are known and the domains specified were based on PONDR predictions. Disordered 386 447 TVTTHSSDSEVPSRVTEVVVKLFDSDPITVVLPEEVSKDNPKFMDTVAEKALQEYRRKSRME Relationship to function unknown Unknown Protein detergent Circular dichroism (CD) spectroscopy, far-UV 298 7 Clusterin protein prepared in PBS 4 Nuclear magnetic resonance (NMR) Sensitivity to proteolysis 310 Clusterin renatured or partially denatured Deionized H2O 200 uL Tris pH 7.3, 10 uL 1 Trypsin 4 ug Paper 11570883 Bailey RW, Dunker AK, Brown CJ, Garner EC, Griswold MD 2001 Biochemistry 40 39 11828-40 This protein has been determined disordered based on numerous experimental results that indicate it contains flexible loops. However, no exact amino acid locations of disorder are known and the domains specified were based on PONDR predictions. This protein has been determined disordered based on numerous experimental results that indicate it contains flexible loops. However, no exact amino acid locations of disorder are known and the domains specified were based on PONDR predictions. cAMP-dependent protein kinase inhibitor alpha IPKA_RABIT cAMP-dependent protein kinase inhibitor, muscle/brain isoform PKI-alpha P61926 IPKA_RABIT 48428971 Oryctolagus cuniculus (Rabbit) 76 MTDVETTYADFIASGRTGRRNAIHDILVSSASGNSNELALKLAGLDINKTEGEEDAQRSSTEQSGEAQGEAAKSES Disordered 1 75 MTDVETTYADFIASGRTGRRNAIHDILVSSASGNSNELALKLAGLDINKTEGEEDAQRSSTEQSGEAQGEAAKSE Native Phosphorylation Substrate/ligand binding Protein inhibitor Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) 7 Mattson Alpha Centaun spectrometer resolution 4 teflon spacer 0.05 protein sample 4.69 sodium phosphate 10 Perkin-Elmer solution cell Circular dichroism (CD) spectroscopy, far-UV 298 7 bandwidth 1 Jasca 40CS spectropolarimeter path length cell Hellma 0.01 protein sample 4.69 sensitivity 5 sodium phosphate buffer 10 Paper 1862343 Knighton DR, Zheng JH, Ten Eyck LF, Xuong NH, Taylor SS, Sowadski JM 1991 Science 253 5018 414-20 2040607 Thomas J, Van Patten SM, Howard P, Day KH, Mitchell RD, Sosnick T, Trewhella J, Walsh DA, Maurer RA 1991 J Biol Chem 266 17 10906-11 Sent for AV (6-15-2010) PubMed: 2040607 Cyclin-dependent kinase inhibitor 1 CDN1A_HUMAN CDK-interacting protein 1 Cyclin-dependent kinase inhibitor p21 p21 Melanoma differentiation-associated protein 6 MDA-6 P38936 Hs.370771 CDN1A_HUMAN 729143 Homo sapiens (Human) 164 MSEPAGDVRQNPCGSKACRRLFGPVDSEQLSRDCDALMAGCIQEARERWNFDFVTETPLEGDFAWERVRGLGLPKLYLPTGPRRGRDELGGGRRPGTSPALLQGTAEEDHVDLSLSCTLVPRSGEQAEGSPGGPGDSQGRKRRQTSMTDFYHSKRRLIFSKRKP Disordered - Extended p21-F (full length) 1 164 MSEPAGDVRQNPCGSKACRRLFGPVDSEQLSRDCDALMAGCIQEARERWNFDFVTETPLEGDFAWERVRGLGLPKLYLPTGPRRGRDELGGGRRPGTSPALLQGTAEEDHVDLSLSCTLVPRSGEQAEGSPGGPGDSQGRKRRQTSMTDFYHSKRRLIFSKRKP Native Function arises via a disorder to order transition Molecular assembly Protein-protein binding SDS-PAGE gel, Aberrant mobility on Circular dichroism (CD) spectroscopy, far-UV Size exclusion/gel filtration chromatography Stability at pH extremes Mass spectrometry-based high resolution hydrogen-deuterium exchange Nuclear magnetic resonance (NMR) Sensitivity to proteolysis Paper 8876165 Kriwacki RW, Hengst L, Tennant L, Reed SI, Wright PE 1996 Proc Natl Acad Sci U S A 93 21 11504-9 9297835 Kriwacki RW, Wu J, Tennant L, Wright PE, Siuzdak G 1997 J Chromatogr A 777 1 23-30 Cyclin-dependent kinase inhibitor 1C CDN1C_HUMAN Cyclin-dependent kinase inhibitor p57 p57KIP2 P49918 Hs.106070 CDN1C_HUMAN 1705731 Homo sapiens (Human) 316 MSDASLRSTSTMERLVARGTFPVLVRTSACRSLFGPVDHEELSRELQARLAELNAEDQNRWDYDFQQDMPLRGPGRLQWTEVDSDSVPAFYRETVQVGRCRLLLAPRPVAVAVAVSPPLEPAAESLDGLEEAPEQLPSVPVPAPASTPPPVPVLAPAPAPAPAPVAAPVAAPVAVAVLAPAPAPAPAPAPAPAPVAAPAPAPAPAPAPAPAPAPAPDAAPQESAEQGANQGQRGQEPLADQLHSGISGRPAAGTAAASANGAAIKKLSGPLISDFFAKRKRSAPEKSSGDVPAPCPSPSAAPGVGSVEQTPRKRLR Disordered - Extended 1 316 MSDASLRSTSTMERLVARGTFPVLVRTSACRSLFGPVDHEELSRELQARLAELNAEDQNRWDYDFQQDMPLRGPGRLQWTEVDSDSVPAFYRETVQVGRCRLLLAPRPVAVAVAVSPPLEPAAESLDGLEEAPEQLPSVPVPAPASTPPPVPVLAPAPAPAPAPVAAPVAAPVAVAVLAPAPAPAPAPAPAPAPVAAPAPAPAPAPAPAPAPAPAPDAAPQESAEQGANQGQRGQEPLADQLHSGISGRPAAGTAAASANGAAIKKLSGPLISDFFAKRKRSAPEKSSGDVPAPCPSPSAAPGVGSVEQTPRKRLR Native Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Analytical ultracentrifugation 278 Circular dichroism (CD) spectroscopy, far-UV 7 DTT 0.001 NaCl salt 50 sodium phosphate salt 10 Size exclusion/gel filtration chromatography 7 DTT 1 NaCl salt 150 sodium phosphate salt 10 Fluorescence, intrinsic 7 DTT 1 NaCl salt 50 sodium phosphate salt 10 Nuclear magnetic resonance (NMR) 303 6.6 DTT 1 NaCl salt 50 sodium phosphate salt 10 Paper 9251023 Dynlacht BD, Ngwu C, Winston J, Swindell EC, Elledge SJ, Harlow E, Harper JW 1997 Methods Enzymol 283 230-44 11746698 Adkins JN, Lumb KJ 2002 Proteins 46 1 1-7 Disordered - Extended inhibition domain 27 91 TSACRSLFGPVDHEELSRELQARLAELNAEDQNRWDYDFQQDMPLRGPGRLQWTEVDSDSVPAFY Fragment Native Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Analytical ultracentrifugation 278 Circular dichroism (CD) spectroscopy, far-UV 7 DTT 0.001 NaCl salt 50 sodium phosphate salt 10 Paper 11746698 Adkins JN, Lumb KJ 2002 Proteins 46 1 1-7 9251023 Dynlacht BD, Ngwu C, Winston J, Swindell EC, Elledge SJ, Harlow E, Harper JW 1997 Methods Enzymol 283 230-44 This fragment had 90% inhibition activity towards A-CDK2. Cyclin-dependent kinase inhibitor 1B CDN1B_HUMAN Cyclin-dependent kinase inhibitor p27 p27Kip1 P46527 Hs.238990 CDN1B_HUMAN 1168871 Homo sapiens (Human) 198 MSNVRVSNGSPSLERMDARQAEHPKPSACRNLFGPVDHEELTRDLEKHCRDMEEASQRKWNFDFQNHKPLEGKYEWQEVEKGSLPEFYYRPPRPPKGACKVPAQESQDVSGSRPAAPLIGAPANSEDTHLVDPKTDPSDSQTGLAEQCAGIRKRPATDDSSTQNKRANRTEENVSDGSPNAGSVEQTPKKPGLRRRQT Disordered domain 1 22 34 EHPKPSACRNLFG Native 1JSUC Function arises via a disorder to order transition Molecular recognition scavengers Phosphorylation Protein inhibitor Nuclear magnetic resonance (NMR) 298 6.5 Varian Inova 600-MHz spectrometer protein sample 1 potassium phosphate buffer 50 2H2O v/v 5 DTT 5 NaN3 w/v 0.02 Paper 15024385 Lacy ER, Filippov I, Lewis WS, Otieno S, Xiao L, Weiss S, Hengst L, Kriwacki RW 2004 Nat Struct Mol Biol 11 4 358-64 8684460 Russo AA, Jeffrey PD, Patten AK, Massague J, Pavletich NP 1996 Nature 382 6589 325-31 Disordered 96 108 KGACKVPAQESQD Native 1JSUC Function arises via a disorder to order transition Molecular recognition effectors Phosphorylation Protein inhibitor Nuclear magnetic resonance (NMR) 298 6.5 2H2O v/v 5 DTT 5 NaN3 w/v 0.02 potassium phosphate buffer 50 protein sample 1 Varian Inova 600-MHz spectrometer Paper 15024385 Lacy ER, Filippov I, Lewis WS, Otieno S, Xiao L, Weiss S, Hengst L, Kriwacki RW 2004 Nat Struct Mol Biol 11 4 358-64 Sent for AV (6-15-2010) PubMed: 15024385 DNA-binding protein RAP1 RAP1_YEAST SBF-E Repressor/activator site-binding protein TUF P11938 RAP1_YEAST 730473 Saccharomyces cerevisiae (Baker's yeast) 827 MSSPDDFETAPAEYVDALDPSMVVVDSGSAAVTAPSDSAAEVKANQNEENTGATAAETSEKVDQTEVEKKDDDDTTEVGVTTTTPSIADTAATANIASTSGASVTEPTTDDTAADEKKEQVSGPPLSNMKFYLNRDADAHDSLNDIDQLARLIRANGGEVLDSKPRESKENVFIVSPYNHTNLPTVTPTYIKACCQSNSLLNMENYLVPYDNFREVVDSRLQEESHSNGVDNSNSNSDNKDSIRPKTEIISTNTNGATEDSTSEKVMVDAEQQARLQEQAQLLRQHVSSTASITSGGHNDLVQIEQPQKDTSNNNNSNVNDEDNDLLTQDNNPQTADEGNASFQAQRSMISRGALPSHNKASFTDEEDEFILDVVRKNPTRRTTHTLYDEISHYVPNHTGNSIRHRFRVYLSKRLEYVYEVDKFGKLVRDDDGNLIKTKVLPPSIKRKFSADEDYTLAIAVKKQFYRDLFQIDPDTGRSLITDEDTPTAIARRNMTMDPNHVPGSEPNFAAYRTQSRRGPIAREFFKHFAEEHAAHTENAWRDRFRKFLLAYGIDDYISYYEAEKAQNREPEPMKNLTNRPKRPGVPTPGNYNSAAKRARNYSSQRNVQPTANAASANAAAAAAAAASNSYAIPENELLDEDTMNFISSLKNDLSNISNSLPFEYPHEIAEAIRSDFSNEDIYDNIDPDTISFPPKIATTDLFLPLFFHFGSTRQFMDKLHEVISGDYEPSQAEKLVQDLCDETGIRKNFSTSILTCLSGDLMVFPRYFLNMFKDNVNPPPNVPGIWTHDDDESLKSNDQEQIRKLVKKHGTGRMEMRKRFFEKDLL Disordered Domain 2 565 571 KAQNREP Complex Native Protein-DNA binding Transactivation (transcriptional activation) X-ray crystallography 100 6 resolution 2.2 MES 20 KCl 20 spermine 2 MPD 30 Paper 8620531 Konig P, Giraldo R, Chapman L, Rhodes D 1996 Cell 85 1 125-36 Disordered Domain 2 579 585 NRPKRPG Complex Native Transactivation (transcriptional activation) Protein-protein binding X-ray crystallography 100 6 KCl 20 MES 20 MPD 30 resolution 2.2 spermine 2 Paper 8620531 Konig P, Giraldo R, Chapman L, Rhodes D 1996 Cell 85 1 125-36 sent for AV (6-15-2010) PubMed: 8620531 Elongation factor G EFG_THETH EF-G P13551 EFG_THETH 119190 Thermus thermophilus 691 MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERERGITITAAVTTCFWKDHRINIIDTPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSETVWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDVLRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEEELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVEIHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHANHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKADQEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDANVGKPQVAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIPAVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYHEVDSSEMAFKIAGSMAIKEAVQKGDPVILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLRSKTQGRGSFVMFFDHYQEVPKQVQEKLIKGQ Disordered 40 65 HKIGEVHEGAATMDFMEQERERGITI Mutant 1FNMA Protein-tRNA binding Substrate/ligand binding X-ray crystallography 7.4 resolution 2.8 wavelength 0.935 GDP 0.5 glycerol v/v 25 Paper 11054294 Laurberg M, Kristensen O, Martemyanov K, Gudkov AT, Nagaev I, Hughes D, Liljas A 2000 J Mol Biol 303 4 593-603 Disordered effector region 38 68 RIHKIGEVHEGAATMDFMEQERERGITITAA Mutant 1FNMA Protein-tRNA binding Substrate/ligand binding X-ray crystallography 7.4 GDP 0.5 glycerol v/v 25 resolution 2.8 wavelength 0.935 Paper 8070397 AEvarsson A, Brazhnikov E, Garber M, Zheltonosova J, Chirgadze Y, al-Karadaghi S, Svensson LA, Liljas A 1994 EMBO J 13 16 3669-77 11054294 Laurberg M, Kristensen O, Martemyanov K, Gudkov AT, Nagaev I, Hughes D, Liljas A 2000 J Mol Biol 303 4 593-603 Sent for AV (6-15-2010) PubMed: 8070397 EMB-1 protein EMB1_DAUCA Embryonic abundant protein P17639 EMB1_DAUCA 119316 Daucus carota (Carrot) 92 MASQQEKKELDARARQGETVVPGGTGGKSLEAQQHLAEGRSKGGQTRKEQLGGEGYHEMGRKGGLSNNDMSGGERAEQEGIDIDESKFRTKK Disordered 1 92 MASQQEKKELDARARQGETVVPGGTGGKSLEAQQHLAEGRSKGGQTRKEQLGGEGYHEMGRKGGLSNNDMSGGERAEQEGIDIDESKFRTKK Native Unknown Unknown Nuclear magnetic resonance (NMR) 294 6 Varian Instruments Unity 500 MHz spectrometer protein sample 10 sodium phosphate buffer 10 D2O 50 Paper Eom J, Baker WR, Kintanar A, Wurtele ES 1996 Plant Science 115 17-24 2339072 Ulrich TU, Wurtele ES, Nikolau BJ 1990 Nucleic Acids Res. 18 9 2826 AV (6-15-2010) PubMed: 2339072 Estradiol 17-beta-dehydrogenase 1 DHB1_HUMAN 17-beta-hydroxysteroid dehydrogenase type 1 17-beta-HSD 1 Placental 17-beta-hydroxysteroid dehydrogenase 20 alpha-hydroxysteroid dehydrogenase 20-alpha-HSD E2DH EC=1.1.1.62 P14061 Hs.654385 DHB1_HUMAN 118554 Homo sapiens (Human) 327 ARTVVLITGCSSGIGLHLAVRLASDPSQSFKVYATLRDLKTQGRLWEAARALACPPGSLETLQLDVRDSKSVAAARERVTEGRVDVLVCNAGLGLLGPLEALGEDAVASVLDVNVVGTVRMLQAFLPDMKRRGSGRVLVTGSVGGLMGLPFNDVYCASKFALEGLCESLAVLLLPFGVHLSLIECGPVHTAFMEKVLGSPEEVLDRTDIHTFHRFYQYLAHSKQVFREAAQNPEEVAEVFLTALRAPKPTLRYFTTERFLPLLRMRLDDPSGSNYVTAMHREVFGDVPAKAEAGAEAGGGAGPGAEDEAGRSAVGDPELGDPPAAPQ Disordered - Extended 285 327 GDVPAKAEAGAEAGGGAGPGAEDEAGRSAVGDPELGDPPAAPQ Native 1BHS_ 1DHTA 1EQUA 1EQUB 1IOL_ 3DHEA Relationship to function unknown Unknown Unknown X-ray crystallography Mass spectrometry-based high resolution hydrogen-deuterium exchange Paper 8756321 Azzi A, Rehse PH, Zhu DW, Campbell RL, Labrie F, Lin SX 1996 Nat Struct Biol 3 8 665-8 7663947 Ghosh D, Pletnev VZ, Zhu DW, Wawrzak Z, Duax WL, Pangborn W, Labrie F, Lin SX 1995 Structure 3 5 503-513 10625652 Han Q, Campbell RL, Gangloff A, Huang YW, Lin SX 2000 J Biol Chem 275 2 1105-1111 9927655 Sawicki MW, Erman M, Puranen T, Vihko P, Ghosh D 1999 Proc Natl Acad Sci U S A 96 3 840-845 The 3DHE:A PDB file gives this protein fragment as complexed with Dehydroepiandrosterone. The 1DHT:A PDB file gives this protein fragment as complexed with Dihydrotestosterone. The 1EQU:A and B PDB files, give this protein fragment as complexed with NADP+ and 3-hydroxyestra-1,3,5,7-tetraen-17-one, (equilin). The 1IOL PDB file gives this protein fragment as complexed with Estradiol. The 1BHS PDB file gives the amino acid sequence for the uncomplexed, unmutated crystal structure of this protein. Disordered - Extended 190 207 TAFMEKVLGSPEEVLDRT Complex Native 1IOL_ Relationship to function unknown Unknown Molecular recognition effectors Substrate/ligand binding X-ray crystallography Paper 8756321 Azzi A, Rehse PH, Zhu DW, Campbell RL, Labrie F, Lin SX 1996 Nat Struct Biol 3 8 665-8 The 1IOL PDB file gives this protein fragment as complexed with Estradiol. Disordered - Extended 191 195 AFMEK Complex 1FDS_ 1FDT_ Function arises from the disordered state Molecular recognition effectors Disordered region is not essential for protein function Substrate/ligand binding X-ray crystallography Mass spectrometry-based high resolution hydrogen-deuterium exchange Paper 8805577 Breton R, Housset D, Mazza C, Fontecilla-Camps JC 1996 Structure 4 8 905-15 The 1FDT PDB gives this protein fragment as complexed with 17-Beta-Estradiol and NADP+ at low temperature, 123 K. The 1FDS PDB file gives this protein fragment as complexed with 17-Beta-Estradiol at room temperature. Disordered - Extended 192 198 FMEKVLG Complex 1FDS_ 1FDT_ Function arises from the disordered state Molecular recognition effectors Disordered region is not essential for protein function Substrate/ligand binding X-ray crystallography Mass spectrometry-based high resolution hydrogen-deuterium exchange Paper 8805577 Breton R, Housset D, Mazza C, Fontecilla-Camps JC 1996 Structure 4 8 905-15 The 1FDT PDB gives this protein fragment as complexed with 17-Beta-Estradiol and NADP+ at low temperature, 123 K. The 1FDS PDB file gives this protein fragment as complexed with 17-Beta-Estradiol at room temperature. Disordered - Extended 286 327 DVPAKAEAGAEAGGGAGPGAEDEAGRSAVGDPELGDPPAAPQ Complex 1FDS_ 1FDT_ 1FDUA 1FDUB 1FDUC 1FDUD 1FDVA 1FDVB 1FDVC 1FDVD 1FDW_ 1I5RA 1JTVA Relationship to function unknown Unknown Disordered region is not essential for protein function Protein-lipid interaction Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) Mass spectrometry-based high resolution hydrogen-deuterium exchange Nuclear magnetic resonance (NMR) X-ray crystallography Paper 8805577 Breton R, Housset D, Mazza C, Fontecilla-Camps JC 1996 Structure 4 8 905-15 12490543 Gangloff A, Shi R, Nahoum V, Lin SX 2003 Faseb J 17 2 274-276 12223444 Qiu W, Campbell RL, Gangloff A, Dupuis P, Boivin RP, Tremblay MR, Poirier D, Lin SX 2002 Faseb J 16 13 1829-1831 9525918 Mazza C, Breton R, Housset D, Fontecilla-Camps JC 1998 J Biol Chem 273 14 8145-8152 The 1I5R:A PDB file gives this protein as complexed with an 8-methylene-based inhibitor- an EM-1745 complex. The 1JTV:A PDB file gives this protein fragment as complexed with testosterone. The 1FDW PDB file gives this protein fragment as complexed with Estradiol and has the mutation H221Q. The 1FDV PDB file gives this protein fragment as complexed with NAD+ and has the mutation H221L. The 1FDU PDB file gives this protein fragment as complexed with Estradiol and NADP+ and has the mutation H221L. The 1FDT PDB file gives this protein fragment as complexed with 17-Beta-Estradiol and NADP+ at low temperature, 123 K. The 1FDS PDB file gives this protein fragment as complexed with 17-Beta-Estradiol at room temperature. The experimental sequence used for the PDB ID 1FDU contained a H221L substitution. The experimental sequence used for PDB ID 1FDV contained a H221L substitution. Disordered - Extended 288 327 PAKAEAGAEAGGGAGPGAEDEAGRSAVGDPELGDPPAAPQ Complex 1FDS_ 1FDT_ Relationship to function unknown Unknown Disordered region is not essential for protein function Protein-lipid interaction X-ray crystallography Mass spectrometry-based high resolution hydrogen-deuterium exchange Paper 8805577 Breton R, Housset D, Mazza C, Fontecilla-Camps JC 1996 Structure 4 8 905-15 The 1FDT PDB gives this protein fragment as complexed with 17-Beta-Estradiol and NADP+ at low temperature, 123 K. The 1FDS PDB file gives this protein fragment as complexed with 17-Beta-Estradiol at room temperature. Disordered - Extended 289 327 AKAEAGAEAGGGAGPGAEDEAGRSAVGDPELGDPPAAPQ Complex 1FDS_ 1FDT_ Relationship to function unknown Unknown Disordered region is not essential for protein function Protein-lipid interaction X-ray crystallography Mass spectrometry-based high resolution hydrogen-deuterium exchange Paper 8805577 Breton R, Housset D, Mazza C, Fontecilla-Camps JC 1996 Structure 4 8 905-15 The 1FDT PDB gives this protein fragment as complexed with 17-Beta-Estradiol and NADP+ at low temperature, 123 K. The 1FDS PDB file gives this protein fragment as complexed with 17-Beta-Estradiol at room temperature. Disordered 190 197 TAFMEKVL Complex 1FDT_ Function arises from the disordered state Molecular recognition effectors Substrate/ligand binding X-ray crystallography 123 Mass spectrometry-based high resolution hydrogen-deuterium exchange Paper 8805577 Breton R, Housset D, Mazza C, Fontecilla-Camps JC 1996 Structure 4 8 905-15 The 1FDT PDB gives this protein fragment as complexed with 17-Beta-Estradiol and NADP+ at low temperature, 123 K. Disordered 192 195 FMEK Complex 1FDT_ Function arises from the disordered state Molecular recognition effectors Substrate/ligand binding X-ray crystallography 123 Mass spectrometry-based high resolution hydrogen-deuterium exchange Paper 8805577 Breton R, Housset D, Mazza C, Fontecilla-Camps JC 1996 Structure 4 8 905-15 The 1FDT PDB gives this protein fragment as complexed with 17-Beta-Estradiol and NADP+ at low temperature, 123 K. Disordered - Extended 199 202 SPEE Complex Engineered 1FDUA Function arises from the disordered state Molecular recognition effectors Disordered region is not essential for protein function Substrate/ligand binding X-ray crystallography Paper 9525918 Mazza C, Breton R, Housset D, Fontecilla-Camps JC 1998 J Biol Chem 273 14 8145-8152 The experimental sequence used for the PDB ID 1FDU contained a H221L substitution. Disordered - Extended 198 202 GSPEE Complex Engineered 1FDUB Function arises from the disordered state Molecular recognition effectors Substrate/ligand binding X-ray crystallography Paper 9525918 Mazza C, Breton R, Housset D, Fontecilla-Camps JC 1998 J Biol Chem 273 14 8145-8152 The experimental sequence included a H221L substitution. Disordered - Extended 198 201 GSPE Complex Engineered 1FDUD Function arises from the disordered state Molecular recognition effectors Substrate/ligand binding X-ray crystallography Paper 9525918 Mazza C, Breton R, Housset D, Fontecilla-Camps JC 1998 J Biol Chem 273 14 8145-8152 The experimental sequence included a H221L substitution. Disordered - Extended 191 200 AFMEKVLGSP Complex Engineered 1FDVA 1FDVB 1FDVC 1FDVD Relationship to function unknown Molecular recognition effectors Substrate/ligand binding X-ray crystallography Mass spectrometry-based high resolution hydrogen-deuterium exchange Paper 9525918 Mazza C, Breton R, Housset D, Fontecilla-Camps JC 1998 J Biol Chem 273 14 8145-8152 The experimental sequence used for PDB ID 1FDV contained a H221L substitution. Disordered - Extended 192 197 FMEKVL Complex Engineered 1FDW_ Function arises from the disordered state Molecular recognition effectors Disordered region is not essential for protein function Substrate/ligand binding X-ray crystallography Paper 9525918 Mazza C, Breton R, Housset D, Fontecilla-Camps JC 1998 J Biol Chem 273 14 8145-8152 The sequence used for PDB ID 1FDW contained a H221Q substitution. Disordered 286 289 DVPA Complex Engineered Fragment 1A27_ Relationship to function unknown Unknown Disordered region is not essential for protein function Protein-lipid interaction X-ray crystallography Paper 9525918 Mazza C, Breton R, Housset D, Fontecilla-Camps JC 1998 J Biol Chem 273 14 8145-8152 The 1A27 PDB file gives this protein fragment as complexed with Estradiol and NADP+. It also has a C-terminal deletion mutation. Disordered 190 201 TAFMEKVLGSPE Complex 1EQUA 1EQUB Function arises from the disordered state Molecular recognition effectors Substrate/ligand binding X-ray crystallography Paper 9927655 Sawicki MW, Erman M, Puranen T, Vihko P, Ghosh D 1999 Proc Natl Acad Sci U S A 96 3 840-845 Disordered - Extended 192 207 FMEKVLGSPEEVLDRT Complex Native 1DHTA 3DHEA Relationship to function unknown Molecular recognition effectors Disordered region is not essential for protein function Substrate/ligand binding X-ray crystallography Paper 10625652 Han Q, Campbell RL, Gangloff A, Huang YW, Lin SX 2000 J Biol Chem 275 2 1105-1111 The 3DHE PDB file gives this protein fragment as complexed with Dehydroepiandrosterone. The 1DHT PDB file gives this protein fragment as complexed with Dihydrotestosterone. Disordered 191 197 AFMEKVL Complex 1JTVA Function arises from the disordered state Molecular recognition effectors Substrate/ligand binding X-ray crystallography Paper 12490543 Gangloff A, Shi R, Nahoum V, Lin SX 2003 Faseb J 17 2 274-276 The 1JTV PDB file gives this protein fragment as complexed with testosterone. Disordered - Extended 191 198 AFMEKVLG Complex Engineered 1FDVA 1FDVB 1FDVC 1FDVD Function arises from the disordered state Molecular recognition effectors Substrate/ligand binding X-ray crystallography Mass spectrometry-based high resolution hydrogen-deuterium exchange Paper 9525918 Mazza C, Breton R, Housset D, Fontecilla-Camps JC 1998 J Biol Chem 273 14 8145-8152 The experimental sequence used for PDB ID 1FDV contained a H221L substitution. UniGene, Hs.655222 Protein E7 VE7_HPV16 P03129 VE7_HPV16 137791 Human papillomavirus type 16 98 MHGDTPTLHEYMLDLQPETTDLYCYEQLSDSSEEEDEIDGPAGQAEPDRAHYNIVTFCCKCDSTLRLCVQSTHVDIRTLEDLLMGTLGIVCPICSQKP Disordered 1 98 MHGDTPTLHEYMLDLQPETTDLYCYEQLSDSSEEEDEIDGPAGQAEPDRAHYNIVTFCCKCDSTLRLCVQSTHVDIRTLEDLLMGTLGIVCPICSQKP Native Function arises via a disorder to order transition Metal binding Phosphorylation Circular dichroism (CD) spectroscopy, far-UV 278 7.5 Jasco J-600 spectropolarimeter path length quartz cell 0.2 protein sample 0.78 Tris 1 EDTA 0.1 DTT 0.1 zinc or cadmium chloride 1 Paper 8245034 Pahel G, Aulabaugh A, Short SA, Barnes JA, Painter GR, Ray P, Phelps WC 1993 J Biol Chem 268 34 26018-25 AV (6-17-10) PubMed: 20088881 Fibronectin-binding protein A FNBA_STAA8 FNBP Fibronectin-binding protein P14738 FNBA_STAA8 120457 Staphylococcus aureus (strain NCTC 8325) 1018 MKNNLRYGIRKHKLGAASVFLGTMIVVGMGQDKEAAASEQKTTTVEENGNSATDNKTSETQTTATNVNHIEETQSYNATVTEQPSNATQVTTEEAPKAVQAPQTAQPANIETVKEEVVKEEAKPQVKETTQSQDNSGDQRQVDLTPKKATQNQVAETQVEVAQPRTASESKPRVTRSADVAEAKEASNAKVETGTDVTSKVTVEIGSIEGHNNTNKVEPHAGQRAVLKYKLKFENGLHQGDYFDFTLSNNVNTHGVSTARKVPEIKNGSVVMATGEVLEGGKIRYTFTNDIEDKVDVTAELEINLFIDPKTVQTNGNQTITSTLNEEQTSKELDVKYKDGIGNYYANLNGSIETFNKANNRFSHVAFIKPNNGKTTSVTVTGTLMKGSNQNGNQPKVRIFEYLGNNEDIAKSVYANTTDTSKFKEVTSNMSGNLNLQNNGSYSLNIENLDKTYVVHYDGEYLNGTDEVDFRTQMVGHPEQLYKYYYDRGYTLTWDNGLVLYSNKANGNEKNGPIIQNNKFEYKEDTIKETLTGQYDKNLVTTVEEEYDSSTLDIDYHTAIDGGGGYVDGYIETIEETDSSAIDIDYHTAVDSEAGHVGGYTESSEESNPIDFEESTHENSKHHADVVEYEEDTNPGGGQVTTESNLVEFDEESTKGIVTGAVSDHTTVEDTKEYTTESNLIELVDELPEEHGQAQGPVEEITKNNHHISHSGLGTENGHGNYDVIEEIEENSHVDIKSELGYEGGQNSGNQSFEEDTEEDKPKYEQGGNIVDIDFDSVPQIHGQNKGNQSFEEDTEKDKPKYEHGGNIIDIDFDSVPHIHGFNKHTEIIEEDTNKDKPSYQFGGHNSVDFEEDTLPKVSGQNEGQQTIEEDTTPPIVPPTPPTPEVPSEPETPTPPTPEVPSEPETPTPPTPEVPSEPETPTPPTPEVPAEPGKPVPPAKEEPKKPSKPVEQGKVVTPVIEINEKVKAVAPTKKPQSKKSELPETGGEESTNKGMLFGGLFSILGLALLRRNKKNHKA Disordered D1-D4 745 874 GQNSGNQSFEEDTEEDKPKYEQGGNIVDIDFDSVPQIHGQNKGDQSFEEDTEKDKPKYEHGGNIIDIDFDSVPHIHGFNKHTEIIEEDTNKDKPNYQFGGHNSVDFEEDTLPQVSGHNEGQQTIEEDTTT Fragment Natural variant Protein-protein binding Nuclear magnetic resonance (NMR) 278 6 protein sample 1 spectrometer 750 Paper 9398523 Penkett CJ, Redfield C, Dodd I, Hubbard J, McBay DL, Mossakowska DE, Smith RA, Dobson CM, Smith LJ 1997 J Mol Biol 274 2 152-9 AV (6-17-2010) PubMed: 9398523 Flagellin FLIC_SALTY Phase-1-I flagellin P06179 FLIC_SALTY 20141325 Salmonella typhimurium 494 AQVINTNSLSLLTQNNLNKSQSALGTAIERLSSGLRINSAKDDAAGQAIANRFTANIKGLTQASRNANDGISIAQTTEGALNEINNNLQRVRELAVQSANSTNSQSDLDSIQAEITQRLNEIDRVSGQTQFNGVKVLAQDNTLTIQVGANDGETIDIDLKQINSQTLGLDTLNVQQKYKVSDTAATVTGYADTTIALDNSTFKASATGLGGTDQKIDGDLKFDDTTGKYYAKVTVTGGTGKDGYYEVSVDKTNGEVTLAGGATSPLTGGLPATATEDVKNVQVANADLTEAKAALTAAGVTGTASVVKMSYTDNNGKTIDGGLAVKVGDDYYSATQNKDGSISINTTKYTADDGTSKTALNKLGGADGKTEVVSIGGKTYAASKAEGHNFKAQPDLAEAAATTTENPLQKIDAALAQVDTLRSDLGAVQNRFNSAITNLGNTVNNLTSARSRIEDSDYATEVSNMSRAQILQQAGTSVLAQANQVPQNVLSLLR Disordered N-terminal 1 65 AQVINTNSLSLLTQNNLNKSQSALGTAIERLSSGLRINSAKDDAAGQAIANRFTANIKGLTQASR Monomeric Native Function arises via a disorder to order transition Polymerization Structural mortar Circular dichroism (CD) spectroscopy, far-UV 298 7 Jasco-600 spectropolarimeter path length cylindrical fused quartz cells 0.2 phosphate buffer 10 NaCl 150 Sensitivity to proteolysis 298 7.8 protein sample 1 protein-enzyme ratio 300:1 (w/w) proteolytic enzyme trypsin Paper 2810365 Vonderviszt F, Kanto S, Aizawa S, Namba K 1989 J Mol Biol 209 1 127-33 Disordered C-terminal 455 494 DSDYATEVSNMSRAQILQQAGTSVLAQANQVPQNVLSLLR Monomeric Native Function arises via a disorder to order transition Structural mortar Polymerization Circular dichroism (CD) spectroscopy, far-UV 298 7 Jasco-600 spectropolarimeter NaCl 150 path length cylindrical fused quartz cells 0.2 phosphate buffer 10 Sensitivity to proteolysis 298 7.8 protein sample 1 proteolytic enzyme 200 Tris-HCl buffer 20 Paper 2810365 Vonderviszt F, Kanto S, Aizawa S, Namba K 1989 J Mol Biol 209 1 127-33 AV (6-17-2010) PubMed: 2810365 Negative regulator of flagellin synthesis FLGM_SALTY Anti-sigma-28 factor FlgM P26477 FLGM_SALTY 120306 Salmonella typhimurium 97 MSIDRTSPLKPVSTVQTRETSDTPVQKTRQEKTSAATSASVTLSDAQAKLMQPGVSDINMERVEALKTAIRNGELKMDTGKIADSLIREAQSYLQSK Disordered 1 97 MSIDRTSPLKPVSTVQTRETSDTPVQKTRQEKTSAATSASVTLSDAQAKLMQPGVSDINMERVEALKTAIRNGELKMDTGKIADSLIREAQSYLQSK Native Function arises via a disorder to order transition Protein inhibitor Protein-protein binding Nuclear magnetic resonance (NMR) 298 6.2 protein sample 10 sodium phosphate buffer 10 NaCl 10 D2O 5 NaN3 0.02 General Electric Omega 500 MHz spectrometer Paper 9095196 Daughdrill GW, Chadsey MS, Karlinsey JE, Hughes KT, Dahlquist FW 1997 Nat Struct Biol 4 4 285-91 AV 7-29-2010 PubMed: 9095196 Eukaryotic translation initiation factor 4E-binding protein 1 4EBP1_HUMAN eIF4E-binding protein 1 4E-binding protein 1 4E-BP1 Phosphorylated heat- and acid-stable protein regulated by insulin 1 PHAS-I Q13541 Hs.411641 4EBP1_HUMAN 34921508 Homo sapiens (Human) 118 MSGGSSCSQTPSRAIPATRRVVLGDGVQLPPGDYSTTPGGTLFSTTPGGTRIIYDRKFLMECRNSPVTKTPPRDLPTIPGVTSPSSDEPPMEASQSHLRNSPEDKRAGGEESQFEMDI Disordered 1 118 MSGGSSCSQTPSRAIPATRRVVLGDGVQLPPGDYSTTPGGTLFSTTPGGTRIIYDRKFLMECRNSPVTKTPPRDLPTIPGVTSPSSDEPPMEASQSHLRNSPEDKRAGGEESQFEMDI Native Function arises from the disordered state Protein inhibitor Nuclear magnetic resonance (NMR) 300 6.5 NaH2P04/Na2HP04 50 NaCl 100 DTT 10 EDTA 1 NaN3 0.1 PMSF 0.1 Boehringer Mannheim protease inhibitor tablet Paper 9684899 Fletcher CM, Wagner G 1998 Protein Sci 7 7 1639-42 AV 6-28-2010 PubMed: 9684899 Glial cell line-derived neurotrophic factor GDNF_RAT GDNF Astrocyte-derived trophic factor ATF Q07731 GDNF_RAT 729568 Rattus norvegicus (Rat) 211 MKLWDVVAVCLVLLHTASAFPLPAGKRLLEAPAEDHSLGHRRVPFALTSDSNMPEDYPDQFDDVMDFIQATIKRLKRSPDKQAAALPRRERNRQAAAASPENSRGKGRRGQRGKNRGCVLTAIHLNVTDLGLGYETKEELIFRYCSGSCEAAETMYDKILKNLSRSRRLTSDKVGQACCRPVAFDDDLSFLDDSLVYHILRKHSAKRCGCI Disordered - Extended 77 113 RSPDKQAAALPRRERNRQAAAASPENSRGKGRRGQRG Engineered 1AGQA 1AGQB 1AGQC 1AGQD Relationship to function unknown Molecular assembly Protein-protein binding X-ray crystallography HEPES pH 7.0 50 soduim azide 0.02 benzamidine 0.1 PEG 6000 20 LiCl 0.8 Paper 9187648 Eigenbrot C, Gerber N 1997 Nat Struct Biol 4 6 435-8 10545102 Eketjäll S, Fainzilber M, Murray-Rust J, Ibáñez CF 1999 EMBO J 18 21 5901-10 The first identifiable residue in 1AGQ was ASN 115 in chain A, LYS 114 in chain B, GLY 117 in chain C, and GLY 117 in chain D. This supports claims in the Eigenbrot paper about dependency on the monomer. The experimental protein consisted of residues 78 - 211 of SwissProt entry Q07731. Disordered - Extended 170 173 TSDK Engineered 1AGQA 1AGQB 1AGQC 1AGQD Relationship to function unknown Unknown Unknown X-ray crystallography benzamidine 0.1 HEPES pH 7.0 50 LiCl 0.8 PEG 6000 20 soduim azide 0.02 Paper 10545102 Eketjäll S, Fainzilber M, Murray-Rust J, Ibáñez CF 1999 EMBO J 18 21 5901-10 This sequence is part of a flexible loop that connects the alpha helix region to the second finger region of the protein. The experimental protein consisted of residues 78 - 211 of SwissProt entry Q07731. Ordered 114 169 KNRGCVLTAIHLNVTDLGLGYETKEELIFRYCSGSCEAAETMYDKILKNLSRSRRL 1AGQA 1AGQB 1AGQC 1AGQD Paper 9187648 Eigenbrot C, Gerber N 1997 Nat Struct Biol 4 6 435-8 Ordered 174 211 VGQACCRPVAFDDDLSFLDDSLVYHILRKHSAKRCGCI 1AGQA 1AGQB 1AGQC 1AGQD Paper 9187648 Eigenbrot C, Gerber N 1997 Nat Struct Biol 4 6 435-8 Glucocorticoid receptor GCR_HUMAN GR Nuclear receptor subfamily 3 group C member 1 P04150 Hs.122926 GCR_HUMAN 121069 Homo sapiens (Human) 777 MDSKESLTPGREENPSSVLAQERGDVMDFYKTLRGGATVKVSASSPSLAVASQSDSKQRRLLVDFPKGSVSNAQQPDLSKAVSLSMGLYMGETETKVMGNDLGFPQQGQISLSSGETDLKLLEESIANLNRSTSVPENPKSSASTAVSAAPTEKEFPKTHSDVSSEQQHLKGQTGTNGGNVKLYTTDQSTFDILQDLEFSSGSPGKETNESPWRSDLLIDENCLLSPLAGEDDSFLLEGNSNEDCKPLILPDTKPKIKDNGDLVLSSPSNVTLPQVKTEKEDFIELCTPGVIKQEKLGTVYCQASFPGANIIGNKMSAISVHGVSTSGGQMYHYDMNTASLSQQQDQKPIFNVIPPIPVGSENWNRCQGSGDDNLTSLGTLNFPGRTVFSNGYSSPSMRPDVSSPPSSSSTATTGPPPKLCLVCSDEASGCHYGVLTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRYRKCLQAGMNLEARKTKKKIKGIQQATTGVSQETSENPGNKTIVPATLPQLTPTLVSLLEVIEPEVLYAGYDSSVPDSTWRIMTTLNMLGGRQVIAAVKWAKAIPGFRNLHLDDQMTLLQYSWMFLMAFALGWRSYRQSSANLLCFAPDLIINEQRMTLPCMYDQCKHMLYVSSELHRLQVSYEEYLCMKTLLLLSSVPKDGLKSQELFDEIRMTYIKELGKAIVKREGNSSQNWQRFYQLTKLLDSMHEVVENLLNYCFQTFLDKTMSIEFPEMLAEIITNQIPKYSNGNIKKLLFHQK Disordered - Extended 77 262 DLSKAVSLSMGLYMGETETKVMGNDLGFPQQGQISLSSGETDLKLLEESIANLNRSTSVPENPKSSASTAVSAAPTEKEFPKTHSDVSSEQQHLKGQTGTNGGNVKLYTTDQSTFDILQDLEFSSGSPGKETNESPWRSDLLIDENCLLSPLAGEDDSFLLEGNSNEDCKPLILPDTKPKIKDNGD Engineered Fragment Function arises via a disorder to order transition Molecular recognition effectors Phosphorylation Protein-DNA binding Protein-protein binding Metal binding Circular dichroism (CD) spectroscopy, far-UV 295 7 dithiothreitol 1 phosphate 3 TFE Nuclear magnetic resonance (NMR) 289 5.9 dithiothreitiol 1 phosphates 20 Paper 10196139 Baskakov IV, Kumar R, Srinivasan G, Ji YS, Bolen DW, Thompson EB 1999 J Biol Chem 274 16 10693-6 7878043 Dahlman-Wright K, Baumann H, McEwan IJ, Almlöf T, Wright AP, Gustafsson JA, Härd T 1995 Proc Natl Acad Sci U S A 92 5 1699-1703 12902338 Li G, Wang S, Gelehrter TD 2003 J Biol Chem 278 43 41779-41788 The 58 residue Tau1 core region of the disordered polypeptide from 187-244 retains 60-70% of the activity of the domain. The disordered region is devoid of structure at neutral pH in aqueous solution. The ligand-binding domain becomes notably more structured in the presence of triflouroethanol (TFE). TFE creates a more non-polar environment and favors secondary structure formation. The propensity towards alpha-helicial structure may be an important step in Tau1-mediated gene activation Disordered 1 500 MDSKESLTPGREENPSSVLAQERGDVMDFYKTLRGGATVKVSASSPSLAVASQSDSKQRRLLVDFPKGSVSNAQQPDLSKAVSLSMGLYMGETETKVMGNDLGFPQQGQISLSSGETDLKLLEESIANLNRSTSVPENPKSSASTAVSAAPTEKEFPKTHSDVSSEQQHLKGQTGTNGGNVKLYTTDQSTFDILQDLEFSSGSPGKETNESPWRSDLLIDENCLLSPLAGEDDSFLLEGNSNEDCKPLILPDTKPKIKDNGDLVLSSPSNVTLPQVKTEKEDFIELCTPGVIKQEKLGTVYCQASFPGANIIGNKMSAISVHGVSTSGGQMYHYDMNTASLSQQQDQKPIFNVIPPIPVGSENWNRCQGSGDDNLTSLGTLNFPGRTVFSNGYSSPSMRPDVSSPPSSSSTATTGPPPKLCLVCSDEASGCHYGVLTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRYRKCLQAGMNLEARKTKKKIKGI Engineered Fragment Function arises via a disorder to order transition Molecular recognition effectors Metal binding Phosphorylation Protein-DNA binding Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV 295 NaCl buffer pH 7.9 10 Tris 10 Paper 10196139 Baskakov IV, Kumar R, Srinivasan G, Ji YS, Bolen DW, Thompson EB 1999 J Biol Chem 274 16 10693-6 The sequence given in Hollenberg (1985) appears to be in error. Blasting against the Swiss-Prot sequence reveals only a 94% similarity with all the discrepancies being tyrosines replacing lysines. Glycine N-methyltransferase GNMT_RAT Folate-binding protein EC=2.1.1.20 P13255 Rn.11142 GNMT_RAT 121328 Rattus norvegicus (Rat) 292 VDSVYRTRSLGVAAEGIPDQYADGEAARVWQLYIGDTRSRTAEYKAWLLGLLRQHGCHRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYALKERWNRRKEPAFDKWVIEEANWLTLDKDVPAGDGFDAVICLGNSFAHLPDSKGDQSEHRLALKNIASMVRPGGLLVIDHKNYDYILSTGCAPPGKNIYYKSDLTKDITTSVLTVNNKAHMVTLDYTVQVPGAGRDGAPGFSKFRLSYYPHCLASFTELVQEAFGGRCQHSVLGDFKPYRPGQAYVPCYFIHVLKKTG Disordered N-terminal domain 1 40 VDSVYRTRSLGVAAEGIPDQYADGEAARVWQLYIGDTRSR Complex Mutant 1D2HA 1D2HB 1D2HC 1D2HD Methylation X-ray crystallography 93 5.6 resolution 3 ethylene glycol v/v 20 NaCl 50 sodium citrate 100 PEG 3400 10 Paper 10756111 Huang Y, Komoto J, Konishi K, Takata Y, Ogawa H, Gomi T, Fujioka M, Takusagawa F 2000 J Mol Biol 298 1 149-62 AV 6-28-2010 PubMed: 10756111 Glycyl-tRNA synthetase SYG_THET8 EC=6.1.1.14 Glycine--tRNA ligase GlyRS P56206 SYG_THET8 62296700 Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) 505 PASSLDELVALCKRRGFIFQSSEIYGGLQGVYDYGPLGVELKNNLKQAWWRRNVYERDDMEGLDASVLTHRLVLHYSGHEATFADPMVDNRITKKRYRLDHLLKEQPEEVLKRLYRAMEVEEENLHALVQAMMQAPERAGGAMTAAGVLDPASGEPGDWTPPRYFNMMFKTYVGPVEDEASLAYLRPETAQGIFVNFKNVLDATSRKLPFGIAQIGKAFRNEITPRNFIFRVREFEQMEIEYFVRPGEDEYWHRYWVEERLKWWQEMGLSRENLVPYQQPPEELAHYAKATVDILYRFPHGLEELEGIANRTDFDLGSHTKDQEALGITARVLRNEHSTQRLAYRDPETGKWFVPYVIEPSAGVDRGVLALLAEAFTREELPNGEERIVLKLKPQLAPIKVAVIPLVKNRPEITEYAKRLKARLLALGLGRVLYEDTGNIGKAYRRHDEVGTPFAVTVDYDTIGQSKDGTTRLKDTVTVRDRDTMEQIRLHVDELEGFLRERLRW Disordered insertion domain 91 158 RITKKRYRLDHLLKEQPEEVLKRLYRAMEVEEENLHALVQAMMQAPERAGGAMTAAGVLDPASGEPGD 1ATIA 1ATIB 1B76A 1B76B Relationship to function unknown Molecular assembly Protein-tRNA binding Fatty acylation (myristolation and palmitoylation) X-ray crystallography 273 ammonium sulfate 0.4 ATP 5 MgCl2 2 Paper 10064708 Arnez JG, Dock-Bregeon AC, Moras D 1999 J Mol Biol 286 5 1449-59 7556056 Logan DT, Mazauric MH, Kern D, Moras D 1995 Embo J 14 17 4156-67 The PDB chains 1B76 A and B have the disordered region spanning residues 96-158. Av 6-28-2010 PubMed: 9490048 Growth hormone receptor [Isoform 1 (GHRfl)] GHR_HUMAN GH receptor Somatotropin receptor Growth hormone-binding protein [cleavage product 1] GH-binding protein GHBP Serum-binding protein P10912-1 Hs.125180 GHR_HUMAN 121180 Homo sapiens (Human) 638 MDLWQLLLTLALAGSSDAFSGSEATAAILSRAPWSLQSVNPGLKTNSSKEPKFTKCRSPERETFSCHWTDEVHHGTKNLGPIQLFYTRRNTQEWTQEWKECPDYVSAGENSCYFNSSFTSIWIPYCIKLTSNGGTVDEKCFSVDEIVQPDPPIALNWTLLNVSLTGIHADIQVRWEAPRNADIQKGWMVLEYELQYKEVNETKWKMMDPILTTSVPVYSLKVDKEYEVRVRSKQRNSGNYGEFSEVLYVTLPQMSQFTCEEDFYFPWLLIIIFGIFGLTVMLFVFLFSKQQRIKMLILPPVPVPKIKGIDPDLLKEGKLEEVNTILAIHDSYKPEFHSDDSWVEFIELDIDEPDEKTEESDTDRLLSSDHEKSHSNLGVKDGDSGRTSCCEPDILETDFNANDIHEGTSEVAQPQRLKGEADLLCLDQKNQNNSPYHDACPATQQPSVIQAEKNKPQPLPTEGAESTHQAAHIQLSNPSSLSNIDFYAQVSDITPAGSVVLSPGQKNKAGMSQCDMHPEMVSLCQENFLMDNAYFCEADAKKCIPVAPHIKVESHIQPSLNQEDIYITTESLTTAAGRPGTGEHVPGSEMPVPDYTSIHIVQSPQGLILNATALPLPDKEFLSSCGYVSTDQLNKIMP Previous entry DP00033 has been split into polyprotein DP00033 and cleavage product DP00033_C001 Growth hormone-binding protein GHR_HUMAN GH-binding protein GHBP Serum-binding protein Cleavage product 1 of Growth hormone receptor [Isoform 1 (GHRfl)] P10912 Hs.125180 GHR_HUMAN 121180 Homo sapiens (Human) 246 FSGSEATAAILSRAPWSLQSVNPGLKTNSSKEPKFTKCRSPERETFSCHWTDEVHHGTKNLGPIQLFYTRRNTQEWTQEWKECPDYVSAGENSCYFNSSFTSIWIPYCIKLTSNGGTVDEKCFSVDEIVQPDPPIALNWTLLNVSLTGIHADIQVRWEAPRNADIQKGWMVLEYELQYKEVNETKWKMMDPILTTSVPVYSLKVDKEYEVRVRSKQRNSGNYGEFSEVLYVTLPQMSQFTCEEDFY Disordered - Extended 144 148 VSLTG Complex 1A22B Function arises via a disorder to order transition Molecular assembly Protein-protein binding X-ray crystallography 1:1 complex structure determined at 2.6 Angstroms 1:2 complex structure determined at 2.6 Angstroms Paper 9571026 Clackson T, Ultsch MH, Wells JA, de Vos AM 1998 J Mol Biol 277 5 1111-28 This region is likely stabilized upon binding of the second receptor to the growth hormone in the 1:2 complex (Clackson, 1998). Disordered - Extended 144 147 VSLT Complex 1A22B Relationship to function unknown Unknown Unknown X-ray crystallography 1:1 complex structure determined at 2.6 Angstroms 1:2 complex structure determined at 2.6 Angstroms Paper 9571026 Clackson T, Ultsch MH, Wells JA, de Vos AM 1998 J Mol Biol 277 5 1111-28 Disordered - Extended 50 62 WTDEVHHGTKNLG Complex 1HWGB 1HWGC Relationship to function unknown Unknown Unknown X-ray crystallography 291 1:1 complex crystals defracted to 2.9 Angstroms 1:2 complex crystals defracted to 2.5 Angstroms 50% saturated LiSO4 solution to stabilize Bis-Tris pH 6.25-6.75 50 LiSO4 3 microliters 1.6 MES pH 5.25 (to stabilize) 0.1 MgCl2 to stabilize 0.5 Paper 8943276 Sundstrom M, Lundqvist T, Rodin J, Giebel LB, Milligan D, Norstedt G 1996 J Biol Chem 271 50 32197-32203 Disordered - Extended 72 78 NTQEWTQ Complex 1HWGB 1HWGC Relationship to function unknown Unknown Unknown X-ray crystallography 291 1:1 complex crystals defracted to 2.9 Angstroms 1:2 complex crystals defracted to 2.5 Angstroms 50% saturated LiSO4 solution to stabilize Bis-Tris pH 6.25-6.75 50 LiSO4 3 microliters 1.6 MES pH 5.25 (to stabilize) 0.1 MgCl2 to stabilize 0.5 Paper 8943276 Sundstrom M, Lundqvist T, Rodin J, Giebel LB, Milligan D, Norstedt G 1996 J Biol Chem 271 50 32197-32203 Disordered - Extended 234 237 PQMS Complex 1HWGB 1HWGC Relationship to function unknown Unknown Unknown X-ray crystallography 291 1:1 complex crystals defracted to 2.9 Angstroms 1:2 complex crystals defracted to 2.5 Angstroms 50% saturated LiSO4 solution to stabilize Bis-Tris pH 6.25-6.75 50 LiSO4 3 microliters 1.6 MES pH 5.25 (to stabilize) 0.1 MgCl2 to stabilize 0.5 Paper 8943276 Sundstrom M, Lundqvist T, Rodin J, Giebel LB, Milligan D, Norstedt G 1996 J Biol Chem 271 50 32197-32203 Disordered - Extended 1 32 FSGSEATAAILSRAPWSLQSVNPGLKTNSSKE Complex 1A22B Relationship to function unknown Unknown Unknown X-ray crystallography 1:1 complex structure determined at 2.6 Angstroms 1:2 complex structure determined at 2.6 Angstroms Paper 9571026 Clackson T, Ultsch MH, Wells JA, de Vos AM 1998 J Mol Biol 277 5 1111-28 Disordered - Extended 52 60 DEVHHGTKN Complex 1A22B Relationship to function unknown Unknown Unknown X-ray crystallography 1:1 complex structure determined at 2.6 Angstroms 1:2 complex structure determined at 2.6 Angstroms Paper 9571026 Clackson T, Ultsch MH, Wells JA, de Vos AM 1998 J Mol Biol 277 5 1111-28 Disordered - Extended 238 238 Q Complex 1A22B Relationship to function unknown Unknown Unknown X-ray crystallography 1:1 complex structure determined at 2.6 Angstroms 1:2 complex structure determined at 2.6 Angstroms Paper 9571026 Clackson T, Ultsch MH, Wells JA, de Vos AM 1998 J Mol Biol 277 5 1111-28 Disordered - Extended 222 226 YGEFS Complex 1A22B Relationship to function unknown Unknown Unknown X-ray crystallography 1:1 complex structure determined at 2.6 Angstroms 1:2 complex structure determined at 2.6 Angstroms X-ray crystallography 5.5 1:2 complex structure determined at 2.8 Angstroms K2AuCl4 K2PtCl4 saturated ammonium sulfate 40 sodium acetate 0.1 Paper 9571026 Clackson T, Ultsch MH, Wells JA, de Vos AM 1998 J Mol Biol 277 5 1111-28 1549776 de Vos AM, Ultsch M, Kossiakoff AA 1992 Science 255 5042 306-312 Residues 222-226 had poor electron density and were not modeled in the crystal structure (Clackson, 1998). Disordered - Extended 73 78 TQEWTQ Complex 1A22B Relationship to function unknown Unknown Unknown X-ray crystallography 1:1 complex structure determined at 2.6 Angstroms 1:2 complex structure determined at 2.6 Angstroms X-ray crystallography 5.5 1:2 complex structure determined at 2.8 Angstroms K2AuCl4 K2PtCl4 saturated ammonium sulfate 40 sodium acetate 0.1 Paper 9571026 Clackson T, Ultsch MH, Wells JA, de Vos AM 1998 J Mol Biol 277 5 1111-28 1549776 de Vos AM, Ultsch M, Kossiakoff AA 1992 Science 255 5042 306-312 The binding proteins of the 1:2 (hormone:binding protein) complex are hGHbp I and hGHbp II. De Vos found this region to be disordered in hGHbp I (de Vos 1992). Disordered - Extended 1 31 FSGSEATAAILSRAPWSLQSVNPGLKTNSSK Complex 1HWGB 1HWGC 1HWHB Relationship to function unknown Unknown Unknown X-ray crystallography 291 1:1 complex crystals defracted to 2.9 Angstroms 1:2 complex crystals defracted to 2.5 Angstroms 50% saturated LiSO4 solution to stabilize Bis-Tris pH 6.25-6.75 50 LiSO4 3 microliters 1.6 MES pH 5.25 (to stabilize) 0.1 MgCl2 to stabilize 0.5 Paper 8943276 Sundstrom M, Lundqvist T, Rodin J, Giebel LB, Milligan D, Norstedt G 1996 J Biol Chem 271 50 32197-32203 The N-terminus region of the hGHbp, for both the native 1:2 complex and the mutated 1:1 complex, had missing electron density for the first 31 residues (Sundstrom, 1996). Disordered - Extended 1 5 FSGSE Complex 1A22B Relationship to function unknown Unknown Unknown X-ray crystallography 1:1 complex structure determined at 2.6 Angstroms 1:2 complex structure determined at 2.6 Angstroms Paper 9571026 Clackson T, Ultsch MH, Wells JA, de Vos AM 1998 J Mol Biol 277 5 1111-28 Disordered - Extended 1 30 FSGSEATAAILSRAPWSLQSVNPGLKTNSS Complex Relationship to function unknown Unknown Unknown X-ray crystallography 5.5 1:2 complex structure determined at 2.8 Angstroms K2AuCl4 K2PtCl4 saturated ammonium sulfate 40 sodium acetate 0.1 Paper 1549776 de Vos AM, Ultsch M, Kossiakoff AA 1992 Science 255 5042 306-312 The binding proteins of the 1:2 (hormone:binding protein) complex are hGHbp I and hGHbp II. De Vos found this region to be disordered in hGHbp II (de Vos 1992). Disordered - Extended 54 60 VHHGTKN Complex Relationship to function unknown Unknown Unknown X-ray crystallography 5.5 1:2 complex structure determined at 2.8 Angstroms K2AuCl4 K2PtCl4 saturated ammonium sulfate 40 sodium acetate 0.1 Paper 1549776 de Vos AM, Ultsch M, Kossiakoff AA 1992 Science 255 5042 306-312 The binding proteins of the 1:2 (hormone:binding protein) complex are hGHbp I and hGHbp II. De Vos found this region to be disordered in hGHbp II (de Vos 1992). Disordered - Extended 73 75 TQE Complex Relationship to function unknown Unknown Unknown X-ray crystallography 5.5 1:2 complex structure determined at 2.8 Angstroms K2AuCl4 K2PtCl4 saturated ammonium sulfate 40 sodium acetate 0.1 Paper 1549776 de Vos AM, Ultsch M, Kossiakoff AA 1992 Science 255 5042 306-312 In the de Vos reference, (de Vos_Science_255_306-312), they refer to both of the binding proteins of the 1:2 (hormone:binding proteins) complex. They are named hGHbp I and hGHbp II. De Vos found this region to be disordered in the hGHbp II. Disordered - Extended 1 28 FSGSEATAAILSRAPWSLQSVNPGLKTN Complex Relationship to function unknown Unknown Unknown X-ray crystallography 5.5 1:2 complex structure determined at 2.8 Angstroms K2AuCl4 K2PtCl4 saturated ammonium sulfate 40 sodium acetate 0.1 Paper 1549776 de Vos AM, Ultsch M, Kossiakoff AA 1992 Science 255 5042 306-312 In the de Vos reference, (de Vos_Science_255_306-312), they refer to both of the binding proteins of the 1:2 (hormone:binding proteins) complex. They are named hGHbp I and hGHbp II. De Vos found this region to be disordered in the hGHbp I. Disordered - Extended 55 58 HHGT Complex Relationship to function unknown Unknown Unknown X-ray crystallography 5.5 1:2 complex structure determined at 2.8 Angstroms K2AuCl4 K2PtCl4 saturated ammonium sulfate 40 sodium acetate 0.1 Paper 1549776 de Vos AM, Ultsch M, Kossiakoff AA 1992 Science 255 5042 306-312 The binding proteins of the 1:2 (hormone:binding protein) complex are hGHbp I and hGHbp II. De Vos found this region to be disordered in hGHbp I (de Vos 1992). Disordered - Extended 235 238 QMSQ Complex Relationship to function unknown Unknown Unknown X-ray crystallography 5.5 1:2 complex structure determined at 2.8 Angstroms K2AuCl4 K2PtCl4 saturated ammonium sulfate 40 sodium acetate 0.1 Paper 1549776 de Vos AM, Ultsch M, Kossiakoff AA 1992 Science 255 5042 306-312 The binding proteins of the 1:2 (hormone:binding protein) complex are hGHbp I and hGHbp II. De Vos found this region to be disordered in hGHbp I (de Vos 1992). Human Growth Hormone binding protein (hGHbp) exists as a fully functional 238 residue protein in serum. These 238 residues are a fragment of a larger protein, human Growth Hormone Receptor, (hGH receptor), which has 638 residues. hGH consists of three domains; an extracellular binding domain- located outside of the membrane, a transmembrane domain, and a cytosolic domain. “It has been proposed that the hGH binding protein in serum derives from proteolysis of the membrane-bound form of the receptor near the transmembrane anchor" (Fuh, 1990). Residues 73-78 were not modeled in the crystal structure due to poor electron density (Clackson, 1998). There is some disagreement about the whether the protein is 238 residues long, as it is when attached to the entire hGH receptor, or if it is 246 residues long, as it is when it is found freely in serum. However, the nine residue segment was shown to be not essential for function (Fuh, 1990). The UniProt entry for this protein mentions that one isoform has a different function: upregulation of the production of GHBP and as a negative inhibitor of GH signaling. The SwissProt entry states that the first 18 residues of the amino acid sequence form a signal sequence and are not considered part of the extracellular binding domain. Therefore, the extracellular binding domain starts at residue 19 and extends through residue 264. This sequence is 246 residues long. One human growth hormone binding protein (hGHbp) binds to a human growth hormone (hGH) followed by the binding of a second hGHbp to the same hGH. After the second hGHbp binds the two hGHbps (I and II) dimerize. Additional UniGene ID, Hs.684631 Previous entry DP00033 has been split into polyprotein DP00033 and cleavage product DP00033_C001 Attachment protein G3P G3P_BPFD Gene 3 protein G3P Minor phage coat protein G3P P03661 G3P_BPFD 116658 Enterobacteria phage fd (Bacteriophage fd) 424 MKKLLFAIPLVVPFYSHSAETVESCLAKPHTENSFTNVWKDDKTLDRYANYEGCLWNATGVVVCTGDETQCYGTWVPIGLAIPENEGGGSEGGGSEGGGSEGGGTKPPEYGDTPIPGYTYINPLDGTYPPGTEQNPANPNPSLEESQPLNTFMFQNNRFRNRQGALTVYTGTVTQGTDPVKTYYQYTPVSSKAMYDAYWNGKFRDCAFHSGFNEDPFVCEYQGQSSDLPQPPVNAGGGSGGGSGGGSEGGGSEGGGSEGGGSEGGGSGGGSGSGDFDYEKMANANKGAMTENADENALQSDAKGKLDSVATDYGAAIDGFIGDVSGLANGNGATGDFAGSNSQMAQVGDGDNSPLMNNFRQYLPSLPQSVECRPYVFGAGKPYEFSIDCDKINLFRGVFAFLLYVATFMYVFSTFANILRNKES Disordered linker 67 90 DETQCYGTWVPIGLAIPENEGGGS Native 1G3PA Flexible linkers/spacers X-ray crystallography 100 wavelength 0.947 Paper 10329170 Holliger P, Riechmann L, Williams RL 1999 J Mol Biol 288 4 649-57 10756036 Nilsson N, Malmborg AC, Borrebaeck CA 2000 J Virol 74 9 4229-35 AV 6-28-2010 PubMed: 10756036 Guanine nucleotide-binding protein G(i), alpha-1 subunit GNAI1_RAT Adenylate cyclase-inhibiting G alpha protein G protein alpha G(i) P10824 Rn.11391 GNAI1_RAT 121020 Rattus norvegicus (Rat) 354 MGCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDAARADDARQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF Disordered N-terminal 1 31 MGCTLSAEDKAAVERSKMIDRNLREDGEKAA Native Function arises via a disorder to order transition Molecular recognition effectors X-ray crystallography 280 CHESS F1 beam wavelength 0.91 Paper 8073283 Coleman DE, Berghuis AM, Lee E, Linder ME, Gilman AG, Sprang SR 1994 Science 265 5177 1405-12 Disordered C-terminal 344 354 IKNNLKDCGLF Native Function arises via a disorder to order transition Molecular recognition effectors X-ray crystallography 280 CHESS F1 beam wavelength 0.91 Paper 8073283 Coleman DE, Berghuis AM, Lee E, Linder ME, Gilman AG, Sprang SR 1994 Science 265 5177 1405-12 Av 6-28-2010 PubMed: 8073283 Heat shock factor protein HSF_KLULA HSF Heat shock transcription factor HSTF P22121 HSF_KLULA 123686 Kluyveromyces lactis (Yeast) (Candida sphaerica) 677 MGHNDSVETMDEISNPNNILLPHDGTGLDATGISGSQEPYGMVDVLNPDSLKDDSNVDEPLIEDIVNPSLDPEGVVSAEPSNEVGTPLLQQPISLDHVITRPASAGGVYSIGNSSTSSAAKLSDGDLTNATDPLLNNAHGHGQPSSESQSHSNGYHKQGQSQQPLLSLNKRKLLAKAHVDKHHSKKKLSTTRARPAFVNKLWSMVNDKSNEKFIHWSTSGESIVVPNRERFVQEVLPKYFKHSNFASFVRQLNMYGWHKVQDVKSGSMLSNNDSRWEFENENFKRGKEYLLENIVRQKSNTNILGGTTNAEVDIHILLNELETVKYNQLAIAEDLKRITKDNEMLWKENMMARERHQSQQQVLEKLLRFLSSVFGPNSAKTIGNGFQPDLIHELSDMQVNHMSNNNHNNTGNINPNAYHNETDDPMANVFGPLTPTDQGKVPLQDYKLRPRLLLKNRSMSSSSSSNLNQRQSPQNRIVGQSPPPQQQQQQQQQQGQPQGQQFSYPIQGGNQMMNQLGSPIGTQVGSPVGSQYGNQYGNQYSNQFGNQLQQQTSRPALHHGSNGEIRELTPSIVSSDSPDPAFFQDLQNNIDKQEESIQEIQDWITKLNPGPGEDGNTPIFPELNMPSYFANTGGSGQSEQPSDYGDSQIEELRNSRLHEPDRSFEEKNNGQKRRRAA Disordered 268 271 MLSN Fragment Transactivation (transcriptional activation) Protein-DNA binding X-ray crystallography 281 Ammonium acetate 200 PEG4000 25-30% Sodium acetate pH 4.6 100 Paper 8284672 Harrison CJ, Bohm AA, Nelson HC 1994 Science 263 5144 224-7 The fragment used for solution structure determination was the DNA-binding domain.(aa194-aa282) Disordered Omega loop 217 222 STSGES Fragment 2HSFA Protein-DNA binding Transactivation (transcriptional activation) Nuclear magnetic resonance (NMR) 298 3.4 H2O/D2O 90/10 Potassium phosphate buffer 10 Protein (2-4mM) Paper 7849597 Damberger FF, Pelton JG, Harrison CJ, Nelson HC, Wemmer DE 1994 Protein Sci 3 10 1806-21 The fragment used for solution structure determination was the DNA-binding domain.(aa194-aa282) Disordered L1 260 276 VQDVKSGSMLSNNDSRW Fragment 2HSFA Transactivation (transcriptional activation) Protein-DNA binding Nuclear magnetic resonance (NMR) 298 3.4 H2O/D2O 90/10 Potassium phosphate buffer 10 protein 2-4 mM Paper 7849597 Damberger FF, Pelton JG, Harrison CJ, Nelson HC, Wemmer DE 1994 Protein Sci 3 10 1806-21 The fragment used for solution structure determination was the DNA-binding domain.