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 Far-UV circular dichroism (CD) Nuclear magnetic resonance (NMR) Analytical ultracentrifugation Hydrogen-deuterium Exchange Thermal stability 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, P. N. van Oosterhout, J. A. Stier, G. Tucker, P. A. van der Vliet, P. C. 1998 Journal of Molecular Biology 277 4 825-838 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 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 PA, Tsernoglou D, Tucker AD, Coenjaerts FE, Leenders H, van der Vliet PC 1994 Embo J 13 13 2994-3002 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 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 PA, Tsernoglou D, Tucker AD, Coenjaerts FE, Leenders H, van der Vliet PC 1994 Embo J 13 13 2994-3002 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 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 PA, Tsernoglou D, Tucker AD, Coenjaerts FE, Leenders H, van der Vliet PC 1994 Embo J 13 13 2994-3002 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, P. N. van Oosterhout, J. A. Stier, G. Tucker, P. A. van der Vliet, P. C. 1998 Journal of Molecular Biology 277 4 825-838 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, P. N. van Oosterhout, J. A. Stier, G. Tucker, P. A. van der Vliet, P. C. 1998 Journal of Molecular Biology 277 4 825-838 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 8039495 Tucker PA, Tsernoglou D, Tucker AD, Coenjaerts FE, Leenders H, van der Vliet PC 1994 Embo J 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 Cathelicidin antimicrobial peptide CAMP_HUMAN 18 kDa cationic antimicrobial protein CAP-18 hCAP-18 Antimicrobial protein CAP-18 LL-37 Antibacterial protein FALL-39 [cleavage product 1] FALL-39 peptide antibiotic Antibacterial protein LL-37 [cleavage product 2] P49913 Hs.51120 CAMP_HUMAN 1706745 Homo sapiens (Human) 170 MKTQRNGHSLGRWSLVLLLLGLVMPLAIIAQVLSYKEAVLRAIDGINQRSSDANLYRLLDLDPRPTMDGDPDTPKPVSFTVKETVCPRTTQQSPEDCDFKKDGLVKRCMGTVTLNQARGSFDISCDKDNKRFALLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES Disordered - Extended 134 170 LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES Engineered Function arises via a disorder to order transition Unknown Unknown Near-UV circular dichroism (CD) spectroscopy 298 6 sodium chloride salt 160 magnesium sulfate salt 84 Paper 9452503 Johansson, J. Gudmundsson, G. H. Rottenberg, M. E. Berndt, K. D. Agerberth, B. 1998 J Biol Chem 273 6 3718-3724 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. 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 Paper 9659923 Mogridge J, Legault P, Li J, Van Oene MD, Kay LE, Greenblatt J 1998 Mol Cell 1 2 265-75 Cytochrome c CYC_HORSE Apocytochrome c P00004 Eca.1571 CYC_HORSE 119388048 Equus caballus (Horse) 104 GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWKEETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE Disordered 1 104 GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWKEETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE Paper 4344990 Stellwagen E, Rysavy R, Babul G 1972 J Biol Chem 247 24 8074-7 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 Paper 10329190 Chang JF, Phillips K, Lundback T, Gstaiger M, Ladbury JE, Luisi B 1999 J Mol Biol 288 5 941-52 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 89 103 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 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 3 521-530 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 3 521-530 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 3 521-530 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 3 521-530 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 3 521-530 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 3 521-530 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 3 521-530 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 3 521-530 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 3 521-530 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 3 521-530 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 708 831 IRKFSIVQKTPLQMNGIEEDSDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSVNQGQNIHRKTTASTRKVSLAPQANLTELDIYSRRLSQETGLEISEEINEEDLKE Paper Ostedgaard Lynda S, Baldursson Olafur, Vermeer Daniel W, Welsh Michael J, Robertson Andrew W 2000 PNAS 97 10 5657-5662 The sequence contains a mismatch at amino acid 470 when compared to PIR and SwissProt. Additional UniGene IDs, Hs.621460 and Hs.661104 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 112 145 DPRFQDSSSSKAPPPSLPSPSRLPGPSDTPILPQ 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 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 Far-UV circular dichroism (CD) 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 Far-UV circular dichroism (CD) 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 Far-UV circular dichroism (CD) 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 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 