(aa194-aa282) Disordered N-terminal 1 195 MGHNDSVETMDEISNPNNILLPHDGTGLDATGISGSQEPYGMVDVLNPDSLKDDSNVDEPLIEDIVNPSLDPEGVVSAEPSNEVGTPLLQQPISLDHVITRPASAGGVYSIGNSSTSSAAKLSDGDLTNATDPLLNNAHGHGQPSSESQSHSNGYHKQGQSQQPLLSLNKRKLLAKAHVDKHHSKKKLSTTRARP Native Function arises via a disorder to order transition Protein-DNA binding Transactivation (transcriptional activation) Nuclear magnetic resonance (NMR) 3.4 D2O 10 H2O 90 KH2PO4 10 Protein 3-5 mM Nuclear magnetic resonance (NMR) 5.75 D2O 10 H2O 90 KH2PO4 10 Protein 3-5 mM Circular dichroism (CD) spectroscopy, far-UV 298 7 sodium phosphate 25 Paper 8745404 Cho HS, Liu CW, Damberger FF, Pelton JG, Nelson HC, Wemmer DE 1996 Protein Sci 5 2 262-9 In the Damberger and Harrison papers the sequences listed are one residue off from the referenced sequence. Regions 2 and 3 are shown as residues 217-222 and 261-277 respectively, but the sequences correspond to residues 216-221 and 260-276 in the referenced sequence. Region 4 is shown as residues 269-272 in the Harrison paper, but correspond to residues 268-271 in the referenced sequence. AV 6-28-2010 PubMed: 1899375 Probable peroxiredoxin TDXH_AERPE EC 1.11.1.15 Q9Y9L0 TDXH_AERPE 14285795 Aeropyrum pernix 250 MPGSIPLIGERFPEMEVTTDHGVIKLPDHYVSQGKWFVLFSHPADFTPVCTTEFVSFARRYEDFQRLGVDLIGLSVDSVFSHIKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAESATHTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKALKLGDSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARMESGQYRCLDWWFCWDTPASRDDVEEARRYLRRAAEKPAKLLYEEARTHLH Disordered N-terminal 2 8 PGSIPLI Monomeric 2CV4A Substrate/ligand binding Apoptosis Regulation X-ray crystallography 291 Tris-HCl pH 8.0 20 NaCl 150 DTT 1 Paper 16214169 Mizohata E, Sakai H, Fusatomi E, Terada T, Murayama K, Shirouzu M, Yokoyama S 2005 J Mol Biol Disordered 197 206 RARMESGQYR Monomeric 2CV4A Substrate/ligand binding Apoptosis Regulation X-ray crystallography 291 DTT 1 NaCl 150 Tris-HCl pH 8.0 20 Paper 16214169 Mizohata E, Sakai H, Fusatomi E, Terada T, Murayama K, Shirouzu M, Yokoyama S 2005 J Mol Biol Disordered C-terminal tail 235 243 EKPAKLLYE Monomeric 2CV4A Substrate/ligand binding Apoptosis Regulation X-ray crystallography 291 DTT 1 NaCl 150 Tris-HCl pH 8.0 20 Paper 16214169 Mizohata E, Sakai H, Fusatomi E, Terada T, Murayama K, Shirouzu M, Yokoyama S 2005 J Mol Biol AV 6-28-2010 PubMed: 16214169 Non-histone chromosomal protein HMG-14 HMGN1_BOVIN High-mobility group nucleosome-binding domain-containing protein 1 P02316 Bt.87121 HMGN1_BOVIN 108935921 Bos taurus (Bovine) 100 PKRKVSSAEGAAKEEPKRRSARLSAKPAPAKVETKPKKAAGKDKSSDKKVQTKGKRGAKGKQAEVANQETKEDLPAENGETKNEESPASDEAEEKEAKSD Disordered - Extended 1 99 PKRKVSSAEGAAKEEPKRRSARLSAKPAPAKVETKPKKAAGKDKSSDKKVQTKGKRGAKGKQAEVANQETKEDLPAENGETKNEESPASDEAEEKEAKS Native Function arises from the disordered state Function arises via a disorder to order transition Molecular recognition effectors Molecular assembly Acetylation Phosphorylation Protein-DNA binding Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV Nuclear magnetic resonance (NMR) Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) Paper 6273163 Cary PD, Crane-Robinson C, Bradbury EM, Dixon GH 1981 Eur J Biochem 119 3 545-51 Non-histone chromosomal protein HMG-17 HMGN2_HUMAN High-mobility group 17 High-mobility group nucleosome-binding domain-containing protein 2 High-mobility group nucleosomal binding domain 2 High-mobility group protein N2 HMGN2 P05204 Hs.181163 HMGN2_HUMAN 123106 Homo sapiens (Human) 89 PKRKAEGDAKGDKAKVKDEPQRRSARLSAKPAPPKPEPKPKKAPAKKGEKVPKGKKGKADAGKEGNNPAENGDAKTDQAQKAEGAGDAK Disordered - Extended 1 89 PKRKAEGDAKGDKAKVKDEPQRRSARLSAKPAPPKPEPKPKKAPAKKGEKVPKGKKGKADAGKEGNNPAENGDAKTDQAQKAEGAGDAK Native Function arises via a disorder to order transition Molecular recognition effectors Molecular assembly Acetylation Phosphorylation Protein-DNA binding Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV protein concentration 0.08 Nuclear magnetic resonance (NMR) Small-angle X-ray scattering (SAXS) wavelength: 0.8 nm Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) 6.8 NaCl salt 1 protein concentration 14 Paper 565710 Abercrombie BD, Kneale GG, Crane-Robinson C, Bradbury EM, Goodwin GH, Walker JM, Johns EW 1978 Eur J Biochem 84 1 173-7 High mobility group protein HMG-I/HMG-Y HMGA1_HUMAN HMG-I(Y) High mobility group A non-histone chromosomal proteins High mobility group AT-hook protein 1 High mobility group protein A1 High mobility group protein R P17096 Hs.518805 HMGA1_HUMAN 123377 Homo sapiens (Human) 107 MSESSSKSSQPLASKQEKDGTEKRGRGRPRKQPPVSPGTALVGSQKEPSEVPTPKRPRGRPKGSKNKGAAKTRKTTTTPGRKPRGRPKKLEKEEEEGISQESSEEEQ Disordered - Extended 1 107 MSESSSKSSQPLASKQEKDGTEKRGRGRPRKQPPVSPGTALVGSQKEPSEVPTPKRPRGRPKGSKNKGAAKTRKTTTTPGRKPRGRPKKLEKEEEEGISQESSEEEQ 2EZDA 2EZEA 2EZFA 2EZGA Function arises from the disordered state Function arises via a disorder to order transition Molecular assembly Protein-DNA binding Protein-protein binding Nuclear magnetic resonance (NMR) Circular dichroism (CD) spectroscopy, far-UV Paper 7559428 Wang, D. Z. Ray, P. Boothby, M. 1995 J Biol Chem 270 39 22924-22932 10372360 Reeves, R. Nissen, M. S. 1996 Methods of Enzymology 304 155-188 11498590 Munshi N, Agalioti T, Lomvardas S, Merika M, Chen G, Thanos D 2001 Science 293 5532 1133-1136 11593421 Pierantoni GM, Fedele M, Pentimalli F, Benvenuto G, Pero R, Viglietto G, Santoro M, Chiariotti L, Fusco A 2001 Oncogene 20 43 6132-6141 Additional UniGene ID: Hs.703764 High mobility group-T protein HMGT_ONCMY HMG-T HMG-T1 HMG-1 P07746 Omy.32291 HMGT_ONCMY 123382 Oncorhynchus mykiss (Rainbow trout)(Salmo gairdneri) 204 MGKDPRKPRGKMSSYAYFVQTRREEHKKKHPEASVNFSEFSKKCSERWKTMSAKEKGKFEDLAKLDKVRYEREMRSYIPPKGEKKKRFKDPNAPKRPSSAFFIFCADFRPQVKGETPGLSIGDVAKKLGEKWNNLTAEDKVPYEKKASRLKEKYEKDITAYRNKGKVPVSMPAKAAAPAKDDDDDDDDDDDDEDDDDDDDEDDE Disordered - Extended 1 204 MGKDPRKPRGKMSSYAYFVQTRREEHKKKHPEASVNFSEFSKKCSERWKTMSAKEKGKFEDLAKLDKVRYEREMRSYIPPKGEKKKRFKDPNAPKRPSSAFFIFCADFRPQVKGETPGLSIGDVAKKLGEKWNNLTAEDKVPYEKKASRLKEKYEKDITAYRNKGKVPVSMPAKAAAPAKDDDDDDDDDDDDEDDDDDDDEDDE Function arises via a disorder to order transition Molecular assembly Protein-DNA binding Circular dichroism (CD) spectroscopy, far-UV 2 Nuclear magnetic resonance (NMR) Paper 6273163 Cary PD, Crane-Robinson C, Bradbury EM, Dixon GH 1981 Eur J Biochem 119 3 545-51 Non-histone chromosomal protein H6 H6_ONCMY Histone T High mobility group H6 Oncorhyncin-3 [cleavage product 1] Oncorhyncin III P02315 H6_ONCMY 462245 Oncorhynchus mykiss (Rainbow trout)(Salmo gairdneri) 70 MPKRKSATKGDEPARRSARLSARPVPKPAAKPKKAAAPKKAVKGKKAAENGDAKAEAKVQAAGDGAGNAK Disordered - Extended 2 70 PKRKSATKGDEPARRSARLSARPVPKPAAKPKKAAAPKKAVKGKKAAENGDAKAEAKVQAAGDGAGNAK Function arises via a disorder to order transition Molecular assembly Protein-DNA binding Circular dichroism (CD) spectroscopy, far-UV Nuclear magnetic resonance (NMR) Paper 6273163 Cary PD, Crane-Robinson C, Bradbury EM, Dixon GH 1981 Eur J Biochem 119 3 545-51 Disordered residues lie within the region corresponding to Oncorhyncin III, however, there are no references to confirm that the cleavage product is disordered. Protein tonB TONB_ECOLI P02929 TONB_ECOLI 401196 Escherichia coli (strain K12) 239 MTLDLPRRFPWPTLLSVCIHGAVVAGLLYTSVHQVIELPAPAQPISVTMVTPADLEPPQAVQPPPEPVVEPEPEPEPIPEPPKEAPVVIEKPKPKPKPKPKPVKKVQEQPKRDVKPVESRPASPFENTAPARLTSSTATAATSKPVTSVASGPRALSRNQPQYPARAQALRIEGQVKVKFDVTPDGRVDNVQILSAKPANMFEREVKNAMRRWRYEPGKPGSGIVVNILFKINGTTEIQ Disordered N-terminus of the C-terminal domain 103 151 VKKVQEQPKRDVKPVESRPASPFENTAPARLTSSTATAATSKPVTSVAS Fragment Monomeric 1XX3A Metal binding Protein-protein binding Nuclear magnetic resonance (NMR) 298 7 Tris 50 NaCl 100 Paper 15644214 Peacock RS, Weljie AM, Howard SP, Price FD, and Vogel HJ 2005 J Mol Biol 345 5 1185-97 The protein sequence referenced in the paper matches 98% with the Swiss-Prot sequence with discrepancies at amino acids 113, 159, 186 and an additional 5-amino acid initiation complex tagged at the beginning. AV 6-28-2010 PubMed: 6310567 Histone H5 H5_CHICK P02259 Gga.16744 H5_CHICK 122112 Gallus gallus (Chicken) 189 TESLVLSPAPAKPKRVKASRRSASHPTYSEMIAAAIRAEKSRGGSSRQSIQKYIKSHYKVGHNADLQIKLSIRRLLAAGVLKQTKGVGASGSFRLAKSDKAKRSPGKKKKAVRRSTSPKKAARPRKARSPAKKPKATARKARKKSRASPKKAKKPKTVKAKSRKASKAKKVKRSKPRAKSGARKSPKKK Disordered - Extended 1 21 TESLVLSPAPAKPKRVKASRR Relationship to function unknown Unknown Unknown X-ray crystallography 8.2 phosphate 2.2 Sensitivity to proteolysis Paper 2181148 Graziano, V. Gerchman, S. E. Wonacott, A. J. Sweet, R. M. Wells, J. R. White, S. W. Ramakrishnan, V. 1990 J Mol Biol 212 2 253-257 Disordered - Extended 101 185 AKRSPGKKKKAVRRSTSPKKAARPRKARSPAKKPKATARKARKKSRASPKKAKKPKTVKAKSRKASKAKKVKRSKPRAKSGARKS Function arises via a disorder to order transition Molecular assembly Protein-DNA binding X-ray crystallography 8.2 phosphate 2.2 Sensitivity to proteolysis Paper 2181148 Graziano, V. Gerchman, S. E. Wonacott, A. J. Sweet, R. M. Wells, J. R. White, S. W. Ramakrishnan, V. 1990 J Mol Biol 212 2 253-257 Ordered 21 100 RSASHPTYSEMIAAAIRAEKSRGGSSRQSIQKYIKSHYKVGHNADLQIKLSIRRLLAAGVLKQTKGVGASGSFRLAKSDK Function arises from the ordered state Molecular assembly Protein-DNA binding Paper 2181148 Graziano, V. Gerchman, S. E. Wonacott, A. J. Sweet, R. M. Wells, J. R. White, S. W. Ramakrishnan, V. 1990 J Mol Biol 212 2 253-257 Hypoxanthine-guanine phosphoribosyltransferase Q27796_TRYCR HGPRTase Guanine phosphoribosyltransferase Hypoxanthine phosphoribosyltransferase HPRT IMP diphosphorylase IMP pyrophosphorylase Transphosphoribosidase Q27796 Q27796_TRYCR 74967377 Trypanosoma cruzi 220 PREYEFAEKILFTEEEIRTRIKEVAKRIADDYKGKGLRPYVNPLVLISVLKGSFMFTADLCRALCDFNVPVRMEFICVSSYGEGLTSSGQVRMLLDTRHSIEGHHVLIVEDIVDTALTLNYLYHMYFTRRPASLKTVVLLDKREGRRVPFSADYVVANIPNAFVIGYGLDYDDTYRELRDIVVLRPEVYAEREAARQKKQRAIGSADTDRDAKREFHSKY Disordered - Extended 191 220 EREAARQKKQRAIGSADTDRDAKREFHSKY 1TC1A Relationship to function unknown Unknown Unknown X-ray crystallography Paper 9790669 Focia PJ, Craig SP 3rd, Nieves-Alicea R, Fletterick RJ, Eakin AE 1998 Biochemistry 37 43 15066-15075 Ordered 5 190 EFAEKILFTEEEIRTRIKEVAKRIADDYKGKGLRPYVNPLVLISVLKGSFMFTADLCRALCDFNVPVRMEFICVSSYGEGLTSSGQVRMLLDTRHSIEGHHVLIVEDIVDTALTLNYLYHMYFTRRPASLKTVVLLDKREGRRVPFSADYVVANIPNAFVIGYGLDYDDTYRELRDIVVLRPEVYA Paper 9790669 Focia PJ, Craig SP 3rd, Nieves-Alicea R, Fletterick RJ, Eakin AE 1998 Biochemistry 37 43 15066-15075 This is subunit I of the protein. Lymphoid enhancer-binding factor 1 LEF1_RAT LEF-1 Q9QXN1 Rn.21926 LEF1_RAT 8928168 Rattus norvegicus (Rat) 397 MPQLSGGGGGGDPELCATDEMIPFKDEGDPQKEKIFAEISHPEEEGDLADIKSSLVNESEIIPASNGHEVVGQTQSSQEPYHDKAREHPDDGKHPDGGLYNKGPSYSSYSGYIMMPNMNSDPYMSNGSLSPPIPRTSNKVPVVQPSHAVHPLTPLITYSDEHFSPGSHPSHIPSEVNPKQGMSRHPPAPEMPTFYPLSPGGVGQITPPLGWQGQPVYPITGGFRQAYPSSLSGDTSMSRFSHHMIPGPPGPHTTGIPHPAIVTPQVKQEHPHTDSDLMHVKPEHEQRKEQEPKRPHIKKPLNAFMLYMKEMRANVVAECTLKESAAINQILGRRWHALSREEQAKYYELARKERQLHMQLYPGWSARDNYGKKKKRKREKLQESTSGTGPRMTAAYI Disordered - Extended 296 397 HIKKPLNAFMLYMKEMRANVVAECTLKESAAINQILGRRWHALSREEQAKYYELARKERQLHMQLYPGWSARDNYGKKKKRKREKLQESTSGTGPRMTAAYI Function arises via a disorder to order transition DNA bending Protein-DNA binding Nuclear magnetic resonance (NMR) Paper 7651541 Love JJ, Li X, Case DA, Giese K, Grosschedl R, Wright PE 1995 Nature 376 6543 791-795 Myelin basic protein MBP_BOVIN MBP Myelin A1 protein 20 kDa microtubule stabilizing protein P02687 Bt.64741 MBP_BOVIN 126796 Bos taurus (Bovine) 169 AAQKRPSQRSKYLASASTMDHARHGFLPRHRDTGILDSLGRFFGSDRGAPKRGSGKDGHHAARTTHYGSLPQKAQGHRPQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQKPGFGYGGRASDYKSAHKGLKGHDAQGTLSKIFKLGGRDSRSGSPMARR Disordered - Extended 1 169 AAQKRPSQRSKYLASASTMDHARHGFLPRHRDTGILDSLGRFFGSDRGAPKRGSGKDGHHAARTTHYGSLPQKAQGHRPQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQKPGFGYGGRASDYKSAHKGLKGHDAQGTLSKIFKLGGRDSRSGSPMARR Function arises via a disorder to order transition Molecular assembly Protein-lipid interaction Circular dichroism (CD) spectroscopy, far-UV Paper 10394626 Polverini, E. Fasano, A. Zito, F. Riccio, P. Cavatorta, P. 1999 Eur Biophys J 28 4 351-355 Protein Nef NEF_HV1BR Negative factor F-protein 3'ORF C-terminal core protein [cleavage product 1] P03406 NEF_HV1BR 128023 Human immunodeficiency virus type 1 (isolate BRU/LAI group M subtype B) (HIV-1) 206 MGGKWSKSSVVGWPTVRERMRRAEPAADGVGAASRDLEKHGAITSSNTAATNAACAWLEAQEEEEVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPGPGVRYPLTFGWCYKLVPVEPDKVEEANKGENTSLLHPVSLHGMDDPEREVLEWRFDSRLAFHHVARELHPEYFKNC Disordered - Extended 149 178 EPDKVEEANKGENTSLLHPVSLHGMDDPER 1AVVA 1AVZA 1EFNA 1QA4A Relationship to function unknown Unknown Protein-protein binding Nuclear magnetic resonance (NMR) X-ray crystallography Paper 9351809 Arold S, Franken P, Strub MP, Hoh F, Benichou S, Benarous R, Dumas C 1997 Structure 5 10 1361-72 This region was disordered according to the PDB files. Disordered - Extended 204 206 KNC 1AVVA 1AVZA 1EFNA 1QA4A Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) X-ray crystallography Paper 9351809 Arold S, Franken P, Strub MP, Hoh F, Benichou S, Benarous R, Dumas C 1997 Structure 5 10 1361-72 This region was disordered according to the PDB files. Disordered - Extended 148 178 VEPDKVEEANKGENTSLLHPVSLHGMDDPER 1AVVA 1AVZA 1EFNA 1QA4A Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) X-ray crystallography Paper 11406408 Arold ST, Baur AS 2001 Trends Biochem Sci 26 6 356-63 Ordered 71 147 TPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPGPGVRYPLTFGWCYKLVP 1AVVA Nuclear magnetic resonance (NMR) X-ray crystallography Paper 11406408 Arold ST, Baur AS 2001 Trends Biochem Sci 26 6 356-63 Ordered 179 203 EVLEWRFDSRLAFHHVARELHPEYF 1AVVA Nuclear magnetic resonance (NMR) X-ray crystallography Paper 11406408 Arold ST, Baur AS 2001 Trends Biochem Sci 26 6 356-63 Disordered - Extended 1 70 MGGKWSKSSVVGWPTVRERMRRAEPAADGVGAASRDLEKHGAITSSNTAATNAACAWLEAQEEEEVGFPV 1AVVA 1AVZA 1EFNA 1QA4A Function arises from the disordered state Function arises via a disorder to order transition Molecular assembly Entropic chain Regulation of proteolysis in vivo Protein-protein binding Protein-lipid interaction Flexible linkers/spacers Phosphorylation Fatty acylation (myristolation and palmitoylation) Nuclear magnetic resonance (NMR) X-ray crystallography Paper 11406408 Arold ST, Baur AS 2001 Trends Biochem Sci 26 6 356-63 Disordered - Extended 1 73 MGGKWSKSSVVGWPTVRERMRRAEPAADGVGAASRDLEKHGAITSSNTAATNAACAWLEAQEEEEVGFPVTPQ 1AVVA 1AVZA 1EFNA 1QA4A Function arises from the disordered state Function arises via a disorder to order transition Molecular assembly Entropic chain Regulation of proteolysis in vivo Protein-protein binding Protein-lipid interaction Flexible linkers/spacers Phosphorylation Fatty acylation (myristolation and palmitoylation) Nuclear magnetic resonance (NMR) X-ray crystallography Paper 9351809 Arold S, Franken P, Strub MP, Hoh F, Benichou S, Benarous R, Dumas C 1997 Structure 5 10 1361-72 This region was disordered according to the PDB files. Additional UniProt ID: Q71VG3 Myelin transcription factor 1-like protein MYT1L_RAT MyT1L protein Neural zinc finger factor 1 NZF-1 P70475 Rn.10559 MYT1L_RAT 76363255 Rattus norvegicus (Rat) 1187 MDVDAEEKRHRTRSKGVRVPVEPAIQELFSCPTPGCDGTGHVSGKYARHRSVYGCPLAKKRKTQDKQPQEPAPKRKPFAVKADSSSVDECYESDGTEDMDDKEEDDDEEFSEDNDEQGDDDDEDEVDREDEEEIEEEDDEDDEDDDDGDDVEEEEDDDDEEEEEEEEEEENEDHQMSCTRIMQDPEKDDNNNDEYDNYDELVAKSLLNLGKIAEDAAYRARTESEVNSNTSNSLEDHSSKNENLGRKSELSLDLDSDVVRETVDSLKLLAQGHGVVLSENISDRSYAEGMSQQDSRNMNYVMLGKPMNNGLMEKMVEESDEEVCLSSLECLRNQCFDLARKLSETNPQDRSQPPNMSVRQHVRQEDDFPGRTPDRSYSDMMNLMRLEEQLSPRSRTFSSCAKEDGCHERDDDTTTVNSDRSEEVFDMTKGNLTLLEKAIALETERAKAMREKMAMDAGRRDNLRSYEDQSPRQLAGEDRKSKSSDSHVKKPYYDPSRTEKRESKCPTPGCDGTGHVNGLYPHHRSLSGCPHKDRVPPEILAMHENVLKCPTPGCTGRGHVNSNRNSHRSLSGCPIAAAEKLAKAQEKHQSCDVSKSNQASDRVLRPMCFVKQLEIPQYGYRNNVPTTTPRSNLAKELEKYSKTSFEYNSYDNHTYGKRAIAPRCKPGTYPPKDMTMPSGTGKNASPSSSTTSSYAPSSSSNLSCGGGSSASSTCSKSSFDYTHDMEAAHMAATAILNLSTRCREMPQNLSTKPQDLCTARNPDMEVDENGTLDLSMNKQRPRDSCCPVLTPLEPMSPQQQAVMSSRCFQLSEGDCWDLPVDYTKMKPRRVDEEDPKEITPEDLDPFQEALEERRYPGEVTIPSPKPKYPQCKESKKDLITLSGCPLADKSIRSMLATSSQELKCPTPGCDGSGHITGNYASHRSLSGCPRAKKSGIRIAQSKEDKEDQEPIRCPVPGCDGQGHITGKYASHRSASGCPLAAKRQKDGYLNGSQFSWKSVKTEGMSCPTPGCDGSGHVSGSFLTHRSLSGCPRATSAMKKAKLSGEQMLTIKQRASNGIENDEEIKQLDEEIKELNESNSQMEADMIKLRTQVTITTMESNLKTIEEENKVIEQQNESLLHELANLSQSLIHSLANIQLPHMDPINEQNFDAYVTTLTEMYTNQDRYQSPENKALLENIKQAVRGIQV Disordered - Extended zinc binding domains 487 606 HVKKPYYDPSRTEKRESKCPTPGCDGTGHVNGLYPHHRSLSGCPHKDRVPPEILAMHENVLKCPTPGCTGRGHVNSNRNSHRSLSGCPIAAAEKLAKAQEKHQSCDVSKSNQASDRVLRP Complex Fragment Function arises via a disorder to order transition Molecular recognition effectors Metal binding Protein-DNA binding Transactivation (transcriptional activation) Nuclear magnetic resonance (NMR) SDS-PAGE gel, Aberrant mobility on +/- Zn Paper 10606515 Berkovits HJ, Berg JM 1999 Biochemistry 38 51 16826-30 Neurofilament heavy polypeptide NFH_MOUSE NF-H Neurofilament H Neurofilament triplet H protein 200 kDa neurofilament protein P19246 Mm.298283 NFH_MOUSE 94730399 Mus musculus (Mouse) 1087 MSFGSADALLGAPFAPLHGGGSLHYSLSRKAGPGGTRSAAGSSSGFHSWARTSVSSVSASPSRFRGAASSTDSLDTLSNGPEGCVVAAVAARSEKEQLQALNDRFAGYIDKVRQLEAHNRSLEGEAAALRQQKGRAAMGELYEREVREMRGAVLRLGAARGQLRLEQEHLLEDIAHVRQRLDEEARQREEAEAAARALAFAQEAEAARVELQKKAQALQEECGYLRRHHQEEVGELLGQIQGCGAAQAQAQAEARDALKCDVTSALREIRAQLEGHAVQSSLQSEEWFRVRLDRLSEAAKVNTDAMRSAQEEITEYRRQLQARTTELEALKSTKESLERQRSELEDRHQADIASYQDAIQQLDSELRNTKWEMAAQLREYQDLLNVKMALDIEIAAYRKLLEGEECRIGFGPSPFSLTEGLPKIPSISTHIKVKSEEMIKVVEKSEKETVIVEGQTEEIRVTEGVTEEEDKEAQGQEGEEAEEGEEKEEEELAAATSPPAEEAASPEKETKSRVKEEAKSPGEAKSPGEAKSPAEAKSPGEAKSPGEAKSPGEAKSPAEPKSPAEPKSPAEAKSPAEPKSPATVKSPGEAKSPSEAKSPAEAKSPAEAKSPAEAKSPAEAKSPAEAKSPAEAKSPATVKSPGEAKSPSEAKSPAEAKSPAEAKSPAEAKSPAEVKSPGEAKSPAEPKSPAEAKSPAEVKSPAEAKSPAEVKSPGEAKSPAAVKSPAEAKSPAAVKSPGEAKSPGEAKSPAEAKSPAEAKSPIEVKSPEKAKTPVKEGAKSPAEAKSPEKAKSPVKEDIKPPAEAKSPEKAKSPVKEGAKPPEKAKPLDVKSPEAQTPVQEEATVPTDIRPPEQVKSPAKEKAKSPEKEEAKTSEKVAPKKEEVKSPVKEEVKAKEPPKKVEEEKTLPTPKTEAKESKKDEAPKEAPKPKVEEKKETPTEKPKDSTAEAKKEEAGEKKKAVASEEETPAKLGVKEEAKPKEKTETTKTEAEDTKAKEPSKPTETEKPKKEEMPAAPEKKDTKEEKTTESRKPEEKPKMEAKVKEDDKSLSKEPSKPKTEKAEKSSSTDQKESQPPEKTTEDKATKGEK Disordered 409 1087 GFGPSPFSLTEGLPKIPSISTHIKVKSEEMIKVVEKSEKETVIVEGQTEEIRVTEGVTEEEDKEAQGQEGEEAEEGEEKEEEELAAATSPPAEEAASPEKETKSRVKEEAKSPGEAKSPGEAKSPAEAKSPGEAKSPGEAKSPGEAKSPAEPKSPAEPKSPAEAKSPAEPKSPATVKSPGEAKSPSEAKSPAEAKSPAEAKSPAEAKSPAEAKSPAEAKSPAEAKSPATVKSPGEAKSPSEAKSPAEAKSPAEAKSPAEAKSPAEVKSPGEAKSPAEPKSPAEAKSPAEVKSPAEAKSPAEVKSPGEAKSPAAVKSPAEAKSPAAVKSPGEAKSPGEAKSPAEAKSPAEAKSPIEVKSPEKAKTPVKEGAKSPAEAKSPEKAKSPVKEDIKPPAEAKSPEKAKSPVKEGAKPPEKAKPLDVKSPEAQTPVQEEATVPTDIRPPEQVKSPAKEKAKSPEKEEAKTSEKVAPKKEEVKSPVKEEVKAKEPPKKVEEEKTLPTPKTEAKESKKDEAPKEAPKPKVEEKKETPTEKPKDSTAEAKKEEAGEKKKAVASEEETPAKLGVKEEAKPKEKTETTKTEAEDTKAKEPSKPTETEKPKKEEMPAAPEKKDTKEEKTTESRKPEEKPKMEAKVKEDDKSLSKEPSKPKTEKAEKSSSTDQKESQPPEKTTEDKATKGEK SDS-PAGE gel, Aberrant mobility on Sensitivity to proteolysis Paper 3220257 Julien JP, Cote F, Beaudet L, Sidky M, Flavell D, Grosveld F, Mushynski W 1988 Gene 68 2 307-314 9424114 Brown HG, Hoh JH 1997 Biochemistry 36 49 15035-40 9714161 Hoh JH 1998 Proteins 32 2 223-8 According to Brown (1997), the disordered region is a portion of the C-terminus. However, the exact numbered amino acids are not documented in the literature. Ornithine decarboxylase DCOR_TRYBB ODC L-ornithine carboxy-lyase EC=4.1.1.17 P07805 DCOR_TRYBB 7404357 Trypanosoma brucei brucei 425 GAMDIVVNDDLSCRFLEGFNTRDALCKKISMNTCDEGDPFFVADLGDIVRKHETWKKCLPRVTPFYAVACNDDWRVLGTLAALGTGFDCASNTEIQRVRGIGVPPEKIIYANPCKQISHIRYARDSGVDVMTFDCVDELEKVAKTHPKAKMVLRISTDDSLARCRLSVKFGAKVEDCRFILEQAKKLNIDVTGVSFHVGSGSTDASTFAQAISDSRFVFDMGTELGFNMHILDIGGGFPGTRDAPLKFEEIAGVINNALEKHFPPDLKLTIVAEPGRYYVASAFTLAVNVIAKKVTPGVQTDVGAHAESNAQSFMYYVNDGVYGSFNCILYDHAVVRPLPQREPIPNEKLYPSSVWGPTCDGLDQIVERYYLPEMQVGEWLLFEDMGAYTVVGTSSFNGFQSPTIYYVVSGLPDHVVRELKSQKS Disordered - Extended 1 35 GAMDIVVNDDLSCRFLEGFNTRDALCKKISMNTCD Engineered 2TODB 1QU4A 1QU4B 1QU4C 1QU4D Relationship to function unknown Unknown Unknown X-ray crystallography Paper Jancarik J, Kim SH 1991 J Appl Cryst 24 Pt. 4 409-11 10563800 Grishin NV, Osterman AL, Brooks HB, Phillips MA, Goldsmith EJ 1999 Biochemistry 38 46 15174-15184 PDB entry 2TOD documents residues 1-36 being absent from the electron density map. PDB entry 1QU4 documents 1-34 being absent form the electron density map. Disordered 158 165 DDSLARCR Engineered 2TODA 2TODB 2TODC 2TODD 1QU4A 1QU4B 1QU4C 1QU4D Relationship to function unknown Unknown Unknown X-ray crystallography Paper 10563800 Grishin NV, Osterman AL, Brooks HB, Phillips MA, Goldsmith EJ 1999 Biochemistry 38 46 15174-15184 Jancarik J, Kim SH 1991 J Appl Cryst 24 Pt. 4 409-11 PDB 1QU4 contains an A69K substitution Disordered 298 310 GVQTDVGAHAESN Engineered 2TODA 2TODB 2TODC 2TODD 1QU4A 1QU4B 1QU4C 1QU4D Relationship to function unknown Unknown Unknown X-ray crystallography Paper 10563800 Grishin NV, Osterman AL, Brooks HB, Phillips MA, Goldsmith EJ 1999 Biochemistry 38 46 15174-15184 Jancarik J, Kim SH 1991 J Appl Cryst 24 Pt. 4 409-11 PDB 1QU4 contains an A69K substitution Disordered 412 425 LPDHVVRELKSQKS Engineered 2TODA 2TODB 2TODC 2TODD 1AQ4A 1AQ4B 1AQ4C 1AQ4D Relationship to function unknown Unknown Unknown X-ray crystallography Paper 10563800 Grishin NV, Osterman AL, Brooks HB, Phillips MA, Goldsmith EJ 1999 Biochemistry 38 46 15174-15184 Jancarik J, Kim SH 1991 J Appl Cryst 24 Pt. 4 409-11 2TOD documents amino acids 411-425 as being absent from the density map. PDB entry 1QU4 contains an A69K substitution Disordered 1 13 GAMDIVVNDDLSC Engineered 1F3TA 1F3TB 1F3TC 1F3TD Relationship to function unknown Unknown Unknown X-ray crystallography 289 7.5 Paper 10985770 Jackson LK, Brooks HB, Osterman AL, Goldsmith EJ, Phillips MA 2000 Biochemistry 39 37 11247-11257 The PDB entry documents absence from density map in regions 1-13 and then 31-36.PDB entry 1QU4 contains an A69K substitution Disordered 160 164 SLARC Engineered 1F3TA 1F3TB 1F3TC 1F3TD Relationship to function unknown Unknown Unknown X-ray crystallography 289 7.5 Paper 10985770 Jackson LK, Brooks HB, Osterman AL, Goldsmith EJ, Phillips MA 2000 Biochemistry 39 37 11247-11257 Disordered 297 311 PGVQTDVGAHAESNA Engineered 1F3TA 1F3TB 1F3TC 1F3TD Relationship to function unknown Unknown Unknown X-ray crystallography 289 7.5 Paper 10985770 Jackson LK, Brooks HB, Osterman AL, Goldsmith EJ, Phillips MA 2000 Biochemistry 39 37 11247-11257 PDB entry 1F3T contains an A69K substitution Disordered 409 425 VSGLPDHVVRELKSQKS Engineered 1F3TA 1F3TB 1F3TC 1F3TD Relationship to function unknown Unknown Unknown X-ray crystallography 289 7.5 Paper 10985770 Jackson LK, Brooks HB, Osterman AL, Goldsmith EJ, Phillips MA 2000 Biochemistry 39 37 11247-11257 1F3T documents 423-425 as being absent from the electron density map. PDB entry 1F3T contains an A69K substitution SPARC SPRC_MOUSE Secreted protein acidic and rich in cysteine Osteonectin ON Basement-membrane protein 40 BM-40 P07214 Mm.291442 SPRC_MOUSE 129284 Mus musculus (Mouse) 302 MRAWIFFLLCLAGRALAAPQQTEVAEEIVEEETVVEETGVPVGANPVQVEMGEFEDGAEETVEEVVADNPCQNHHCKHGKVCELDESNTPMCVCQDPTSCPAPIGEFEKVCSNDNKTFDSSCHFFATKCTLEGTKKGHKLHLDYIGPCKYIAPCLDSELTEFPLRMRDWLKNVLVTLYERDEGNNLLTEKQKLRVKKIHENEKRLEAGDHPVELLARDFEKNYNMYIFPVHWQFGQLDQHPIDGYLSHTELAPLRAPLIPMEHCTTRFFETCDLDNDKYIALEEWAGCFGIKEQDINKDLVI Disordered - Extended 18 302 APQQTEVAEEIVEEETVVEETGVPVGANPVQVEMGEFEDGAEETVEEVVADNPCQNHHCKHGKVCELDESNTPMCVCQDPTSCPAPIGEFEKVCSNDNKTFDSSCHFFATKCTLEGTKKGHKLHLDYIGPCKYIAPCLDSELTEFPLRMRDWLKNVLVTLYERDEGNNLLTEKQKLRVKKIHENEKRLEAGDHPVELLARDFEKNYNMYIFPVHWQFGQLDQHPIDGYLSHTELAPLRAPLIPMEHCTTRFFETCDLDNDKYIALEEWAGCFGIKEQDINKDLVI Native Function arises via a disorder to pre-molten globule transition Unknown Unknown X-ray crystallography Circular dichroism (CD) spectroscopy, far-UV 293 Paper 3427055 Engel J, Taylor W, Paulsson M, Sage H, Hogan B 1987 Biochemistry 26 22 6958-65 Two calcium binding domains are known but more may exist. Phenylalanyl-tRNA synthetase alpha chain SYFA_THETH Phenylalanine--tRNA ligase alpha chain PheRS Phenylalanine translase EC=6.1.1.20 P27001 SYFA_THETH 135112 Thermus thermophilus 350 MLEEALAAIQNARDLEELKALKARYLGKKGLLTQEMKGLSALPLEERRKRGQELNAIKAALEAALEAREKALEEAALKEALERERVDVSLPGASLFSGGLHPITLMERELVEIFRALGYQAVEGPEVESEFFNFDALNIPEHHPARDMWDTFWLTGEGFRLEGPLGEEVEGRLLLRTHTSPMQVRYMVAHTPPFRIVVPGRVFRFEQTDATHEAVFHQLEGLVVGEGIAMAHLKGAIYELAQALFGPDSKVRFQPVYFPFVEPGAQFAVWWPEGGKWLELGGAGMVHPKVFQAVDAYRERLGLPPAYRGVTGFAFGLGVERLAMLRYGIPDIRYFFGGRLKFLEQFKGVL Disordered N-terminal 1 85 MLEEALAAIQNARDLEELKALKARYLGKKGLLTQEMKGLSALPLEERRKRGQELNAIKAALEAALEAREKALEEAALKEALERER Complex 1PYSA 1PYSB Function arises via a disorder to order transition Protein-tRNA binding Substrate/ligand binding X-ray crystallography MAR Research image plate detector Rigaku RU-300 rotating anode generator Xentronics area detector resolution 2.9 Paper 9016717 Goldgur Y, Mosyak L, Reshetnikova L, Ankilova V, Lavrik O, Khodyreva S, Safro M 1997 Structure 5 1 59-68 7664121 Mosyak L, Reshetnikova L, Goldgur Y, Delarue M, Safro MG 1995 Nat Struct Biol 2 7 537-47 AV 6-28-2010 PubMed: 7664121 Phosphatidylinositol-4-phosphate 5-kinase type II beta PI42B_HUMAN Phosphatidylinositol-5-phosphate 4-kinase type II beta 1-phosphatidylinositol-5-phosphate 4-kinase 2-beta PtdIns(5)P-4-kinase isoform 2-beta PIP4KII-beta Diphosphoinositide kinase 2-beta Type II PIP kinase EC=2.7.1.149 P78356 Hs.260603 PI42B_HUMAN 47605991 Homo sapiens (Human) 416 MSSNCTSTTAVAVAPLSASKTKTKKKHFVCQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVDRAEQEEMEVEERAEDEECENDGVGGNLLCSYGTPPDSPGNLLSFPRFFGPGEFDPSVDVYAMKSHESSPKKEVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSNILT Disordered - Extended G-Loop 130 137 DSQGRCGT Native 1BO1A Function arises from the disordered state Molecular assembly Protein-protein binding X-ray crystallography 95 5.6 Sodium citrate 100 Lithium acetate 100 PEG 1000 20 MPD 5 Paper 9753329 Rao VD, Misra S, Boronenkov IV, Anderson RA, Hurley JH 1998 Cell 94 6 829-839 The G-loop aids in conformational stabilization of consecutive peptide groups in alignment with each other so that their amide NH groups can interact with the phosphates of ATP. Disordered - Extended N-Terminal 1 33 MSSNCTSTTAVAVAPLSASKTKTKKKHFVCQKV Native 1BO1A Relationship to function unknown Unknown Unknown X-ray crystallography 95 5.6 Sodium citrate 100 Lithium acetate 100 PEG 1000 20 MPD 5 Paper 9753329 Rao VD, Misra S, Boronenkov IV, Anderson RA, Hurley JH 1998 Cell 94 6 829-839 Disordered 373 390 PYDTKKKAAHAAKTVKHG Native 1BO1A Relationship to function unknown Unknown Unknown X-ray crystallography lithium acetate 100 MPD 5 PEG 1000 20 sodium citrate pH 5.6 100 Paper 9753329 Rao VD, Misra S, Boronenkov IV, Anderson RA, Hurley JH 1998 Cell 94 6 829-839 Disordered 307 341 CENDGVGGNLLCSYGTPPDSPGNLLSFPRFFGPGE Native 1BO1A Relationship to function unknown Unknown Unknown X-ray crystallography lithium acetate 100 MPD 5 PEG 1000 20 sodium citrate pH 5.6 100 Paper 9753329 Rao VD, Misra S, Boronenkov IV, Anderson RA, Hurley JH 1998 Cell 94 6 829-839 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-1 PLCD1_RAT Phosphoinositide phospholipase C Phosphatidylinositol phospholipase C Phospholipase C-delta-1 PLC-delta-1 PLC-III 1-phosphatidyl-D-myo-inositol-4,5-bisphosphate inositoltrisphosphohydrolase Monophosphatidylinositol phosphodiesterase PI-PLC Triphosphoinositide phosphodiesterase EC 3.1.4.11 P10688 Rn.12324 PLCD1_RAT 130228 Rattus norvegicus (Rat) 756 MDSGRDFLTLHGLQDDPDLQALLKGSQLLKVKSSSWRRERFYKLQEDCKTIWQESRKVMRSPESQLFSIEDIQEVRMGHRTEGLEKFARDIPEDRCFSIVFKDQRNTLDLIAPSPADAQHWVQGLRKIIHHSGSMDQRQKLQHWIHSCLRKADKNKDNKMNFKELKDFLKELNIQVDDGYARKIFRECDHSQTDSLEDEEIETFYKMLTQRAEIDRAFEEAAGSAETLSVERLVTFLQHQQREEEAGPALALSLIERYEPSETAKAQRQMTKDGFLMYLLSADGNAFSLAHRRVYQDMDQPLSHYLVSSSHNTYLLEDQLTGPSSTEAYIRALCKGCRCLELDCWDGPNQEPIIYHGYTFTSKILFCDVLRAIRDYAFKASPYPVILSLENHCSLEQQRVMARHLRAILGPILLDQPLDGVTTSLPSPEQLKGKILLKGKKLGGLLPAGGENGSEATDVSDEVEAAEMEDEAVRSQVQHKPKEDKLKLVPELSDMIIYCKSVHFGGFSSPGTSGQAFYEMASFSESRALRLLQESGNGFVRHNVSCLSRIYPAGWRTDSSNYSPVEMWNGGCQIVALNFQTPGPEMDVYLGCFQDNGGCGYVLKPAFLRDPNTTFNSRALTQGPWWRPERLRVRIISGQQLPKVNKNKNSIVDPKVIVEIHGVGRDTGSRQTAVITNNGFNPRWDMEFEFEVTVPDLALVRFMVEDYDSSSKNDFIGQSTIPWNSLKQGYRHVHLLSKNGDQHPSATLFVKISIQD Disordered 645 650 NKNKNS Fragment Function arises via a disorder to order transition X-ray crystallography Paper 8784353 Grobler JA, Essen LO, Williams RL, Hurley JH 1996 Nat Struct Biol 3 9 788-95 Disordered 706 714 DYDSSSKND Fragment X-ray crystallography Paper 8784353 Grobler JA, Essen LO, Williams RL, Hurley JH 1996 Nat Struct Biol 3 9 788-95 Disordered 643 653 KVNKNKNSIVD Fragment X-ray crystallography Paper 8784353 Grobler JA, Essen LO, Williams RL, Hurley JH 1996 Nat Struct Biol 3 9 788-95 Disordered 445 485 LLPAGGENGSEATDVSDEVEAAEMEDEAVRSQVQHKPKEDK Fragment X-ray crystallography Paper 8784353 Grobler JA, Essen LO, Williams RL, Hurley JH 1996 Nat Struct Biol 3 9 788-95 Disordered 135 206 MDQRQKLQHWIHSCLRKADKNKDNKMNFKELKDFLKELNIQVDDGYARKIFRECDHSQTDSLEDEEIETFYK Fragment X-ray crystallography Paper 8784353 Grobler JA, Essen LO, Williams RL, Hurley JH 1996 Nat Struct Biol 3 9 788-95 Disordered Catalytic domain loop 502 517 VHFGGFSSPGTSGQAF Fragment Metal binding Substrate/ligand binding X-ray crystallography 100 ammonium phosphate 1.4 CHAPSO w/v 0.1 DTT 1 EGTA 0.5 NaCl 100 NaN3 w/v 0.01 protein sample 10 Tris-HCl 10 Paper 8602259 Essen LO, Perisic O, Cheung R, Katan M, Williams RL 1996 Nature 380 6575 595-602 Disordered 446 488 LPAGGENGSEATDVSDEVEAAEMEDEAVRSQVQHKPKEDKLKL Fragment Metal binding Flexible linkers/spacers Substrate/ligand binding X-ray crystallography 100 ammonium phosphate 1.4 CHAPSO w/v 0.1 DTT 1 EGTA 0.5 NaCl 100 NaN3 w/v 0.01 protein sample 10 Tris-HCl 10 Paper 8602259 Essen LO, Perisic O, Cheung R, Katan M, Williams RL 1996 Nature 380 6575 595-602 Grobler article is no longer publically available to verify this record. Sperm histone HSP1_CHICK Protamine Galline P15340 HSP1_CHICK 123705 Gallus gallus (Chicken) 62 MARYRRSRTRSRSPRSRRRRRRSGRRRSPRRRRRYGSARRSRRSVGGRRRRYGSRRRRRRRY Disordered 1 62 MARYRRSRTRSRSPRSRRRRRRSGRRRSPRRRRRYGSARRSRRSVGGRRRRYGSRRRRRRRY Complex Native Function arises via a disorder to order transition Metal binding Protein-DNA binding Circular dichroism (CD) spectroscopy, far-UV Jasco 500 spectropolarimeter sensitivity 0.5 scan speed 0.2 time constant 8 wavelength expansion 10 Tris-HF buffer 10 DTT 0.1 Paper 2243113 Gatewood JM, Schroth GP, Schmid CW, Bradbury EM 1990 J Biol Chem 265 33 20667-72 2738040 Nakano M, Kasai K, Yoshida K, Tanimoto T, Tamaki Y, Tobita T 1989 J Biochem (Tokyo) 105 1 133-7 This record is not able to be completed with the Nakano article which is no longer publicly available. Prothymosin alpha PTMA_RAT Thymosin alpha [cleavage chain 1] P06302 Rn.817 PTMA_RAT 135836 Rattus norvegicus (Rat) 112 MSDAAVDTSSEITTKDLKEKKEVVEEAENGRDAPANGNAQNEENGEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGDEDEEAEAPTGKRVAEDDEDDDVETKKQKKTDEDD Disordered 1 112 MSDAAVDTSSEITTKDLKEKKEVVEEAENGRDAPANGNAQNEENGEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGDEDEEAEAPTGKRVAEDDEDDDVETKKQKKTDEDD Monomeric Native Unknown Unknown Dynamic light scattering 293 scattering angle 90 wavelength 514.5 output power 1 Static light scattering 293 output power 1 scattering angle 90 wavelength 514.5 Small-angle X-ray scattering (SAXS) URD6 X-ray diffractometer Circular dichroism (CD) spectroscopy, far-UV 293 7.4 Jasco J-720 spectrometer PBS buffer Paper 7548085 Gast K, Damaschun H, Eckert K, Schulze-Forster K, Maurer HR, Muller-Frohne M, Zirwer D, Czarnecki J, Damaschun G 1995 Biochemistry 34 40 13211-8 AV 6-28-2010 PubMed: 7548085 Modification methylase PvuII MTP2_PROVU M.PvuII N-4 cytosine-specific methyltransferase PvuII N(4)-cytosine-specific DNA methylase EC 2.1.1.113 P11409 MTP2_PROVU 1709165 Proteus vulgaris 323 MLNFGKKPAYTTSNGSMYIGDSLELLESFPEESISLVMTSPPFALQRKKEYGNLEQHEYVDWFLSFAKVVNKKLKPDGSFVVDFGGAYMKGVPARSIYNFRVLIRMIDEVGFFLAEDFYWFNPSKLPSPIEWVNKRKIRVKDAVNTVWWFSKTEWPKSDITKVLAPYSDRMKKLIEDPDKFYTPKTRPSGHDIGKSFSKDNGGSIPPNLLQISNSESNGQYLANCKLMGIKAHPARFPAKLPEFFIRMLTEPDDLVVDIFGGSNTTGLVAERESRKWISFEMKPEYVAASAFRFLDNNISEEKITDIYNRILNGESLDLNSII Disordered 166 203 PYSDRMKKLIEDPDKFYTPKTRPSGHDIGKSFSKDNGG Complex Native Methylation X-ray crystallography MarResearch imaging plate detector beamline X12-C Paper 9207015 Gong W, O'Gara M, Blumenthal RM, Cheng X 1997 Nucleic Acids Res 25 14 2702-15 Disordered P loop 70 81 VNKKLKPDGSFV Complex Native Function arises via a disorder to order transition Protein-DNA binding Methylation X-ray crystallography beamline X12-C MarResearch imaging plate detector Paper 9207015 Gong W, O'Gara M, Blumenthal RM, Cheng X 1997 Nucleic Acids Res 25 14 2702-15 The SwissProt sequence is the long form of the protein(aa1-aa336). The disordered regions were found using the short form of the protein. (aa14-aa336) The referenced paper has disordered region 1 as residues 179-216 and region 2 as residues 57-68. They used the short form of Modification methylase PvuII which has 13 less N-terminal residues and is numbered 14-336. AV 6-28-2010 PubMed: 9207015 Replication protein A 70 kDa DNA-binding subunit RFA1_HUMAN RP-A p70 Replication factor A protein 1 RF-A protein 1 Single-stranded DNA-binding protein P27694 Hs.461925 RFA1_HUMAN 1350579 Homo sapiens (Human) 616 MVGQLSEGAIAAIMQKGDTNIKPILQVINIRPITTGNSPPRYRLLMSDGLNTLSSFMLATQLNPLVEEEQLSSNCVCQIHRFIVNTLKDGRRVVILMELEVLKSAEAVGVKIGNPVPYNEGLGQPQVAPPAPAASPAASSRPQPQNGSSGMGSTVSKAYGASKTFGKAAGPSLSHTSGGTQSKVVPIASLTPYQSKWTICARVTNKSQIRTWSNSRGEGKLFSLELVDESGEIRATAFNEQVDKFFPLIEVNKVYYFSKGTLKIANKQFTAVKNDYEMTFNNETSVMPCEDDHHLPTVQFDFTGIDDLENKSKDSLVDIIGICKSYEDATKITVRSNNREVAKRNIYLMDTSGKVVTATLWGEDADKFDGSRQPVLAIKGARVSDFGGRSLSVLSSSTIIANPDIPEAYKLRGWFDAEGQALDGVSISDLKSGGVGGSNTNWKTLYEVKSENLGQGDKPDYFSSVATVVYLRKENCMYQACPTQDCNKKVIDQQNGLYRCEKCDTEFPNFKYRMILSVNIADFQENQWVTCFQESAEAILGQNAAYLGELKDKNEQAFEEVFQNANFRSFIFRVRVKVETYNDESRIKATVMDVKPVDYREYGRRLVMSIRRSALM Disordered 115 168 PVPYNEGLGQPQVAPPAPAASPAASSRPQPQNGSSGMGSTVSKAYGASKTFGKA Fragment Flexible linkers/spacers Protein-DNA binding Protein-protein binding Nuclear magnetic resonance (NMR) 298 6.5 Varian spectrometer Paper 10526407 Jacobs DM, Lipton AS, Isern NG, Daughdrill GW, Lowry DF, Gomes X, Wold MS 1999 J Biomol NMR 14 4 321-31 Additional UniGene ID: Hs.595562 AV 6-28-2010 PubMed: 10526407 Retinoic acid receptor RXR-alpha RXRA_HUMAN Retinoid X receptor alpha Nuclear receptor subfamily 2 group B member 1 P19793 Hs.590886 RXRA_HUMAN 133701 Homo sapiens (Human) 462 MDTKHFLPLDFSTQVNSSLTSPTGRGSMAAPSLHPSLGPGIGSPGQLHSPISTLSSPINGMGPPFSVISSPMGPHSMSVPTTPTLGFSTGSPQLSSPMNPVSSSEDIKPPLGLNGVLKVPAHPSGNMASFTKHICAICGDRSSGKHYGVYSCEGCKGFFKRTVRKDLTYTCRDNKDCLIDKRQRNRCQYCRYQKCLAMGMKREAVQEERQRGKDRNENEVESTSSANEDMPVERILEAELAVEPKTETYVEANMGLNPSSPNDPVTNICQAADKQLFTLVEWAKRIPHFSELPLDDQVILLRAGWNELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGVGAIFDRVLTELVSKMRDMQMDKTELGCLRAIVLFNPDSKGLSNPAEVEALREKVYASLEAYCKHKYPEQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQMT Disordered - Extended C-terminal helix 202 206 REAVQ Engineered 1RXR1 Function arises via an order to disorder transition Molecular assembly Protein-DNA binding Substrate/ligand binding Protein-protein binding Nuclear magnetic resonance (NMR) 300 6.6 2H2O 100 KCl 100 KH2PO4 20 ZnCl2 0.3 Nuclear magnetic resonance (NMR) 300 6.6 2H2O 5 H2O 95 KCl 100 KH2PO4 20 ZnCl2 0.3 Paper 9698548 Holmbeck SM, Foster MP, Casimiro DR, Sem DS, Dyson HJ, Wright PE 1998 J Mol Biol 281 2 271-84 9826495 Holmbeck SM, Dyson HJ, Wright PE 1998 J Mol Biol 284 3 533-9 The C-terminal helix undergoes an order to disorder transition upon binding to DNA. The unwinding of the helix most likely facilitates homodimer formation by maximizing interactions between the two DNA-bound RXR proteins. Disordered - Extended Second Zinc binding domain 181 187 KRQRNRC Engineered 1RXR1 Function arises via a disorder to order transition Molecular assembly Metal binding Protein-DNA binding Nuclear magnetic resonance (NMR) 300 6.8 Paper 9698548 Holmbeck SM, Foster MP, Casimiro DR, Sem DS, Dyson HJ, Wright PE 1998 J Mol Biol 281 2 271-84 9826495 Holmbeck SM, Dyson HJ, Wright PE 1998 J Mol Biol 284 3 533-9 Disordered - Extended D-BOX 172 176 RDNKD Engineered 1RXR1 Molecular assembly Protein-protein binding Protein-DNA binding Nuclear magnetic resonance (NMR) 300 6.6 KH2PO4 pH 6.7 20 KCl 100 ZnCl2 0.3 2H2O 100 Nuclear magnetic resonance (NMR) 300 6.6 KH2PO4 pH 6.7 20 KCl 100 ZnCl2 0.3 H2O 95 2H2O 5 Paper 9698548 Holmbeck SM, Foster MP, Casimiro DR, Sem DS, Dyson HJ, Wright PE 1998 J Mol Biol 281 2 271-84 9826495 Holmbeck SM, Dyson HJ, Wright PE 1998 J Mol Biol 284 3 533-9 Disordered - Extended Second Zinc Finger Binding Domain 178 187 LIDKRQRNRC Engineered 1RXR1 Function arises via a disorder to order transition Molecular assembly Metal binding Protein-DNA binding Nuclear magnetic resonance (NMR) 300 6.6 KCl 100 KH2PO4 pH 6.7 20 ZnCl2 0.3 2H2O 100 Nuclear magnetic resonance (NMR) 300 6.6 2H2O 5 H2O 95 KCl 100 KH2PO4 pH 6.7 20 ZnCl2 0.3 Paper 9698548 Holmbeck SM, Foster MP, Casimiro DR, Sem DS, Dyson HJ, Wright PE 1998 J Mol Biol 281 2 271-84 9826495 Holmbeck SM, Dyson HJ, Wright PE 1998 J Mol Biol 284 3 533-9 Disordered - Extended 169 189 YTCRDNKDCLIDKRQRNRCQY Engineered IRXR1 Function arises via a disorder to order transition Molecular assembly Metal binding Protein-DNA binding Nuclear magnetic resonance (NMR) 300 6.6 KH2PO4 pH 6.7 20 KCl 100 ZnCl2 0.3 2H2O 100 Nuclear magnetic resonance (NMR) 300 6.6 2H2O 5 H2O 95 KCl 100 KH2PO4 pH 6.7 20 ZnCl2 0.3 Paper 9698548 Holmbeck SM, Foster MP, Casimiro DR, Sem DS, Dyson HJ, Wright PE 1998 J Mol Biol 281 2 271-84 9826495 Holmbeck SM, Dyson HJ, Wright PE 1998 J Mol Biol 284 3 533-9 This region contains the D-box as well as the second zinc binding domain and lies between the first and second helices. Regulator of G-protein signaling 4 RGS4_RAT RGS4 RGP4 Signal transduction inhibitor RGS4 P49799 Rn.11065 RGS4_RAT 1710149 Rattus norvegicus (Rat) 205 MCKGLAGLPASCLRSAKDMKHRLGFLLQKSDSCEHSSSHSKKDKVVTCQRVSQEEVKKWAESLENLINHECGLAAFKAFLKSEYSEENIDFWISCEEYKKIKSPSKLSPKAKKIYNEFISVQATKEVNLDSCTREETSRNMLEPTITCFDEAQKKIFNLMEKDSYRRFLKSRFYLDLTNPSSCGAEKQKGAKSSADCTSLVPQCA Disordered 1 50 MCKGLAGLPASCLRSAKDMKHRLGFLLQKSDSCEHSSSHSKKDKVVTCQR Native Function arises via a disorder to order transition Molecular recognition effectors Substrate/ligand binding X-ray crystallography 5.3 sodium citrate 100 NaF 70 AlCl3 140 DTT fresh 5 PEG 10K w/v 14.4 Paper 9108480 Tesmer JJ, Berman DM, Gilman AG, Sprang SR 1997 Cell 89 2 251-61 Disordered 179 205 NPSSCGAEKQKGAKSSADCTSLVPQCA Native Molecular recognition effectors Substrate/ligand binding X-ray crystallography 5.3 AlCl3 140 DTT fresh 5 NaF 70 PEG 10K w/v 14.4 sodium citrate 100 Paper 9108480 Tesmer JJ, Berman DM, Gilman AG, Sprang SR 1997 Cell 89 2 251-61 Capsid protein CAPSD_SBMV Coat protein SBMV coat protein P03607 CAPSD_SBMV 116795 Southern bean mosaic virus (SBMV) 279 MSGLFHHRTKPREIRAFVMATRLTKKQLAQAIQNTLPNPPRRKRRAKRRAAQVPKPTQAGVSMAPIAQGTMVKLRPPMLRSSMDVTILSHCELSTELAVTVTIVVTSELVMPFTVGTWLRGVAQNWSKYAWVAIRYTYLPSCPTTTSGAIHMGFQYDMADTLPVSVNQLSNLKGYVTGPVWEGQSGLCFVNNTKCPDTSRAITIALDTNEVSEKRYPFKTATDYATAVGVNANIGNILVPARLVTAMEGGSSKTAVNTGRLYASYTIRLIEPIAAALNL Ordered beta A 51 64 TMVKLRPPMLRSSM Fragment 4SBVA 4SBVB 4SBVC Function arises from the ordered state Unknown Unknown X-ray crystallography (NH4)2SO4 0.015 Paper Hermodson MA, Abad-Zapatero C, Abdel-Meguid S, Pundak S, Rossmann MG, Tremaine J 1982 Virology 119 133-149 6854633 Rossmann MG, Abad-Zapatero C, Hermodson MA, Erickson JW 1983 J Mol Biol 166 1 37-73 This region is only ordered in the C subunit. Ordered beta-annulus 42 50 VSMAPIAQG Fragment 4SBVA 4SBVB 4SBVC Function arises from the ordered state Molecular assembly Protein-protein binding X-ray crystallography ammonium sulfate 0.015 Paper Hermodson MA, Abad-Zapatero C, Abdel-Meguid S, Pundak S, Rossmann MG, Tremaine J 1982 Virology 119 133-149 6854633 Rossmann MG, Abad-Zapatero C, Hermodson MA, Erickson JW 1983 J Mol Biol 166 1 37-73 This region is only ordered in the C subunit. Ordered 39 63 QAGVSMAPIAQGTMVKLRPPMLRSS Fragment 4SBVA 4SBVB 4SBVC Function arises from the ordered state Unknown Unknown X-ray crystallography ammonium sulfate 0.015 Paper 6854633 Rossmann MG, Abad-Zapatero C, Hermodson MA, Erickson JW 1983 J Mol Biol 166 1 37-73 3681993 Silva AM, Rossmann MG 1987 J Mol Biol 197 1 69-87 This section is only ordered in the C subunit, and is important in stabilizing the capsid. Disordered 1 64 ATRLTKKQLAQAIQNTLPNPPRRKRRAKRRAAQVPKPTQAGVSMAPIAQGTMVKLRPPMLRSSM Fragment 4SBVA 4SBVB 4SBVC Relationship to function unknown Unknown Unknown X-ray crystallography ammonium sulfate 0.015 Paper 6854633 Rossmann MG, Abad-Zapatero C, Hermodson MA, Erickson JW 1983 J Mol Biol 166 1 37-73 6401119 Rossmann MG, Abad-Zapatero C, Erickson JW, Savithri HS 1983 J Biomol Struct Dyn 1 2 565-79 This region corresponds to the B subunit only. Disordered 1 62 ATRLTKKQLAQAIQNTLPNPPRRKRRAKRRAAQVPKPTQAGVSMAPIAQGTMVKLRPPMLRS Fragment 4SBVA 4SBVB 4SBVC Relationship to function unknown Unknown Unknown X-ray crystallography ammonium sulfate 0.015 Paper 6854633 Rossmann MG, Abad-Zapatero C, Hermodson MA, Erickson JW 1983 J Mol Biol 166 1 37-73 6401119 Rossmann MG, Abad-Zapatero C, Erickson JW, Savithri HS 1983 J Biomol Struct Dyn 1 2 565-79 This region corresponds to the A subunit only. Disordered 1 38 ATRLTKKQLAQAIQNTLPNPPRRKRRAKRRAAQVPKPT Fragment 4SBVA 4SBVB 4SBVC Relationship to function unknown Unknown Unknown X-ray crystallography ammonium sulfate 0.015 Paper 6854633 Rossmann MG, Abad-Zapatero C, Hermodson MA, Erickson JW 1983 J Mol Biol 166 1 37-73 6401119 Rossmann MG, Abad-Zapatero C, Erickson JW, Savithri HS 1983 J Biomol Struct Dyn 1 2 565-79 This region corresponds to the C subunit only. This region is part of the flexible arm that helps to determine binding specificity. Disordered 1 41 ATRLTKKQLAQAIQNTLPNPPRRKRRAKRRAAQVPKPTQAG Fragment 4SBVA 4SBVB 4SBVC Relationship to function unknown Unknown Unknown X-ray crystallography ammonium sulfate 0.015 Paper Hermodson MA, Abad-Zapatero C, Abdel-Meguid S, Pundak S, Rossmann MG, Tremaine J 1982 Virology 119 133-149 6854633 Rossmann MG, Abad-Zapatero C, Hermodson MA, Erickson JW 1983 J Mol Biol 166 1 37-73 This region is disordered in all three subunits. Disordered beta-annulus 42 50 VSMAPIAQG Fragment 4SBVA 4SBVB 4SBVC Relationship to function unknown Unknown Protein-protein binding X-ray crystallography ammonium sulfate 0.015 Paper Hermodson MA, Abad-Zapatero C, Abdel-Meguid S, Pundak S, Rossmann MG, Tremaine J 1982 Virology 119 133-149 6854633 Rossmann MG, Abad-Zapatero C, Hermodson MA, Erickson JW 1983 J Mol Biol 166 1 37-73 This region is disordered in both the A and B subunits. Disordered beta-A 51 64 TMVKLRPPMLRSSM Fragment 4SBVA 4SBVB 4SBVC Relationship to function unknown Unknown Unknown X-ray crystallography ammonium sulfate 0.015 Paper Hermodson MA, Abad-Zapatero C, Abdel-Meguid S, Pundak S, Rossmann MG, Tremaine J 1982 Virology 119 133-149 6854633 Rossmann MG, Abad-Zapatero C, Hermodson MA, Erickson JW 1983 J Mol Biol 166 1 37-73 This region is disordered in both the A and B subunits. The Swiss-Prot entry for this protein has a 19 amino acid propeptide attachment on the N-terminal region. The coat protein follows immediately after is 260 amino acids long. Serine-aspartate repeat-containing protein D SDRD_STAAE SdrD protein O86488 SDRD_STAAE 75499264 Staphylococcus aureus (strain Newman) 1315 MLNRENKTAITRKGMVSNRLNKFSIRKYTVGTASILVGTTLIFGLGNQEAKAAESTNKELNEATTSASDNQSSDKVDMQQLNQEDNTKNDNQKEMVSSQGNETTSNGNKLIEKESVQSTTGNKVEVSTAKSDEQASPKSTNEDLNTKQTISNQEALQPDLQENKSVVNVQPTNEENKKVDAKTESTTLNVKSDAIKSNDETLVDNNSNSNNENNADIILPKSTAPKRLNTRMRIAAVQPSSTEAKNVNDLITSNTTLTVVDADKNNKIVPAQDYLSLKSQITVDDKVKSGDYFTIKYSDTVQVYGLNPEDIKNIGDIKDPNNGETIATAKHDTANNLITYTFTDYVDRFNSVQMGINYSIYMDADTIPVSKNDVEFNVTIGNTTTKTTANIQYPDYVVNEKNSIGSAFTETVSHVGNKENPGYYKQTIYVNPSENSLTNAKLKVQAYHSSYPNNIGQINKDVTDIKIYQVPKGYTLNKGYDVNTKELTDVTNQYLQKITYGDNNSAVIDFGNADSAYVVMVNTKFQYTNSESPTLVQMATLSSTGNKSVSTGNALGFTNNQSGGAGQEVYKIGNYVWEDTNKNGVQELGEKGVGNVTVTVFDNNTNTKVGEAVTKEDGSYLIPNLPNGDYRVEFSNLPKGYEVTPSKQGNNEELDSNGLSSVITVNGKDNLSADLGIYKPKYNLGDYVWEDTNKNGIQDQDEKGISGVTVTLKDENGNVLKTVTTDADGKYKFTDLDNGNYKVEFTTPEGYTPTTVTSGSDIEKDSNGLTTTGVINGADNMTLDSGFYKTPKYNLGNYVWEDTNKDGKQDSTEKGISGVTVTLKNENGEVLQTTKTDKDGKYQFTGLENGTYKVEFETPSGYTPTQVGSGTDEGIDSNGTSTTGVIKDKDNDTIDSGFYKPTYNLGDYVWEDTNKNGVQDKDEKGISGVTVTLKDENDKVLKTVTTDENGKYQFTDLNNGTYKVEFETPSGYTPTSVTSGNDTEKDSNGLTTTGVIKDADNMTLDSGFYKTPKYSLGDYVWYDSNKDGKQDSTEKGIKDVKVTLLNEKGEVIGTTKTDENGKYCFDNLDSGKYKVIFEKPAGLTQTGTNTTEDDKDADGGEVDVTITDHDDFTLDNGYYEEETSDSDSDSDSDSDSDRDSDSDSDSDSDSDSDSDSDSDSDSDSDSDRDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDAGKHTPVKPMSTTKDHHNKAKALPETGNENSGSNNATLFGGLFAALGSLLLFGRRKKQNK Disordered B1-B5 569 1123 VYKIGNYVWEDTNKNGVQELGEKGVGNVTVTVFDNNTNTKVGEAVTKEDGSYLIPNLPNGDYRVEFSNLPKGYEVTPSKQGNNEELDSNGLSSVITVNGKDNLSADLGIYKPKYNLGDYVWEDTNKNGIQDQDEKGISGVTVTLKDENGNVLKTVTTDADGKYKFTDLDNGNYKVEFTTPEGYTPTTVTSGSDIEKDSNGLTTTGVINGADNMTLDSGFYKTPKYNLGNYVWEDTNKDGKQDSTEKGISGVTVTLKNENGEVLQTTKTDKDGKYQFTGLENGTYKVEFETPSGYTPTQVGSGTDEGIDSNGTSTTGVIKDKDNDTIDSGFYKPTYNLGDYVWEDTNKNGVQDKDEKGISGVTVTLKDENDKVLKTVTTDENGKYQFTDLNNGTYKVEFETPSGYTPTSVTSGNDTEKDSNGLTTTGVIKDADNMTLDSGFYKTPKYSLGDYVWYDSNKDGKQDSTEKGIKDVKVTLLNEKGEVIGTTKTDENGKYCFDNLDSGKYKVIFEKPAGLTQTGTNTTEDDKDADGGEVDVTITDHDDFTLDNGYYEEET Complex Native Function arises via a disorder to order transition Metal binding Size exclusion/gel filtration chromatography 7.5 TSK column protein sample 50 Tris-HCl buffer 50 KCl 150 Ca2+ 1 EGTA 1 Circular dichroism (CD) spectroscopy, far-UV 7.5 Jasco J-715 spectropolarimeter protein sample 0.25 Tris-HCl buffer 10 optical path 1 Circular dichroism (CD) spectroscopy, near-UV 7.5 Jasco J-715 spectropolarimeter optical path 1 protein sample 1.8 Tris-HCl buffer 10 Fluorescent probes 298 CaCl2 5 EGTA 25 excitation wavelength 278 guanidine-HCl 4 MgCl2 50 Perkin-Elmer LS-5B spectrofluorimeter protein sample 2 slits 5 Paper 9813018 Josefsson E, O'Connell D, Foster TJ, Durussel I, Cox JA 1998 J Biol Chem 273 47 31145-52 AV (6-29-2010) PubMed: 9813018 Structural polyprotein POLS_SINDO p130 Capsid protein [cleavage product 1] Coat protein C p62 [cleavage product 2] E3/E2 E3 protein [cleavage product 3] Spike glycoprotein E3 E2 envelope glycoprotein [cleavage product 4] Spike glycoprotein E2 6K protein [cleavage product 5] E1 envelope glycoprotein [cleavage product 6] Spike glycoprotein E1 P27285 POLS_SINDO 130578 Sindbis virus subtype Ockelbo (strain Edsbyn 82-5)(OCKV)(Ockelbo virus) 1245 MNRGFFNMLGRRPFPAPTAMWRPRRRRQAAPMPARNGLASQIQQLTTAVSALVIGQATRPQNPRPRPPPRQKKQAPKQPPKPKKPKPQEKKKKQPAKTKPGKRQRMALKLEADRLFDVKNEDGDVIGHALAMEGKVMKPLHVKGTIDHPVLSKLKFTKSSAYDMEFAQLPVNMRSEAFTYTSEHPEGFYNWHHGAVQYSGGRFTIPRGVGGRGDSGRPIMDNSGRVVAIVLGGADEGTRTALSVVTWNSKGKTIKTTPEGTEEWSAAPLVTAMCLLGNVSFPCNRPPTCYTREPSRALDILEENVNHEAYDTLLNAILRCGSSGRSKRSVTDDFTLTSPYLGTCSYCHHTEPCFSPIKIEQVWDEADDNTIRIQTSAQFGYDKSGAASTNKYRYMSFEQDHTVKEGTMDDIKISTSGPCRRLSYKGYFLLAKCPPGDSVTVSIASSNSATSCTMARKIKPKFVGREKYDLPPVHGKKIPCTVYDRLKETTAGYITMHRPGPHAYTSYLEESSGKVYAKPPSGKNITYECKCGDYKTGTVTTRTEITGCTAIKQCVAYKSDQTKWVFNSPDLIRHADHTAQGKLHLPFKLIPSTCMVPVAHAPNVIHGFKHISLQLDTDHLTLLTTRRLGANPEPTTEWIIGKTVRNFTVDRDGLEYIWGNHEPVRVYAQESAPGDPHGWPHEIVQHYYHRHPVYTILAVASAAVAMMIGVTVAALCACKARRECLTPYALAPNAVIPTSLALLCCVRSANAETFTETMSYFWSNSQPFFWVQLCIPLAAVIVLMRCCSCCLPFLVVAGAYLAKVDAYEHATTVPNVPQIPYKALVERAGYAPLNLEITVMSSEVLPSTNQEYITCKFTTVVPSPKVKCCGSLECQPAAHADYTCKVFGGVYPFMWGGAQCFCDSENSQMSEAYVELSADCATDHAQAIKVHTAAMKVGLRIVYGNTTSFLDVYVNGVTPGTSKDLKVIAGPISASFTPFDHKVVIHRGLVYNYDFPEYGAMKPGVFGDIQATSLTSKDLIASTDIRLLKPSAKNVHVPYTQAASGFEMWKNNSGRPLQETAPFGCKIAVNPLRAVDCSYGNIPISIDIPNAAFIRTSDAPLVSTVKCDVSECTYSADFGGMATLQYVSDREGQCPVHSHSSTATLQESTVHVLEKGAVTVHFSTASPQANFIVSLCGKKTTCNAECKPPADHIVSTPHKNDQEFQAAISKTSWSWLFALFGGASSLLIIGLTIFACSMMLTSTRR Previous entry DP00066 has been split into polyprotein DP00066 and cleavage product DP00066_C001 Capsid protein POLS_SINDO Coat protein C Cleavage product 1 of Structural polyprotein P27285 POLS_SINDO 130578 Sindbis virus subtype Ockelbo (strain Edsbyn 82-5)(OCKV)(Ockelbo virus) 264 MNRGFFNMLGRRPFPAPTAMWRPRRRRQAAPMPARNGLASQIQQLTTAVSALVIGQATRPQNPRPRPPPRQKKQAPKQPPKPKKPKPQEKKKKQPAKTKPGKRQRMALKLEADRLFDVKNEDGDVIGHALAMEGKVMKPLHVKGTIDHPVLSKLKFTKSSAYDMEFAQLPVNMRSEAFTYTSEHPEGFYNWHHGAVQYSGGRFTIPRGVGGRGDSGRPIMDNSGRVVAIVLGGADEGTRTALSVVTWNSKGKTIKTTPEGTEEW Disordered N-terminal 1 113 MNRGFFNMLGRRPFPAPTAMWRPRRRRQAAPMPARNGLASQIQQLTTAVSALVIGQATRPQNPRPRPPPRQKKQAPKQPPKPKKPKPQEKKKKQPAKTKPGKRQRMALKLEAD Native Protein-genomic RNA binding X-ray crystallography Siemans area detector Paper 1944569 Choi HK, Tong L, Minor W, Dumas P, Boege U, Rossmann MG, Wengler G 1991 Nature 354 6348 37-43 Previous entry DP00066 has been split into polyprotein DP00066 and cleavage product DP00066_C001 AV (6-29-2010) PubMed: 1944569 Small heat shock protein HSP16.5 HSPS_METJA Q57733 HSPS_METJA 2495337 Methanocaldococcus jannaschii (Methanococcus jannaschii) 147 MFGRDPFDSLFERMFKEFFATPMTGTTMIQSSTGIQISGKGFMPISIIEGDQHIKVIAWLPGVNKEDIILNAVGDTLEIRAKRSPLMITESERIIYSEIPEEEEIYRTIKLPATVKEENASAKFENGVLSVILPKAESSIKKGINIE Disordered N-terminal 1 32 MFGRDPFDSLFERMFKEFFATPMTGTTMIQSS Monomeric Native Chaperones Protein-protein binding X-ray crystallography beamline X12C resolution 2.9 X-ray crystallography resolution 3.2 Rigaku R-Axis IIC imaging plate system Paper 9707123 Kim KK, Kim R, Kim SH 1998 Nature 394 6693 595-9 AV (6-29-2010) PubMed: 9707123 Synaptosomal-associated protein 25 SNP25_RAT SNAP-25 Synaptosomal-associated 25 kDa protein Super protein SUP P60881 Rn.107689 SNP25_RAT 46397720 Rattus norvegicus (Rat) 206 MAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLDRVEEGMNHINQDMKEAEKNLKDLGKCCGLYICPCNKLKSSDAYKKAWGNNQDQVVASQPARVVDEREQMAISGGFIRRVTNDARENEMDEDLEQVSGIIGNLRHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEANQRATKMLGSG Disordered - Extended 1 206 MAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLDRVEEGMNHINQDMKEAEKNLKDLGKCCGLYICPCNKLKSSDAYKKAWGNNQDQVVASQPARVVDEREQMAISGGFIRRVTNDARENEMDEDLEQVSGIIGNLRHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEANQRATKMLGSG Native Function arises via a disorder to order transition Molecular assembly Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV 277 7.4 phosphate buffer 10 NaCl salt 100 Nuclear magnetic resonance (NMR) Sensitivity to proteolysis 298 chymotrypsin NaCl salt 100 proteinase K trypsin Size exclusion/gel filtration chromatography 368 6.8 betamercaptoethanol buffer 3 glycerol buffer 10 SDS buffer 2 Tris buffer 60 Size exclusion/gel filtration chromatography 298 6.8 betamercaptoethanol buffer 3 glycerol buffer 10 SDS buffer 2 Tris buffer 60 Paper 9671503 Fasshauer D, Eliason WK, Brünger AT, Jahn R 1998 Biochemistry 37 29 10354-62 The sequence has 98% similarity to that of chicken and human SNAP-25 but there is no 100% match to any organism when Blasted. Vesicle-associated membrane protein 2 VAMP2_HUMAN VAMP-2 Synaptobrevin-2 P63027 Hs.25348 VAMP2_HUMAN 51704192 Homo sapiens (Human) 116 MSATAATAPPAAPAGEGGPPAPPPNLTSNRRLQQTQAQVDEVVDIMRVNVDKVLERDQKLSELDDRADALQAGASQFETSAAKLKRKYWWKNLKMMIILGVICAIILIIIIVYFSS Disordered - Extended 1 116 MSATAATAPPAAPAGEGGPPAPPPNLTSNRRLQQTQAQVDEVVDIMRVNVDKVLERDQKLSELDDRADALQAGASQFETSAAKLKRKYWWKNLKMMIILGVICAIILIIIIVYFSS Native Function arises via a disorder to order transition Molecular assembly Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV 298 7.4 dithiothreitol 1 NaCl salt 100 Tris 20 Paper 9346956 Fasshauer D, Otto H, Eliason WK, Jahn R, Brunger AT 1997 J Biol Chem 272 44 28036-41 Disordered - Extended 1 96 MSATAATAPPAAPAGEGGPPAPPPNLTSNRRLQQTQAQVDEVVDIMRVNVDKVLERDQKLSELDDRADALQAGASQFETSAAKLKRKYWWKNLKMM Fragment Function arises via a disorder to order transition Molecular assembly Protein-protein binding Nuclear magnetic resonance (NMR) 278 6.1 phosphate buffer 60 protein 0.45 water/D2O solvent (9:1) Paper 10481273 Hazzard J, Sudhof TC, Rizo J 1999 J Biomol NMR 14 3 203-207 Disordered - Extended 40 67 DEVVDIMRVNVDKVLERDQKLSELDDRA Fragment Function arises via a disorder to order transition Molecular assembly Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV 298 7.4 NaCl salt 100 sodium phosphate 10 Experimental 9852083 Cánaves JM, Montal M 1998 J Biol Chem 273 51 34214-21 Alpha-synuclein SYUA_HUMAN Non-A beta component of AD amyloid Non-A4 component of amyloid precursor NACP SNCA NACP140 [Isoform 1] P37840-1 Hs.21374 SYUA_HUMAN 586067 Homo sapiens (Human) 140 MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA Disordered - Extended 1 140 MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA Isoform Native Relationship to function unknown Molecular assembly Metal binding Polymerization Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV 7.5 Tris buffer 10 Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) Calcium fluoride solution cell 0.05 NACP per mL of D2O 4 Nuclear magnetic resonance (NMR) 7.4 H2O/2H2O 90%/10% Na2HPO4 10 NaCl 100 Paper 11312271 Nielsen, M. S. Vorum, H. Lindersson, E. Jensen, P. H. 2001 J Biol Chem 276 25 22680-22684 8901511 Weinreb PH, Zhen W, Poon AW, Conway KA, Lansbury PT Jr 1996 Biochemistry 35 43 13709-13715 11590151 Bussell R Jr, Eliezer D 2001 J Biol Chem 276 49 45996-6003 11286556 Eliezer D, Kutluay E, Bussell R Jr, Browne G 2001 J Mol Biol 307 4 1061-73 This region is composed of an N-terminal membrane anchoring region (residues 1 - 60), the central hydrophobic/amyloidogenic NAC region (residues 61-95), and a C-terminal acidic region (residues 96-140) that is inhibitory to amyloid formation. Amyloid formation may be the result of both phosphorylation of Ser129 and metal binding in the C-terminal region. When this occurs, residues 36 - 99 take on a cross-beta sheet structure characteristic of most amyloids, while the N- and C-termini remain statically and dynamically disordered, respectively. Homeobox protein Nkx-2.1 NKX21_RAT Thyroid transcription factor 1 TTF-1 Thyroid nuclear factor 1 P23441 Rn.34265 NKX21_RAT 136462 Rattus norvegicus (Rat) 372 MSMSPKHTTPFSVSDILSPLEESYKKVGMEGGGLGAPLAAYRQGQAAPPAAAMQQHAVGHHGAVTAAYHMTAAGVPQLSHSAVGGYCNGNLGNMSELPPYQDTMRNSASGPGWYGANPDPRFPAISRFMGPASGMNMSGMGGLGSLGDVSKNMAPLPSAPRRKRRVLFSQAQVYELERRFKQQKYLSAPEREHLASMIHLTPTQVKIWFQNHRYKMKRQAKDKAAQQQLQQDSGGGGGGGGGAGCPQQQQAQQQSPRRVAVPVLVKDGKPCQAGAPAPGAASLQGHAQQQAQQQAQAAQAAAAAISVGSGGAGLGAHPGHQPGSAGQSPDLAHHAASPAALQGQVSSLSHLNSSGSDYGAMSCSTLLYGRTW Disordered TTF-1 N domain 1 157 MSMSPKHTTPFSVSDILSPLEESYKKVGMEGGGLGAPLAAYRQGQAAPPAAAMQQHAVGHHGAVTAAYHMTAAGVPQLSHSAVGGYCNGNLGNMSELPPYQDTMRNSASGPGWYGANPDPRFPAISRFMGPASGMNMSGMGGLGSLGDVSKNMAPLP Fragment Native Function arises via a disorder to order transition Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV Paper 9425125 Tell G, Perrone L, Fabbro D, Pellizzari L, Pucillo C, De Felice M, Acquaviva R, Formisano S, Damante G 1998 Biochem J 329 ( Pt 2) 395-403 Disordered 58 78 VGHHGAVTAAYHMTAAGVPQL Fragment Native Function arises via a disorder to order transition Protein-protein binding Sensitivity to proteolysis 298 protease/substrate 1:50 TFE 10 Paper 9425125 Tell G, Perrone L, Fabbro D, Pellizzari L, Pucillo C, De Felice M, Acquaviva R, Formisano S, Damante G 1998 Biochem J 329 ( Pt 2) 395-403 Thymidylate synthase TYSY_HUMAN TSase TS EC 2.1.1.45 P04818 Hs.592338 TYSY_HUMAN 136611 Homo sapiens (Human) 313 MPVAGSELPRRPLPPAAQERDAEPRPPHGELQYLGQIQHILRCGVRKDDRTGTGTLSVFGMQARYSLRDEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKGVKIWDANGSRDFLDSLGFSTREEGDLGPVYGFQWRHFGAEYRDMESDYSGQGVDQLQRVIDTIKTNPDDRRIIMCAWNPRDLPLMALPPCHALCQFYVVNSELSCQLYQRSGDMGLGVPFNIASYALLTYMIAHITGLKPGDFIHTLGDAHIYLNHIEPLKIQLQREPRPFPKLRILRKVEKIDDFKAEDFQIEGYNPHPTIKMEMAV Disordered 93 132 KGSTNAKELSSKGVKIWDANGSRDFLDSLGFSTREEGDLG Native Function arises via a disorder to order transition Molecular assembly Protein-protein binding X-ray crystallography 7 Ammonium sulfate 1.5 Beta-Mercaptoethanol pH 6.5-8.0 20 Tris-HCl buffer wavelength 0.9 Paper 8845352 Schiffer CA, Clifton IJ, Davisson VJ, Santi DV, Stroud RM 1995 Biochemistry 34 50 16279-87 Disordered 142 157 FGAEYRDMESDYSGQG Native Function arises via a disorder to order transition Molecular assembly Protein-protein binding X-ray crystallography 7 Ammonium sulfate 1.5 Beta-Mercaptoethanol pH 6.5-8.0 20 Tris-HCl buffer wavelength 0.9 Paper 8845352 Schiffer CA, Clifton IJ, Davisson VJ, Santi DV, Stroud RM 1995 Biochemistry 34 50 16279-87 Disordered 107 128 KIWDANGSRDFLDSLGFSTREE Engineered 1HW3A 1HW4A Substrate/ligand binding X-ray crystallography PEG 4000 15-30%(weight/volume) saturated ammonium sulfate 42-50% Tris-HCL pH 8.5 100 Paper 11278511 Phan J, Steadman DJ, Koli S, Ding WC, Minor W, Dunlap RB, Berger SH, Lebioda L 2001 J Biol Chem 276 17 14170-7 The protein used in the Phan paper had an N-terminal extension of 42 residues. It was noted that these residues have no significant effect on the protein structure. Disordered N-terminal 1 27 MPVAGSELPRRPLPPAAQERDAEPRPP Native Function arises via a disorder to order transition Molecular assembly Protein-protein binding X-ray crystallography 7 Ammonium sulfate 1.5 Beta-Mercaptoethanol pH 6.5-8.0 20 Tris-HCl buffer wavelength 0.9 Paper 8845352 Schiffer CA, Clifton IJ, Davisson VJ, Santi DV, Stroud RM 1995 Biochemistry 34 50 16279-87 11278511 Phan J, Steadman DJ, Koli S, Ding WC, Minor W, Dunlap RB, Berger SH, Lebioda L 2001 J Biol Chem 276 17 14170-7 Estrogen receptor [Isoform long] ESR1_HUMAN ER Estradiol receptor Estrogen receptor alpha ER-alpha Nuclear receptor subfamily 3 group A member 1 P03372 Hs.208124 ESR1_HUMAN 544257 Homo sapiens (Human) 595 MTMTLHTKASGMALLHQIQGNELEPLNRPQLKIPLERPLGEVYLDSSKPAVYNYPEGAAYEFNAAAAANAQVYGQTGLPYGPGSEAAAFGSNGLGGFPPLNSVSPSPLMLLHPPPQLSPFLQPHGQQVPYYLENEPSGYTVREAGPPAFYRPNSDNRRQGGRERLASTNDKGSMAMESAKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGRMLKHKRQRDDGEGRGEVGSAGDMRAANLWPSPLMIKRSKKNSLALSLTADQMVSALLDAEPPILYSEYDPTRPFSEASMMGLLTNLADRELVHMINWAKRVPGFVDLTLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHQRLAQLLLILSHIRHMSNKGMEHLYSMKCKNVVPLYDLLLEMLDAHRLHAPTSRGGASVEETDQSHLATAGSTSSHSLQKYYITGEAEGFPATV Disordered N-terminal domain 1 184 MTMTLHTKASGMALLHQIQGNELEPLNRPQLKIPLERPLGEVYLDSSKPAVYNYPEGAAYEFNAAAAANAQVYGQTGLPYGPGSEAAAFGSNGLGGFPPLNSVSPSPLMLLHPPPQLSPFLQPHGQQVPYYLENEPSGYTVREAGPPAFYRPNSDNRRQGGRERLASTNDKGSMAMESAKETRY Fragment Function arises via a disorder to order transition Protein-protein binding Nuclear magnetic resonance (NMR) 283 5.3 NaCl 100 Sodium azide 0.01% Sodium dihydrogen phosphate 10 Circular dichroism (CD) spectroscopy, far-UV 298 6 Sodium acetate 15 Sodium phosphate 10 Paper 11595744 Warnmark A, Wikstrom A, Wright AP, Gustafsson JA, Hard T 2001 J Biol Chem 276 49 45939-44 The fragment used consisted of residues 1-184. Disordered 221 237 CPATNQCTIDKNRRKSC Fragment Monomeric Function arises via a disorder to order transition Molecular assembly Protein-DNA binding Protein-protein binding Nuclear magnetic resonance (NMR) 6.5 sodium pyrophosphate 40 ZnSO4 50 2H2O Nuclear magnetic resonance (NMR) 6.5 H2O/2H2O 85/15% sodium pyrophosphate 40 ZnSO4 50 Paper 16100953 Schwabe JW, Chapman L, Finch JT, Rhodes D, Neuhaus D 1993 Structure 1 3 187-204 Disordered ERDBD C-terminus 253 262 GGIRKDRRGG Fragment Monomeric Function arises from the disordered state Molecular assembly Protein-DNA binding Nuclear magnetic resonance (NMR) 6.5 2H2O sodium pyrophosphate 40 ZnSO4 50 Nuclear magnetic resonance (NMR) 6.5 H2O/2H2O 85/15% sodium pyrophosphate 40 ZnSO4 50 Paper 16100953 Schwabe JW, Chapman L, Finch JT, Rhodes D, Neuhaus D 1993 Structure 1 3 187-204 AV (6-29-2010) PubMed: 3755102 DNA topoisomerase 1 TOP1_HUMAN EC 5.99.1.2 DNA topoisomerase I Eukaryotic DNA topoisomerase I Human Top1 Human topo I HsTop1 hTop1p hTopo hTopol DNA topoisomerase 1B DNA topoisomerase type 1B TopIB P11387 Hs.472737 TOP1_HUMAN 12644118 Homo sapiens (Human) 765 MSGDHLHNDSQIEADFRLNDSHKHKDKHKDREHRHKEHKKEKDREKSKHSNSEHKDSEKKHKEKEKTKHKDGSSEKHKDKHKDRDKEKRKEEKVRASGDAKIKKEKENGFSSPPQIKDEPEDDGYFVPPKEDIKPLKRPRDEDDADYKPKKIKTEDTKKEKKRKLEEEEDGKLKKPKNKDKDKKVPEPDNKKKKPKKEEEQKWKWWEEERYPEGIKWKFLEHKGPVFAPPYEPLPENVKFYYDGKVMKLSPKAEEVATFFAKMLDHEYTTKEIFRKNFFKDWRKEMTNEEKNIITNLSKCDFTQMSQYFKAQTEARKQMSKEEKLKIKEENEKLLKEYGFCIMDNHKERIANFKIEPPGLFRGRGNHPKMGMLKRRIMPEDIIINCSKDAKVPSPPPGHKWKEVRHDNKVTWLVSWTENIQGSIKYIMLNPSSRIKGEKDWQKYETARRLKKCVDKIRNQYREDWKSKEMKVRQRAVALYFIDKLALRAGNEKEEGETADTVGCCSLRVEHINLHPELDGQEYVVEFDFLGKDSIRYYNKVPVEKRVFKNLQLFMENKQPEDDLFDRLNTGILNKHLQDLMEGLTAKVFRTYNASITLQQQLKELTAPDENIPAKILSYNRANRAVAILCNHQRAPPKTFEKSMMNLQTKIDAKKEQLADARRDLKSAKADAKVMKDAKTKKVVESKKKAVQRLEEQLMKLEVQATDREENKQIALGTSKLNYLDPRITVAWCKKWGVPIEKIYNKTQREKFAWAIDMADEDYEF Disordered - Extended 1 197 MSGDHLHNDSQIEADFRLNDSHKHKDKHKDREHRHKEHKKEKDREKSKHSNSEHKDSEKKHKEKEKTKHKDGSSEKHKDKHKDRDKEKRKEEKVRASGDAKIKKEKENGFSSPPQIKDEPEDDGYFVPPKEDIKPLKRPRDEDDADYKPKKIKTEDTKKEKKRKLEEEEDGKLKKPKNKDKDKKVPEPDNKKKKPKK Function arises from the disordered state Molecular assembly Autoregulatory Disordered region is not essential for protein function Nuclear localization Phosphorylation Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV 298 7.4 Jasco 3000 spectropolarimeter path length 0.1 guanidine hypochlorite 6 KPO4 10 Size exclusion/gel filtration chromatography 298 7.4 flow rate 0.75 Superose 12 (Pharmacia) column KPO4 200 EDTA 1 DTT 1 Sensitivity to proteolysis Paper 8567649 Bharti AK, Olson MO, Kufe DW, Rubin EH 1996 J Biol Chem 271 4 1993-7 9611241 Labourier E, Rossi F, Gallouzi IE, Allemand E, Divita G, Tazi J 1998 Nucleic Acids Res 26 12 2955-2962 10380229 Shaiu WL, Hu T, Hsieh TS 1999 Pac Symp Biocomput 578-589 8631793 Stewart L, Ireton GC, Parker LH, Madden KR, Champoux JJ 1996 J Biol Chem 271 13 7593-7601 8631794 Stewart L, Ireton GC, Champoux JJ 1996 J Biol Chem 271 13 7602-7608 Charged residues contained within the interacting region of topo I/kinase (139 - 175) make electrostatic interactions with SF2/ASF (splice factor). Topo I/kinase phosphorylates at least six members of the SR protein family on serines contained in the RS domain of these proteins. Binding of SR proteins or other nuclear factors to DNA topoisomerase I may be a mechanism through which DNA topoisomerase I enters the nucleus. The N-terminal domain is highly extended and thereby accessible for specific interaction with other proteins. Human DNA topoisomerase I is a constitutively expressed nuclear phospho-protein that localizes to active transcription sites in which its kinase activity may allow this protein to participate in the coordination between transcription and splicing, since sites of transcription in the nucleus colocalize with sites of splicing. (Labourier, et al., 1998) Proposed functions of N-terminus include regulation of Topo I activity through the phosphorylation of the N-terminal domain, phosphorylation by a number of protein kinases, nuclear targeting (NLS), and possible protein-protein interactions between the Topo I N-terminus and other chromosomal proteins. Since this domain is flexible and extended, it may be proficient in providing an interacting surface to allow for binding with other proteins. A 44-residue segment in the human Topo I N-terminus can bind to an abundant nucleolar protein nucleolin. (Shaiu, et al.) The critical residues involved in nucleolin binding appear to be contained in the region of 166 - 210. Nucleolin binding to topo I may be the mechanism by which topo I enters the nucleus. While the 166 - 210 region of topo I does contain a NLS, the 140 - 167 and 1 - 139 regions of topo I also contain NLSs that do not bind nucleolin. (Bharti AK, et al.) Disordered - Extended 174 214 KKPKNKDKDKKVPEPDNKKKKPKKEEEQKWKWWEEERYPEG X-ray crystallography 295 crystallant 6 water 2 duplex oligonucleotide 2 protein 4 Paper 8567649 Bharti AK, Olson MO, Kufe DW, Rubin EH 1996 J Biol Chem 271 4 1993-7 14654701 Christensen MO, Barthelmes HU, Boege F, Mielke C 2003 Nucleic Acids Res 31 24 7255-63 14741206 Frohlich RF, Andersen FF, Westergaard O, Andersen AH, Knudsen BR 2004 J Mol Biol 336 1 93-103 11283003 Lisby M, Olesen JR, Skouboe C, Krogh BO, Straub T, Boege F, Velmurugan S, Martensen PM, Andersen AH, Jayaram M, Westergaard O, Knudsen BR 2001 J Biol Chem 276 23 20220-20227 9488652 Stewart L, Redinbo MR, Qiu X, Hol WG, Champoux JJ 1998 Science 279 5356 1534-1541 Disordered - Extended 627 659 AILCNHQRAPPKTFEKSMMNLQTKIDAKKEQLA X-ray crystallography 295 crystallant 6 water 2 duplex oligonucleotide 2 protein 4 Paper 9488652 Stewart L, Redinbo MR, Qiu X, Hol WG, Champoux JJ 1998 Science 279 5356 1534-1541 Disordered - Extended 636 659 PPKTFEKSMMNLQTKIDAKKEQLA X-ray crystallography 295 crystallant 3 water 3 duplex oligonucleotide 1 Paper 9488644 Redinbo MR, Stewart L, Kuhn P, Champoux JJ, Hol WG 1998 Science 279 5356 1504-1153 Disordered - Extended 634 640 RAPPKTF X-ray crystallography 295 crystallant 6 duplex oligonucleotide 2 protein 4 water 2 X-ray crystallography 295 crystallant 3 duplex oligonucleotide 1 water 3 Paper 10497031 Redinbo MR, Stewart L, Champoux JJ, Hol WG 1999 J Mol Biol 292 3 685-696 9488652 Stewart L, Redinbo MR, Qiu X, Hol WG, Champoux JJ 1998 Science 279 5356 1534-1541 Disordered - Extended 636 640 PPKTF X-ray crystallography 295 crystallant 6 duplex oligonucleotide 2 protein 4 water 2 Paper 9488652 Stewart L, Redinbo MR, Qiu X, Hol WG, Champoux JJ 1998 Science 279 5356 1534-1541 Disordered - Extended 628 635 ILCNHQRA X-ray crystallography 295 crystallant 3 duplex oligonucleotide 1 water 3 Paper 9488644 Redinbo MR, Stewart L, Kuhn P, Champoux JJ, Hol WG 1998 Science 279 5356 1504-1153 Disordered - Extended 713 719 QIALGTS X-ray crystallography 295 crystallant 3 duplex oligonucleotide 1 water 3 Paper 9488644 Redinbo MR, Stewart L, Kuhn P, Champoux JJ, Hol WG 1998 Science 279 5356 1504-1153 Disordered - Extended 711 716 NKQIAL X-ray crystallography 295 crystallant 6 duplex oligonucleotide 2 protein 4 water 2 Paper 9488652 Stewart L, Redinbo MR, Qiu X, Hol WG, Champoux JJ 1998 Science 279 5356 1534-1541 Disordered - Extended 715 719 ALGTS X-ray crystallography 295 crystallant 3 duplex oligonucleotide 1 water 3 Paper 9488644 Redinbo MR, Stewart L, Kuhn P, Champoux JJ, Hol WG 1998 Science 279 5356 1504-1153 Disordered - Extended 636 712 PPKTFEKSMMNLQTKIDAKKEQLADARRDLKSAKADAKVMKDAKTKKVVESKKKAVQRLEEQLMKLEVQATDREENK X-ray crystallography 295 crystallant 3 duplex oligonucleotide 1 water 3 Paper 10497031 Redinbo MR, Stewart L, Champoux JJ, Hol WG 1999 J Mol Biol 292 3 685-696 Disordered - Extended 627 632 AILCNH X-ray crystallography 295 crystallant 3 duplex oligonucleotide 1 water 3 Paper 10497031 Redinbo MR, Stewart L, Champoux JJ, Hol WG 1999 J Mol Biol 292 3 685-696 Disordered - Extended 673 678 KVMKDA X-ray crystallography 295 crystallant 3 duplex oligonucleotide 1 water 3 Paper 10497031 Redinbo MR, Stewart L, Champoux JJ, Hol WG 1999 J Mol Biol 292 3 685-696 Disordered - Extended 708 721 REENKQIALGTSKL X-ray crystallography 295 crystallant 3 duplex oligonucleotide 1 water 3 Paper 10497031 Redinbo MR, Stewart L, Champoux JJ, Hol WG 1999 J Mol Biol 292 3 685-696 Disordered - Extended 712 718 KQIALGT X-ray crystallography 295 crystallant 3 duplex oligonucleotide 1 water 3 Paper 10497031 Redinbo MR, Stewart L, Champoux JJ, Hol WG 1999 J Mol Biol 292 3 685-696 Disordered - Extended 620 633 NRANRAVAILCNHQ X-ray crystallography 295 crystallant 3 duplex oligonucleotide 1 water 3 Paper 10497031 Redinbo MR, Stewart L, Champoux JJ, Hol WG 1999 J Mol Biol 292 3 685-696 Disordered - Extended 642 712 KSMMNLQTKIDAKKEQLADARRDLKSAKADAKVMKDAKTKKVVESKKKAVQRLEEQLMKLEVQATDREENK X-ray crystallography 295 crystallant 3 duplex oligonucleotide 1 water 3 Paper 10497031 Redinbo MR, Stewart L, Champoux JJ, Hol WG 1999 J Mol Biol 292 3 685-696 Disordered - Extended 713 724 QIALGTSKLNYL X-ray crystallography 295 crystallant 3 duplex oligonucleotide 1 water 3 Paper 10497031 Redinbo MR, Stewart L, Champoux JJ, Hol WG 1999 J Mol Biol 292 3 685-696 Disordered - Extended 634 641 RAPPKTFE X-ray crystallography 295 crystallant 3 duplex oligonucleotide 1 water 3 Paper 10497031 Redinbo MR, Stewart L, Champoux JJ, Hol WG 1999 J Mol Biol 292 3 685-696 Disordered - Extended 626 721 VAILCNHQRAPPKTFEKSMMNLQTKIDAKKEQLADARRDLKSAKADAKVMKDAKTKKVVESKKKAVQRLEEQLMKLEVQATDREENKQIALGTSKL X-ray crystallography 295 crystallant 3 duplex oligonucleotide 1 water 3 Paper 10497031 Redinbo MR, Stewart L, Champoux JJ, Hol WG 1999 J Mol Biol 292 3 685-696 Disordered - Extended 633 641 QRAPPKTFE X-ray crystallography 295 crystallant 3 duplex oligonucleotide 1 water 3 Paper 10497031 Redinbo MR, Stewart L, Champoux JJ, Hol WG 1999 J Mol Biol 292 3 685-696 Disordered - Extended 626 632 VAILCNH X-ray crystallography 295 crystallant 3 duplex oligonucleotide 1 water 3 Paper 10497031 Redinbo MR, Stewart L, Champoux JJ, Hol WG 1999 J Mol Biol 292 3 685-696 The loop leading up to His632 (residues 626- 632) is disordered in four out of five structures A-E. His632 may stabilize the transition state of the scissile phosphorus atom that was exposed through nucleophilic attack by an activated C4-oxygen atom of Tyr723. Disordered - Extended 1 174 MSGDHLHNDSQIEADFRLNDSHKHKDKHKDREHRHKEHKKEKDREKSKHSNSEHKDSEKKHKEKEKTKHKDGSSEKHKDKHKDRDKEKRKEEKVRASGDAKIKKEKENGFSSPPQIKDEPEDDGYFVPPKEDIKPLKRPRDEDDADYKPKKIKTEDTKKEKKRKLEEEEDGKLK Function arises from the ordered state Function arises via a disorder to order transition Molecular assembly Nuclear localization Autoregulatory Protein-protein binding Disordered region is not essential for protein function Circular dichroism (CD) spectroscopy, far-UV 310 KPO₄ (pH 7.4) 10 Size exclusion/gel filtration chromatography 298 KPO₄ (pH 7.4) 200 DTT 1 EDTA 1 Paper 8567649 Bharti AK, Olson MO, Kufe DW, Rubin EH 1996 J Biol Chem 271 4 1993-7 10380229 Shaiu WL, Hu T, Hsieh TS 1999 Pac Symp Biocomput 578-589 8631793 Stewart L, Ireton GC, Parker LH, Madden KR, Champoux JJ 1996 J Biol Chem 271 13 7593-7601 Proposed functions of N-terminus include regulation of Topo I activity through the phosphorylation of the N-terminal domain, phosphorylation by a number of protein kinases, nuclear targeting (NLS), and possible protein-protein interactions between the Topo I N-terminus and other chromosomal proteins. Since this domain is flexible and extended, it may be proficient in providing an interacting surface to allow for binding with other proteins. A 44-residue segment in the human Topo I N-terminus can bind to an abundant nucleolar protein nucleolin. (Shaiu, et al.) The critical residues involved in nucleolin binding appear to be contained in the region of 166 - 210. Nucleolin binding to topo I may be the mechanism by which topo I enters the nucleus. While the 166 - 210 region of topo I does contain a NLS, the 140 - 167 and 1 - 139 regions of topo I also contain NLSs that do not bind nucleolin. (Bharti AK, et al.) Disordered - Extended 175 214 KPKNKDKDKKVPEPDNKKKKPKKEEEQKWKWWEEERYPEG Complex Engineered Fragment 1A31A 1A35A X-ray crystallography 295 crystallant 3 water 3 duplex oligonucleotide 1 Paper 8567649 Bharti AK, Olson MO, Kufe DW, Rubin EH 1996 J Biol Chem 271 4 1993-7 14654701 Christensen MO, Barthelmes HU, Boege F, Mielke C 2003 Nucleic Acids Res 31 24 7255-63 14741206 Frohlich RF, Andersen FF, Westergaard O, Andersen AH, Knudsen BR 2004 J Mol Biol 336 1 93-103 11283003 Lisby M, Olesen JR, Skouboe C, Krogh BO, Straub T, Boege F, Velmurugan S, Martensen PM, Andersen AH, Jayaram M, Westergaard O, Knudsen BR 2001 J Biol Chem 276 23 20220-20227 9488644 Redinbo MR, Stewart L, Kuhn P, Champoux JJ, Hol WG 1998 Science 279 5356 1504-1153 Additional UniGene ID: Hs.712686 Additional synonyms that are not specific to humans: Deoxiribonucleate topoisomerase, Deoxiribonucleic topoisomerase, Late protein H6, Nicking-closing enzyme, Omega-protein, Relaxing enzyme, Reverse gyrase, Swivelase, and Untwisting enzyme. DNA topoisomerase 2 TOP2_YEAST EC 5.99.1.3 DNA topoisomerase II Top2 Topo II P06786 TOP2_YEAST 1351262 Saccharomyces cerevisiae (Baker's yeast) 1428 MSTEPVSASDKYQKISQLEHILKRPDTYIGSVETQEQLQWIYDEETDCMIEKNVTIVPGLFKIFDEILVNAADNKVRDPSMKRIDVNIHAEEHTIEVKNDGKGIPIEIHNKENIYIPEMIFGHLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTEFILETADLNVGQKYVQKWENNMSICHPPKITSYKKGPSYTKVTFKPDLTRFGMKELDNDILGVMRRRVYDINGSVRDINVYLNGKSLKIRNFKNYVELYLKSLEKKRQLDNGEDGAAKSDIPTILYERINNRWEVAFAVSDISFQQISFVNSIATTMGGTHVNYITDQIVKKISEILKKKKKKSVKSFQIKNNMFIFINCLIENPAFTSQTKEQLTTRVKDFGSRCEIPLEYINKIMKTDLATRMFEIADANEENALKKSDGTRKSRITNYPKLEDANKAGTKEGYKCTLVLTEGDSALSLAVAGLAVVGRDYYGCYPLRGKMLNVREASADQILKNAEIQAIKKIMGLQHRKKYEDTKSLRYGHLMIMTDQDHDGSHIKGLIINFLESSFPGLLDIQGFLLEFITPIIKVSITKPTKNTIAFYNMPDYEKWREEESHKFTWKQKYYKGLGTSLAQEVREYFSNLDRHLKIFHSLQGNDKDYIDLAFSKKKADDRKEWLRQYEPGTVLDPTLKEIPISDFINKELILFSLADNIRSIPNVLDGFKPGQRKVLYGCFKKNLKSELKVAQLAPYVSECTAYHHGEQSLAQTIIGLAQNFVGSNNIYLLLPNGAFGTRATGGKDAAAARYIYTELNKLTRKIFHPADDPLYKYIQEDEKTVEPEWYLPILPMILVNGAEGIGTGWSTYIPPFNPLEIIKNIRHLMNDEELEQMHPWFRGWTGTIEEIEPLRYRMYGRIEQIGDNVLEITELPARTWTSTIKEYLLLGLSGNDKIKPWIKDMEEQHDDNIKFIITLSPEEMAKTRKIGFYERFKLISPISLMNMVAFDPHGKIKKYNSVNEILSEFYYVRLEYYQKRKDHMSERLQWEVEKYSFQVKFIKMIIEKELTVTNKPRNAIIQELENLGFPRFNKEGKPYYGSPNDEIAEQINDVKGATSDEEDEESSHEDTENVINGPEELYGTYEYLLGMRIWSLTKERYQKLLKQKQEKETELENLLKLSAKDIWNTDLKAFEVGYQEFLQRDAEARGGNVPNKGSKTKGKGKRKLVDDEDYDPSKKNKKSTARKGKKIKLEDKNFERILLEQKLVTKSKAPTKIKKEKTPSVSETKTEEEENAPSSTSSSSIFDIKKEDKDEGELSKISNKFKKISTIFDKMGSTSATSKENTPEQDDVATKKNQTTAKKTAVKPKLAKKPVRKQQKVVELSGESDLEILDSYTDREDSNKDEDDAIPQRSRRQRSSRAASVPKKSYVETLELSDDSFIEDDEEENQGSDVSFNEED Disordered 410 420 NALKKSDGTRK Fragment 1BGWA Relationship to function unknown Unknown Unknown X-ray crystallography 277 protein 3 reservoir buffer 3 Paper 8538787 Berger JM, Gamblin SJ, Harrison SC, Wang JC 1996 Nature 379 6562 225-32 DP00076 - The experimental fragment was composed of residues 410 - 1202. Disordered 634 681 DKDYIDLAFSKKKADDRKEWLRQYEPGTVLDPTLKEIPISDFINKELI Fragment 1BGWA Relationship to function unknown Unknown Unknown X-ray crystallography 277 protein 3 reservoir buffer 3 Paper 8538787 Berger JM, Gamblin SJ, Harrison SC, Wang JC 1996 Nature 379 6562 225-32 DP00076 - The experimental fragment was composed of residues 410 - 1202. Disordered 1077 1107 EQINDVKGATSDEEDEESSHEDTENVINGPE Fragment 1BGWA Relationship to function unknown Unknown Unknown X-ray crystallography 277 protein 3 reservoir buffer 3 Paper 8538787 Berger JM, Gamblin SJ, Harrison SC, Wang JC 1996 Nature 379 6562 225-32 12022860 Dunker AK, Brown CJ, Lawson JD, Iakoucheva LM, Obradović Z 2002 Biochemistry 41 21 6573-82 DP00076 - The experimental fragment was composed of residues 410 - 1202. Disordered 1179 1202 GNVPNKGSKTKGKGKRKLVDDEDY Fragment 1BGWA Relationship to function unknown Unknown Unknown X-ray crystallography 277 protein 3 reservoir buffer 3 Paper 8538787 Berger JM, Gamblin SJ, Harrison SC, Wang JC 1996 Nature 379 6562 225-32 DP00076 - The experimental fragment was composed of residues 410 - 1202. Disordered 485 489 SADQI Fragment Monomeric Native 1BJTA Function arises from the disordered state Unknown Unknown X-ray crystallography 277 protein 3 reservoir buffer 3 Paper 8538787 Berger JM, Gamblin SJ, Harrison SC, Wang JC 1996 Nature 379 6562 225-32 DP00076 - The experimental fragment was composed of residues 410 - 1202. Disordered 1072 1106 NDEIAEQINDVKGATSDEEDEESSHEDTENVINGP Fragment Monomeric Native 1BJTA Function arises from the disordered state Unknown Unknown X-ray crystallography 277 protein 3 reservoir buffer 3 Paper 8538787 Berger JM, Gamblin SJ, Harrison SC, Wang JC 1996 Nature 379 6562 225-32 DP00076 - The experimental fragment was composed of residues 410 - 1202. Disordered 527 531 QDHDG Fragment Monomeric Native 1BJTA Function arises from the disordered state Unknown Unknown X-ray crystallography 277 protein 3 reservoir buffer 3 Paper 8538787 Berger JM, Gamblin SJ, Harrison SC, Wang JC 1996 Nature 379 6562 225-32 DP00076 - The experimental fragment was composed of residues 410 - 1202. Disordered 631 652 QGNDKDYIDLAFSKKKADDRKE Fragment Monomeric Native 1BJTA Function arises from the disordered state Entropic chain Flexible linkers/spacers X-ray crystallography 277 protein 3 reservoir buffer 3 Paper 8538787 Berger JM, Gamblin SJ, Harrison SC, Wang JC 1996 Nature 379 6562 225-32 DP00076 - The experimental fragment was composed of residues 410 - 1202. Disordered 660 674 GTVLDPTLKEIPISD Fragment Monomeric Native 1BJTA Function arises from the disordered state Entropic chain Flexible linkers/spacers Unknown X-ray crystallography 277 protein 3 reservoir buffer 3 Paper 8538787 Berger JM, Gamblin SJ, Harrison SC, Wang JC 1996 Nature 379 6562 225-32 DP00076 - The experimental fragment was composed of residues 410 - 1202. Disordered 1179 1201 GNVPNKGSKTKGKGKRKLVDDED Fragment Monomeric Native 1BJTA Function arises from the disordered state Unknown Unknown X-ray crystallography 277 protein 3 reservoir buffer 3 Paper 8538787 Berger JM, Gamblin SJ, Harrison SC, Wang JC 1996 Nature 379 6562 225-32 DP00076 - The experimental fragment was composed of residues 410 - 1202. Disordered 1203 1428 DPSKKNKKSTARKGKKIKLEDKNFERILLEQKLVTKSKAPTKIKKEKTPSVSETKTEEEENAPSSTSSSSIFDIKKEDKDEGELSKISNKFKKISTIFDKMGSTSATSKENTPEQDDVATKKNQTTAKKTAVKPKLAKKPVRKQQKVVELSGESDLEILDSYTDREDSNKDEDDAIPQRSRRQRSSRAASVPKKSYVETLELSDDSFIEDDEEENQGSDVSFNEED Monomeric Native Function arises from the disordered state Unknown Unknown Paper 10380229 Shaiu WL, Hu T, Hsieh TS 1999 Pac Symp Biocomput 578-589 12022860 Dunker AK, Brown CJ, Lawson JD, Iakoucheva LM, Obradović Z 2002 Biochemistry 41 21 6573-82 The C-terminal domain is enriched in charged amino acids and hypersensitive to protease digestion, both indications that the region is disordered. PMID 8538787, erratum in: Nature 1996 Mar 14;380(6570):179. Regulatory protein ADR1 ADR1_YEAST Transcription factor ADR1 P07248 ADR1_YEAST 56757368 Saccharomyces cerevisiae (Baker's yeast) 1323 MANVEKPNDCSGFPVVDLNSCFSNGFNNEKQEIEMETDDSPILLMSSSASRENSNTFSVIQRTPDGKIITTNNNMNSKINKQLDKLPENLRLNGRTPSGKLRSFVCEVCTRAFARQEHLKRHYRSHTNEKPYPCGLCNRCFTRRDLLIRHAQKIHSGNLGETISHTKKVSRTITKARKNSASSVKFQTPTYGTPDNGNFLNRTTANTRRKASPEANVKRKYLKKLTRRASFSAQSASSYALPDQSSLEQHPKDRVKFSTPELVPLDLKNPELDSSFDLNMNLDLNLNLDSNFNIALNRSDSSGSTMNLDYKLPESANNYTYSSGSPTRAYVGANTNSKNASFNDADLLSSSYWIKAYNDHLFSVSESDETSPMNSELNDTKLIVPDFKSTIHHLKDSRSSSWTVAIDNNSNNNKVSDNQPDFVDFQELLDNDTLGNDLLETTAVLKEFELLHDDSVSATATSNEIDLSHLNLSNSPISPHKLIYKNKEGTNDDMLISFGLDHPSNREDDLDKLCNMTRDVQAIFSQYLKGEESKRSLEDFLSTSNRKEKPDSGNYTFYGLDCLTLSKISRALPASTVNNNQPSHSIESKLFNEPMRNMCIKVLRYYEKFSHDSSESVMDSNPNLLSKELLMPAVSELNEYLDLFKNNFLPHFPIIHPSLLDLDLDSLQRYTNEDGYDDAENAQLFDRLSQGTDKEYDYEHYQILSISKIVCLPLFMATFGSLHKFGYKSQTIELYEMSRRILHSFLETKRRCRSTTVNDSYQNIWLMQSLILSFMFALVADYLEKIDSSLMKRQLSALCSTIRSNCLPTISANSEKSINNNNEPLTFGSPLQYIIFESKIRCTLMAYDFCQFLKCFFHIKFDLSIKEKDVETIYIPDNESKWASESIICNGHVVQKQNFYDFRNFYYSFTYGHLHSIPEFLGSSMIYYEYDLRKGTKSHVFLDRIDTKRLERSLDTSSYGNDNMAATNKNIAILIDDTIILKNNLMSMRFIKQIDRSFTEKVRKGQIAKIYDSFLNSVRLNFLKNYSVEVLCEFLVALNFSIRNISSLYVEEESDCSQRMNSPELPRIHLNNQALSVFNLQGYYYCFILIIKFLLDFEATPNFKLLRIFIELRSLANSILLPTLSRLYPQEFSGFPDVVFTQQFINKDNGMLVPGLSANEHHNGASAAVKTKLAKKINVEGLAMFINEILVNSFNDTSFLNMEDPIRNEFSFDNGHRAVTDLPRSAHFLSDTGLEGINFSGLNDSHQTVSTLNLLRYGENHSSKHKNGGKGQGFAEKYQLSLKYVTIAKLFFTNVKENYIHCHMLDKMASDFHTLENHLKGNS Disordered - Extended 75 104 MNSKINKQLDKLPENLRLNGRTPSGKLRSF Engineered 1ADRA 2ADRA Function arises via a disorder to order transition Molecular assembly Protein-DNA binding Nuclear magnetic resonance (NMR) 310 6.8 Nuclear magnetic resonance (NMR) 288 6.1 Nuclear magnetic resonance (NMR) 290 6.3 Paper 9642072 Hyre DE, Klevit RE 1998 Journal of Molecular Biology 279 4 929-943 3515197 Hartshorne TA, Blumberg H, Young ET 1986 Nature 320 6059 283-7 Disordered - Extended 155 161 HSGNLGE Engineered Function arises via a disorder to order transition Molecular assembly Protein-DNA binding Nuclear magnetic resonance (NMR) 310 6.8 Nuclear magnetic resonance (NMR) 288 6.1 Nuclear magnetic resonance (NMR) 290 6.3 Paper 9642072 Hyre DE, Klevit RE 1998 Journal of Molecular Biology 279 4 929-943 3515197 Hartshorne TA, Blumberg H, Young ET 1986 Nature 320 6059 283-7 Proto-oncogene protein c-fos FOS_HUMAN Cellular oncogene fos G0/G1 switch regulatory protein 7 Transcription factor c-Fos P01100 Hs.707896 FOS_HUMAN 120470 Homo sapiens (Human) 380 MMFSGFNADYEASSSRCSSASPAGDSLSYYHSPADSFSSMGSPVNAQDFCTDLAVSSANFIPTVTAISTSPDLQWLVQPALVSSVAPSQTRAPHPFGVPAPSAGAYSRAGVVKTMTGGRAQSIGRRGKVEQLSPEEEEKRRIRRERNKMAAAKCRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEKLEFILAAHRPACKIPDDLGFPEEMSVASLDLTGGLPEVATPESEEAFTLPLLNDPEPKPSVEPVKSISSMELKTEPFDDFLFPASSRPSGSETARSVPDMDLSGSFYAADWEPLHSGSLGMGPMATELEPLCTPVVTCTPSCTAYTSSFVFTYPEADSFPSCAAAHRKGSSSNEPSSDSLSSPTLLAL Disordered - Extended FosAD - Fragment 216 380 MSVASLDLTGGLPEVATPESEEAFTLPLLNDPEPKPSVEPVKSISSMELKTEPFDDFLFPASSRPSGSETARSVPDMDLSGSFYAADWEPLHSGSLGMGPMATELEPLCTPVVTCTPSCTAYTSSFVFTYPEADSFPSCAAAHRKGSSSNEPSSDSLSSPTLLAL Fragment Function arises via a disorder to order transition Molecular assembly Protein-protein binding Autoregulatory Circular dichroism (CD) spectroscopy, near-UV sodium phosphate 10 NaCl 1 DTT 1 Nuclear magnetic resonance (NMR) 298 d₁₀-DTT 1 NaCl 150 sodium phosphate 10 Size exclusion/gel filtration chromatography DTT 1 NaCl 150 sodium phosphate 10 Paper 10704222 Campbell KM, Terrell AR, Laybourn PJ, Lumb KJ 2000 Biochemistry 39 10 2708-13 11749217 Flaugh SL, Lumb KJ 2001 Biomacromolecules 2 2 538-540 It has been shown that the active acidic and proline-rich C-terminal activation domain of human c-Fos is structurally disordered and has the properties of an unfolded protein. It was found that disorder was not due to the deletion of a sequence necessary for structure. Structural disorder has also been found with the acidic activation domains from VP16, NF-kB, and p53. Results for c-Fos and for the p53 proline-rich activation domain have indicated that proline-rich activation domains can exhibit structural disorder. Proposed mechanistic advantages of these disordered protein domains include increased binding specificity at the expense of thermodynamic stability, regulation of proteolysis, and the ability to recognize a range of different proteins. The C-terminal activation domain contains a number of phosphorylation sites that moderate Fos activity. The conformational freedom of the structurally disordered C-terminal activation domain contributes to the functional diversity of c-Fos by allowing the formation of numerous protein complexes (with transcription factors and with regulatory kinases). Estrogen receptor beta [Isoform 1 (Beta-1)] ESR2_HUMAN ER-beta Nuclear receptor subfamily 3 group A member 2 Q92731-1 Hs.525392 ESR2_HUMAN 6166154 Homo sapiens (Human) 530 MDIKNSPSSLNSPSSYNCSQSILPLEHGSIYIPSSYVDSHHEYPAMTFYSPAVMNYSIPSNVTNLEGGPGRQTTSPNVLWPTPGHLSPLVVHRQLSHLYAEPQKSPWCEARSLEHTLPVNRETLKRKVSGNRCASPVTGPGSKRDAHFCAVCSDYASGYHYGVWSCEGCKAFFKRSIQGHNDYICPATNQCTIDKNRRKSCQACRLRKCYEVGMVKCGSRRERCGYRLVRRQRSADEQLHCAGKAKRSGGHAPRVRELLLDALSPEQLVLTLLEAEPPHVLISRPSAPFTEASMMMSLTKLADKELVHMISWAKKIPGFVELSLFDQVRLLESCWMEVLMMGLMWRSIDHPGKLIFAPDLVLDRDEGKCVEGILEIFDMLLATTSRFRELKLQHKEYLCVKAMILLNSSMYPLVTATQDADSSRKLAHLLNAVTDALVWVIAKSGISSQQQSMRLANLLMLLSHVRHASNKGMEHLLNMKCKNVVPVYDLLLEMLNAHVLRGCKSSITGSECSPAEDSKSKEGSQNPQSQ Disordered N-terminal domain 1 103 MDIKNSPSSLNSPSSYNCSQSILPLEHGSIYIPSSYVDSHHEYPAMTFYSPAVMNYSIPSNVTNLEGGPGRQTTSPNVLWPTPGHLSPLVVHRQLSHLYAEPQ Fragment Native Relationship to function unknown Substrate/ligand binding Protein-protein binding Nuclear magnetic resonance (NMR) 283 6.5 Sodium phosphate 20 Sodium azide 0.01% Circular dichroism (CD) spectroscopy, far-UV 298 6 Sodium azide 15 Sodium phosphate 10 Paper 11595744 Warnmark A, Wikstrom A, Wright AP, Gustafsson JA, Hard T 2001 J Biol Chem 276 49 45939-44 The fragment consisted of residues 1-103. Additional UniGene ID: Hs.660607 AV (6-29-2010) PubMed: 11595744 Cyclic AMP-responsive element-binding protein 1 CREB1_RAT cAMP-responsive element-binding protein 1 CREB-1 P15337 Rn.90061 CREB1_RAT 117435 Rattus norvegicus (Rat) 341 MTMESGAENQQSGDAAVTEAENQQMTVQAQPQIATLAQVSMPAAHATSSAPTVTLVQLPNGQTVQVHGVIQAAQPSVIQSPQVQTVQSSCKDLKRLFSGTQISTIAESEDSQESVDSVTDSQKRREILSRRPSYRKILNDLSSDAPGVPRIEEEKSEEETSAPAITTVTVPTPIYQTSSGQYIAITQGGAIQLANNGTDGVQGLQTLTMTNAAATQPGTTILQYAQTTDGQQILVPSNQVVVQAASGDVQTYQIRTAPTSTIAPGVVMASSPALPTQPAEEAARKREVRLMKNREAARECRRKKKEYVKCLENRVAVLENQNKTLIEELKALKDLYCHKSD Disordered pKID 101 120 QISTIAESEDSQESVDSVTD Engineered Fragment 1KDXB Function arises from the disordered state Unknown Unknown Nuclear magnetic resonance (NMR) 315 5.5 acetate-d buffer guanidinium hydrochloride solubilization 0.6 NaCl salt, buffer 50 Tris-d buffer 20 Nuclear magnetic resonance (NMR) 290 5.5 acetate-d buffer guanidinium hydrochloride solubilization 0.6 NaCl salt, buffer 50 Tris-d buffer 20 Paper 9413984 Radhakrishnan I, Perez-Alvarado GC, Parker D, Dyson HJ, Montminy MR, Wright PE 1997 Cell 91 6 741-752 Upon binding to the KIX domain of the CREB binding protein this region remains disordered. The PDB reference 1KDX chain B has the disordered region from residues 101-118. Disordered pKID 119 146 TDSQKRREILSRRPSYRKILNDLSSDAP Engineered Fragment 1KDXB Function arises via a disorder to order transition Molecular assembly Protein-protein binding Nuclear magnetic resonance (NMR) 315 5.5 acetate-d buffer guanidinium hydrochloride solubilization 0.6 NaCl salt, buffer 50 Tris-d buffer 20 Nuclear magnetic resonance (NMR) 290 5.5 acetate-d buffer guanidinium hydrochloride solubilization 0.6 NaCl salt, buffer 50 Tris-d buffer 20 Paper 9413984 Radhakrishnan I, Perez-Alvarado GC, Parker D, Dyson HJ, Montminy MR, Wright PE 1997 Cell 91 6 741-752 9688563 Radhakrishnan I, Perez-Alvarado GC, Dyson HJ, Wright PE 1998 FEBS Lett 430 3 317-322 Upon binding to the KIX domain of the CREB binding protein this region forms two alpha helices, alphaA and alphaB. The two fold into mutually perpendicular helices that run from Asp-120 to Ser-129 and Pro-132 to Asp-144, respectively. Disordered pKID 146 160 PGVPRIEEEKSEEET Engineered Fragment 1KDXB Function arises from the disordered state Unknown Unknown Nuclear magnetic resonance (NMR) 315 5.5 acetate-d buffer guanidinium hydrochloride solubilization 0.6 NaCl salt, buffer 50 Tris-d buffer 20 Nuclear magnetic resonance (NMR) 290 5.5 acetate-d buffer guanidinium hydrochloride solubilization 0.6 NaCl salt, buffer 50 Tris-d buffer 20 Paper 9413984 Radhakrishnan I, Perez-Alvarado GC, Parker D, Dyson HJ, Montminy MR, Wright PE 1997 Cell 91 6 741-752 Upon binding to the KIX domain of the CREB binding protein this region remains unstructured. The PDB reference 1KDX chain B has the disordered region from residues 147-160. Transcription initiation factor TFIID subunit 1 TAF1_DROME EC=2.7.11.1 Transcription initiation factor TFIID 230 kDa subunit TAFII-230 TAFII250 TBP-associated factor 230 kDa p230 Transcription factor dTAFII230 P51123 Dm.7380 TAF1_DROME 71153181 Drosophila melanogaster (Fruit fly) 2068 MEMESDNSDDEGSIGNGLDLTGILFGNIDSEGRLLQDDDGEGRGGTGFDAELRENIGSLSKLGLDSMLLEVIDLKEAEPPSDDEEEEDARPSAVSASGGMSAFDALKAGVKREEREDGAVKAQDDAIDYSDITELSEDCPRTPPEETSTYDDLEDAIPASKVEAKLTKDDKELMPPPSAPMRSGSGGGIEEPAKSNDASSPSDDSKSTDSKDADRKLDTPLADILPSKYQNVDVRELFPDFRPQKVLRFSRLFGPGKPTSLPQIWRHVRQSRRKRNQSRDQKTTNTGGSDSPSDTEEPRKRGFSLHYAAEPTPAECMSDDEDKLLGDFNSEDVRPEGPDNGENSDQKPKVADWRFGPAQIWYDILEVPDSGEGFNYGFKTKAASTSSQQQLKDERRVKSPEDDVEDPSIADDAFLMVSQLHWEDDVVWDGNDIKAKVLQKLNSKTNAAGWLPSSGSRTAGAFSQPGKPSMPVGSGSSKQGSGASSKKAQQNAQAKPAEAPDDTWYSLFPVENEELIYYKWEDEVIWDAQQVSKVPKPKVLTLDPNDENIILGIPDDIDPSKINKSTGPPPKIKIPHPHVKKSKILLGKAGVINVLAEDTPPPPPKSPDRDPFNISNDTYYTPKTEPTLRLKVGGNLIQHSTPVVELRAPFVPTHMGPMNVRAFHRPPLKKYSHGPMAQSIPHPVFPLLKTIAKKAKQREVERIASGGGDVFFMRNPEDLSGRDGDIVLAEFCEEHPPLINQVGMCSKIKNYYKRKAEKDSGPQDYVYGEVAFAHTSPFLGILHPGQCIQAIENNMYRAPIYPHKMAHNDFLVIRTRNNYWIRSVNSIYTVGQECPLYEVPGPNSKRANNFTRDFLQVFIYRLFWKSRDNPRRIRMDDIKQAFPAHSESSIRKRLKQCADFKRTGMDSNWWVIKPEFRLPSEEEIRAMVSPEQCCAYFSMIAAEQRLKDAGYGEKFLFAPQEDDDEEAQLKLDDEVKVAPWNTTRAYIQAMRGKCLLQLSGPADPTGCGEGFSYVRVPNKPTQTKEEQESQPKRSVTGTDADLRRLPLQRAKELLRQFKVPEEEIKKLSRWEVIDVVRTLSTEKAKAGEEGMDKFSRGNRFSIAEHQERYKEECQRIFDLQNRVLASSEVLSTDEAESSASEESDLEELGKNLENMLSNKKTSTQLSREREELERQELLRQLDEEHGGPSGSGGAKGAKGKDDPGQQMLATNNQGRILRITRTFRGNDGKEYTRVETVRRQPVIDAYIKIRTTKDEQFIKQFATLDEQQKEEMKREKRRIQEQLRRIKRNQERERLAQLAQNQKLQPGGMPTSLGDPKSSGGHSHKERDSGYKEVSPSRKKFKLKPDLKLKCGACGQVGHMRTNKACPLYSGMQSSLSQSNPSLADDFDEQSEKEMTMDDDDLVNVDGTKVTLSSKILKRHGGDDGKRRSGSSSGFTLKVPRDAMGKKKRRVGGDLHCDYLQRHNKTANRRRTDPVVVLSSILEIIHNELRSMPDVSPFLFPVSAKKVPDYYRVVTKPMDLQTMREYIRQRRYTSREMFLEDLKQIVDNSLIYNGPQSAYTLAAQRMFSSCFELLAEREDKLMRLEKAINPLLDDDDQVALSFIFDKLHSQIKQLPESWPFLKPVNKKQVKDYYTVIKRPMDLETIGKNIEAHRYHSRAEYLADIELIATNCEQYNGSDTRYTKFSKKILEYAQTQLIEFSEHCGQLENNIAKTQERARENAPEFDEAWGNDDYNFDRGSRASSPGDDYIDVEGHGGHASSSNSIHRSMGAEAGSSHTAPAVRKPAPPGPGEVKRGRGRPRKQRDPVEEDLQCSTDDEDDDEEEDFQEVSEDENNAASILDQGERINAPADAMDGMFDPKNIKTEIDLEAHQMADESMDVDPNYDPSDFLAMHKQRQSLGEPSSLQGAFTNFLSHEQDDNGPYNPAEASTSAASGADLGMDASMAMQMAPEMPVNTMNNGMGIDDDLDISESDEEDDGSRVRIKKEVFDDGDYALQHQQMGQAASQSQIYMVDSSNEPTTLDYQQPPQLDFQQVQEMEQLQHQVMPPMQSEQLQQQQTPQGDNDYAWTF Disordered 11 77 EGSIGNGLDLTGILFGNIDSEGRLLQDDDGEGRGGTGFDAELRENIGSLSKLGLDSMLLEVIDLKEA Fragment Native 1TBAA Function arises via a disorder to order transition Protein-protein binding Nuclear magnetic resonance (NMR) 298 7 Varian 600 MHz spectrometer protein sample 0.7 H2O 95 D2O 5 Paper 9741622 Liu D, Ishima R, Tong KI, Bagby S, Kokubo T, Muhandiram DR, Kay LE, Nakatani Y, Ikura M 1998 Cell 94 5 573-583 AV (6-29-2010) PubMed: 9741622 Eukaryotic initiation factor 4F subunit p150 IF4F1_YEAST eIF-4F p150 eIF4F p150 eIF4G1 mRNA cap-binding protein complex subunit p150 Tif4631p P39935 IF4F1_YEAST 1708417 Saccharomyces cerevisiae (Baker's yeast) 952 MTDETAHPTQSASKQESAALKQTGDDQQESQQQRGYTNYNNGSNYTQKKPYNSNRPHQQRGGKFGPNRYNNRGNYNGGGSFRGGHMGANSSNVPWTGYYNNYPVYYQPQQMAAAGSAPANPIPVEEKSPVPTKIEITTKSGEHLDLKEQHKAKLQSQERSTVSPQPESKLKETSDSTSTSTPTPTPSTNDSKASSEENISEAEKTRRNFIEQVKLRKAALEKKRKEQLEGSSGNNNIPMKTTPENVEEKGSDKPEVTEKTKPAEEKSAEPEVKQETPAEEGEQGEKGQIKEESTPKVLTFAERLKLKKQQKEREEKTEGKENKEVPVQEETKSAIESAPVPPSEQVKEETEVAETEQSNIDESATTPAIPTKSDEAEAEVEAEAGDAGTKIGLEAEIETTTDETDDGTNTVSHILNVLKDATPIEDVFSFNYPEGIEGPDIKYKKEHVKYTYGPTFLLQFKDKLNVKADAEWVQSTASKIVIPPGMGRGNRSRDSGRFGNNSSRGHDFRNTSVRNMDDRANSRTSSKRRSKRMNDDRRSNRSYTSRRDRERGSYRNEEKREDDKPKEEVAPLVPSANRWVPKFKSKKTEKKLAPDGKTELLDKDEVERKMKSLLNKLTLEMFDAISSEILAIANISVWETNGETLKAVIEQIFLKACDEPHWSSMYAQLCGKVVKELNPDITDETNEGKTGPKLVLHYLVARCHAEFDKGWTDKLPTNEDGTPLEPEMMSEEYYAAASAKRRGLGLVRFIGFLYRLNLLTGKMMFECFRRLMKDLTDSPSEETLESVVELLNTVGEQFETDSFRTGQATLEGSQLLDSLFGILDNIIQTAKISSRIKFKLIDIKELRHDKNWNSDKKDNGPKTIQQIHEEEERQRQLKNNSRSNSRRTNNSSNRHSFRRDAPPASKDSFITTRTYSQRNSQRAPPPKEEPAAPTSTATNMFSALMGESDDEE Disordered - Extended 393 490 LEAEIETTTDETDDGTNTVSHILNVLKDATPIEDVFSFNYPEGIEGPDIKYKKEHVKYTYGPTFLLQFKDKLNVKADAEWVQSTASKIVIPPGMGRGN Complex Fragment Function arises via a disorder to order transition Molecular assembly Protein-protein binding SDS-PAGE gel, Aberrant mobility on Nuclear magnetic resonance (NMR) 299 7.5 Sensitivity to proteolysis Paper 10409688 Hershey PE, McWhirter SM, Gross JD, Wagner G, Alber T, Sachs AB 1999 J Biol Chem 274 30 21297-304 Additional UniProt IDs: B3LI68 (Strain RM11-1a) and C7GQ70 (Strain JAY291) General control protein GCN4 GCN4_YEAST Amino acid biosynthesis regulatory protein Transcription factor GCN4 P03069 GCN4_YEAST 121066 Saccharomyces cerevisiae (Baker's yeast) 281 MSEYQPSLFALNPMGFSPLDGSKSTNENVSASTSTAKPMVGQLIFDKFIKTEEDPIIKQDTPSNLDFDFALPQTATAPDAKTVLPIPELDDAVVESFFSSSTDSTPMFEYENLEDNSKEWTSLFDNDIPVTTDDVSLADKAIESTEEVSLVPSNLEVSTTSFLPTPVLEDAKLTQTRKVKKPNSVVKKSHHVGKDDESRLDHLGVVAYNRKQRSIPLSPIVPESSDPAALKRARNTEAARRSRARKLQRMKQLEDKVEELLSKNYHLENEVARLKKLVGER Disordered DNA binding domain 225 281 SDPAALKRARNTEAARRSRARKLQRMKQLEDKVEELLSKNYHLENEVARLKKLVGER Complex Native Function arises via a disorder to order transition Protein-DNA binding Circular dichroism (CD) spectroscopy, far-UV 298 7 KCl 200 potassium phosphate 50 Size exclusion/gel filtration chromatography Paper 2145515 Weiss MA, Ellenberger T, Wobbe CR, Lee JP, Harrison SC, Struhl K 1990 Nature 347 6293 575-8 Protein max [Isoform 1] MAX_HUMAN Myc-associated factor X p21 Max P61244 Hs.285354 MAX_HUMAN 47117704 Homo sapiens (Human) 160 MSDNDDIEVESDEEQPRFQSAADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQVRALEKARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQSRKKLRMEAS Disordered N terminal to b/HLH/Z region 1 110 MSDNDDIEVESDEEQPRFQSAADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQVRALEKARSSAQ Fragment Protein-DNA binding Circular dichroism (CD) spectroscopy, far-UV 310 6.8 Jasco J-720 spectropolarimeter sodium phosphate buffer 20 NaCl 150 MgCl2 10 Analytical ultracentrifugation 310 6.8 Beckman Optima XL-A analytical ultracentrifuge MgCl2 10 NaCl 150 sodium phosphate buffer 20 speed 18000 Paper 9399572 Horiuchi M, Kurihara Y, Katahira M, Maeda T, Saito T, Uesugi S 1997 J Biochem (Tokyo) 122 4 711-6 The experimental sequence consisted of the first 110 residues of Max. Additional UniGene ID: Hs.712926 Previous entry DP00084 has been split into canonical isoform 1 (DP00084) and isoform 2 (DP00084_A002). Protein max [Isoform 2] MAX_HUMAN Myc-associated factor X p21 Max P61244-2 Hs.285354 MAX_HUMAN 47117704 Homo sapiens (Human) 151 MSDNDDIEVESDADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQVRALEKARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQSRKKLRMEAS Disordered N-terminal 1 12 MSDNDDIEVESD Engineered Function arises from the disordered state Unknown Unknown Nuclear magnetic resonance (NMR) 308 6.8 D2O 10 KCl 100 NaN3 50 Phosphate 50 DSS Circular dichroism (CD) spectroscopy, far-UV 293 6.8 KCl 100 Sodium Phosphate 50 Paper 16171389 Naud JF, McDuff FO, Sauve S, Montagne M, Webb BA, Smith SP, Chabot B, Lavigne P 2005 Biochemistry 44 38 12746-12758 Disordered C-terminal 95 151 KARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQSRKKLRMEAS Engineered Function arises from the disordered state Unknown Unknown Nuclear magnetic resonance (NMR) 308 6.8 D2O 10 DSS KCl 100 NaN3 50 Phosphate 50 Circular dichroism (CD) spectroscopy, far-UV 293 6.8 KCl 100 Sodium Phosphate 50 Paper 16171389 Naud JF, McDuff FO, Sauve S, Montagne M, Webb BA, Smith SP, Chabot B, Lavigne P 2005 Biochemistry 44 38 12746-12758 Additional UniGene ID: Hs.712926 Previous entry DP00084 has been split into canonical isoform 1 (DP00084) and isoform 2 (DP00084_A002). Transcription factor p65 TF65_HUMAN Nuclear factor NF-kappa-B p65 subunit Transcription factor NF-kappa B p65 Q04206 Hs.502875 TF65_HUMAN 62906901 Homo sapiens (Human) 551 MDELFPLIFPAEPAQASGPYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINGYTGPGTVRISLVTKDPPHRPHPHELVGKDCRDGFYEAELCPDRCIHSFQNLGIQCVKKRDLEQAISQRIQTNNNPFQVPIEEQRGDYDLNAVRLCFQVTVRDPSGRPLRLPPVLPHPIFDNRAPNTAELKICRVNRNSGSCLGGDEIFLLCDKVQKEDIEVYFTGPGWEARGSFSQADVHRQVAIVFRTPPYADPSLQAPVRVSMQLRRPSDRELSEPMEFQYLPDTDDRHRIEEKRKRTYETFKSIMKKSPFSGPTDPRPPPRRIAVPSRSSASVPKPAPQPYPFTSSLSTINYDEFPTMVFPSGQISQASALAPAPPQVLPQAPAPAPAPAMVSALAQAPAPVPVLAPGPPQAVAPPAPKPTQAGEGTLSEALLQLQFDDEDLGALLGNSTDPAVFTDLASVDNSEFQQLLNQGIPVAPHTTEPMLMEYPEAITRLVTGAQRPPDPAPAPLGAPGLPNGLLSGDEDFSSIADMDFSALLSQISS Disordered - Extended Transactivation domain 1 (TA1) 522 551 GLPNGLLSGDEDFSSIADMDFSALLSQISS Function arises via a disorder to order transition Modification site Molecular assembly Autoregulatory Transactivation (transcriptional activation) Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV 293 quartz cells (1 mm path length) Nuclear magnetic resonance (NMR) 5.5 10% D₂O 90% H₂O NaCl 50 protein 2 sodium phosphate 50 Paper 1935902 Schmitz ML, Baeuerle PA 1991 Embo J 10 12 3805-3817 7929265 Schmitz ML, dos Santos Silva MA, Altmann H, Czisch M, Holak TA, Baeuerle PA 1994 J Biol Chem 269 41 25613-25620 CD and NMR spectra revealed that TA1 exists in aqueous solution at physiological pH in a random coil conformation or is unstructured. The acidic activation domians of p65 TA1 are all capable of forming an alpha-helix in hydrophobic solvents. In an aqueous solution, negatively charged amino acids might prevent formation of a secondary structure due to electrostatic repulsion and/or steric hindrance imposed by hydrate shells. A transition of positively charged random coil sequence into an alpha-helical structure has been reported to occur when leucine zipper proteins contact DNA with their basic domains. Domains of the p65 molecule required for initiating transcription were subjected to deletion analysis. Removal of only 30 amino acids from the C-terminus of p65 reduced the transactivating potential of p65, whereas removal of 250 amino acids from the C-terminus completely negated the transactivating potential. A feature of TA1 appears to be the clustering of serine residues on one side of an alleged amphipathic helix, in which the serine residues may be involved in a zipper-like structure serving a role in protein-protein interaction as has been proposed for leucine repeats. Ser529 and Ser536 are important for inhibiting NF-kB activation, and phosphorylation of these residues is essential for NF-kB activation. Disordered - Extended Transactivation domain 2 (TA2) 441 518 LQLQFDDEDLGALLGNSTDPAVFTDLASVDNSEFQQLLNQGIPVAPHTTEPMLMEYPEAITRLVTGAQRPPDPAPAPL Function arises via a disorder to order transition Molecular assembly Transactivation (transcriptional activation) Protein-protein binding Nuclear magnetic resonance (NMR) 5.5 10% D₂O 90% H₂O NaCl 50 sodium phosphate 50 Paper 1935902 Schmitz ML, Baeuerle PA 1991 Embo J 10 12 3805-3817 7929265 Schmitz ML, dos Santos Silva MA, Altmann H, Czisch M, Holak TA, Baeuerle PA 1994 J Biol Chem 269 41 25613-25620 NMR spectra revealed that TA2 exists in aqueous solution at physiological pH in a random coil conformation or is unstructured. NMR analysis the C-terminal 123 amino acids showed a random coil conformation, which indicates that the entire transactivating C-terminus is unstructured. C-terminal deletion of the TA2 domain causes a gradual loss in transactivating activity. A region within TA2 homologous to TA1 is referred to as TA'1. TA'1 is necessary for the activity of TA2 because any deletion affecting the integrity of TA'1 leads to a decrease in the ability of TA2 to stimulate transcription. TA2 activity might also be dependent upon a leucine zipper, but this needs to be studied further. Disordered - Extended TA1 and TA2 plus mini leucine zipper (C-terminal region) 429 551 TQAGEGTLSEALLQLQFDDEDLGALLGNSTDPAVFTDLASVDNSEFQQLLNQGIPVAPHTTEPMLMEYPEAITRLVTGAQRPPDPAPAPLGAPGLPNGLLSGDEDFSSIADMDFSALLSQISS Fragment Function arises via a disorder to order transition Modification site Molecular assembly Transactivation (transcriptional activation) Protein-protein binding Nuclear magnetic resonance (NMR) 5.5 10% D₂O 90% H₂O NaCl 50 sodium phosphate 50 Paper 7929265 Schmitz ML, dos Santos Silva MA, Altmann H, Czisch M, Holak TA, Baeuerle PA 1994 J Biol Chem 269 41 25613-25620 NMR analysis of a protein corresponding to the C-terminal 123 amino acids showed a random coil conformation, which indicates that the entire transactivating C-terminus is unstructured. Cellular tumor antigen p53 P53_HUMAN Tumor suppressor p53 Oncoprotein p53 Phosphoprotein p53 p53 transformation suppressor Transformation-related protein 53 TRP53 Antigen NY-CO-13 P04637 Hs.654481 P53_HUMAN 269849759 Homo sapiens (Human) 393 MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD Disordered - Extended 1 73 MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPV Engineered Fragment Function arises from the disordered state Molecular recognition effectors Unknown Circular dichroism (CD) spectroscopy, near-UV 6.1 Phosphate Buffer TFE Paper 7559631 Chang J, Kim DH, Lee SW, Choi KY, Sung YC 1995 J Biol Chem 270 42 25014-9 This disordered region was discovered in an engineered fragment containing residues 1-73. Disordered - Extended 15 16 SQ Complex Engineered Fragment Function arises from the disordered state Unknown Unknown X-ray crystallography 308 MDM2 Paper 8875929 Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP 1996 Science 274 5289 948-53 This disordered region was discovered in an engineered fragment containing residues 15-29. Disordered - Extended 27 29 PEN Complex Engineered Fragment Function arises from the disordered state Unknown Unknown X-ray crystallography 308 MDM2 Paper 8875929 Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP 1996 Science 274 5289 948-53 The protein studied was an engineered fragment containing residues 15-29. Disordered - Extended 183 188 SDSDGL Engineered Fragment 1GZHA Relationship to function unknown Unknown Unknown X-ray crystallography PDB 12351827 Derbyshire DJ, Basu BP, Date T, Iwabuchi K, Doherty AJ 2002 Acta Crystallogr D Biol Crystallogr 58 Pt 10 Pt 2 1826-9 12110597 Derbyshire DJ, Basu BP, Serpell LC, Joo WS, Date T, Iwabuchi K, Doherty AJ 2002 EMBO J 21 14 3863-72 The disordered region characterized was studied in an engineered fragment containing residues 95-292. Disordered - Extended 200 200 N Engineered Fragment 1GZHA Relationship to function unknown Unknown Unknown X-ray crystallography PDB 12351827 Derbyshire DJ, Basu BP, Date T, Iwabuchi K, Doherty AJ 2002 Acta Crystallogr D Biol Crystallogr 58 Pt 10 Pt 2 1826-9 12110597 Derbyshire DJ, Basu BP, Serpell LC, Joo WS, Date T, Iwabuchi K, Doherty AJ 2002 EMBO J 21 14 3863-72 The disordered region characterized was studied in an engineered fragment containing residues 95-292. Disordered - Extended 224 227 EVGS Engineered Fragment 1GZHA Relationship to function unknown Unknown Unknown X-ray crystallography PDB 12351827 Derbyshire DJ, Basu BP, Date T, Iwabuchi K, Doherty AJ 2002 Acta Crystallogr D Biol Crystallogr 58 Pt 10 Pt 2 1826-9 12110597 Derbyshire DJ, Basu BP, Serpell LC, Joo WS, Date T, Iwabuchi K, Doherty AJ 2002 EMBO J 21 14 3863-72 The disordered region characterized was studied in an engineered fragment containing residues 95-292. Disordered - Extended 319 323 KKKPL Engineered Fragment 1OLGA 1OLHA 1SAEA 1SAEB 1SAEC 1SAED 1SAFA 1SAFB 1SAFC 1SAFD 1SAGA 1SAGB 1SAGC 1SAGD 1SAHA 1SAHB 1SAHC 1SAHD 1SAIA 1SAIB 1SAIC 1SAID 1SAKA 1SAKB 1SAKC 1SAKD 1SALA 1SALB 1SALC 1SALD 3SAKA 3SAKB 3SAKC 3SAKD Function arises from the disordered state Unknown Unknown Nuclear magnetic resonance (NMR) Paper Kuszewski J, Gronenborn AM, Clore GM 1999 J Am Chem Soc 121 10 2337-8 Disordered - Extended 357 360 KEPG Engineered Fragment 1OLGA 1OLHA 1SAEA 1SAEB 1SAEC 1SAED 1SAFA 1SAFB 1SAFC 1SAFD 1SAGA 1SAGB 1SAGC 1SAGD 1SAHA 1SAHB 1SAHC 1SAHD 1SAIA 1SAIB 1SAIC 1SAID 1SAKA 1SAKB 1SAKC 1SAKD 1SALA 1SALB 1SALC 1SALD 3SAKA 3SAKB 3SAKC 3SAKD Function arises from the disordered state Unknown Unknown Nuclear magnetic resonance (NMR) Paper Kuszewski J, Gronenborn AM, Clore GM 1999 J Am Chem Soc 121 10 2337-8 This disordered region was located in an engineered fragment containing residues 319-360. Disordered - Extended 291 312 KKGEPHHELPPGSTKRALPNNT Engineered Fragment Mutant 1UOLA Relationship to function unknown Unknown Unknown X-ray crystallography Paper 14534297 Joerger AC, Allen MD, Fersht AR 2004 J Biol Chem 279 2 1291-6 The disordered region characterized was from an engineered fragment containing residues 94-312 and mutations at M133L, V203A, N239Y, N268D. Tegument protein VP16 VP16_HHV2H Alpha trans-inducing protein Alpha-TIF Vmw65 ICP25 Transcriptional activator VP16 P68336 VP16_HHV2H 55584017 Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2) 490 MDLLVDDLFADADGVSPPPPRPAGGPKNTPAAPPLYATGRLSQAQLMPSPPMPVPPAALFNRLLDDLGFSAGPALCTMLDTWNEDLFSGFPTNADMYRECKFLSTLPSDVIDWGDAHVPERSPIDIRAHGDVAFPTLPATRDELPSYYEAMAQFFRGELRAREESYRTVLANFCSALYRYLRASVRQLHRQAHMRGRNRDLREMLRTTIADRYYRETARLARVLFLHLYLFLSREILWAAYAEQMMRPDLFDGLCCDLESWRQLACLFQPLMFINGSLTVRGVPVEARRLRELNHIREHLNLPLVRSAAAEEPGAPLTTPPVLQGNQARSSGYFMLLIRAKLDSYSSVATSEGESVMREHAYSRGRTRNNYGSTIEGLLDLPDDDDAPAEAGLVAPRMSFLSAGQRPRRLSTTAPITDVSLGDELRLDGEEVDMTPADALDDFDLEMLGDVESPSPGMTHDPVSYGALDVDDFEFEQMFTDAMGIDDFGG Disordered 350 394 TSEGESVMREHAYSRGRTRNNYGSTIEGLLDLPDDDDAPAEAGLV Native 16VPA Protein-DNA binding Protein-protein binding X-ray crystallography 289 4 polyethylene glycol 8000 w/v 20 potassium phosphate 50 Sensitivity to proteolysis Paper 10398682 Liu Y, Gong W, Huang CC, Herr W, Cheng X 1999 Genes Dev 13 13 1692-703 Disordered C terminal 403 490 AGQRPRRLSTTAPITDVSLGDELRLDGEEVDMTPADALDDFDLEMLGDVESPSPGMTHDPVSYGALDVDDFEFEQMFTDAMGIDDFGG Native 16VPA Protein-protein binding X-ray crystallography 289 4 polyethylene glycol 8000 w/v 20 potassium phosphate 50 Sensitivity to proteolysis Paper 10398682 Liu Y, Gong W, Huang CC, Herr W, Cheng X 1999 Genes Dev 13 13 1692-703 Ubiquinol oxidase subunit 1 CYOB_ECOLI Ubiquinol oxidase polypeptide I Cytochrome o subunit 1 Oxidase BO(3) subunit 1 Cytochrome o ubiquinol oxidase subunit 1 Ubiquinol oxidase chain A P0ABI8 CYOB_ECOLI 78099993 Escherichia coli (strain K12) 663 MFGKLSLDAVPFHEPIVMVTIAGIILGGLALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQALASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDPQFHTMLMIAASGAVLIALGILCLVIQMYVSIRDRDQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHVHERDAFWEMKEKGEAYKKPDHYEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVPVAEIEKLENQHFDEITKAGLKNGN Disordered 553 663 AVVPHVHERDAFWEMKEKGEAYKKPDHYEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVPVAEIEKLENQHFDEITKAGLKNGN Engineered 1FFTA 1FFTF Relationship to function unknown Unknown Unknown X-ray crystallography PEG 1500 approximately (w/v) 9 NaCl 100 MgCl2 100 ethanol (v/v) 5 Paper 11017202 Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikstrom M 2000 Nat Struct Biol 7 10 910-7 2162835 Chepuri V, Lemieux L, Au DC, Gennis RB 1990 J Biol Chem 265 19 11185-92 Disordered 1 51 MFGKLSLDAVPFHEPIVMVTIAGIILGGLALVGLITYFGKWTYLWKEWLTS Engineered 1FFTA 1FFTF Relationship to function unknown Unknown Unknown X-ray crystallography ethanol (v/v) 5 MgCl2 100 NaCl 100 PEG 1500 approximately (w/v) 9 Paper 11017202 Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikstrom M 2000 Nat Struct Biol 7 10 910-7 2162835 Chepuri V, Lemieux L, Au DC, Gennis RB 1990 J Biol Chem 265 19 11185-92 Disordered 521 540 RDRDQNRDLTGDPWGGRTLE Engineered Relationship to function unknown Unknown Unknown X-ray crystallography ethanol (v/v) 5 MgCl2 100 NaCl 100 PEG 1500 approximately (w/v) 9 Paper 11017202 Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikstrom M 2000 Nat Struct Biol 7 10 910-7 2162835 Chepuri V, Lemieux L, Au DC, Gennis RB 1990 J Biol Chem 265 19 11185-92 Disordered 82 95 QQALASAGEAGFLP Engineered Relationship to function unknown Unknown Unknown X-ray crystallography ethanol (v/v) 5 MgCl2 100 NaCl 100 PEG 1500 approximately (w/v) 9 Paper 11017202 Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikstrom M 2000 Nat Struct Biol 7 10 910-7 2162835 Chepuri V, Lemieux L, Au DC, Gennis RB 1990 J Biol Chem 265 19 11185-92 Disordered 180 185 EYSPGV Engineered Relationship to function unknown Unknown Unknown X-ray crystallography ethanol (v/v) 5 MgCl2 100 NaCl 100 PEG 1500 approximately (w/v) 9 Paper 11017202 Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikstrom M 2000 Nat Struct Biol 7 10 910-7 2162835 Chepuri V, Lemieux L, Au DC, Gennis RB 1990 J Biol Chem 265 19 11185-92 Ubiquinol oxidase subunit 2 CYOA_ECOLI Ubiquinol oxidase polypeptide II Cytochrome o subunit 2 Oxidase BO(3) subunit 2 Cytochrome o ubiquinol oxidase subunit 2 Ubiquinol oxidase chain B P0ABJ1 CYOA_ECOLI 78099990 Escherichia coli (strain K12) 315 MRLRKYNKSLGWLSLFAGTVLLSGCNSALLDPKGQIGLEQRSLILTAFGLMLIVVIPAILMAVGFAWKYRASNKDAKYSPNWSHSNKVEAVVWTVPILIIIFLAVLTWKTTHALEPSKPLAHDEKPITIEVVSMDWKWFFIYPEQGIATVNEIAFPANTPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKAIATPDRAAFDQWVAKAKQSPNTMSDMAAFEKLAAPSEYNQVEYFSNVKPDLFADVINKFMAHGKSMDMTQPEGEHSAHEGMEGMDMSHAESAH Disordered 283 315 AHGKSMDMTQPEGEHSAHEGMEGMDMSHAESAH Fragment 1FFTB 1FFTG Relationship to function unknown Unknown Unknown X-ray crystallography 277 ammonium sulfphate precipitant 35 citrate/bis-Tris-propane (pH 9.0-9.5) 100 dimethylsuphoxide (to obtain sharp edges) v/v 2 DTT buffer 1 EDTA buffer 1 NaN3 buffer 1 Paper 1324168 van der Oost J, Lappalainen P, Musacchio A, Warne A, Lemieux L, Rumbley J, Gennis RB, Aasa R, Pascher T, Malmstrom BG, et al 1992 Embo J 11 9 3209-17 8433374 van der Oost J, Musacchio A, Pauptit RA, Ceska TA, Wierenga RK, Saraste M 1993 J Mol Biol 229 3 794-6 8618822 Wilmanns M, Lappalainen P, Kelly M, Sauer-Eriksson E, Saraste M 1995 Proc Natl Acad Sci U S A 92 26 11955-9 This region is located in the periplasmic space. Disordered 1 14 MRLRKYNKSLGWLS Fragment 1FFTB 1FFTG Relationship to function unknown Unknown Unknown X-ray crystallography 277 ammonium sulfate precipitant 35 citrate/bis-Tris-propane (pH 9.0-9.5) 100 dimethylsulphoxide (to obtain sharp edges) v/v 2 DTT buffer 1 EDTA buffer 1 NaN3 buffer 1 Paper 1324168 van der Oost J, Lappalainen P, Musacchio A, Warne A, Lemieux L, Rumbley J, Gennis RB, Aasa R, Pascher T, Malmstrom BG, et al 1992 Embo J 11 9 3209-17 8433374 van der Oost J, Musacchio A, Pauptit RA, Ceska TA, Wierenga RK, Saraste M 1993 J Mol Biol 229 3 794-6 8618822 Wilmanns M, Lappalainen P, Kelly M, Sauer-Eriksson E, Saraste M 1995 Proc Natl Acad Sci U S A 92 26 11955-9 This region is located in the periplasmic space. Disordered 284 315 HGKSMDMTQPEGEHSAHEGMEGMDMSHAESAH Engineered 1FFTB 1FFTG Relationship to function unknown Unknown Unknown X-ray crystallography PEG 1500 approximate (w/v) 9 sodium chloride 100 magnesium chloride 100 ethanol (v/v) 5 Paper 11017202 Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikstrom M 2000 Nat Struct Biol 7 10 910-7 This region is located in the periplasmic space. Disordered 1 26 MRLRKYNKSLGWLSLFAGTVLLSGCN Engineered 1FFTB 1FFTG Relationship to function unknown Unknown Unknown X-ray crystallography PEG 1500 approximate (w/v) 9 sodium chloride 100 magnesium chloride 100 ethanol (v/v) 5 Paper 11017202 Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikstrom M 2000 Nat Struct Biol 7 10 910-7 This region is located in the periplasmic space. Abramson et al. could not assign a sequence for residues 1-36 or 113-124. However the PDB file locates electron density for residues 27-283. A periplasmic fragment of subunit II is located under the PDB identification of 1CYW. It is residues 125-283 of subunit II as described by Abramson et. al. Voltage-gated potassium channel subunit beta-1 [Isoform KvB1.1] KCAB1_HUMAN K(+) channel subunit beta-1 Kv-beta-1 Potassium channel shaker chain beta 1a Potassium voltage-gated channel, shaker-related subfamily, beta member 1, isoform 3 Q14722-2 Hs.654519 KCAB1_HUMAN 18202500 Homo sapiens (Human) 401 MQVSIACTEHNLKSRNGEDRLLSKQSSTAPNVVNAARAKFRTVAIIARSLGTFTPQHHISLKESTAKQTGMKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNKPYSKKDYRS Disordered N-terminal domain 1 62 MQVSIACTEHNLKSRNGEDRLLSKQSSTAPNVVNAARAKFRTVAIIARSLGTFTPQHHISLK Fragment Native Function arises from the disordered state Entropic chain Flexible linkers/spacers Nuclear magnetic resonance (NMR) 283 Bruker DRX 600 spectrometer Bruker DMX 800 spectrometer D2O 99.9 Paper 10585425 Wissmann R, Baukrowitz T, Kalbacher H, Kalbitzer HR, Ruppersberg JP, Pongs O, Antz C, Fakler B 1999 J Biol Chem 274 50 35521-5 Additional UniGene ID: Hs.703187 DNA repair protein complementing XP-A cells homolog XPA_XENLA Xeroderma pigmentosum group A-complementing protein homolog DNA repair protein XPAC P27088 Xl.902 XPA_XENLA 139817 Xenopus laevis (African clawed frog) 267 MEPEPEPEQEANKEEEKILSAAVRAKIERNRQRALMLRQARLACRPYPTGEGISTVKAPPKVIDSGGGFFIEEEEAEEQHVENVVRQPGPVLECDYLICEECGKDFMDSYLSNHFDLAVCDSCRDAEEKHKLITRTEAKQEYLLKDCDIDKREPVLKFILKKNPHNTHWGDMKLYLKAQVIKRSLEVWGSEEALEEAKEVRKDNRDKMKQKKFDKKVKELRRTVRSSLWKKEASGHQHEYGPEEHVEEDSYKKTCITCGYEMNYEKM Disordered - Extended 1 84 MEPEPEPEQEANKEEEKILSAAVRAKIERNRQRALMLRQARLACRPYPTGEGISTVKAPPKVIDSGGGFFIEEEEAEEQHVENV Engineered Function arises from the disordered state Molecular assembly Protein-protein binding Sensitivity to proteolysis 310 7.5 Hepes-KOH 25 KCl 100 trypsin Second Concentration 0.05 trypsin First Concentration 0.5 ESI-FTICR mass spectrometry 433 Paper 11344324 Iakoucheva LM, Kimzey AL, Masselon CD, Bruce JE, Garner EC, Brown CJ, Dunker AK, Smith RD, Ackerman EJ 2001 Protein Sci 10 3 560-71 The results from the laboratory experiments were compared to PONDR predictions and found to be identical. Disordered - Extended 181 265 IKRSLEVWGSEEALEEAKEVRKDNRDKMKQKKFDKKVKELRRTVRSSLWKKEASGHQHEYGPEEHVEEDSYKKTCITCGYEMNYE Engineered Function arises from the disordered state Molecular assembly Protein-protein binding Sensitivity to proteolysis 310 7.5 Hepes-KOH 25 KCl 100 trypsin First Concentration 0.5 trypsin Second Concentration 0.05 ESI-FTICR mass spectrometry 433 Paper 11344324 Iakoucheva LM, Kimzey AL, Masselon CD, Bruce JE, Garner EC, Brown CJ, Dunker AK, Smith RD, Ackerman EJ 2001 Protein Sci 10 3 560-71 The results from the laboratory experiments were compared to PONDR predictions and found to be identical. Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform PP2BA_HUMAN Calmodulin-dependent calcineurin A subunit alpha isoform CAM-PRP catalytic subunit Calcineurin A alpha CaNA Protein phosphatase 3, catalytic subunit, alpha isoform PPP3CA Protein phosphatase 2B PP2B Q08209 Hs.435512 PP2BA_HUMAN 1352673 Homo sapiens (Human) 521 MSEPKAIDPKLSTTDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKEGRLEESVALRIITEGASILRQEKNLLDIDAPVTVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHGGLSPEINTLDDIRKLDRFKEPPAYGPMCDILWSDPLEDFGNEKTQEHFTHNTVRGCSYFYSYPAVCEFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLNICSDDELGSEEDGFDGATAAARKEVIRNKIRAIGKMARVFSVLREESESVLTLKGLTPTGMLPSGVLSGGKQTLQSATVEAIEADEAIKGFSPQHKITSFEEAKGLDRINERMPPRRDAMPSDANLNSINKALTSETNGTDSNGSNSSNIQ Disordered - Extended 1 13 MSEPKAIDPKLST 1AUIA Relationship to function unknown Unknown Unknown X-ray crystallography CaCl2 polyethylene glycol (PEG) 6000 Paper 8524402 Kissinger CR, Parge HE, Knighton DR, Lewis CT, Pelletier LA, Tempczyk A, Kalish VJ, Tucker KD, Showalter RE, Moomaw EW, et al 1995 Nature 378 6557 641-4 Mass spectrometry combined with enzymatic digestion showed that the N-terminal residues were sensitive to proteolysis. (PMID 12357034) Disordered - Extended CaM-binding domain 390 414 AARKEVIRNKIRAIGKMARVFSVLR 1AUIA Function arises via a disorder to order transition Molecular assembly Protein-protein binding Autoregulatory X-ray crystallography CaCl2 polyethylene glycol (PEG) 6000 Paper 8524402 Kissinger CR, Parge HE, Knighton DR, Lewis CT, Pelletier LA, Tempczyk A, Kalish VJ, Tucker KD, Showalter RE, Moomaw EW, et al 1995 Nature 378 6557 641-4 Disordered - Extended 374 468 DDELGSEEDGFDGATAAARKEVIRNKIRAIGKMARVFSVLREESESVLTLKGLTPTGMLPSGVLSGGKQTLQSATVEAIEADEAIKGFSPQHKIT 1AUIA Function arises via a disorder to order transition Molecular assembly Autoregulatory Protein-protein binding X-ray crystallography CaCl2 polyethylene glycol (PEG) 6000 Paper 8524402 Kissinger CR, Parge HE, Knighton DR, Lewis CT, Pelletier LA, Tempczyk A, Kalish VJ, Tucker KD, Showalter RE, Moomaw EW, et al 1995 Nature 378 6557 641-4 The disordered region from 374-468 includes the CaM-binding domain predicted to lie between residues 390-414. As in the crystal structure of native CaN, the C-terminal portion of CaNA is disordered beyond the CaNB-binding helix (343-373), and electron density for the CaM-binding domain of CaNA is not visible. Mass spectrometry combined with enzymatic digestion showed that the calmodulin-binding region was removed by trypsin, indicating that this disordered region is sensitive to proteolysis. Calmodulin binds to this disordered region between the CnB-binding site and the autoinhibitory helix, and this segment takes on an alpha-helical conformation to pull the AI helix away from the catalytic site in order to activate the phosphatase activity. Calmodulin is a protein that wraps around a target helix in calcineurin upon binding. The ~20-residue target helix is located within a 95-residue disordered region that is not observed in crystal structures. The disorder allows the target helix to separate from the rest of the protein, thus permitting access for binding. For the calmodulin/target helix interaction, it is unknown whether the other ~75 disordered residues become ordered upon binding, but it is thought that this region takes on an alpha-helical conformation when calmodulin binds. The function of the disordered region is to make the helix accessible for calmodulin binding, and this region of disorder is essential to the regulation of calcineurin by calcium/calmodulin. Binding of calcium/calcineurin activates calcineurin's serine/threonine phosphatase activity. Disordered - Extended Autoinhibitory region 469 486 SFEEAKGLDRINERMPPR 1AUIA Function arises via an order to disorder transition Function arises via a disorder to order transition Molecular assembly Protein-protein binding Autoregulatory X-ray crystallography CaCl2 polyethylene glycol (PEG) 6000 Paper 8524402 Kissinger CR, Parge HE, Knighton DR, Lewis CT, Pelletier LA, Tempczyk A, Kalish VJ, Tucker KD, Showalter RE, Moomaw EW, et al 1995 Nature 378 6557 641-4 As in the crystal structure of native CaN, the C-terminal portion of CaNA is disordered beyond the CaNB-binding helix (343-373), which indicates that the autoinhibitory domain is disordered. However, this disordered region is present for PDB 1AUI. Unlike the native CaN crystal structure, the AI segment of CaN is not seen in the crystal structure of the FKBP12-FK506-CaN complex. This might indicate that the autoinhibitory complex is ordered when CaNA is in a complex with CaNB, but other evidence suggests that when the AI domain is either not in contact with the catalytic domain (as is the case with immunosuppressants) or when CaNA exists as a monomer, the AI domain may not be structured. Calmodulin binds to the disordered region between the CnB-binding site and the autoinhibitory helix, and this segment takes on an alpha-helical conformation to pull the AI helix away from the catalytic site in order to activate the phosphatase activity according to Jin and Harrison. When this occurs, the structure of the AI helix may change as well, leading to disorder. Further evidence needs to be found in order to indicate the state of the AI domain. For now, the AI domain will be considered disordered based on the statement made by Kissinger above and the information provided by Jin and Harrison in regards to proteolytic sensitivity. The autoinhibitory domain lies over the substrate-binding cleft in the catalytic domain and consists of two short alpha-helical regions plus five residues in an extended conformation. The helical regions restrict interaction with the substrate-binding cleft when the AI segment contacts the cleft. Mass spectrometry combined with enzymatic digestion showed that the autoinhibitory helix was removed by trypsin, indicating that this disordered region is sensitive to proteolysis. Disordered - Extended 487 521 RDAMPSDANLNSINKALTSETNGTDSNGSNSSNIQ 1AUIA Relationship to function unknown Unknown Unknown X-ray crystallography CaCl2 polyethylene glycol (PEG) 6000 Paper 8524402 Kissinger CR, Parge HE, Knighton DR, Lewis CT, Pelletier LA, Tempczyk A, Kalish VJ, Tucker KD, Showalter RE, Moomaw EW, et al 1995 Nature 378 6557 641-4 CaNA residues 487-521 are not visible in the electron density map of the crystal structure and are disordered. Ordered 14 373 TDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKEGRLEESVALRIITEGASILRQEKNLLDIDAPVTVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHGGLSPEINTLDDIRKLDRFKEPPAYGPMCDILWSDPLEDFGNEKTQEHFTHNTVRGCSYFYSYPAVCEFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLNICS 1AUIA X-ray crystallography CaCl2 polyethylene glycol (PEG) 6000 Paper 8524402 Kissinger CR, Parge HE, Knighton DR, Lewis CT, Pelletier LA, Tempczyk A, Kalish VJ, Tucker KD, Showalter RE, Moomaw EW, et al 1995 Nature 378 6557 641-4 Catalytic subunit of calcineurin. Interacts with DP00565, Calcineurin subunit B type 1. Tyrosine 3-monooxygenase TY3H_RAT Tyrosine 3-hydroxylase TH EC=1.14.16.2 P04177 Rn.11082 TY3H_RAT 136577 Rattus norvegicus (Rat) 498 MPTPSAPSPQPKGFRRAVSEQDAKQAEAVTSPRFIGRRQSLIEDARKEREAAAAAAAAAVASSEPGNPLEAVVFEERDGNAVLNLLFSLRGTKPSSLSRAVKVFETFEAKIHHLETRPAQRPLAGSPHLEYFVRFEVPSGDLAALLSSVRRVSDDVRSAREDKVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQYKHGEPIPHVEYTAEEIATWKEVYVTLKGLYATHACREHLEGFQLLERYCGYREDSIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTVYWFTVEFGLCKQNGELKAYGAGLLSSYGELLHSLSEEPEVRAFDPDTAAVQPYQDQTYQPVYFVSESFNDAKDKLRNYASRIQRPFSVKFDPYTLAIDVLDSPHTIQRSLEGVQDELHTLAHALSAIS Disordered N-terminal domain 1 155 MPTPSAPSPQPKGFRRAVSEQDAKQAEAVTSPRFIGRRQSLIEDARKEREAAAAAAAAAVASSEPGNPLEAVVFEERDGNAVLNLLFSLRGTKPSSLSRAVKVFETFEAKIHHLETRPAQRPLAGSPHLEYFVRFEVPSGDLAALLSSVRRVSDD Mutant Native Substrate/ligand binding Circular dichroism (CD) spectroscopy, far-UV 7 JASCO J-600 spectrophotometer Circular dichroism (CD) spectroscopy, near-UV 7 JASCO -600 spectrophotometer Size exclusion/gel filtration chromatography 277 7.5 flow rate 0.5 NaCl 150 sodium phosphate 50 Superose 12 HR 10/30 column Paper 8104613 Daubner SC, Lohse DL, Fitzpatrick PF 1993 Protein Sci 2 9 1452-60 Tyrosyl-tRNA synthetase SYY_BACST Tyrosine-tRNA ligase TyrRS Tyrosine-transfer ribonucleate synthetase Tyrosine translase EC=6.1.1.1 P00952 SYY_BACST 135197 Bacillus stearothermophilus (Geobacillus stearothermophilus) 419 MDLLAELQWRGLVNQTTDEDGLRKLLNEERVTLYCGFDPTADSLHIGHLATILTMRRFQQAGHRPIALVGGATGLIGDPSGKKSERTLNAKETVEAWSARIKEQLGRFLDFEADGNPAKIKNNYDWIGPLDVITFLRDVGKHFSVNYMMAKESVQSRIETGISFTEFSYMMLQAYDFLRLYETEGCRLQIGGSDQWGNITAGLELIRKTKGEARAFGLTIPLVTKADGTKFGKTESGTIWLDKEKTSPYEFYQFWINTDDRDVIRYLKYFTFLSKEEIEALEQELREAPEKRAAQKTLAEEVTKLVHGEEALRQAIRISEALFSGDIANLTAAEIEQGFKDVPSFVHEGGDVPLVELLVSAGISPSKRQAREDIQNGAIYVNGERLQDVGAILTAEHRLEGRFTVIRRGKKKYYLIRYA Disordered C-terminal domain 320 419 EALFSGDIANLTAAEIEQGFKDVPSFVHEGGDVPLVELLVSAGISPSKRQAREDIQNGAIYVNGERLQDVGAILTAEHRLEGRFTVIRRGKKKYYLIRYA 2TS1A Function arises via a disorder to order transition Protein-tRNA binding Substrate/ligand binding X-ray crystallography 2.3 A Nuclear magnetic resonance (NMR) time scale 1e+08 Paper 2504923 Brick P, Bhat TN, Blow DM 1989 J Mol Biol 208 1 83-98 12005430 Guijarro JI, Pintar A, Prochnicka-Chalufour A, Guez V, Gilquin B, Bedouelle H, Delepierre M 2002 Structure (Camb) 10 3 311-7 Lipoate-protein ligase A subunit 1 Lipoate-protein ligase subunit 1 LPL EC=2.7.7.63 Q9HKT1 LPLA_THEAC 13878582 Thermoplasma acidophilum 262 MEGRLLLLETPGNTRMSLAYDEAIYRSFQYGDKPILRFYRHDRSVIIGYFQVAEEEVDLDYMKKNGIMLARRYTGGGAVYHDLGDLNFSVVRSSDDMDITSMFRTMNEAVVNSLRILGLDARPGELNDVSIPVNKKTDIMAGEKKIMGAAGAMRKGAKLWHAAMLVHTDLDMLSAVLKVPDEKFRDKIAKSTRERVANVTDFVDVSIDEVRNALIRGFSETLHIDFREDTITEKEESLARELFDKKYSTEEWNMGLLRKEVV Disordered 179 193 VPDEKFRDKIAKSTR Fragment 2ARUA 2C8MA 2C8MB 2C8MC 2C8MD Molecular assembly Substrate/ligand binding X-ray crystallography PEG 8000 20 sodium cacodylate buffer pH 6.5 0.1 magnesium acetate 0.2 Sensitivity to proteolysis 273 7.5 DTT 1 NaCl 150 trypsin w/w 4 Paper 16384580 McManus E, Luisi BF, Perham RN 2006 J Mol Biol 356 3 625-37 Histone H1.0 H10_MOUSE Histone H1(0) Histone H1' MyD196 H1 histone family, member 0 P10922 Mm.24350 H10_MOUSE 1346247 Mus musculus (Mouse) 193 TENSTSAPAAKPKRAKASKKSTDHPKYSDMIVAAIQAEKNRAGSSRQSIQKYIKSHYKVGENADSQIKLSIKRLVTTGVLKQTKGVGASGSFRLAKGDEPKRSVAFKKTKKEVKKVATPKKAAKPKKAASKAPSKKPKATPVKKAKKKPAATPKKAKKPKVVKVKPVKASKPKKAKTVKPKAKSSAKRASKKK Disordered 99 121 EPKRSVAFKKTKKEVKKVATPKK Fragment Function arises via a disorder to order transition Protein-DNA binding Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) 295 HEPES pD 7.0 10 NaCl 10 mM or 70 mM peptide 4.6 Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) 295 HEPES pD 7.0 10 Murine DNA 6.7 NaCl 10 mM or 70 mM Circular dichroism (CD) spectroscopy, far-UV 278 3.5 Phosphate buffer 5 Water Circular dichroism (CD) spectroscopy, far-UV 278 3.5 Phosphate buffer 5 TFE 50% Water 50% Circular dichroism (CD) spectroscopy, far-UV 278 3.5 H2O 10% Phosphate buffer 5 TFE 90% Nuclear magnetic resonance (NMR) 298 3.5 TFE 50% Nuclear magnetic resonance (NMR) 298 3.5 TFE 90% Paper 10794405 Vila R, Ponte I, Jimenez MA, Rico M, Suau P 2000 Protein Sci 9 4 627-36 11413144 Vila R, Ponte I, Collado M, Arrondo JL, Suau P 2001 J Biol Chem 276 33 30898-903 The fragment used consisted of residues 99-121. Disordered 96 193 KGDEPKRSVAFKKTKKEVKKVATPKKAAKPKKAASKAPSKKPKATPVKKAKKKPAATPKKAKKPKVVKVKPVKASKPKKAKTVKPKAKSSAKRASKKK Fragment Function arises via a disorder to order transition Protein-DNA binding Circular dichroism (CD) spectroscopy, far-UV 293 Phosphate buffer pH 7.0 10 Circular dichroism (CD) spectroscopy, far-UV 293 Phosphate buffer pH 7.0 10 TFE 60% (v/v) Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) 295 HEPES 10 NaCl 10 mM or 140 mM peptide 5 Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) 295 HEPES 10 Murine DNA 7 NaCl 10 mM or 140 mM peptide 5 Paper 16006555 Roque A, Iloro I, Ponte I, Arrondo JL, Suau P 2005 J Biol Chem 280 37 32141-7 The fragment used consisted of residues 96-193. Disordered 8 30 PAAKPKRAKASKKSTDHPKYSDM Fragment Function arises via a disorder to order transition Protein-DNA binding Circular dichroism (CD) spectroscopy, far-UV 293 3.5 H2O NaCl 10 Sodium phosphate buffer 5 Circular dichroism (CD) spectroscopy, far-UV 293 3.5 H2O 10% NaCl 10 Sodium phosphate buffer 5 TFE 90% Nuclear magnetic resonance (NMR) 298 3.5 deuterated TFE 90% H2O 10% NaCl 10 peptide 2.7 Phosphate buffer 5 Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) D2O HEPES pH 7.0 10 NaCl 10 mM or 70 mM peptide 4.6 Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) HEPES pH 7.0 10 Murine DNA 6.7 NaCl 10 mM or 70 mM TFE Paper 11584004 Vila R, Ponte I, Collado M, Arrondo JL, Jimenez MA, Rico M, Suau P 2001 J Biol Chem 276 49 46429-35 The fragment used consisted of residues 8-30. Disordered 1 20 TENSTSAPAAKPKRAKASKK Fragment Function arises via a disorder to order transition Protein-DNA binding Circular dichroism (CD) spectroscopy, far-UV 293 3.5 Water NaCl 10 Sodium phosphate buffer 5 Circular dichroism (CD) spectroscopy, far-UV 293 3.5 Water 10% NaCl 10 Sodium phosphate buffer 5 TFE 90% Nuclear magnetic resonance (NMR) 298 3.5 Deuterated TFE 90% H2O 10% NaCl 10 Peptide 2.7 Phosphate buffer 5 Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) D2O HEPES pH 7.0 10 NaCl 10 mM or 70 mM peptide 4.6 Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) HEPES pH 7.0 10 Murine DNA 6.7 NaCl 10 mM or 70 mM TFE Paper 11584004 Vila R, Ponte I, Collado M, Arrondo JL, Jimenez MA, Rico M, Suau P 2001 J Biol Chem 276 49 46429-35 The fragment used consisted of residues 1-20. Collagen adhesin CNA_STAAU Q53654 CNA_STAAU 3913259 Staphylococcus aureus 1183 MNKNVLKFMVFIMLLNIITPLFNKNEAFAARDISSTNVTDLTVSPSKIEDGGKTTVKMTFDDKNGKIQNGDMIKVAWPTSGTVKIEGYSKTVPLTVKGEQVGQAVITPDGATITFNDKVEKLSDVSGFAEFEVQGRNLTQTNTSDDKVATITSGNKSTNVTVHKSEAGTSSVFYYKTGDMLPEDTTHVRWFLNINNEKSYVSKDITIKDQIQGGQQLDLSTLNINVTGTHSNYYSGQSAITDFEKAFPGSKITVDNTKNTIDVTIPQGYGSYNSFSINYKTKITNEQQKEFVNNSQAWYQEHGKEEVNGKSFNHTVHNINANAGIEGTVKGELKVLKQDKDTKAPIANVKFKLSKKDGSVVKDNQKEIEIITDANGIANIKALPSGDYILKEIEAPRPYTFDKDKEYPFTMKDTDNQGYFTTIENAKAIEKTKDVSAQKVWEGTQKVKPTIYFKLYKQDDNQNTTPVDKAEIKKLEDGTTKVTWSNLPENDKNGKAIKYLVKEVNAQGEDTTPEGYTKKENGLVVTNTEKPIETTSISGEKVWDDKDNQDGKRPEKVSVNLLANGEKVKTLDVTSETNWKYEFKDLPKYDEGKKIEYTVTEDHVKDYTTDINGTTITNKYTPGETSATVTKNWDDNNNQDGKRPTEIKVELYQDGKATGKTAILNESNNWTHTWTGLDEKAKGQQVKYTVEELTKVKGYTTHVDNNDMGNLIVTNKYTPETTSISGEKVWDDKDNQDGKRPEKVSVNLLADGEKVKTLDVTSETNWKYEFKDLPKYDEGKKIEYTVTEDHVKDYTTDINGTTITNKYTPGETSATVTKNWDDNNNQDGKRPTEIKVELYQDGKATGKTAILNESNNWTHTWTGLDEKAKGQQVKYTVEELTKVKGYTTHVDNNDMGNLIVTNKYTPETTSISGEKVWDDKDNQDGKRPEKVSVNLLANGEKVKTLDVTSETNWKYEFKDLPKYDEGKKIEYTVTEDHVKDYTTDINGTTITNKYTPGETSATVTKNWDDNNNQDGKRPTEIKVELYQDGKATGKTAILNESNNWTHTWTGLDEKAKGQQVKYTVDELTKVNGYTTHVDNNDMGNLIVTNKYTPKKPNKPIYPEKPKDKTPPTKPDHSNKVKPTPPDKPSKVDKDDQPKDNKTKPENPLKELPKTGMKIITSWITWVFIGILGLYLILRKRFNS Disordered 151 168 ITSGNKSTNVTVHKSEAG Fragment 1AMXA Relationship to function unknown Unknown Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV 298 Circular dichroism (CD) spectroscopy, near-UV 298 Paper 9334749 Symersky J, Patti JM, Carson M, House-Pompeo K, Teale M, Moore D, Jin L, Schneider A, DeLucas LJ, Hook M, Narayana SV 1997 Nat Struct Biol 4 10 833-8 8218209 Patti JM, Boles JO, Hook M 1993 Biochemistry 32 42 11428-35 As the Patti article does not contain evidence for disorder and the Symersky article is not publicly available, this record cannot be verified. Glycine amidinotransferase, mitochondrial GATM_HUMAN EC 2.1.4.1 L-arginine:glycine amidinotransferase Transamidinase Arginine-glycine transamidinase P50440 Hs.75335 GATM_HUMAN 1730201 Homo sapiens (Human) 423 MLRVRCLRGGSRGAEAVHYIGSRLGRTLTGWVQRTFQSTQAATASSRNSCAADDKATEPLPKDCPVSSYNEWDPLEEVIVGRAENACVPPFTIEVKANTYEKYWPFYQKQGGHYFPKDHLKKAVAEIEEMCNILKTEGVTVRRPDPIDWSLKYKTPDFESTGLYSAMPRDILIVVGNEIIEAPMAWRSRFFEYRAYRSIIKDYFHRGAKWTTAPKPTMADELYNQDYPIHSVEDRHKLAAQGKFVTTEFEPCFDAADFIRAGRDIFAQRSQVTNYLGIEWMRRHLAPDYRVHIISFKDPNPMHIDATFNIIGPGIVLSNPDRPCHQIDLFKKAGWTIITPPTPIIPDDHPLWMSSKWLSMNVLMLDEKRVMVDANEVPIQKMFEKLGITTIKVNIRNANSLGGGFHCWTCDVRRRGTLQSYLD Disordered - Extended 38 63 STQAATASSRNSCAADDKATEPLPKD Engineered 1JDWA 2JDXA Relationship to function unknown Unknown Unknown X-ray crystallography 295 7 protein solution approximately 2 PEG 6000 buffer 3 HEPES buffer 40 Beta-ME buffer 2 Paper 9218780 Humm A, Fritsche E, Steinbacher S, Huber R. 1997 EMBO J 16 12 3373-85 9165070 Humm A, Fritsche E, Steinbacher S 1997 Biol Chem 378 3-4 193-7 ATP-dependent hsl protease ATP-binding subunit hslU HSLU_ECOLI Heat shock protein hslU P0A6H5 HSLU_ECOLI 62288339 Escherichia coli 443 MSEMTPREIVSELDKHIIGQDNAKRSVAIALRNRWRRMQLNEELRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVGYVGKEVDSIIRDLTDAAVKMVRVQAIEKNRYRAEELAEERILDVLIPPAKNNWGQTEQQQEPSAARQAFRKKLREGQLDDKEIEIDLAAAPMGVEIMAPPGMEEMTSQLQSMFQNLGGQKQKARKLKIKDAMKLLIEEEAAKLVNPEELKQDAIDAVEQHGIVFIDEIDKICKRGESSGPDVSREGVQRDLLPLVEGCTVSTKHGMVKTDHILFIASGAFQIAKPSDLIPELQGRLPIRVELQALTTSDFERILTEPNASITVQYKALMATEGVNIEFTDSGIKRIAEAAWQVNESTENIGARRLHTVLERLMEEISYDASDLSGQNITIDADYVSKHLDALVADEDLSRFIL Disordered I domain 175 209 IDLAAAPMGVEIMAPPGMEEMTSQLQSMFQNLGGQ Complex Native 1DO0A 1DO0B 1DO0C 1DO0D 1DO0E 1DO0F 1DO2A 1DO2B 1DO2C 1DO2D Function arises via an order to disorder transition Chaperones Protein-protein binding X-ray crystallography Paper 10693812 Bochtler M, Hartmann C, Song HK, Bourenkov GP, Bartunik HD, Huber R 2000 Nature 403 6771 800-5 Gag polyprotein GAG_HV1N5 Pr55Gag Matrix protein p17 [cleavage product 1] MA Capsid protein p24 [cleavage product 2] CA Spacer peptide p2 [cleavage product 3] Nucleocapsid protein p7 [cleavage product 4] NC Spacer peptide p1 [cleavage product 5] p6-gag [cleavage product 6] P12493 GAG_HV1N5 120839 Human immunodeficiency virus type 1 (isolate NY5 group M subtype B)(HIV-1) 500 MGARASVLSGGELDKWEKIRLRPGGKKQYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTIAVLYCVHQRIDVKDTKEALDKIEEEQNKSKKKAQQAAADTGNNSQVSQNYPIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTHNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPGATLEEMMTACQGVGGPGHKARVLAEAMSQVTNPATIMIQKGNFRNQRKTVKCFNCGKEGHIAKNCRAPRKKGCWKCGKEGHQMKDCTERQANFLGKIWPSHKGRPGNFLQSRPEPTAPPEESFRFGEETTTPSQKQEPIDKELYPLASLRSLFGSDPSSQ Previous entry DP00101 has been split into polyprotein (DP00101) and cleavage product (DP00101_C006). p6-gag GAG_HV1N5 cleavage product 6 of Gag polyprotein P12493 GAG_HV1N5 120839 Human immunodeficiency virus type 1 (isolate NY5 group M subtype B)(HIV-1) 52 LQSRPEPTAPPEESFRFGEETTTPSQKQEPIDKELYPLASLRSLFGSDPSSQ Disordered 1 13 LQSRPEPTAPPEE Engineered Circular dichroism (CD) spectroscopy, far-UV 7.2 Phosphate buffer protein 0.2 Nuclear magnetic resonance (NMR) 308 3 H2O super distilled TFE-d2 Paper 16234236 Fossen T, Wray V, Bruns K, Rachmat J, Henklein P, Tessmer U, Maczurek A, Klinger P, Schubert U 2005 J Biol Chem Disordered flexible hinge region 19 32 EETTTPSQKQEPID Engineered Circular dichroism (CD) spectroscopy, far-UV 7.2 Phosphate buffer protein 0.2 Nuclear magnetic resonance (NMR) 308 3 H2O super distilled TFE-d2 Paper 16234236 Fossen T, Wray V, Bruns K, Rachmat J, Henklein P, Tessmer U, Maczurek A, Klinger P, Schubert U 2005 J Biol Chem Disordered 44 52 LFGSDPSSQ Engineered Circular dichroism (CD) spectroscopy, far-UV 7.2 Phosphate buffer protein 0.2 Nuclear magnetic resonance (NMR) 308 3 H2O super distilled TFE-d2 Paper 16234236 Fossen T, Wray V, Bruns K, Rachmat J, Henklein P, Tessmer U, Maczurek A, Klinger P, Schubert U 2005 J Biol Chem The sequence given is the sequence of the Pr55 Gag polyprotein from HIV Type 1. p6 protein is the C-terminal part of Pr55. In its mature state p6 protein is free from Pr55. This entry is for the mature free state of p6. Secondary structure, elucidated by CD and NMR spectroscopy, strongly depends on the structure-stabilizing effect of TFE. Previous entry DP00101 has been split into polyprotein (DP00101) and cleavage product (DP00101_C006). Myosin-11 MYH11_CHICK Myosin heavy chain 11 Myosin heavy chain, gizzard smooth muscle P10587 Gga.3225 MYH11_CHICK 3915778 Gallus gallus (Chicken) 1979 MSQKPLSDDEKFLFVDKNFVNNPLAQADWSAKKLVWVPSEKHGFEAASIKEEKGDEVTVELQENGKKVTLSKDDIQKMNPPKFSKVEDMAELTCLNEASVLHNLRERYFSGLIYTYSGLFCVVINPYKQLPIYSEKIIDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDTSITQGPSFSYGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHIFYYLIAGASEQMRNDLLLEGFNNYTFLSNGHVPIPAQQDDEMFQETLEAMTIMGFTEEEQTSILRVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADFAIEALAKAKFERLFRWILTRVNKALDKTKRQGASFLGILDIAGFEIFEINSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPTNPPGVLALLDEECWFPKATDTSFVEKLIQEQQNHAKFQKSKQLKDKTEFCILHYAGKVTYNASAWLTKNMDPLNDNVTSLLNQSSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYKEQLTKLMTTLRNTNPNFVRCIIPNHEKRAGKLDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFRTGVLAHLEEERDLKITDVIIAFQAQCRGYLARKAFAKRQQQLTAMLVIQRNCAAYLKLRNWQWWRLFTKVKPLLQVTRQEEEMQAKDEELQRTKERQQKAEAELKELEQKHTQLCEEKNLLQEKLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARIEEEEERSQQLQAEKKKMQQQMLDLEEQLEEEEAARQKLQLEKVTADGKIKKMEDDILIMEDQNNKLTKERKLLEERVSDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKIKRKLEGESSDLHEQIAELQAQIAELKAQLAKKEEELQAALARLEDETSQKNNALKKIRELESHISDLQEDLESEKAARNKAEKQKRDLSEELEALKTELEDTLDTTATQQELRAKREQEVTVLKRALEEETRTHGAQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKTKQTLEKDNADLANEIRSLSQAKQDVEHKKKKLEVQLQDLQSKYSDGERVRTELNEKVHKLQIEVENVTSLLNEAESKNIKLTKDVATLGSQLQDTQELLQEETRQKLNVTTKLRQLEDDKNSLQEQLDEEVEAKQNLERHISTLTIQLSDSKKKLQEFTATVETMEEGKKKLQREIESLTQQFEEKAASYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQMLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRTLEQQVEEMKTQLEELEDELQAAEDAKLRLEVNMQAMKSQFERDLQARDEQNEEKRRQLLKQLHEHETELEDERKQRALAAAAKKKLEVDVKDLESQVDSANKAREEAIKQLRKLQAQMKDYQRDLDDARAAREEIFATARENEKKAKNLEAELIQLQEDLAAAERARKQADLEKEEMAEELASANSGRTSLQDEKRRLEARIAQLEEELDEEHSNIETMSDRMRKAVQQAEQLNNELATERATAQKNENARQQLERQNKELRSKLQEMEGAVKSKFKSTIAALEAKIASLEEQLEQEAREKQAAAKTLRQKDKKLKDALLQVEDERKQAEQYKDQAEKGNLRLKQLKRQLEEAEEESQRINANRRKLQRELDEATESNDALGREVAALKSKLRRGNEPVSFAPPRRSGGRRVIENATDGGEEEIDGRDGDFNGKASE Disordered 790 791 LK Engineered 1BR2A 1BR2B 1BR2C 1BR2D 1BR2E 1BR2F Relationship to function unknown Unknown Unknown X-ray crystallography 100 6.8 cryoprotectant 25% polyethylene glycol 200 Paper 9741621 Dominguez R, Freyzon Y, Trybus KM, Cohen C 1998 Cell 94 5 559-71 Disordered 627 656 DVDRIVGLDQMAKMTESSLPSASKTKKGMF Engineered 1BR2A 1BR2B 1BR2C 1BR2D 1BR2E 1BR2F Relationship to function unknown Unknown Unknown X-ray crystallography 100 6.8 cryoprotectant 25% polyethylene glycol 200 Paper 9741621 Dominguez R, Freyzon Y, Trybus KM, Cohen C 1998 Cell 94 5 559-71 Disordered 573 577 KQLKD Engineered 1BR2A 1BR2B 1BR2C 1BR2D 1BR2E 1BR2F Relationship to function unknown Unknown Unknown X-ray crystallography 100 6.8 cryoprotectant 25% polyethylene glycol 200 Paper 9741621 Dominguez R, Freyzon Y, Trybus KM, Cohen C 1998 Cell 94 5 559-71 Disordered 546 549 WFPK Engineered 1BR2A 1BR2B 1BR2C 1BR2D 1BR2E 1BR2F Relationship to function unknown Unknown Unknown X-ray crystallography 100 6.8 cryoprotectant 25% polyethylene glycol 200 Paper 9741621 Dominguez R, Freyzon Y, Trybus KM, Cohen C 1998 Cell 94 5 559-71 The PDB file 1BR2 shows the disordered region ending at amino acid PRO-548. Disordered 452 457 KTKRQG Engineered 1BR2A 1BR2B 1BR2C 1BR2D 1BR2E 1BR2F Relationship to function unknown Unknown Unknown X-ray crystallography 100 6.8 cryoprotectant 25% polyethylene glycol 200 Paper 9741621 Dominguez R, Freyzon Y, Trybus KM, Cohen C 1998 Cell 94 5 559-71 Disordered 371 374 RNTD Engineered 1BR2A 1BR2B 1BR2C 1BR2D 1BR2E 1BR2F Relationship to function unknown Unknown Unknown X-ray crystallography 100 6.8 cryoprotectant 25% polyethylene glycol 200 Paper 9741621 Dominguez R, Freyzon Y, Trybus KM, Cohen C 1998 Cell 94 5 559-71 Disordered 50 55 KEEKGD Engineered 1BR2A 1BR2B 1BR2C 1BR2D 1BR2E 1BR2F Relationship to function unknown Unknown Unknown X-ray crystallography 100 6.8 cryoprotectant 25% polyethylene glycol 200 Paper 9741621 Dominguez R, Freyzon Y, Trybus KM, Cohen C 1998 Cell 94 5 559-71 Disordered 1 33 MSQKPLSDDEKFLFVDKNFVNNPLAQADWSAKK Engineered 1BR2A 1BR2B 1BR2C 1BR2D 1BR2E 1BR2F Relationship to function unknown Unknown Unknown X-ray crystallography 100 6.8 cryoprotectant 25% polyethylene glydol 200 Paper 9741621 Dominguez R, Freyzon Y, Trybus KM, Cohen C 1998 Cell 94 5 559-71 Disordered 200 217 SHKGKKDTSITQGPSFSY Engineered 1BR2A 1BR2B 1BR2C 1BR2D 1BR2E 1BR2F Relationship to function unknown Unknown Unknown X-ray crystallography 100 6.8 cryoprotectant 25% polyethylene glycol 200 Paper 9147986 Rovner, A. S. Freyzon, Y. Trybus, K. M. 1997 Journal of Muscle Research and Cell Motility 18 1 103-110 The sequence information for this region came from Rovner et. al. (1997). It is a deviation from the Yanagisawa et. al sequence. This region is part of a 7 AA insert that helps to differentiate between fast and slow smooth muscle. The insert increases the protein’s enzymatic capabilities, as well as its ability to bind and move actin filaments. Disordered 406 415 RIKVGRDVVQ Engineered 1BR2A 1BR2B 1BR2C 1BR2D 1BR2E 1BR2F Relationship to function unknown Unknown Unknown X-ray crystallography 100 6.8 cryoprotectant 25% polyethylene glycol 200 Paper 9741621 Dominguez R, Freyzon Y, Trybus KM, Cohen C 1998 Cell 94 5 559-71 Protein grpE GRPE_ECOLI HSP-70 cofactor Heat shock protein B25.3 HSP24 P09372 GRPE_ECOLI 121638 Escherichia coli (strain K12) 197 MSSKEQKTPEGQAPEEIIMDQHEEIEAVEPEASAEQVDPRDEKVANLEAQLAEAQTRERDGILRVKAEMENLRRRTELDIEKAHKFALEKFINELLPVIDSLDRALEVADKANPDMSAMVEDIELTLKSMLDVVRKFGVEVIAETNVPLDPNVHQAIAMVESDDVAPGNVLGIMQKGYTLNGRTIRAAMVTVAKAKA Disordered Flexible loop 108 115 VADKANPD Mutant 1DGKA 1DGKB Function arises from the disordered state Chaperones Flexible linkers/spacers Protein-DNA binding Substrate/ligand binding X-ray crystallography 100 4.6 resolution 2.8 Paper 9103205 Harrison CJ, Hayer-Hartl M, Di Liberto M, Hartl F, Kuriyan J 1997 Science 276 5311 431-5 Mutant G122D, in which Gly at position 122 is mutated to Asp was used. Transcription initiation factor IIA large subunit TOA1_YEAST TFIIA large subunit TFIIA 32 kDa subunit P32773 TOA1_YEAST 418108 Saccharomyces cerevisiae (Baker's yeast) 286 MSNAEASRVYEIIVESVVNEVREDFENAGIDEQTLQDLKNIWQKKLTETKVTTFSWDNQFNEGNINGVQNDLNFNLATPGVNSSEFNIKEENTGNEGLILPNINSNNNIPHSGETNINTNTVEATNNSGATLNTNTSGNTNADVTSQPKIEVKPEIELTINNANITTVENIDDESEKKDDEEKEEDVEKTRKEKEQIEQVKLQAKKEKRSALLDTDEVGSELDDSDDDYLISEGEEDGPDENLMLCLYDKVTRTKARWKCSLKDGVVTINRNDYTFQKAQVEAEWV Disordered 210 240 SALLDTDEVGSELDDSDDDYLISEGEEDGPD Complex Fragment Transactivation (transcriptional activation) Protein-protein binding X-ray crystallography 103 Paper 8610010 Tan S, Hunziker Y, Sargent DF, Richmond TJ 1996 Nature 381 6578 127-51 The fragment used for structure determination consisted of the C-terminal 76 residues.(aa210-aa286) Diol dehydrase beta subunit Q59471_KLEOX EC=4.2.1.28 Q59471 Q59471_KLEOX 75350363 Klebsiella oxytoca 224 MEINEKLLRQIIEDVLSEMKGSDKPVSFNAPAASAAPQATPPAGDGFLTEVGEARQGTQQDEVIIAVGPAFGLAQTVNIVGIPHKSILREVIAGIEEEGIKARVIRCFKSSDVAFVAVEGNRLSGSGISIGIQSKGTTVIHQQGLPPLSNLELFPQAPLLTLETYRQIGKNAARYAKRESPQPVPTLNDQMARPKYQAKSAILHIKETKYVVTGKNPQELRVAL Disordered 1 45 MEINEKLLRQIIEDVLSEMKGSDKPVSFNAPAASAAPQATPPAGD Complex 1EGMB X-ray crystallography Potassium phosphate buffer pH 8.0 10 Cyanocobalamin 2.5 1,2-propanediol 2.0% lauryldimethylamine oxide (LDAO) 0.10% Paper 10467140 Shibata N, Masuda J, Tobimatsu T, Toraya T, Suto K, Morimoto Y, Yasuoka N 1999 Structure Fold Des 7 8 997-1008 Diol dehydrase gamma subunit Q59472_KLEOX EC=4.2.1.28 Q59472 Q59472_KLEOX 75350364 Klebsiella oxytoca 173 MNTDAIESMVRDVLSRMNSLQGEAPAAAPAAGGASRSARVSDYPLANKHPEWVKTATNKTLDDFTLENVLSNKVTAQDMRITPETLRLQASIAKDAGRDRLAMNFERAAELTAVPDDRILEIYNALRPYRSTKEELLAIADDLESRYQAKICAAFVREAATLYVERKKLKGDD Disordered 1 36 MNTDAIESMVRDVLSRMNSLQGEAPAAAPAAGGASR Complex 1EGMG X-ray crystallography Potassium phosphate buffer pH 8.0 10 Cyanocobalamin 2.5 1,2-propanediol 2.0% lauryldimethylamine oxide (LDAO) 0.10% Paper 10467140 Shibata N, Masuda J, Tobimatsu T, Toraya T, Suto K, Morimoto Y, Yasuoka N 1999 Structure Fold Des 7 8 997-1008 Ribonucleoside-diphosphate reductase 1 subunit beta RIR2_ECOLI EC=1.17.4.1 Ribonucleotide reductase 1 Protein B2 Protein R2 P69924 RIR2_ECOLI 57014104 Escherichia coli (strain K12) 376 MAYTTFSQTKNDQLKEPMFFGQPVNVARYDQQKYDIFEKLIEKQLSFFWRPEEVDVSRDRIDYQALPEHEKHIFISNLKYQTLLDSIQGRSPNVALLPLISIPELETWVETWAFSETIHSRSYTHIIRNIVNDPSVVFDDIVTNEQIQKRAEGISSYYDELIEMTSYWHLLGEGTHTVNGKTVTVSLRELKKKLYLCLMSVNALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLNLLRSGADDPEMAEIAEECKQECYDLFVQAAQQEKDWADYLFRDGSMIGLNKDILCQYVEYITNIRMQAVGLDLPFQTRSNPIPWINTWLVSDNVQVAPQEVEVSSYLVGQIDSEVDTDDLSNFQL Disordered 342 376 SDNVQVAPQEVEVSSYLVGQIDSEVDTDDLSNFQL Paper 8805591 Logan DT, Su XD, Aberg A, Regnstrom K, Hajdu J, Eklund H, Nordlund P 1996 Structure 4 9 1053-64 Periplasmic [Fe] hydrogenase large subunit PHFL_DESVH EC=1.12.7.2 Fe hydrogenlyase P07598 PHFL_DESVH 130070 Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303) 421 MSRTVMERIEYEMHTPDPKADPDKLHFVQIDEAKCIGCDTCSQYCPTAAIFGEMGEPHSIPHIEACINCGQCLTHCPENAIYEAQSWVPEVEKKLKDGKVKCIAMPAPAVRYALGDAFGMPVGSVTTGKMLAALQKLGFAHCWDTEFTADVTIWEEGSEFVERLTKKSDMPLPQFTSCCPGWQKYAETYYPELLPHFSTCKSPIGMNGALAKTYGAERMKYDPKQVYTVSIMPCIAKKYEGLRPELKSSGMRDIDATLTTRELAYMIKKAGIDFAKLPDGKRDSLMGESTGGATIFGVTGGVMEAALRFAYEAVTGKKPDSWDFKAVRGLDGIKEATVNVGGTDVKVAVVHGAKRFKQVCDDVKAGKSPYHFIEYMACPGGCVCGGGQPVMPGVLEAMDRTTTRLYAGLKKRLAMASANKA Disordered 398 421 MDRTTTRLYAGLKKRLAMASANKA Paper 10368269 Nicolet Y, Piras C, Legrand P, Hatchikian CE, Fontecilla-Camps JC 1999 Structure Fold Des 7 1 13-23 Carbonic anhydrase CAH_METTE EC=4.2.1.1 Carbonate dehydratase Carbonic dehydratase Carbonate hydro-lyase P40881 CAH_METTE 729004 Methanosarcina thermophila 247 MMFNKQIFTILILSLSLALAGSGCISEGAEDNVAQEITVDEFSNIRENPVTPWNPEPSAPVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGMPIFVGDRSNVQDGVVLHALETINEEGEPIEDNIVEVDGKEYAVYIGNNVSLAHQSQVHGPAAVGDDTFIGMQAFVFKSKVGNNCVLEPRSAAIGVTIPDGRYIPAGMVVTSQAEADKLPEVTDDYAYSHTNEAVVYVNVHLAEGYKETS Disordered 1 37 MMFNKQIFTILILSLSLALAGSGCISEGAEDNVAQEI X-ray crystallography Paper 10924115 Iverson TM, Alber BE, Kisker C, Ferry JG, Rees DC 2000 Biochemistry 39 31 9222-31 Protein C-ets-1 ETS1_MOUSE p54 P27577 Mm.292415 ETS1_MOUSE 729453 Mus musculus (Mouse) 440 MKAAVDLKPTLTIIKTEKVDLELFPSPDMECADVPLLTPSSKEMMSQALKATFSGFTKEQQRLGIPKDPRQWTETHVRDWVMWAVNEFSLKGVDFQKFCMSGAALCALGKECFLELAPDFVGDILWEHLEILQKEDVKPYQVNGANPTYPESCYTSDYFISYGIEHAQCVPPSEFSEPSFITESYQTLHPISSEELLSLKYENDYPSVILQDPLQTDTLQTDYFAIKQEVLTPDNMCLGRASRGKLGGQDSFESVESYDSCDRLTQSWSSQSSFNSLQRVPSYDSFDYEDYPAALPNHKPKGTFKDYVRDRADLNKDKPVIPAAALAGYTGSGPIQLWQFLLELLTDKSCQSFISWTGDGWEFKLSDPDEVARRWGKRKNKPKMNYEKLSRGLRYYYDKNIIHKTAGKRYVYRFVCDLQSLLGYTPEELHAMLDVKPDAD Disordered N-terminal region 1 49 MKAAVDLKPTLTIIKTEKVDLELFPSPDMECADVPLLTPSSKEMMSQAL Fragment Native 1BQVA Nuclear magnetic resonance (NMR) 303 6.5 10% D2O 10 mM KCl, 10 mM KH2PO4, 10 mM DTT 1.2 mM Ets-1 amide 1HN and 15N chemical shifts Sensitivity to proteolysis 296 6 200 ng trypsin 20mMcitrate, 150mMKCl, 1mMDTT 2.75 microg protein Paper 9770451 Slupsky CM, Gentile LN, Donaldson LW, Mackereth CD, Seidel JJ, Graves BJ, McIntosh LP 1998 Proc Natl Acad Sci U S A 95 21 12129-34 Disordered SRR 244 301 GKLGGQDSFESVESYDSCDRLTQSWSSQSSFNSLQRVPSYDSFDYEDYPAALPNHKPK Fragment Function arises via a disorder to order transition Molecular assembly Phosphorylation Protein-DNA binding Autoregulatory Nuclear magnetic resonance (NMR) Paper 15994560 Pufall MA, Lee GM, Nelson ML, Kang HS, Velyvis A, Kay LE, McIntosh LP, Graves BJ 2005 Science 309 5731 142-5 Desiccation-related protein clone PCC6-19 DHB_CRAPL CDET6-19 P22239 DHB_CRAPL 118518 Craterostigma plantagineum 155 MAQFGGEKYGGRHTDEYGNPIQQGAGAHRGGGIMGGGQQAGQHGTTGVLGHGTAGQHGTTGGGLGHGTAGTGGALGGQHRRSGSSSSSSSSESDGEGGRRKKGMKDKMKEKLPGGHGTTTDQQQYGTAATHGQAQQHEKKGIMDKIKEKLPGGQH Disordered - Molten Globule 1 155 MAQFGGEKYGGRHTDEYGNPIQQGAGAHRGGGIMGGGQQAGQHGTTGVLGHGTAGQHGTTGGGLGHGTAGTGGALGGQHRRSGSSSSSSSSESDGEGGRRKKGMKDKMKEKLPGGHGTTTDQQQYGTAATHGQAQQHEKKGIMDKIKEKLPGGQH Native Function arises via a molten globule to order transition Molecular recognition effectors Substrate/ligand binding Circular dichroism (CD) spectroscopy, far-UV Nuclear magnetic resonance (NMR) 283 D2O 50 Dsp16 protein 11.6 EDTA 1 KCl 100 phosphate buffer 10 water 450 Nuclear magnetic resonance (NMR) 308 D2O 50 Dsp16 protein 11.6 EDTA 1 KCl 100 phosphate buffer 10 water 450 Paper 9067253 Lisse T, Bartels D, Kalbitzer HR, Jaenicke R 1996 Biol Chem 377 9 555-61 Piatkowski D Schneider K Salamini F Bartels D 1990 Plant Physiol 94 1682-1688 Synaptobrevin homolog 1 SNC1_YEAST P31109 SNC1_YEAST 401107 Saccharomyces cerevisiae (Baker's yeast) 117 MSSSTPFDPYALSEHDEERPQNVQSKSRTAELQAEIDDTVGIMRDNINKVAERGERLTSIEDKADNLAVSAQGFKRGANRVRKAMWYKDLKMKMCLALVIIILLVVIIVPIAVHFSR Disordered 1 93 MSSSTPFDPYALSEHDEERPQNVQSKSRTAELQAEIDDTVGIMRDNINKVAERGERLTSIEDKADNLAVSAQGFKRGANRVRKAMWYKDLKMK Fragment Paper 9326367 Rice LM, Brennwald P, Brunger AT 1997 FEBS Lett 415 1 49-55 Tubulin beta-4 chain TBB4_HUMAN Tubulin 5 beta P04350 Hs.110837 TBB4_HUMAN 93141323 Homo sapiens (Human) 444 MREIVHLQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLERINVYYNEATGGNYVPRAVLVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDAVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKMREEFPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPAFAPLTSRGSQQYRGLTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGRMSMKEVDEQMLSVQSKNSSYFVEWIPNNVKTAVCDIPPRGLKMAVTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEQGEFEEEAEEEVA Disordered 394 444 FLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEQGEFEEEAEEEVA Fragment Native Relationship to function unknown Unknown Unknown Circular dichroism (CD) spectroscopy, far-UV Paper 10211825 Jimenez MA, Evangelio JA, Aranda C, Lopez-Brauet A, Andreu D, Rico M, Lagos R, Andreu JM, Monasterio O 1999 Protein Sci 8 4 788-799 Osteocalcin OSTCN_CANFA Gamma-carboxyglutamic acid-containing protein Bone Gla protein BGP P81455 OSTCN_CANFA 3914247 Canis familiaris (dog) 49 YLDSGLGAPVPYPDPLEPKREVCELNPNCDELADHIGFQEAYQRFYGPV Disordered - Extended 1 49 YLDSGLGAPVPYPDPLEPKREVCELNPNCDELADHIGFQEAYQRFYGPV Native Function arises via a disorder to order transition Molecular assembly Substrate/ligand binding Nuclear magnetic resonance (NMR) 298 6.8 imidazole buffer 30 sodium chloride buffer 20 calcium chloride buffer 5 Size exclusion/gel filtration chromatography 298 6.8 calcium chloride buffer 5 imidazole buffer 30 sodium chloride buffer 20 Paper 8101026 Colombo G, Fanti P, Yao C, Malluche HH 1993 J Bone Miner Res 8 6 733-43 8218200 Isbell DT, Du S, Schroering AG, Colombo G, Shelling JG 1993 Biochemistry 32 42 11352-11362 This protein is only disordered in the absence of calcium. When calcium is present, the conformation dramatically changes to a more ordered state. Protein transport protein Sec61 subunit gamma SC61G_CANFA P60058 Cfa.40294 SC61G_CANFA 38503385 Canis familiaris (dog) 68 MDQVMQFVEPSRQFVKDSIRLVKRCTKPDRKEFQKIAMATAIGFAIMGFIGFFVKLIHIPINNIIVGG Disordered - Extended 1 9 MDQVMQFVE Engineered Fragment Mutant Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 274 5 Paper 8942632 Beswick V, Baleux F, Huynh-Dinh T, Kepes F, Neumann JM, Sanson A 1996 Biochemistry 35 47 14717-24 This disordered region was characterized by the study of an engineered fragment containing residues 1-43. This fragment was synthesized via the Merrifield solid-phase method with a mutation at Cys24Ser. This mutation was inserted to prevent dimerization. Disordered - Extended 18 43 SIRLVKRCTKPDRKEFQKIAMATAIG Engineered Fragment Mutant Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 274 5 Paper 8942632 Beswick V, Baleux F, Huynh-Dinh T, Kepes F, Neumann JM, Sanson A 1996 Biochemistry 35 47 14717-24 This disordered region was characterized by the study of an engineered fragment containing residues 1-43. This fragment was synthesized via the Merrifield solid-phase method with a mutation at Cys24Ser. This mutation was inserted to prevent dimerization. Disordered - Extended 1 4 MDQV Engineered Fragment Mutant Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 311 6 perdeuterated DPC Paper 8942632 Beswick V, Baleux F, Huynh-Dinh T, Kepes F, Neumann JM, Sanson A 1996 Biochemistry 35 47 14717-24 This disordered region was characterized by the study of an engineered fragment containing residues 1-43. This fragment was synthesized via the Merrifield solid-phase method with a mutation at Cys24Ser. This mutation was inserted to prevent dimerization. Disordered - Extended 40 43 TAIG Engineered Fragment Mutant Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 311 5 perdeuterated DPC Paper 8942632 Beswick V, Baleux F, Huynh-Dinh T, Kepes F, Neumann JM, Sanson A 1996 Biochemistry 35 47 14717-24 This disordered region was characterized by the study of an engineered fragment containing residues 1-43. This fragment was synthesized via the Merrifield solid-phase method with a mutation at Cys24Ser. This mutation was inserted to prevent dimerization. Chromogranin-A CMGA_BOVIN CgA Pituitary secretory protein I SP-I Vasostatin-1 [cleavage product 1] Chromostatin [cleavage product 2] Chromacin [cleavage product 3] Pancreastatin [cleavage product 4] WE-14 [cleavage product 5] Catestatin [cleavage product 6] P05059 Bt.49630 CMGA_BOVIN 116548 Bos taurus (Bovine) 449 MRSAAVLALLLCAGQVIALPVNSPMNKGDTEVMKCIVEVISDTLSKPSPMPVSKECFETLRGDERILSILRHQNLLKELQDLALQGAKERTHQQKKHSSYEDELSEVLEKPNDQAEPKEVTEEVSSKDAAEKRDDFKEVEKSDEDSDGDRPQASPGLGPGPKVEEDNQAPGEEEEAPSNAHPLASLPSPKHPGPQAKEDSEGPSQGPASREKGLSAEQGRQTEREEEEEKWEEAEAREKAVPEEESPPTAAFKAPPSLGNKETQRAAPGWPEDGAGKMGAEEAKPPEGKGEWAHSRQEEEEMARAPQVLFRGGKSGEPEQEEQLSKEWEDAKRWSKMDQLAKELTAEKRLEGEEEEEEDPDRSMRLSFRARGYGFRGPGLQLRRGWRPNSREDSVEAGLPLQVRGYPEEKKEEEGSANRRPEDQELESLSAIEAELEKVAHQLEELRRG Disordered - Extended 407 431 PEEKKEEEGSANRRPEDQELESLSA Engineered Fragment Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding SDS-PAGE gel, Aberrant mobility on 310 7.5 Tris-HCl 0.2 Circular dichroism (CD) spectroscopy, near-UV 295 5.5 sodium acetate salt 15 Circular dichroism (CD) spectroscopy, near-UV 295 7.5 Tris-HCl 15 Sensitivity to proteolysis Paper 3473966 Grimes M, Iacangelo A, Eiden LE, Godfrey B, Herbert E 1987 Ann N Y Acad Sci 493 351-378 8243650 Yoo SH, Ferretti JA 1993 FEBS Lett 334 3 373-377 The disordered region is not found within any of the cleavage products. Basic salivary proline-rich protein 4 PRB4_HUMAN Salivary proline-rich protein Po Parotid o protein Salivary proline-rich protein II-1 Protein N1 [cleavage product 1] Glycosylated protein A [cleavage product 2] Peptide P-D [cleavage product 3] Proline-rich peptide IB-5 P10163 Hs.528651 PRB4_HUMAN 158517854 Homo sapiens (Human) 310 MLLILLSVALLALSSAESSSEDVSQEESLFLISGKPEGRRPQGGNQPQRPPPPPGKPQGPPPQGGNQSQGPPPPPGKPEGRPPQGGNQSQGPPPHPGKPERPPPQGGNQSQGPPPHPGKPESRPPQGGHQSQGPPPTPGKPEGPPPQGGNQSQGTPPPPGKPEGRPPQGGNQSQGPPPHPGKPERPPPQGGNQSHRPPPPPGKPERPPPQGGNQSQGPPPHPGKPEGPPPQEGNKSRSARSPPGKPQGPPQQEGNKPQGPPPPGKPQGPPPPGGNPQQPQAPPAGKPQGPPPPPQGGRPPRPAQGQQPPQ Disordered 17 310 ESSSEDVSQEESLFLISGKPQGRRPQGGNQPQRPPPPPGKPQGPPPQGGNQSQGPPPPPGKPEGRPPQGGNQSQGPPPHPGKPERPPPQGGNQSQGPPPHPGKPESRPPQGGHQSQGPPPTPGKPEGPPPQGGNQSQGTPPPPGKPEGRPPQGGNQSQGPPPHPGKPERPPPQGGNQSHRPPPPPGKPERPPPQGGNQSQGPPPHPGKPEGPPPQEGNKSRSARSPPGKPQGPPQQEGNKPQGPPPPGKPQGPPPPGGNPQQPQAPPAGKPQGPPPPPQGGRPPRPAQGQQPPQ Paper 4093242 Loomis RE, Bergey EJ, Levine MJ, Tabak LA 1985 Int J Pept Protein Res 26 6 621-9 Loomis RE, Tseng Ching-Chung, Levine MJ 1986 Int J Biol Macromol 8 149-52 Disordered residues are found within the regions corresponding to cleavage products 1 - 3, however, these products are not discussed in the references provided. Caldesmon CALD1_CHICK CDM P12957 Gga.4988 CALD1_CHICK 2506984 Gallus gallus (Chicken) 771 MDDFERRRELRRQKREEMRLEAERLSYQRNDDDEEEAARERRRRARQERLRQKEEGDVSGEVTEKSEVNAQNSVAEEETKRSTDDEAALLERLARREERRQKRLQEALERQKEFDPTITDGSLSVPSRREVNNVEENEITGKEEKVETRQGRCEIEETETVTKSYQRNNWRQDGEEEGKKEEKDSEEEKPKEVPTEENQVDVAVEKSTDKEEVVETKTLAVNAENDTNAMLEGEQSITDAADKEKEEAEKEREKLEAEEKERLKAEEEKKAAEEKQKAEEEKKAAEERERAKAEEEKRAAEERERAKAEEERKAAEERERAKAEEERKAAEERAKAEEERKAAEERAKAEEERKAAEERAKAEKERKAAEERERAKAEEEKRAAEEKARLEAEKLKEKKKMEEKKAQEEKAQANLLRKQEEDKEAKVEAKKESLPEKLQPTSKKDQVKDNKDKEKAPKEEMKSVWDRKRGVPEQKAQNGERELTTPKLKSTENAFGRSNLKGAANAEAGSEKLKEKQQEAAVELDELKKRREERRKILEEEEQKKKQEEAERKIREEEEKKRMKEEIERRRAEAAEKRQKVPEDGVSEEKKPFKCFSPKGSSLKIEERAEFLNKSAQKSGMKPAHTTAVVSKIDSRLEQYTSAVVGNKAAKPAKPAASDLPVPAEGVRNIKSMWEKGNVFSSPGGTGTPNKETAGLKVGVSSRINEWLTKTPEGNKSPAPKPSDLRPGDVSGKRNLWEKQSVEKPAASSSKVTATGKKSETNGLRQFEKEP Disordered - Extended 636 771 RLEQYTSAVVGNKAAKPAKPAASDLPVPAEGVRNIKSMWEKGNVFSSPGGTGTPNKETAGLKVGVSSRINEWLTKTPEGNKSPAPKPSDLRPGDVSGKRNLWEKQSVEKPAASSSKVTATGKKSETNGLRQFEKEP Complex Engineered Fragment Isoform Function arises via a pre-molten globule to order transition Molecular recognition effectors Phosphorylation Protein-protein binding SDS-PAGE gel, Aberrant mobility on 293 Calcium Calmodulin Circular dichroism (CD) spectroscopy, far-UV 293 Calcium Calmodulin Size exclusion/gel filtration chromatography 293 Calcium Calmodulin Small-angle X-ray scattering (SAXS) 293 Calcium Calmodulin Stability at thermal extremes 293 Calcium Calmodulin Paper 2803315 Hayashi K, Kanda K, Kimizuka F, Kato I, Sobue K 1989 Biochem Biophys Res Commun 164 1 503-511 14635127 Permyakov SE, Millett IS, Doniach S, Permyakov EA, Uversky VN 2003 Proteins 53 4 855-862 11996092 Czuryło EA 2000 Acta Biochim Pol 47 4 1019-26 Protein L precursor Q51912_PEPMA Q51912 Q51912_PEPMA 75504278 Peptostreptococcus magnus (Finegoldia magna) 719 MAALAGAIVVTGGVGSYAADEPIDLEKLEEKRDKENVGNLPKFDNEVKDGSENPMAKYPDFDDEASTRFETENNEFEEKKVVSDNFFDQSEHPFVENKEETPETPETDSEEEVTIKANLIFANGSTQTAEFKGTFEKATSEAYAYADTLKKDNGEYTVDVADKGYTLNIKFAGKEKTPEEPKEEVTIKANLIYADGKTQTAEFKGTFEEATAEAYRYADALKKDNGEYTVDVADKGYTLNIKFAGKEKTPEEPKEEVTIKANLIYADGKTQTAEFKGTFEEATAEAYRYADLLAKENGKYTVDVADKGYTLNIKFAGKEKTPEEPKEEVTIKANLIYADGKTQTAEFKGTFAEATAEAYRYADLLAKENGKYTADLEDGGYTINIRFAGKKVDEKPEEKEQVTIKENIYFEDGTVQTATFKGTFAEATAEAYRYADLLSKEHGKYTADLEDGGYTINIRFAGKEEPEETPEKPEVQDGYASYEEAEAAAKEALKNDDVNKSYTIRQGADGRYYYVLSPVEAEEEKPEAQNGYATYEEAEAAAKKALENDPINKSYSIRQGADGRYYYVLSPVEAETPEKPVEPSEPSTPDVPSNPSNPSTPDVPSTPDVPSNPSTPEVPSNPSTPGNEEKPGNEQKPGNEQKPGNEQKPGNEQKPGNEQKPDQPSKPEKEENGKGGVDSPKKKEKAALPKAGSEAEILTLAAASLSSVAGAFISLKKRK Disordered - Extended 1 17 MAALAGAIVVTGGVGSY Engineered Fragment 2PTLA Function arises from the disordered state Unknown Unknown Nuclear magnetic resonance (NMR) PDB Wikstroem M, Sjoebring U, Kastern W, Bjoerck L 1993 32 3381 Disordered - Extended 95 115 VENKEETPETPETDSEEEVTI Engineered Fragment Function arises via a disorder to order transition Unknown Unknown Circular dichroism (CD) spectroscopy, far-UV 4.1 Paper 9007989 Ramirez-Alvarado M, Serrano L, Blanco FJ 1997 Protein Sci 6 1 162-174 Disordered - Extended 114 123 TIKANLIFAN Engineered Fragment Function arises from the disordered state Unknown Unknown Nuclear magnetic resonance (NMR) TFE Paper 9007989 Ramirez-Alvarado M, Serrano L, Blanco FJ 1997 Protein Sci 6 1 162-174 Disordered - Extended 114 138 TIKANLIFANGSTQTAEFKGTFEKA Engineered Fragment Function arises via a disorder to order transition Unknown Unknown Circular dichroism (CD) spectroscopy, far-UV Nuclear magnetic resonance (NMR) Paper 9007989 Ramirez-Alvarado M, Serrano L, Blanco FJ 1997 Protein Sci 6 1 162-174 Disordered - Extended 135 138 FEKA Engineered Fragment Function arises from the disordered state Unknown Unknown Nuclear magnetic resonance (NMR) TFE Paper 9007989 Ramirez-Alvarado M, Serrano L, Blanco FJ 1997 Protein Sci 6 1 162-174 Disordered - Extended 136 155 EKATSEAYAYADTLKKDNGE Engineered Fragment Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV Nuclear magnetic resonance (NMR) 295 Paper 9007989 Ramirez-Alvarado M, Serrano L, Blanco FJ 1997 Protein Sci 6 1 162-174 Microtubule-associated protein 2 MAP2_RAT MAP-2 P15146 Rn.10484 MAP2_RAT 547890 Rattus norvegicus (Rat) 1861 MADERKDEGKAPHWTSASLTEAAAHPHSPEMKDQGGSGEGLSRSANGFPYREEEEGAFGEHGSQGTYSDTKENGINGELTSADRETAEEVSARIVQVVTAEAVAVLKGEQEKEAQHKDQPAALPLAAEETVNLPPSPPPSPASEQTAALEEDLLTASKMEFPEQQKLPSSFAEPLDKEETEFKMQSKPGEDFEHAALVPQPDTSKTPQDKKDPQDMEGEKSPASPFAQTFGTNLEDIKQITEPSITVPSIGLSAEPLAPKDQKDWFIEMPVESKKDEWGLAAPISPGPLTPMREKDVLEDIPRWEGKQFDSPMPSPFHGGSFTLPLDTVKDERVTEGSQPFAPVFFQSDDKMSLQDTSGSATSKESSKDEEPQKDKADKVADVPVSEATTVLGDVHSPAVEGFVGENISGEEKGTTDQEKKETSTPSVQEPTLTETEPQTKLEETSKVSIEETVAKEEESLKLKDDKAGVIQTSTEQSFSKEDQKGQEQTIEALKQDSFPISLEQAVTDAAMATKTLEKVTSEPEAVSEKREIQGLFEEDIADKSKLEGAGSATVAEVEMPFYEDKSGMSKYFETSALKEDVTRSTGLGSDYYELSDSRGNAQESLDTVSPKNQQDEKELLAKASQPSPPAHEAGYSTLAQSYTSDHPSELPEEPSSPQERMFTIDPKVYGEKRDLHSKNKDDLTLSRSLGLGGRSAIEQRSMSINLPMSCLDSIALGFNFGRGHDLSPLASDILTNTSGSMDEGDDYLPPTTPAVEKIPCFPIESKEEEDKTEQAKVTGGQTTQVETSSESPFPAKEYYKNGTVMAPDLPEMLDLAGTRSRLASVSADAEVARRKSVPSEAVVAESSTGLPPVADDSQPVKPDSQLEDMGYCVFNKYTVPLPSPVQDSENLSGESGSFYEGTDDKVRRDLATDLSLIEVKLAAAGRVKDEFTAEKEASPPSSADKSGLSREFDQDRKANDKLDTVLEKSEEHVDSKEHAKESEEVGDKVELFGLGVTYEQTSAKELITTKETAPERAEKGLSSVPEVAEVETTTKADQGLDVAAKKDDQSPLDIKVSDFGQMASGMSVDAGKTIELKFEVDQQLTLSSEAPQETDSFMGIESSHVKDGAKVSETEVKEKVAKPDLVHQEAVDKEESYESSGEHESLTMESLKPDEGKKETSPETSLIQDEVALKLSVEIPCPPPVSEADSSIDEKAEVQMEFIQLPKEESTETPDIPAIPSDVTQPQPEAVVSEPAEVRGEEEEIEAEGEYDKLLFRSDTLQITDLLVPGSREEFVETCPGEHKGVVESVVTIEDDFITVVQTTTDEGELGSHSVRFAAPVQPEEERRPYPHDEELEVLMAAEAQAEPKDGSPDAPATPEKEEVPFSEYKTETYDDYKDETTIDDSIMDADSLWVDTQDDDRSILTEQLETIPKEERAEKEARRPSLEKHRKEKPFKTGRGRISTPERREVAKKEPSTVSRDEVRRKKAVYKKAELAKESEVQAHSPSRKLILKPAIKYTRPTHLSCVKRKTTATSGESAQAPSAFKQAKDKVTDGITKSPEKRSSLPRPSSILPPRRGVSGDREENSFSLNSSISSARRTTRSEPIRRAGKSGTSTPTTPGSTAITPGTPPSYSSRTPGTPGTPSYPRTPGTPKSGILVPSEKKVAIIRTPPKSPATPKQLRLINQPLPDLKNVKSKIGSTDNIKYQPKGGQVRILNKKMDFSKVQSRCGSKDNIKHSAGGGNVQIVTKKIDLSHVTSKCGSLKNIRHRPGGGRVKIESVKLDFKEKAQAKVGSLDNAHHVPGGGNVKIDSQKLNFREHAKARVDHGAEIITQSPSRSSVASPRRLSNVSSSGSINLLESPQLATLAEDVTAALAKQGL Disordered 1 1861 MADERKDEGKAPHWTSASLTEAAAHPHSPEMKDQGGSGEGLSRSANGFPYREEEEGAFGEHGSQGTYSDTKENGINGELTSADRETAEEVSARIVQVVTAEAVAVLKGEQEKEAQHKDQPAALPLAAEETVNLPPSPPPSPASEQTAALEEDLLTASKMEFPEQQKLPSSFAEPLDKEETEFKMQSKPGEDFEHAALVPQPDTSKTPQDKKDPQDMEGEKSPASPFAQTFGTNLEDIKQITEPSITVPSIGLSAEPLAPKDQKDWFIEMPVESKKDEWGLAAPISPGPLTPMREKDVLEDIPRWEGKQFDSPMPSPFHGGSFTLPLDTVKDERVTEGSQPFAPVFFQSDDKMSLQDTSGSATSKESSKDEEPQKDKADKVADVPVSEATTVLGDVHSPAVEGFVGENISGEEKGTTDQEKKETSTPSVQEPTLTETEPQTKLEETSKVSIEETVAKEEESLKLKDDKAGVIQTSTEQSFSKEDQKGQEQTIEALKQDSFPISLEQAVTDAAMATKTLEKVTSEPEAVSEKREIQGLFEEDIADKSKLEGAGSATVAEVEMPFYEDKSGMSKYFETSALKEDVTRSTGLGSDYYELSDSRGNAQESLDTVSPKNQQDEKELLAKASQPSPPAHEAGYSTLAQSYTSDHPSELPEEPSSPQERMFTIDPKVYGEKRDLHSKNKDDLTLSRSLGLGGRSAIEQRSMSINLPMSCLDSIALGFNFGRGHDLSPLASDILTNTSGSMDEGDDYLPPTTPAVEKIPCFPIESKEEEDKTEQAKVTGGQTTQVETSSESPFPAKEYYKNGTVMAPDLPEMLDLAGTRSRLASVSADAEVARRKSVPSEAVVAESSTGLPPVADDSQPVKPDSQLEDMGYCVFNKYTVPLPSPVQDSENLSGESGSFYEGTDDKVRRDLATDLSLIEVKLAAAGRVKDEFTAEKEASPPSSADKSGLSREFDQDRKANDKLDTVLEKSEEHVDSKEHAKESEEVGDKVELFGLGVTYEQTSAKELITTKETAPERAEKGLSSVPEVAEVETTTKADQGLDVAAKKDDQSPLDIKVSDFGQMASGMSVDAGKTIELKFEVDQQLTLSSEAPQETDSFMGIESSHVKDGAKVSETEVKEKVAKPDLVHQEAVDKEESYESSGEHESLTMESLKPDEGKKETSPETSLIQDEVALKLSVEIPCPPPVSEADSSIDEKAEVQMEFIQLPKEESTETPDIPAIPSDVTQPQPEAVVSEPAEVRGEEEEIEAEGEYDKLLFRSDTLQITDLLVPGSREEFVETCPGEHKGVVESVVTIEDDFITVVQTTTDEGELGSHSVRFAAPVQPEEERRPYPHDEELEVLMAAEAQAEPKDGSPDAPATPEKEEVPFSEYKTETYDDYKDETTIDDSIMDADSLWVDTQDDDRSILTEQLETIPKEERAEKEARRPSLEKHRKEKPFKTGRGRISTPERREVAKKEPSTVSRDEVRRKKAVYKKAELAKESEVQAHSPSRKLILKPAIKYTRPTHLSCVKRKTTATSGESAQAPSAFKQAKDKVTDGITKSPEKRSSLPRPSSILPPRRGVSGDREENSFSLNSSISSARRTTRSEPIRRAGKSGTSTPTTPGSTAITPGTPPSYSSRTPGTPGTPSYPRTPGTPKSGILVPSEKKVAIIRTPPKSPATPKQLRLINQPLPDLKNVKSKIGSTDNIKYQPKGGQVRILNKKMDFSKVQSRCGSKDNIKHSAGGGNVQIVTKKIDLSHVTSKCGSLKNIRHRPGGGRVKIESVKLDFKEKAQAKVGSLDNAHHVPGGGNVKIDSQKLNFREHAKARVDHGAEIITQSPSRSSVASPRRLSNVSSSGSINLLESPQLATLAEDVTAALAKQGL Native Paper 15751971 Csizmok V, Bokor M, Banki P, Klement E, Medzihradszky KF, Friedrich P, Tompa K, Tompa P 2005 Biochemistry 44 10 3955-64 T-cell surface glycoprotein CD4 CD4_HUMAN T-cell surface antigen T4/Leu-3 P01730 Hs.631659 CD4_HUMAN 116013 Homo sapiens (Human) 458 MNRGVPFRHLLLVLQLALLPAATQGKKVVLGKKGDTVELTCTASQKKSIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRADSRRSLWDQGNFPLIIKNLKIEDSDTYICEVEDQKEEVQLLVFGLTANSDTHLLQGQSLTLTLESPPGSSPSVQCRSPRGKNIQGGKTLSVSQLELQDSGTWTCTVLQNQKKVEFKIDIVVLAFQKASSIVYKKEGEQVEFSFPLAFTVEKLTGSGELWWQAERASSSKSWITFDLKNKEVSVKRVTQDPKLQMGKKLPLHLTLPQALPQYAGSGNLTLALEAKTGKLHQEVNLVVMRATQLQKNLTCEVWGPTSPKLMLSLKLENKEAKVSKREKAVWVLNPEAGMWQCLLSDSGQVLLESNIKVLPTWSTPVQPMALIVLGGVAGLLLFIGLGIFFCVRCRHRRRQAERMSQIKRLLSEKKTCQCPHRFQKTCSPI Disordered cytoplasmic tail 421 458 RCRHRRRQAERMSQIKRLLSEKKTCQCPHRFQKTCSPI Fragment Native Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV 298 Nuclear magnetic resonance (NMR) 300 1.9 0.3 mg 1,4-dithiothreitol 9 mg peptide in 600 microl 50% TFE-d2 Paper 9622505 Wray V, Mertins D, Kiess M, Henklein P, Trowitzsch-Kienast W, Schubert U. 1998 Biochemistry 37 23 8527-38 CD and NMR results in aqueous solution were characteristic of a disordered peptide conformation with very little evidence of stable secondary structure. However, both the qualitative and quantitative NMR data provide convincing evidence for the presence of predominantly alfa-helical secondary structure upon increasing the content of TFE, but only a fraction of the complete CD4CYTO tail (from Gln-428 to Arg-437) has the ability of adopting stabilized helical structure in this environment. The N- and C-terminal regions, which are inherently nonstructured, destabilize the alfa-helical core structure. Addition of TFE causes a stabilization of the helical region in the molecule that already has a tendency for such a structure when this helical region of CD4CYTO was studied in water alone. However, in the context of full-length CD4CYTO, the helical core structure requires stabilizing factors which could be provided either by the membrane itself or by other CD4 interacting factors such as Vpu, Nef, or p56lck. Secretogranin-1 SCG1_BOVIN Secretogranin I SgI Chromogranin-B CgB Secretogranin-1(476-566) [cleavage product 1] Peptide BAM-1745 [cleavage product 2] Secretolytin [cleavage product 3] P23389 Bt.5448 SCG1_BOVIN 12644006 Bos taurus (Bovine) 646 MQPAALLGLLGATVVAAVSSMPVDIRNHNEEVVTHCIIEVLSNALLKSSAPPITPECRQVLKKNGKELKDEEKSENENTRFEVRLLRDPADTSEAPGLSSREDSGEGDAQVPTVADTESGGHSRERAGEPPGSQVAKEAKTRYSKSEGQNREEEMVKYQKRERGEVGSEERLSEGPGKAQMAFLNQRNQTPAKKEELVSRYDTQSARGLEKSHSRERSSQESGEETKSQENWPQELQRHPEGQEAPGESEEDASPEVDKRRSRPRHHHGRSRPDRSSQEGNPPLEEESHVGTGNSDEEKARHPAHFRALEEGAEYGEEVRRHSAAQAPGDLQGARFGGRGRGEHQALRRPSEESLEQENKRHGLSPDLNMAQGYSEESEEERGPARGPSYRARGGEAAAYSTLGQTDEKRFLGETHHRVQESQRDKARRRLPGELRNYLDYGEEKGEEAARGKWQPQGDPRDADENREEARLRGKQYAPHHITEKRLGELLNPFYDPSQWKSSRFERKDPMDDSFLEGEEENGLTLNEKNFFPEYNYDWWEKKPFEEDVNWGYEKRNPVPKLDLKRQYDRVAELDQLLHYRKKSAEFPDFYDSEEQVSPQHTAENEEEKAGQGVLTEEEEKELENLAAMDLELQKIAEKFSGTRRG Disordered 1 646 MQPAALLGLLGATVVAAVSSMPVDIRNHNEEVVTHCIIEVLSNALLKSSAPPITPECRQVLKKNGKELKDEEKSENENTRFEVRLLRDPADTSEAPGLSSREDSGEGDAQVPTVADTESGGHSRERAGEPPGSQVAKEAKTRYSKSEGQNREEEMVKYQKRERGEVGSEERLSEGPGKAQMAFLNQRNQTPAKKEELVSRYDTQSARGLEKSHSRERSSQESGEETKSQENWPQELQRHPEGQEAPGESEEDASPEVDKRRSRPRHHHGRSRPDRSSQEGNPPLEEESHVGTGNSDEEKARHPAHFRALEEGAEYGEEVRRHSAAQAPGDLQGARFGGRGRGEHQALRRPSEESLEQENKRHGLSPDLNMAQGYSEESEEERGPARGPSYRARGGEAAAYSTLGQTDEKRFLGETHHRVQESQRDKARRRLPGELRNYLDYGEEKGEEAARGKWQPQGDPRDADENREEARLRGKQYAPHHITEKRLGELLNPFYDPSQWKSSRFERKDPMDDSFLEGEEENGLTLNEKNFFPEYNYDWWEKKPFEEDVNWGYEKRNPVPKLDLKRQYDRVAELDQLLHYRKKSAEFPDFYDSEEQVSPQHTAENEEEKAGQGVLTEEEEKELENLAAMDLELQKIAEKFSGTRRG Paper 9136897 Yoo SH, Kang YK 1997 FEBS Lett 406 3 259-62 There are a number sequence conflicts according to the UniProt entry. So the sequence associated with the disorder-related paper does not match the sequence provided by UniProt. Disordered residues lie within the residues corresponding to each of the cleavage products, however, the cleavage products are not discussed in the given reference. Somatoliberin SLIB_BOVIN Growth hormone-releasing factor GRF Growth hormone-releasing hormone GHRH P63292 Bt.45045 SLIB_BOVIN 54039610 Bos taurus (Bovine) 106 MLLWVFFLVTLTLSSGSHGSLPSQPLRIPRYADAIFTNSYRKVLGQLSARKLLQDIMNRQQGERNQEQGAKVRLGRQVDGVWTDQQQMALESTLVSLLQERRNSQG Disordered U-90600F 31 59 YADAIFTNSYRKVLGQLSARKLLQDIMNR Engineered Fragment Mutant Function arises via a disorder to order transition Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) 323 5.6 Protein 100 mg/ml Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) 513 5.6 Protein 100 mg/ml Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) 297 5.6 Protein 100 mg/ml Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) 278 5.6 Protein 100 mg/ml Raman optical activity 313 Paper 9375414 Sarver RW Jr, Friedman AR, Thamann TJ 1997 Spectrochim Acta A Mol Biomol Spectrosc 53A 11 1889-900 U-90699F is an analog of the bovine growth hormone releasing factor. It is a fragment that contains the following substitutions: Ile32, Ser38, Ala45, Leu57, and Ser58. It also has a C-terminal tag of Hse-NH-ethyl x Ch3COOH. Microtubule-associated protein tau [Isoform Tau-F] TAU_HUMAN Neurofibrillary tangle protein Paired helical filament-tau PHF-tau Tau-4 P10636-8 Hs.101174 TAU_HUMAN 13124806 Homo sapiens (Human) 441 MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL Disordered - Extended 1 243 MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRL Engineered Isoform Relationship to function unknown Molecular assembly Protein-protein binding Circular dichroism (CD) spectroscopy, near-UV 295 7 Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) Small-angle X-ray scattering (SAXS) Stability at thermal extremes Rotory shadowing electron microscopy Paper 14769047 Barghorn S, Davies P, Mandelkow E 2004 Biochemistry 43 6 1694-703 2484340 Goedert M, Spillantini MG, Jakes R, Rutherford D, Crowther RA 1989 Neuron 3 4 519-526 15147841 Santarella RA, Skiniotis G, Goldie KN, Tittmann P, Gross H, Mandelkow EM, Mandelkow E, Hoenger A 2004 J Mol Biol 339 3 539-553 7929085 Schweers O, Schonbrunn-Hanebeck E, Marx A, Mandelkow E 1994 J Biol Chem 269 39 24290-24297 Disordered - Extended Core Domain/Binding Domain 244 368 QTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGN Engineered Isoform Function arises via a disorder to order transition Molecular assembly Protein-protein binding Stability at thermal extremes Rotory shadowing electron microscopy Paper 2484340 Goedert M, Spillantini MG, Jakes R, Rutherford D, Crowther RA 1989 Neuron 3 4 519-526 15147841 Santarella RA, Skiniotis G, Goldie KN, Tittmann P, Gross H, Mandelkow EM, Mandelkow E, Hoenger A 2004 J Mol Biol 339 3 539-553 7929085 Schweers O, Schonbrunn-Hanebeck E, Marx A, Mandelkow E 1994 J Biol Chem 269 39 24290-24297 Disordered - Extended Core Domain/Binding Domain 244 369 QTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNK Engineered Isoform Function arises via a disorder to order transition Molecular assembly Protein-protein binding Circular dichroism (CD) spectroscopy, near-UV 295 7 Rotory shadowing electron microscopy Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) Small-angle X-ray scattering (SAXS) Stability at thermal extremes Paper 14769047 Barghorn S, Davies P, Mandelkow E 2004 Biochemistry 43 6 1694-703 2484340 Goedert M, Spillantini MG, Jakes R, Rutherford D, Crowther RA 1989 Neuron 3 4 519-526 7929085 Schweers O, Schonbrunn-Hanebeck E, Marx A, Mandelkow E 1994 J Biol Chem 269 39 24290-24297 This the microtubule binding domain. Disordered - Extended 369 441 KKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL Engineered Isoform Relationship to function unknown Molecular assembly Protein-protein binding Rotory shadowing electron microscopy Stability at thermal extremes Paper 2484340 Goedert M, Spillantini MG, Jakes R, Rutherford D, Crowther RA 1989 Neuron 3 4 519-526 15147841 Santarella RA, Skiniotis G, Goldie KN, Tittmann P, Gross H, Mandelkow EM, Mandelkow E, Hoenger A 2004 J Mol Biol 339 3 539-553 7929085 Schweers O, Schonbrunn-Hanebeck E, Marx A, Mandelkow E 1994 J Biol Chem 269 39 24290-24297 Disordered - Extended 370 441 KIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL Engineered Isoform Function arises via a disorder to order transition Molecular assembly Protein-protein binding Circular dichroism (CD) spectroscopy, near-UV 295 7 Rotory shadowing electron microscopy Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) Small-angle X-ray scattering (SAXS) Stability at thermal extremes Paper 14769047 Barghorn S, Davies P, Mandelkow E 2004 Biochemistry 43 6 1694-703 2484340 Goedert M, Spillantini MG, Jakes R, Rutherford D, Crowther RA 1989 Neuron 3 4 519-526 7929085 Schweers O, Schonbrunn-Hanebeck E, Marx A, Mandelkow E 1994 J Biol Chem 269 39 24290-24297 Disordered K19 244 372 QTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIE Fragment Function arises via a disorder to order transition Molecular assembly Protein-protein binding Nuclear magnetic resonance (NMR) 283 7.4 H2O/D2O 90%/10% Na2HPO4 10 NaCl 100 Paper 15654759 Eliezer D, Barre P, Kobaslija M, Chan D, Li X, Heend L 2005 Biochemistry 44 3 1026-36 PHF-tau is generally found as dimers but can also form larger complexes. Fibronectin binding protein Q06556_STRDY Q06556 Q06556_STRDY 75499704 Streptococcus dysgalactiae 1091 MTNCKYKLRKLSIGLVSVGTMFMAAPVMGEDASQPTASVTTESPAIQTEEDQGSQAEALEEPTPAPQTSPSTVSAVPAEAAAMADEKGIAEAPAHEPAPKASVQAEAASPAGKAEATTNTGQPTNTEQARSRSKRAAEIAPQTIEVEKLEVDKENSSLTVKDGEKDKQLIKHRDGNQRDIFDISRDVKVNQDGTMDVTLTVKPKQIDEGAEVIVLLDTSQKMTETDFNTAKENIKKLVTTLTGTTDKEGKNVSHYNNRNSVRLIDFYRKVGESTDLSGWDAKKIDEKLNEVWKKAKDDYNGWGVDLQGAIHKAREIFNLDKEKRSGKRQHIVLFSQGESTFSYDIKDKSKMDKVAVEEPVTYSNPLFPWPFYFDTTTRTHNVVNDAKKLIDFLNKLGISQFNGAVDNVATVGNTLLGLGSFFGLKNPLDYISLADLETSKLNSEKFDYSRRVGEGYNFRSYFDREVDKVGFKKILVEKIKGNLKKFQPKQTDTWLSSLGLNSIKEKIQDWMIDKALDNLFYRRQYQFYNHNLSAQAEARMAREEGIKFYAVDVTEPERIAKEINSQKYSEAYTNHLKKKAEEARELAKKRNEKFDKYLKEMSESQKFFKDVEDPEKFKDILTELKVTETFEEKVSVNNSEQRKSNKEVEYKKASSNSSFLSFIFSSSTNESITWTLSKDKLQKALQSGETLTLEYKLKIHKDKFKLAPQTRSKRSLDTSENKKSVTEKVITSDVKYKINDKEVKGKELDDVSLTYSKETVRKPQVEPNVPDTPQEKPLTPLAPSEPSQPSIPETPLIPSEPSVPETSTPEGPTEGENNLGGQSEEITITEDSQSGMSGQNPGSGNETVVEDTQTSQEDIVLGGPGQVIDFTEDSQPGMSGNNSHTITEDSKPSQEDEVIIGGQGQVIDFTEDTQSGMSGDNSHTDGTVLEEDSKPSQEDEVIIGGQGQVIDFTEDTQTGMSGAGQVESPTITEETHKPEIIMGGQSDPIDMVEDTLPGMSGSNEATVVEEDTRPKLQFHFDNEEPVPATVPTVSQTPIAQVESKVPHAKAESALPQTGDTNKLETFFTITALTVIGAAGLLGKKRRNNQTD Disordered 810 969 EGPTEGENNLGGQSEEITITEDSQSGMSGQNPGSGNETVVEDTQTSQEDIVLGGPGQVIDFTEDSQPGMSGNNSHTITEDSKPSQEDEVIIGGQGQVIDFTEDTQSGMSGDNSHTDGTVLEEDSKPSQEDEVIIGGQGQVIDFTEDTQTGMSGAGQVESP Paper 8576127 House-Pompeo K, Xu Y, Joh D, Speziale P, Hook M 1996 J Biol Chem 271 3 1379-84 Protein transport protein SEC9 SEC9_YEAST Sec9p P40357 SEC9_YEAST 730733 Saccharomyces cerevisiae (Baker's yeast) 651 MGLKKFFKIKPPEEATPEQNKDTLMELGISVKNPSKKRKEKFAAYGKFANDKAEDKVYAPPGYEQYARPQDELEDLNASPLDANANEATAGSNRGSSGTQDLGNGAESNSMQDPYAIENDDYRYDDDPYARFQANKSNGRGSVNAAPYGDYGGGYNGTSLNSYNNDGPYSNQNTSNSWVNANGRNSLNHSNSTLNVGPSRQTRQPPVSTSTNSLSLDQRSPLANPMQEKRNPYADMNSYGGAYDSNTNRSSGTRQGSSKNANPYASMANDSYSNGNLNRSANPYSSRSVRQPQSQQAPMTYTPSFIASDEAARNSEVDLNEEPRTGEFDFEEVYADKSAENRAALDEPDLNAVMTNEDSIDLNASEVDHSSRQQQQQQWFMDEQQQQQQHFNATNNQYGDQRGYKTFEEIQKEEEARQQQEEDEAVDEIKQEIKFTKQSSVASTRNTLKMAQDAERAGMNTLGMLGHQSEQLNNVEGNLDLMKVQNKVADEKVAELKKLNRSILAVHVSNPFNSKRRRREREEQLKNRKIEEKLMREQTSQQLSQSTQRIEGAMNANNNISEVRERYQRKNVLEKAKRYQFENDEEDDEMELEIDRNLDQIQQVSNRLKKMALTTGKELDSQQKRLNNIEESTDDLDINLHMNTNRLAGIR Disordered - Extended 1 651 MGLKKFFKIKPPEEATPEQNKDTLMELGISVKNPSKKRKEKFAAYGKFANDKAEDKVYAPPGYEQYARPQDELEDLNASPLDANANEATAGSNRGSSGTQDLGNGAESNSMQDPYAIENDDYRYDDDPYARFQANKSNGRGSVNAAPYGDYGGGYNGTSLNSYNNDGPYSNQNTSNSWVNANGRNSLNHSNSTLNVGPSRQTRQPPVSTSTNSLSLDQRSPLANPMQEKRNPYADMNSYGGAYDSNTNRSSGTRQGSSKNANPYASMANDSYSNGNLNRSANPYSSRSVRQPQSQQAPMTYTPSFIASDEAARNSEVDLNEEPRTGEFDFEEVYADKSAENRAALDEPDLNAVMTNEDSIDLNASEVDHSSRQQQQQQWFMDEQQQQQQHFNATNNQYGDQRGYKTFEEIQKEEEARQQQEEDEAVDEIKQEIKFTKQSSVASTRNTLKMAQDAERAGMNTLGMLGHQSEQLNNVEGNLDLMKVQNKVADEKVAELKKLNRSILAVHVSNPFNSKRRRREREEQLKNRKIEEKLMREQTSQQLSQSTQRIEGAMNANNNISEVRERYQRKNVLEKAKRYQFENDEEDDEMELEIDRNLDQIQQVSNRLKKMALTTGKELDSQQKRLNNIEESTDDLDINLHMNTNRLAGIR Native Function arises via a disorder to order transition Molecular assembly Protein-protein binding Paper 10048921 Fiebig KM, Rice LM, Pollock E, Brunger AT 1999 Nat Struct Biol 6 2 117-23 Sec9 is completely disordered in isolation, but acquires some structure when forming a complex with Sso1. Disordered 401 651 QRGYKTFEEIQKEEEARQQQEEDEAVDEIKQEIKFTKQSSVASTRNTLKMAQDAERAGMNTLGMLGHQSEQLNNVEGNLDLMKVQNKVADEKVAELKKLNRSILAVHVSNPFNSKRRRREREEQLKNRKIEEKLMREQTSQQLSQSTQRIEGAMNANNNISEVRERYQRKNVLEKAKRYQFENDEEDDEMELEIDRNLDQIQQVSNRLKKMALTTGKELDSQQKRLNNIEESTDDLDINLHMNTNRLAGIR Complex Engineered Fragment Function arises via a disorder to order transition Molecular assembly Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV 298 8.4 phosphate buffer 10 sodium chloride 300 Fluorescent probes 298 8.4 Sncl 2.5 sodium chloride 300 sodium phosphate 10 SDS-PAGE gel, Aberrant mobility on Paper 9326367 Rice LM, Brennwald P, Brunger AT 1997 FEBS Lett 415 1 49-55 Transcription factor p65 TF65_MOUSE Nuclear factor NF-kappa-B p65 subunit Q04207 Mm.249966 TF65_MOUSE 417926 Mus musculus (Mouse) 549 MDDLFPLIFPSEPAQASGPYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINGYTGPGTVRISLVTKDPPHRPHPHELVGKDCRDGYYEADLCPDRSIHSFQNLGIQCVKKRDLEQAISQRIQTNNNPFHVPIEEQRGDYDLNAVRLCFQVTVRDPAGRPLLLTPVLSHPIFDNRAPNTAELKICRVNRNSGSCLGGDEIFLLCDKVQKEDIEVYFTGPGWEARGSFSQADVHRQVAIVFRTPPYADPSLQAPVRVSMQLRRPSDRELSEPMEFQYLPDTDDRHRIEEKRKRTYETFKSIMKKSPFNGPTEPRPPTRRIAVPTRNSTSVPKPAPQPYTFPASLSTINFDEFSPMLLPSGQISNQALALAPSSAPVLAQTMVPSSAMVPLAQPPAPAPVLTPGPPQSLSAPVPKSTQAGEGTLSEALLHLQFDADEDLGALLGNSTDPGVFTDLASVDNSEFQQLLNQGVSMSHSTAEPMLMEYPEAITRLVTGSQRPPDPAPTPLGTSGLPNGLSGDEDFSSIADMDFSALLSQISS Disordered 321 326 PTEPRP Complex Engineered Fragment 1K3ZA Relationship to function unknown Unknown Unknown X-ray crystallography Paper 12686541 Malek S, Huang DB, Huxford T, Ghosh S, Ghosh G 2003 J Biol Chem 278 25 23094-100 Disordered 309 326 FKSIMKKSPFNGPTEPRP Complex Engineered Fragment 1K3ZB Relationship to function unknown Unknown Unknown X-ray crystallography Paper 12686541 Malek S, Huang DB, Huxford T, Ghosh S, Ghosh G 2003 J Biol Chem 278 25 23094-100 Disordered 19 304 PYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINGYTGPGTVRISLVTKDPPHRPHPHELVGKDCRDGYYEADLCPDRSIHSFQNLGIQCVKKRDLEQAISQRIQTNNNPFHVPIEEQRGDYDLNAVRLCFQVTVRDPAGRPLLLTPVLSHPIFDNRAPNTAELKICRVNRNSGSCLGGDEIFLLCDKVQKEDIEVYFTGPGWEARGSFSQADVHRQVAIVFRTPPYADPSLQAPVRVSMQLRRPSDRELSEPMEFQYLPDTDDRHRIEEKRKR Fragment Native 1IKNA Relationship to function unknown Molecular recognition effectors Nuclear localization Paper 9384558 Huang DB, Huxford T, Chen YQ, Ghosh G 1997 Structure 5 11 1427-36 Small proline-rich protein 2E SPR2E_HUMAN SPR-2E Small proline-rich protein II SPR-II P22531 Hs.568518 SPR2E_HUMAN 45644952 Homo sapiens (Human) 72 MSYQQQQCKQPCQPPPVCPTPKCPEPCPPPKCPEPCPPPKCPQPSPPQQCQQKCPPVTPSPPCQPKCPPKSK Disordered - Extended 1 20 MSYQQQQCKQPCQPPPVCPT Native Function arises via a disorder to order transition Molecular assembly Protein-protein binding SDS-PAGE gel, Aberrant mobility on 310 TGase 1 or 3 trypsin Circular dichroism (CD) spectroscopy, near-UV Phosphate Buffer Sensitivity to proteolysis 310 TGase 1 or 3 trypsin Stability at thermal extremes 293 Paper 3133554 Kartasova T, van de Putte P 1988 Mol Cell Biol 8 5 2195-2203 9722562 Tarcsa E, Candi E, Kartasova T, Idler WW, Marekov LN, Steinert PM 1998 J Biol Chem 273 36 23297-23303 Disordered - Extended 48 72 QQCQQKCPPVTPSPPCQPKCPPKSK Native Function arises via a disorder to order transition Molecular assembly Protein-protein binding SDS-PAGE gel, Aberrant mobility on 310 TGase 1 or 3 trypsin Circular dichroism (CD) spectroscopy, near-UV 293 Phosphate Buffer Sensitivity to proteolysis 310 TGase 1 or 2 trypsin Stability at thermal extremes 293 Paper 3133554 Kartasova T, van de Putte P 1988 Mol Cell Biol 8 5 2195-2203 9722562 Tarcsa E, Candi E, Kartasova T, Idler WW, Marekov LN, Steinert PM 1998 J Biol Chem 273 36 23297-23303 Tropomodulin Q91006_CHICK Tropomodulin 1 TMOD1 Q91006 Gga.2614 Q91006_CHICK 75570324 Gallus gallus (Chicken) 359 MSYRKELEKYRDLDEDKILGALTEEELRKLENELEELDPDNALLPAGLRQRDQTQKPPTGPFKREELMAHLEQQAKDIKDREDLVPFTGEKRGKAWIPKQKPMDPVLESVTLEPELEEALANASDAELCDIAAILGMHTLMSNQQYYEALGSSTIVNKEGLNSVIKPTKYKPVPDEEPNSTDVEETLKRIQNNDPDLEEVNLNNIMNIPVPTLKALAEALKTNTYVKKFSIVGTRSNDPVAFALAEMLKVNNTLKSLNVESNFISGSGILALVEALQSNTSLIELRIDNQSQPLGNNVEMEIANMLEKNTTLLKFGYHFTQQGPRLRASNAMMNNNDLVRKRRLAELNGPIFPKCRTGV Disordered N-terminal capping domain 1 92 MSYRKELEKYRDLDEDKILGALTEEELRKLENELEELDPDNALLPAGLRQRDQTQKPPTGPFKREELMAHLEQQAKDIKDREDLVPFTGEKR Fragment Function arises via a disorder to order transition Molecular assembly Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV 6.5 100 mM NaCl, 10 mM sodium phosphate 5 to 20 microM peptide Nuclear magnetic resonance (NMR) 283 6.5 0.8 mM 13C15N labeled peptide 100 mM NaCl, 10 mM sodium phosphate, 5% D2O 1.1 mM 15N labeled peptide Paper 11423419 Kostyukova AS, Tiktopulo EI, Maeda Y. 2001 Biophys J 81 1 345-51 15475586 Greenfield NJ, Kostyukova AS, Hitchcock-DeGregori SE. 2005 Biophys J 88 1 372-83 Calsequestrin-1 CASQ1_RABIT Calsequestrin, skeletal muscle isoform Aspartactin Laminin-binding protein P07221 Ocu.6275 CASQ1_RABIT 115537 Oryctolagus cuniculus (Rabbit) 395 MNAADRMGARVALLLLLVLGSPQSGVHGEEGLDFPEYDGVDRVINVNAKNYKNVFKKYEVLALLYHEPPEDDKASQRQFEMEELILELAAQVLEDKGVGFGLVDSEKDAAVAKKLGLTEEDSIYVFKEDEVIEYDGEFSADTLVEFLLDVLEDPVELIEGERELQAFENIEDEIKLIGYFKNKDSEHYKAFKEAAEEFHPYIPFFATFDSKVAKKLTLKLNEIDFYEAFMEEPVTIPDKPNSEEEIVNFVEEHRRSTLRKLKPESMYETWEDDMDGIHIVAFAEEADPDGYEFLEILKSVAQDNTDNPDLSIIWIDPDDFPLLVPYWEKTFDIDLSAPQIGVVNVTDADSVWMEMDDEEDLPSAEELEDWLEDVLEGEINTEDDDDEDDDDDDDD Disordered - Extended 1 395 MNAADRMGARVALLLLLVLGSPQSGVHGEEGLDFPEYDGVDRVINVNAKNYKNVFKKYEVLALLYHEPPEDDKASQRQFEMEELILELAAQVLEDKGVGFGLVDSEKDAAVAKKLGLTEEDSIYVFKEDEVIEYDGEFSADTLVEFLLDVLEDPVELIEGERELQAFENIEDEIKLIGYFKNKDSEHYKAFKEAAEEFHPYIPFFATFDSKVAKKLTLKLNEIDFYEAFMEEPVTIPDKPNSEEEIVNFVEEHRRSTLRKLKPESMYETWEDDMDGIHIVAFAEEADPDGYEFLEILKSVAQDNTDNPDLSIIWIDPDDFPLLVPYWEKTFDIDLSAPQIGVVNVTDADSVWMEMDDEEDLPSAEELEDWLEDVLEGEINTEDDDDEDDDDDDDD Isoform Native Function arises via a disorder to order transition Molecular assembly Substrate/ligand binding Protein-protein binding Circular dichroism (CD) spectroscopy, near-UV 7.5 Nuclear magnetic resonance (NMR) 278 7.5 Analytical ultracentrifugation SDS-PAGE gel, Aberrant mobility on 7.5 Paper 4472093 Ostwald TJ, MacLennan DH, Dorrington KJ 1974 J Biol Chem 249 18 5867-71 6725251 Cozens B, Reithmeier RA 1984 J Biol Chem 259 10 6248-52 6480588 Aaron BM, Oikawa K, Reithmeier RA, Sykes BD 1984 J Biol Chem 259 19 11876-81 Disordered 1 4 MNAA Isoform Native 1A8YA Function arises via a disorder to order transition Unknown Protein-protein binding Substrate/ligand binding X-ray crystallography 277 6.5 Paper 9628486 Wang S, Trumble WR, Liao H, Wesson CR, Dunker AK, Kang CH 1998 Nat Struct Biol 5 6 476-83 Disordered 328 333 EKTFDI Isoform Native 1A8YA Function arises via a disorder to order transition Unknown Substrate/ligand binding Protein-protein binding X-ray crystallography 277 6.5 Paper 9628486 Wang S, Trumble WR, Liao H, Wesson CR, Dunker AK, Kang CH 1998 Nat Struct Biol 5 6 476-83 Disordered 352 367 WMEMDDEEDLPSAEEL Isoform Native 1A8YA Function arises via a disorder to order transition Unknown Substrate/ligand binding Protein-protein binding X-ray crystallography 277 6.5 Paper 9628486 Wang S, Trumble WR, Liao H, Wesson CR, Dunker AK, Kang CH 1998 Nat Struct Biol 5 6 476-83 Phosphoprotein PHOSP_MEASE Protein P P03422 PHOSP_MEASE 133668 Measles virus (strain Edmonston) (Subacute sclerose panencephalitis virus) 507 MAEEQARHVKNGLECIRALKAEPIGSLAIEEAMAAWSEISDNPGQERATCREEKAGSSGLSKPCLSAIGSTEGGAPRIRGQGPGESDDDAETLGIPPRNLQASSTGLQCYYVYDHSGEAVKGIQDADSIMVQSGLDGDSTLSGGDNESENSDVDIGEPDTEGYAITDRGSAPISMGFRASDVETAEGGEIHELLRLQSRGNNFPKLGKTLNVPPPPDPGRASTSGTPIKKGTERRLASFGTEIASLLTGGATQCARKSPSEPSGPGAPAGNVPECVSNAALIQEWTPESGTTISPRSQNNEEGGDYYDDELFSDVQDIKTALAKIHEDNQKIISKLESLLLLKGEVESIKKQINRQNISISTLEGHLSSIMIAIPGLGKDPNDPTADVEINPDLKPIIGRDSGRALAEVLKKPVASRQLQGMTNGRTSSRGQLLKEFQLKPIGKKMSSAVGFVPDTGPASRSVIRSIIKSSRLEEDRKRYLMTLLDDIKGANDLAKFHQMLMKIIMK Disordered PNT 1 230 MAEEQARHVKNGLECIRALKAEPIGSLAIEEAMAAWSEISDNPGQERATCREEKAGSSGLSKPCLSAIGSTEGGAPRIRGQGPGESDDDAETLGIPPRNLQASSTGLQCYYVYDHSGEAVKGIQDADSIMVQSGLDGDSTLSGGDNESENSDVDIGEPDTEGYAITDRGSAPISMGFRASDVETAEGGEIHELLRLQSRGNNFPKLGKTLNVPPPPDPGRASTSGTPIKK Engineered Fragment Native Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV 293 7 10 mM sodium phosphate buffer 1-mm-thick quartz cells Sensitivity to proteolysis 298 7.8 1 mg/ml protein in 20 mM Tris/HCl Horse heart cytochrome c (type VI) and thermolysin protease:protein substrate ratio 1:100 Dynamic light scattering 293 8 1 mg/ml protein in 100 mM NaCl Size exclusion/gel filtration chromatography 7 100 mM NaCl 50 mM sodium phosphate buffer Superdex 200 column Nuclear magnetic resonance (NMR) 300 5.6 0.3 mM protein 30 mM NaCl 50 mM sodium acetate Paper 12069524 Karlin D, Longhi S, Receveur V, Canard B. 2002 Virology 296 2 251-62 Additional reference regarding the modular organization of DP133 'Protein P': Karlin et al., J Gen Virol. 2003 Dec;84(Pt 12):3239-52., PMID 14645906. Disordered linker 376 458 GLGKDPNDPTADVEINPDLKPIIGRDSGRALAEVLKKPVASRQLQGMTNGRTSSRGQLLKEFQLKPIGKKMSSAVGFVPDTGP Native Function arises from the disordered state Entropic chain Flexible linkers/spacers Sensitivity to proteolysis Paper Additional reference regarding the modular organization of DP133 'Protein P': Karlin et al., J Gen Virol. 2003 Dec;84(Pt 12):3239-52., PMID 14645906. The main reference for Region 3: Longhi et al. (2003) PMID 12621042. See overall References section below for complete record. Disordered Flexible loop of the nucleocapsid-binding domain (XD) 489 491 KGA Fragment Monomeric 1OKSA 1T6OA 2K9DA Function arises from the disordered state Entropic chain Flexible linkers/spacers Nuclear magnetic resonance (NMR) 300 8 1.6mM in 10mM sodium phosphate, 10%D(2)O Paper 12944395 Johansson K, Bourhis JM, Campanacci V, Cambillau C, Canard B, Longhi S 2003 J Biol Chem 278 45 44567-73 20058326 Gely S, Lowry DF, Bernard C, Jensen MR, Blackledge M, Costanzo S, Bourhis JM, Darbon H, Daughdrill G, Longhi S 2010 J Mol Recognit This flexible loop is part of an ordered domain, the extreme C-terminal domain (XD) (aa 459-507). XD also serves as the nucleocapsid-binding domain. The 3D solution structure of XD consists of three alpha helices (aa 462-470, 475-487 and 492-505), a turn between helices 1 and 2 (aa 471-474) and a highly dynamic flexible turn (aa 488-491). Additional reference regarding the modular organization of DP133 'Protein P': Karlin et al., J Gen Virol. 2003 Dec;84(Pt 12):3239-52., PMID 14645906. Additional references for Protein P (DP00133) and Protein N (DP00160): Belle et al. Proteins. 2008 Dec;73(4):973-88. PMID: 18536007; Bernard et al. FEBS Lett. 2009 Apr 2;583(7):1084-9. Epub 2009 Mar 9. PMID: 19275899; Couturier et al. J Mol Recognit. 2010 May;23(3):301-15. PMID: 19718689; Kavalenka et al. Biophys J. 2010 Mar 17;98(6):1055-64. PMID: 20303863; Longhi, Oglesbee. Protein Pept Lett. 2010;17(8):961-78. PMID: 20450481; Longhi. Curr Top Microbiol Immunol. 2009;329:103-28. Review. PMID: 19198564; Morin et al. J Phys Chem B. 2006 Oct 19;110(41):20596-608. PMID: 17034249. Sent for [AV Longhi S.] Fragile X mental retardation 1 protein FMR1_HUMAN Protein FMR-1 FMRP Q06787 Hs.103183 FMR1_HUMAN 544328 Homo sapiens (Human) 632 MEELVVEVRGSNGAFYKAFVKDVHEDSITVAFENNWQPDRQIPFHDVRFPPPVGYNKDINESDEVEVYSRANEKEPCCWWLAKVRMIKGEFYVIEYAACDATYNEIVTIERLRSVNPNKPATKDTFHKIKLDVPEDLRQMCAKEAAHKDFKKAVGAFSVTYDPENYQLVILSINEVTSKRAHMLIDMHFRSLRTKLSLIMRNEEASKQLESSRQLASRFHEQFIVREDLMGLAIGTHGANIQQARKVPGVTAIDLDEDTCTFHIYGEDQDAVKKARSFLEFAEDVIQVPRNLVGKVIGKNGKLIQEIVDKSGVVRVRIEAENEKNVPQEEEIMPPNSLPSNNSRVGPNAPEEKKHLDIKENSTHFSQPNSTKVQRVLVASSVVAGESQKPELKAWQGMVPFVFVGTKDSIANATVLLDYHLNYLKEVDQLRLERLQIDEQLRQIGASSRPPPNRTDKEKSYVTDDGQGMGRGSRPYRNRGHGRRGPGYTSGTNSEASNASETESDHRDELSDWSLAPTEEERESFLRRGDGRRRGGGGRGQGGRGRGGGFKGNDDHSRTDNRPRNPREAKGRTTDGSLQIRVDCNNERSVHTKTLQNTSSEGSRLRTGKDRNQKKEKPDSVDGQQPLVNGVP Disordered KH2 domain 281 422 FAEDVIQVPRNLVGKVIGKNGKLIQEIVDKSGVVRVRIEAENEKNVPQEEEIMPPNSLPSNNSRVGPNAPEEKKHLDIKENSTHFSQPNSTKVQRVLVASSVVAGESQKPELKAWQGMVPFVFVGTKDSIANATVLLDYHLN Fragment Function arises via an order to disorder transition Protein-mRNA binding Circular dichroism (CD) spectroscopy, far-UV 298 0.1 cm pathlength 17 microM protein Nuclear magnetic resonance (NMR) 300 0.5–1.0 mM samples in 90% H2O/10% D2O Paper 10496225 Adinolfi S, Bagni C, Musco G, Gibson T, Mazzarella L, Pastore A 1999 RNA 5 9 1248-58 Disordered FCT domain 516 632 APTEEERESFLRRGDGRRRGGGGRGQGGRGRGGGFKGNDDHSRTDNRPRNPREAKGRTTDGSLQIRVDCNNERSVHTKTLQNTSSEGSRLRTGKDRNQKKEKPDSVDGQQPLVNGVP Fragment Function arises from the disordered state Protein-mRNA binding Circular dichroism (CD) spectroscopy, far-UV 298 10 microM protein Paper 10496225 Adinolfi S, Bagni C, Musco G, Gibson T, Mazzarella L, Pastore A 1999 RNA 5 9 1248-58 Heat shock factor protein HSF_YEAST HSF Heat shock transcription factor HSTF P10961 HSF_YEAST 123687 Saccharomyces cerevisiae (Baker's yeast) 833 MNNAANTGTTNESNVSDAPRIEPLPSLNDDDIEKILQPNDIFTTDRTDASTTSSTAIEDIINPSLDPQSAASPVPSSSFFHDSRKPSTSTHLVRRGTPLGIYQTNLYGHNSRENTNPNSTLLSSKLLAHPPVPYGQNPDLLQHAVYRAQPSSGTTNAQPRQTTRRYQSHKSRPAFVNKLWSMLNDDSNTKLIQWAEDGKSFIVTNREEFVHQILPKYFKHSNFASFVRQLNMYGWHKVQDVKSGSIQSSSDDKWQFENENFIRGREDLLEKIIRQKGSSNNHNSPSGNGNPANGSNIPLDNAAGSNNSNNNISSSNSFFNNGHLLQGKTLRLMNEANLGDKNDVTAILGELEQIKYNQIAISKDLLRINKDNELLWQENMMARERHRTQQQALEKMFRFLTSIVPHLDPKMIMDGLGDPKVNNEKLNSANNIGLNRDNTGTIDELKSNDSFINDDRNSFTNATTNARNNMSPNNDDNSIDTASTNTTNRKKNIDENIKNNNDIINDIIFNTNLANNLSNYNSNNNAGSPIRPYKQRYLLKNRANSSTSSENPSLTPFDIESNNDRKISEIPFDDEEEEETDFRPFTSRDPNNQTSENTFDPNRFTMLSDDDLKKDSHTNDNKHNESDLFWDNVHRNIDEQDARLQNLENMVHILSPGYPNKSFNNKTSSTNTNSNMESAVNVNSPGFNLQDYLTGESNSPNSVHSVPSNGSGSTPLPMPNDNDTEHASTSVNQGENGSGLTPFLTVDDHTLNDNNTSEGSTRVSPDIKFSATENTKVSDNLPSFNDHSYSTQADTAPENAKKRFVEEIPEPAIVEIQDPTEYNDHRLPKRAKK Disordered N-terminal activation domain 1 167 MNNAANTGTTNESNVSDAPRIEPLPSLNDDDIEKILQPNDIFTTDRTDASTTSSTAIEDIINPSLDPQSAASPVPSSSFFHDSRKPSTSTHLVRRGTPLGIYQTNLYGHNSRENTNPNSTLLSSKLLAHPPVPYGQNPDLLQHAVYRAQPSSGTTNAQPRQTTRRYQ Native Function arises from the disordered state Modification site Transactivation (transcriptional activation) Nuclear magnetic resonance (NMR) heteronuclear NOE spectrum pH 3.4 and 5.75 Circular dichroism (CD) spectroscopy, far-UV 298 7 1 mg/mL protein solutions in 25 mM sodium phosphate buffer Paper 8745404 Cho HS, Liu CW, Damberger FF, Pelton JG, Nelson HC, Wemmer DE 1996 Protein Sci 5 2 262-9 Histone H1.2 H12_RAT H1d P15865 Rn.196361 H12_RAT 1170152 Rattus norvegicus (Rat) 217 MSETAPAAPAAPAPAEKTPIKKKARKAAGGAKRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPKAKKAGAAKAKKPAGAAKKPKKATGTATPKKSTKKTPKKAKKPAAGAKKAKSPKKAKATKAKKAPKSPAKARAVKPKAAKPKTSKPKAAKPKKTAAKKK Disordered - Extended 1 30 MSETAPAAPAAPAPAEKTPIKKKARKAAGG Complex Engineered Function arises via a disorder to order transition Molecular assembly Protein-DNA binding Protein-protein binding Circular dichroism (CD) spectroscopy, near-UV 7.5 Paper 9109385 Tarkka T, Oikarinen J, Grundstrom T 1997 FEBS Lett 406 1-2 56-60 2373370 Cole KD, Kandala JC, Kremer E, Kistler WS 1990 Gene 89 2 265-9 Disordered - Molten Globule 31 119 AKRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPK Complex Engineered Function arises via a molten globule to order transition Molecular assembly Protein-DNA binding Protein-protein binding Circular dichroism (CD) spectroscopy, near-UV 7.5 Paper 9109385 Tarkka T, Oikarinen J, Grundstrom T 1997 FEBS Lett 406 1-2 56-60 2373370 Cole KD, Kandala JC, Kremer E, Kistler WS 1990 Gene 89 2 265-9 Disordered - Extended 120 217 AKKAGAAKAKKPAGAAKKPKKATGTATPKKSTKKTPKKAKKPAAGAKKAKSPKKAKATKAKKAPKSPAKARAVKPKAAKPKTSKPKAAKPKKTAAKKK Complex Engineered Function arises via a disorder to order transition Molecular assembly Protein-DNA binding Protein-protein binding Circular dichroism (CD) spectroscopy, near-UV 7.5 Paper 9109385 Tarkka T, Oikarinen J, Grundstrom T 1997 FEBS Lett 406 1-2 56-60 2373370 Cole KD, Kandala JC, Kremer E, Kistler WS 1990 Gene 89 2 265-9 Hirudin variant-1 HIRV1_HIRME Hirudin-1 Hirudin-I Lepirudin P01050 HIRV1_HIRME 124981 Hirudo medicinalis (Medicinal leech) 65 VVYTDCTESGQNLCLCEGSNVCGQGNKCILGSDGEKNQCVTGEGTPKPQSHNDGDFEEIPEEYLQ Disordered - Extended C-Terminal Tail 50 65 SHNDGDFEEIPEEYLQ Native 1HRTA 2HIRA 5HIRA Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 300 H20 D20 Paper 2567183 Folkers PJ, Clore GM, Driscoll PC, Dodt J, Kohler S, Gronenborn AM 1989 Biochemistry 28 6 2601-17 3013692 Dodt J, Schmitz T, Schafer T, Bergmann C 1986 FEBS Lett 202 2 373-7 Parathyroid hormone-related protein PTHR_HUMAN PTH-rP PTHrP PTHrP[1-36][cleavage product 1] PTHrP[38-94][cleavage product 2] Osteostatin [cleavage product 3] PTHrP[107-139] P12272 Hs.591159 PTHR_HUMAN 131542 Homo sapiens (Human) 177 MQRRLVQQWSVAVFLLSYAVPSCGRSVEGLSRRLKRAVSEHQLLHDKGKSIQDLRRRFFLHHLIAEIHTAEIRATSEVSPNSKPSPNTKNHPVRFGSDDEGRYLTQETNKVETYKEQPLKTPGKKKKGKPGKRKEQEKKKRRTRSAWLDSGVTGSGLEGDHLSDTSTTSLELDSRRH Disordered - Extended 1 4 MQRR Engineered Fragment Relationship to function unknown Molecular assembly Molecular recognition effectors Substrate/ligand binding Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV 298 5.1 Nuclear magnetic resonance (NMR) 277 5.1 Paper 10050767 Weidler M, Marx UC, Seidel G, Schafer W, Hoffmann E, Esswein A, Rosch P 1999 FEBS Lett 444 2-3 239-244 8138348 Willis KJ 1994 Int J Pept Protein Res 43 1 23-28 Disordered - Extended 9 15 WSVAVFL Engineered Fragment Function arises via a disorder to order transition Molecular assembly Entropic chain Flexible linkers/spacers Circular dichroism (CD) spectroscopy, far-UV 298 5.1 Nuclear magnetic resonance (NMR) 277 5.1 Paper 10050767 Weidler M, Marx UC, Seidel G, Schafer W, Hoffmann E, Esswein A, Rosch P 1999 FEBS Lett 444 2-3 239-244 8138348 Willis KJ 1994 Int J Pept Protein Res 43 1 23-28 Disordered - Extended 28 34 EGLSRRL Engineered Fragment Relationship to function unknown Molecular recognition effectors Molecular assembly Substrate/ligand binding Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV 298 5.1 Nuclear magnetic resonance (NMR) 277 5.1 Paper 10050767 Weidler M, Marx UC, Seidel G, Schafer W, Hoffmann E, Esswein A, Rosch P 1999 FEBS Lett 444 2-3 239-244 8138348 Willis KJ 1994 Int J Pept Protein Res 43 1 23-28 Disordered regions are not associated with any of the cleavage products. 50S ribosomal protein L27 RL27_ECOLI P0A7L8 RL27_ECOLI 67472010 Escherichia coli 85 MAHKKAGGSTRNGRDSEAKRLGVKRFGGESVLAGSIIVRQRGTKFHAGANVGCGRDHTLFAKADGKVKFEVKGPKNRKFISIEAE Disordered 1 85 MAHKKAGGSTRNGRDSEAKRLGVKRFGGESVLAGSIIVRQRGTKFHAGANVGCGRDHTLFAKADGKVKFEVKGPKNRKFISIEAE Native Relationship to function unknown Molecular assembly Protein-protein binding Circular dichroism (CD) spectroscopy, near-UV 277 7 beta-mercaptoethanol 1 sodium phosphate 1 Nuclear magnetic resonance (NMR) 293 7 2D heteronuclear NMR M9 medium with 15NH4SO4 supplement beta-mercaptoethanol 1 sodium phosphate 1 Tetramethylsilane phosphate as internal chemical shift standard Nuclear magnetic resonance (NMR) 353 7 2D heteronuclear NMR M9 medium with 15NH4SO4 supplement beta-mercaptoethanol 1 sodium phosphate 1 Tetramethylsilane phosphate as internal chemical shift standard Paper 11673426 Maguire BA, Manuilov AV, Zimmermann RA 2001 J Bacteriol 183 22 6565-72 3297162 Littlechild J, Malcolm A, Paterakis K, Ackermann I, Dijk J 1987 Biochim Biophys Acta 913 2 245-55 Zinc finger FYVE domain-containing protein 9 [Isoform 1] ZFYV9_HUMAN Mothers against decapentaplegic homolog-interacting protein Madh-interacting protein Smad anchor for receptor activation Receptor activation anchor hSARA Novel serine protease NSP O95405-1 Hs.532345 ZFYV9_HUMAN 15214067 Homo sapiens (Human) 1425 MENYFQAEAYNLDKVLDEFEQNEDETVSSTLLDTKWNKILDPPSHRLSFNPTLASVNESAVSNESQPQLKVFSLAHSAPLTTEEEDHCANGQDCNLNPEIATMWIDENAVAEDQLIKRNYSWDDQCSAVEVGEKKCGNLACLPDEKNVLVVAVMHNCDKRTLQNDLQDCNNYNSQSLMDAFSCSLDNENRQTDQFSFSINESTEKDMNSEKQMDPLNRPKTEGRSVNHLCPTSSDSLASVCSPSQLKDDGSIGRDPSMSAITSLTVDSVISSQGTDGCPAVKKQENYIPDEDLTGKISSPRTDLGSPNSFSHMSEGILMKKEPAEESTTEESLRSGLPLLLKPDMPNGSGRNNDCERCSDCLVPNEVRADENEGYEHEETLGTTEFLNMTEHFSESQDMTNWKLTKLNEMNDSQVNEEKEKFLQISQPEDTNGDSGGQCVGLADAGLDLKGTCISESEECDFSTVIDTPAANYLSNGCDSYGMQDPGVSFVPKTLPSKEDSVTEEKEIEESKSECYSNIYEQRGNEATEGSGLLLNSTGDLMKKNYLHNFCSQVPSVLGQSSPKVVASLPSISVPFGGARPKQPSNLKLQIPKPLSDHLQNDFPANSGNNTKNKNDILGKAKLGENSATNVCSPSLGNISNVDTNGEHLESYEAEISTRPCLALAPDSPDNDLRAGQFGISARKPFTTLGEVAPVWVPDSQAPNCMKCEARFTFTKRRHHCRACGKVFCASCCSLKCKLLYMDRKEARVCVICHSVLMNAQAWENMMSASSQSPNPNNPAEYCSTIPPLQQAQASGALSSPPPTVMVPVGVLKHPGAEVAQPREQRRVWFADGILPNGEVADAAKLTMNGTSSAGTLAVSHDPVKPVTTSPLPAETDICLFSGSITQVGSPVGSAMNLIPEDGLPPILISTGVKGDYAVEEKPSQISVMQQLEDGGPDPLVFVLNANLLSMVKIVNYVNRKCWCFTTKGMHAVGQSEIVILLQCLPDEKCLPKDIFNHFVQLYRDALAGNVVSNLGHSFFSQSFLGSKEHGGFLYVTSTYQSLQDLVLPTPPYLFGILIQKWETPWAKVFPIRLMLRLGAEYRLYPCPLFSVRFRKPLFGETGHTIMNLLADFRNYQYTLPVVQGLVVDMEVRKTSIKIPSNRYNEMMKAMNKSNEHVLAGGACFNEKADSHLVCVQNDDGNYQTQAISIHNQPRKVTGASFFVFSGALKSSSGYLAKSSIVEDGVMVQITAENMDSLRQALREMKDFTITCGKADAEEPQEHIHIQWVDDDKNVSKGVVSPIDGKSMETITNVKIFHGSEYKANGKVIRWTEVFFLENDDQHNCLSDPADHSRLTEHVAKAFCLALCPHLKLLKEDGMTKLGLRVTLDSDQVGYQAGSNGQPLPSQYMNDLDSALVPVIHGGACQLSEGPVVMELIFYILENIV Disordered Smad binding domain 765 853 NMMSASSQSPNPNNPAEYCSTIPPLQQAQASGALSSPPPTVMVPVGVLKHPGAEVAQPREQRRVWFADGILPNGEVADAAKLTMNGTSS Native Function arises via a disorder to order transition Molecular assembly Protein-protein binding Nuclear magnetic resonance (NMR) Paper 15231848 Chong PA, Ozdamar B, Wrana JL, Forman-Kay JD 2004 J Biol Chem 279 39 40707-14 Heat shock protein beta-1 HSPB1_MOUSE HspB1 Heat shock 27 kDa protein HSP 27 Growth-related 25 kDa protein P25 HSP25 P14602 Mm.13849 HSPB1_MOUSE 547679 Mus musculus (Mouse) 209 MTERRVPFSLLRSPSWEPFRDWYPAHSRLFDQAFGVPRLPDEWSQWFSAAGWPGYVRPLPAATAEGPAAVTLAAPAFSRALNRQLSSGVSEIRQTADRWRVSLDVNHFAPEELTVKTKEGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTLVSSSLSPEGTLTVEAPLPKAVTQSAEITIPVTFEARAQIGGPEAGKSEQSGAK Disordered C-terminal extension 192 209 RAQIGGPEAGKSEQSGAK Native Function arises from the disordered state Chaperones Nuclear magnetic resonance (NMR) Paper 7649277 Carver JA, Esposito G, Schwedersky G, Gaestel M 1995 FEBS Lett 369 2-3 305-10 50S ribosomal protein L33 RL33_ECOLI P0A7N9 RL33_ECOLI 67472328 Escherichia coli 55 MAKGIREKIKLVSSAGTGHFYTTTKNKRTKPEKLELKKFDPVVRQHVIYKEAKIK Disordered 1 55 MAKGIREKIKLVSSAGTGHFYTTTKNKRTKPEKLELKKFDPVVRQHVIYKEAKIK Paper 3297162 Littlechild J, Malcolm A, Paterakis K, Ackermann I, Dijk J 1987 Biochim Biophys Acta 913 2 245-55 Histone RNA hairpin-binding protein SLBP_DROME Histone stem-loop-binding protein Histone mRNA Binding Protein SLBP Q9VAN6 Dm.4801 SLBP_DROME 9789800 Drosophila melanogaster (Fruit fly) 276 MLCEDQHMSVENTPQKGSGSLNSSASSISIDVKPTMQSWAQEVRAEFGHSDEASSSLNSSAASCGSLAKKETADGNLESKDGEGREMAFEFLDGVNEVKFERLVKEEKLKTPYKRRHSFTPPSNENSRSNSPNSSNSSANGDAAAPKGGNNPHSRNSKKSGNFRAHKEEKRVRHNSYTSSTSSSSSYTEADPAILSRRQKQIDYGKNTAAYERYVEMVPKDERTRDHPRTPNKYGKYSRRAFDGLVKIWRKSLHIYDPPTQARDTAKDSNSDSDSD Disordered N-terminal domain 1 175 MLCEDQHMSVENTPQKGSGSLNSSASSISIDVKPTMQSWAQEVRAEFGHSDEASSSLNSSAASCGSLAKKETADGNLESKDGEGREMAFEFLDGVNEVKFERLVKEEKLKTPYKRRHSFTPPSNENSRSNSPNSSNSSANGDAAAPKGGNNPHSRNSKKSGNFRAHKEEKRVRHN Fragment Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 298 7 2D (15N,1H) HSQC and 3D HNCA 3D (13C, 1H) NOESY-HSQC (mixing time of 100 ms) 3D (15N,1H) NOESY-HSQC (mixing time of 75 ms) 3D HNHA 600 MHz Circular dichroism (CD) spectroscopy, far-UV 298 7 20 mM sodium phosphate 50 microM protein Paper 15260482 Thapar R, Mueller GA, Marzluff WF 2004 43 29 9390-400 The N-terminal domain of SLBP is intrinsically or natively unfolded but it has transient helical structure in four regions. The N-terminal domain of SLBP gives one cross-peak per residue indicating that, although unfolded, the different conformations are in fast exchange on the NMR time scale. 30S ribosomal protein S12 RS12_ECOLI P0A7S3 RS12_ECOLI 62288954 Escherichia coli (strain MRE-600) 124 MATVNQLVRKPRARKVAKSNVPALEACPQKRGVCTRVYTTTPKKPNSALRKVCRVRLTNGFEVTSYIGGEGHNLQEHSVILIRGGRVKDLPGVRYHTVRGALDCSGVKDRKQARSKYGVKRPKA Disordered 1 124 MATVNQLVRKPRARKVAKSNVPALEACPQKRGVCTRVYTTTPKKPNSALRKVCRVRLTNGFEVTSYIGGEGHNLQEHSVILIRGGRVKDLPGVRYHTVRGALDCSGVKDRKQARSKYGVKRPKA Paper 6751823 Venyaminov SY, Gogia ZV 1982 Eur J Biochem 126 2 299-309 30S ribosomal protein S18 RS18_ECOLI P0A7T7 RS18_ECOLI 67472372 Escherichia coli 75 MARYFRRRKFCRFTAEGVQEIDYKDIATLKNYITESGKIVPSRITGTRAKYQRQLARAIKRARYLSLLPYTDRHQ Disordered 1 75 MARYFRRRKFCRFTAEGVQEIDYKDIATLKNYITESGKIVPSRITGTRAKYQRQLARAIKRARYLSLLPYTDRHQ Paper 6751823 Venyaminov SY, Gogia ZV 1982 Eur J Biochem 126 2 299-309 30S ribosomal protein S19 RS19_ECOLI P0A7U3 RS19_ECOLI 62288960 Escherichia coli 92 MPRSLKKGPFIDLHLLKKVEKAVESGDKKPLRTWSRRSTIFPNMIGLTIAVHNGRQHVPVFVTDEMVGHKLGEFAPTRTYRGHAADKKAKKK Disordered 1 92 MPRSLKKGPFIDLHLLKKVEKAVESGDKKPLRTWSRRSTIFPNMIGLTIAVHNGRQHVPVFVTDEMVGHKLGEFAPTRTYRGHAADKKAKKK Paper 6751823 Venyaminov SY, Gogia ZV 1982 Eur J Biochem 126 2 299-309 Gag polyprotein [Isoform Gag polyprotein] GAG_HV1B1 Pr55Gag Matrix protein p17 [cleavage product 1] MA Capsid protein p24 [cleavage product 2] CA Spacer peptide p2 [cleavage product 3] Nucleocapsid protein p7 [cleavage product 4] NC Spacer peptide p1 [cleavage product 5] p6-gag [cleavage product 6] P03347 GAG_HV1B1 120827 Human immunodeficiency virus type 1 (isolate BH10 group M subtype B)(HIV-1) 512 MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEALDKIEEEQNKSKKKAQQAAADTGHSSQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVLAEAMSQVTNTATIMMQRGNFRNQRKMVKCFNCGKEGHTARNCRAPRKKGCWKCGKEGHQMKDCTERQANFLGKIWPSYKGRPGNFLQSRPEPTAPPFLQSRPEPTAPPEESFRSGVETTTPPQKQEPIDKELYPLTSLRSLFGNDPSSQ Previous UniProt ID Q9PY17 was permanently deleted and there was no replacement entry for the protein. The entry DP00148 was modified to include full-length Gag polyprotein (not the same as DP00101, which is a different isolate), which includes the disordered region for nucleocapsid protein p7. A cleavage product entry (DP00148_C004) was added. Previous entry DP00148 has been split into polyprotein (DP00148) and cleavage product (DP00148_C004). Nucleocapsid protein p7 GAG_HV1B1 NC Cleavage product 4 of Gag polyprotein [Isoform Gag polyprotein] P03347 GAG_HV1B1 120827 Human immunodeficiency virus type 1 (isolate BH10 group M subtype B)(HIV-1) 55 MQRGNFRNQRKMVKCFNCGKEGHTARNCRAPRKKGCWKCGKEGHQMKDCTERQAN Disordered - Extended 1 55 MQRGNFRNQRKMVKCFNCGKEGHTARNCRAPRKKGCWKCGKEGHQMKDCTERQAN Native Function arises from the disordered state Chaperones DNA unwinding Protein-tRNA binding Nuclear magnetic resonance (NMR) 293 5.5 100% D20 5.0 mM protein 600 MHz 'H frequency Paper 1304355 Summers MF, Henderson LE, Chance MR, Bess JW Jr, South TL, Blake PR, Sagi I, Perez-Alvarado G, Sowder RC 3rd, Hare DR, et al. 1992 1 5 563-74 1639074 Morellet N, Jullian N, De Rocquigny H, Maigret B, Darlix JL, Roques BP 1992 11 8 3059-65 Previous UniProt ID Q9PY17 was permanently deleted and there was no replacement entry for the protein. The entry DP00148 was modified to include full-length Gag polyprotein (not the same as DP00101, which is a different isolate), which includes the disordered region for nucleocapsid protein p7. A cleavage product entry (DP00148_C004) was added. Previous entry DP00148 has been split into polyprotein (DP00148) and cleavage product (DP00148_C004). Neurofilament light polypeptide NFL_PIG NF-L Neurofilament triplet L protein 68 kDa neurofilament protein P02547 NFL_PIG 143811426 Sus scrofa (Pig) 549 MSSFYSEPYYSTSYKRRYVETPRVHISSVRSGYSTARSAYSSYSAPVSSSLSVRRSYSSSSGLMPSLENLDLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAQLLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLKKVHEEEIAELQAQIQYAQISVEMDVSSKPDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELEDKQNADISAMQDTINKLENELRTTKSEMARYLKEYQDLLNVKMALDIEIAAYRKLLEGEETRLSFTSVGSLTTGYSQSSQVFGRSAYGGLQTSSYLMSTRSFPSYYTSHVQEEQIEVEETIEAAKAEEAKDEPPSEGEAEEEGKEKEEAEAEAEAEEEGAQEEEEAAEKEESEEAKEEEGGEGEQGEETKEAEEEEKKDEGAGEEQATKKKD Disordered - Extended 444 549 TSHVQEEQIEVEETIEAAKAEEAKDEPPSEGEAEEEGKEKEEAEAEAEAEEEGAQEEEEAAEKEESEEAKEEEGGEGEQGEETKEAEEEEKKDEGAGEEQATKKKD Native Function arises from the disordered state Entropic chain Entropic bristle zz IR/FTIR (Duplicate, to be deleted) 277 7.5 Paper 8634266 Heimburg T, Schuenemann J, Weber K, Geisler N 1996 Biochemistry 35 5 1375-82 3920075 Geisler N, Plessmann U, Weber K 1985 FEBS Lett 182 2 475-8 DNA repair protein XRCC4 XRCC4_HUMAN X-ray repair cross-complementing protein 4 Q13426 Hs.567359 XRCC4_HUMAN 44888352 Homo sapiens (Human) 336 MERKISRIHLVSEPSITHFLQVSWEKTLESGFVITLTDGHSAWTGTVSESEISQEADDMAMEKGKYVGELRKALLSGAGPADVYTFNFSKESCYFFFEKNLKDVSFRLGSFNLEKVENPAEVIRELICYCLDTIAENQAKNEHLQKENERLLRDWNDVQGRFEKCVSAKEALETDLYKRFILVLNEKKTKIRSLHNKLLNAAQEREKDIKQEGETAICSEMTADRDPVYDESTDEESENQTDLSGLASAAVSKDDSIISSLDVTDIAPSRKRRQRMQRNLGTEPKMAPQENQLQEKENSRPDSSLPETSKKEHISAENMSLETLRNSSPEDLFDEI Disordered 212 213 EG Engineered Fragment 1IK9A Relationship to function unknown Molecular assembly Protein-DNA binding X-ray crystallography 6 2-(N-morpholino)ethanesulfonic acid 0.1 NaCl buffer 150 PEG 6000 (w/v) 3 protein 100 Tris-HCl pH 8.0 20 xylitol precipitant solution (w/v) 3 Paper 11702069 Sibanda BL, Critchlow SE, Begun J, Pei XY, Jackson SP, Blundell TL, Pellegrini L 2001 Nat Struct Biol 8 12 1015-9 The experiments were conducted using a fragment of Xrcc4 spanning residues 1 - 213. Disordered 77 80 GAGP Engineered Fragment 1IK9A Relationship to function unknown Unknown Unknown X-ray crystallography 6 2-(N-morpholino)ethanesulfonic acid 0.1 NaCl buffer 150 PEG 6000 (w/v) 3 protein 100 Tris-HCl pH 8.0 20 xylitol precipitant solution (w/v) 3 Paper 11702069 Sibanda BL, Critchlow SE, Begun J, Pei XY, Jackson SP, Blundell TL, Pellegrini L 2001 Nat Struct Biol 8 12 1015-9 The experiments were conducted using a fragment of Xrcc4 spanning residues 1 - 213. Disordered 77 82 GAGPAD Engineered Fragment 1IK9B Relationship to function unknown Unknown Unknown X-ray crystallography 6 2-(N-morpholino)ethanesulfonic acid 0.1 NaCl buffer 150 PEG 6000 (w/v) 3 protein 100 Tris-HCl pH 8.0 20 xylitol precipitant solution (w/v) 3 Paper 11702069 Sibanda BL, Critchlow SE, Begun J, Pei XY, Jackson SP, Blundell TL, Pellegrini L 2001 Nat Struct Biol 8 12 1015-9 The experiments were conducted using a fragment of Xrcc4 spanning residues 1 - 213. Disordered 202 213 AQEREKDIKQEG Engineered Fragment 1IK9B Relationship to function unknown Molecular assembly Protein-DNA binding X-ray crystallography 6 2-(N-morpholino)ethanesulfonic acid 0.1 NaCl buffer 150 PEG 6000 (w/v) 3 protein 100 Tris-HCl pH 8.0 20 xylitol precipitant solution (w/v) 3 Paper 11702069 Sibanda BL, Critchlow SE, Begun J, Pei XY, Jackson SP, Blundell TL, Pellegrini L 2001 Nat Struct Biol 8 12 1015-9 The experiments were conducted using a fragment of Xrcc4 spanning residues 1 - 213. Disordered 204 265 EREKDIKQEGETAICSEMTADRDPVYDESTDEESENQTDLSGLASAAVSKDDSIISSLDVTD Fragment 1FU1A Relationship to function unknown Unknown Unknown X-ray crystallography 293 6.5 ammonium sulfate well solution 1.2 DTT well solution 10 magnesium acetate well solution 10 protein per mL 8 sodium cacodylate well solution 100 Paper 11080143 Junop MS, Modesti M, Guarne A, Ghirlando R, Gellert M, Yang W 2000 Embo J 19 22 5962-70 The experiments were conducted using a fragment of Xrcc4 spanning residues 1 - 265. Disordered - Extended 179 203 RFILVLNEKKTKIRSLHNKLLNAAQ Fragment 1FU1A Function arises via a disorder to order transition Molecular assembly Protein-DNA binding X-ray crystallography 293 6.5 ammonium sulfate well solution 1.2 DTT well solution 10 magnesium acetate well solution 10 protein per mL 8 sodium cacodylate well solution 100 Paper 11080143 Junop MS, Modesti M, Guarne A, Ghirlando R, Gellert M, Yang W 2000 Embo J 19 22 5962-70 This region is disordered in the S subunit. The experiments were conducted using a fragment of Xrcc4 spanning residues 1 - 213. GTPase HRas RASH_HUMAN Transforming protein p21 p21ras H-Ras-1 c-H-ras Ha-Ras GTPase HRas, N-terminally processed [cleavage product 1] P01112 Hs.37003 RASH_HUMAN 131869 Homo sapiens (Human) 189 MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPGCMSCKCVLS Disordered - Extended 10 13 GAGG Complex Engineered Fragment Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Nuclear magnetic resonance (NMR) 5.5 1H2O 90 2H2O 10 Na2HPO4-NaH2PO4 20 NaCl 150 MgCl2 10 Paper 9230043 Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T 1997 Biochemistry 36 30 9109-9119 Disordered - Extended 10 16 GAGGVGK Complex Engineered Fragment Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Nuclear magnetic resonance (NMR) 5.5 1H2O 90 2H2O 10 MgCl2 10 Na2HPO4-NaH2PO4 20 NaCl 150 Paper 9230043 Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T 1997 Biochemistry 36 30 9109-9119 Disordered 21 21 I Complex Engineered Fragment Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Nuclear magnetic resonance (NMR) 5.5 1H2O 90 2H2O 10 Na2HPO4-NaH2PO4 20 NaCl 150 MgCl2 10 Paper 9230043 Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T 1997 Biochemistry 36 30 9109-9119 Disordered 27 32 HFVDEY Complex Engineered Fragment Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Nuclear magnetic resonance (NMR) 5.5 1H2O 90 2H2O 10 Na2HPO4-NaH2PO4 20 NaCl 150 MgCl2 10 Nuclear magnetic resonance (NMR) 303 D2O 10 DTT 5 GDP 30 H2O 90 MgCl2 5 NaCl 40 sodium azide 0.01 Tris-maleate-d15 pH 6.5 20 Nuclear magnetic resonance (NMR) 303 D2O 100 DTT 5 GDP 30 MgCl2 5 NaCl 40 sodium azide 0.01 Tris-maleate-d15 pH 6.5 20 Paper 9230043 Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T 1997 Biochemistry 36 30 9109-9119 8142349 Kraulis PJ, Domaille PJ, Campbell-Burk SL, Van Aken T, Laue ED 1994 Biochemistry 33 12 3515-3531 Disordered 30 38 DEYDPTIED Complex Engineered Fragment 1CRPA 1CRQA 1CRRA 1Q21A Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 303 6.5 H2O 90 D2O 10 Tris-maleate-d15 20 NaCl 40 MgCl2 5 DTT 5 sodium azide 0.01 GDP 30 Nuclear magnetic resonance (NMR) 303 6.5 D2O 100 DTT 5 GDP 30 MgCl2 5 NaCl 40 sodium azide 0.01 Tris-maleate-d15 20 X-ray crystallography Paper 8142349 Kraulis PJ, Domaille PJ, Campbell-Burk SL, Van Aken T, Laue ED 1994 Biochemistry 33 12 3515-3531 2406906 Milburn MV, Tong L, deVos AM, Brunger A, Yamaizumi Z, Nishimura S, Kim SH 1990 Science 247 4945 939-945 Disordered 31 39 EYDPTIEDS Complex Engineered Fragment 1AA9A Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Nuclear magnetic resonance (NMR) 5.5 1H2O 90 2H2O 10 MgCl2 10 Na2HPO4-NaH2PO4 20 NaCl 150 Paper 9230043 Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T 1997 Biochemistry 36 30 9109-9119 Disordered 32 38 YDPTIED Complex Engineered Fragment Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding X-ray crystallography 298 1,6-hexanediol 60 2,2,2-trifluoroethanol 50 isopropanol 50 Paper 12842038 Buhrman G, de Serrano V, Mattos C 2003 Structure 11 7 747-51 Disordered 32 40 YDPTIEDSY Complex Engineered Fragment Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Nuclear magnetic resonance (NMR) 5.5 1H2O 90 2H2O 10 MgCl2 10 Na2HPO4-NaH2PO4 20 NaCl 150 Paper 9230043 Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T 1997 Biochemistry 36 30 9109-9119 Disordered 57 61 DTAGQ Complex Engineered Fragment Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Nuclear magnetic resonance (NMR) 5.5 1H2O 90 2H2O 10 MgCl2 10 Na2HPO4-NaH2PO4 20 NaCl 150 Paper 9230043 Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T 1997 Biochemistry 36 30 9109-9119 Disordered 57 64 DTAGQEEY Complex Engineered Fragment 1AA9A 1IOZA Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Nuclear magnetic resonance (NMR) 5.5 1H2O 90 2H2O 10 MgCl2 10 Na2HPO4-NaH2PO4 20 NaCl 150 Paper 9230043 Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T 1997 Biochemistry 36 30 9109-9119 Disordered 58 66 TAGQEEYSA Complex Engineered Fragment 1AA9A 1CRPA 1CRQA 1CRRA 1IOZA Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Nuclear magnetic resonance (NMR) 303 D2O 10 DTT 5 GDP 30 H2O 90 MgCl2 5 NaCl 40 sodium azide 0.01 Tris-maleate-d15 pH 6.5 20 Nuclear magnetic resonance (NMR) 303 5.5 D2O 100 DTT 5 GDP 30 MgCl2 5 NaCl 40 sodium azide 0.01 Tris-maleate-d15 pH 6.5 20 Nuclear magnetic resonance (NMR) 5.5 1H2O 90 2H2O 10 MgCl2 10 Na2-HPO4-NaH2PO4 20 NaCl 150 X-ray crystallography Paper 9230043 Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T 1997 Biochemistry 36 30 9109-9119 8142349 Kraulis PJ, Domaille PJ, Campbell-Burk SL, Van Aken T, Laue ED 1994 Biochemistry 33 12 3515-3531 2406906 Milburn MV, Tong L, deVos AM, Brunger A, Yamaizumi Z, Nishimura S, Kim SH 1990 Science 247 4945 939-945 Disordered 59 72 AGQEEYSAMRDQYM Complex Engineered Fragment 121PA 1P2UA Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding X-ray crystallography 298 1,6-hexanediol 60 2,2,2-trifluoroethanol 50 isopropanol 50 Paper 12842038 Buhrman G, de Serrano V, Mattos C 2003 Structure 11 7 747-51 Disordered 60 64 GQEEY Complex Engineered Fragment 4Q21A Relationship to function unknown Unknown Unknown X-ray crystallography PDB 2406906 Milburn MV, Tong L, deVos AM, Brunger A, Yamaizumi Z, Nishimura S, Kim SH 1990 Science 247 4945 939-945 Disordered 60 68 GQEEYSAMR Complex Engineered Fragment 1Q21A 6Q21A Relationship to function unknown Unknown Unknown X-ray crystallography Paper 2406906 Milburn MV, Tong L, deVos AM, Brunger A, Yamaizumi Z, Nishimura S, Kim SH 1990 Science 247 4945 939-945 Disordered 61 65 QEEYS Complex Engineered Fragment 1Q21A 6Q21A Relationship to function unknown Unknown Unknown X-ray crystallography Paper 2406906 Milburn MV, Tong L, deVos AM, Brunger A, Yamaizumi Z, Nishimura S, Kim SH 1990 Science 247 4945 939-945 Disordered 62 65 EEYS Complex Engineered Fragment 1Q21A 6Q21A Relationship to function unknown Unknown Unknown X-ray crystallography Paper 2406906 Milburn MV, Tong L, deVos AM, Brunger A, Yamaizumi Z, Nishimura S, Kim SH 1990 Science 247 4945 939-945 Disordered 71 71 Y Complex Engineered Fragment Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Nuclear magnetic resonance (NMR) 5.5 1H2O 90 2H2O 10 MgCl2 10 Na2HPO4-NaH2PO4 20 NaCl 150 Paper 9230043 Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T 1997 Biochemistry 36 30 9109-9119 Disordered 107 109 DDV Complex Engineered Fragment Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Nuclear magnetic resonance (NMR) 303 6.5 D2O 10 DTT 5 GDP 30 H2O 90 MgCl2 5 NaCl 40 sodium azide 0.01 Tris-maleate-d15 20 Nuclear magnetic resonance (NMR) 303 6.5 D2O 100 DTT 5 GDP 30 MgCl2 5 NaCl 40 sodium azide 0.01 Tris-maleate-d15 20 Nuclear magnetic resonance (NMR) 5.5 1H2O 90 2H2O 10 MgCl2 10 Na2-HPO4-NaH2PO4 20 NaCl 150 Paper 9230043 Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T 1997 Biochemistry 36 30 9109-9119 8142349 Kraulis PJ, Domaille PJ, Campbell-Burk SL, Van Aken T, Laue ED 1994 Biochemistry 33 12 3515-3531 Disordered 168 189 LRKLNPPDESGPGCMSCKCVLS Complex Engineered Fragment 4Q21A Relationship to function unknown Unknown Unknown X-ray crystallography Paper 2406906 Milburn MV, Tong L, deVos AM, Brunger A, Yamaizumi Z, Nishimura S, Kim SH 1990 Science 247 4945 939-945 Disordered 172 189 NPPDESGPGCMSCKCVLS Complex Engineered Fragment Relationship to function unknown Unknown Unknown X-ray crystallography Paper 2406906 Milburn MV, Tong L, deVos AM, Brunger A, Yamaizumi Z, Nishimura S, Kim SH 1990 Science 247 4945 939-945 Disordered residues lie within the region corresponding to cleavage product 1, however, there is no indication that the cleavage product was discussed in the references provided. The N-terminally processed cleavage product differs from the full-length protein by a single methionine removed at the N-terminus. SHC-transforming protein 1 SHC1_HUMAN Src homology 2 domain-containing-transforming protein C1 SH2 domain protein C1 P29353 Hs.433795 SHC1_HUMAN 182676455 Homo sapiens (Human) 583 MDLLPPKPKYNPLRNESLSSLEEGASGSTPPEELPSPSASSLGPILPPLPGDDSPTTLCSFFPRMSNLRLANPAGGRPGSKGEPGRAADDGEGIDGAAMPESGPLPLLQDMNKLSGGGGRRTRVEGGQLGGEEWTRHGSFVNKPTRGWLHPNDKVMGPGVSYLVRYMGCVEVLQSMRALDFNTRTQVTREAISLVCEAVPGAKGATRRRKPCSRPLSSILGRSNLKFAGMPITLTVSTSSLNLMAADCKQIIANHHMQSISFASGGDPDTAEYVAYVAKDPVNQRACHILECPEGLAQDVISTIGQAFELRFKQYLRNPPKLVTPHDRMAGFDGSAWDEEEEEPPDHQYYNDFPGKEPPLGGVVDMRLREGAAPGAARPTAPNAQTPSHLGATLPVGQPVGGDPEVRKQMPPPPPCPGRELFDDPSYVNVQNLDKARQAVGGAGPPNPAINGSAPRDLFDMKPFEDALRVPPPPQSVSMAEQLRGEPWFHGKLSRREAEALLQLNGDFLVRESTTTPGQYVLTGLQSGQPKHLLLVDPEGVVRTKDHRFESVSHLISYHMDNHLPIISAGSELCLQQPVERKL Disordered - Extended 128 166 QLGGEEWTRHGSFVNKPTRGWLHPNDKVMGPGVSYLVRY Complex Engineered Fragment Isoform Function arises via a disorder to order transition Molecular recognition effectors Substrate/ligand binding Protein-protein binding Nuclear magnetic resonance (NMR) 308 6.5 Paper 12906822 Farooq A, Zeng L, Yan KS, Ravichandran KS, Zhou MM 2003 Structure 11 8 905-13 This entry is from the characterization of the experimental fragment in complex with a 12 residue tyrosine-phosphated peptide. The experimental fragment consisted of residues 128 - 318 of the Swiss-Prot sequence. Disordered - Extended 128 152 QLGGEEWTRHGSFVNKPTRGWLHPN Engineered Fragment Isoform Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Substrate/ligand binding Nuclear magnetic resonance (NMR) 308 6.5 Paper 12906822 Farooq A, Zeng L, Yan KS, Ravichandran KS, Zhou MM 2003 Structure 11 8 905-13 This entry is from the characterization of a fragment containing residues 17-207 in solution. The experimental fragment consisted of residues 128 - 318 of the Swiss-Prot sequence. Disordered 303 318 TIGQAFELRFKQYLRN Engineered Fragment Isoform Function arises via a disorder to order transition Molecular recognition effectors Substrate/ligand binding Protein-protein binding Nuclear magnetic resonance (NMR) 308 6.5 Paper 12906822 Farooq A, Zeng L, Yan KS, Ravichandran KS, Zhou MM 2003 Structure 11 8 905-13 This entry is from the characterization of a fragment containing residues 17-207 in solution. The experimental fragment consisted of residues 128 - 318 of the Swiss-Prot sequence. Disordered 311 318 RFKQYLRN Complex Engineered Fragment Isoform Function arises via a disorder to order transition Molecular recognition effectors Substrate/ligand binding Protein-protein binding Nuclear magnetic resonance (NMR) 308 6.5 Paper 12906822 Farooq A, Zeng L, Yan KS, Ravichandran KS, Zhou MM 2003 Structure 11 8 905-13 This entry is from the characterization of the experimental fragment in complex with a 12 residue tyrosine-phosphated peptide. The experimental fragment consisted of residues 128 - 318 of the Swiss-Prot sequence. Syntaxin-1A STX1A_RAT Synaptotagmin-associated 35 kDa protein P35A Neuron-specific antigen HPC-1 P32851 Rn.9943 STX1A_RAT 417842 Rattus norvegicus (Rat) 288 MKDRTQELRTAKDSDDDDDVTVTVDRDRFMDEFFEQVEEIRGFIDKIAENVEEVKRKHSAILASPNPDEKTKEELEELMSDIKKTANKVRSKLKSIEQSIEQEEGLNRSSADLRIRKTQHSTLSRKFVEVMSEYNATQSDYRERCKGRIQRQLEITGRTTTSEELEDMLESGNPAIFASGIIMDSSISKQALSEIETRHSEIIKLENSIRELHDMFMDMAMLVESQGEMIDRIEYNVEHAVDYVERAVSDTKKAVKYQSKARRKKIMIIICCVILGIIIASTIGGIFG Disordered - Extended 149 182 IQRQLEITGRTTTSEELEDMLESGNPAIFASGII Engineered Fragment Function arises via a disorder to order transition Molecular assembly Protein-protein binding X-ray crystallography Paper 12680753 Margittai M, Fasshauer D, Jahn R, Langen R 2003 Biochemistry 42 14 4009-4014 The sequence was cited in Fasshauer (1998) and confirmed to match Swiss-Prot ST1A_RAT (P32851) for residues 1-206 which are characterized in this entry. UV excision repair protein RAD23 homolog A RD23A_HUMAN DNA-repair protein hHR23A hHR23A P54725 Hs.643267 RD23A_HUMAN 1709983 Homo sapiens (Human) 363 MAVTITLKTLQQQTFKIRMEPDETVKVLKEKIEAEKGRDAFPVAGQKLIYAGKILSDDVPIRDYRIDEKNFVVVMVTKTKAGQGTSAPPEASPTAAPESSTSFPPAPTSGMSHPPPAAREDKSPSEESAPTTSPESVSGSVPSSGSSGREEDAASTLVTGSEYETMLTEIMSMGYERERVVAALRASYNNPHRAVEYLLTGIPGSPEPEHGSVQESQVSEQPATEAAGENPLEFLRDQPQFQNMRQVIQQNPALLPALLQQLGQENPQLLQQISRHQEQFIQMLNEPPGELADISDVEGEVGAIGEEAPQMNYIQVTPQEKEAIERLKALGFPESLVIQAYFACEKNENLAANFLLSQNFDDE Ordered UBL 3 78 VTITLKTLQQQTFKIRMEPDETVKVLKEKIEAEKGRDAFPVAGQKLIYAGKILSDDVPIRDYRIDEKNFVVVMVTK Engineered Function arises from the ordered state Molecular assembly Protein-protein binding Nuclear magnetic resonance (NMR) Paper 14557549 Walters KJ, Lech PJ, Goh AM, Wang Q, Howley PM 2003 Proc Natl Acad Sci U S A 100 22 12694-12699 The UBL region interacts with UBA domains of the same protein. It is unable to bind to both simultaneously, but does so in equilibrium with each. Ordered UBA1 161 200 SEYETMLTEIMSMGYERERVVAALRASYNNPHRAVEYLLT Engineered Function arises from the ordered state Relationship to function unknown Molecular assembly Protein-protein binding Nuclear magnetic resonance (NMR) Paper 14557549 Walters KJ, Lech PJ, Goh AM, Wang Q, Howley PM 2003 Proc Natl Acad Sci U S A 100 22 12694-12699 The UBA1 domain binds with the UBL domain of the same protein. It does so at equilibrium with UBA2. Ordered XBC-binding 232 282 LEFLRDQPQFQNMRQVIQQNPALLPALLQQLGQENPQLLQQISRHQEQFIQ Engineered Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) Paper 14557549 Walters KJ, Lech PJ, Goh AM, Wang Q, Howley PM 2003 Proc Natl Acad Sci U S A 100 22 12694-12699 Ordered UBA2 317 359 TPQEKEAIERLKALGFPESLVIQAYFACEKNENLAANFLLSQN Engineered Function arises from the ordered state Molecular assembly Protein-protein binding Nuclear magnetic resonance (NMR) Paper 14557549 Walters KJ, Lech PJ, Goh AM, Wang Q, Howley PM 2003 Proc Natl Acad Sci U S A 100 22 12694-12699 The UBA2 domain binds with the UBL domain of the same protein. It does so at equilibrium with UBA1. Disordered - Extended 79 160 TKAGQGTSAPPEASPTAAPESSTSFPPAPTSGMSHPPPAAREDKSPSEESAPTTSPESVSGSVPSSGSSGREEDAASTLVTG Function arises from the disordered state Molecular assembly Entropic chain Flexible linkers/spacers Nuclear magnetic resonance (NMR) Paper 14557549 Walters KJ, Lech PJ, Goh AM, Wang Q, Howley PM 2003 Proc Natl Acad Sci U S A 100 22 12694-12699 Disordered - Extended 201 231 GIPGSPEPEHGSVQESQVSEQPATEAAGENP Function arises from the disordered state Entropic chain Molecular assembly Flexible linkers/spacers Nuclear magnetic resonance (NMR) Paper 14557549 Walters KJ, Lech PJ, Goh AM, Wang Q, Howley PM 2003 Proc Natl Acad Sci U S A 100 22 12694-12699 Disordered - Extended 283 316 MLNEPPGELADISDVEGEVGAIGEEAPQMNYIQV Function arises from the disordered state Molecular assembly Entropic chain Flexible linkers/spacers Nuclear magnetic resonance (NMR) Paper 14557549 Walters KJ, Lech PJ, Goh AM, Wang Q, Howley PM 2003 Proc Natl Acad Sci U S A 100 22 12694-12699 Cell invasion protein sipA SIPA_SALTY Effector protein sipA Q56027 SIPA_SALTY 62903507 Salmonella typhimurium 684 MVTSVRTQPPVIMPGMQTEIKTQATNLAANLSAVRAKCHSDAVREIKGPQLEDFPALIKQASLDALFKCGKDAEALKEVFTNSNNVAGKKAIMEFAGLFRSALNATSDSPEAKTLLMKVGAEYAAQIIKDGLKEKSAFGPWLPETKKAEAKLENLEKQLLDIIKNNTGGELSKLSTNLVMQEVMPYIASCIEHNFGCTLDPLTRSNLTHLVDKAAAKAVEALDMCPQKLTQEQGTSVGREARHLEMQTLIPLLLRNVFAQIPADKLPDPKIPEPAAGPVPDGGKKAEPTGINININIDSSNHSVDNSKHINNAEPVDNGQRHIDNSNHDNSRKTIDNSRTFIDNSQRNGESHHSTNSSNVSHSHSRVDSTTHQTETAHSASTGAIDHGIAGKIDVTAHATAEAVTNASSESKDGKVVTSEKGTTGETTSFDEVDGVTSKSIIGKPVQATVHGVDDNKQQSQTAEIVNVKPLASQLAGVENVKTDTLQSDTTVITGNKAGTTDNDNSQTDKTGPFSGLKFKQNSFLSTVPSVTNMHSMHFDARETFLGVIRKALEPDTSTPFPVRRAFDGLRAEILPNDTIKSAALKAQCSDIDKHPELKAKMETLKEVITHHPQKEKLAEIALQFAREAGLTRLKGETDYVLSNVLDGLIGDGSWRAGPAYESYLNKPGVDRVITTVDGLHMQR Disordered - Extended 425 512 GETTSFDEVDGVTSKSIIGKPVQATVHGVDDNKQQSQTAEIVNVKPLASQLAGVENVKTDTLQSDTTVITGNKAGTTDNDNSQTDKTG Engineered Fragment 1Q5ZA Function arises from the disordered state Molecular assembly Protein-protein binding X-ray crystallography Rotory shadowing electron microscopy Sensitivity to proteolysis Paper 14512630 Lilic M, Galkin VE, Orlova A, VanLoock MS, Egelman EH, Stebbins CE 2003 Science 301 5641 1918-1921 Ordered 513 657 PFSGLKFKQNSFLSTVPSVTNMHSMHFDARETFLGVIRKALEPDTSTPFPVRRAFDGLRAEILPNDTIKSAALKAQCSDIDKHPELKAKMETLKEVITHHPQKEKLAEIALQFAREAGLTRLKGETDYVLSNVLDGLIGDGSWRA Engineered Fragment 1Q5ZA Function arises from the ordered state Molecular assembly Polymerization X-ray crystallography Rotory shadowing electron microscopy Sensitivity to proteolysis Paper 14512630 Lilic M, Galkin VE, Orlova A, VanLoock MS, Egelman EH, Stebbins CE 2003 Science 301 5641 1918-1921 Disordered - Extended 658 684 GPAYESYLNKPGVDRVITTVDGLHMQR Engineered Fragment 1Q5ZA Function arises from the disordered state Molecular assembly Protein-protein binding X-ray crystallography Rotory shadowing electron microscopy Sensitivity to proteolysis Paper 14512630 Lilic M, Galkin VE, Orlova A, VanLoock MS, Egelman EH, Stebbins CE 2003 Science 301 5641 1918-1921 Ssl1911 protein P73124_SYNY3 P73124 P73124_SYNY3 81670500 Synechocystis sp. (strain PCC 6803) 65 MSTQQQARALMMRHHQFIKNRQQSMLSRAAAEIGVEAEKDFWTTVQGKPQSSFRTTYDRSNASLS Disordered 1 65 MSTQQQARALMMRHHQFIKNRQQSMLSRAAAEIGVEAEKDFWTTVQGKPQSSFRTTYDRSNASLS Native Relationship to function unknown Molecular recognition effectors Protein-protein binding Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) 283 NaCl pH 6.5 0.1 Tris 10 Nuclear magnetic resonance (NMR) 298 Phosphate buffer pH 6.5 10 Nuclear magnetic resonance (NMR) 278 Phosphate buffer pH 6.5 10 Size exclusion/gel filtration chromatography 298 NaCl 150 Circular dichroism (CD) spectroscopy, far-UV 298 Circular dichroism (CD) spectroscopy, near-UV Stability at thermal extremes 363 Paper 12824490 Muro-Pastor MI, Barrera FN, Reyes JC, Florencio FJ, Neira JL 2003 Protein Sci 12 7 1443-1454 Cadherin-1 CADH1_MOUSE Epithelial cadherin E-cadherin Uvomorulin ARC-1 Antigen CD324 E-Cad/CTF1 [cleavage product 1] E-Cad/CTF2 [cleavage product 2] E-Cad/CTF3 [cleavage product 3] P09803 Mm.35605 CADH1_MOUSE 115419 Mus musculus (Mouse) 884 MGARCRSFSALLLLLQVSSWLCQELEPESCSPGFSSEVYTFPVPERHLERGHVLGRVRFEGCTGRPRTAFFSEDSRFKVATDGTITVKRHLKLHKLETSFLVRARDSSHRELSTKVTLKSMGHHHHRHHHRDPASESNPELLMFPSVYPGLRRQKRDWVIPPISCPENEKGEFPKNLVQIKSNRDKETKVFYSITGQGADKPPVGVFIIERETGWLKVTQPLDREAIAKYILYSHAVSSNGEAVEDPMEIVITVTDQNDNRPEFTQEVFEGSVAEGAVPGTSVMKVSATDADDDVNTYNAAIAYTIVSQDPELPHKNMFTVNRDTGVISVLTSGLDRESYPTYTLVVQAADLQGEGLSTTAKAVITVKDINDNAPVFNPSTYQGQVPENEVNARIATLKVTDDDAPNTPAWKAVYTVVNDPDQQFVVVTDPTTNDGILKTAKGLDFEAKQQYILHVRVENEEPFEGSLVPSTATVTVDVVDVNEAPIFMPAERRVEVPEDFGVGQEITSYTAREPDTFMDQKITYRIWRDTANWLEINPETGAIFTRAEMDREDAEHVKNSTYVALIIATDDGSPIATGTGTLLLVLLDVNDNAPIPEPRNMQFCQRNPQPHIITILDPDLPPNTSPFTAELTHGASVNWTIEYNDAAQESLILQPRKDLEIGEYKIHLKLADNQNKDQVTTLDVHVCDCEGTVNNCMKAGIVAAGLQVPAILGILGGILALLILILLLLLFLRRRTVVKEPLLPPDDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTLMSVPQYRPRPANPDEIGNFIDENLKAADSDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDQDQDYDYLNEWGNRFKKLADMYGGGEDD Disordered 736 884 RTVVKEPLLPPDDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTLMSVPQYRPRPANPDEIGNFIDENLKAADSDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDQDQDYDYLNEWGNRFKKLADMYGGGEDD Engineered Function arises via a disorder to order transition Molecular assembly Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV 273 7 phosphate 10 Fluorescence polarization/anisotropy DTT 1 NaCl buffer 20 protein 12 Tris-HCl or HEPES pH 7.0 to 8.5 (10 to 100 mM) Fluorescence polarization/anisotropy B-mercaptoethanol 10 NaCl buffer 20 protein 12 Tris-HCl or HEPES pH 7.0 to 8.5 (10 to 100 mM) Fluorescence polarization/anisotropy 7 guanidine HCl 6 protein 12 Tris-HCl 100 Nuclear magnetic resonance (NMR) 323 8 D2O 50 NaCl 10 trimethyl silyl propionate 0.35 Tris-HCl 5 Nuclear magnetic resonance (NMR) 298 8 D2O 50 NaCl 10 trimethyl silyl propionate 0.35 Tris-HCl 5 Nuclear magnetic resonance (NMR) 276 8 D2O 50 NaCl 10 trimethyl silyl propionate 0.35 Tris-HCl 5 Sensitivity to proteolysis 298 CaCl2 2 CHES pH 9.2 100 DTT 5 Paper 11121423 Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI 2001 J Biol Chem 276 15 12301-12309 Disordered residues lie within the regions corresponding to cleavage products 1 - 3, however, there is no experimental evidence to confirm that these products are disordered. Nucleoprotein NCAP_MEASE Nucleocapsid protein NP Protein N Q784S3_9PARA P04851 NCAP_MEASE 127900 Measles virus (strain Edmonston) (MeV) (Subacute sclerose panencephalitis virus) 525 MATLLRSLALFKRNKDKPPITSGSGGAIRGIKHIIIVPIPGDSSITTRSRLLDRLVRLIGNPDVSGPKLTGALIGILSLFVESPGQLIQRITDDPDVSIRLLEVVQSDQSQSGLTFASRGTNMEDEADQYFSHDDPSSSDQSRSGWFENKEISDIEVQDPEGFNMILGTILAQIWVLLAKAVTAPDTAADSELRRWIKYTQQRRVVGEFRLERKWLDVVRNRIAEDLSLRRFMVALILDIKRTPGNKPRIAEMICDIDTYIVEAGLASFILTIKFGIETMYPALGLHEFAGELSTLESLMNLYQQMGETAPYMVILENSIQNKFSAGSYPLLWSYAMGVGVELENSMGGLNFGRSYFDPAYFRLGQEMVRRSAGKVSSTLASELGITAEDARLVSEIAMHTTEDRISRAVGPRQAQVSFLHGDQSENELPGLGGKEDRRVKQGRGEARESYRETGSSRASDARAAHPPTSMPLDIDTASESGQDPQDSRRSADALLRLQAMAGILEEQGSDTDTPRVYNDRDLLD Disordered - Pre-Molten Globule N Tail 401 525 TTEDRISRAVGPRQAQVSFLHGDQSENELPGLGGKEDRRVKQGRGEARESYRETGSSRASDARAAHPPTSMPLDIDTASESGQDPQDSRRSADALLRLQAMAGILEEQGSDTDTPRVYNDRDLLD Engineered Fragment Monomeric Native Function arises via a disorder to order transition Molecular recognition effectors Molecular assembly Protein-protein binding Nuclear magnetic resonance (NMR) 7 sodium phosphate 10 protein 0.5 Circular dichroism (CD) spectroscopy, far-UV 293 7 sodium phosphate 10 TFE increasing concentrations (0,10,20,30) 30 Small-angle X-ray scattering (SAXS) 281 EDTA buffer 5 glycerol radiation scavenger 10 Tris/HCl buffer 10 Dynamic light scattering 7 sodium phosphate 10 Dynamic light scattering 8 NaCl concentrated at 1.25mg/ml. 75 Tris/HCl 10 Size exclusion/gel filtration chromatography Sensitivity to proteolysis N tail purified 1 SDS-PAGE 12 trypsin 0.25 Paper 3211755 Buckland R, Gerald C, Barker D, Wild F 1988 Nucleic Acids Res 16 24 11821 12621042 Longhi S, Receveur-Brechot V, Karlin D, Johansson K, Darbon H, Bhella D, Yeo R, Finet S, Canard B 2003 J Biol Chem 278 20 18638-18648 20058326 Gely S, Lowry DF, Bernard C, Jensen MR, Blackledge M, Costanzo S, Bourhis JM, Darbon H, Daughdrill G, Longhi S 2010 J Mol Recognit 14749181 Bourhis JM, Johansson K, Receveur-Brechot V, Oldfield CJ, Dunker KA, Canard B, Longhi S 2004 Virus Res 99 2 157-67 16046624 Bourhis JM, Receveur-Brechot V, Oglesbee M, Zhang X, Buccellato M, Darbon H, Canard B, Finet S, Longhi S 2005 Protein Sci 14 8 1975-92 12944395 Johansson K, Bourhis JM, Campanacci V, Cambillau C, Canard B, Longhi S 2003 J Biol Chem 278 45 44567-73 15914856 Laine D, Bourhis JM, Longhi S, Flacher M, Cassard L, Canard B, Sautès-Fridman C, Rabourdin-Combe C, Valentin H 2005 J. Gen. Virol. 86 Pt 6 1771-84 14557619 Laine D, Trescol-Biemont MC, Longhi S, Libeau G, Marie JC, Vidalain PO, Azocar O, Diallo A, Canard B, Rabourdin-Combe C, Valentin H 2003 J Virol 77 21 11332-11346 15914229 Zhang X, Bourhis JM, Longhi S, Carsillo T, Buccellato M, Morin B, Canard B, Oglesbee M 2005 Virology 337 1 162-74 The experimental NTAIL sequence in the Longhi et al. (2003) article contained four additional amino acids plus a 6X Histidine tag fused to the N-terminus of amino acids 399-523 of the SwissProt sequence. The experimental sequence was obtained through direct correspondence with Longhi. The secondary structure predictor, JPRED, predicts an alpha-helix at amino acids 489-504. The Gely et al. (2010), paper offers NMR evidence of a gain in alpha-helical structure for aa 490-504, and for structural transitions of NTAIL induced by interaction with the nucleocapsid-binding domain (XD, aa 459-507) of Phosphoprotein. (See DP00133: MeV Phosphoprotein) The N-tail region belongs to the premolten globule subfamily and shows alpha-helical propensity (as seen by CD studies with TFE). Longhi et al. (2003). The part of the N-tail region undergoing alpha-helical induced folding: aa 488-505. Johansson et al. (2003); Bourhis et al. (2004). The parts of the N-tail region involved in binding to the C-terminal domain of P (X domain, aa 457-507): aa 488-505 and 517-525. Bourhis et al. (2005). See DP00133 for MeV Phosphoprotein (aka protein P). The part of the N-tail region involved in binding to the extracellular nuceloprotein receptor NR: aa 401-420. Laine et al. (2003); Laine et al. (2005). The part of the N-tail region involved in binding to Hsp72: aa 488-505 and 517-525. Zhang et al. (2005). The native sequence used in DP00160 is from UniProt ID (unreviewed): Q784S3 (Q784S3_9PARA); Takeuchi, et al. (2000) PMID 10949953. A reviewed UniProt entry with slight sequence variations exists at P04851 (NCAP_MEASE). Additional references for Protein P (DP00133) and Protein N (DP00160): Belle et al. Proteins. 2008 Dec;73(4):973-88. PMID: 18536007; Bernard et al. FEBS Lett. 2009 Apr 2;583(7):1084-9. Epub 2009 Mar 9. PMID: 19275899; Couturier et al. J Mol Recognit. 2010 May;23(3):301-15. PMID: 19718689; Kavalenka et al. Biophys J. 2010 Mar 17;98(6):1055-64. PMID: 20303863; Longhi, Oglesbee. Protein Pept Lett. 2010;17(8):961-78. PMID: 20450481; Longhi. Curr Top Microbiol Immunol. 2009;329:103-28. Review. PMID: 19198564; Morin et al. J Phys Chem B. 2006 Oct 19;110(41):20596-608. PMID: 17034249. [AV 08/06/2010 Longhi, S.] Cell division protein zipA ZIPA_ECOLI P77173 ZIPA_ECOLI 34395999 Escherichia coli (strain K12) 328 MMQDLRLILIIVGAIAIIALLVHGFWTSRKERSSMFRDRPLKRMKSKRDDDSYDEDVEDDEGVGEVRVHRVNHAPANAQEHEAARPSPQHQYQPPYASAQPRQPVQQPPEAQVPPQHAPHPAQPVQQPAYQPQPEQPLQQPVSPQVAPAPQPVHSAPQPAQQAFQPAEPVAAPQPEPVAEPAPVMDKPKRKEAVIIMNVAAHHGSELNGELLLNSIQQAGFIFGDMNIYHRHLSPDGSGPALFSLANMVKPGTFDPEMKDFTTPGVTIFMQVPSYGDELQNFKLMLQSAQHIADEVGGVVLDDQRRMMTPQKLREYQDIIREVKDANA Disordered 39 185 RPLKRMKSKRDDDSYDEDVEDDEGVGEVRVHRVNHAPANAQEHEAARPSPQHQYQPPYASAQPRQPVQQPPEAQVPPQHAPHPAQPVQQPAYQPQPEQPLQQPVSPQVAPAPQPVHSAPQPAQQAFQPAEPVAAPQPEPVAEPAPVM Rotory shadowing electron microscopy modeling as a worm-like chain Paper 12107152 Ohashi T, Hale CA, de Boer PA, Erickson HP 2002 J Bacteriol 184 15 4313-4315 The EM used in this study is a novel approach to demonstrate an unstructured protein. The unstructured protein is placed between two small globular domains and imaged by EM. Knowing the contour length, one can determine the persistance lengh from the average spacing of the two globular domains. A persistence length of 0.3-0.6 nm is characteristic of an unstructrured protein. Stannin SNN_HUMAN AG8_1 O75324 Hs.700592 SNN_HUMAN 6094313 Homo sapiens (Human) 88 MSIMDHSPTTGVVTVIVILIAIAALGALILGCWCYLRLQRISQSEDEESIVGDGETKEPFLLVQYSAKGPCVERKAKLMTPNGPEVHG Disordered 36 58 LRLQRISQSEDEESIVGDGETKE Monomeric Function arises from the disordered state Entropic chain Flexible linkers/spacers Nuclear magnetic resonance (NMR) 333 d25-SDS 600 DTT 0.05-1 mM H2O 10% NaN3 0.02% Phosphate-buffered saline pH 4.0 20 Paper 16246365 Buck-Koehntop BA, Mascioni A, Buffy JJ, Veglia G 2005 J Mol Biol 354 3 652-65 Protein GIR2 GIR2_YEAST DRG family-regulatory protein 2 Q03768 GIR2_YEAST 30913066 Saccharomyces cerevisiae (Baker's yeast) 265 MDYKEEQKQELEVLESIYPDELRIINDEYPKIKFEVAIKLELDTGDSTSVLTKEHTIIAEFKLPENYPDEPCLISLEAQEVALNDNEEDNEEDEDEVEYDDHGNKVLKKFENLPDLISFKGYLPELTVQLESQIETDMLLGMQMCFALISSIKERCEQWYSEQLNKLEKQYELEAQEREKKEQAKFHGTKVTRESYLEWRSKFRQELKLDERDQVRRMKAHHGKLTGKQMFEQGVVGTGDEYMEEDDASVDDVAKGLAKTEIANQ Disordered 1 265 MDYKEEQKQELEVLESIYPDELRIINDEYPKIKFEVAIKLELDTGDSTSVLTKEHTIIAEFKLPENYPDEPCLISLEAQEVALNDNEEDNEEDEDEVEYDDHGNKVLKKFENLPDLISFKGYLPELTVQLESQIETDMLLGMQMCFALISSIKERCEQWYSEQLNKLEKQYELEAQEREKKEQAKFHGTKVTRESYLEWRSKFRQELKLDERDQVRRMKAHHGKLTGKQMFEQGVVGTGDEYMEEDDASVDDVAKGLAKTEIANQ Native Relationship to function unknown Unknown Unknown SDS-PAGE gel, Aberrant mobility on Stability at thermal extremes Sensitivity to proteolysis Paper 15896712 Alves VS, Castilho BA 2005 Biochem Biophys Res Commun 332 2 450-5 60S acidic ribosomal protein P1-alpha RLA1_YEAST P1A YP1alpha A1 L12EIIA P05318 RLA1_YEAST 133056 Saccharomyces cerevisiae (Baker's yeast) 106 MSTESALSYAALILADSEIEISSEKLLTLTNAANVPDENIWADIFAKALDGQNLKDLLVNFSAGAAAPAGVAGGVAGGEAGEAEAEKEEEEAKEESDDDMGFGLFD Disordered 1 106 MSTESALSYAALILADSEIEISSEKLLTLTNAANVPDENIWADIFAKALDGQNLKDLLVNFSAGAAAPAGVAGGVAGGEAGEAEAEKEEEEAKEESDDDMGFGLFD Native Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV Nuclear magnetic resonance (NMR) Fluorescence, intrinsic Stability at thermal extremes Sensitivity to proteolysis Paper 10913306 Zurdo J, Gonzalez C, Sanz JM, Rico M, Remacha M, Ballesta JP 2000 Biochemistry 39 30 8935-43 Pyridoxine/pyridoxamine 5'-phosphate oxidase PDXH_ECOLI EC 1.4.3.5 PNP/PMP oxidase PNPOx Pyridoxal 5'-phosphate synthase P0AFI7 PDXH_ECOLI 84028916 Escherichia coli (strain K12) 218 MSDNDELQQIAHLRREYTKGGLRRRDLPADPLTLFERWLSQACEAKLADPTAMVVATVDEHGQPYQRIVLLKHYDEKGMVFYTNLGSRKAHQIENNPRVSLLFPWHTLERQVMVIGKAERLSTLEVMKYFHSRPRDSQIGAWVSKQSSRISARGILESKFLELKQKFQQGEVPLPSFWGGFRVSLEQIEFWQGGEHRLHDRFLYQRENDAWKIDRLAP Disordered domain 2 128 175 KYFHSRPRDSQIGAWVSKQSSRISARGILESKFLELKQKFQQGEVPLP Complex Native Function arises from the disordered state Modification site X-ray crystallography 100 2-mercaptoethanol 5 HEPES pH 6.8 60 K2PO4 pH 7.5 100 KH2PO4/NH4H2PO4 0.65 protein 5 Paper 15858270 Safo MK, Musayev FN, Schirch V 2005 Acta Crystallogr D Biol Crystallogr 61 Pt 5 599-604 Disorder in this region is found in monomer B of the tetragonal unit cell. Disordered domain 2 130 175 FHSRPRDSQIGAWVSKQSSRISARGILESKFLELKQKFQQGEVPLP Complex Native Function arises from the disordered state Modification site X-ray crystallography 100 2-mercaptoethanol 5 HEPES pH 6.8 60 K2PO4 pH 7.5 100 KH2PO4/NH4H2PO4 0.65 protein 5 Paper 15858270 Safo MK, Musayev FN, Schirch V 2005 Acta Crystallogr D Biol Crystallogr 61 Pt 5 599-604 Disorder in this region is found in monomer A of the tetragonal unit cell. Disordered 1 16 MSDNDELQQIAHLRRE Complex Native Function arises via a disorder to order transition Modification site Protein-protein binding X-ray crystallography 100 protein 5 K2PO4 pH 7.5 100 2-mercaptoethanol 5 HEPES pH 6.8 60 KH2PO4/NH4H2PO4 0.65 Paper 15858270 Safo MK, Musayev FN, Schirch V 2005 Acta Crystallogr D Biol Crystallogr 61 Pt 5 599-604 Disorder in this region is found in monomer B of the tetragonal unit cell. Disordered 1 10 MSDNDELQQI Complex Native Function arises via a disorder to order transition Modification site Protein-protein binding X-ray crystallography 100 K2PO4 pH 7.5 100 protein 5 2-mercaptoethanol 5 HEPES pH 6.8 60 KH2PO4/NH4H2PO4 0.65 Paper 15858270 Safo MK, Musayev FN, Schirch V 2005 Acta Crystallogr D Biol Crystallogr 61 Pt 5 599-604 Disorder in this region is found in monomer A of the tetragonal unit cell. The sequence referenced in the paper has an M at position 1. However, the SwissProt sequence does not include this M. Troponin I, cardiac muscle TNNI3_HUMAN Cardiac troponin I P19429 Hs.709179 TNNI3_HUMAN 136213 Homo sapiens (Human) 210 MADGSSDAAREPRPAPAPIRRRSSNYRAYATEPHAKKKSKISASRKLQLKTLLLQIAKQELEREAEERRGEKGRALSTRCQPLELAGLGFAELQDLCRQLHARVDKVDEERYDIEAKVTKNITEIADLTQKIFDLRGKFKRPTLRRVRISADAMMQALLGARAKESLDLRAHLKQVKKEDTEKENREVGDWRKNIDALSGMEGRKKKFES Disordered - Extended C-terminus 192 210 RKNIDALSGMEGRKKKFES Complex Engineered Fragment Mutant 1J1EF Function arises via a disorder to order transition Molecular assembly Protein-protein binding X-ray crystallography 293 8 CaCl2 5 glycerol 15% LiCl 0.1 PEG3350 20% protein 10 Tris-HCl 50 Paper 12840750 Takeda S, Yamashita A, Maeda K, Maeda Y 2003 Nature 424 6944 35-41 Disordered - Extended 31 34 TEPH Complex Engineered Fragment Mutant 1J1DC 1J1EC Function arises from the disordered state Unknown Unknown X-ray crystallography 293 8 CaCl2 5 glycerol 15% LiCl 0.1 PEG 3350 20% protein 10 Tris-HCl 50 Paper 12840750 Takeda S, Yamashita A, Maeda K, Maeda Y 2003 Nature 424 6944 35-41 Disordered - Extended 66 89 EERRGEKGRALSTRCQPLELAGLG Complex Engineered Fragment Mutant Function arises via a disorder to order transition Entropic chain Molecular assembly Flexible linkers/spacers Protein-protein binding X-ray crystallography 293 8 CaCl2 5 glycerol 15% LiCl 0.1 PEG3350 20% protein 10 Tris-HCl 50 Paper 12840750 Takeda S, Yamashita A, Maeda K, Maeda Y 2003 Nature 424 6944 35-41 This disordered region becomes ordered when in complex with Troponin T. Disordered - Extended TnI Inhibitory Region 137 148 GKFKRPTLRRVR Complex Engineered Fragment Mutant Relationship to function unknown Molecular recognition effectors Entropic chain Flexible linkers/spacers Protein-protein binding X-ray crystallography 293 8 CaCl2 5 glycerol 15% LiCl 0.1 PEG3350 20% protein 10 Tris-HCl 50 Paper 12840750 Takeda S, Yamashita A, Maeda K, Maeda Y 2003 Nature 424 6944 35-41 This disordered region is thought to be the binding sites for actin and tropomyosin. Disordered - Extended C-Terminus 163 210 AKESLDLRAHLKQVKKEDTEKENREVGDWRKNIDALSGMEGRKKKFES Complex Engineered Fragment Mutant 1J1EC Function arises via a disorder to order transition Molecular assembly Entropic chain Molecular recognition effectors Flexible linkers/spacers Protein-protein binding X-ray crystallography 293 8 CaCl2 5 glycerol 15% LiCl 0.1 PEG3350 20% protein 10 Tris-HCl 50 Paper 12840750 Takeda S, Yamashita A, Maeda K, Maeda Y 2003 Nature 424 6944 35-41 Residues 163-191 were disordered in one of the two Troponin I molecules that were obtained through crystallization. Disordered - Extended 189 191 GDW Complex Engineered Fragment Mutant Function arises via a disorder to order transition Molecular assembly Entropic chain Molecular recognition effectors Flexible linkers/spacers Protein-protein binding X-ray crystallography 293 8 CaCl2 5 glycerol 15% LiCl 0.1 PEG3350 20% Tris-HCl 50 Paper 12840750 Takeda S, Yamashita A, Maeda K, Maeda Y 2003 Nature 424 6944 35-41 This disordered region undergoes a conformational change when interacting with other Troponin moledules. Ras-related protein Rap-2a RAP2A_HUMAN RbBP-30 RAP2A P10114 Hs.508480 RAP2A_HUMAN 131852 Homo sapiens (Human) 183 MREYKVVVLGSGGVGKSALTVQFVTGTFIEKYDPTIEDFYRKEIEVDSSPSVLEILDTAGTEQFASMRDLYIKNGQGFILVYSLVNQQSFQDIKPMRDQIIRVKRYEKVPVILVGNKVDLESEREVSSSEGRALAEEWGCPFMETSAKSKTMVDELFAEIVRQMNYAAQPDKDDPCCSACNIQ Disordered - Extended Switch II 62 66 EQFAS Complex Fragment Native 1KAOA 2RAPA 3RAPR 3RAPS Function arises via a disorder to order transition Molecular assembly Protein-protein binding X-ray crystallography 8 LiSO4 100 PEG 8000 20-25% Tris/HCl 100 X-ray crystallography 8 MgCl2 100 PEG 8000 20-25% Tris/HCl 100 Paper 10591105 Menetrey J, Cherfils J 1999 Proteins 37 3 465-473 Disordered - Extended Switch II 62 63 EQ Complex Fragment Native 1KAOA 2RAPA 3RAPR 3RAPS Function arises via a disorder to order transition Molecular assembly Protein-protein binding X-ray crystallography 8 LiSO4 100 PEG 8000 20-25% Tris/HCl 100 X-ray crystallography 8 MgCl2 100 PEG 8000 20-25% Tris/HCl 100 Paper 10591105 Menetrey J, Cherfils J 1999 Proteins 37 3 465-473 Disordered - Extended Switch II 60 63 GTEQ Complex Fragment 1KAOA 2RAPA 3RAPR 3RAPS Function arises via a disorder to order transition Molecular assembly Protein-protein binding X-ray crystallography 7.5 protein per mL 10 PEG 4000 19 magnesium chloride 100 Tris 100 Paper 9312017 Cherfils J, Menetrey J, Le Bras G, Janoueix-Lerosey I, de Gunzburg J, Garel JR, Auzat I 1997 EMBO J 16 18 5582-91 Disordered - Extended L3 Loop 45 55 EVDSSPSVLEI Complex Fragment Native 1KAOA 2RAPA 3RAPR 3RAPS Function arises from the disordered state Entropic chain Flexible linkers/spacers X-ray crystallography 8 PEG 8000 20-25% Tris/HCl 100 LiSO4 100 X-ray crystallography 8 MgCl2 100 PEG 8000 20-25% Tris/HCl 100 Paper 10591105 Menetrey J, Cherfils J 1999 Proteins 37 3 465-473 Disordered - Extended Switch I 32 36 YDPTI Complex Fragment 1KAOA 2RAPA 3RAPR 3RAPS Function arises via a disorder to order transition Molecular assembly Molecular recognition effectors Protein-protein binding X-ray crystallography 7.5 protein per mL 10 PEG 4000 19 magnesium chloride 100 Tris 100 Paper 9312017 Cherfils J, Menetrey J, Le Bras G, Janoueix-Lerosey I, de Gunzburg J, Garel JR, Auzat I 1997 EMBO J 16 18 5582-91 Pyridoxine-5'-phosphate oxidase PNPO_HUMAN EC 1.4.3.5 Pyridoxamine-phosphate oxidase Q9NVS9 Hs.631742 PNPO_HUMAN 37082126 Homo sapiens (Human) 261 MTCWLRGVTATFGRPAEWPGYLSHLCGRSAAMDLGPMRKSYRGDREAFEETHLTSLDPVKQFAAWFEEAVQCPDIGEANAMCLATCTRDGKPSARMLLLKGFGKDGFRFFTNFESRKGKELDSNPFASLVFYWEPLNRQVRVEGPVKKLPEEEAECYFHSRPKSSQIGAVVSHQSSVIPDREYLRKKNEELEQLYQDQEVPKPKSWGGYVLYPQVMEFWQGQTNRLHDRIVFRRGLPTGDSPLGPMTHRGEEDWLYERLAP Disordered 1 48 MTCWLRGVTATFGRPAEWPGYLSHLCGRSAAMDLGPMRKSYRGDREAF Engineered Relationship to function unknown Modification site Protein-protein binding X-ray crystallography 100 Beta-mercaptoethanol 2.5 NaCl 250 polyethyleneimine 1.5% potassium phosphate pH 7.5 50 protein 7 Sodium citrate 20 Paper 12824491 Musayev FN, Di Salvo ML, Ko TP, Schirch V, Safo MK 2003 Protein Sci 12 7 1455-63 Tubulin beta-2 chain TBB2_CHICK Beta-tubulin class-II P32882 Gga.1815 TBB2_CHICK 417855 Gallus gallus (Chicken) 445 MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEGEEDEA Disordered - Extended 394 407 FLHWYTGEGMDEME Engineered Fragment Function arises via a disorder to order transition Molecular assembly Protein-protein binding Substrate/ligand binding Nuclear magnetic resonance (NMR) 298 7 TFE Paper 10211825 Jimenez MA, Evangelio JA, Aranda C, Lopez-Brauet A, Andreu D, Rico M, Lagos R, Andreu JM, Monasterio O 1999 Protein Sci 8 4 788-799 Disordered - Extended 394 404 FLHWYTGEGMD Engineered Fragment Function arises via a disorder to order transition Molecular assembly Protein-protein binding Substrate/ligand binding Circular dichroism (CD) spectroscopy, near-UV 298 Paper 10211825 Jimenez MA, Evangelio JA, Aranda C, Lopez-Brauet A, Andreu D, Rico M, Lagos R, Andreu JM, Monasterio O 1999 Protein Sci 8 4 788-799 Disordered - Extended 412 414 ESN Engineered Fragment Function arises via a disorder to order transition Molecular assembly Substrate/ligand binding Protein-protein binding Circular dichroism (CD) spectroscopy, near-UV 298 TFE Paper 10211825 Jimenez MA, Evangelio JA, Aranda C, Lopez-Brauet A, Andreu D, Rico M, Lagos R, Andreu JM, Monasterio O 1999 Protein Sci 8 4 788-799 Disorder may be caused by the truncation of this fragment Disordered - Extended 431 431 D Engineered Fragment Function arises via a disorder to order transition Molecular assembly Substrate/ligand binding Protein-protein binding Circular dichroism (CD) spectroscopy, near-UV 298 TFE Paper 10211825 Jimenez MA, Evangelio JA, Aranda C, Lopez-Brauet A, Andreu D, Rico M, Lagos R, Andreu JM, Monasterio O 1999 Protein Sci 8 4 788-799 Disorder may be caused by the truncation of this fragment Disordered - Extended 432 445 EQGEFEEEGEEDEA Engineered Fragment Function arises via a disorder to order transition Molecular assembly Substrate/ligand binding Protein-protein binding Nuclear magnetic resonance (NMR) 298 7 TFE Circular dichroism (CD) spectroscopy, near-UV 298 Paper 10211825 Jimenez MA, Evangelio JA, Aranda C, Lopez-Brauet A, Andreu D, Rico M, Lagos R, Andreu JM, Monasterio O 1999 Protein Sci 8 4 788-799 Dehydrin-like protein Q39805_SOYBN Q39805 Gma.33428 Q39805_SOYBN 75281899 Glycine max (Soybean) 226 MASYQKHYDDQGRKVDEYGNVEKQTDEYGNPVHAASVTYVATRTAAGGYSDDINKQHDTTNAYGVDTGRQHSSGGYDGDTNKHHGTTGGYNDDTNRHHGTTGVYGIDTDRQQHGTTGGYAGDTGRQHGNIGGPYYGTNTADTGTGPRSGTTGGTGYGGTGGTDYGTTGGTGYGSGTGYGVNTGGAHTEAGYRKEHRQHDQSHGDQNEKKGIMDKIKEKLPGGHSDK Disordered - Extended 1 226 MASYQKHYDDQGRKVDEYGNVEKQTDEYGNPVHAASVTYVATRTAAGGYSDDINKQHDTTNAYGVDTGRQHSSGGYDGDTNKHHGTTGGYNDDTNRHHGTTGVYGIDTDRQQHGTTGGYAGDTGRQHGNIGGPYYGTNTADTGTGPRSGTTGGTGYGGTGGTDYGTTGGTGYGSGTGYGVNTGGAHTEAGYRKEHRQHDQSHGDQNEKKGIMDKIKEKLPGGHSDK Native Function arises from the disordered state Unknown Unknown Stability at thermal extremes from 0°C to 100°C Circular dichroism (CD) spectroscopy, far-UV 7 buffer sodium phosphate increasing temperatures from 12 to 80°C Paper 12644649 Soulages JL, Kim K, Arrese EL, Walters C, Cushman JC 2003 Plant Physiol 131 3 963-75 RAF proto-oncogene serine/threonine-protein kinase RAF1_HUMAN EC=2.7.11.1 C-RAF cRaf Raf-1 P04049 Hs.159130 RAF1_HUMAN 125651 Homo sapiens (Human) 648 MEHIQGAWKTISNGFGFKDAVFDGSSCISPTIVQQFGYQRRASDDGKLTDPSKTSNTIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKKARLDWNTDAASLIGEELQVDFLDHVPLTTHNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMCVDWSNIRQLLLFPNSTIGDSGVPALPSLTMRRMRESVSRMPVSSQHRYSTPHAFTFNTSSPSSEGSLSQRQRSTSTPNVHMVSTTLPVDSRMIEDAIRSHSESASPSALSSSPNNLSPTGWSQPKTPVPAQRERAPVSGTQEKNKIRPRGQRDSSYYWEIEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTGSVLWMAPEVIRMQDNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMVGRGYASPDLSKLYKNCPKAMKRLVADCVKKVKEERPLFPQILSSIELLQHSLPKINRSASEPSLHRAAHTEDINACTLTTSPRLPVF Disordered 51 54 PSKT Engineered Fragment Relationship to function unknown Unknown Unknown X-ray crystallography 298 7.6 monomethylether PEG 5000 (Fluka) 10 ammonium sulphate 50 CaCl2 5 MgCl2 2.5 Dithioerythritol (DTE) 0.5 Tris-HCl 32.2 Paper 7791872 Nassar N, Horn G, Herrmann C, Scherer A, McCormick F, Wittinghofer A 1995 Nature 375 6532 554-560 Disordered region may be present due to the fragmentation of the sequence. Disordered 55 55 S Engineered Fragment Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 298 5.3 15N labeled protein 1.4 dithiothreitol 0.1 sodium acetate-d3 10 sodium azide in 100%D2O or 94% H2O/6% D2O 0.05 Nuclear magnetic resonance (NMR) 298 5.3 13C/15N labeled protein 1.4 dithiolthreitol 0.1 sodium acetate-d3 10 sodium azide in 100%D2O or 94% H2O/6% D2O 0.05 Paper 7766599 Emerson SD, Madison VS, Palermo RE, Waugh DS, Scheffler JE, Tsao KL, Kiefer SE, Liu SP, Fry DC 1995 Biochemistry 34 21 6911-8 Disordered region may be present due to the fragmentation of the sequence. Disordered 73 76 RNGM Engineered Fragment Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 298 5.3 15N labeled protein 1.4 sodium acetate-d3 10 dithiothreitol 0.1 sodium azide in 100%D2O or 94% H2O/6% D2O 0.05 Nuclear magnetic resonance (NMR) 298 5.3 13C/15N labeled protein 1.4 dithiolthreitol 0.1 sodium acetate-d3 10 sodium azide in 100%D2O or 94% H2O/6% D2O 0.05 Paper 7766599 Emerson SD, Madison VS, Palermo RE, Waugh DS, Scheffler JE, Tsao KL, Kiefer SE, Liu SP, Fry DC 1995 Biochemistry 34 21 6911-8 Disordered region may be present due to the fragmentation of the sequence. Disordered 64 64 N Engineered Fragment Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 298 5.3 15N labeled protein 1.4 dithiothreitol 1 sodium acetate-d3 10 sodium azide in 100%D2O or 94% H2O/6% D2O 0.05 Nuclear magnetic resonance (NMR) 298 5.3 13C/15N labeled protein 1.4 dithiolthreitol 0.1 sodium acetate-d3 10 sodium azide in 100%D2O or 94% H2O/6% D2O 0.05 Paper 7766599 Emerson SD, Madison VS, Palermo RE, Waugh DS, Scheffler JE, Tsao KL, Kiefer SE, Liu SP, Fry DC 1995 Biochemistry 34 21 6911-8 Disordered region may be present due to the fragmentation of the sequence. Disordered 102 108 LHEHKGK Engineered Fragment Relationship to function unknown Unknown Unknown X-ray crystallography 298 7.6 monomethylether PEG 5000 (Fluka) 10 ammonium sulphate 50 CaCl2 5 MgCl2 2.5 Dithioerythritol (DTE) 0.5 Tris-HCl 32.2 Paper 7791872 Nassar N, Horn G, Herrmann C, Scherer A, McCormick F, Wittinghofer A 1995 Nature 375 6532 554-560 Disordered region may be present due to the fragmentation of the sequence. Disordered - Extended 104 107 EHKG Engineered Fragment 1GUAB Relationship to function unknown Unknown Unknown X-ray crystallography 292 calcium acetate 20-50 mM dithiothreitol 2 MgCl2 5 PEG 4000 11 Tris-HCl pH 7.6 80 PDB 8756332 Nassar N, Horn G, Herrmann C, Block C, Janknecht R, Wittinghofer A 1996 Nat Struct Biol 3 8 723-729 Disordered 113 117 DWNTD Engineered Fragment Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 298 5.3 15N labeled protein 1.4 dithiothreitol 0.1 sodium acetate-d3 10 sodium azide in 100%D2O or 94% H2O/6% D2O 0.05 Nuclear magnetic resonance (NMR) 298 5.3 13C/15N labeled protein 1.4 dithiolthreitol 0.1 sodium acetate-d3 10 sodium azide in 100%D2O or 94% H2O/6% D2O 0.05 Paper 7766599 Emerson SD, Madison VS, Palermo RE, Waugh DS, Scheffler JE, Tsao KL, Kiefer SE, Liu SP, Fry DC 1995 Biochemistry 34 21 6911-8 Disordered region may be present due to the fragmentation of the sequence. Disordered 136 138 LTT Engineered Fragment 1FAQA 1FARA Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 298 6.2 d10-DTT 1 d11-Tris d3-acetate 30 D2O 10 Na2SO4 75 NaN3 0.01 ZnCl2 10 Paper 8710867 Mott HR, Carpenter JW, Zhong S, Ghosh S, Bell RM, Campbell SL 1996 Proc Natl Acad Sci U S A 93 16 8312-8317 Disordered region may be present due to the fragmentation of the sequence. Disordered 132 132 D Engineered Fragment Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 298 5.3 15N labeled protein 1.4 dithiothreitol 0.1 sodium acetate-d3 10 sodium azide in 100%D2O or 94% H2O/6% D2O 0.05 Nuclear magnetic resonance (NMR) 298 5.3 13C/15N labeled protein 1.4 dithiolthreitol 0.1 sodium acetate-d3 10 sodium azide in 100%D2O or 94% H2O/6% D2O 0.05 Paper 7766599 Emerson SD, Madison VS, Palermo RE, Waugh DS, Scheffler JE, Tsao KL, Kiefer SE, Liu SP, Fry DC 1995 Biochemistry 34 21 6911-8 Disordered region may be present due to the fragmentation of the sequence. Disordered 185 187 VDW Engineered Fragment 1FAQA 1FARA Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 298 6.2 d10-DTT 1 d11-Tris d3-acetate 30 D2O 10 Na2SO4 75 NaN3 0.01 ZnCl2 10 Paper 8710867 Mott HR, Carpenter JW, Zhong S, Ghosh S, Bell RM, Campbell SL 1996 Proc Natl Acad Sci U S A 93 16 8312-8317 Disordered region may be present due to the fragmentation of the sequence. Disordered 146 150 FLKLA Engineered Fragment Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 298 6.2 d10-DTT 1 d11-Tris d3-acetate 30 D2O 10 Na2SO4 75 NaN3 0.01 ZnCl2 10 Paper 8710867 Mott HR, Carpenter JW, Zhong S, Ghosh S, Bell RM, Campbell SL 1996 Proc Natl Acad Sci U S A 93 16 8312-8317 Disordered region may be present due to the fragmentation of the sequence. POU domain class 2-associating factor 1 OBF1_HUMAN B-cell-specific coactivator OBF-1 OCT-binding factor 1 OBF-1 BOB-1 OCA-B Q16633 Hs.654525 OBF1_HUMAN 2833276 Homo sapiens (Human) 256 MLWQKPTAPEQAPAPARPYQGVRVKEPVKELLRRKRGHASSGAAPAPTAVVLPHQPLATYTTVGPSCLDMEGSVSAVTEEAALCAGWLSQPTPATLQPLAPWTPYTEYVPHEAVSCPYSADMYVQPVCPSYTVVGPSSVLTYASPPLITNVTTRSSATPAVGPPLEGPEHQAPLTYFPWPQPLSTLPTSTLQYQPPAPALPGPQFVQLPISIPEPVLQDMEDPRRAASSLTIDKLLLEEEDSDAYALNHTLSVEGF Disordered - Extended 1 15 MLWQKPTAPEQAPAP Complex Engineered Fragment 1CQTI Function arises from the disordered state Molecular assembly Protein-DNA binding Protein-protein binding X-ray crystallography Paper 10541551 Chasman D, Cepek K, Sharp PA, Pabo CO 1999 Genes Dev 13 20 2650-7 Disordered - Extended 1 16 MLWQKPTAPEQAPAPA Complex Engineered Fragment 1CQTJ Function arises from the disordered state Molecular assembly Protein-DNA binding Protein-protein binding X-ray crystallography PDB 10541551 Chasman D, Cepek K, Sharp PA, Pabo CO 1999 Genes Dev 13 20 2650-7 Disordered - Extended 38 44 HASSGAA Complex Engineered Fragment 1CQTI Function arises from the disordered state Molecular assembly Protein-DNA binding Protein-protein binding X-ray crystallography Paper 10541551 Chasman D, Cepek K, Sharp PA, Pabo CO 1999 Genes Dev 13 20 2650-7 Disordered - Extended 39 44 ASSGAA Complex Engineered Fragment 1CQTJ Function arises from the disordered state Molecular assembly Protein-DNA binding Protein-protein binding X-ray crystallography Paper 10541551 Chasman D, Cepek K, Sharp PA, Pabo CO 1999 Genes Dev 13 20 2650-7 DNA fragmentation factor subunit alpha [Isoform DFF45] DFFA_HUMAN DNA fragmentation factor 45 kDa subunit DFF-45 Inhibitor of CAD ICAD O00273-1 Hs.484782 DFFA_HUMAN 2810997 Homo sapiens (Human) 331 MEVTGDAGVPESGEIRTLKPCLLRRNYSREQHGVAASCLEDLRSKACDILAIDKSLTPVTLVLAEDGTIVDDDDYFLCLPSNTKFVALASNEKWAYNNSDGGTAWISQESFDVDETDSGAGLKWKNVARQLKEDLSSIILLSEEDLQMLVDAPCSDLAQELRQSCATVQRLQHTLQQVLDQREEVRQSKQLLQLYLQALEKEGSLLSKQEESKAAFGEEVDAVDTGISRETSSDVALASHILTALREKQAPELSLSSQDLELVTKEDPKALAVALNWDIKKTETVQEACERELALRLQQTQSLHSLRSISASKASPPGDLQNPKRARQDPT Disordered 1 116 MEVTGDAGVPESGEIRTLKPCLLRRNYSREQHGVAASCLEDLRSKACDILAIDKSLTPVTLVLAEDGTIVDDDDYFLCLPSNTKFVALASNEKWAYNNSDGGTAWISQESFDVDET Fragment Function arises via a disorder to order transition Molecular assembly Protein-protein binding Circular dichroism (CD) spectroscopy, near-UV 6 phosphate buffer 20 sodium chloride 50 Nuclear magnetic resonance (NMR) 296 6 DTT 5 phosphate buffer 20 sodium chloride in D2O ( 1 vol/vol) 50 sodium chloride in water (9 vol/vol) 50 Paper 11371636 Zhou P, Lugovskoy AA, McCarty JS, Li P, Wagner G 2001 Proc Natl Acad Sci U S A 98 11 6051-6055 This fragment is disordered in solution and becomes ordered when it interacts with DFF40. Stathmin STMN1_HUMAN Phosphoprotein p19 pp19 Leukemia-associated phosphoprotein p18 Proliferation-related phosphoprotein p18 Oncoprotein 18 Op18 pp17 Prosolin Metablastin Protein Pr22 P16949 Hs.209983 STMN1_HUMAN 134973 Homo sapiens (Human) 149 MASSDIQVKELEKRASGQAFELILSPRSKESVPEFPLSPPKKKDLSLEEIQKKLEAAEERRKSHEAEVLKQLAEKREHEKEVLQKAIEENNNFSKMAEEKLTHKMEANKENREAQMAAKLERLREKDKHIEEVRKNKESKDPADETEAD Disordered 1 149 MASSDIQVKELEKRASGQAFELILSPRSKESVPEFPLSPPKKKDLSLEEIQKKLEAAEERRKSHEAEVLKQLAEKREHEKEVLQKAIEENNNFSKMAEEKLTHKMEANKENREAQMAAKLERLREKDKHIEEVRKNKESKDPADETEAD Native Function arises via a disorder to order transition Molecular assembly Protein-protein binding Nuclear magnetic resonance (NMR) 296 6.8 Circular dichroism (CD) spectroscopy, far-UV 6.8 EGTA 1 GTP 1 MgCl2 1 PIPES-KOH 8 Nuclear magnetic resonance (NMR) 296 7.5 Circular dichroism (CD) spectroscopy, far-UV 7.5 EGTA 1 GTP 1 MgCl2 1 PIPES-KOH 8 Paper 12860982 Honnappa S, Cutting B, Jahnke W, Seelig J, Steinmetz MO 2003 J Biol Chem 278 40 38926-38934 10675326 Steinmetz MO, Kammerer RA, Jahnke W, Goldie KN, Lustig A, van Oostrum J 2000 Embo J 19 4 572-80 pH had little to no effect upon the disordered regions of this protein. Temperature however, did play a factor in measurement of the disordered regions. At lower temperatures, such as 5◦C, this protein was found to be extensively helical. Transcription factor 7-like 2 TF7L2_HUMAN HMG box transcription factor 4 T-cell-specific transcription factor 4 TCF-4 hTCF-4 T7L2 Q9NQB0 Hs.593995 TF7L2_HUMAN 29337146 Homo sapiens (Human) 619 MPQLNGGGGDDLGANDELISFKDEGEQEEKSSENSSAERDLADVKSSLVNESETNQNSSSDSEAERRPPPRSESFRDKSRESLEEAAKRQDGGLFKGPPYPGYPFIMIPDLTSPYLPNGSLSPTARTLHFQSGSTHYSAYKTIEHQIAVQYLQMKWPLLDVQAGSLQSRQALKDARSPSPAHIVSNKVPVVQHPHHVHPLTPLITYSNEHFTPGNPPPHLPADVDPKTGIPRPPHPPDISPYYPLSPGTVGQIPHPLGWLVPQQGQPVYPITTGGFRHPYPTALTVNASMSRFPPHMVPPHHTLHTTGIPHPAIVTPTVKQESSQSDVGSLHSSKHQDSKKEEEKKKPHIKKPLNAFMLYMKEMRAKVVAECTLKESAAINQILGRRWHALSREEQAKYYELARKERQLHMQLYPGWSARDNYGKKKKRKRDKQPGETNEHSECFLNPCLSLPPITDLSAPKKCRARFGLDQQNNWCGPCRRKKKCVRYIQGEGSCLSPPSSDGSLLDSPPPSPNLLGSPPRDAKSQTEQTQPLSLSLKPDPLAHLSMMPPPPALLLAEATHKASALCPNGALDLPPAALQPAAPSSSIAQPSTSSLHSHSSLAGTQPQPLSLVTKSLE Disordered catenin-binding domain 1 56 MPQLNGGGGDDLGANDELISFKDEGEQEEKSSENSSAERDLADVKSSLVNESETNQ Native 1JPWD Function arises via a disorder to order transition Molecular recognition effectors Molecular assembly Transactivation (transcriptional activation) Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV Paper 11237626 Knapp S, Zamai M, Volpi D, Nardese V, Avanzi N, Breton J, Plyte S, Flocco M, Marconi M, Isacchi A, Caiolfa VR 2001 J Mol Biol 306 5 1179-1189 11713476 Poy F, Lepourcelet M, Shivdasani RA, Eck MJ 2001 Nat Struct Biol 8 12 1053-1057 In the PDB file, the disorder to order transition upon binding with beta-catenin can be seen: residues 13-25 and 40-50 form alpha helicies upon binding to the armadillo repeats of catenin. Fe(3+)-pyochelin receptor FPTA_PSEAE Fe(III)-pyochelin receptor P42512 FPTA_PSEAE 1169730 Pseudomonas aeruginosa 720 MKTETKVIKGRQGIARNRHTPLCLGLLLALSPLAAAVADARKDGETELPDMVISGESTSATQPPGVTTLGKVPLKPRELPQSASVIDHERLEQQNLFSLDEAMQQATGVTVQPFQLLTTAYYVRGFKVDSFELDGVPALLGNTASSPQDMAIYERVEILRGSNGLLHGTGNPAATVNLVRKRPQREFAASTTLSAGRWDRYRAEVDVGGPLSASGNVRGRAVAAYEDRDYFYDVADQGTRLLYGVTEFDLSPDTLLTVGAQYQHIDSITNMAGVPMAKDGSNLGLSRDTYLDVDWDRFKWDTYRAFGSLEQQLGGGWKGKVSAEYQEADSRLRYAGSFGAIDPQTGDGGQLMGAAYKFKSIQRSLDANLNGPVRLFGLTHELLGGVTYAQGETRQDTARFLNLPNTPVNVYRWDPHGVPRPQIGQYTSPGTTTTTQKGLYALGRIKLAEPLTLVVGGRESWWDQDTPATRFKPGRQFTPYGGLIWDFARDWSWYVSYAEVYQPQADRQTWNSEPLSPVEGKTYETGIKGELADGRLNLSLAAFRIDLENNPQEDPDHPGPPNNPFYISGGKVRSQGFELEGTGYLTPYWSLSAGYTYTSTEYLKDSQNDSGTRYSTFTPRHLLRLWSNYDLPWQDRRWSVGGGLQAQSDYSVDYRGVSMRQGGYALVNMRLGYKIDEHWTAAVNVNNLFDRTYYQSLSNPNWNNRYGEPRSFNVSLRGAF Disordered 38 55 ADARKDGETELPDMVISG Complex Function arises from the disordered state Molecular assembly Substrate/ligand binding X-ray crystallography ethylene glycol 25% (v/v) (NH4)2SO4 0.15 PEG 10,000 6% (w/v) Sodium acetate buffer pH 4.6 0.1 Paper 16139844 Cobessi D, Celia H, Pattus F 2005 J Mol Biol 352 4 893-904 Disordered Loop L8 551 568 PQEDPDHPGPPNNPFYIS Complex Substrate/ligand binding X-ray crystallography ethylene glycol 25% (v/v) (NH4)2SO4 0.15 PEG 10,000 6% (w/v) Sodium acetate buffer pH 4.6 0.1 Paper 16139844 Cobessi D, Celia H, Pattus F 2005 J Mol Biol 352 4 893-904 Disordered Loop L7 504 513 QADRQTWNSE Complex Substrate/ligand binding X-ray crystallography ethylene glycol 25% (v/v) (NH4)2SO4 0.15 PEG 10,000 6% (w/v) Sodium acetate buffer pH 4.6 0.1 Paper 16139844 Cobessi D, Celia H, Pattus F 2005 J Mol Biol 352 4 893-904 RNA polymerase II subunit A C-terminal domain phosphatase CTDP1_HUMAN EC=3.1.3.16 TFIIF-associating CTD phosphatase Q9Y5B0 Hs.465490 CTDP1_HUMAN 46396052 Homo sapiens (Human) 961 MEVPAAGRVPAEGAPTAAVAEVRCPGPAPLRLLEWRVAAGAAVRIGSVLAVFEAAASAQSAGASQSRVASGGCVRPARPERRLRSERAGVVRELCAQPGQVVAPGAVLVRLEGCSHPVVMKGLCAECGQDLTQLQSKNGKQQVPLSTATVSMVHSVPELMVSSEQAEQLGREDQQRLHRNRKLVLMVDLDQTLIHTTEQHCQQMSNKGIFHFQLGRGEPMLHTRLRPHCKDFLEKIAKLYELHVFTFGSRLYAHTIAGFLDPEKKLFSHRILSRDECIDPFSKTGNLRNLFPCGDSMVCIIDDREDVWKFAPNLITVKKYVYFQGTGDMNAPPGSRESQTRKKVNHSRGTEVSEPSPPVRDPEGVTQAPGVEPSNGLEKPARELNGSEAATPRDSPRPGKPDERDIWPPAQAPTSSQELAGAPEPQGSCAQGGRVAPGQRPAQGATGTDLDFDLSSDSESSSESEGTKSSSSASDGESEGKRGRQKPKAAPEGAGALAQGSSLEPGRPAAPSLPGEAEPGAHAPDKEPELGGQEEGERDGLCGLGNGCADRKEAETESQNSELSGVTAGESLDQSMEEEEEEDTDEDDHLIYLEEILVRVHTDYYAKYDRYLNKEIEEAPDIRKIVPELKSKVLADVAIIFSGLHPTNFPIEKTREHYHATALGAKILTRLVLSPDAPDRATHLIAARAGTEKVLQAQECGHLHVVNPDWLWSCLERWDKVEEQLFPLRDDHTKAQRENSPAAFPDREGVPPTALFHPMPVLPKAQPGPEVRIYDSNTGKLIRTGARGPPAPSSSLPIRQEPSSFRAVPPPQPQMFGEELPDAQDGEQPGPSRRKRQPSMSETMPLYTLCKEDLESMDKEVDDILGEGSDDSDSEKRRPEEQEEEPQPRKPGTRRGADARAPASSERSAAGGRGPRGHKRKLNEEDAASESSRESSNEDEGSSSEADEMAKALEAELNDLM Disordered cterFCP 879 961 PEEQEEEPQPRKPGTRRGADARAPASSERSAAGGRGPRGHKRKLNEEDAASESSRESSNEDEGSSSEADEMAKALEAELNDLM Engineered Fragment Function arises via a disorder to order transition Molecular assembly Protein-protein binding Paper 12732728 Nguyen BD, Abbott KL, Potempa K, Kobor MS, Archambault J, Greenblatt J, Legault P, Omichinski JG 2003 Proc Natl Acad Sci U S A 100 10 5688-93 Protease A inhibitor 3 IPA3_YEAST Proteinase inhibitor I(A)3 Saccharopepsin inhibitor Proteinase yscA-inhibitor P01094 IPA3_YEAST 124811 Saccharomyces cerevisiae (Baker's yeast) 68 MNTDQQKVSEIFQSSKEKLQGDAKVVSDAFKKMASQDKDGKTTDADESEKHNYQEQYNKLKGAGHKKE Disordered - Extended 33 68 MASQDKDGKTTDADESEKHNYQEQYNKLKGAGHKKE 1DP5B Paper 10655612 Li M, Phylip LH, Lees WE, Winther JR, Dunn BM, Wlodawer A, Kay J, Gustchina A 2000 Nat Struct Biol 7 2 113-7 Salt-mediated killer protoxin 1 TOXK_PICFA Salt-mediated killer toxin 1 alpha chain [cleavage product 1] SMK toxin alpha chain Salt-mediated killer toxin 1 gamma chain [cleavage product 2] SMK toxin gamma chain Salt-mediated killer toxin 1 beta chain [cleavage product 3] SMK toxin beta chain P19972 TOXK_PICFA 18266832 Pichia farinosa (Yeast) 222 MRKETLIGLAFITANVIAWSLRWRMQKSTTIAAIAGCSGAATFGGLAGGIVGCIAAGILAILQGFEVNWHNGGGGDRSNPVKRSSDSFSIVNHNGEKVDSYAHLVPGKVGKVIIDNIELSAIRYANNHTSLGYHFTSDGSGPAARGEATTIWGVGADEAIDKGTPSKNDLQNMSADLAKNGFKGHQGVACSTVKDGNKDVYMIKFSLAGGSNDPGGSPCSDD Previous entry DP00180 has been split into polyprotein entry DP00180 and cleavage product 3 entry DP00180_C003. Salt-mediated killer toxin 1 beta chain TOXK_PICFA SMK toxin beta chain cleavage product 3 of Salt-mediated killer protoxin 1 P19972 TOXK_PICFA 18266832 Pichia farinosa (Yeast) 77 GEATTIWGVGADEAIDKGTPSKNDLQNMSADLAKNGFKGHQGVACSTVKDGNKDVYMIKFSLAGGSNDPGGSPCSDD Disordered SMK toxin beta chain 1 77 GEATTIWGVGADEAIDKGTPSKNDLQNMSADLAKNGFKGHQGVACSTVKDGNKDVYMIKFSLAGGSNDPGGSPCSDD Native Function arises via a disorder to order transition Molecular assembly Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV 298 7 Paper 9089808 Suzuki C, Kashiwagi T, Tsuchiya F, Kunishima N, Morikawa K, Nikkuni S, Arata Y 1997 Protein Eng 10 2 99-101 Previous entry DP00180 has been split into polyprotein entry DP00180 and cleavage product 3 entry DP00180_C003. DNA-directed RNA polymerase II subunit RPB1 RPB1_MOUSE EC 2.7.7.6 DNA-directed RNA polymerase II subunit A DNA-directed RNA polymerase III largest subunit P08775 Mm.16533 RPB1_MOUSE 133327 Mus musculus (Mouse) 1970 MHGGGPPSGDSACPLRTIKRVQFGVLSPDELKRMSVTEGGIKYPETTEGGRPKLGGLMDPRQGVIERTGRCQTCAGNMTECPGHFGHIELAKPVFHVGFLVKTMKVLRCVCFFCSKLLVDSNNPKIKDILAKSKGQPKKRLTHVYDLCKGKNICEGGEEMDNKFGVEQPEGDEDLTKEKGHGGCGRYQPRIRRSGLELYAEWKHVNEDSQEKKILLSPERVHEIFKRISDEECFVLGMEPRYARPEWMIVTVLPVPPLSVRPAVVMQGSARNQDDLTHKLADIVKINNQLRRNEQNGAAAHVIAEDVKLLQFHVATMVDNELPGLPRAMQKSGRPLKSLKQRLKGKEGRVRGNLMGKRVDFSARTVITPDPNLSIDQVGVPRSIAANMTFAEIVTPFNIDRLQELVRRGNSQYPGAKYIIRDNGDRIDLRFHPKPSDLHLQTGYKVERHMCDGDIVIFNRQPTLHKMSMMGHRVRILPWSTFRLNLSVTTPYNADFDGDEMNLHLPQSLETRAEIQELAMVPRMIVTPQSNRPVMGIVQDTLTAVRKFTKRDVFLERGEVMNLLMFLSTWDGKVPQPAILKPRPLWTGKQIFSLIIPGHINCIRTHSTHPDDEDSGPYKHISPGDTKVVVENGELIMGILCKKSLGTSAGSLVHISYLEMGHDITRLFYSNIQTVINNWLLIEGHTIGIGDSIADSKTYQDIQNTIKKAKQDVIEVIEKAHNNELEPTPGNTLRQTFENQVNRILNDARDKTGSSAQKSLSEYNNFKSMVVSGAKGSKINISQVIAVVGQQNVEGKRIPFGFKHRTLPHFIKDDYGPESRGFVENSYLAGLTPTEFFFHAMGGREGLIDTAVKTAETGYIQRRLIKSMESVMVKYDATVRNSINQVVQLRYGEDGLAGESVEFQNLATLKPSNKAFEKKFRFDYTNERALRRTLQEDLVKDVLSNAHIQNELEREFERMREDREVLRVIFPTGDSKVVLPCNLLRMIWNAQKIFHINPRLPSDLHPIKVVEGVKELSKKLVIVNGDDPLSRQAQENATLLFNIHLRSTLCSRRMAEEFRLSGEAFDWLLGEIESKFNQAIAHPGEMVGALAAQSLGEPATQMTLNTFHYAGVSAKNVTLGVPRLKELINISKKPKTPSLTVFLLGQSARDAERAKDILCRLEHTTLRKVTANTAIYYDPNPQSTVVAEDQEWVNVYYEMPDFDVARISPWLLRVELDRKHMTDRKLTMEQIAEKINAGFGDDLNCIFNDDNAEKLVLRIRIMNSDENKMQEEEEVVDKMDDDVFLRCIESNMLTDMTLQGIEQISKVYMHLPQTDNKKKIIITEDGEFKALQEWILETDGVSLMRVLSEKDVDPVRTTSNDIVEIFTVLGIEAVRKALERELYHVISFDGSYVNYRHLALLCDTMTCRGHLMAITRHGVNRQDTGPLMKCSFEETVDVLMEAAAHGESDPMKGVSENIMLGQLAPAGTGCFDLLLDAEKCKYGMEIPTNIPGLGAAGPTGMFFGSAPSPMGGISPAMTPWNQGATPAYGAWSPSVGSGMTPGAAGFSPSAASDASGFSPGYSPAWSPTPGSPGSPGPSSPYIPSPGGAMSPSYSPTSPAYEPRSPGGYTPQSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPNYTPTSPSYSPTSPSYSPTSPNYTPTSPNYSPTSPSYSPTSPSYSPTSPSYSPSSPRYTPQSPTYTPSSPSYSPSSPSYSPTSPKYTPTSPSYSPSSPEYTPASPKYSPTSPKYSPTSPKYSPTSPTYSPTTPKYSPTSPTYSPTSPVYTPTSPKYSPTSPTYSPTSPKYSPTSPTYSPTSPKGSTYSPTSPGYSPTSPTYSLTSPAISPDDSDEEN Disordered 1686 1741 SPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSY Fragment Native Relationship to function unknown Unknown Unknown Circular dichroism (CD) spectroscopy, far-UV water Paper 10704311 Bienkiewicz EA, Moon Woody A, Woody RW 2000 J Mol Biol 297 1 119-33 The first 8 repeats of SPTSPSY that make up this region are essential. Disordered CTD 1592 1959 SYSPTSPAYEPRSPGGYTPQSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPNYTPTSPSYSPTSPSYSPTSPNYTPTSPNYSPTSPSYSPTSPSYSPTSPSYSPSSPRYTPQSPTYTPSSPSYSPSSPSYSPTSPKYTPTSPSYSPSSPEYTPASPKYSPTSPKYSPTSPKYSPTSPTYSPTTPKYSPTSPTYSPTSPVYTPTSPKYSPTSPTYSPTSPKYSPTSPTYSPTSPKGSTYSPTSPGYSPTSPTYSLTSP Circular dichroism (CD) spectroscopy, far-UV water Paper 10704311 Bienkiewicz EA, Moon Woody A, Woody RW 2000 J Mol Biol 297 1 119-33 Major capsid protein VP1 VP1_SV40 Major structural protein VP1 P03087-1 VP1_SV40 215274111 Simian virus 40 (SV40) 362 MAPTKRKGSCPGAAPKKPKEPVQVPKLVIKGGIEVLGVKTGVDSFTEVECFLNPQMGNPDEHQKGLSKSLAAEKQFTDDSPDKEQLPCYSVARIPLPNINEDLTCGNILMWEAVTVKTEVIGVTAMLNLHSGTQKTHENGAGKPIQGSNFHFFAVGGEPLELQGVLANYRTKYPAQTVTPKNATVDSQQMNTDHKAVLDKDNAYPVECWVPDPSKNENTRYFGTYTGGENVPPVLHITNTATTVLLDEQGVGPLCKADSLYVSAVDICGLFTNTSGTQQWKGLPRYFKITLRKRSVKNPYPISFLLSDLINRRTQRVDGQPMIGMSSQVEEVRVYEDTEELPGDPDMIRYIDEFGQTTTRMQ Disordered regions need to be checked. Ferripyoverdine receptor FPVA_PSEAE P48632 FPVA_PSEAE 12230910 Pseudomonas aeruginosa 815 MPAPHGLSPLSKAFLMRRAFQRRILPHSLAMALSLPLAGYVQAQEVEFDIPPQALGSALQEFGRQADIQVLYRPEEVRNKRSSAIKGKLEPNQAITELLRGTGASVDFQGNAITISVAEAADSSVDLGATMITSNQLGTITEDSGSYTPGTIATATRLVLTPRETPQSITVVTRQNMDDFGLNNIDDVMRHTPGITVSAYDTDRNNYYARGFSINNFQYDGIPSTARNVGYSAGNTLSDMAIYDRVEVLKGATGLLTGAGSLGATINLIRKKPTHEFKGHVELGAGSWDNYRSELDVSGPLTESGNVRGRAVAAYQDKHSFMDHYERKTSVYYGILEFDLNPDTMLTVGADYQDNDPKGSGWSGSFPLFDSQGNRNDVSRSFNNGAKWSSWEQYTRTVFANLEHNFANGWVGKVQLDHKINGYHAPLGAIMGDWPAPDNSAKIVAQKYTGETKSNSLDIYLTGPFQFLGREHELVVGTSASFSHWEGKSYWNLRNYDNTTDDFINWDGDIGKPDWGTPSQYIDDKTRQLGSYMTARFNVTDDLNLFLGGRVVDYRVTGLNPTIRESGRFIPYVGAVYDLNDTYSVYASYTDIFMPQDSWYRDSSNKLLEPDEGQNYEIGIKGEYLDGRLNTSLAYFEIHEENRAEEDALYNSKPTNPAITYAYKGIKAKTKGYEAEISGELAPGWQVQAGYTHKIIRDDSGKKVSTWEPQDQLSLYTSYKFKGALDKLTVGGGARWQGKSWQMVYNNPRSRWEKFSQEDYWLVDLMARYQITDKLSASVNVNNVFDKTYYTNIGFYTSASYGDPRNLMFSTRWDF Disordered - Extended TonB box 129 134 ATMITS Complex Function arises from the disordered state Molecular assembly Protein-protein binding X-ray crystallography protein 1-4 ul 5 C8E5 0.75% PEG 4000 13-16% (w/v) Magnesium sulfate 50 ethylene glycol 20-25% Sodium citrate buffer pH 5.6 0.1 Paper 15733922 Cobessi D, Celia H, Folschweiller N, Schalk IJ, Abdallah MA, Pattus F 2005 J Mol Biol 347 1 121-34 Vitamin D3 receptor VDR_HUMAN VDR 1,25-dihydroxyvitamin D3 receptor Nuclear receptor subfamily 1 group I member 1 P11473 Hs.524368 VDR_HUMAN 137617 Homo sapiens (Human) 427 MEAMAASTSLPDPGDFDRNVPRICGVCGDRATGFHFNAMTCEGCKGFFRRSMKRKALFTCPFNGDCRITKDNRRHCQACRLKRCVDIGMMKEFILTDEEVQRKREMILKRKEEEALKDSLRPKLSEEQQRIIAILLDAHHKTYDPTYSDFCQFRPPVRVNDGGGSHPSRPNSRHTPSFSGDSSSSCSDHCITSSDMMDSSSFSNLDLSEEDSDDPSVTLELSQLSMLPHLADLVSYSIQKVIGFAKMIPGFRDLTSEDQIVLLKSSAIEVIMLRSNESFTMDDMSWTCGNQDYKYRVSDVTKAGHSLELIEPLIKFQVGLKKLNLHEEEHVLLMAICIVSPDRPGVQDAALIEAIQDRLSNTLQTYIRCRHPPPGSHLLYAKMIQKLADLRSLNEEHSKQYRCLSFQPECSMKLTPLVLEVFGNEIS Disordered 424 427 NEIS Fragment Native Relationship to function unknown Unknown Unknown Paper 10678179 Rochel N, Wurtz JM, Mitschler A, Klaholz B, Moras D 2000 Mol Cell 5 1 173-9 Experimental sequence extended from 410 to 1202 of the SwissProt sequence. Late embryogenesis-abundant protein P93165_SOYBN Em protein P93165 Gma.10 P93165_SOYBN 75101067 Glycine max (soybean) 105 MASRQNNKQELDERARQGETVVPGGTGGKSLEAQQHLAEGRSKGGQTRKEQLGTEGYQEMGRKGGLSTVDKSGEERAQEEGIGIDESKFRTGNNKNQNQNEDQDK Disordered - Extended 1 105 MASRQNNKQELDERARQGETVVPGGTGGKSLEAQQHLAEGRSKGGQTRKEQLGTEGYQEMGRKGGLSTVDKSGEERAQEEGIGIDESKFRTGNNKNQNQNEDQDK Native Function arises from the disordered state Unknown Unknown Circular dichroism (CD) spectroscopy, far-UV 0.1-cm path-length 7.7 microM protein solution in 50 mM buffer Na-phosphate pH 5, 8, and 9 temperature from 10°C to 80°C Paper 11891239 Soulages JL, Kim K, Walters C, Cushman JC 2002 Plant Physiol 128 3 822-32 Late embryogenesis abundant protein 1 LEA1_APHAV AavLea1 Q95V77 LEA1_APHAV 24418520 Aphelenchus avenae (Mycophagous nematode worm) 143 MSSQQNQNRQGEQQEQGYMEAAKEKVVNAWESTKETLSSTAQAAAEKTAEFRDSAGETIRDLTGQAQEKGQEFKERAGEKAEETKQRAGEKMDETKQRAGEMRENAGQKMEEYKQQGKGKAEELRDTAAEKLHQAGEKVKGRD Disordered 1 143 MSSQQNQNRQGEQQEQGYMEAAKEKVVNAWESTKETLSSTAQAAAEKTAEFRDSAGETIRDLTGQAQEKGQEFKERAGEKAEETKQRAGEKMDETKQRAGEMRENAGQKMEEYKQQGKGKAEELRDTAAEKLHQAGEKVKGRD Native Function arises from the disordered state Unknown Unknown Circular dichroism (CD) spectroscopy, far-UV 7 0.1 and 2 mg/ml of AavLEA1 in 50 mM phosphate buffer 0.1-cm path length Fluorescence polarization/anisotropy 0.1 and 0.5 mg/ml AavLEA1 Excitation wavelength of 280 nm Scan rate of 60 nm/min Slit widths of 2.5 nm Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) 298 Protein 15 mg/ml Paper 12569097 Goyal K, Tisi L, Basran A, Browne J, Burnell A, Zurdo J, Tunnacliffe A 2003 J Biol Chem 278 15 12977-84 Major prion protein PRIO_MESAU PrP PrP27-30 PrP33-35C P04273 PRIO_MESAU 130913 Mesocricetus auratus (Golden hamster) 254 MANLSYWLLALFVAMWTDVGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGTWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMMHFGNDWEDRYYRENMNRYPNQVYYRPVDQYNNQNNFVHDCVNITIKQHTVTTTTKGENFTETDIKIMERVVEQMCTTQYQKESQAYYDGRRSSAVLFSSPPVILLISFLIFLMVG Disordered - Extended 90 124 GQGGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGG Fragment Native Function arises from the disordered state Unknown Unknown Nuclear magnetic resonance (NMR) 5.5 1H2p 90% 2H2O 10% sodium acetate-d5 buffer 20 sodium azide 0.005 % Paper 9391046 Donne DG, Viles JH, Groth D, Mehlhorn I, James TL, Cohen FE, Prusiner SB, Wright PE, Dyson HJ 1997 Proc Natl Acad Sci U S A 94 25 13452-7 Disordered PrP(29-231) 29 124 GGWNTGGSRYPGQGSPGGNRYPPQGGGTWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGG Fragment Native Function arises from the disordered state Unknown Unknown Nuclear magnetic resonance (NMR) Paper 9391046 Donne DG, Viles JH, Groth D, Mehlhorn I, James TL, Cohen FE, Prusiner SB, Wright PE, Dyson HJ 1997 Proc Natl Acad Sci U S A 94 25 13452-7 Oxygen-evolving enhancer protein 1, chloroplastic PSBO_SPIOL OEE1 33 kDa subunit of oxygen evolving system of photosystem II OEC 33 kDa subunit 33 kDa thylakoid membrane protein Manganese stabilizing protein P12359 PSBO_SPIOL 131386 Spinacea oleracea (Spinach) 332 MAASLQASTTFLQPTKVASRNTLQLRSTQNVCKAFGVESASSGGRLSLSLQSDLKELANKCVDATKLAGLALATSALIASGANAEGGKRLTYDEIQSKTYLEVKGTGTANQCPTVEGGVDSFAFKPGKYTAKKFCLEPTKFAVKAEGISKNSGPDFQNTKLMTRLTYTLDEIEGPFEVSSDGTVKFEEKDGIDYAAVTVQLPGGERVPFLFTIKQLVASGKPESFSGDFLVPSYRGSSFLDPKGRGGSTGYDNAVALPAGGRGDEEELQKENNKNVASSKGTITLSVTSSKPETGEVIGVFQSLQPSDTDLGAKVPKDVKIEGVWYAQLEQQ Disordered 85 332 EGGKRLTYDEIQSKTYLEVKGTGTANQCPTVEGGVDSFAFKPGKYTAKKFCLEPTKFAVKAEGISKNSGPDFQNTKLMTRLTYTLDEIEGPFEVSSDGTVKFEEKDGIDYAAVTVQLPGGERVPFLFTIKQLVASGKPESFSGDFLVPSYRGSSFLDPKGRGGSTGYDNAVALPAGGRGDEEELQKENNKNVASSKGTITLSVTSSKPETGEVIGVFQSLQPSDTDLGAKVPKDVKIEGVWYAQLEQQ Function arises from the disordered state Molecular assembly Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV 6 KH2PO4 10 Size exclusion/gel filtration chromatography Paper 9890923 Lydakis-Simantiris N, Hutchison RS, Betts SD, Barry BA, Yocum CF 1999 Biochemistry 38 1 404-14 10569936 Lydakis-Simantiris N, Betts SD, Yocum CF 1999 Biochemistry 38 47 15528-35 Also known as PsbO, OEE33, or 33 kDa extrinsic polypeptide of photosystem II. This extrinsic subunit is found in photosystem II of prokaryotes and eukaryotes. It is required to maintain the stability of the tetranuclear Mn cluster that catalyzes water oxidation. A low resolution (3.5 A) structure of the bound subunit in cyanobacterial photosystem II is available (PDB 1S5L; manganese stabilizing protein is labeled PsbO in the structure). Protein Nef NEF_HV112 Negative factor F-protein 3'ORF C-terminal core protein [cleavage product 1] P04324 NEF_HV112 128018 Human immunodeficiency virus type 1 (isolate PCV12 group M subtype B) (HIV-1) 206 MGGKWSKSSVVGWPAVRERMRRAEPAADGVGAASRDLEKHGAITSSNTAANNAACAWLEAQEEEKVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPGPGIRYPLTFGWCYKLVPVEPEKLEEANKGENTSLLHPVSLHGMDDPEREVLEWRFDSRLAFHHVARELHPEYFKNC Disordered 42 57 AITSSNTAANNAACAW Fragment Native Relationship to function unknown Unknown Unknown Paper 10339411 Geyer M, Munte CE, Schorr J, Kellner R, Kalbitzer HR 1999 J Mol Biol 289 1 123-38 The experimental protein consisted of residues 2 - 57 of SwissProt entry P04324. Ordered 17 22 RERMRR Fragment Native Paper 10339411 Geyer M, Munte CE, Schorr J, Kellner R, Kalbitzer HR 1999 J Mol Biol 289 1 123-38 The experimental protein consisted of residues 2 - 57 of SwissProt entry P04324. Disordered 23 34 AEPAADGVGAAS Fragment Native Relationship to function unknown Unknown Unknown Paper 10339411 Geyer M, Munte CE, Schorr J, Kellner R, Kalbitzer HR 1999 J Mol Biol 289 1 123-38 The experimental protein consisted of residues 2 - 57 of SwissProt entry P04324. Ordered 35 41 RDLEKHG Fragment Native Paper 10339411 Geyer M, Munte CE, Schorr J, Kellner R, Kalbitzer HR 1999 J Mol Biol 289 1 123-38 The experimental protein consisted of residues 2 - 57 of SwissProt entry P04324. Disordered 2 16 GGKWSKSSVVGWPAV Fragment Native Relationship to function unknown Unknown Unknown Paper 10339411 Geyer M, Munte CE, Schorr J, Kellner R, Kalbitzer HR 1999 J Mol Biol 289 1 123-38 The experimental protein consisted of residues 2 - 57 of SwissProt entry P04324. The disordered region is not found in the C-terminal core protein. Sulfite reductase [NADPH] flavoprotein alpha-component CYSJ_ECOLI SiR-FP EC=1.8.1.2 P38038 CYSJ_ECOLI 109940071 Escherichia coli (strain K12) 598 TTQVPPSALLPLNPEQLARLQAATTDLTPTQLAWVSGYFWGVLNQQPAALAATPAPAAEMPGITIISASQTGNARRVAEALRDDLLAAKLNVKLVNAGDYKFKQIASEKLLIVVTSTQGEGEPPEEAVALHKFLFSKKAPKLENTAFAVFSLGDTSYEFFCQSGKDFDSKLAELGGERLLDRVDADVEYQAAASEWRARVVDALKSRAPVAAPSQSVATGAVNEIHTSPYSKDAPLVASLSVNQKITGRNSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPALVKELVELLWLKGDEPVTVEGKTLPLNEALQWHFELTVNTANIVENYATLTRSETLLPLVGDKAKLQHYAATTPIVDMVRFSPAQLDAEALINLLRPLTPRLYSIASSQAEVENEVHVTVGVVRYDVEGRARAGGASSFLADRVEEEGEVRVFIEHNDNFRLPANPETPVIMIGPGTGIAPFRAFMQQRAADEAPGKNWLFFGNPHFTEDFLYQVEWQRYVKEGVLTRIDLAWSRDQKEKVYVQDKLREQGAELWRWINDGAHIYVCGDANRMAKDVEQALLEVIAEFGGMDTEAADEFLSELRVERRYQRDVY Ordered NADP(H)-binding domain 445 598 RLPANPETPVIMIGPGTGIAPFRAFMQQRAADEAPGKNWLFFGNPHFTEDFLYQVEWQRYVKEGVLTRIDLAWSRDQKEKVYVQDKLREQGAELWRWINDGAHIYVCGDANRMAKDVEQALLEVIAEFGGMDTEAADEFLSELRVERRYQRDVY Fragment 1DDGA 1DDGB 1DDIA Relationship to function unknown Unknown Unknown X-ray crystallography 277 1-4 methyl-pentane-diol 10 ammonium sulfate 2 NADP+ (5mM) 2 SiR-FP60 (15 g/mL) protein 2 Tris-HCl pH 7.0 50 Paper 10860732 Gruez A, Pignol D, Zeghouf M, Coves J, Fontecave M, Ferrer JL, Fontecilla-Camps JC 2000 J Mol Biol 299 1 199-212 Ordered FAD-binding domain 385 444 RLYSIASSQAEVENEVHVTVGVVRYDVEGRARAGGASSFLADRVEEEGEVRVFIEHNDNF Fragment 1DDGA 1DDGB 1DDIA Function arises from the ordered state Molecular recognition effectors Cofactor/heme binding X-ray crystallography 277 1-4 methyl-pentane-diol 10 ammonium sulfate 2 NADP+ (5mM) 2 SiR-FP60 (15 g/mL) protein 2 Tris-HCl pH 7.0 50 Paper 10860732 Gruez A, Pignol D, Zeghouf M, Coves J, Fontecave M, Ferrer JL, Fontecilla-Camps JC 2000 J Mol Biol 299 1 199-212 Ordered connecting domain 280 384 QNDPALVKELVELLWLKGDEPVTVEGKTLPLNEALQWHFELTVNTANIVENYATLTRSETLLPLVGDKAKLQHYAATTPIVDMVRFSPAQLDAEALINLLRPLTP Fragment 1DDGA 1DDGB 1DDIA Relationship to function unknown Molecular assembly Protein-protein binding X-ray crystallography 277 1-4 methyl-pentane-diol 10 ammonium sulfate 2 NADP+ (5mM) 2 SiR-FP60 (15 g/mL) protein 2 Tris-HCl pH 7.0 50 Paper 10860732 Gruez A, Pignol D, Zeghouf M, Coves J, Fontecave M, Ferrer JL, Fontecilla-Camps JC 2000 J Mol Biol 299 1 199-212 Ordered FAD-binding domain 225 279 IHTSPYSKDAPLVASLSVNQKITGRNSEKDVRHIEIDLGDSGLRYQPGDALGVWY Fragment 1DDGA 1DDGB 1DDIA Function arises from the ordered state Molecular recognition effectors Cofactor/heme binding X-ray crystallography 277 1-4 methyl-pentane-diol 10 ammonium sulfate 2 NADP+ (5mM) 2 SiR-FP60 (15 g/mL) protein 2 Tris-HCl pH 7.0 50 Paper 10860732 Gruez A, Pignol D, Zeghouf M, Coves J, Fontecave M, Ferrer JL, Fontecilla-Camps JC 2000 J Mol Biol 299 1 199-212 Disordered FMN binding domain 52 224 ATPAPAAEMPGITIISASQTGNARRVAEALRDDLLAAKLNVKLVNAGDYKFKQIASEKLLIVVTSTQGEGEPPEEAVALHKFLFSKKAPKLENTAFAVFSLGDTSYEFFCQSGKDFDSKLAELGGERLLDRVDADVEYQAAASEWRARVVDALKSRAPVAAPSQSVATGAVNE Fragment 1DDGA 1DDGB 1DDIA Function arises from the disordered state Molecular recognition effectors Cofactor/heme binding Electron transfer X-ray crystallography 277 1-4 methyl-pentane-diol 10 ammonium sulfate 2 NADP+ (5mM) 2 SiR-FP60 (15 g/mL) protein 2 Tris-HCl pH 7.0 50 Paper 10860732 Gruez A, Pignol D, Zeghouf M, Coves J, Fontecave M, Ferrer JL, Fontecilla-Camps JC 2000 J Mol Biol 299 1 199-212 This is the FMN binding domain of this protein. It transfers electrons from the ferredoxin NADP+ reductase (FNR) module to the beta subunit, which contains Fe4S4 and siroheme. The FMN of one molecule binds to the FNR of an adjacent molecule. The flexibility of this region is believed to be important in optimal molecular arrangment during electron transfer. Disordered 55 255 APAAEMPGITIISASQTGNARRVAEALRDDLLAAKLNVKLVNAGDYKFKQIASEKLLIVVTSTQGEGEPPEEAVALHKFLFSKKAPKLENTAFAVFSLGDTSYEFFCQSGKDFDSKLAELGGERLLDRVDADVEYQAAASEWRARVVDALKSRAPVAAPSQSVATGAVNEIHTSPYSKDAPLVASLSVNQKITGRNSEKDV Fragment 1DDGA 1DDGB 1DDIA Function arises from the disordered state Molecular recognition effectors Cofactor/heme binding Electron transfer X-ray crystallography 277 1-4 methyl-pentane-diol 10 ammonium sulfate 2 NADP+ (5mM) 2 SiR-FP60 (15mg/ml) protein 2 Tris-HCl pH 7.0 50 Paper 10860732 Gruez A, Pignol D, Zeghouf M, Coves J, Fontecave M, Ferrer JL, Fontecilla-Camps JC 2000 J Mol Biol 299 1 199-212 Four polymorphs were created for this protein. #1 was used to determine the structure, and was thus used for this entry. Polymorphs 2-4 were analyzed and their structures were also determined. They had no regions of electron density from residues 55-255, and were assumed to be disordered in these regions. The paper by Ostrowski et al. contains the full protein sequence. Plasminogen PLMN_HUMAN EC=3.4.21.7 Plasmin heavy chain A [cleavage product 1] Activation peptide [cleavage product 2] Angiostatin [cleavage product 3] Plasmin heavy chain A, short form [cleavage product 4] Plasmin light chain B [cleavage product 5] P00747 Hs.143436 PLMN_HUMAN 130316 Homo sapiens (Human) 810 MEHKEVVLLLLLFLKSGQGEPLDDYVNTQGASLFSVTKKQLGAGSIEECAAKCEEDEEFTCRAFQYHSKEQQCVIMAENRKSSIIIRMRDVVLFEKKVYLSECKTGNGKNYRGTMSKTKNGITCQKWSSTSPHRPRFSPATHPSEGLEENYCRNPDNDPQGPWCYTTDPEKRYDYCDILECEEECMHCSGENYDGKISKTMSGLECQAWDSQSPHAHGYIPSKFPNKNLKKNYCRNPDRELRPWCFTTDPNKRWELCDIPRCTTPPPSSGPTYQCLKGTGENYRGNVAVTVSGHTCQHWSAQTPHTHNRTPENFPCKNLDENYCRNPDGKRAPWCHTTNSQVRWEYCKIPSCDSSPVSTEQLAPTAPPELTPVVQDCYHGDGQSYRGTSSTTTTGKKCQSWSSMTPHRHQKTPENYPNAGLTMNYCRNPDADKGPWCFTTDPSVRWEYCNLKKCSGTEASVVAPPPVVLLPDVETPSEEDCMFGNGKGYRGKRATTVTGTPCQDWAAQEPHRHSIFTPETNPRAGLEKNYCRNPDGDVGGPWCYTTNPRKLYDYCDVPQCAAPSFDCGKPQVEPKKCPGRVVGGCVAHPHSWPWQVSLRTRFGMHFCGGTLISPEWVLTAAHCLEKSPRPSSYKVILGAHQEVNLEPHVQEIEVSRLFLEPTRKDIALLKLSSPAVITDKVIPACLPSPNYVVADRTECFITGWGETQGTFGAGLLKEAQLPVIENKVCNRYEFLNGRVQSTELCAGHLAGGTDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRFVTWIEGVMRNN Disordered 384 384 S Fragment 1KRNA X-ray crystallography 277 6 1.68 Angstroms 22% PEG in reservoir equilibrated against CAC Buffer 50 PEG 10% concentration stabilized at 10% BASA Paper 15299951 Stec B, Yamano A, Whitlow M, Teeter MM 1997 Acta Crystallogr D Biol Crystallogr 53 Pt 2 169-178 Disordered 389 389 S Fragment 1KRNA X-ray crystallography 277 6 1.68 Angstroms 22% PEG in reservoir equilibrated against CAC Buffer 50 PEG 10% concentration stabilized at 10% BASA Paper 15299951 Stec B, Yamano A, Whitlow M, Teeter MM 1997 Acta Crystallogr D Biol Crystallogr 53 Pt 2 169-178 Disordered 391 391 T Fragment 1KRNA X-ray crystallography 277 6 1.68 Angstroms 22% PEG in reservoir equilibrated against CAC Buffer 50 PEG 10% concentration stabilized at 10% BASA Paper 15299951 Stec B, Yamano A, Whitlow M, Teeter MM 1997 Acta Crystallogr D Biol Crystallogr 53 Pt 2 169-178 This residue is part of the first disordered residue patch on the surface of the protein. Disordered 400 400 S Fragment 1KRNA X-ray crystallography 277 6 1.68 Angstroms 22% PEG in reservoir equilibrated against CAC Buffer 50 PEG 10% concentration stabilized at 10% BASA Paper 15299951 Stec B, Yamano A, Whitlow M, Teeter MM 1997 Acta Crystallogr D Biol Crystallogr 53 Pt 2 169-178 This residue is part of the second disordered residue patch on the surface of the protein. Disordered 402 402 S Fragment 1KRNA X-ray crystallography 277 6 1.68 Angstroms 22% PEG in reservoir equilibrated against CAC Buffer 50 PEG 10% concentration stabilized at 10% BASA Paper 15299951 Stec B, Yamano A, Whitlow M, Teeter MM 1997 Acta Crystallogr D Biol Crystallogr 53 Pt 2 169-178 This residue is part of the second disordered residue patch on the surface of the protein. Disordered 403 403 S Fragment 1KRNA X-ray crystallography 277 6 1.68 Angstroms 22% PEG in reservoir equilibrated against CAC Buffer 50 PEG 10% concentration stabilized at 10% BASA Paper 15299951 Stec B, Yamano A, Whitlow M, Teeter MM 1997 Acta Crystallogr D Biol Crystallogr 53 Pt 2 169-178 This residue is part of the second disordered residue patch on the surface of the protein. Disordered 423 423 M Fragment 1KRNA Function arises via a disorder to order transition X-ray crystallography 277 6 1.68 Angstroms 22% PEG in reservoir equilibrated against CAC Buffer 50 PEG 10% concentration stabilized at 10% BASA Paper 15299951 Stec B, Yamano A, Whitlow M, Teeter MM 1997 Acta Crystallogr D Biol Crystallogr 53 Pt 2 169-178 The carbonyl group of this residue is associated with serine 91 via a strong water-mediated hydrogen bond to the nitrogen atom of the amide group. This residue is part of the second disordered residue patch on the surface of the protein. Disordered 449 449 C Fragment 1KRNA X-ray crystallography 277 6 1.68 Angstroms 22% PEG in reservoir equilibrated against CAC Buffer 50 PEG 10% concentration stabilized at 10% BASA Paper 15299951 Stec B, Yamano A, Whitlow M, Teeter MM 1997 Acta Crystallogr D Biol Crystallogr 53 Pt 2 169-178 Part of a disordered disulfide bridge (with residue 426). Disordered 453 453 K Fragment 1KRNA X-ray crystallography 277 6 1.68 Angstroms 22% PEG in reservoir equilibrated against CAC Buffer 50 PEG 10% concentration stabilized at 10% BASA Paper 15299951 Stec B, Yamano A, Whitlow M, Teeter MM 1997 Acta Crystallogr D Biol Crystallogr 53 Pt 2 169-178 Disordered 443 443 S Fragment 1KRNA X-ray crystallography 277 6 1.68 Angstroms 22% PEG in reservoir equilibrated against CAC Buffer 50 PEG 10% concentration stabilized at 10% BASA Paper 15299951 Stec B, Yamano A, Whitlow M, Teeter MM 1997 Acta Crystallogr D Biol Crystallogr 53 Pt 2 169-178 Disordered 426 426 C Fragment 1KRNA Relationship to function unknown Unknown Unknown Paper 15299951 Stec B, Yamano A, Whitlow M, Teeter MM 1997 Acta Crystallogr D Biol Crystallogr 53 Pt 2 169-178 Part of a disordered disulfide bridge (with residue 449). Some of the disordered residues combine together, forming patches on the surface of the protein, which may be relevant to quaternary assemblage of proteins with kringle domains. Disordered residues lie within the regions corresponding to cleavage products 1, 3, and 4, however, there is no experimental evidence to show that these products are disordered. Kappa-casein CASK_BOVIN Casoxin-C [cleavage product 1] Casoxin-6 [cleavage product 2] Casoxin-A [cleavage product 3] Casoxin-B [cleavage product 4] Casoplatelin [cleavage product 5] P02668 Bt.49421 CASK_BOVIN 115667 Bos taurus (Bovine) 190 MMKSFFLVVTILALTLPFLGAQEQNQEQPIRCEKDERFFSDKIAKYIPIQYVLSRYPSYGLNYYQQKPVALINNQFLPYPYYAKPAAVRSPAQILQWQVLSNTVPAKSCQAQPTTMARHPHPHLSFMAIPPKKNQDKTEIPTINTIASGEPTSTPTTEAVESTVATLEDSPEVIESPPEINTVQVTSTAV Disordered 1 182 MMKSFFLVVTILALTLPFLGAQEQNQEQPIRCEKDERFFSDKIAKYIPIQYVLSRYPSYGLNYYQQKPVALINNQFLPYPYYAKPAAVRSPAQILQWQVLSNTVPAKSCQAQPTTMARHPHPHLSFMAIPPKKNQDKTEIPTINTIASGEPTSTPTTEAVESTVATLEDSPEVIESPPEINT Native Relationship to function unknown Molecular assembly Unknown Raman optical activity Stability at thermal extremes Paper 11784308 Syme CD, Blanch EW, Holt C, Jakes R, Goedert M, Hecht L, Barron LD 2002 Eur J Biochem 269 1 148-56 Disordered 125 129 SFMAI Fragment Relationship to function unknown Unknown Unknown Circular dichroism (CD) spectroscopy, far-UV 295 sodium dodecyl sulfate 0.9 Paper 6402987 Raap J, Kerling KE, Vreeman HJ, Visser S 1983 Arch Biochem Biophys 221 1 117-24 Disordered 124 128 LSFMA Fragment Relationship to function unknown Unknown Unknown Circular dichroism (CD) spectroscopy, far-UV 295 sodium dodecyl sulfate 0.9 Paper 6402987 Raap J, Kerling KE, Vreeman HJ, Visser S 1983 Arch Biochem Biophys 221 1 117-24 Disordered 124 129 LSFMAI Fragment Relationship to function unknown Unknown Unknown Circular dichroism (CD) spectroscopy, far-UV 295 sodium dodecyl sulfate 0.9 Paper 6402987 Raap J, Kerling KE, Vreeman HJ, Visser S 1983 Arch Biochem Biophys 221 1 117-24 Disordered 124 130 LSFMAIP Fragment Relationship to function unknown Unknown Unknown Circular dichroism (CD) spectroscopy, far-UV 295 sodium dodecyl sulfate 0.9 Paper 6402987 Raap J, Kerling KE, Vreeman HJ, Visser S 1983 Arch Biochem Biophys 221 1 117-24 Disordered residues lie within the regions for cleavage products 1 - 5, however, there is no experimental evidence to show that these products are disordered. Beta-lactoglobulin LACB_BOVIN Beta-LG Bos d 5 P02754 Bt.385 LACB_BOVIN 125910 Bos taurus (Cow) 178 MKCLLLALALTCGAQALIVTQTMKGLDIQKVAGTWYSLAMAASDISLLDAQSAPLRVYVEELKPTPEGDLEILLQKWENGECAQKKIIAEKTKIPAVFKIDALNENKVLVLDTDYKKYLLFCMENSAEPEQSLACQCLVRTPEVDDEALEKFDKALKALPMHIRLSFNPTQLEEQCHI Disordered - Molten Globule 1 178 MKCLLLALALTCGAQALIVTQTMKGLDIQKVAGTWYSLAMAASDISLLDAQSAPLRVYVEELKPTPEGDLEILLQKWENGECAQKKIIAEKTKIPAVFKIDALNENKVLVLDTDYKKYLLFCMENSAEPEQSLACQCLVRTPEVDDEALEKFDKALKALPMHIRLSFNPTQLEEQCHI Native Relationship to function unknown Unknown Unknown Circular dichroism (CD) spectroscopy, far-UV 298 1.5 potasium cirate buffer 10 Size exclusion/gel filtration chromatography 277 1.5 HCl-KCl buffer 100 Analytical ultracentrifugation 1.5 HCl-KCl buffer 100 Paper 9141136 Ikeguchi M, Kato S, Shimizu A, Sugai S 1997 Proteins 27 4 567-75 Beta-lactoglobulin has a compact globular structure at neutral pH. Stringent starvation protein B SSPB_ECOLI SspB P0AFZ3 SSPB_ECOLI 84028797 Escherichia coli 165 MDLSQLTPRRPYLLRAFYEWLLDNQLTPHLVVDVTLPGVQVPMEYARDGQIVLNIAPRAVGNLELANDEVRFNARFGGIPRQVSVPLAAVLAIYARENGAGTMFEPEAAYDEDTSIMNDEEASADNETVMSVIDGDKPDHDDDTHPDDEPPQPPRGGRPALRVVK Disordered 111 165 DEDTSIMNDEEASADNETVMSVIDGDKPDHDDDTHPDDEPPQPPRGGRPALRVVK Native Function arises from the disordered state Molecular assembly Entropic chain Flexible linkers/spacers Substrate/ligand binding Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV 298 7.5 1 mm pathlenght 20 microM SspB in 10 mM potassium phosphate Paper 14536075 Wah DA, Levchenko I, Rieckhof GE, Bolon DN, Baker TA, Sauer RT 2003 Mol Cell 12 2 355-63 Non-histone chromosomal protein HMG-17 HMGN2_BOVIN High-mobility group nucleosome-binding domain-containing protein 2 HMG-17 P02313 Bt.1758 HMGN2_BOVIN 189047100 Bos taurus (Bovine) 89 PKRKAEGDAKGDKAKVKDEPQRRSARLSAKPAPPKPEPKPKKAPAKKGEKVPKGKKGKADAGKBGBBPAZBGBAKTBZAZKAEGAGDAK Disordered 1 89 PKRKAEGDAKGDKAKVKDEPQRRSARLSAKPAPPKPEPKPKKAPAKKGEKVPKGKKGKADAGKBGBBPAZBGBAKTBZAZKAEGAGDAK Monomeric Mutant Function arises via a disorder to order transition Molecular assembly Protein-DNA binding Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) 6.8 NaCl 1 Small-angle neutron scattering (SANS) 7 Phosphate buffer 50 Circular dichroism (CD) spectroscopy, far-UV 7.9 NaCl 1 Tris-HCl buffer 20 Paper 565710 Abercrombie BD, Kneale GG, Crane-Robinson C, Bradbury EM, Goodwin GH, Walker JM, Johns EW 1978 Eur J Biochem 84 1 173-7 Calpastatin ICAL_HUMAN Calpain inhibitor Sperm BS-17 component P20810 Hs.436186 ICAL_HUMAN 126302556 Homo sapiens (Human) 708 MNPTETKAIPVSQQMEGPHLPNKKKHKKQAVKTEPEKKSQSTKLSVVHEKKSQEGKPKEHTEPKSLPKQASDTGSNDAHNKKAVSRSAEQQPSEKSTEPKTKPQDMISAGGESVAGITAISGKPGDKKKEKKSLTPAVPVESKPDKPSGKSGMDAALDDLIDTLGGPEETEEENTTYTGPEVSDPMSSTYIEELGKREVTIPPKYRELLAKKEGITGPPADSSKPIGPDDAIDALSSDFTCGSPTAAGKKTEKEESTEVLKAQSAGTVRSAAPPQEKKRKVEKDTMSDQALEALSASLGTRQAEPELDLRSIKEVDEAKAKEEKLEKCGEDDETIPSEYRLKPATDKDGKPLLPEPEEKPKPRSESELIDELSEDFDRSECKEKPSKPTEKTEESKAAAPAPVSEAVSRTSMCSIQSAPPEPATLKGTVPDDAVEALADSLGKKEADPEDGKPVMDKVKEKAKEEDREKLGEKEETIPPDYRLEEVKDKDGKPLLPKESKEQLPPMSEDFLLDALSEDFSGPQNASSLKFEDAKLAAAISEVVSQTPASTTQAGAPPRDTSQSDKDLDDALDKLSDSLGQRQPDPDENKPMGDKVKEKAKAEHRDKLGERDDTIPPEYRHLLDDNGQDKPVKPPTKKSEDSKKPADDQDPIDALSGDLDSCPSTTETSQNTAKDKCKKAASSSKAPKNGGKAKDSAKTTEETSKPKDD Disordered 137 277 AVPVESKPDKPSGKSGMDAALDDLIDTLGGPEETEEENTTYTGPEVSDPMSSTYIEELGKREVTIPPKYRELLAKKEGITGPPADSSKPIGPDDAIDALSSDFTCGSPTAAGKKTEKEESTEVLKAQSAGTVRSAAPPQEK Fragment Circular dichroism (CD) spectroscopy, far-UV 298 Na2HPO4 pH 7.5 10 NaCl 150 Sensitivity to proteolysis 298 EDTA 1 mercaptoethanol 5 NaCl 150 Tris pH 7.5 20 Nuclear magnetic resonance (NMR) EDTA 1 mercaptoethanol 5 NaCl 150 protein 50 Tris pH 7.5 20 Paper 15751971 Csizmok V, Bokor M, Banki P, Klement E, Medzihradszky KF, Friedrich P, Tompa K, Tompa P 2005 Biochemistry 44 10 3955-64 Toke reference provided by Maya. Moved from DP00686 due to duplication. Translation initiation factor IF-3 IF3_ECOLI Translation initiation factor IF-3, N-terminally processed [cleavage product 1] Translation initiation factor IF-3S [cleavage product 2] P0A707 IF3_ECOLI 67466073 Escherichia coli 180 MKGGKRVQTARPNRINGEIRAQEVRLTGLEGEQLGIVSLREALEKAEEAGVDLVEISPNAEPPVCRIMDYGKFLYEKSKSSKEQKKKQKVIQVKEIKFRPGTDEGDYQVKLRSLIRFLEEGDKAKITLRFRGREMAHQQIGMEVLNRVKDDLQELAVVESFPTKIEGRQMIMVLAPKKKQ Disordered inter-domain linker 78 89 SKSSKEQKKKQK Native Relationship to function unknown Entropic chain Flexible linkers/spacers Nuclear magnetic resonance (NMR) 6.5 20mM potassium phosphate Paper 9054966 Moreau M, de Cock E, Fortier PL, Garcia C, Albaret C, Blanquet S, Lallemand JY, Dardel F 1997 J Mol Biol 266 1 15-22 Disordered residues lie within the regions corresponding to cleavage products 1 and 2, however, there is no experimental evidence indicating that these products are disordered. The N-terminally processed cleavage product 1 differs from the full-length protein by removal of a single initiator methionine and cleavage product 2 has the first 6 residues removed. Transcriptional activator protein traR TRAR_RHIRD TraR P33905 TRAR_RHIRD 6094514 Rhizobium radiobacter (Agrobacterium tumefaciens)(Agrobacterium radiobacter) 234 MQHWLDKLTDLAAIEGDECILKTGLADIADHFGFTGYAYLHIQHRHITAVTNYHRQWQSTYFDKKFEALDPVVKRARSRKHIFTWSGEHERPTLSKDERAFYDHASDFGIRSGITIPIKTANGFMSMFTMASDKPVIDLDREIDAVAAAATIGQIHARISFLRTTPTAEDAAWLDPKEATYLRWIAVGKTMEEIADVEGVKYNSVRVKLREAMKRFDVRSKAHLTALAIRRKLI Disordered 1 234 MQHWLDKLTDLAAIEGDECILKTGLADIADHFGFTGYAYLHIQHRHITAVTNYHRQWQSTYFDKKFEALDPVVKRARSRKHIFTWSGEHERPTLSKDERAFYDHASDFGIRSGITIPIKTANGFMSMFTMASDKPVIDLDREIDAVAAAATIGQIHARISFLRTTPTAEDAAWLDPKEATYLRWIAVGKTMEEIADVEGVKYNSVRVKLREAMKRFDVRSKAHLTALAIRRKLI Native Function arises via a disorder to order transition Molecular recognition effectors Transactivation (transcriptional activation) Substrate/ligand binding Sensitivity to proteolysis Paper 11171981 Zhu J, Winans SC 2001 Proc Natl Acad Sci U S A 98 4 1507-12 Beta-casein CASB_HUMAN P05814 Hs.2242 CASB_HUMAN 115661 Homo sapiens (Human) 226 MKVLILACLVALALARETIESLSSSEESITEYKQKVEKVKHEDQQQGEDEHQDKIYPSFQPQPLIYPFVEPIPYGFLPQNILPLAQPAVVLPVPQPEIMEVPKAKDTVYTKGRVMPVLKSPTIPFFDPQIPKLTDLENLHLPLPLLQPLMQQVPQPIPQTLALPPQPLWSVPQPKVLPIPQQVVPYPQRAVPVQALLLNQELLLNPTHQIYPVTQPLAPVHNPISV Disordered - Extended 1 226 MKVLILACLVALALARETIESLSSSEESITEYKQKVEKVKHEDQQQGEDEHQDKIYPSFQPQPLIYPFVEPIPYGFLPQNILPLAQPAVVLPVPQPEIMEVPKAKDTVYTKGRVMPVLKSPTIPFFDPQIPKLTDLENLHLPLPLLQPLMQQVPQPIPQTLALPPQPLWSVPQPKVLPIPQQVVPYPQRAVPVQALLLNQELLLNPTHQIYPVTQPLAPVHNPISV Native Function arises from the disordered state Modification site Molecular recognition scavengers Metal binding Phosphorylation X-ray crystallography Circular dichroism (CD) spectroscopy, near-UV 298 7 protein solution 0.04 Circular dichroism (CD) spectroscopy, near-UV 283 7 protein solution 0.04 Circular dichroism (CD) spectroscopy, near-UV 277 7 protein solution 0.04 Paper 3074304 Holt C, Sawyer L 1988 Protein Eng 2 4 251-9 4624541 Toyoda M, Yamauchi K 1972 Biochim Biophys Acta 263 3 555-63 T-cell surface glycoprotein CD3 zeta chain [Isoform 1] CD3Z_HUMAN T-cell receptor T3 zeta chain CD-3-zeta P20963-1 Hs.156445 CD3Z_HUMAN 23830999 Homo sapiens (Human) 164 MKWKALFTAAILQAQLPITEAQSFGLLDPKLCYLLDGILFIYGVILTALFLRVKFSRSADAPAYQQGQNQLYNELNLGRREEYDVLDKRRGRDPEMGGKPQRRKNPQEGLYNELQKDKMAEAYSEIGMKGERRRGKGHDGLYQGLSTATKDTYDALHMQALPPR Disordered cytoplasmic domain 52 164 RVKFSRSADAPAYQQGQNQLYNELNLGRREEYDVLDKRRGRDPEMGGKPQRRKNPQEGLYNELQKDKMAEAYSEIGMKGERRRGKGHDGLYQGLSTATKDTYDALHMQALPPR Fragment Native Function arises from the disordered state Molecular recognition effectors Molecular assembly Polymerization Phosphorylation Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV 298 7 0.01 and 1.0 mM protein in PBS 1.0 and 0.01 mm path-length Nuclear magnetic resonance (NMR) 293 6.2 0.9 mM protein in 20 mM sodium phosphate buffer 600 MHz Paper 14967045 Sigalov A, Aivazian D, Stern L. 2004 Biochemistry 43 7 2049-61 ATP synthase-coupling factor 6, mitochondrial ATP5J_BOVIN ATPase subunit F6 P02721 Bt.404 ATP5J_BOVIN 114687 Bos taurus (Bovine) 108 MILQRLFRLSSAVQSAISVSWRRNIGITAVAFNKELDPVQKLFVDKIREYRTKRQTSGGPVDAGPEYQQDLDRELFKLKQMYGKADMNTFPNFTFEDPKFEVVEKPQS Disordered - Extended ATP synthase coupling factor 6 33 108 NKELDPVQKLFVDKIREYRTKRQTSGGPVDAGPEYQQDLDRELFKLKQMYGKADMNTFPNFTFEDPKFEVVEKPQS Native 1VZSA Relationship to function unknown Molecular assembly Protein-protein binding Nuclear magnetic resonance (NMR) 300 6.5 sodium phosphate 20 sodium chloride 50 Paper 15327958 Carbajo RJ, Silvester JA, Runswick MJ, Walker JE, Neuhaus D 2004 J Mol Biol 342 2 593-603 The SwissProt sequence includes a signal sequence that spans from residue 1 to 32 and was not included in the experimental sequence. Disordered 56 66 TSGGPVDAGPE Native Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 300 6.5 sodium chloride 50 sodium phosphate 20 Paper 15327958 Carbajo RJ, Silvester JA, Runswick MJ, Walker JE, Neuhaus D 2004 J Mol Biol 342 2 593-603 The SwissProt sequence includes a signal sequence that spans from residue 1 to 32 and was not included in the experimental sequence. Disordered 84 108 KADMNTFPNFTFEDPKFEVVEKPQS Native Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 300 6.5 sodium chloride 50 sodium phosphate 20 Paper 15327958 Carbajo RJ, Silvester JA, Runswick MJ, Walker JE, Neuhaus D 2004 J Mol Biol 342 2 593-603 The SwissProt sequence includes a signal sequence that spans from residue 1 to 32 and was not included in the experimental sequence. The ATP synthase is embedded in the inner membranes of mitochondria where it uses the proton motive force generated across the membrane by respiration to make ATP from ADP and inorganic phosphate. The enzyme has two major domains, a globular catalytic domain known as F1 that extends into the mitochondrial matrix, and a membrane domain known as Fo. The two domains are linked together by a central stalk and a peripheral stalk. The central stalk consists of subunits gamma, delta, and epsilon and its foot is intimately associated with a ring of c-subunits in the Fo domain. The peripheral stalk in bovine mitochondria consists of one copy of each of subunits OSCP, F6, b and d. F6 subunit was described first almost 40 years ago and shown to be required for restoration of ATP-Pi exchange and oligomycin-sensitive ATPase activity to F6-depleted ATP synthase. Subunit F6 or coupling factor 6 is a 9 kDa (76 residues) acidic protein that is soluble and heat stable over a broad pH range. It is derived from the precursor protein (108 residues), deposited in Swiss-Prot as P02721 (ATPR_BOVIN). UPF0243 zinc-binding protein yacG YACG_ECO57 P0A8H9 YACG_ECO57 67476024 Escherichia coli 65 MSETITVNCPTCGKTVVWGEISPFRPFCSKRCQLIDLGEWAAEEKRIPSSGDLSESDDWSEEPKQ Disordered 1 3 MSE Engineered Function arises from the disordered state Molecular assembly Metal binding Protein-protein binding Nuclear magnetic resonance (NMR) 298 6.5 benzamidine 1 DTT 10 inhibitor cocktail Na2HPO4 25 NaN3 in 10% v/v D2O/H2O 0.01 sodium chloride 450 Zn 2+ 20 Paper 12211008 Ramelot TA, Cort JR, Yee AA, Semesi A, Edwards AM, Arrowsmith CH, Kennedy MA 2002 Proteins 49 2 289-293 Disordered 40 65 WAAEEKRIPSSGDLSESDDWSEEPKQ Engineered Function arises from the disordered state Molecular assembly Metal binding Protein-protein binding Nuclear magnetic resonance (NMR) 298 6.5 benzamidine 1 DTT 10 inhibitor cocktail Na2HPO4 25 NaN3 in 10% v/v D2O/H2O 0.01 sodium chloride 450 Zn 2+ 20 Paper 12211008 Ramelot TA, Cort JR, Yee AA, Semesi A, Edwards AM, Arrowsmith CH, Kennedy MA 2002 Proteins 49 2 289-293 Thermonuclease NUC_STAAU TNase EC=3.1.31.1 Micrococcal nuclease Staphylococcal nuclease Nuclease B [cleavage product 1] Nuclease A [cleavage product 2] P00644 NUC_STAAU 128852 Staphylococcus aureus 231 MLVMTEYLLSAGICMAIVSILLIGMAISNVSKGQYAKRFFFFATSCLVLTLVVVSSLSSSANASQTDNGVNRSGSEDPTVYSATSTKKLHKEPATLIKAIDGDTVKLMYKGQPMTFRLLLVDTPETKHPKKGVEKYGPEASAFTKKMVENAKKIEVEFDKGQRTDKYGRGLAYIYADGKMVNEALVRQGLAKVAYVYKPNNTHEQHLRKSEAQAKKEKLNIWSEDNADSGQ Disordered residues lie within the regions corresponding to cleavage products 1 and 2, however, there is no experimental evidence to indicate that these products are disordered. Metal-binding protein smbP SMBP_NITEU Q82S91 SMBP_NITEU 75539977 Nitrosomonas europaea 117 MKTTLIKVIAASVTALFLSMQVYASGHTAHVDEAVKHAEEAVAHGKEGHTDQLLEHAKESLTHAKAASEAGGNTHVGHGIKHLEDAIKHGEEGHVGVATKHAQEAIEHLRASEHKSH Disordered - Extended Small metal binding protein 1 117 MKTTLIKVIAASVTALFLSMQVYASGHTAHVDEAVKHAEEAVAHGKEGHTDQLLEHAKESLTHAKAASEAGGNTHVGHGIKHLEDAIKHGEEGHVGVATKHAQEAIEHLRASEHKSH Monomeric Native Function arises via a disorder to order transition Metal sponge Metal binding Size exclusion/gel filtration chromatography 7.5 Circular dichroism (CD) spectroscopy, far-UV 7.5 Paper 15366930 Barney BM, LoBrutto R, Francisco WA 2004 Biochemistry 43 35 11206-13 SmbP is characterized by an unusually high number of histidine residues (17%). The apoprotein has negligible absorbance between 260 and 280 nm resulting from the lack of tryptophan, tyrosine, and phenylalanine residues. The protein also does not contain any methionine or cysteine residues. Besides histidine, the protein is primarily an assembly of alanine (16%), glutamate (14%), glycine (11%), and lysine (9%), accounting for 67% of the amino acid composition. The percentage of nonpolar amino acids is also very low, although a nonpolar residue is the predominant amino acid for the second position of the seven-unit repeat and likely contributes to the stabilization of a hydrophobic core. This unique protein is distinguished by 10 sequential repeats of a seven amino acid motif characterized by an absolutely conserved histidine residue in the fourth position and conserved residues at each of the other six positions. Extensive searches of the current databases did not identify any proteins with significant homology. The protein, as isolated from N. europaea, had approximately one copper atom bound per protein molecule. Fimbrial protein FMP1_PSEAE Pilin Strain P1 P17838 FMP1_PSEAE 120420 Pseudomonas aeruginosa 157 MKAAQKGFTLIELMIVVAIIGILAAIAIPAYQDYTARAQLSERMTLASGLKTKVSDIFSQDGSCPANTAATAGIEKDTDINGKYVAKVTTGGTAAASGGCTIVATMKASDVATPLRGKTLTLTLGNADKGSYTWACTSNADNKYLPKTCQTATTTTP Disordered - Extended 35 37 TAR Engineered Fragment 1HPWA Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 303 7.2 sodium phosphate 20 sodium chloride 100 Paper 11294863 Keizer DW, Slupsky CM, Kalisiak M, Campbell AP, Crump MP, Sastry PA, Hazes B, Irvin RT, Sykes BD 2001 J Biol Chem 276 26 24186-24193 The experimental sequence consisted of seven residues from the cloning vector followed by residues 8 through 157 of SwissProt sequence P17838. Disordered - Extended 62 64 GSC Engineered Fragment 1HBWA Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 303 7.2 sodium chloride 100 sodium phosphate 20 Paper 11294863 Keizer DW, Slupsky CM, Kalisiak M, Campbell AP, Crump MP, Sastry PA, Hazes B, Irvin RT, Sykes BD 2001 J Biol Chem 276 26 24186-24193 The experimental sequence consisted of seven residues from the cloning vector followed by residues 8 through 157 of SwissProt sequence P17838. Disordered - Extended 95 97 AAS Engineered Fragment 1HBWA Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 303 7.2 sodium chloride 100 sodium phosphate 20 Paper 11294863 Keizer DW, Slupsky CM, Kalisiak M, Campbell AP, Crump MP, Sastry PA, Hazes B, Irvin RT, Sykes BD 2001 J Biol Chem 276 26 24186-24193 The experimental sequence consisted of seven residues from the cloning vector followed by residues 8 through 157 of SwissProt sequence P17838. Disordered - Extended 108 116 ASDVATPLR Engineered Fragment 1HBWA Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 303 7.2 sodium chloride 100 sodium phosphate 20 Paper 11294863 Keizer DW, Slupsky CM, Kalisiak M, Campbell AP, Crump MP, Sastry PA, Hazes B, Irvin RT, Sykes BD 2001 J Biol Chem 276 26 24186-24193 The experimental sequence consisted of seven residues from the cloning vector followed by residues 8 through 157 of SwissProt sequence P17838. Disordered - Extended 127 132 ADKGSY Engineered Fragment 1HBWA Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 303 7.2 sodium chloride 100 sodium phosphate 20 Paper 11294863 Keizer DW, Slupsky CM, Kalisiak M, Campbell AP, Crump MP, Sastry PA, Hazes B, Irvin RT, Sykes BD 2001 J Biol Chem 276 26 24186-24193 The experimental sequence consisted of seven residues from the cloning vector followed by residues 8 through 157 of SwissProt sequence P17838. Disordered - Extended 141 157 DNKYLPKTCQTATTTTP Engineered Fragment Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 303 7.2 sodium chloride 100 sodium phosphate 20 Paper 11294863 Keizer DW, Slupsky CM, Kalisiak M, Campbell AP, Crump MP, Sastry PA, Hazes B, Irvin RT, Sykes BD 2001 J Biol Chem 276 26 24186-24193 The experimental sequence consisted of seven residues from the cloning vector followed by residues 8 through 157 of SwissProt sequence P17838. Ribonuclease E RNE_ECOLI RNase E P21513 RNE_ECOLI 34395929 Escherichia coli 1061 MKRMLINATQQEELRVALVDGQRLYDLDIESPGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPLKEIAREYFPANYSAHGRPNIKDVLREGQEVIVQIDKEERGNKGAALTTFISLAGSYLVLMPNNPRAGGISRRIEGDDRTELKEALASLELPEGMGLIVRTAGVGKSAEALQWDLSFRLKHWEAIKKAAESRPAPFLIHQESNVIVRAFRDYLRQDIGEILIDNPKVLELARQHIAALGRPDFSSKIKLYTGEIPLFSHYQIESQIESAFQREVRLPSGGSIVIDSTEALTAIDINSARATRGGDIEETAFNTNLEAADEIARQLRLRDLGGLIVIDFIDMTPVRHQRAVENRLREAVRQDRARIQISHISRFGLLEMSRQRLSPSLGESSHHVCPRCSGTGTVRDNESLSLSILRLIEEEALKENTQEVHAIVPVPIASYLLNEKRSAVNAIETRQDGVRCVIVPNDQMETPHYHVLRVRKGEETPTLSYMLPKLHEEAMALPSEEEFAERKRPEQPALATFAMPDVPPAPTPAEPAAPVVAPAPKAAPATPAAPAQPGLLSRFFGALKALFSGGEETKPTEQPAPKAEAKPERQQDRRKPRQNNRRDRNERRDTRSERTEGSDNREENRRNRRQAQQQTAETRESRQQAEVTEKARTADEQQAPRRERSRRRNDDKRQAQQEAKALNVEEQSVQETEQEERVRPVQPRRKQRQLNQKVRYEQSVAEEAVVAPVVEETVAAEPIVQEAPAPRTELVKVPLPVVAQTAPEQQEENNADNRDNGGMPRRSRRSPRHLRVSGQRRRRYRDERYPTQSPMPLTVACASPELASGKVWIRYPIVRPQDVQVEEQREQEEVHVQPMVTEVPVAAAIEPVVSAPVVEEVAGVVEAPVQVAEPQPEVVETTHPEVIAAAVTEQPQVITESDVAVAQEVAEQAEPVVEPQEETADIEEVVETAEVVVAEPEVVAQPAAPVVAEVAAEVETVAAVEPEVTVEHNHATAPMTRAPAPEYVPEAPRHSDWQRPTFAFEGKGAAGGHTATHHASAAPARPQPVE Disordered CTD (C-terminal domain) 499 1061 SYMLPKLHEEAMALPSEEEFAERKRPEQPALATFAMPDVPPAPTPAEPAAPVVAPAPKAAPATPAAPAQPGLLSRFFGALKALFSGGEETKPTEQPAPKAEAKPERQQDRRKPRQNNRRDRNERRDTRSERTEGSDNREENRRNRRQAQQQTAETRESRQQAEVTEKARTADEQQAPRRERSRRRNDDKRQAQQEAKALNVEEQSVQETEQEERVRPVQPRRKQRQLNQKVRYEQSVAEEAVVAPVVEETVAAEPIVQEAPAPRTELVKVPLPVVAQTAPEQQEENNADNRDNGGMPRRSRRSPRHLRVSGQRRRRYRDERYPTQSPMPLTVACASPELASGKVWIRYPIVRPQDVQVEEQREQEEVHVQPMVTEVPVAAAIEPVVSAPVVEEVAGVVEAPVQVAEPQPEVVETTHPEVIAAAVTEQPQVITESDVAVAQEVAEQAEPVVEPQEETADIEEVVETAEVVVAEPEVVAQPAAPVVAEVAAEVETVAAVEPEVTVEHNHATAPMTRAPAPEYVPEAPRHSDWQRPTFAFEGKGAAGGHTATHHASAAPARPQPVE Fragment Native Function arises from the disordered state Function arises via a disorder to order transition Unknown Protein-rRNA binding Autoregulatory Protein-protein binding Sensitivity to proteolysis Circular dichroism (CD) spectroscopy, far-UV 275 collected between 185 nm and 260 nm 1 nm steps Circular dichroism (CD) spectroscopy, far-UV 295 collected between 185 nm and 260 nm 1 nm steps Circular dichroism (CD) spectroscopy, far-UV 315 collected between 185 nm and 260 nm 1 nm steps Circular dichroism (CD) spectroscopy, far-UV 335 collected between 185 nm and 260 nm 1 nm steps Circular dichroism (CD) spectroscopy, far-UV 355 collected between 185 nm and 260 nm 1 nm steps Small-angle X-ray scattering (SAXS) Paper 15236960 Callaghan AJ, Aurikko JP, Ilag LL, Gunter Grossmann J, Chandran V, Kuhnel K, Poljak L, Carpousis AJ, Robinson CV, Symmons MF, Luisi BF 2004 J Mol Biol 340 5 965-79 CTD can be cross-linked to itself, thus forming dimers. The region that can self-interact is from 500-752 residues. Within the disordered CTD, there are four regions that have predicted structural propensity. These segments are called RISPs (regions of increased structural propensity). The RISPs are; segment A- residues 565-585, segment B- residues 633-712, segment C- residues 839-850 and segment D- residues 1021-1061. Disordered - Extended 796 819 RRSRRSPRHLRVSGQRRRRYRDER Fragment Function arises via a disorder to order transition Unknown Protein-rRNA binding Paper 15236960 Callaghan AJ, Aurikko JP, Ilag LL, Gunter Grossmann J, Chandran V, Kuhnel K, Poljak L, Carpousis AJ, Robinson CV, Symmons MF, Luisi BF 2004 J Mol Biol 340 5 965-79 This region is completely contained within the R-domain. This region is disordered because it is within the CTD domain of the protein but it is thought to gain structure upon the binding of RNA. Disordered R-domain 628 843 ERTEGSDNREENRRNRRQAQQQTAETRESRQQAEVTEKARTADEQQAPRRERSRRRNDDKRQAQQEAKALNVEEQSVQETEQEERVRPVQPRRKQRQLNQKVRYEQSVAEEAVVAPVVEETVAAEPIVQEAPAPRTELVKVPLPVVAQTAPEQQEENNADNRDNGGMPRRSRRSPRHLRVSGQRRRRYRDERYPTQSPMPLTVACASPELASGKVW Engineered Fragment Function arises from the disordered state Unknown Protein-rRNA binding Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV Size exclusion/gel filtration chromatography Paper 15236960 Callaghan AJ, Aurikko JP, Ilag LL, Gunter Grossmann J, Chandran V, Kuhnel K, Poljak L, Carpousis AJ, Robinson CV, Symmons MF, Luisi BF 2004 J Mol Biol 340 5 965-79 The experimental domain included the coiled coil segment B region. The 7SrRNA binding region is within this domain. There is an arginine-rich region within this domain, residues 796-819, that may gain some structure upon the binding to RNA. This domain contains the portion of the disordered CTD that binds helicase RhlB. It binds helicase RhlB in a 1:1 ratio. The binding of helicase RhlB to this domain stimulates the ATPase activity of the helicase. Binding to the helicase protein does not induce folding of the R-domain. Disordered - Extended native-CTD 580 1038 ALFSGGEETKPTEQPAPKAEAKPERQQDRRKPRQNNRRDRNERRDTRSERTEGSDNREENRRNRRQAQQQTAETRESRQQAEVTEKARTADEQQAPRRERSRRRNDDKRQAQQEAKALNVEEQSVQETEQEERVRPVQPRRKQRQLNQKVRYEQSVAEEAVVAPVVEETVAAEPIVQEAPAPRTELVKVPLPVVAQTAPEQQEENNADNRDNGGMPRRSRRSPRHLRVSGQRRRRYRDERYPTQSPMPLTVACASPELASGKVWIRYPIVRPQDVQVEEQREQEEVHVQPMVTEVPVAAAIEPVVSAPVVEEVAGVVEAPVQVAEPQPEVVETTHPEVIAAAVTEQPQVITESDVAVAQEVAEQAEPVVEPQEETADIEEVVETAEVVVAEPEVVAQPAAPVVAEVAAEVETVAAVEPEVTVEHNHATAPMTRAPAPEYVPEAPRHSDWQRPTFAFEGK Complex Fragment Function arises from the disordered state Unknown Protein-protein binding Sensitivity to proteolysis Complex, (native-CTD-enolase) less sensitive to chymotrypsin Complex, (native-CTD-enolase) very sensitive to Protease K Paper 15236960 Callaghan AJ, Aurikko JP, Ilag LL, Gunter Grossmann J, Chandran V, Kuhnel K, Poljak L, Carpousis AJ, Robinson CV, Symmons MF, Luisi BF 2004 J Mol Biol 340 5 965-79 This domain contains the entire C segment, residues 839-850. This fragment is a version of CTD isolated under native conditions without affinity tags. This domain was co-purified with enolase. The binding region included residues 816-1038. PDB entries 1SLJ:A, 1SMX:A, B, and 1SN8:A, B pertain to the ordered region of RNase E. These entries are related to amino acid residues 35-125. Sortase Q9S446_STAAU Sortase A SrtA Q9S446 Q9S446_STAAU 75421586 Staphylococcus aureus 206 MKKWTNRLMTIAGVVLILVAAYLFAKPHIDNYLHDKDKDEKIEQYDKNVKEQASKDKKQQAKPQIPKDKSKVAGYIEIPDADIKEPVYPGPATPEQLNRGVSFAEENESLDDQNISIAGHTFIDRPNYQFTNLKAAKKGSMVYFKVGNETRKYKMTSIRDVKPTDVGVLDEQKGKDKQLTLITCDDYNEKTGVWEKRKIFVATEVK Disordered - Extended disordered loop 162 174 KPTDVGVLDEQKG Engineered 1IJAA Function arises from the disordered state Molecular assembly Substrate/ligand binding Nuclear magnetic resonance (NMR) 306 6.7 SrtAN59 protein 2.5 Tris-HCl 50 NaCl 100 NaN3 0.01 CaCl2 20 DTT 3 H2O 7 Paper 11371637 Ilangovan U, Ton-That H, Iwahara J, Schneewind O, Clubb RT 2001 Proc Natl Acad Sci U S A 98 11 6056-61 15117963 Zong Y, Bice TW, Ton-That H, Schneewind O, Narayana SV 2004 J Biol Chem 279 30 31383-9 The PDB file does not contain the first 59 amino acids of the sequence (Zhong 2004). It was shown that the removal of this N terminal region had no effect on the enzymatic activity of the protein. The disordered region is part of the “catalytic core” of the protein (Ilangovan 2001). Beta-defensin 12 BNDB-12 BNBD-12 DFB12_BOVIN P46170 DFB12_BOVIN 1168638 Bos taurus (Bovine) 38 GPLSCGRNGGVCIPIRCPVPMRQIGTCFGRPVKCCRSW Disordered 1 4 GPLS Native 1BNBA Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) Paper 7577957 Zimmermann GR, Legault P, Selsted ME, Pardi A 1995 Biochemistry 34 41 13663-71 Growth factor receptor-bound protein 2 GRB2_HUMAN Adapter protein GRB2 SH2/SH3 adapter GRB2 Protein Ash P62993 Hs.444356 GRB2_HUMAN 51702266 Homo sapiens 217 MEAIAKYDFKATADDELSFKRGDILKVLNEECDQNWYKAELNGKDGFIPKNYIEMKPHPWFFGKIPRAKAEEMLSKQRHDGAFLIRESESAPGDFSLSVKFGNDVQHFKVLRDGAGKYFLWVVKFNSLNELVDYHRSTSVSRNQQIFLRDIEQVPQQPTYVQALFDFDPQEDGELGFRRGDFIHVMDNSDPNWWKGACHGQTGMFPRNYVTPVNRNV Disordered 58 59 HP Native Function arises from the disordered state Entropic chain Flexible linkers/spacers Nuclear magnetic resonance (NMR) Paper 11178911 Yuzawa S, Yokochi M, Hatanaka H, Ogura K, Kataoka M, Miura K, Mandiyan V, Schlessinger J, Inagaki F 2001 J Mol Biol 306 3 527-37 Disordered 153 159 QVPQQPT Native Function arises from the disordered state Entropic chain Flexible linkers/spacers Nuclear magnetic resonance (NMR) Paper 11178911 Yuzawa S, Yokochi M, Hatanaka H, Ogura K, Kataoka M, Miura K, Mandiyan V, Schlessinger J, Inagaki F 2001 J Mol Biol 306 3 527-37 Additional UniGene: Hs.708119 Insulin-like growth factor-binding protein 6 IBP6_HUMAN IGF-binding protein 6 IGFBP-6 IBP-6 P24592 Hs.274313 IBP6_HUMAN 124068 Homo sapiens (Human) 240 MTPHRLLPPLLLLLALLLAASPGGALARCPGCGQGVQAGCPGGCVEEEDGGSPAEGCAEAEGCLRREGQECGVYTPNCAPGLQCHPPKDDEAPLRALLLGRGRCLPARAPAVAEENPKESKPQAGTARPQDVNRRDQQRNPGTSTTPSQPNSAGVQDTEMGPCRRHLDSVLQQLQTEVYRGAQTLYVPNCDHRGFYRKRQCRSSQGQRRGPCWCVDRMGKSLPGSPDGNGSSSCPTGSSG Disordered - Extended Loop 177 184 EVYRGAQT Fragment Native 1RMJA Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 298 4.5 sodium acetate 10 sodium azide 0.02 H2O 95 D2O 5 Paper 15308688 Headey SJ, Keizer DW, Yao S, Brasier G, Kantharidis P, Bach LA, Norton RS 2004 Mol Endocrinol 18 11 2740-2750 Disordered - Extended Loop 205 211 QGQRRGP Fragment Native 1RMJA Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 298 4.5 D2O 5 H2O 95 sodium acetate 10 sodium azide 0.02 Paper 15308688 Headey SJ, Keizer DW, Yao S, Brasier G, Kantharidis P, Bach LA, Norton RS 2004 Mol Endocrinol 18 11 2740-2750 Disordered - Extended 223 240 PGSPDGNGSSSCPTGSSG Fragment Native 1RMJA Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 298 4.5 D2O 5 H2O 95 sodium acetate 10 sodium azide 0.02 Paper 15308688 Headey SJ, Keizer DW, Yao S, Brasier G, Kantharidis P, Bach LA, Norton RS 2004 Mol Endocrinol 18 11 2740-2750 The experimental fragment was the C-terminal domain of human IGFHB-6. Histone-binding protein N1/N2 HIBN_XENLA P06180 Xl.48795 HIBN_XENLA 123127 Xenopus laevis (African clawed frog) 590 MAEETAALSTEKTEDTSTAPSTSAEKADGIDIDTEAKRLMGAGQKHLVMKDVRSAVNLFQEASSLLAKQYGETADECAEAFYSYGMSLLELARLENGVLGNALEGMPEDDEEEAEKEEDPNIPSADNLDEKEREQLREQVYDAMAEDQRAPDDTSESEAKGKPEGDSKDKEADEKMKNGQKETEKVTDDLKIDSASRDVPMDKSGKGEPPESKDAETLVEQKESKPETLKEKSIETKEKDLSKEKTDAKETANQSPDSTEVAEEKMDSEASESKESTSIPPTENEANKPDDPEKMEEEEEGEDSEENEDGTEENEGTEEKETEEEDVGNLQLAWEMLDLCKTIFKRQQSKEAQLKAAQAHQKLGEVCIESENYSQAVEDFLACLNIQKEHLEEHDRLLAETHYHLGLAYQYSSKHEEAISHFTQSIGVIEKRMDVLTKQLEASVGELVDEVKKEMDELKDLLPDIKEKIEDSKEAQKNATVTEKALKETLVGGSSGFSKENGSTSSSSAVEKSGDSTVPVTNCVSDISHLVRKKRKTEEESPLKDKDAKKSKQEPVANGAGNGDAVVPTNEEAEKAEEASMETATVESTA Disordered nuclear location sequence (NLS) 532 552 RKKRKTEEESPLKDKAKKSKG Complex Engineered Fragment 1PJNA Function arises from the disordered state Chaperones Nuclear localization Flexible linkers/spacers X-ray crystallography 293 6 Sodium citrate DTT Paper 12695505 Fontes MR, Teh T, Jans D, Brinkworth RI, Kobe B 2003 J. Biol. Chem. 278 30 27981-7 The numbering used by Fontes et al (2003) for the NLS--aa 335-355--differs slightly from UniProt--aa 532-552--for the same sequence. UniProt numbering is used in DP00213. Additionally, the authors used a synthetically constructed peptide which varies from UniProt (listed first) at these positions: D547A, A548K, K550S, S551K, K552G. The Fontes et al (2003) experiment was performed in complex with importin-alpha. According to Kleinschmidt et al (1986), this protein shows aberrant migration on SDS-PAGE gels and is heat stable. These two properties strongly suggest that the protein is totally disordered but are not considered definitive evidence that it is, in fact, disordered. Osteopontin OSTP_HUMAN Bone sialoprotein 1 Secreted phosphoprotein 1 SPP-1 Urinary stone protein Nephropontin Uropontin P10451 Hs.313 OSTP_HUMAN 129260 Homo sapiens (Human) 314 MRIAVICFCLLGITCAIPVKQADSGSSEEKQLYNKYPDAVATWLNPDPSQKQNLLAPQNAVSSEETNDFKQETLPSKSNESHDHMDDMDDEDDDDHVDSQDSIDSNDSDDVDDTDDSHQSDESHHSDESDELVTDFPTDLPATEVFTPVVPTVDTYDGRGDSVVYGLRSKSKKFRRPDIQYPDATDEDITSHMESEELNGAYKAIPVAQDLNAPSDWDSRGKDSYETSQLDDQSAETHSHKQSRLYKRKANDESNEHSDVIDSQELSKVSREFHSHEFHSHEDMLVVDPKSKEEDKHLKFRISHELDSASSEVN Disordered 1 314 MRIAVICFCLLGITCAIPVKQADSGSSEEKQLYNKYPDAVATWLNPDPSQKQNLLAPQNAVSSEETNDFKQETLPSKSNESHDHMDDMDDEDDDDHVDSQDSIDSNDSDDVDDTDDSHQSDESHHSDESDELVTDFPTDLPATEVFTPVVPTVDTYDGRGDSVVYGLRSKSKKFRRPDIQYPDATDEDITSHMESEELNGAYKAIPVAQDLNAPSDWDSRGKDSYETSQLDDQSAETHSHKQSRLYKRKANDESNEHSDVIDSQELSKVSREFHSHEFHSHEDMLVVDPKSKEEDKHLKFRISHELDSASSEVN Native Function arises via a disorder to order transition Molecular assembly Substrate/ligand binding Protein-protein binding Nuclear magnetic resonance (NMR) 303 6 protein per mL water (BSP) 15 Nuclear magnetic resonance (NMR) 303 6 protein 15 sodium phosphate 10 Paper 11162539 Fisher LW, Torchia DA, Fohr B, Young MF, Fedarko NS 2001 Biochem Biophys Res Commun 280 2 460-5 Wiskott-Aldrich syndrome protein WASP_HUMAN WASp P42768 Hs.2157 WASP_HUMAN 1722836 Homo sapiens (Human) 501 SGGPMGGRPGGRGAPAVQQNIPSTLLQDHENQRLFEMLGRKCLTLATAVVQLYLALPPGAEHWTKEHCGAVCFVKDNPQKSYFIRLYGLQAGRLLWEQELYSQLVYSTPTPFFHTFAGDDCQAGLNFADEDEAQAFRALVQEKIQKRNQRQSGDRRQLPPPPTPANEERRGGLPPLPLHPGGDQGGPPVGPLSLGLATVDIQNPDITSSRYRGLPAPGPSPADKKRSGKKKISKADIGAPSGFKHVSHVGWDPQNGFDVNNLDPDLRSLFSRAGISEAQLTDAETSKLIYDFIEDQGGLEAVRQEMRRQEPLPPPPPPSRGGNQLPRPPIVGGNKGRSGPLPPVPLGIAPPPPTPRGPPPPGRGGPPPPPPPATGRSGPLPPPPPGAGGPPMPPPPPPPPPPPSSGNGPAPPPLPPALVPAGGLAPGGGRGALLDQIRQGIQLNKTPGAPESSALQPPPQSSEGLVGALMHVMQKRSRAIHSSDEGEDQAGDEDEDDEWDD Disordered 230 249 KKISKADIGAPSGFKHVSHV Engineered Fragment Native Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Paper 10724160 Kim AS, Kakalis LT, Abdul-Manan N, Liu GA, Rosen MK 2000 Nature 404 6774 151-8 Experimental sequence was KKISKADIGAPSGFKHVSHVGWDPQNGFDVNNLDPDLRSLFSRAGISEAQLTDAETSKLI YDFIEDQGGLEAVRQEMRRQ. Disordered 241 249 SGFKHVSHV Engineered Fragment Mutant Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Paper 10724160 Kim AS, Kakalis LT, Abdul-Manan N, Liu GA, Rosen MK 2000 Nature 404 6774 151-8 Experimental sequence was a fusion of two fragments of WASp joined by a short GS linker. The experimental sequence was K KISKADIGAP SGFKHVSHVG WDPQNGFDVN NLDPDLRSLF SRAGISEAQL TDAETSKLIY DFIEDQGGLE AVRQEMRRQE ggsggs SSEGLVGALM HVMQKRSRAI HSSDEGEDQA GD. Disordered 480 492 IHSSDEGEDQAGD Engineered Fragment Mutant Relationship to function unknown Unknown Unknown Paper 10724160 Kim AS, Kakalis LT, Abdul-Manan N, Liu GA, Rosen MK 2000 Nature 404 6774 151-8 Experimental sequence was a fusion of two fragments of WASp joined by a short GS linker. The experimental sequence was K KISKADIGAP SGFKHVSHVG WDPQNGFDVN NLDPDLRSLF SRAGISEAQL TDAETSKLIY DFIEDQGGLE AVRQEMRRQE ggsggs SSEGLVGALM HVMQKRSRAI HSSDEGEDQA GD. BN28a Q9FUM5_BRANA Q9FUM5 Q9FUM5_BRANA 75172513 Brassica napus (Rape) 65 MADNKQSFQAGQAAGRAEEKGNVLMDKVKDAATAAGASAQTAGQKITEAAGGAVNLVKEKTGMNK Disordered 1 65 MADNKQSFQAGQAAGRAEEKGNVLMDKVKDAATAAGASAQTAGQKITEAAGGAVNLVKEKTGMNK Native Relationship to function unknown Unknown Unknown Circular dichroism (CD) spectroscopy, far-UV Nuclear magnetic resonance (NMR) Paper 9046590 Boothe JG, Sonnichsen FD, de Beus MD, Johnson-Flanagan AM 1997 Plant Physiol 113 2 367-76 Nucleoplasmin NUPL_XENLA P05221 Xl.1262 NUPL_XENLA 128910 Xenopus laevis (African clawed frog) 200 MASTVSNTSKLEKPVSLIWGCELNEQDKTFEFKVEDDEEKCEHQLALRTVCLGDKAKDEFNIVEIVTQEEGAEKSVPIATLKPSILPMATMVGIELTPPVTFRLKAGSGPLYISGQHVAMEEDYSWAEEEDEGEAEGEEEEEEEEDQESPPKAVKRPAATKKAGQAKKKKLDKEDESSEEDSPTKKGKGAGRGRKPAAKK Disordered 120 200 MEEDYSWAEEEDEGEAEGEEEEEEEEDQESPPKAVKRPAATKKAGQAKKKKLDKEDESSEEDSPTKKGKGAGRGRKPAAKK Fragment Native Relationship to function unknown Unknown Unknown Circular dichroism (CD) spectroscopy, far-UV Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) Sensitivity to proteolysis Paper 11248694 Hierro A, Arizmendi JM, De Las Rivas J, Urbaneja MA, Prado A, Muga A 2001 Eur J Biochem 268 6 1739-48 Additional UniGene: Xl.1264 Protein phosphatase 1 regulatory subunit 12A [Isoform 2] MYPT1_CHICK Myosin phosphatase-targeting subunit 1 Myosin phosphatase target subunit 1 Protein phosphatase myosin-binding subunit PP1M subunit M110 130 kDa myosin-binding subunit of smooth muscle myosin phophatase M130 Q90623-2 Gga.3159 MYPT1_CHICK 82216979 Gallus gallus (Chicken) 963 MKMADAKQKRNEQLKRWIGSETDLEPPVVKRKKTKVKFDDGAVFLAACSSGDTEEVLRLLERGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEYLISQGAHVGAVNSEGDTPLDIAEEEAMEELLQNEVNRQGVDIEAARKEEERIMLRDARQWLNSGHINDVRHAKSGGTALHVAAAKGYTEVLKLLIQARYDVNIKDYDGWTPLHAAAHWGKEEACRILVENLCDMEAVNKVGQTAFDVADEDILGYLEELQKKQNLLHSEKREKKSPLIESTANLDNNQTQKTFKNKETLIMEQEKNASSIESLEHEKADEEEEGKKDESSCSSEEEEDDDSESEAETDKAKTLANANTTSTQSASMTAPSVAGGQGTPTSPLKKFPTSTTKVSPKEEERKDESPASWRLGLRKTGSYGALAEITASKEAQKEKDSAGVIRSASSPRLSSSLDNKEKEKDGKGTRLAYVAPTIPRRLASTSDIDEKENSGSFGRRQDDLVSSNVPSTASTVTSSAGLQKTLPASANTTTKSTTGSTSAGVQSSTSNRLWAEDSTEKEKDSVPTAVTVPVAPSVVNAAATTTAMTTATSGTVSSTSEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRSRSTRTREQENEEKEKEEKEKQDKEKQEEKKESETKDDDYRQRYSRTVEEPYHRYRPTSTSTSTSSTSSLSTSTSSLSSSSQLNRPNSLIGITSAYSRSGTKESEREGGKKEEEKEEDKSQPKSIRERRRPREKRRSTGVSFWTQDSDENEQEHQSDSEEGTNKKETQSDSLSRYDTGSLSVSSGDRYDSAQGRSGSQSYLEDRKPYCSRLEKEDSTDFKKLYEQILAENEKLKAQLHDTNMELTDLKLQLEKTTQRQERFADRSLLEMEKRVSGKSQYLLGGKKSSRKKDI Disordered 1 299 MKMADAKQKRNEQLKRWIGSETDLEPPVVKRKKTKVKFDDGAVFLAACSSGDTEEVLRLLERGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEYLISQGAHVGAVNSEGDTPLDIAEEEAMEELLQNEVNRQGVDIEAARKEEERIMLRDARQWLNSGHINDVRHAKSGGTALHVAAAKGYTEVLKLLIQARYDVNIKDYDGWTPLHAAAHWGKEEACRILVENLCDMEAVNKVGQTAFDVADEDILGYLEELQKKQNLLHSEKREKKS Fragment Native 1S70B Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Paper 15164081 Terrak M, Kerff F, Langsetmo K, Tao T, Dominguez R 2004 Nature 429 6993 780-4 Protein phosphatase 1 regulatory subunit 11 PP1RB_HUMAN Protein phosphatase inhibitor 3 Hemochromatosis candidate protein V HCG V HCG-V O60927 Hs.82887 PP1RB_HUMAN 74739598 Homo sapiens (Human) 126 MAEAGAGLSETVTETTVTVTTEPENRSLTIKLRKRKPEKKVEWTSDTVDNEHMGRRSSKCCCIYEKPRAFGESSTESDEEEEEGCGHTHCVRGHRKGRRRATLGPTPTTPPQPPDPSQPPPGPMQH Disordered 1 126 MAEAGAGLSETVTETTVTVTTEPENRSLTIKLRKRKPEKKVEWTSDTVDNEHMGRRSSKCCCIYEKPRAFGESSTESDEEEEEGCGHTHCVRGHRKGRRRATLGPTPTTPPQPPDPSQPPPGPMQH Native Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Stability at thermal extremes SDS-PAGE gel, Aberrant mobility on Size exclusion/gel filtration chromatography Paper 9843442 Zhang J, Zhang L, Zhao S, Lee EY 1998 Biochemistry 37 47 16728-34 Peripherin-2 PRPH2_BOVIN Retinal degeneration slow protein P17810 Bt.12752 PRPH2_BOVIN 132211 Bos taurus (Bovine) 345 ALLKVKFDQKKRVKLAQGLWLMNWFSVLAGIIIFGLGLFLKIELRKRSDVMNNSESHFVPNSLIGVGVLSCVFNSLAGKICYDALDPAKYAKWKPWLKPYLAVCVLFNVVLFLVALCCFLLRGSLESTLAHGLKNGMKFYRDTDTPGRCFMKKTIDMLQIEFKCCGNNGFRDWFEIQWISNRYLDFSSKEVKDRIKSNVDGRYLVDGVPFSCCNPNSPRPCIQYQLTNNSAHYSYDHQTEELNLWLRGCRAALLSYYSNLMNTTGAVTLLVWLFEVTITVGLRYLHTALEGMANPEDPECESEGWLLEKSVPETWKAFLESVKKLGKGNQVEAEGEDAGQAPAAG Disordered - Extended C-terminal domain 283 345 RYLHTALEGMANPEDPECESEGWLLEKSVPETWKAFLESVKKLGKGNQVEAEGEDAGQAPAAG Fragment Native Function arises from the disordered state Unknown Unknown Sensitivity to proteolysis 310 7.5 0.4 mg/ml protein 2 microg/ml Proteinase K 50 mM Tris-HCl, 150 mM NaCl Fluorescence, intrinsic 298 7.5 50 mM Tris-HCl, 150 mM NaCl, 1 mM TCEP 5 microg/ml protein excitation at 295nm, emission scan from 295 to 430nm Circular dichroism (CD) spectroscopy, far-UV 283 7.5 0.1 cm cell 0.3 mg/ml protein 50 mM Tris-HCl, 150 mM NaCl, 1 mM TCEP Size exclusion/gel filtration chromatography 298 7.5 0.2 ml/min flow rate 0.5 to 1.5 mg protein 1 cm x 46 cm Sephacryl S-100HR column 50 mM Tris-HCl, 150 mM NaCl, 1 mM TCEP Analytical ultracentrifugation 293 7.5 1.0, 0.3 and 0.1 mg/ml protein 500 microl aliquots 50k rpm 50 mM Tris-HCl, 150 mM NaCl, 1 mM TCEP Paper 16522184 Ritter LM, Arakawa T, Goldberg AF 2005 Protein Pept Lett 12 7 677-86 Involucrin INVO_HUMAN P07476 Hs.516439 INVO_HUMAN 254763301 Homo sapiens (Human) 585 MSQQHTLPVTLSPALSQELLKTVPPPVNTHQEQMKQPTPLPPPCQKVPVELPVEVPSKQEEKHMTAVKGLPEQECEQQQKEPQEQELQQQHWEQHEEYQKAENPEQQLKQEKTQRDQQLNKQLEEEKKLLDQQLDQELVKRDEQLGMKKEQLLELPEQQEGHLKHLEQQEGQLKHPEQQEGQLELPEQQEGQLELPEQQEGQLELPEQQEGQLELPEQQEGQLELPQQQEGQLELSEQQEGQLELSEQQEGQLELSEQQEGQLKHLEHQEGQLEVPEEQMGQLKYLEQQEGQLKHLDQQEKQPELPEQQMGQLKHLEQQEGQPKHLEQQEGQLEQLEEQEGQLKHLEQQEGQLEHLEHQEGQLGLPEQQVLQLKQLEKQQGQPKHLEEEEGQLKHLVQQEGQLKHLVQQEGQLEQQERQVEHLEQQVGQLKHLEEQEGQLKHLEQQQGQLEVPEQQVGQPKNLEQEEKQLELPEQQEGQVKHLEKQEAQLELPEQQVGQPKHLEQQEKHLEHPEQQDGQLKHLEQQEGQLKDLEQQKGQLEQPVFAPAPGQVQDIQPALPTKGEVLLPVEHQQQKQEVQWPPKHK Disordered 336 365 LEEQEGQLKHLEQQEGQLEHLEHQEGQLGL Engineered Mutant Relationship to function unknown Unknown Unknown Paper 10601302 Lazo ND, Downing DT 1999 J Biol Chem 274 52 37340-4 Experimental fragment was three repeats of LEQQEGQLEH. This consensus repeat sequence had the following deviations from the native sequence; E248Q and E354K. Note that there are several LEQQEGQLEH repeats in native sequence. Disordered 196 225 PEQQEGQLELPEQQEGQLELPEQQEGQLEL Engineered Fragment Native Relationship to function unknown Unknown Unknown Paper 10601302 Lazo ND, Downing DT 1999 J Biol Chem 274 52 37340-4 The experimental sequence consisted of three repeats of PEQQEGQLEL. Note that there are several PEQQEGQLEL repeats in the native sequence. Nucleoporin NUP2 NUP2_YEAST Nuclear pore protein NUP2 p95 P32499 NUP2_YEAST 30923217 Saccharomyces cerevisiae (Baker's yeast) 720 MAKRVADAQIQRETYDSNESDDDVTPSTKVASSAVMNRRKIAMPKRRMAFKPFGSAKSDETKQASSFSFLNRADGTGEAQVDNSPTTESNSRLKALNLQFKAKVDDLVLGKPLADLRPLFTRYELYIKNILEAPVKSIENPTQTKGNDAKPAKVEDVQKSSDSSSEDEVKVEGPKFTIDAKPPISDSVFSFGPKKENRKKDESDSENDIEIKGPEFKFSGTVSSDVFKLNPSTDKNEKKTETNAKPFSFSSATSTTEQTKSKNPLSLTEATKTNVDNNSKAEASFTFGTKHAADSQNNKPSFVFGQAAAKPSLEKSSFTFGSTTIEKKNDENSTSNSKPEKSSDSNDSNPSFSFSIPSKNTPDASKPSFSFGVPNSSKNETSKPVFSFGAATPSAKEASQEDDNNNVEKPSSKPAFNLISNAGTEKEKESKKDSKPAFSFGISNGSESKDSDKPSLPSAVDGENDKKEATKPAFSFGINTNTTKTADTKAPTFTFGSSALADNKEDVKKPFSFGTSQPNNTPSFSFGKTTANLPANSSTSPAPSIPSTGFKFSLPFEQKGSQTTTNDSKEESTTEATGNESQDATKVDATPEESKPINLQNGEEDEVALFSQKAKLMTFNAETKSYDSRGVGEMKLLKKKDDPSKVRLLCRSDGMGNVLLNATVVDSFKYEPLAPGNDNLIKAPTVAADGKLVTYIVKFKQKEEGRSFTKAIEDAKKEMK Disordered 1 720 MAKRVADAQIQRETYDSNESDDDVTPSTKVASSAVMNRRKIAMPKRRMAFKPFGSAKSDETKQASSFSFLNRADGTGEAQVDNSPTTESNSRLKALNLQFKAKVDDLVLGKPLADLRPLFTRYELYIKNILEAPVKSIENPTQTKGNDAKPAKVEDVQKSSDSSSEDEVKVEGPKFTIDAKPPISDSVFSFGPKKENRKKDESDSENDIEIKGPEFKFSGTVSSDVFKLNPSTDKNEKKTETNAKPFSFSSATSTTEQTKSKNPLSLTEATKTNVDNNSKAEASFTFGTKHAADSQNNKPSFVFGQAAAKPSLEKSSFTFGSTTIEKKNDENSTSNSKPEKSSDSNDSNPSFSFSIPSKNTPDASKPSFSFGVPNSSKNETSKPVFSFGAATPSAKEASQEDDNNNVEKPSSKPAFNLISNAGTEKEKESKKDSKPAFSFGISNGSESKDSDKPSLPSAVDGENDKKEATKPAFSFGINTNTTKTADTKAPTFTFGSSALADNKEDVKKPFSFGTSQPNNTPSFSFGKTTANLPANSSTSPAPSIPSTGFKFSLPFEQKGSQTTTNDSKEESTTEATGNESQDATKVDATPEESKPINLQNGEEDEVALFSQKAKLMTFNAETKSYDSRGVGEMKLLKKKDDPSKVRLLCRSDGMGNVLLNATVVDSFKYEPLAPGNDNLIKAPTVAADGKLVTYIVKFKQKEEGRSFTKAIEDAKKEMK Monomeric Native Relationship to function unknown Unknown Unknown Circular dichroism (CD) spectroscopy, far-UV Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) Sensitivity to proteolysis Size exclusion/gel filtration chromatography Analytical ultracentrifugation Paper 12065587 Denning DP, Uversky V, Patel SS, Fink AL, Rexach M 2002 J Biol Chem 277 36 33447-55 G2/mitotic-specific cyclin-B1 CCNB1_HUMAN P14635 Hs.23960 CCNB1_HUMAN 116176 Homo sapiens (Human) 433 MALRVTRNSKINAENKAKINMAGAKRVPTAPAATSKPGLRPRTALGDIGNKVSEQLQAKMPMKKEAKPSATGKVIDKKLPKPLEKVPMLVPVPVSEPVPEPEPEPEPEPVKEEKLSPEPILVDTASPSPMETSGCAPAEEDLCQAFSDVILAVNDVDAEDGADPNLCSEYVKDIYAYLRQLEEEQAVRPKYLLGREVTGNMRAILIDWLVQVQMKFRLLQETMYMTVSIIDRFMQNNCVPKKMLQLVGVTAMFIASKYEEMYPPEIGDFAFVTDNTYTKHQIRQMEMKILRALNFGLGRPLPLHFLRRASKIGEVDVEQHTLAKYLMELTMLDYDMVHFPPSQIAAGAFCLALKILDNGEWTPTLQHYLSYTEESLLPVMQHLAKNVVMVNQGLTKHMTVKNKYATSKHAKISTLPQLNSALVQDLAKAVAKV Disordered ND-cycB 1 78 MALRVTRNSKINAENKAKINMAGAKRVPTAPAATSKPGLRPRTALGDIGNKVSEQLQAKMPMKKEAKPSATGKVIDKK Fragment Native Function arises from the disordered state Molecular recognition effectors Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV Nuclear magnetic resonance (NMR) Paper 12220679 Cox CJ, Dutta K, Petri ET, Hwang WC, Lin Y, Pascal SM, Basavappa R 2002 FEBS Lett 527 1-3 303-8 Transcription factor 4 ITF2_HUMAN Immunoglobulin transcription factor 2 ITF-2 SL3-3 enhancer factor 2 SEF-2 P15884 Hs.605153 ITF2_HUMAN 3915747 Homo sapiens (Human) 667 MHHQQRMAALGTDKELSDLLDFSAMFSPPVSSGKNGPTSLASGHFTGSNVEDRSSSGSWGNGGHPSPSRNYGDGTPYDHMTSRDLGSHDNLSPPFVNSRIQSKTERGSYSSYGRESNLQGCHQQSLLGGDMDMGNPGTLSPTKPGSQYYQYSSNNPRRRPLHSSAMEVQTKKVRKVPPGLPSSVYAPSASTADYNRDSPGYPSSKPATSTFPSSFFMQDGHHSSDPWSSSSGMNQPGYAGMLGNSSHIPQSSSYCSLHPHERLSYPSHSSADINSSLPPMSTFHRSGTNHYSTSSCTPPANGTDSIMANRGSGAAGSSQTGDALGKALASIYSPDHTNNSFSSNPSTPVGSPPSLSAGTAVWSRNGGQASSSPNYEGPLHSLQSRIEDRLERLDDAIHVLRNHAVGPSTAMPGGHGDMHGIIGPSHNGAMGGLGSGYGTGLLSANRHSLMVGTHREDGVALRGSHSLLPNQVPVPQLPVQSATSPDLNPPQDPYRGMPPGLQGQSVSSGSSEIKSDDEGDENLQDTKSSEDKKLDDDKKDIKSITSNNDDEDLTPEQKAEREKERRMANNARERLRVRDINEAFKELGRMVQLHLKSDKPQTKLLILHQAVAVILSLEQQVRERNLNPKAACLKRREEEKVSSEPPPLSLAGPHPGMGDASNHMGQM Disordered 1 53 MHHQQRMAALGTDKELSDLLDFSAMFSPPVSSGKNGPTSLASGHFTGSNVEDR Fragment Native Function arises via a disorder to order transition Molecular assembly Protein-DNA binding Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV Fluorescence, intrinsic 7.4 DTT 2 sodium chloride 100 sodium phosphate buffer 50 Paper 11237626 Knapp S, Zamai M, Volpi D, Nardese V, Avanzi N, Breton J, Plyte S, Flocco M, Marconi M, Isacchi A, Caiolfa VR 2001 J Mol Biol 306 5 1179-1189 Disordered 1 56 MHHQQRMAALGTDKELSDLLDFSAMFSPPVSSGKNGPTSLASGHFTGSNVEDRSSS Fragment Native Function arises via a disorder to order transition Molecular assembly Protein-DNA binding Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV Fluorescence, intrinsic 7.4 DTT 2 sodium chloride 100 sodium phosphate buffer 50 Paper 11237626 Knapp S, Zamai M, Volpi D, Nardese V, Avanzi N, Breton J, Plyte S, Flocco M, Marconi M, Isacchi A, Caiolfa VR 2001 J Mol Biol 306 5 1179-1189 Disordered 1 130 MHHQQRMAALGTDKELSDLLDFSAMFSPPVSSGKNGPTSLASGHFTGSNVEDRSSSGSWGNGGHPSPSRNYGDGTPYDHMTSRDLGSHDNLSPPFVNSRIQSKTERGSYSSYGRESNLQGCHQQSLLGGD Fragment Native Function arises via a disorder to order transition Molecular assembly Protein-DNA binding Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV Fluorescence, intrinsic 7.4 DTT 2 sodium chloride 100 sodium phosphate buffer 50 Paper 11237626 Knapp S, Zamai M, Volpi D, Nardese V, Avanzi N, Breton J, Plyte S, Flocco M, Marconi M, Isacchi A, Caiolfa VR 2001 J Mol Biol 306 5 1179-1189 Three constructs of TCF4 were used in the Knapp paper. They extended from residues 1-53, 1-56, and 1-130. Each was found to be disordered in solution. Clathrin coat assembly protein AP180 AP180_RAT Clathrin coat-associated protein AP180 91 kDa synaptosomal-associated protein Q05140 Rn.11022 AP180_RAT 2492686 Rattus norvegicus (Rat) 915 MSGQTLTDRIAAAQYSVTGSAVARAVCKATTHEVMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLASRNTLFNLSNFLDKSGSHGYDMSTFIRRYSRYLNEKAFSYRQMAFDFARVKKGADGVMRTMVPEKLLKSMPILQGQIDALLEFDVHPNELTNGVINAAFMLLFKDLIKLFACYNDGVINLLEKFFEMKKGQCKDALEIYKRFLTRMTRVSEFLKVADEVGIDKGDIPDLTQAPSSLMETLEQHLNTLEGKKPGNNEGSGAPSPLSKSSPATTVTSPNSTPAKTIDTSPPVDIFATASAAAPVSSAKPSSDLLDLQPDFSGARAGAAAPVPPPTGGATAWGDLLGEDSLAALSSVPSEAPISDPFAPEPSPPTTTTEPASASASATTAVTAATTEVDLFGDAFAASPGEAPAASEGATAPATPAPVAAALDACSGNDPFAPSEGSAEAAPELDLFAMKPPETSAPVVTPTASTAPPVPATAPSPAPTAVAATAATTTAAAAATTTATTSAAAATTAAAPPALDIFGDLFDSAPEVAAASKPDVAPSIDLFGTDAFSSPPRGASPVPESSLTADLLSGSGFHCAEDDRHVPLFFTAVDAFAAPSPASTASPAKAESSGVIDLFGDAFGSSASETQPAPQAVSSSSASADLLAGFGGSFMAPSTTPVTPAQNNLLQPNFEAAFGTTPSTSSSSSFDPSGDLLMPTMAPSGQPAPVSMVPPSPAMSASKGLGSDLDSSLASLVGNLGISGTTSKKGDLQWNAGEKKLTGGANWQPKVTPATWSAGVPPQGTVPPTSSVPPGAGAPSVGQPGAGYGMPPAGTGMTMMPQQPVMFAQPMMRPPFGAAAVPGTQLSPSPTPATQSPKKPPAKDPLADLNIKDFL Disordered 328 896 VDIFATASAAAPVSSAKPSSDLLDLQPDFSGARAGAAAPVPPPTGGATAWGDLLGEDSLAALSSVPSEAPISDPFAPEPSPPTTTTEPASASASATTAVTAATTEVDLFGDAFAASPGEAPAASEGATAPATPAPVAAALDACSGNDPFAPSEGSAEAAPELDLFAMKPPETSAPVVTPTASTAPPVPATAPSPAPTAVAATAATTTAAAAATTTATTSAAAATTAAAPPALDIFGDLFDSAPEVAAASKPDVAPSIDLFGTDAFSSPPRGASPVPESSLTADLLSGSGFHCAEDDRHVPLFFTAVDAFAAPSPASTASPAKAESSGVIDLFGDAFGSSASETQPAPQAVSSSSASADLLAGFGGSFMAPSTTPVTPAQNNLLQPNFEAAFGTTPSTSSSSSFDPSGDLLMPTMAPSGQPAPVSMVPPSPAMSASKGLGSDLDSSLASLVGNLGISGTTSKKGDLQWNAGEKKLTGGANWQPKVTPATWSAGVPPQGTVPPTSSVPPGAGAPSVGQPGAGYGMPPAGTGMTMMPQQPVMFAQPMMRPPFGAAAVPGTQLSPSPTPATQS Fragment Monomeric Native Relationship to function unknown Unknown Unknown Circular dichroism (CD) spectroscopy, far-UV Analytical ultracentrifugation Size exclusion/gel filtration chromatography Paper 11756460 Kalthoff C, Alves J, Urbanke C, Knorr R, Ungewickell EJ 2002 J Biol Chem 277 10 8209-16 Calcyclin-binding protein CYBP_MOUSE CacyBP Siah-interacting protein SIP Q9CXW3 Mm.10702 CYBP_MOUSE 46576641 Mus musculus (Mouse) 229 MASVLEELQKDLEEVKVLLEKSTRKRLRDTLTSEKSKIETELKNKMQQKSQKKPELDNEKPAAVVAPLTTGYTVKISNYGWDQSDKFVKIYITLTGVHQVPTENVQVHFTERSFDLLVKNLNGKNYSMIVNNLLKPISVESSSKKVKTDTVIILCRKKAENTRWDYLTQVEKECKEKEKPSYDTEADPSEGLMNVLKKIYEDGDDDMKRTINKAWVESREKQAREDTEF Ordered SIPN Domain 1 47 MASVLEELQKDLEEVKVLLEKSTRKRLRDTLTSEKSKIETELKNKMQ Native Function arises from the ordered state Nuclear magnetic resonance (NMR) 303 7 NaCl 50 NaPi 20 Paper 15996101 Bhattacharya S, Lee YT, Michowski W, Jastrzebska B, Filipek A, Kuznicki J, Chazin WJ 2005 Biochemistry 44 27 9462-71 Disordered 48 73 QKSQKKPELDNEKPAAVVAPLTTGYT Native Function arises from the disordered state Molecular assembly Protein-protein binding Nuclear magnetic resonance (NMR) 303 7 NaCl 50 NaPi 20 Paper 15996101 Bhattacharya S, Lee YT, Michowski W, Jastrzebska B, Filipek A, Kuznicki J, Chazin WJ 2005 Biochemistry 44 27 9462-71 Ordered CS Domain 74 177 VKISNYGWDQSDKFVKIYITLTGVHQVPTENVQVHFTERSFDLLVKNLNGKNYSMIVNNLLKPISVESSSKKVKTDTVIILCRKKAENTRWDYLTQVEKECKEK Native Function arises from the ordered state Protein-protein binding Nuclear magnetic resonance (NMR) 303 7 NaCl 50 NaPi 20 Paper 15996101 Bhattacharya S, Lee YT, Michowski W, Jastrzebska B, Filipek A, Kuznicki J, Chazin WJ 2005 Biochemistry 44 27 9462-71 Disordered SGS Domain 178 229 EKPSYDTEADPSEGLMNVLKKIYEDGDDDMKRTINKAWVESREKQAREDTEF Native Function arises from the disordered state Molecular assembly Protein-protein binding Nuclear magnetic resonance (NMR) 303 7 NaCl 50 NaPi 20 Paper 15996101 Bhattacharya S, Lee YT, Michowski W, Jastrzebska B, Filipek A, Kuznicki J, Chazin WJ 2005 Biochemistry 44 27 9462-71 Omega gliadin storage protein Q9FUW7_WHEAT Q9FUW7 Q9FUW7_WHEAT 75172559 Triticum aestivum (Wheat) 280 MKTFLIFVLLAMAMKIATAARELNPSNKELQSPQQSFSYQQQPFPQQPYPQQPYPSQQPYPSQQPFPTPQQQFPEQSQQPFTQPQQPTPIQPQQPFPQQPQQPQQPFPQPQQPFPWQPQQPFPQTQQSFPLQPQQPFPQQPQQPFPQPQLPFPQQSEQIIPQQLQQPFPLQPQQPFPQQPQQPFPQPQQPIPVQPQQSFPQQSQQSQQPFAQPQQLFPELQQPIPQQPQQPFPLQPQQPFPQQPQQPFPQQPQQSFPQQPQQPYPQQQPYGSSLTSIGGQ Disordered 1 280 MKTFLIFVLLAMAMKIATAARELNPSNKELQSPQQSFSYQQQPFPQQPYPQQPYPSQQPYPSQQPFPTPQQQFPEQSQQPFTQPQQPTPIQPQQPFPQQPQQPQQPFPQPQQPFPWQPQQPFPQTQQSFPLQPQQPFPQQPQQPFPQPQLPFPQQSEQIIPQQLQQPFPLQPQQPFPQQPQQPFPQPQQPIPVQPQQSFPQQSQQSQQPFAQPQQLFPELQQPIPQQPQQPFPLQPQQPFPQQPQQPFPQQPQQSFPQQPQQPYPQQQPYGSSLTSIGGQ Native Relationship to function unknown Unknown Unknown Raman optical activity Paper 12741823 Blanch EW, Kasarda DD, Hecht L, Nielsen K, Barron LD 2003 Biochemistry 42 19 5665-73 Voltage-dependent L-type calcium channel subunit alpha-1S CAC1S_RABIT Voltage-gated calcium channel subunit alpha Cav1.1 Calcium channel, L type, alpha-1 polypeptide, isoform 3, skeletal muscle P07293 Ocu.1826 CAC1S_RABIT 116408 Oryctolagus cuniculus (Rabbit) 1873 MEPSSPQDEGLRKKQPKKPLPEVLPRPPRALFCLTLQNPLRKACISIVEWKPFETIILLTIFANCVALAVYLPMPEDDNNSLNLGLEKLEYFFLTVFSIEAAMKIIAYGFLFHQDAYLRSGWNVLDFIIVFLGVFTAILEQVNVIQSNTAPMSSKGAGLDVKALRAFRVLRPLRLVSGVPSLQVVLNSIFKAMLPLFHIALLVLFMVIIYAIIGLELFKGKMHKTCYYIGTDIVATVENEKPSPCARTGSGRPCTINGSECRGGWPGPNHGITHFDNFGFSMLTVYQCITMEGWTDVLYWVNDAIGNEWPWIYFVTLILLGSFFILNLVLGVLSGEFTKEREKAKSRGTFQKLREKQQLEEDLRGYMSWITQGEVMDVEDLREGKLSLEEGGSDTESLYEIEGLNKIIQFIRHWRQWNRVFRWKCHDLVKSRVFYWLVILIVALNTLSIASEHHNQPLWLTHLQDIANRVLLSLFTIEMLLKMYGLGLRQYFMSIFNRFDCFVVCSGILELLLVESGAMTPLGISVLRCIRLLRLFKITKYWTSLSNLVASLLNSIRSIASLLLLLFLFIIIFALLGMQLFGGRYDFEDTEVRRSNFDNFPQALISVFQVLTGEDWNSVMYNGIMAYGGPSYPGVLVCIYFIILFVCGNYILLNVFLAIAVDNLAEAESLTSAQKAKAEERKRRKMSRGLPDKTEEEKSVMAKKLEQKPKGEGIPTTAKLKVDEFESNVNEVKDPYPSADFPGDDEEDEPEIPVSPRPRPLAELQLKEKAVPIPEASSFFIFSPTNKVRVLCHRIVNATWFTNFILLFILLSSAALAAEDPIRAESVRNQILGYFDIAFTSVFTVEIVLKMTTYGAFLHKGSFCRNYFNILDLLVVAVSLISMGLESSTISVVKILRVLRVLRPLRAINRAKGLKHVVQCVFVAIRTIGNIVLVTTLLQFMFACIGVQLFKGKFFSCNDLSKMTEEECRGYYYVYKDGDPTQMELRPRQWIHNDFHFDNVLSAMMSLFTVSTFEGWPQLLYRAIDSNEEDMGPVYNNRVEMAIFFIIYIILIAFFMMNIFVGFVIVTFQEQGETEYKNCELDKNQRQCVQYALKARPLRCYIPKNPYQYQVWYVVTSSYFEYLMFALIMLNTICLGMQHYHQSEEMNHISDILNVAFTIIFTLEMILKLLAFKARGYFGDPWNVFDFLIVIGSIIDVILSEIDTFLASSGGLYCLGGGCGNVDPDESARISSAFFRLFRVMRLIKLLSRAEGVRTLLWTFIKSFQALPYVALLIVMLFFIYAVIGMQMFGKIALVDGTQINRNNNFQTFPQAVLLLFRCATGEAWQEILLACSYGKLCDPESDYAPGEEYTCGTNFAYYYFISFYMLCAFLIINLFVAVIMDNFDYLTRDWSILGPHHLDEFKAIWAEYDPEAKGRIKHLDVVTLLRRIQPPLGFGKFCPHRVACKRLVGMNMPLNSDGTVTFNATLFALVRTALKIKTEGNFEQANEELRAIIKKIWKRTSMKLLDQVIPPIGDDEVTVGKFYATFLIQEHFRKFMKRQEEYYGYRPKKDTVQIQAGLRTIEEEAAPEIRRTISGDLTAEEELERAMVEAAMEERIFRRTGGLFGQVDTFLERTNSLPPVMANQRPLQFAEIEMEELESPVFLEDFPQDARTNPLARANTNNANANVAYGNSNHSNNQMFSSVHCEREFPGEAETPAAGRGALSHSHRALGPHSKPCAGKLNGQLVQPGMPINQAPPAPCQQPSTDPPERGQRRTSLTGSLQDEAPQRRSSEGSTPRRPAPATALLIQEALVRGGLDTLAADAGFVTATSQALADACQMEPEEVEVAATELLKARESVQGMASVPGSLSRRSSLGSLDQVQGSQETLIPPRP Disordered peptide C 724 760 EFESNVNEVKDPYPSADFPGDDEEDEPEIPVSPRPRP Fragment Native Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV Nuclear magnetic resonance (NMR) Analytical ultracentrifugation Paper 12620094 Haarmann CS, Green D, Casarotto MG, Laver DR, Dulhunty AF 2003 Biochem J 372 Pt 2 305-16 Peptide C is sufficient to activate the ryanodine receptor at physiological concentrations. Structure determination experiments were conducted on isolated peptide C. Lupus La protein LA_HUMAN Sjoegren syndrome type B antigen SS-B La ribonucleoprotein La autoantigen P05455 Hs.632535 LA_HUMAN 125985 Homo sapiens (Human) 408 MAENGDNEKMAALEAKICHQIEYYFGDFNLPRDKFLKEQIKLDEGWVPLEIMIKFNRLNRLTTDFNVIVEALSKSKAELMEISEDKTKIRRSPSKPLPEVTDEYKNDVKNRSVYIKGFPTDATLDDIKEWLEDKGQVLNIQMRRTLHKAFKGSIFVVFDSIESAKKFVETPGQKYKETDLLILFKDDYFAKKNEERKQNKVEAKLRAKQEQEAKQKLEEDAEMKSLEEKIGCLLKFSGDLDDQTCREDLHILFSNHGEIKWIDFVRGAKEGIILFKEKAKEALGKAKDANNGNLQLRNKEVTWEVLEGEVEKEALKKIIEDQQESLNKWKSKGRRFKGKGKGNKAAQPGSGKGKVQFQGKKTKFASDDEHDEHDENGATGPVKRAREETDKEEPASKQQKTENGAGDQ Disordered 326 408 LNKWKSKGRRFKGKGKGNKAAQPGSGKGKVQFQGKKTKFASDDEHDEHDENGATGPVKRAREETDKEEPASKQQKTENGAGDQ Fragment Native Relationship to function unknown Unknown Unknown Analytical ultracentrifugation 293 7 DTT 0.5 KCl 100 Tris-HCl buffer 20 Nuclear magnetic resonance (NMR) DTT pH 7.0 1 KCl buffer 100 Tris-HCl buffer 20 Nuclear magnetic resonance (NMR) DTT pH 5.8 to 6.5 1 KCl buffer 100 sodium acetate buffer 20 Circular dichroism (CD) spectroscopy, far-UV 295 KF pH 7 100 NaH2PO4 10 Paper 12842046 Jacks A, Babon J, Kelly G, Manolaridis I, Cary PD, Curry S, Conte MR 2003 Structure (Camb) 11 7 833-43 Disordered 1 5 MAENG Engineered Fragment 1YTYA PDB 16387655 Teplova M, Yuan YR, Phan AT, Malinina L, Ilin S, Teplov A, Patel DJ 2006 Mol Cell 21 1 75-85 This disordered protein entry is based solely on missing electron density in the Protein Data Bank. Disordered 190 194 AKKNE Engineered Fragment 1YTYA PDB 16387655 Teplova M, Yuan YR, Phan AT, Malinina L, Ilin S, Teplov A, Patel DJ 2006 Mol Cell 21 1 75-85 This disordered protein entry is based solely on missing electron density in the Protein Data Bank. Disordered 225 230 SLEEKI Fragment Relationship to function unknown Unknown Unknown Analytical ultracentrifugation 293 DTT pH 7.0 0.5 KCl 100 Tris-HCl 20 Nuclear magnetic resonance (NMR) 7 DTT 1 KCl 100 Tris-HCl 20 Nuclear magnetic resonance (NMR) DTT pH 5.8-6.5 1 KCl 100 sodium acetate 20 Circular dichroism (CD) spectroscopy, far-UV 295 KF pH 7.0 100 NaH2PO4 10 Paper 12842046 Jacks A, Babon J, Kelly G, Manolaridis I, Cary PD, Curry S, Conte MR 2003 Structure (Camb) 11 7 833-43 Disordered 1 8 MAENGDNE Native Function arises from the disordered state Unknown Unknown Nuclear magnetic resonance (NMR) 293 7 DTT 1 KCl 100 Tris-HCl 20 Paper 15004549 Alfano C, Sanfelice D, Babon J, Kelly G, Jacks A, Curry S, Conte MR 2004 Nat Struct Mol Biol 11 4 323-9 Growth factor receptor-bound protein 14 GRB14_HUMAN GRB14 adapter protein Q14449 Hs.411881 GRB14_HUMAN 59802920 Homo sapiens (Human) 540 MTTSLQDGQSAASRAAARDSPLAAQVCGAAQGRGDAHDLAPAPWLHARALLPLPDGTRGCAADRRKKKDLDVPEMPSIPNPFPELCCSPITSVLSADLFPKANSRKKQVIKVYSEDETSRALDVPSDITARDVCQLLILKNHYIDDHSWTLFEHLPHIGVERTIEDHELVIEVLSNWGIEEENKLYFRKNYAKYEFFKNPMYFFPEHMVSFATETNGEISPTQILQMFLSSSTYPEIHGFLHAKEQGKKSWKKIYFFLRRSGLYFSTKGTSKEPRHLQFFSEFGNSDIYVSLAGKKKHGAPTNYGFCFKPNKAGGPRDLKMLCAEEEQSRTCWVTAIRLLKYGMQLYQNYMHPYQGRSGCSSQSISPMRSISENSLVAMDFSGQKSRVIENPTEALSVAVEEGLAWRKKGCLRLGTHGSPTASSQSSATNMAIHRSQPWFHHKISRDEAQRLIIQQGLVDGVFLVRDSQSNPKTFVLSMSHGQKIKHFQIIPVEDDGEMFHTLDDGHTRFTDLIQLVEFYQLNKGVLPCKLKHYCARIAL Disordered PIR domain 361 435 SSQSISPMRSISENSLVAMDFSGQKSRVIENPTEALSVAVEEGLAWRKKGCLRLGTHGSPTASSQSSATNMAIHR Fragment Native Function arises via a disorder to order transition Molecular assembly Protein-protein binding Nuclear magnetic resonance (NMR) 300 Stability at thermal extremes Paper 14623073 Moncoq K, Broutin I, Larue V, Perdereau D, Cailliau K, Browaeys-Poly E, Burnol AF, Ducruix A 2003 FEBS Lett 554 3 240-6 POU domain, class 2, transcription factor 1 PO2F1_HUMAN Octamer-binding transcription factor 1 Oct-1 OTF-1 NF-A1 P14859 Hs.493649 PO2F1_HUMAN 28202257 Homo sapiens (Human) 743 MNNPSETSKPSMESGDGNTGTQTNGLDFQKQPVPVGGAISTAQAQAFLGHLHQVQLAGTSLQAAAQSLNVQSKSNEESGDSQQPSQPSQQPSVQAAIPQTQLMLAGGQITGLTLTPAQQQLLLQQAQAQAQLLAAAVQQHSASQQHSAAGATISASAATPMTQIPLSQPIQIAQDLQQLQQLQQQNLNLQQFVLVHPTTNLQPAQFIISQTPQGQQGLLQAQNLLTQLPQQSQANLLQSQPSITLTSQPATPTRTIAATPIQTLPQSQSTPKRIDTPSLEEPSDLEELEQFAKTFKQRRIKLGFTQGDVGLAMGKLYGNDFSQTTISRFEALNLSFKNMCKLKPLLEKWLNDAENLSSDSSLSSPSALNSPGIEGLSRRRKKRTSIETNIRVALEKSFLENQKPTSEEITMIADQLNMEKEVIRVWFCNRRQKEKRINPPSSGGTSSSPIKAIFPSPTSLVATTPSLVTSSAATTLTVSPVLPLTSAAVTNLSVTGTSDTTSNNTATVISTAPPASSAVTSPSLSPSPSASASTSEASSASETSTTQTTSTPLSSPLGTSQVMVTASGLQTAAAAALQGAAQLPANASLAAMAAAAGLNPSLMAPSQFAAGGALLSLNPGTLSGALSPALMSNSTLATIQALASGGSLPITSLDATGNLVFANAGGAPNIVTAPLFLNPQNLSLLTSNPVSLVSAAAASAGNSAPVASLHATSTSAESIQNSLFTVASASGAASTTTTASKAQ Disordered 355 359 NLSSD Fragment Native Function arises from the disordered state Entropic chain Flexible linkers/spacers Nuclear magnetic resonance (NMR) Paper 8479524 Dekker N, Cox M, Boelens R, Verrijzer CP, van der Vliet PC, Kaptein R 1993 Nature 362 6423 852-5 Disordered activation domain 1 200 MNNPSETSKPSMESGDGNTGTQTNGLDFQKQPVPVGGAISTAQAQAFLGHLHQVQLAGTSLQAAAQSLNVQSKSNEESGDSQQPSQPSQQPSVQAAIPQTQLMLAGGQITGLTLTPAQQQLLLQQAQAQAQLLAAAVQQHSASQQHSAAGATISASAATPMTQIPLSQPIQIAQDLQQLQQLQQQNLNLQQFVLVHPTTN Complex Fragment Native Function arises from the disordered state Molecular recognition effectors Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV Paper 11380252 Lee L, Stollar E, Chang J, Grossmann JG, O'Brien R, Ladbury J, Carpenter B, Roberts S, Luisi B 2001 Biochemistry 40 22 6580-8 There was no increase in structure when a fragment of Oct-1 containing the activation domain was incubated with the binding partner, Bob-1. Disordered activation domain 1 200 MNNPSETSKPSMESGDGNTGTQTNGLDFQKQPVPVGGAISTAQAQAFLGHLHQVQLAGTSLQAAAQSLNVQSKSNEESGDSQQPSQPSQQPSVQAAIPQTQLMLAGGQITGLTLTPAQQQLLLQQAQAQAQLLAAAVQQHSASQQHSAAGATISASAATPMTQIPLSQPIQIAQDLQQLQQLQQQNLNLQQFVLVHPTTN Fragment Monomeric Native Function arises from the disordered state Molecular recognition effectors Protein-protein binding Small-angle X-ray scattering (SAXS) Nuclear magnetic resonance (NMR) Circular dichroism (CD) spectroscopy, far-UV Fluorescence, intrinsic Paper 11380252 Lee L, Stollar E, Chang J, Grossmann JG, O'Brien R, Ladbury J, Carpenter B, Roberts S, Luisi B 2001 Biochemistry 40 22 6580-8 Disordered 355 378 NLSSDSSLSSPSALNSPGIEGLSR Function arises from the disordered state Entropic chain Flexible linkers/spacers X-ray crystallography Paper 8479524 Dekker N, Cox M, Boelens R, Verrijzer CP, van der Vliet PC, Kaptein R 1993 Nature 362 6423 852-5 8156594 Klemm JD, Rould MA, Aurora R, Herr W, Pabo CO 1994 Cell 77 1 21-32 Protein phosphatase inhibitor 2 IPP2_RABIT IPP-2 P11845 Ocu.1811 IPP2_RABIT 1170582 Oryctolagus cuniculus (Rabbit) 205 MAASTASHRPIKGILKNKTSSTSSRVASAEQPRGSVDEELSKKSQKWDEMNILATYHPADKDYGLMKIDEPSTPYHSMIGDDDDAYSDTETTEAMTPDTLAKKLAAAEGSEPKYRIREQESSGEEDSDLSPEEREKKRQFEMKRKLHYNEGLNIKLARQLISKDLHDDEEDEEMSETADGESMNTEESNQGSTPSDQRQNKSQSS Disordered 1 205 MAASTASHRPIKGILKNKTSSTSSRVASAEQPRGSVDEELSKKSQKWDEMNILATYHPADKDYGLMKIDEPSTPYHSMIGDDDDAYSDTETTEAMTPDTLAKKLAAAEGSEPKYRIREQESSGEEDSDLSPEEREKKRQFEMKRKLHYNEGLNIKLARQLISKDLHDDEEDEEMSETADGESMNTEESNQGSTPSDQRQNKSQSS Monomeric Native Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Analytical ultracentrifugation Size exclusion/gel filtration chromatography Stability at thermal extremes SDS-PAGE gel, Aberrant mobility on Stability at pH extremes Paper 6245879 Foulkes JG, Cohen P 1980 Eur J Biochem 105 1 195-203 10807923 Yang J, Hurley TD, DePaoli-Roach AA 2000 J Biol Chem 275 30 22635-44 Additional UniGene: Ocu.6939 Fibrinogen alpha chain [Isoform 1 (Alpha-E)] FIBA_CHICK Fibrinopeptide A [cleavage product 1] P14448-1 Gga.34280 FIBA_CHICK 1706798 Gallus gallus (Chicken) 741 MIPVTILCVLLCLNLAWAQDGKTTFEKEGGGGRGPRILENMHESSCKYEKNWPICVDDDWGTKCPSCCRMQGIIDDTDQNYSQRIDNIRQQLADSQNKYKTSNRVIVETINILKPGLEGAQQLDENYGHVSTELRRRIVTLKQRVATQVNRIKALQNSIQEQVVEMKRLEVDIDIKIRACKGSCARSFDYQVDKEGYDNIQKHLTQASSIDMHPDFQTTTLSTLKMRPLKDSNVPEHFKLKPSPEMQAMSAFNNIKQMQVVLERPETDHVAEARGDSSPSHTGKLITSSHRRESPSLVDKTSSASSVHRCTRTVTKKVISGPDGPREEIVEKMVSSDGSDCSHLQGGREGSTYHFSGTGDFHKLDRLLPDLESFFTHDSVSTSSRHSIGSSTSSHVTGAGSSHLGTGGKDKFTDLGEEEEDDFGGLQPSGFAAGSASHSKTVLTSSSSSFNKGGSTFETKSLKTRETSEQLGGVQHDQSAEDTPDFKARSFRPAAMSTRRSYNGKDCDDIRQKHTSGAKSGIFKIKPEGSNKVLSVYCDQETTLGGWLLIQQRMDGSVNFNRTWQDYRRGFGSVDGKGQGELWLGNENIHLLTQNDTLLRVELEDWDGNAAYAEYIVQVGTEAEGYALTVSSYEGTAGDALVAGWLEEGSEYTSHAQMQFSTFDRDQDHWEESCAEVYGGGWWYNSCQAANLNGIYYPGGHYDPRYNVPYEIENGVVWIPFRASDYSLKVVRMKIRPLETL Disordered 19 44 QDGKTTFEKEGGGGRGPRILENMHES Fragment Native 1M1JA X-ray crystallography Paper 11601975 Yang Z, Kollman JM, Pandi L, Doolittle RF 2001 Biochemistry 40 42 12515-23 Disordered 237 509 HFKLKPSPEMQAMSAFNNIKQMQVVLERPETDHVAEARGDSSPSHTGKLITSSHRRESPSLVDKTSSASSVHRCTRTVTKKVISGPDGPREEIVEKMVSSDGSDCSHLQGGREGSTYHFSGTGDFHKLDRLLPDLESFFTHDSVSTSSRHSIGSSTSSHVTGAGSSHLGTGGKDKFTDLGEEEEDDFGGLQPSGFAAGSASHSKTVLTSSSSSFNKGGSTFETKSLKTRETSEQLGGVQHDQSAEDTPDFKARSFRPAAMSTRRSYNGKDCDD Fragment Native 1M1JA Paper 11601975 Yang Z, Kollman JM, Pandi L, Doolittle RF 2001 Biochemistry 40 42 12515-23 Disordered residues lie within the region for cleavage product 1, however, there is no experimental evidence that indicates that this product is disordered. Fibrinogen beta chain FIBB_CHICK Fibrinopeptide B [cleavage product 1] Q02020 Gga.41812 FIBB_CHICK 399491 Gallus gallus (Chicken) 463 ASVEYDNEEDSPQIDARAHRPLDKRQEAAPTLRPVAPPISGTGYQPRPPKQDKQAMKKGPIIYPDAGGCKHPLDELGVLCPTGCELQTTLLKQEKTVKPVLRDLKDRVAKFSDTSTTMYQYVNMIDNKLVKTQKQRKDNDIILSEYNTEMELHYNYIKDNLDNNIPSSLRVLRAVIDSLHKKIQKLENAIATQTDYCRSPCVASCNIPVVSGRECEDIYRKGGETSEMYIIQPDPFTTPYRVYCDMETDNGGWTLIQNRQDGSVNFGRAWDEYKRGFGNIAKSGGKKYCDTPGEYWLGNDKISQLTKIGPTKVLIEMEDWNGDKVSALYGGFTIHNEGNKYQLSVSNYKGNAGNALMEGASQLYGENRTMTIHNGMYFSTYDRDNDGWLTTDPRKQCSKEDGGGWWYNRCHAANPNGRYYWGGTYSWDMAKHGTDDGIVWMNWKGSWYSMKKMSMKIKPYFPD Disordered 1 62 ASVEYDNEEDSPQIDARAHRPLDKRQEAAPTLRPVAPPISGTGYQPRPPKQDKQAMKKGPII Fragment Native 1M1JB X-ray crystallography Paper 11601975 Yang Z, Kollman JM, Pandi L, Doolittle RF 2001 Biochemistry 40 42 12515-23 Disordered residues lie within the region for cleavage product 1, however, there is no experimental evidence that indicates that this product is disordered. Fibrinogen gamma chain O93568_CHICK O93568 Gga.1165 O93568_CHICK 82123696 Gallus gallus (Chicken) 435 MMGVKSVTSRLAVGDLLSLLFSTSMAYIATRENCCILDERFGSYCPTTCGIADFFNKYRLTTDGELLEIEGLLQQATNSTGSIEYLIQHIKTIYPSEKQTLPQSIEQLTQKSKKIIEEIIRYENTILAHENTIQQLTDMHIMNSNKITQLKQKIAQLESHCQEPCKDTAEIQETTGRDCQDIANKGARKSGLYFIKPQKAKQSFLVYCEIDTYGNGWTVLQRRLDGSEDFRRNWVQYKEGFGHLSPDDTTEFWLGNEKIHLITTQSTLPYALRIELEDWSGKKGTADYAVFKVGTEEDKYRLTYAYFIGGERGDAFDGFNFGDDPSDKSYTYHNGMRFSTFDNDNDNFEGNCAEQDGSGWWMNRCHAGHLNGPYYIGGVYSRDTGTNSYDNGIIWATWRDRWYSMKKTTMKIIPFNRLSIDGQQHSGGLKQVGDS Disordered 27 29 YIA Fragment Native 1M1JC X-ray crystallography Paper 11601975 Yang Z, Kollman JM, Pandi L, Doolittle RF 2001 Biochemistry 40 42 12515-23 Disordered 420 435 IDGQQHSGGLKQVGDS Fragment Native 1M1JC X-ray crystallography Paper 11601975 Yang Z, Kollman JM, Pandi L, Doolittle RF 2001 Biochemistry 40 42 12515-23 Myelin basic protein MBP_HUMAN MBP Myelin A1 protein Myelin membrane encephalitogenic protein P02686 Hs.551713 MBP_HUMAN 17378805 Homo sapiens (Human) 304 MGNHAGKRELNAEKASTNSETNRGESEKKRNLGELSRTTSEDNEVFGEADANQNNGTSSQDTAVTDSKRTADPKNAWQDAHPADPGSRPHLIRLFSRDAPGREDNTFKDRPSESDELQTIQEDSAATSESLDVMASQKRPSQRHGSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFGGDRGAPKRGSGKDSHHPARTAHYGSLPQKSHGRTQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQRPGFGYGGRASDYKSAHKGFKGVDAQGTLSKIFKLGGRDSRSGSPMARR Disordered 134 304 MASQKRPSQRHGSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFGGDRGAPKRGSGKDSHHPARTAHYGSLPQKSHGRTQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQRPGFGYGGRASDYKSAHKGFKGVDAQGTLSKIFKLGGRDSRSGSPMARR Isoform Mutant Relationship to function unknown Molecular assembly Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV 294 7.2 Tris buffer 0.3 Paper 7500383 Deibler GE, Burlin TV, Stone AL 1995 J Neurosci Res 41 6 819-27 The experimental sequence was the 18.5 kDa isoform and therefore did not include residues 1 - 133 of the sequence listed in SwissProt. Myelin basic protein MBP_MOUSE MBP Myelin A1 protein P04370 Mm.252063 MBP_MOUSE 17378829 Mus musculus (Mouse) 169 MASQKRPSQRSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFSGDRGAPKRGSGKDSHTRTTHYGSLPQKSQHGRTQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQKPGFGYGGRASDYKSAHKGFKGAYDAQGTLSKIFKLGGRDSRSGSPMARR Disordered 1 169 MASQKRPSQRSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFSGDRGAPKRGSGKDSHTRTTHYGSLPQKSQHGRTQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQKPGFGYGGRASDYKSAHKGFKGAYDAQGTLSKIFKLGGRDSRSGSPMARR Engineered Isoform Mutant Relationship to function unknown Molecular assembly Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV Paper 12372316 Hill CM, Bates IR, White GF, Hallett FR, Harauz G 2002 J Struct Biol 139 1 13-26 The experimental sequence was the 18.5 kDa isoform. The experimental sequence had a C-terminal hexahistidine tagged. Disordered 33 46 Function arises via a disorder to order transition Paper 18326633 Libich DS, Harauz G 2008 Biophys J 94 12 4847-66 Additional UniGene IDs: Mm.392350 and Mm.454459 Breast cancer type 1 susceptibility protein BRCA1_HUMAN RING finger protein 53 BRCA1 P38398 Hs.194143 BRCA1_HUMAN 728984 Homo sapiens (Human) 1863 MDLSALRVEEVQNVINAMQKILECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCKNDITKRSLQESTRFSQLVEELLKIICAFQLDTGLEYANSYNFAKKENNSPEHLKDEVSIIQSMGYRNRAKRLLQSEPENPSLQETSLSVQLSNLGTVRTLRTKQRIQPQKTSVYIELGSDSSEDTVNKATYCSVGDQELLQITPQGTRDEISLDSAKKAACEFSETDVTNTEHHQPSNNDLNTTEKRAAERHPEKYQGSSVSNLHVEPCGTNTHASSLQHENSSLLLTKDRMNVEKAEFCNKSKQPGLARSQHNRWAGSKETCNDRRTPSTEKKVDLNADPLCERKEWNKQKLPCSENPRDTEDVPWITLNSSIQKVNEWFSRSDELLGSDDSHDGESESNAKVADVLDVLNEVDEYSGSSEKIDLLASDPHEALICKSERVHSKSVESNIEDKIFGKTYRKKASLPNLSHVTENLIIGAFVTEPQIIQERPLTNKLKRKRRPTSGLHPEDFIKKADLAVQKTPEMINQGTNQTEQNGQVMNITNSGHENKTKGDSIQNEKNPNPIESLEKESAFKTKAEPISSSISNMELELNIHNSKAPKKNRLRRKSSTRHIHALELVVSRNLSPPNCTELQIDSCSSSEEIKKKKYNQMPVRHSRNLQLMEGKEPATGAKKSNKPNEQTSKRHDSDTFPELKLTNAPGSFTKCSNTSELKEFVNPSLPREEKEEKLETVKVSNNAEDPKDLMLSGERVLQTERSVESSSISLVPGTDYGTQESISLLEVSTLGKAKTEPNKCVSQCAAFENPKGLIHGCSKDNRNDTEGFKYPLGHEVNHSRETSIEMEESELDAQYLQNTFKVSKRQSFAPFSNPGNAEEECATFSAHSGSLKKQSPKVTFECEQKEENQGKNESNIKPVQTVNITAGFPVVGQKDKPVDNAKCSIKGGSRFCLSSQFRGNETGLITPNKHGLLQNPYRIPPLFPIKSFVKTKCKKNLLEENFEEHSMSPEREMGNENIPSTVSTISRNNIRENVFKEASSSNINEVGSSTNEVGSSINEIGSSDENIQAELGRNRGPKLNAMLRLGVLQPEVYKQSLPGSNCKHPEIKKQEYEEVVQTVNTDFSPYLISDNLEQPMGSSHASQVCSETPDDLLDDGEIKEDTSFAENDIKESSAVFSKSVQKGELSRSPSPFTHTHLAQGYRRGAKKLESSEENLSSEDEELPCFQHLLFGKVNNIPSQSTRHSTVATECLSKNTEENLLSLKNSLNDCSNQVILAKASQEHHLSEETKCSASLFSSQCSELEDLTANTNTQDPFLIGSSKQMRHQSESQGVGLSDKELVSDDEERGTGLEENNQEEQSMDSNLGEAASGCESETSVSEDCSGLSSQSDILTTQQRDTMQHNLIKLQQEMAELEAVLEQHGSQPSNSYPSIISDSSALEDLRNPEQSTSEKAVLTSQKSSEYPISQNPEGLSADKFEVSADSSTSKNKEPGVERSSPSKCPSLDDRWYMHSCSGSLQNRNYPSQEELIKVVDVEEQQLEESGPHDLTETSYLPRQDLEGTPYLESGISLFSDDPESDPSEDRAPESARVGNIPSSTSALKVPQLKVAESAQSPAAAHTTDTAGYNAMEESVSREKPELTASTERVNKRMSMVVSGLTPEEFMLVYKFARKHHITLTNLITEETTHVVMKTDAEFVCERTLKYFLGIAGGKWVVSYFWVTQSIKERKMLNEHDFEVRGDVVNGRNHQGPKRARESQDRKIFRGLEICCYGPFTNMPTDQLEWMVQLCGASVVKELSSFTLGTGVHPIVVVQPDAWTEDNGFHAIGQMCEAPVVTREWVLDSVALYQCQELDTYLIPQIPHSHY Disordered 170 1649 RIQPQKTSVYIELGSDSSEDTVNKATYCSVGDQELLQITPQGTRDEISLDSAKKAACEFSETDVTNTEHHQPSNNDLNTTEKRAAERHPEKYQGSSVSNLHVEPCGTNTHASSLQHENSSLLLTKDRMNVEKAEFCNKSKQPGLARSQHNRWAGSKETCNDRRTPSTEKKVDLNADPLCERKEWNKQKLPCSENPRDTEDVPWITLNSSIQKVNEWFSRSDELLGSDDSHDGESESNAKVADVLDVLNEVDEYSGSSEKIDLLASDPHEALICKSERVHSKSVESNIEDKIFGKTYRKKASLPNLSHVTENLIIGAFVTEPQIIQERPLTNKLKRKRRPTSGLHPEDFIKKADLAVQKTPEMINQGTNQTEQNGQVMNITNSGHENKTKGDSIQNEKNPNPIESLEKESAFKTKAEPISSSISNMELELNIHNSKAPKKNRLRRKSSTRHIHALELVVSRNLSPPNCTELQIDSCSSSEEIKKKKYNQMPVRHSRNLQLMEGKEPATGAKKSNKPNEQTSKRHDSDTFPELKLTNAPGSFTKCSNTSELKEFVNPSLPREEKEEKLETVKVSNNAEDPKDLMLSGERVLQTERSVESSSISLVPGTDYGTQESISLLEVSTLGKAKTEPNKCVSQCAAFENPKGLIHGCSKDNRNDTEGFKYPLGHEVNHSRETSIEMEESELDAQYLQNTFKVSKRQSFAPFSNPGNAEEECATFSAHSGSLKKQSPKVTFECEQKEENQGKNESNIKPVQTVNITAGFPVVGQKDKPVDNAKCSIKGGSRFCLSSQFRGNETGLITPNKHGLLQNPYRIPPLFPIKSFVKTKCKKNLLEENFEEHSMSPEREMGNENIPSTVSTISRNNIRENVFKEASSSNINEVGSSTNEVGSSINEIGSSDENIQAELGRNRGPKLNAMLRLGVLQPEVYKQSLPGSNCKHPEIKKQEYEEVVQTVNTDFSPYLISDNLEQPMGSSHASQVCSETPDDLLDDGEIKEDTSFAENDIKESSAVFSKSVQKGELSRSPSPFTHTHLAQGYRRGAKKLESSEENLSSEDEELPCFQHLLFGKVNNIPSQSTRHSTVATECLSKNTEENLLSLKNSLNDCSNQVILAKASQEHHLSEETKCSASLFSSQCSELEDLTANTNTQDPFLIGSSKQMRHQSESQGVGLSDKELVSDDEERGTGLEENNQEEQSMDSNLGEAASGCESETSVSEDCSGLSSQSDILTTQQRDTMQHNLIKLQQEMAELEAVLEQHGSQPSNSYPSIISDSSALEDLRNPEQSTSEKAVLTSQKSSEYPISQNPEGLSADKFEVSADSSTSKNKEPGVERSSPSKCPSLDDRWYMHSCSGSLQNRNYPSQEELIKVVDVEEQQLEESGPHDLTETSYLPRQDLEGTPYLESGISLFSDDPESDPSEDRAPESARVGNIPSSTSALKVPQLKVAESAQSPAAAHTTDTAGYNAMEESVSREKPELTASTERVNKR Fragment Native Relationship to function unknown Molecular recognition effectors Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV Nuclear magnetic resonance (NMR) Paper 15571721 Mark WY, Liao JC, Lu Y, Ayed A, Laister R, Szymczyna B, Chakrabartty A, Arrowsmith CH 2005 J Mol Biol 345 2 275-87 The structure of the 1480 residue central region was investigated by characterizing 21 different fragments. Disordered 1812 1823 PDAWTEDNGFHA Nuclear magnetic resonance (NMR) 296 6.8 DTT 10 K2HPO4 10 KCl 5 KH2PO4 10 Paper 15609993 Gaiser OJ, Ball LJ, Schmieder P, Leitner D, Strauss H, Wahl M, Kuhne R, Oschkinat H, Heinemann U 2004 Biochemistry 43 51 15983-95 Disordered 1799 1804 TLGTGV Nuclear magnetic resonance (NMR) 296 6.8 DTT 10 K2HPO4 10 KCl 5 KH2PO4 10 Paper 15609993 Gaiser OJ, Ball LJ, Schmieder P, Leitner D, Strauss H, Wahl M, Kuhne R, Oschkinat H, Heinemann U 2004 Biochemistry 43 51 15983-95 Disordered 1773 1777 TNMPT Nuclear magnetic resonance (NMR) 296 6.8 DTT 10 K2HPO4 10 KCl 5 KH2PO4 10 Paper 15609993 Gaiser OJ, Ball LJ, Schmieder P, Leitner D, Strauss H, Wahl M, Kuhne R, Oschkinat H, Heinemann U 2004 Biochemistry 43 51 15983-95 Disordered 1755 1758 SQDR Nuclear magnetic resonance (NMR) 296 6.8 KH2PO4 10 K2HPO4 10 KCl 5 DTT 10 Paper 15609993 Gaiser OJ, Ball LJ, Schmieder P, Leitner D, Strauss H, Wahl M, Kuhne R, Oschkinat H, Heinemann U 2004 Biochemistry 43 51 15983-95 Carbon monoxide dehydrogenase COOS_RHORU CODH EC=1.2.99.2 P31896 COOS_RHORU 399279 Rhodospirillum rubrum 639 MTHHDCAHCSSDACATEMLNLAEANSIETAWHRYEKQQPQCGFGSAGLCCRICLKGPCRIDPFGEGPKYGVCGADRDTIVARHLVRMIAAGTAAHSEHGRHIALAMQHISQGELHDYSIRDEAKLYAIAKTLGVATEGRGLLAIVGDLAAITLGDFQNQDYDKPCAWLAASLTPRRVKRLGDLGLLPHNIDASVAQTMSRTHVGCDADPTNLILGGLRVAMADLDGSMLATELSDALFGTPQPVVSAANLGVMKRGAVNIAVNGHNPMLSDIICDVAADLRDEAIAAGAAEGINIIGICCTGHEVMMRHGVPLATNYLSQELPILTGALEAMVVDVQCIMPSLPRIAECFHTQIITTDKHNKISGATHVPFDEHKAVETAKTIIRMAIAAFGRRDPNRVAIPAFKQKSIVGFSAEAVVAALAKVNADDPLKPLVDNVVNGNIQGIVLFVGCNTTKVQQDSAYVDLAKSLAKRNVLVLATGCAAGAFAKAGLMTSEATTQYAGEGLKGVLSAIGTAAGLGGPLPLVMHMGSCVDNSRAVALATALANKLGVDLSDLPLVASAPECMSEKALAIGSWAVTIGLPTHVGSVPPVIGSQIVTKLVTETAKDLVGGYFIVDTDPKSAGDKLYAAIQERRAGLGL Disordered 1 27 MTHHDCAHCSSDACATEMLNLAEANSI Complex Function arises from the disordered state Unknown Substrate/ligand binding X-ray crystallography polyethylene glycol 8000 10% 2-methyl-2,4-pentanediol 5% calcium chloride 0.4 Tris buffer pH 7.5 0.1 Paper 11593006 Drennan CL, Heo J, Sintchak MD, Schreiter E, Ludden PW 2001 Proc Natl Acad Sci U S A 98 21 11973-8 Disordered 638 639 GL Complex Function arises from the disordered state Unknown Substrate/ligand binding X-ray crystallography 2-methyl-2,4-pentanediol 5% calcium chloride 0.4 polyethylene glycol 8000 10% Tris buffer pH 7.5 0.1 Paper 11593006 Drennan CL, Heo J, Sintchak MD, Schreiter E, Ludden PW 2001 Proc Natl Acad Sci U S A 98 21 11973-8 CODH is organized as a dimer which has two Ni-Fe-S C-clusters, two [Fe4S4] B-clusters, and an [Fe4S4] cluster (bridge between the monomers). Alpha-adducin [Isoform 1] ADDA_HUMAN Erythrocyte adducin subunit alpha P35611-1 Hs.183706 ADDA_HUMAN 12644231 Homo sapiens (Human) 737 MNGDSRAAVVTSPPPTTAPHKERYFDRVDENNPEYLRERNMAPDLRQDFNMMEQKKRVSMILQSPAFCEELESMIQEQFKKGKNPTGLLALQQIADFMTTNVPNVYPAAPQGGMAALNMSLGMVTPVNDLRGSDSIAYDKGEKLLRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDRGSTNLGVNQAGFTLHSAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSLGEVAYHDYHGILVDEEEKVLIQKNLGPKSKVLILRNHGLVSVGESVEEAFYYIHNLVVACEIQVRTLASAGGPDNLVLLNPEKYKAKSRSPGSPVGEGTGSPPKWQIGEQEFEALMRMLDNLGYRTGYPYRYPALREKSKKYSDVEVPASVTGYSFASDGDSGTCSPLRHSFQKQQREKTRWLNSGRGDEASEEGQNGSSPKSKTKWTKEDGHRTSTSAVPNLFVPLNTNPKEVQEMRNKIREQNLQDIKTAGPQSQVLCGVVMDRSLVQGELVTASKAIIEKEYQPHVIVSTTGPNPFTTLTDRELEEYRREVERKQKGSEENLDEAREQKEKSPPDQPAVPHPPPSTPIKLEEDLVPEPTTGDDSDAATFKPTLPDLSPDEPSEALGFPMLEKEEEAHRPPSPTEAPTEASPEPAPDPAPVAEEAAPSAVEEGAAADPGSDGSPGKSPSKKKKKFRTPSFLKKSKKKSDS Disordered tail 430 737 CSPLRHSFQKQQREKTRWLNSGRGDEASEEGQNGSSPKSKTKWTKEDGHRTSTSAVPNLFVPLNTNPKEVQEMRNKIREQNLQDIKTAGPQSQVLCGVVMDRSLVQGELVTASKAIIEKEYQPHVIVSTTGPNPFTTLTDRELEEYRREVERKQKGSEENLDEAREQKEKSPPDQPAVPHPPPSTPIKLEEDLVPEPTTGDDSDAATFKPTLPDLSPDEPSEALGFPMLEKEEEAHRPPSPTEAPTEASPEPAPDPAPVAEEAAPSAVEEGAAADPGSDGSPGKSPSKKKKKFRTPSFLKKSKKKSDS Fragment Monomeric Native Relationship to function unknown Molecular assembly Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV SDS-PAGE gel, Aberrant mobility on Sensitivity to proteolysis Paper 7642559 Hughes CA, Bennett V 1995 J Biol Chem 270 32 18990-6 Beta-adducin [Isoform 1] ADDB_HUMAN Erythrocyte adducin subunit beta P35612-1 Hs.188528 ADDB_HUMAN 543774 Homo sapiens (Human) 726 MSEETVPEAASPPPPQGQPYFDRFSEDDPEYMRLRNRAADLRQDFNLMEQKKRVTMILQSPSFREELEGLIQEQMKKGNNSSNIWALRQIADFMASTSHAVFPTSSMNVSMMTPINDLHTADSLNLAKGERLMRCKISSVYRLLDLYGWAQLSDTYVTLRVSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKGSSCFPVDTTGFCLHSAIYAARPDVRCIIHLHTPATAAVSAMKWGLLPVSHNALLVGDMAYYDFNGEMEQEADRINLQKCLGPTCKILVLRNHGVVALGDTVEEAFYKIFHLQAACEIQVSALSSAGGVENLILLEQEKHRPHEVGSVQWAGSTFGPMQKSRLGEHEFEALMRMLDNLGYRTGYTYRHPFVQEKTKHKSEVEIPATVTAFVFEEDGAPVPALRQHAQKQQKEKTRWLNTPNTYLRVNVADEVQRSMGSPRPKTTWMKADEVEKSSSGMPIRIENPNQFVPLYTDPQEVLEMRNKIREQNRQDVKSAGPQSQLLASVIAEKSRSPSTESQLMSKGDEDTKDDSEETVPNPFSQLTDQELEEYKKEVERKKLELDGEKETAPEEPGSPAKSAPASPVQSPAKEAETKSPLVSPSKSLEEGTKKTETSKAATTEPETTQPEGVVVNGREEEQTAEEILSKGLSQMTTSADTDVDTSKDKTESVTSGPMSPEGSPSKSPSKKKKKFRTPSFLKKSKKKEKVES Disordered tail 409 726 FEEDGAPVPALRQHAQKQQKEKTRWLNTPNTYLRVNVADEVQRSMGSPRPKTTWMKADEVEKSSSGMPIRIENPNQFVPLYTDPQEVLEMRNKIREQNRQDVKSAGPQSQLLASVIAEKSRSPSTESQLMSKGDEDTKDDSEETVPNPFSQLTDQELEEYKKEVERKKLELDGEKETAPEEPGSPAKSAPASPVQSPAKEAETKSPLVSPSKSLEEGTKKTETSKAATTEPETTQPEGVVVNGREEEQTAEEILSKGLSQMTTSADTDVDTSKDKTESVTSGPMSPEGSPSKSPSKKKKKFRTPSFLKKSKKKEKVES Fragment Monomeric Native Relationship to function unknown Molecular assembly Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV SDS-PAGE gel, Aberrant mobility on Sensitivity to proteolysis Paper 7642559 Hughes CA, Bennett V 1995 J Biol Chem 270 32 18990-6 30S ribosomal protein S17 RS17_ECOLI P0AG63 RS17_ECOLI 84028294 Escherichia coli 83 TDKIRTLQGRVVSDKMEKSIVVAIERFVKHPIYGKFIKRTTKLHVHDENNECGIGDVVEIRECRPLSKTKSWTLVRVVEKAVL Disordered 1 83 TDKIRTLQGRVVSDKMEKSIVVAIERFVKHPIYGKFIKRTTKLHVHDENNECGIGDVVEIRECRPLSKTKSWTLVRVVEKAVL Monomeric Native Relationship to function unknown Molecular assembly Unknown Circular dichroism (CD) spectroscopy, far-UV Paper 6751823 Venyaminov SY, Gogia ZV 1982 Eur J Biochem 126 2 299-309 DNA-repair protein complementing XP-A cells Xeroderma pigmentosum group A complementing protein [H. sapiens] XPA XPA_HUMAN P23025 XPA_HUMAN Homo sapiens (Human) 273 MAAADGALPEAAALEQPAELPASVRASIERKRQRALMLRQARLAARPYSATAAAATGGMANVKAAPKIIDTGGGFILEEEEEEEQKIGKVVHQPGPVMEFDYVICEECGKEFMDSYLMNHFDLPTCDNCRDADDKHKLITKTEAKQEYLLKDCDLEKREPPLKFIVKKNPHHSQWGDMKLYLKLQIVKRSLEVWGSQEALEEAKEVRQENREKMKQKKFDKKVKELRRAVRSSVWKRETIVHQHEYGPEENLEDDMYRKTCTMCGHELTYEKM Disordered 158 158 R Fragment 1XPAA Nuclear magnetic resonance (NMR) 303 6.5 Paper 9699634 Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M 1998 Nat Struct Biol 5 8 701-706 10050037 Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M 1999 J Biochem (Tokyo) 125 3 495-506 Disordered 168 179 KNPHHSQWGDMK Fragment 1XPAA Nuclear magnetic resonance (NMR) 303 6.5 Paper 9699634 Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M 1998 Nat Struct Biol 5 8 701-706 10050037 Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M 1999 J Biochem (Tokyo) 125 3 495-506 Disordered 206 219 VRQENREKMKQKKF Fragment 1XPAA Nuclear magnetic resonance (NMR) 303 6.5 Paper 9699634 Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M 1998 Nat Struct Biol 5 8 701-706 10050037 Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M 1999 J Biochem (Tokyo) 125 3 495-506 Ordered 10 157 EAAALEQPAELPASVRASIERKRQRALMLRQARLAARPYSATAAAATGGMANVKAAPKIIDTGGGFILEEEEEEEQKIGKVVHQPGPVMEFDYVICEECGKEFMDSYLMNHFDLPTCDNCRDADDKHKLITKTEAKQEYLLKDCDLEK 1XPAA Nuclear magnetic resonance (NMR) 303 6.5 Paper 9699634 Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M 1998 Nat Struct Biol 5 8 701-706 10050037 Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M 1999 J Biochem (Tokyo) 125 3 495-506 Ordered 159 167 EPPLKFIVK 1XPAA Nuclear magnetic resonance (NMR) 303 6.5 Paper 9699634 Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M 1998 Nat Struct Biol 5 8 701-706 10050037 Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M 1999 J Biochem (Tokyo) 125 3 495-506 Ordered 180 205 LYLKLQIVKRSLEVWGSQEALEEAKE 1XPAA Nuclear magnetic resonance (NMR) 303 6.5 Paper 9699634 Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M 1998 Nat Struct Biol 5 8 701-706 10050037 Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M 1999 J Biochem (Tokyo) 125 3 495-506 cAMP-dependent protein kinase type I-alpha regulatory subunit KAP0_BOVIN PKA Regulatory Subunit PRKAR1A P00514 Bt.10903 KAP0_BOVIN 145559486 Bos taurus (Bovine) 379 ASGTTASEEERSLRECELYVQKHNIQALLKDSIVQLCTARPERPMAFLREYFEKLEKEEAKQIQNLQKAGSRADSREDEISPPPPNPVVKGRRRRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFDAMFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNEWATSVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGSAAVLQRRSENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCVKLDRPRFERVLGPCSDILKRNIQQYNSFVSLSV Disordered 91 112 GRRRRGAISAEVYTEEDAASYV Complex Function arises via a disorder to order transition X-ray crystallography Paper 15692043 Kim C, Xuong NH, Taylor SS 2005 Science 307 5710 690-6 6487597 Titani K, Sasagawa T, Ericsson LH, Kumar S, Smith SB, Krebs EG, Walsh KA 1984 Biochemistry 23 18 4193-9 Macrophage scavenger receptor types I and II [Isoform 1] MSRE_BOVIN Macrophage acetylated LDL receptor I and II P21758-1 Bt.4482 MSRE_BOVIN 127356 Bos taurus (Bovine) 453 MAQWDDFPDQQEDTDSCTESVKFDARSVTALLPPHPKNGPTLQERMKSYKTALITLYLIVFVVLVPIIGIVAAQLLKWETKNCTVGSVNADISPSPEGKGNGSEDEMRFREAVMERMSNMESRIQYLSDNEANLLDAKNFQNFSITTDQRFNDVLFQLNSLLSSIQEHENIIGDISKSLVGLNTTVLDLQFSIETLNGRVQENAFKQQEEMRKLEERIYNASAEIKSLDEKQVYLEQEIKGEMKLLNNITNDLRLKDWEHSQTLKNITLLQGPPGPPGEKGDRGPPGQNGIPGFPGLIGTPGLKGDRGISGLPGVRGFPGPMGKTGKPGLNGQKGQKGEKGSGSMQRQSNTVRLVGGSGPHEGRVEIFHEGQWGTVCDDRWELRGGLVVCRSLGYKGVQSVHKRAYFGKGTGPIWLNEVFCFGKESSIEECRIRQWGVRACSHDEDAGVTCTT Disordered cytoplasmic domain 1 50 MAQWDDFPDQQEDTDSCTESVKFDARSVTALLPPHPKNGPTLQERMKSYK Engineered Fragment Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV 7 peptide monomer or trimer (10 or 25 uM) sodium phosphate 0.1 Paper 11785981 Nakamura T, Hinagata J, Tanaka T, Imanishi T, Wada Y, Kodama T, Doi T 2002 Biochem Biophys Res Commun 290 2 858-64 The experimental sequence consisted of the first 50 residues of bovine MSR with a C17A substitution and a GC appended to the C-terminus. The C17A substitution has been shown to have no affect on the cell surface expression and endocytosis of MSR. Probable transcriptional regulatory protein pdtaR PDTAR_MYCTU O06143 PDTAR_MYCTU 81668632 Mycobacterium tuberculosis 205 MTGPTTDADAAVPRRVLIAEDEALIRMDLAEMLREEGYEIVGEAGDGQEAVELAELHKPDLVIMDVKMPRRDGIDAASEIASKRIAPIVVLTAFSQRDLVERARDAGAMAYLVKPFSISDLIPAIELAVSRFREITALEGEVATLSERLETRKLVERAKGLLQTKHGMTEPDAFKWIQRAAMDRRTTMKRVAEVVLETLGTPKDT Disordered 21 21 D Engineered Monomeric X-ray crystallography PEG 1.5K 14-18% Paper 15341725 Morth JP, Feng V, Perry LJ, Svergun DI, Tucker PA 2004 Structure (Camb) 12 9 1595-605 Disordered 68 73 MPRRDG Engineered Monomeric X-ray crystallography PEG 1.5K 14-18% Paper 15341725 Morth JP, Feng V, Perry LJ, Svergun DI, Tucker PA 2004 Structure (Camb) 12 9 1595-605 Disordered 103 107 ARDAG Monomeric Native X-ray crystallography BaCl2 10 PEG 1.5K 15 sodium iodide soak 0.5 Paper 15341725 Morth JP, Feng V, Perry LJ, Svergun DI, Tucker PA 2004 Structure (Camb) 12 9 1595-605 Acylamino-acid-releasing enzyme APEH_AERPE AARE EC 3.4.19.1 Acyl-peptide hydrolase APH Acylaminoacyl-peptidase Q9YBQ2 APEH_AERPE 38257797 Aeropyrum pernix (Strain K1) 582 MRIIMPVEFSRIVRDVERLIAVEKYSLQGVVDGDKLLVVGFSEGSVNAYLYDGGETVKLNREPINSVLDPHYGVGRVILVRDVSKGAEQHALFKVNTSRPGEEQRLEAVKPMRILSGVDTGEAVVFTGATEDRVALYALDGGGLRELARLPGFGFVSDIRGDLIAGLGFFGGGRVSLFTSNLSSGGLRVFDSGEGSFSSASISPGMKVTAGLETAREARLVTVDPRDGSVEDLELPSKDFSSYRPTAITWLGYLPDGRLAVVARREGRSAVFIDGERVEAPQGNHGRVVLWRGKLVTSHTSLSTPPRIVSLPSGEPLLEGGLPEDLRRSIAGSRLVWVESFDGSRVPTYVLESGRAPTPGPTVVLVHGGPFAEDSDSWDTFAASLAAAGFHVVMPNYRGSTGYGEEWRLKIIGDPCGGELEDVSAAARWARESGLASELYIMGYSYGGYMTLCALTMKPGLFKAGVAGASVVDWEEMYELSDAAFRNFIEQLTGGSREIMRSRSPINHVDRIKEPLALIHPQNDSRTPLKPLLRLMGELLARGKTFEAHIIPDAGHAINTMEDAVKILLPAVFFLATQRERR Disordered 1 7 MRIIMPV 1VE6A X-ray crystallography 291 4.6 PEG4000 6 NaAC per l 50 DTT per l 15 EDTA per l 0.2 Paper 15296741 Bartlam M, Wang G, Yang H, Gao R, Zhao X, Xie G, Cao S, Feng Y, Rao Z 2004 Structure 12 8 1481-8 Disordered 582 582 R 1VE6A 1VE7A X-ray crystallography 291 4.6 DTT per l 15 EDTA per l 0.2 NaAC per l 50 PEG4000 6 Paper 15296741 Bartlam M, Wang G, Yang H, Gao R, Zhao X, Xie G, Cao S, Feng Y, Rao Z 2004 Structure 12 8 1481-8 Disordered 1 8 MRIIMPVE Complex 1VE7A X-ray crystallography 291 4.6 DTT per l 15 EDTA per l 0.2 NaAC per l 50 PEG4000 6 Paper 15296741 Bartlam M, Wang G, Yang H, Gao R, Zhao X, Xie G, Cao S, Feng Y, Rao Z 2004 Structure 12 8 1481-8 This region is disordered when in a complex with p-nitrophenyl phosphate (pNP). Troponin C, slow skeletal and cardiac muscles TNNC1_BOVIN TN-C P63315 Bt.49083 TNNC1_BOVIN 54039740 Bos taurus (Bovine) 161 MDDIYKAAVEQLTEEQKNEFKAAFDIFVLGAEDGCISTKELGKVMRMLGQNPTPEELQEMIDEVDEDGSGTVDFDEFLVMMVRCMKDDSKGKSEEELSDLFRMFDKNADGYIDLEELKIMLQATGETITEDDIEELMKDGDKNNDGRIDYDEFLEFMKGVE Disordered 103 158 MFDKNADGYIDLEELKIMLQATGETITEDDIEELMKDGDKNNDGRIDYDEFLEFMK Function arises via a disorder to order transition Metal binding Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV 298 Circular dichroism (CD) spectroscopy, near-UV 298 Paper 2933134 McCubbin WD, Kay CM 1985 Can J Biochem Cell Biol 63 8 812-23 Cholera enterotoxin subunit A CHTA_VIBCH Cholera enterotoxin, A chain Cholera enterotoxin subunit A1 [cleavage product 1] (aa 19-212) Cholera enterotoxin A1 chain Cholera enterotoxin alpha chain NAD(+)--diphthamide ADP-ribosyltransferase Cholera enterotoxin subunit A2 [cleavage product 2] (aa 213-258) Cholera enterotoxin A2 chain Cholera enterotoxin gamma chain P01555 CHTA_VIBCH 116397 Vibrio cholerae 258 MVKIIFVFFIFLSSFSYANDDKLYRADSRPPDEIKQSGGLMPRGQSEYFDRGTQMNINLYDHARGTQTGFVRHDDGYVSTSISLRSAHLVGQTILSGHSTYYIYVIATAPNMFNVNDVLGAYSPHPDEQEVSALGGIPYSQIYGWYRVHFGVLDEQLHRNRGYRDRYYSNLDIAPAADGYGLAGFPPEHRAWREEPWIHHAPPGCGNAPRSSMSNTCDEKTQSLGVKFLDEYQSKVKRQIFSGYQSDIDTHNRIKDEL Ordered Activation loop 44 54 GQSEYFDRGTQ Monomeric Mutant Native 1S5BA 1S5CA 1S5DA 1S5EA 1S5FA Function arises via an order to disorder transition Entropic chain Autoregulatory X-ray crystallography 298 7 CTY30S form 1 MES pH 6 - 7 100 PEG 2000 monomethyl ether 14 - 20% Protein PBS buffer X-ray crystallography 298 7 CTY30S form 2 D-galactose Buffer G 300 PEG 3350 20% Protein Buffer G Sodium citrate 100 X-ray crystallography 298 7 CTY30S form 3 Kemptide 250 MES pH 6 - 7 100 PEG 2000 monomethyl ether 14 - 20% Protein PBS buffer X-ray crystallography 298 7 CT-wt form 1 D-galactose Buffer G 300 Magnesium acetate 150 PEG 3350 18-20% Protein Buffer G X-ray crystallography 298 7 CT-wt form 2 D-galactose Buffer G 300 Lithium citrate 200 PEG 3350 20% Protein Buffer G Paper 15049684 O'Neal CJ, Amaya EI, Jobling MG, Holmes RK, Hol WG 2004 Biochemistry 43 13 3772-82 After modification by limited proteolysis and/or disulfide bond reduction, this activation loop is thought to undergo a order-to-disorder transition that results in the destabilization of the active site loop. Of the three CTY30S crystal forms, 1 and 3 show this region to be fully disordered, whereas residues 48-55 are shown to be disordered in form 2, with high B factors being seen for residues 45 - 47. The loop is ordered in the wt-CT, however, form 2 indicated high B factors for some of the residues along the loop, indicating a propensity towards disorder. Ordered Active site loop 66 75 TQTGFVRHDD Monomeric Mutant Native 1S5BA 1S5CA 1S5DA 1S5EA 1S5FA Function arises via an order to disorder transition Unknown Autoregulatory X-ray crystallography 298 7 CTY30S form 1 MES pH 6 - 7 100 PEG 2000 monomethyl ether 14 - 20% Protein PBS buffer X-ray crystallography 298 7 CTY30S form 2 D-galactose Buffer G 300 PEG 3350 20% Protein Buffer G 100 Sodium citrate X-ray crystallography 298 7 CTY30S form 3 Kemptide 250 MES pH 6 - 7 100 PEG 2000 monomethyl ether 14 - 20% Protein PBS buffer X-ray crystallography 298 7 CT-wt form 1 D-galactose Buffer G 300 Magnesium acetate 150 PEG 3350 18-20% Protein Buffer G X-ray crystallography 298 7 CT-wt form 2 D-galactose Buffer G 300 Lithium citrate 200 PEG 3350 20% Protein Buffer G Paper 15049684 O'Neal CJ, Amaya EI, Jobling MG, Holmes RK, Hol WG 2004 Biochemistry 43 13 3772-82 It is thought that destabilization of the active site loop makes it more flexible, thus allowing substrates to enter the active site, which undergo ADP-ribosylation. The active site loop is ordered in the wild-type structures, in addition to CTY30S forms 1 and 2. With the addition of the kemptide inhibitor to CTY30S form 3, poor electron density was seen for residues 66 - 71, a possible indication of a order-to-disorder transition of the active site loop when substrate binds. Disordered - Extended KDEL binding region 245 255 QSDIDTHNRIK Monomeric Mutant Native 1S5BA 1S5CA 1S5DA 1S5EA 1S5FA Relationship to function unknown Unknown Protein-protein binding X-ray crystallography 298 7 CTY30S form 1 MES pH 6 - 7 100 PEG 2000 monomethyl ether 14 - 20% Protein PBS buffer X-ray crystallography 298 7 CTY30S form 2 D-galactose Buffer G 300 PEG 3350 20% Protein Buffer G Sodium citrate 100 X-ray crystallography 298 7 CTY30S form 3 Kemptide 250 MES pH 6 - 7 100 PEG 2000 monomethyl ether 14 - 20% Protein PBS buffer X-ray crystallography 298 7 CT-wt form 1 D-galactose Buffer G 300 Magnesium acetate 150 PEG 3350 18-20% Protein Buffer G X-ray crystallography 298 7 CT-wt form 2 D-galactose Buffer G 300 Lithium citrate 200 PEG 3350 20% Protein Buffer G Paper 15049684 O'Neal CJ, Amaya EI, Jobling MG, Holmes RK, Hol WG 2004 Biochemistry 43 13 3772-82 All crystal structures showed an elongated conformation for the disordered region of A2. This region extends through the B5 pore of of CT-subunit B in order to interact with the KDEL receptor. Crystallography by O'Neal et al (2004) was performed on the full length protein minus the signal peptide (aa 1-18), therefore the disordered regions are attached to the parent protein rather than cleavage products (subunits A1 and A2). DP regions are numbered according the the whole protein, the O'Neal paper disregards the signal peptide (author's aa 1 = DisProt/UniProt aa 19). Epsin-1 EPN1_RAT EPS-15-interacting protein 1 O88339 Rn.30007 EPN1_RAT 41016934 Rattus norvegicus (Rat) 575 MSTSSLRRQMKNIVHNYSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREERAHALKTKEKLAQTATASSAAVGSGPPPEAEQAWPQSSGEEELQLQLALAMSKEEADQPPSCGPEDDVQLQLALSLSREEHDKEERIRRGDDLRLQMAIEESKRETGGKEESSLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGAPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTSDPWGSADGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGAKASNPFLPSGAPATGPSVTNPFQPAPPATLTLNQLRLSPVPPVPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNPFLL Disordered 144 575 RAHALKTKEKLAQTATASSAAVGSGPPPEAEQAWPQSSGEEELQLQLALAMSKEEADQPPSCGPEDDVQLQLALSLSREEHDKEERIRRGDDLRLQMAIEESKRETGGKEESSLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGAPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTSDPWGSADGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGAKASNPFLPSGAPATGPSVTNPFQPAPPATLTLNQLRLSPVPPVPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNPFLL Fragment Monomeric Function arises from the disordered state Molecular assembly Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV Size exclusion/gel filtration chromatography cytosol 500 Analytical ultracentrifugation 293 Paper 11756460 Kalthoff C, Alves J, Urbanke C, Knorr R, Ungewickell EJ 2002 J Biol Chem 277 10 8209-16 Tryptophan synthase alpha chain TRPA_ECOLI EC 4.2.1.20 P0A877 TRPA_ECOLI 67473577 Escherichia coli 268 MERYESLFAQLKERKEGAFVPFVTLGDPGIEQSLKIIDTLIEAGADALELGIPFSDPLADGPTIQNATLRAFAAGVTPAQCFEMLALIRQKHPTIPIGLLMYANLVFNKGIDEFYAQCEKVGVDSVLVADVPVEESAPFRQAALRHNVAPIFICPPNADDDLLRQIASYGRGYTYLLSRAGVTGAENRAALPLNHLVAKLKEYNAAPPLQGFGISAPDQVKAAIDAGAAGAISGSAIVKIIEQHINEPEKMLAALKVFVQPMKAATRS Disordered 57 64 PLADGPTI Function arises via an order to disorder transition Molecular assembly Protein-protein binding X-ray crystallography 288 protein solution (20 mg/mL) 1 potassium phosphate buffer (pH 7.0) 5 ammonium sulfate 1.8 sodium cacodylate pH 6.5 0.1 Paper 15667212 Nishio K, Morimoto Y, Ishizuka M, Ogasahara K, Tsukihara T, Yutani K 2005 Biochemistry 44 4 1184-92 These densities were unclear in molecule A only. The region stayed disordered when in a complex with molecule B. Disordered 184 185 GA Relationship to function unknown Unknown Unknown X-ray crystallography 288 ammonium sulfate 1.8 potassium phosphate buffer (pH 7.0) 5 protein solution (20 mg/mL) 1 sodium cacodylate pH 6.5 0.1 Paper 15667212 Nishio K, Morimoto Y, Ishizuka M, Ogasahara K, Tsukihara T, Yutani K 2005 Biochemistry 44 4 1184-92 These densities were unclear in molecules A and B. Disordered 59 63 ADGPT Function arises via an order to disorder transition Molecular assembly Protein-protein binding X-ray crystallography 288 ammonium sulfate 1.8 potassium phosphate buffer (pH 7.0) 5 protein solution (20 mg/mL) 1 sodium cacodylate pH 6.5 0.1 Paper 15667212 Nishio K, Morimoto Y, Ishizuka M, Ogasahara K, Tsukihara T, Yutani K 2005 Biochemistry 44 4 1184-92 These densities are unclear in molecule B only. The region stayed disordered when in complex with molecule A. Myristoylated alanine-rich C-kinase substrate MARCS_MOUSE MARCKS P26645 Mm.477725 MARCS_MOUSE 126752 Mus musculus (Mouse) 309 MGAQFSKTAAKGEATAERPGEAAVASSPSKANGQENGHVKVNGDASPAAAEPGAKEELQANGSAPAADKEEPASGSAATPAAAEKDEAAAATEPGAGAADKEAAEAEPAEPSSPAAEAEGASASSTSSPKAEDGAAPSPSSETPKKKKKRFSFKKSFKLSGFSFKKSKKESGEGAEAEGATAEGAKDEAAAAAGGEGAAAPGEQAGGAGAEGAAGGEPREAEAAEPEQPEQPEQPAAEEPQAEEQSEAAGEKAEEPAPGATAGDASSAAGPEQEAPAATDEAAASAAPAASPEPQPECSPEAPPAPTAE Disordered 1 309 MGAQFSKTAAKGEATAERPGEAAVASSPSKANGQENGHVKVNGDASPAAAEPGAKEELQANGSAPAADKEEPASGSAATPAAAEKDEAAAATEPGAGAADKEAAEAEPAEPSSPAAEAEGASASSTSSPKAEDGAAPSPSSETPKKKKKRFSFKKSFKLSGFSFKKSKKESGEGAEAEGATAEGAKDEAAAAAGGEGAAAPGEQAGGAGAEGAAGGEPREAEAAEPEQPEQPEQPAAEEPQAEEQSEAAGEKAEEPAPGATAGDASSAAGPEQEAPAATDEAAASAAPAASPEPQPECSPEAPPAPTAE Function arises from the disordered state Phosphorylation Substrate/ligand binding Circular dichroism (CD) spectroscopy, far-UV 298 protein 1 Tris-HCl buffer (pH 7.5) 20 NaCl 0.1 CaCl2 0.5 Paper 9468306 Matsubara M, Yamauchi E, Hayashi N, Taniguchi H 1998 FEBS Lett 421 3 203-7 15640140 Tapp H, Al-Naggar IM, Yarmola EG, Harrison A, Shaw G, Edison AS, Bubb MR 2005 J Biol Chem 280 11 9946-56 Disordered 1 309 MGAQFSKTAAKGEATAERPGEAAVASSPSKANGQENGHVKVNGDASPAAAEPGAKEELQANGSAPAADKEEPASGSAATPAAAEKDEAAAATEPGAGAADKEAAEAEPAEPSSPAAEAEGASASSTSSPKAEDGAAPSPSSETPKKKKKRFSFKKSFKLSGFSFKKSKKESGEGAEAEGATAEGAKDEAAAAAGGEGAAAPGEQAGGAGAEGAAGGEPREAEAAEPEQPEQPEQPAAEEPQAEEQSEAAGEKAEEPAPGATAGDASSAAGPEQEAPAATDEAAASAAPAASPEPQPECSPEAPPAPTAE Complex Function arises from the disordered state Phosphorylation Substrate/ligand binding Circular dichroism (CD) spectroscopy, far-UV 298 CaCl2 0.5 calmodulin 1 NaCl 0.1 protein 1 Tris-HCl buffer (pH 7.5) 20 Paper 9468306 Matsubara M, Yamauchi E, Hayashi N, Taniguchi H 1998 FEBS Lett 421 3 203-7 15640140 Tapp H, Al-Naggar IM, Yarmola EG, Harrison A, Shaw G, Edison AS, Bubb MR 2005 J Biol Chem 280 11 9946-56 This protein was found to be disordered while in a complex with calmodulin. Protein tyrosine phosphatase type IVA 3 [Isoform 1] TP4A3_HUMAN EC=3.1.3.48 Protein-tyrosine phosphatase 4a3 Protein-tyrosine phosphatase of regenerating liver 3 PRL-3 PRL-R O75365-1 Hs.43666 TP4A3_HUMAN 68566154 Homo sapiens (Human) 173 MARMNRPAPVEVSYKHMRFLITHNPTNATLSTFIEDLKKYGATTVVRVCEVTYDKTPLEKDGITVVDWPFDDGAPPPGKVVEDWLSLVKAKFCEAPGSCVAVHCVAGLGRAPVLVALALIESGMKYEDAIQFIRQKRRGAINSKQLTYLEKYRPKQRLRFKDPHTHKTRCCVM Disordered 1 7 MARMNRP Nuclear magnetic resonance (NMR) 308 6.8 protein 3 phosphate buffer 50 NaCl 100 DTT 10 to 12 mM sodium azide 0.1 Paper 14704153 Kozlov G, Cheng J, Ziomek E, Banville D, Gehring K, Ekiel I 2004 J Biol Chem 279 12 11882-9 Disordered 157 173 RLRFKDPHTHKTRCCVM Nuclear magnetic resonance (NMR) 308 6.8 protein 3 phosphate buffer 50 NaCl 100 DTT 10 to 12 mM sodium azide 0.1 Paper 14704153 Kozlov G, Cheng J, Ziomek E, Banville D, Gehring K, Ekiel I 2004 J Biol Chem 279 12 11882-9 Disordered acid loop 69 78 PFDDGAPPPG Nuclear magnetic resonance (NMR) 308 6.8 DTT 10 to 12 mM NaCl 100 phosphate buffer 50 protein 3 sodium azide 0.1 Paper 14704153 Kozlov G, Cheng J, Ziomek E, Banville D, Gehring K, Ekiel I 2004 J Biol Chem 279 12 11882-9 Protein tyrosine phosphatase type IVA 1 [Isoform 1] TP4A1_HUMAN EC=3.1.3.48 Protein-tyrosine phosphatase 4a1 Protein-tyrosine phosphatase of regenerating liver 1 PRL-1 PTP(CAAXI) Q93096 Hs.227777 TP4A1_HUMAN 68566217 Homo sapiens (Human) 173 MARMNRPAPVEVTYKNMRFLITHNPTNATLNKFIEELKKYGVTTIVRVCEATYDTTLVEKEGIHVLDWPFDDGAPPSNQIVDDWLSLVKIKFREEPGCCIAVHCVAGLGRAPVLVALALIEGGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRFKDSNGHRNNCCIQ Disordered 1 6 MARMNR Nuclear magnetic resonance (NMR) 310 D2O 5 Paper 15213447 Laurence JS, Hallenga K, Stauffacher CV 2004 J Biomol NMR 29 3 417-8 Disordered P-loop 25 29 PTNAT Nuclear magnetic resonance (NMR) 310 D2O 5 Paper 15213447 Laurence JS, Hallenga K, Stauffacher CV 2004 J Biomol NMR 29 3 417-8 Disordered 136 173 KRRGAFNSKQLLYLEKYRPKMRLRFKDSNGHRNNCCIQ Nuclear magnetic resonance (NMR) 310 D2O 5 Paper 15213447 Laurence JS, Hallenga K, Stauffacher CV 2004 J Biomol NMR 29 3 417-8 Additional UniGene: Hs.706850 Securin SECU_YEAST P40316 SECU_YEAST 730288 Saccharomyces cerevisiae (Baker's yeast) 373 MMPANEDKENNIVYTGNESSGINFPQTPAHLLKRSHSNILKPPVRLDQLKRDANSNNGNTLKYIQGGKEVSPTKRLHTHAQQQGRLPLAAKDNNRSKSFIFPETSNQSKDADLPQLQNTLSIRKNDQLRKLSQISRSRSRANHNDLLSNSRKLQKYGSVLGYNALPKMKSLVLKDLADSGKNEESSDDDEGNEDSESKLGKKLQSALLKQDSSDGENELNGGLGLFNEQGGLQQLIKNSTKNEQKTKNDKSDKTDDYDIEIAPQRQEPLPYVPEGYSPFQQDDIEKLKTFNSPYKLDLEDEDDTPDKVDLLPLEQIDEEGEKDETECITRNQEEGAALPLLSKNFKEVAAVPTMELVYSEEGLDPEELEDLVT Disordered 1 110 MMPANEDKENNIVYTGNESSGINFPQTPAHLLKRSHSNILKPPVRLDQLKRDANSNNGNTLKYIQGGKEVSPTKRLHTHAQQQGRLPLAAKDNNRSKSFIFPETSNQSKD Engineered Fragment Circular dichroism (CD) spectroscopy, near-UV 7 ND-Pds1 per ml 0.05 sodium phosphate 10 Nuclear magnetic resonance (NMR) 298 7.2 D2O v/v 5 NaCl 140 NaN3 50 NaPi 12 ND-Pds1 1 Paper 12220679 Cox CJ, Dutta K, Petri ET, Hwang WC, Lin Y, Pascal SM, Basavappa R 2002 FEBS Lett 527 1-3 303-8 The destruction of securin facilitates sister chromatid segregation by releasing the binding partner of securin, separase, which then cleaves the protein complexes that bind together the sister chromatids. Superoxide dismutase-like protein yojM YOJM_BACSU O31851 YOJM_BACSU 12230851 Bacillus subtilis 196 MHRLLLLMMLTALGVAGCGQKKPPDPPNRVPEKKVVETSAFGHHVQLVNREGKAVGFIEIKESDDEGLDIHISANSLRPGASLGFHIYEKGSCVRPDFESAGGPFNPLNKEHGFNNPMGHHAGDLPNLEVGADGKVDVIMNAPDTSLKKGSKLNILDEDGSAFIIHEQADDYLTNPSGNSGARIVCGALLGNNEKQ Disordered 191 196 GNNEKQ Fragment Monomeric Function arises via a disorder to order transition Metal binding Nuclear magnetic resonance (NMR) 298 X-ray crystallography 100 Paper 15897454 Banci L, Bertini I, Calderone V, Cramaro F, Del Conte R, Fantoni A, Mangani S, Quattrone A, Viezzoli MS 2005 Proc Natl Acad Sci U S A 102 21 7541-6 Disordered Electrostatic loop VII 172 177 YLTNPS Fragment Monomeric Function arises via a disorder to order transition Metal binding Nuclear magnetic resonance (NMR) 298 X-ray crystallography 100 Paper 15897454 Banci L, Bertini I, Calderone V, Cramaro F, Del Conte R, Fantoni A, Mangani S, Quattrone A, Viezzoli MS 2005 Proc Natl Acad Sci U S A 102 21 7541-6 Disordered Long loop IV 89 125 EKGSCVRPDFESAGGPFNPLNKEHGFNNPMGHHAGDL Fragment Monomeric Function arises via a disorder to order transition Metal binding Nuclear magnetic resonance (NMR) 298 X-ray crystallography 100 Paper 15897454 Banci L, Bertini I, Calderone V, Cramaro F, Del Conte R, Fantoni A, Mangani S, Quattrone A, Viezzoli MS 2005 Proc Natl Acad Sci U S A 102 21 7541-6 Disordered 35 39 VVETS Fragment Monomeric Function arises via a disorder to order transition Metal binding Nuclear magnetic resonance (NMR) 298 X-ray crystallography 100 Paper 15897454 Banci L, Bertini I, Calderone V, Cramaro F, Del Conte R, Fantoni A, Mangani S, Quattrone A, Viezzoli MS 2005 Proc Natl Acad Sci U S A 102 21 7541-6 Lysozyme C LYSC_MELGA EC 3.2.1.17 1,4-beta-N-acetylmuramidase C P00703 LYSC_MELGA 126619 Meleagris gallopavo (Common turkey) 147 MRSLLILVLCFLPLAALGKVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKFESNFNTHATNRNTDGSTDYGILQINSRWWCNDGRTPGSKNLCNIPCSALLSSDITASVNCAKKIASGGNGMNAWVAWRNRCKGTDVHAWIRGCRL Disordered 78 80 SRW Fragment Relationship to function unknown Molecular assembly Protein-protein binding X-ray crystallography 295 6 NaCl 0.5 M 200 protein per ml 100 Paper 15805597 Margiolaki I, Wright JP, Fitch AN, Fox GC, Von Dreele RB 2005 Acta Crystallogr D Biol Crystallogr 61 Pt 4 423-32 Disordered 88 92 PGSKN Fragment Relationship to function unknown Molecular assembly Protein-protein binding X-ray crystallography 295 6 NaCl 0.5 M 200 protein per ml 100 Paper 15805597 Margiolaki I, Wright JP, Fitch AN, Fox GC, Von Dreele RB 2005 Acta Crystallogr D Biol Crystallogr 61 Pt 4 423-32 Disordered 119 125 GGNGMNA Fragment Relationship to function unknown Molecular assembly Protein-protein binding X-ray crystallography 295 6 NaCl 0.5 M 200 protein per ml 100 Paper 15805597 Margiolaki I, Wright JP, Fitch AN, Fox GC, Von Dreele RB 2005 Acta Crystallogr D Biol Crystallogr 61 Pt 4 423-32 Disordered beta-hairpin 64 66 NTD Fragment Relationship to function unknown Unknown Unknown X-ray crystallography 8 protein 6 mg per ml 50 NaCl 9% w/v 50 ammonium acetate buffer 100 Paper 1515108 Howell PL, Almo SC, Parsons MR, Hajdu J, Petsko GA 1992 Acta Crystallogr B 48 ( Pt 2) 200-7 15805597 Margiolaki I, Wright JP, Fitch AN, Fox GC, Von Dreele RB 2005 Acta Crystallogr D Biol Crystallogr 61 Pt 4 423-32 Disordered 147 147 L Fragment 1TEWA Relationship to function unknown Unknown Unknown X-ray crystallography 295 6 NaCl 0.5 M 200 protein per ml 100 Paper 15805597 Margiolaki I, Wright JP, Fitch AN, Fox GC, Von Dreele RB 2005 Acta Crystallogr D Biol Crystallogr 61 Pt 4 423-32 The sequence for this protein was obtained from LaRue et al. SwissProt has a Asn instead of a Asp at postion 103 of the fragment. Myc proto-oncogene protein [Isoform 1] MYC_HUMAN c-Myc Transcription factor p64 P01106-1 Hs.202453 MYC_HUMAN 127619 Homo sapiens (Human) 439 MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENVKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEEDLLRKRREQLKHKLEQLRNSCA Disordered 1 88 MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDG Fragment Transactivation (transcriptional activation) Circular dichroism (CD) spectroscopy, far-UV 278 Circular dichroism (CD) spectroscopy, far-UV 298 Circular dichroism (CD) spectroscopy, far-UV 343 Fluorescence resonance energy transfer (FRET) 298 8 ANS 20 GuHCl 6 NaCl 100 NaH2PO4 20 Fluorescence resonance energy transfer (FRET) 298 8 ANS 20 NaCl 100 NaH2PO4 20 Sensitivity to proteolysis 298 2-mercaptoethanol 0.02 bromophenol blue w/v 0.002 glycerol v/v 35 SDS w/v 3 Tris-HCl pH 6.8 80 Paper 15663936 Fladvad M, Zhou K, Moshref A, Pursglove S, Safsten P, Sunnerhagen M 2005 J Mol Biol 346 1 175-89 Disordered - Molten Globule 1 167 MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARG Fragment Function arises from the molten globule state Transactivation (transcriptional activation) Protein-protein binding Stability at thermal extremes Circular dichroism (CD) spectroscopy, far-UV 278 Circular dichroism (CD) spectroscopy, far-UV 298 Circular dichroism (CD) spectroscopy, far-UV 343 Fluorescence resonance energy transfer (FRET) 298 8 ANS 20 GuHCl 6 NaCl 100 NaH2PO4 20 Fluorescence resonance energy transfer (FRET) 298 8 ANS 20 NaCl 100 NaH2PO4 20 Sensitivity to proteolysis 298 2-mercaptoethanol 0.02 bromophenol blue w/v 0.002 glycerol v/v 35 SDS w/v 3 Tris-HCl pH 6.8 80 Paper 15663936 Fladvad M, Zhou K, Moshref A, Pursglove S, Safsten P, Sunnerhagen M 2005 J Mol Biol 346 1 175-89 Disordered transactivation domain (TAD) 1 143 MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAK Engineered Fragment Function arises via a disorder to order transition Modification site Molecular assembly Transactivation (transcriptional activation) Protein-protein binding Circular dichroism (CD) spectroscopy, far-UV phosphate buffer 3 Circular dichroism (CD) spectroscopy, far-UV phosphate buffer 10 Paper 8755740 McEwan IJ, Dahlman-Wright K, Ford J, Wright AP 1996 Biochemistry 35 29 9584-93 15663936 Fladvad M, Zhou K, Moshref A, Pursglove S, Safsten P, Sunnerhagen M 2005 J Mol Biol 346 1 175-89 Sialidase-2 NEUR2_HUMAN EC 3.2.1.18 Cytosolic sialidase N-acetyl-alpha-neuraminidase 2 Q9Y3R4 Hs.532681 NEUR2_HUMAN 229462907 Homo sapiens (Human) 380 MASLPVLQKESVFQSGAHAYRIPALLYLPGQQSLLAFAEQRASKKDEHAELIVLRRGDYDAPTHQVQWQAQEVVAQARLDGHRSMNPCPLYDAQTGTLFLFFIAIPGQVTEQQQLQTRANVTRLCQVTSTDHGRTWSSPRDLTDAAIGPAYREWSTFAVGPGHCLQLNDRARSLVVPAYAYRKLHPIQRPIPSAFCFLSHDHGRTWARGHFVAQDTLECQVAEVETGEQRVVTLNARSHLRARVQAQSTNDGLDFQESQLVKKLVEPPPQGCQGSVISFPSPRSGPGSPAQWLLYTHPTHSWQRADLGAYLNPRPPAPEAWSEPVLLAKGSCAYSDLQSMGTGPDGSPLFGCLYEANDYEEIVFLMFTLKQAFPAEYLPQ Disordered alpha-1 helix 42 48 ASKKDEH Function arises via a disorder to order transition X-ray crystallography 298 6.2 protein per ml 10 sodium/potassium phosphate buffer 100 NaCl 2.5 Paper 15501818 Chavas LM, Tringali C, Fusi P, Venerando B, Tettamanti G, Kato R, Monti E, Wakatsuki S 2005 J Biol Chem 280 1 469-75 Disordered alpha-2 helix 107 118 GQVTEQQQLQTR Function arises via a disorder to order transition Substrate/ligand binding X-ray crystallography 298 6.2 NaCl 2.5 protein per ml 10 sodium/potassium phosphate buffer 100 Paper 15501818 Chavas LM, Tringali C, Fusi P, Venerando B, Tettamanti G, Kato R, Monti E, Wakatsuki S 2005 J Biol Chem 280 1 469-75 Hypoxia-inducible factor 1 alpha [Isoform 1] HIF1A_HUMAN HIF-1 alpha HIF1 alpha ARNT-interacting protein Member of PAS protein 1 Basic-helix-loop-helix-PAS protein MOP1 Q16665-1 Hs.597216 HIF1A_HUMAN 2498017 Homo sapiens (Human) 826 MEGAGGANDKKKISSERRKEKSRDAARSRRSKESEVFYELAHQLPLPHNVSSHLDKASVMRLTISYLRVRKLLDAGDLDIEDDMKAQMNCFYLKALDGFVMVLTDDGDMIYISDNVNKYMGLTQFELTGHSVFDFTHPCDHEEMREMLTHRNGLVKKGKEQNTQRSFFLRMKCTLTSRGRTMNIKSATWKVLHCTGHIHVYDTNSNQPQCGYKKPPMTCLVLICEPIPHPSNIEIPLDSKTFLSRHSLDMKFSYCDERITELMGYEPEELLGRSIYEYYHALDSDHLTKTHHDMFTKGQVTTGQYRMLAKRGGYVWVETQATVIYNTKNSQPQCIVCVNYVVSGIIQHDLIFSLQQTECVLKPVESSDMKMTQLFTKVESEDTSSLFDKLKKEPDALTLLAPAAGDTIISLDFGSNDTETDDQQLEEVPLYNDVMLPSPNEKLQNINLAMSPLPTAETPKPLRSSADPALNQEVALKLEPNPESLELSFTMPQIQDQTPSPSDGSTRQSSPEPNSPSEYCFYVDSDMVNEFKLELVEKLFAEDTEAKNPFSTQDTDLDLEMLAPYIPMDDDFQLRSFDQLSPLESSSASPESASPQSTVTVFQQTQIQEPTANATTTTATTDELKTVTKDRMEDIKILIASPSPTHIHKETTSATSSPYRDTQSRTASPNRAGKGVIEQTEKSHPRSPNVLSVALSQRTTVPEEELNPKILALQNAQRKRKMEHDGSLFQAVGIGTLLQQPDDHAATTSLSWKRVKGCKSSEQNGMEQKTIILIPSDLACRLLGQSMDESGLPQLTSYDCEVNAPIQGSRNLLQGEELLRALDQVN Disordered - Extended N-TAD and inhibitory domain 530 698 EFKLELVEKLFAEDTEAKNPFSTQDTDLDLEMLAPYIPMDDDFQLRSFDQLSPLESSSASPESASPQSTVTVFQQTQIQEPTANATTTTATTDELKTVTKDRMEDIKILIASPSPTHIHKETTSATSSPYRDTQSRTASPNRAGKGVIEQTEKSHPRSPNVLSVALSQR Fragment Circular dichroism (CD) spectroscopy, far-UV DTE buffer 1 KCl buffer 150 NaPi buffer (pH 7.2) 25 protein 30 Analytical ultracentrifugation 283 DTT buffer 1 KCl buffer 150 NaPi buffer (pH 7.2) 25 Fluorescence polarization/anisotropy 283 DTT buffer 1 HEPES pH 7.2 50 Fluorescence polarization/anisotropy 283 DTT 1 NaCl buffer (0, 90, and 150 mM) NaPi pH 7.2 25 Paper 15629713 Sanchez-Puig N, Veprintsev DB, Fersht AR 2005 Mol Cell 17 1 11-21 Disordered - Extended ODD domain 403 603 AAGDTIISLDFGSNDTETDDQQLEEVPLYNDVMLPSPNEKLQNINLAMSPLPTAETPKPLRSSADPALNQEVALKLEPNPESLELSFTMPQIQDQTPSPSDGSTRQSSPEPNSPSEYCFYVDSDMVNEFKLELVEKLFAEDTEAKNPFSTQDTDLDLEMLAPYIPMDDDFQLRSFDQLSPLESSSASPESASPQSTVTVFQ Fragment Circular dichroism (CD) spectroscopy, far-UV DTE buffer 1 KCl buffer 150 NaPi buffer (pH 7.2) 25 protein 10 Analytical ultracentrifugation 283 DTT buffer 1 KCl buffer 150 NaPi buffer (7.2) 25 Fluorescence polarization/anisotropy 283 DTT buffer 1 HEPES pH 7.2 50 Fluorescence polarization/anisotropy 283 DTT 1 NaCl buffer (0, 90, 150 mM) NaPi pH 7.2 25 Paper 15629713 Sanchez-Puig N, Veprintsev DB, Fersht AR 2005 Mol Cell 17 1 11-21 Disordered C-terminal activation domain 776 826 SDLACRLLGQSMDESGLPQLTSYDCEVNAPIQGSRNLLQGEELLRALDQVN Native Function arises via a disorder to order transition Transactivation (transcriptional activation) Nuclear magnetic resonance (NMR) 298 Paper 11959977 Dames SA, Martinez-Yamout M, De Guzman RN, Dyson HJ, Wright PE 2002 Proc Natl Acad Sci U S A 99 8 5271-6 Fatty acid-binding protein, intestinal FABPI_RAT Intestinal-type fatty acid-binding protein I-FABP Fatty acid-binding protein 2 P02693 Rn.91358 FABPI_RAT 1345948 Rattus norvegicus (Rat) 131 AFDGTWKVDRNENYEKFMEKMGINVVKRKLGAHDNLKLTITQEGNKFTVKESSNFRNIDVVFELGVDFAYSLADGTELTGTWTMEGNKLVGKFKRVDNGKELIAVREISGNELIQTYTYEGVEAKRIFKKE Disordered 29 36 KLGAHDNL Nuclear magnetic resonance (NMR) 306 7.2 X-ray crystallography Paper 9063893 Hodsdon ME, Cistola DP 1997 Biochemistry 36 6 1450-60 Disordered 54 57 NFRN Optical rotatory dispersion 306 7.2 X-ray crystallography Paper 9063893 Hodsdon ME, Cistola DP 1997 Biochemistry 36 6 1450-60 Major prion protein PRIO_MOUSE PrP PrP27-30 PrP33-35C P04925 Mm.648 PRIO_MOUSE 130914 Mus musculus (Mouse) 254 MANLGYWLLALFVTMWTDVGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYDGRRSSSTVLFSSPPVILLISFLIFLIVG Disordered 23 120 KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAV Fragment Nuclear magnetic resonance (NMR) 293 4.5 protein 0.8 H2O 90 D2O 10 EDTA 0.01 PMSF 0.01 Pepstatin 0.1 COMPLETE protease inhibitor cocktail Paper 9280298 Riek R, Hornemann S, Wider G, Glockshuber R, Wuthrich K 1997 FEBS Lett 413 2 282-8 Potassium voltage-gated channel protein Shaker [Isoform E] KCNAS_DROME Protein minisleep P08510-1 Dm.7088 KCNAS_DROME 92090610 Drosophila melanogaster (Fruit fly) 655 MAAVAGLYGLGEDRQHRKKQQQQQQHQKEQLEQKEEQKKIAERKLQLREQQLQRNSLDGYGSLPKLSSQDEEGGAGHGFGGGPQHFEPIPHDHDFCERVVINVSGLRFETQLRTLNQFPDTLLGDPARRLRYFDPLRNEYFFDRSRPSFDAILYYYQSGGRLRRPVNVPLDVFSEEIKFYELGDQAINKFREDEGFIKEEERPLPDNEKQRKVWLLFEYPESSQAARVVAIISVFVILLSIVIFCLETLPEFKHYKVFNTTTNGTKIEEDEVPDITDPFFLIETLCIIWFTFELTVRFLACPNKLNFCRDVMNVIDIIAIIPYFITLATVVAEEEDTLNLPKAPVSPQDKSSNQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGRTLKASMRELGLLIFFLFIGVVLFSSAVYFAEAGSENSFFKSIPDAFWWAVVTMTTVGYGDMTPVGVWGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETDQEEMQSQNFNHVTSCPYLPGTLGQHMKKSSLSESSSDMMDLDDGVESTPGLTETHPGRSAVAPFLGAQQQQQQPVASSLSMSIDKQLQHPLQQLTQTQLYQQQQQQQQQQQNGFKQQQQQTQQQLQQQQSHTINASAAAATSGSGSSGLTMRHNNALAVSIETDV Disordered 20 83 QQQQQQHQKEQLEQKEEQKKIAERKLQLREQQLQRNSLDGYGSLPKLSSQDEEGGAGHGFGGGP Mutant Native Function arises from the disordered state Entropic chain Flexible linkers/spacers Entropic clock Paper 2122519 Hoshi T, Zagotta WN, Aldrich RW 1990 Science 250 4980 533-8 Coat protein VG05_BPP22 Protein gp5 P26747 VG05_BPP22 137894 Enterobacteria phage P22 (Bacteriophage P22) 430 MALNEGQIVTLAVDEIIETISAITPMAQKAKKYTPPAASMQRSSNTIWMPVEQESPTQEGWDLTDKATGLLELNVAVNMGEPDNDFFQLRADDLRDETAYRRRIQSAARKLANNVELKVANMAAEMGSLVITSPDAIGTNTADAWNFVADAEEIMFSRELNRDMGTSYFFNPQDYKKAGYDLTKRDIFGRIPEEAYRDGTIQRQVAGFDDVLRSPKLPVLTKSTATGITVSGAQSFKPVAWQLDNDGNKVNVDNRFATVTLSATTGMKRGDKISFAGVKFLGQMAKNVLAQDATFSVVRVVDGTHVEITPKPVALDDVSLSPEQRAYANVNTSLADAMAVNILNVKDARTNVFWADDAIRIVSQPIPANHELFAGMKTTSFSIPDVGLNGIFATQGDISTLSGLCRIALWYGVNATRPEAIGVGLPGQTA Disordered N-terminal domain 2 191 ALNEGQIVTLAVDEIIETISAITPMAQKAKKYTPPAASMQRSSNTIWMPVEQESPTQEGWDLTDKATGLLELNVAVNMGEPDNDFFQLRADDLRDETAYRRRIQSAARKLANNVELKVANMAAEMGSLVITSPDAIGTNTADAWNFVADAEEIMFSRELNRDMGTSYFFNPQDYKKAGYDLTKRDIFGRI Engineered Fragment Function arises via a disorder to molten globule transition Molecular assembly Protein-protein binding Circular dichroism (CD) spectroscopy, near-UV 293 PO4 25 NaCl pH 7.6 25 Hydrogen-deuterium exchange 294 7.6 2H2O 90 Paper 15784254 Kang S, Prevelige PE Jr 2005 J Mol Biol 347 5 935-48 The N-terminal domain adopts additional structure in the context of the C-terminal domain but retains some flexibility. DE-cadherin CADE_DROME Protein shotgun Q24298 Dm.4731 CADE_DROME 13124007 Drosophila melanogaster (Fruit fly) 1507 MSTSVQRMSRSYHCINMSATPQAGHLNPAQQQTHQQHKRKCRDLGRRLIPARLLLGVIVAISLLSPALALHSPPDKNFSGDNRKPAFKNCAGYAPKVKEEQPENTYVLTVEAVDPDPDQVIRYSIVQSPFERPKFFINPSTGVIFTTHTFDRDEPIHEKFVFVTVQATDNGLPPLDDVCTFNVTIEDINDNAPAFNKARYDESMSENAQPDAVVMTISASDFDDGNNSLVEYEILRERDFQYFKIDKESGIIYLKRPIDKRPGQSYAIIVRAYNVVPDPPQDAQIEVRIRVVESSIKPPSFVNPIDTPIYLKENLKNFTHPIATLRAVSNMPDKPEVIFELNTGRTEQTNSKNTFVFNQIGNEVTISLGKTLDYEAITDYTLTMIVRNTHELGTEHQIKIQVEDVNDNIPYYTEVKSGTILENEPPGTPVMQVRAFDMDGTSANNIVSFELADNREYFTIDPNTGNITALTTFDREERDFYNVKVIASDNSPSSLFDNGEPNRGHQVFRISIGDKNDHKPHFQQDKYLAERLLEDANTNTEVIEVKAEDEDNASQILYSIESGNVGDAFKIGLKTGKITVNQKLDYETITEYELKVRAFDGIYDDYTTVVIKIEDVNDNPPVFKQDYSVTILEETTYDDCILTVEAYDPDIKDRNADQHIVYSIHQNDGNRWTIDNSGCLRLVKTLDRDPPNGHKNWQVLIKANDEDGVGTTVSTVKEVTVTLKDINDNAPFLINEMPVYWQENRNPGHVVQLQANDYDDTPGAGNFTFGIDSEATPDIKTKFSMDGDYLHANVQFDREAQKEYFIPIRISDSGVPRQSAVSILHLVIGDVNDNAMSEGSSRIFIYNYKGEAPETDIGRVFVDDLDDWDLEDKYFEWKDLPHDQFRLNPSTGMITMLVHTAEGEYDLSFVVTEDSMFVPRHSVDAYVTVVVRELPEEAVDKSGSIRFINVTKEEFISVPRDFQSPDALSLKDRLQLSLAKLFNTSVSNVDVFTVLQNENHTLDVRFSAHGSPYYAPEKLNGIVAQNQQRLENELDLQMLMVNIDECLIEKFKCEESCTNELHKSSVPYMIYSNTTSFVGVNAFVQAQCVCEAPLMRRCLNGGSPRYGENDVCDCIDGFTGPHCELVSVAFYGSGYAFYEPIAACNNTKISLEITPQIDQGLIMYLGPLNFNPLLAISDFLALELDNGYPVLTVDYGSGAIRIRHQHIKMVADRTYQLDIILQRTSIEMTVDNCRLSTCQTLGAPIGPNEFLNVNAPLQLGGTPVDLEQLGRQLNWTHVPNQKGFFGCIRNLTINEQTYNLGMPSVFRNIDSGCQQSVAVAFSFGIDRNFIIAIIVCLALLLIILLAVVVQKKQKNGWHEKDIDDIRETIINYEDEGGGERDTDYDLNVLRTQPFYEEKLYKDPHALQGNMRDPNDIPDIADFLGDKKENCDRDVGATTVDDVRHYAYEGDGNSDGSLSSLASCTDDGDLNFDYLSNFGPRFRKLADMYGEEPSDTDSNVDDDQGWRI Disordered cytoplasmic domain 1350 1507 QKKQKNGWHEKDIDDIRETIINYEDEGGGERDTDYDLNVLRTQPFYEEKLYKDPHALQGNMRDPNDIPDIADFLGDKKENCDRDVGATTVDDVRHYAYEGDGNSDGSLSSLASCTDDGDLNFDYLSNFGPRFRKLADMYGEEPSDTDSNVDDDQGWRI Fragment Fluorescence polarization/anisotropy beta76 2 beta-catenin 3.5 bovin serum albumin 3 protein 6,3, or 1.5 mM tryptophan 12 or 14 mM Circular dichroism (CD) spectroscopy, near-UV 273 7 phosphate 10 Paper 11121423 Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI 2001 J Biol Chem 276 15 12301-12309 7958432 Oda H, Uemura T, Harada Y, Iwai Y, Takeichi M 1994 Dev Biol 165 2 716-26 It appears that the sequence has been updated since the release of the Oda paper in 1994. The sequence originally had a phenylalanine for residue 974, but this has since been changed to a leucine with further analysis of the genome. The Oda paper is still used as the sequence reference for the UniProt entry listed. Fab DNA-1 Antigen binding fragment DNA-1 anti-ssDNA Fab DNA-1 Mm.342177 3399661 Mus musculus (Mouse) 220 LESGPELVKPGASVKMSCKASGYTFTSYVMHWVKQKPGQGLEWIGYINPYNDGTKYNEKFKGKATLTSDKSSSTAYMELSSLTSEDSAVYYCVRGGYRPYYAMDYWGQGTSVTVSSAKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSTWPSETVTCNVAHPASSTKVDKKIVPRDCTS Disordered apical residues of HCDR3 97 100 YRPY Function arises via a disorder to order transition Protein-DNA binding Substrate/ligand binding X-ray crystallography 298 isopranol 20 PEG4000 w/v 14 sodium citrate pH 5.5 0.1 Paper 15784256 Schuermann JP, Prewitt SP, Davies C, Deutscher SL, Tanner JJ 2005 J Mol Biol 347 5 965-78 Disordered HCDR3 95 105 GGYRPYYAMDY Function arises via a disorder to order transition Molecular assembly Substrate/ligand binding X-ray crystallography isopropanol 20 PEG4000 w/v 14 sodium citrate pH 5.5 0.1 Paper 7506692 Calcutt MJ, Kremer MT, Giblin MF, Quinn TP, Deutscher SL 1993 Gene 137 1 77-83 15784256 Schuermann JP, Prewitt SP, Davies C, Deutscher SL, Tanner JJ 2005 J Mol Biol 347 5 965-78 A UniProt ID cannot be located for this protein. The Vh sequence for DNA-1 is similar to an anti-ssDNA mAB from NZB x NZW F1 autoimmune mice (NCBI Accession CAA80108.1, GI 297744). In UniProt, there is 98% sequence identity with entries P01868 and P01869, the IgG-1 chain C region. Rhodopsin OPSD_BOVIN P02699 Bt.12753 OPSD_BOVIN 129204 Bos taurus (Bovine) 348 MNGTEGPNFYVPFSNKTGVVRSPFEAPQYYLAEPWQFSMLAAYMFLLIMLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVFGGFTTTLYTSLHGYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLVGWSRYIPEGMQCSCGIDYYTPHEETNNESFVIYMFVVHFIIPLIVIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVIAFLICWLPYAGVAFYIFTHQGSDFGPIFMTIPAFFAKTSAVYNPVIYIMMNKQFRNCMVTTLCCGKNPLGDDEASTTVSKTETSQVAPA Disordered 236 239 QQQE Relationship to function unknown X-ray crystallography Paper 10926528 Palczewski K, Kumasaka T, Hori T, Behnke CA, Motoshima H, Fox BA, Le Trong I, Teller DC, Okada T, Stenkamp RE, Yamamoto M, Miyano M 2000 Science 289 5480 739-45 Disordered 328 333 LGDDEA X-ray crystallography Paper 10926528 Palczewski K, Kumasaka T, Hori T, Behnke CA, Motoshima H, Fox BA, Le Trong I, Teller DC, Okada T, Stenkamp RE, Yamamoto M, Miyano M 2000 Science 289 5480 739-45 Disordered 133 137 IERYV X-ray crystallography Paper 10926528 Palczewski K, Kumasaka T, Hori T, Behnke CA, Motoshima H, Fox BA, Le Trong I, Teller DC, Okada T, Stenkamp RE, Yamamoto M, Miyano M 2000 Science 289 5480 739-45 Disordered 327 348 PLGDDEASTTVSKTETSQVAPA X-ray crystallography Paper 10926528 Palczewski K, Kumasaka T, Hori T, Behnke CA, Motoshima H, Fox BA, Le Trong I, Teller DC, Okada T, Stenkamp RE, Yamamoto M, Miyano M 2000 Science 289 5480 739-45 Disordered 207 222 MFVVHFIIPLIVIFFC X-ray crystallography Paper 10926528 Palczewski K, Kumasaka T, Hori T, Behnke CA, Motoshima H, Fox BA, Le Trong I, Teller DC, Okada T, Stenkamp RE, Yamamoto M, Miyano M 2000 Science 289 5480 739-45 Mu-type opioid receptor [Isoform 1] OPRM_HUMAN Mu opioid receptor MOP hMOP Mu opiate receptor MOR-1 P35372-1 Hs.2353 OPRM_HUMAN 2851402 Homo sapiens (Human) 400 MDSSAAPTNASNCTDALAYSSCSPAPSPGSWVNLSHLDGNLSDPCGPNRTDLGGRDSLCPPTGSPSMITAITIMALYSIVCVVGLFGNFLVMYVIVRYTKMKTATNIYIFNLALADALATSTLPFQSVNYLMGTWPFGTILCKIVISIDYYNMFTSIFTLCTMSVDRYIAVCHPVKALDFRTPRNAKIINVCNWILSSAIGLPVMFMATTKYRQGSIDCTLTFSHPTWYWENLLKICVFIFAFIMPVLIITVCYGLMILRLKSVRMLSGSKEKDRNLRRITRMVLVVVAVFIVCWTPIHIYVIIKALVTIPETTFQTVSWHFCIALGYTNSCLNPVLYAFLDENFKRCFREFCIPTSSNIEQQNSTRIRQNTRDHPSTANTVDRTNHQLENLEAETAPLP Disordered 128 143 VNYLMGTWPFGTILCK Fragment Mutant Molecular recognition effectors Circular dichroism (CD) spectroscopy, near-UV 7 Tris-HCl buffer 10 NaCl buffer 50 protein 15 Paper 15680247 Kerman A, Ananthanarayanan VS 2005 Biochim Biophys Acta 1747 1 133-40 The fragment used for structure determination contained residues 97-176 of the human µR. Guanine nucleotide-binding protein G(t) subunit alpha-1 GNAT1_BOVIN Transducin alpha-1 chain P04695 Bt.4774 GNAT1_BOVIN 121031 Bos taurus (Bovine) 350 MGAGASAEEKHSRELEKKLKEDAEKDARTVKLLLLGAGESGKSTIVKQMKIIHQDGYSLEECLEFIAIIYGNTLQSILAIVRAMTTLNIQYGDSARQDDARKLMHMADTIEEGTMPKEMSDIIQRLWKDSGIQACFDRASEYQLNDSAGYYLSDLERLVTPGYVPTEQDVLRSRVKTTGIIETQFSFKDLNFRMFDVGGQRSERKKWIHCFEGVTCIIFIAALSAYDMVLVEDDEVNRMHESLHLFNSICNHRYFATTSIVLFLNKKDVFSEKIKKAHLSICFPDYNGPNTYEDAGNYIKVQFLELNMRRDVKEIYSHMTCATDTQNVKFVFDAVTDIIIKENLKDCGLF Disordered Gt alpha 340 350 IKENLKDCGLF Function arises via an order to disorder transition Nuclear magnetic resonance (NMR) 274 2H2O 10 DTT 1 EDTA 0.1 KCl 100 sodium phosphate pH 7.5 20 Paper 9539726 Kisselev OG, Kao J, Ponder JW, Fann YC, Gautam N, Marshall GR 1998 Proc Natl Acad Sci U S A 95 8 4270-5 Collagen alpha-1(II) chain [Isoform 2] CO2A1_HUMAN Alpha-1 type II collagen Chondrocalcin [cleavage product 1] P02458-2 Hs.408182 CO2A1_HUMAN 124056489 Homo sapiens (Human) 1487 MIRLGAPQSLVLLTLLVAAVLRCQGQDVQEAGSCVQDGQRYNDKDVWKPEPCRICVCDTGTVLCDDIICEDVKDCLSPEIPFGECCPICPTDLATASGQPGPKGQKGEPGDIKDIVGPKGPPGPQGPAGEQGPRGDRGDKGEKGAPGPRGRDGEPGTPGNPGPPGPPGPPGPPGLGGNFAAQMAGGFDEKAGGAQLGVMQGPMGPMGPRGPPGPAGAPGPQGFQGNPGEPGEPGVSGPMGPRGPPGPPGKPGDDGEAGKPGKAGERGPPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGENGSPGPMGPRGLPGERGRTGPAGAAGARGNDGQPGPAGPPGPVGPAGGPGFPGAPGAKGEAGPTGARGPEGAQGPRGEPGTPGSPGPAGASGNPGTDGIPGAKGSAGAPGIAGAPGFPGPRGPPGPQGATGPLGPKGQTGEPGIAGFKGEQGPKGEPGPAGPQGAPGPAGEEGKRGARGEPGGVGPIGPPGERGAPGNRGFPGQDGLAGPKGAPGERGPSGLAGPKGANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQGARGQPGVMGFPGPKGANGEPGKAGEKGLPGAPGLRGLPGKDGETGAAGPPGPAGPAGERGEQGAPGPSGFQGLPGPPGPPGEGGKPGDQGVPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDGPKGASGPAGPPGAQGPPGLQGMPGERGAAGIAGPKGDRGDVGEKGPEGAPGKDGGRGLTGPIGPPGPAGANGEKGEVGPPGPAGSAGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGEQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGRVGPPGSNGNPGPPGPPGPSGKDGPKGARGDSGPPGRAGEPGLQGPAGPPGEKGEPGDDGPSGAEGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGASGDRGPPGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGVKGDRGETGAVGAPGAPGPPGSPGPAGPTGKQGDRGEAGAQGPMGPSGPAGARGIQGPQGPRGDKGEAGEPGERGLKGHRGFTGLQGLPGPPGPSGDQGASGPAGPSGPRGPPGPVGPSGKDGANGIPGPIGPPGPRGRSGETGPAGPPGNPGPPGPPGPPGPGIDMSAFAGLGPREKGPDPLQYMRADQAAGGLRQHDAEVDATLKSLNNQIESIRSPEGSRKNPARTCRDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMETGETCVYPNPANVPKKNWWSSKSKEKKHIWFGETINGGFHFSYGDDNLAPNTANVQMTFLRLLSTEGSQNITYHCKNSIAYLDEAAGNLKKALLIQGSNDVEIRAEGNSRFTYTALKDGCTKHTGKWGKTVIEYRSQKTSRLPIIDIAPMDIGGPEQEFGVDIGPVCFL Disordered linker region 71 75 DVKDC Engineered Fragment 1U5MA Function arises via a disorder to order transition Substrate/ligand binding Nuclear magnetic resonance (NMR) 298 6 protein 0.8 potassium phosphate buffer (90% v/v) 50 2H2O v/v 10 sodium azide v/v 0.02 Paper 15466413 O'Leary JM, Hamilton JM, Deane CM, Valeyev NV, Sandell LJ, Downing AK 2004 J Biol Chem 279 51 53857-66 Yersinia crystallin Q7CJN0_YERPE Beta-gamma-crystallin Putative exported protein Putative uncharacterized protein Q7CJN0 Q7CJN0_YERPE 123776891 Yersinia pestis 806 MRYNRNHMLTLMFSLLIFDAYANEPKVCFYMDDDYNGESLCAAQGNSVASIPDKWNDRISSISIPHGLVVTVYEDVDFLGASRSFEADVDLVSDKDLIYLNDNISAFKIKKAVCFYGESNFTGDSLCLSSGEQFDLYRGNYPERKQSHLVNPLNDEVYSIKIPPGMQTTVYEDDDYNGKYFVLTEDYTPDDLLIIRMNNKISSMRVSQDEDFICDRFCSIKKSIKFKIQKSFGSYWIDPRIKYRDILLDFQLSDTDDYSIKFFDEGLIKVKNYKLFFFDGNEKHGEGFLFNLSDKSSNLSFLLRFNGGFFQIQFVESLNNEIVYSSPLIGTLFDDANSDVIFDINNVDANSPIVIDKMVLTVGKEHNRAERSTLGLATCWAIPILSIYNYIVQGHCNQADKFVHNAADFFGSPADKILQIFGSSLPLPPKNSNETLDDESALINFMSDVKGTLTYITTNMGEHALTVPATALACKASMREKILPHLRNRRDLAPGCIDWTLSILTDFTLLFGASIEYWNSKNFGRVIENIVREGEIGSAVADVDTASRLIESVQAHVAEATEVADIIHLKTAFDFSQLSYVSYVRHTEEEVVSPQSAQALPLGRYELALVDYHFIETVPRIRQDGRWVERPDLHFDIEVISGVPEETDASRQVLLPIIEAWQHSYSQQELLFHASDILPESSLARYEIEPLLEASRLTSEVAISWLRTSRDDFVYVVVRLEGEVISLTMAVDININDVGVAGSLTNPDYVITPNAEGAVRGAGTAAIRALADHFKRKGKISLVSSVISQPSAIVKKKVGFRFIEEL Disordered Domain 1 21 112 YANEPKVCFYMDDDYNGESLCAAQGNSVASIPDKWNDRISSISIPHGLVVTVYEDVDFLGASRSFEADVDLVSDKDLIYLNDNISAFKIKKA Engineered Fragment Monomeric Function arises via a disorder to order transition Metal sponge Metal binding Circular dichroism (CD) spectroscopy, far-UV 298 Calcium chloride DTT 1 KCl 150 Tris pH 7.5 20 Circular dichroism (CD) spectroscopy, near-UV Calcium chloride NaCl 100 Tris pH 7.5 50 Paper 15536081 Jobby MK, Sharma Y 2005 J Biol Chem 280 2 1209-16 Disordered Domain 2 110 215 KKAVCFYGESNFTGDSLCLSSGEQFDLYRGNYPERKQSHLVNPLNDEVYSIKIPPGMQTTVYEDDDYNGKYFVLTEDYTPDDLLIIRMNNKISSMRVSQDEDFICD Engineered Relationship to function unknown Metal sponge Metal binding Circular dichroism (CD) spectroscopy, far-UV 298 Calcium chloride DTT 1 KCl 100 Tris pH 7.5 15 Paper 15536081 Jobby MK, Sharma Y 2005 J Biol Chem 280 2 1209-16 16470515 Jobby MK, Sharma Y 2006 Biomed Chromatogr 20 9 956-63 Membrane fusion protein p14 Q80FJ1_9REOV Q80FJ1 Q80FJ1_9REOV 75564240 Reptilian orthoreovirus 125 MGSGPSNFVNHAPGEAIVTGLEKGADKVAGTISHTIWEVIAGLVALLTFLAFGFWLFKYLQKRRERRRQLTEFQKRYLRNSYRLSEIQRPISQHEYEDPYEPPSRRKPPPPPYSTYVNIDNVSAI Disordered 2 14 GSGPSNFVNHAPG Function arises via a disorder to order transition Circular dichroism (CD) spectroscopy, far-UV 298 protein 10-80 uM in water Nuclear magnetic resonance (NMR) 278 7.2 1H2O 90 2H2O 10 lyophilized acetyl-p14 peptide 5 potassium phosphate buffer 50 Nuclear magnetic resonance (NMR) 278 7.2 1H2O 90 2H2O 10 myristoylated p14 peptide 0.5 potassium phosphate buffer 50 Paper 15448165 Corcoran JA, Syvitski R, Top D, Epand RM, Epand RF, Jakeman D, Duncan R 2004 J Biol Chem 279 49 51386-94 This region contains an extended "loop structure" comprising residues Pro5 to Pro13. Disordered 15 31 EAIVTGLEKGADKVAGT Function arises via a disorder to order transition Entropic chain Flexible linkers/spacers Circular dichroism (CD) spectroscopy, far-UV 298 protein 10-80 uM in water Nuclear magnetic resonance (NMR) 278 7.2 1H2O 90 2H2O 10 lyophilized acetyl-p14 peptide 5 potassium phosphate buffer 50 Nuclear magnetic resonance (NMR) 278 7.2 1H2O 90 2H2O 10 myristoylated p14 peptide 0.5 potassium phosphate buffer 50 Paper 15448165 Corcoran JA, Syvitski R, Top D, Epand RM, Epand RF, Jakeman D, Duncan R 2004 J Biol Chem 279 49 51386-94 Cytochrome c oxidase copper chaperone COX17_YEAST COX copper chaperone Cox17 Q12287 COX17_YEAST 2493874 Saccharomyces cerevisiae (Baker's yeast) 69 MTETDKKQEQENHAECEDKPKPCCVCKPEKEERDTCILFNGQDSEKCKEFIEKYKECMKGYGFEVPSAN Disordered 64 69 EVPSAN Complex Function arises from the disordered state Metal binding Protein-protein binding Nuclear magnetic resonance (NMR) 298 6 CuCl anaerobic solution 6.1 HCl anaerobic solution 10 NaCl 100 potassium phosphate 100 protein 1 sodium chloride anaerobic solution 1 Paper 15465825 Abajian C, Yatsunyk LA, Ramirez BE, Rosenzweig AC 2004 J Biol Chem 279 51 53584-92 This is the Cox17 protein in complex with copper. Disordered 64 69 EVPSAN Function arises from the disordered state Metal binding Protein-protein binding Nuclear magnetic resonance (NMR) 298 6 D2O v/v 7 potassium phosphate 20 protein 1 TCEP 1 Paper 15465825 Abajian C, Yatsunyk LA, Ramirez BE, Rosenzweig AC 2004 J Biol Chem 279 51 53584-92 This is the Cox17 protein is its apo form. Disordered 1 22 MTETDKKQEQENHAECEDKPKP Complex Function arises from the disordered state Metal binding Protein-protein binding Nuclear magnetic resonance (NMR) 298 6 CuCl anaerobic solution 6.1 HCl anaerobic solution 10 NaCl 100 potassium phosphate 100 protein 1 sodium chloride anaerobic solution 1 Paper 15465825 Abajian C, Yatsunyk LA, Ramirez BE, Rosenzweig AC 2004 J Biol Chem 279 51 53584-92 This is the Cox17 protein in complex with copper. Disordered 1 26 MTETDKKQEQENHAECEDKPKPCCVC Function arises from the disordered state Metal binding Protein-protein binding Nuclear magnetic resonance (NMR) 298 6 protein 1 potassium phosphate 20 TCEP 1 D2O v/v 7 Paper 15465825 Abajian C, Yatsunyk LA, Ramirez BE, Rosenzweig AC 2004 J Biol Chem 279 51 53584-92 This is the Cox17 protein in the apo form Gap junction alpha-1 protein CXA1_RAT Connexin-43 Cx43 Gap junction 43 kDa heart protein P08050 Rn.10346 CXA1_RAT 117708 Rattus norvegicus (Rat) 381 GDWSALGKLLDKVQAYSTAGGKVWLSVLFIFRILLLGTAVESAWGDEQSAFRCNTQQPGCENVCYDKSFPISHVRFWVLQIIFVSVPTLLYLAHVFYVMRKEEKLNKKEEELKVAQTDGVNVEMHLKQIEIKKFKYGIEEHGKVKMRGGLLRTYIISILFKSVFEVAFLLIQWYIYGFSLSAVYTCKRDPCPHQVDCFLSRPTEKTIFIIFMLVVSLVSLALNIIELFYVFFKGVKDRVKGRSDPYHATTGPLSPSKDCGSPKYAYFNGCSSPTAPLSPMSPPGYKLVTGDRNNSSCRNYNKQASEQNWANYSAEQNRMGQAGSTISNSHAQPFDFPDDNQNAKKVAAGHELQPLAIVDQRPSSRASSRASSRPRPDDLEI Disordered 250 313 TGPLSPSKDCGSPKYAYFNGCSSPTAPLSPMSPPGYKLVTGDRNNSSCRNYNKQASEQNWANYS Fragment Function arises via a disorder to order transition Molecular assembly Entropic chain Protein-protein binding Flexible linkers/spacers Phosphorylation Nuclear magnetic resonance (NMR) 280 5.8 phosphate saline buffer Paper 15492000 Sorgen PL, Duffy HS, Sahoo P, Coombs W, Delmar M, Spray DC 2004 J Biol Chem 279 52 54695-701 14699011 Duffy HS, Ashton AW, O'Donnell P, Coombs W, Taffet SM, Delmar M, Spray DC 2004 Circ Res 94 2 215-22 12151412 Duffy HS, Sorgen PL, Girvin ME, O'Donnell P, Coombs W, Taffet SM, Delmar M, Spray DC 2002 J Biol Chem 277 39 36706-14 15284189 Seki A, Duffy HS, Coombs W, Spray DC, Taffet SM, Delmar M 2004 Circ Res 95 4 e22-8 Disordered 326 338 ISNSHAQPFDFPD Fragment Function arises via a disorder to order transition Molecular assembly Entropic chain Flexible linkers/spacers Phosphorylation Protein-protein binding Nuclear magnetic resonance (NMR) 280 5.8 phosphate saline buffer Paper 15492000 Sorgen PL, Duffy HS, Sahoo P, Coombs W, Delmar M, Spray DC 2004 J Biol Chem 279 52 54695-701 14699011 Duffy HS, Ashton AW, O'Donnell P, Coombs W, Taffet SM, Delmar M, Spray DC 2004 Circ Res 94 2 215-22 12151412 Duffy HS, Sorgen PL, Girvin ME, O'Donnell P, Coombs W, Taffet SM, Delmar M, Spray DC 2002 J Biol Chem 277 39 36706-14 15284189 Seki A, Duffy HS, Coombs W, Spray DC, Taffet SM, Delmar M 2004 Circ Res 95 4 e22-8 Disordered 348 381 AGHELQPLAIVDQRPSSRASSRASSRPRPDDLEI Fragment Function arises via a disorder to order transition Molecular assembly Entropic chain Flexible linkers/spacers Phosphorylation Protein-protein binding Nuclear magnetic resonance (NMR) 280 5.8 phosphate saline buffer Paper 15492000 Sorgen PL, Duffy HS, Sahoo P, Coombs W, Delmar M, Spray DC 2004 J Biol Chem 279 52 54695-701 14699011 Duffy HS, Ashton AW, O'Donnell P, Coombs W, Taffet SM, Delmar M, Spray DC 2004 Circ Res 94 2 215-22 12151412 Duffy HS, Sorgen PL, Girvin ME, O'Donnell P, Coombs W, Taffet SM, Delmar M, Spray DC 2002 J Biol Chem 277 39 36706-14 15284189 Seki A, Duffy HS, Coombs W, Spray DC, Taffet SM, Delmar M 2004 Circ Res 95 4 e22-8 Olfactory marker protein OMP_RAT Olfactory neuronal-specific protein P08523 Rn.9720 OMP_RAT 129096 Rattus norvegicus (Rat) 163 MAEDGPQKQQLDMPLVLDQDLTKQMRLRVESLKQRGEKKQDGEKLLRPAESVYRLDFIQQQKLQFDHWNVVLDKPGKVTITGTSQNWTPDLTNLMTRQLLDPAAIFWRKEDSDAMDWNEADALEFGERLSDLAKIRKVMYFLITFGEGVEPANLKASVVFNQL Disordered Loop 1 35 49 RGEKKQDGEKLLRPA Nuclear magnetic resonance (NMR) 310 D2O 5 H2O 95 Na2EDTA 0.1 Na2HPO4 pH 6.6 5 NaN3 0.3 Paper 16008352 Gitti RK, Wright NT, Margolis JW, Varney KM, Weber DJ, Margolis FL 2005 Biochemistry 44 28 9673-9679 Disordered Loop 2 57 68 FIQQQKLQFDHW Nuclear magnetic resonance (NMR) H2O 95 D2O 5 Na2HPO4 pH 6.6 5 NaN3 0.3 Na2EDTA 0.1 Paper 16008352 Gitti RK, Wright NT, Margolis JW, Varney KM, Weber DJ, Margolis FL 2005 Biochemistry 44 28 9673-9679 Disordered Omega Loop 84 99 SQNWTPDLTNLMTRQL Nuclear magnetic resonance (NMR) D2O 5 H2O 95 Na2EDTA 0.1 Na2HPO4 pH 6.6 5 NaN3 0.3 Paper 16008352 Gitti RK, Wright NT, Margolis JW, Varney KM, Weber DJ, Margolis FL 2005 Biochemistry 44 28 9673-9679 Perfringolysin O TACY_CLOPE Theta-toxin Thiol-activated cytolysin P0C2E9 TACY_CLOPE 124053391 Clostridium perfringens 500 MIRFKKTKLIASIAMALCLFSQPVISFSKDITDKNQSIDSGISSLSYNRNEVLASNGDKIESFVPKEGKKTGNKFIVVERQKRSLTTSPVDISIIDSVNDRTYPGALQLADKAFVENRPTILMVKRKPININIDLPGLKGENSIKVDDPTYGKVSGAIDELVSKWNEKYSSTHTLPARTQYSESMVYSKSQISSALNVNAKVLENSLGVDFNAVANNEKKVMILAYKQIFYTVSADLPKNPSDLFDDSVTFNDLKQKGVSNEAPPLMVSNVAYGRTIYVKLETTSSSKDVQAAFKALIKNTDIKNSQQYKDIYENSSFTAVVLGGDAQEHNKVVTKDFDEIRKVIKDNATFSTKNPAYPISYTSVFLKDNSVAAVHNKTDYIETTSTEYSKGKINLDHSGAYVAQFEVAWDEVSYDKEGNEVLTHKTWDGNYQDKTAHYSTVIPLEANARNIRIKARECTGLAWEWWRDVISEYDVPLTNNINVSIWGTTLYPGSSITYN Disordered TMH1 190 217 SQISSALNVNAKVLENSLGVDFNAVANN Monomeric Mutant Fluorescent probes 298 HEPES pH 7.5 50 NaCl 100 Paper 15797734 Dang TX, Hotze EM, Rouiller I, Tweten RK, Wilson-Kubalek EM 2005 J Struct Biol 150 1 100-8 10555145 Shatursky O, Heuck AP, Shepard LA, Rossjohn J, Parker MW, Johnson AE, Tweten RK 1999 Cell 99 3 293-9 The six alpha-helices in domain 3 undergo a conformational change into two beta-hairpins that span the membrane. This order to order transition proceeds through a disordered intermediate. Disordered TMH2 288 311 KDVQAAFKALIKNTDIKNSQQYKD Monomeric Mutant Fluorescent probes 298 HEPES pH 7.5 50 NaCl 100 Paper 15797734 Dang TX, Hotze EM, Rouiller I, Tweten RK, Wilson-Kubalek EM 2005 J Struct Biol 150 1 100-8 10555145 Shatursky O, Heuck AP, Shepard LA, Rossjohn J, Parker MW, Johnson AE, Tweten RK 1999 Cell 99 3 293-9 The six alpha-helices in domain 3 undergo a conformational change into two beta-hairpins that span the membrane. This order to order transition proceeds through a disordered intermediate. Copper-transporting ATPase 1 [Isoform 4] ATP7A_HUMAN EC 3.6.3.4 Copper pump 1 Menkes disease-associated protein Q04656-1 Hs.496414 ATP7A_HUMAN 223590241 Homo sapiens (Human) 1500 MDPSMGVNSVTISVEGMTCNSCVWTIEQQIGKVNGVHHIKVSLEEKNATIIYDPKLQTPKTLQEAIDDMGFDAVIHNPDPLPVLTDTLFLTVTASLTLPWDHIQSTLLKTKGVTDIKIYPQKRTVAVTIIPSIVNANQIKELVPELSLDTGTLEKKSGACEDHSMAQAGEVVLKMKVEGMTCHSCTSTIEGKIGKLQGVQRIKVSLDNQEATIVYQPHLISVEEMKKQIEAMGFPAFVKKQPKYLKLGAIDVERLKNTPVKSSEGSQQRSPSYTNDSTATFIIDGMHCKSCVSNIESTLSALQYVSSIVVSLENRSAIVKYNASSVTPESLRKAIEAVSPGLYRVSITSEVESTSNSPSSSSLQKIPLNVVSQPLTQETVINIDGMTCNSCVQSIEGVISKKPGVKSIRVSLANSNGTVEYDPLLTSPETLRGAIEDMGFDATLSDTNEPLVVIAQPSSEMPLLTSTNEFYTKGMTPVQDKEEGKNSSKCYIQVTGMTCASCVANIERNLRREEGIYSILVALMAGKAEVRYNPAVIQPPMIAEFIRELGFGATVIENADEGDGVLELVVRGMTCASCVHKIESSLTKHRGILYCSVALATNKAHIKYDPEIIGPRDIIHTIESLGFEASLVKKDRSASHLDHKREIRQWRRSFLVSLFFCIPVMGLMTYMMVMDHHFATLHHNQNMSKEEMINLHSSMFLERQILPGLSVMNLLSFLLCVPVQFFGGWYFYIQAYKALKHKTANMDVLIVLATTIAFAYSLIILLVAMYERAKVNPITFFDTPPMLFVFIALGRWLEHIAKGKTSEALAKLISLQATEATIVTLDSDNILLSEEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKPGSTVIAGSINQNGSLLICATHVGADTTLSQIVKLVEEAQTSKAPIQQFADKLSGYFVPFIVFVSIATLLVWIVIGFLNFEIVETYFPGYNRSISRTETIIRFAFQASITVLCIACPCSLGLATPTAVMVGTGVGAQNGILIKGGEPLEMAHKVKVVVFDKTGTITHGTPVVNQVKVLTESNRISHHKILAIVGTAESNSEHPLGTAITKYCKQELDTETLGTCIDFQVVPGCGISCKVTNIEGLLHKNNWNIEDNNIKNASLVQIDASNEQSSTSSSMIIDAQISNALNAQQHKVLIGNREWMIRNGLVINNDVNDFMTEHERKGRTAVLVAVDDELCGLIAIADTVKPEAELAIHILKSMGLEVVLMTGDNSKTARSIASQVGITKVFAEVLPSHKVAKVKQLQEEGKRVAMVGDGINDSPALAMANVGIAIGTGTDVAIEAADVVLIRNDLLDVVASIDLSRKTVKRIRINFVFALIYNLVGIPIAAGVFMPIGLVLQPWMGSAAMAASSVSVVLSSLFLKLYRKPTYESYELPARSQIGQKSPSEISVHVGIDDTSRNSPKLGLLDRIVNYSRASINSLLSDKRSLNSVVTSEPDKHSLLVGDFREDDDTAL Disordered 164 168 SMAQA Fragment Mutant Nuclear magnetic resonance (NMR) 298 Paper 14572476 Jones CE, Daly NL, Cobine PA, Craik DJ, Dameron CT 2003 J Struct Biol 143 3 209-18 A single point mutation of MNKr2 was created with a F72I substitution, as discussed in the Jones et al. article. Disordered Loop 1 171 180 VVLKMKVEGM Monomeric Function arises via a disorder to order transition Substrate/ligand binding Nuclear magnetic resonance (NMR) 298 Nuclear magnetic resonance (NMR) 298 7 2H2O v/v 10 DTT excess protein 1 sodium phsophate buffer 100 Paper 15035611 Banci L, Bertini I, Del Conte R, D'Onofrio M, Rosato A 2004 Biochemistry 43 12 3396-403 14572476 Jones CE, Daly NL, Cobine PA, Craik DJ, Dameron CT 2003 J Struct Biol 143 3 209-18 Disordered 239 246 KKQPKYLK Fragment Mutant Nuclear magnetic resonance (NMR) 298 Paper 14572476 Jones CE, Daly NL, Cobine PA, Craik DJ, Dameron CT 2003 J Struct Biol 143 3 209-18 A single point mutation of MNKr2 was created with a F72I substitution, as discussed in the Jones et al. article. Tail-associated lysozyme VG05_BPT4 EC 3.2.1.17 Protein Gp5 P16009 VG05_BPT4 137895 Enterobacteria phage T4 (Bacteriophage T4) 575 MEMISNNLNWFVGVVEDRMDPLKLGRVRVRVVGLHPPQRAQGDVMGIPTEKLPWMSVIQPITSAAMSGIGGSVTGPVEGTRVYGHFLDKWKTNGIVLGTYGGIVREKPNRLEGFSDPTGQYPRRLGNDTNVLNQGGEVGYDSSSNVIQDSNLDTAINPDDRPLSEIPTDDNPNMSMAEMLRRDEGLRLKVYWDTEGYPTIGIGHLIMKQPVRDMAQINKVLSKQVGREITGNPGSITMEEATTLFERDLADMQRDIKSHSKVGPVWQAVNRSRQMALENMAFQMGVGGVAKFNTMLTAMLAGDWEKAYKAGRDSLWYQQTKGRASRVTMIILTGNLESYGVEVKTPARSLSAMAATVAKSSDPADPPIPNDSRILFKEPVSSYKGEYPYVHTMETESGHIQEFDDTPGQERYRLVHPTGTYEEVSPSGRRTRKTVDNLYDITNADGNFLVAGDKKTNVGGSEIYYNMDNRLHQIDGSNTIFVRGDETKTVEGNGTILVKGNVTIIVEGNADITVKGDATTLVEGNQTNTVNGNLSWKVAGTVDWDVGGDWTEKMASMSSISSGQYTIDGSRIDIG Disordered 343 361 VKTPARSLSAMAATVAKSS Complex Native Substrate/ligand binding X-ray crystallography 285 PEG 8000 5.2 to 5.6%(w/v) Tris-HCl pH 7.2 to 8.0 0.65 glycerol v/v 35 Paper 15701513 Kanamaru S, Ishiwata Y, Suzuki T, Rossmann MG, Arisaka F 2005 J Mol Biol 346 4 1013-20 Glutenin, high molecular weight subunit DX5 GLT5_WHEAT P10388 GLT5_WHEAT 193806387 Triticum aestivum (Wheat) 839 MAKRLVLFVAVVVALVALTVAEGEASEQLQCERELQELQERELKACQQVMDQQLRDISPECHPVVVSPVAGQYEQQIVVPPKGGSFYPGETTPPQQLQQRIFWGIPALLKRYYPSVTCPQQVSYYPGQASPQRPGQGQQPGQGQQGYYPTSPQQPGQWQQPEQGQPGYYPTSPQQPGQLQQPAQGQQPGQGQQGQQPGQGQPGYYPTSSQLQPGQLQQPAQGQQGQQPGQAQQGQQPGQGQQPGQGQQGQQPGQGQQPGQGQQGQQLGQGQQGYYPTSLQQSGQGQPGYYPTSLQQLGQGQSGYYPTSPQQPGQGQQPGQLQQPAQGQQPGQGQQGQQPGQGQQGQQPGQGQQPGQGQPGYYPTSPQQSGQGQPGYYPTSSQQPTQSQQPGQGQQGQQVGQGQQAQQPGQGQQPGQGQPGYYPTSPQQSGQGQPGYYLTSPQQSGQGQQPGQLQQSAQGQKGQQPGQGQQPGQGQQGQQPGQGQQGQQPGQGQPGYYPTSPQQSGQGQQPGQWQQPGQGQPGYYPTSPLQPGQGQPGYDPTSPQQPGQGQQPGQLQQPAQGQQGQQLAQGQQGQQPAQVQQGQQPAQGQQGQQLGQGQQGQQPGQGQQGQQPAQGQQGQQPGQGQHGQQPGQGQQGQQPGQGQQPGQGQPWYYPTSPQESGQGQQPGQWQQPGQGQPGYYLTSPLQLGQGQQGYYPTSLQQPGQGQQPGQWQQSGQGQHWYYPTSPKLSGQGQRPGQWLQPGQGQQGYYPTSPQQPPQGQQLGQWLQPGQGQQGYYPTSLQQTGQGQQSGQGQQGYYSSYHVSVEHQAASLKVAKAQQLAAQLPAMCRLEGGDALSASQ Disordered - Pre-Molten Globule T-A-1 147 440 YYPTSPQQPGQWQQPEQGQPRYYPTSPQQSGQLQQPAQGQQPGQGQQGQQPGQGQPGYYPTSSQLQPGQLQQPAQGQQGQQPGQAQQGQQPGQGQQPGQGQQGQQPGQGQQPGQGQQGQQLGQGQQGYYPTSLQQSGQGQPGYYPTSLQQLGQGQSGYYPTSPQQPGQGQQPGQLQQPAQGQQPGQGQQGQQPGQGQQGQQPGQGQQPGQGQPGYYPTSPQQSGQGQPGYYPTSSQQPTQSQQPGQGQQGQQVGQGQQAQQPGQGQQPGQGQPGYYPTSPQQSGQGQPGYYLTS Fragment Raman optical activity Dynamic light scattering protein 3 to 4 mg/mL Paper 12741823 Blanch EW, Kasarda DD, Hecht L, Nielsen K, Barron LD 2003 Biochemistry 42 19 5665-73 Protein quaking-A [Isoform 1] QKIA_XENLA Xqua Q32NN2-1 Xl.55586 QKIA_XENLA 108860915 Xenopus laevis (African clawed frog) 341 MVGEMETKEKPKPTPDYLMQLMNDKKLMSSLPNFCGIFTHLERLLDEEISRVRKDMYNDTMNSSSNEKRTSELPDGIGPIVQLQEKLYVPVKEYPDFNFVGRILGPRGLTAKQLEAETGCKIMVRGKGSMRDKKKEEQNRGKPNWEHLNEDLHVLITVEDAQNRAELKLKRAVEEVKKLLVPAAEGEDSLKKMQLMELAILNGTYRDANLKSPALAFSLAATGQAPRIITGPAPVLSPAALRTPTPAGHTLMPLIRQIQTAVMPNGTPHPTATLMQQAPEGGLIYTPYEYPYTLAPATSILEYPIEASGVLGAVATKVRRHDMRVHPYQRIVTADRAATGN Disordered flexible linker 184 189 AEGEDS Fragment 2BL5A Function arises from the disordered state Entropic chain Flexible linkers/spacers Nuclear magnetic resonance (NMR) 298 6.5 pXqua KH-QUA2 protein 1 dithio-1,4-threitol 5 sodium phosphate 50 sodium azide w/v 0.05 3,3,3-trimethylsilylpropionate 20 2H2O v/v 10 Paper 15811367 Maguire ML, Guler-Gane G, Nietlispach D, Raine AR, Zorn AM, Standart N, Broadhurst RW 2005 J Mol Biol 348 2 265-79 Disordered 203 215 GTYRDANLKSPAL Fragment 2BL5A Nuclear magnetic resonance (NMR) 298 6.5 2H2O v/v 10 3,3,3-trimethysilylpropionate 20 dithio-1,4-threitol 5<