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 Aberrant mobility on SDS-PAGE gel Far-UV circular dichroism (CD) Gel filtration/size exclusion chromatography Insensitivity to 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 Far-UV circular dichroism (CD) 7 DTT 0.001 NaCl salt 50 sodium phosphate salt 10 Gel filtration/size exclusion chromatography 7 DTT 1 NaCl salt 150 sodium phosphate salt 10 Intrinsic fluorescence 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 Far-UV circular dichroism (CD) 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 22 106 EHPKPSACRNLFGPVDHEELTRDLEKHCRDMEEASQRKWNFDFQNHKPLEGKYEWQEVEKGSLPEFYYRPPRPPKGACKVPAQES 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 Cytochrome b-c1 complex subunit Rieske, mitochondrial UCRI_BOVIN Ubiquinol-cytochrome c reductase iron-sulfur subunit Rieske iron-sulfur protein RISP Cytochrome b-c1 complex subunit 5 Complex III subunit 5 EC=1.10.2.2 Cytochrome b-c1 complex subunit 11 [cleavage product 1] Ubiquinol-cytochrome c reductase 8 kDa protein Complex III subunit IX P13272 Bt.265 UCRI_BOVIN 1351360 Bos taurus (Bovine) 274 MLSVAARSGPFAPVLSATSRGVAGALRPLVQAAVPATSESPVLDLKRSVLCRESLRGQAAGRPLVASVSLNVPASVRYSHTDIKVPDFSDYRRPEVLDSTKSSKESSEARKGFSYLVTATTTVGVAYAAKNVVSQFVSSMSASADVLAMSKIEIKLSDIPEGKNMAFKWRGKPLFVRHRTKKEIDQEAAVEVSQLRDPQHDLERVKKPEWVILIGVCTHLGCVPIANAGDFGGYYCPCHGSHYDASGRIRKGPAPLNLEVPSYEFTSDDMVIVG Disordered 1 45 MLSVAARSGPFAPVLSATSRGVAGALRPLVQAAVPATSESPVLDL Paper 9651245 Iwata S, Lee JW, Okada K, Lee JK, Iwata M, Rasmussen B, Link TA, Ramaswamy S, Jap BK 1998 Science 281 5373 64-71 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 482 512 TDEDTPTAIARRNMTMDPNHVPGSEPNFAAY Paper 8620531 Konig P, Giraldo R, Chapman L, Rhodes D 1996 Cell 85 1 125-36 Elongation factor G EFG_THETH EF-G P13551 EFG_THETH 119190 Thermus thermophilus 691 MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERERGITITAAVTTCFWKDHRINIIDTPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSETVWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDVLRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEEELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVEIHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHANHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKADQEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDANVGKPQVAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIPAVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYHEVDSSEMAFKIAGSMAIKEAVQKGDPVILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLRSKTQGRGSFVMFFDHYQEVPKQVQEKLIKGQ Disordered 40 67 HKIGEVHEGAATMDFMEQERERGITITA 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 400 475 ESIEVPEPVIDVAIEPKTKADQEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDAN Paper 11054294 Laurberg M, Kristensen O, Martemyanov K, Gudkov AT, Nagaev I, Hughes D, Liljas A 2000 J Mol Biol 303 4 593-603 EMB-1 protein EMB1_DAUCA Embryonic abundant protein P17639 EMB1_DAUCA 119316 Daucus carota (Carrot) 92 MASQQEKKELDARARQGETVVPGGTGGKSLEAQQHLAEGRSKGGQTRKEQLGGEGYHEMGRKGGLSNNDMSGGERAEQEGIDIDESKFRTKK Disordered 1 92 MASQQEKKELDARARQGETVVPGGTGGKSLEAQQHLAEGRSKGGQTRKEQLGGEGYHEMGRKGGLSNNDMSGGERAEQEGIDIDESKFRTKK Paper Eom J, Baker WR, Kintanar A, Wurtele ES 1996 Plant Science 115 17-24 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 8 665-668 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 8 665-668 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 8 905-915 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 8 905-915 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 Infrared spectroscopy;Fourier transform 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 8 905-915 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 8 905-915 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 8 905-915 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 8 905-915 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 8 905-915 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 Paper 8245034 Pahel G, Aulabaugh A, Short SA, Barnes JA, Painter GR, Ray P, Phelps WC 1993 J Biol Chem 268 34 26018-25 Fibronectin-binding protein A FNBA_STAA8 FNBP Fibronectin-binding protein P14738 FNBA_STAA8 120457 Staphylococcus aureus (strain NCTC 8325) 1018 MKNNLRYGIRKHKLGAASVFLGTMIVVGMGQDKEAAASEQKTTTVEENGNSATDNKTSETQTTATNVNHIEETQSYNATVTEQPSNATQVTTEEAPKAVQAPQTAQPANIETVKEEVVKEEAKPQVKETTQSQDNSGDQRQVDLTPKKATQNQVAETQVEVAQPRTASESKPRVTRSADVAEAKEASNAKVETGTDVTSKVTVEIGSIEGHNNTNKVEPHAGQRAVLKYKLKFENGLHQGDYFDFTLSNNVNTHGVSTARKVPEIKNGSVVMATGEVLEGGKIRYTFTNDIEDKVDVTAELEINLFIDPKTVQTNGNQTITSTLNEEQTSKELDVKYKDGIGNYYANLNGSIETFNKANNRFSHVAFIKPNNGKTTSVTVTGTLMKGSNQNGNQPKVRIFEYLGNNEDIAKSVYANTTDTSKFKEVTSNMSGNLNLQNNGSYSLNIENLDKTYVVHYDGEYLNGTDEVDFRTQMVGHPEQLYKYYYDRGYTLTWDNGLVLYSNKANGNEKNGPIIQNNKFEYKEDTIKETLTGQYDKNLVTTVEEEYDSSTLDIDYHTAIDGGGGYVDGYIETIEETDSSAIDIDYHTAVDSEAGHVGGYTESSEESNPIDFEESTHENSKHHADVVEYEEDTNPGGGQVTTESNLVEFDEESTKGIVTGAVSDHTTVEDTKEYTTESNLIELVDELPEEHGQAQGPVEEITKNNHHISHSGLGTENGHGNYDVIEEIEENSHVDIKSELGYEGGQNSGNQSFEEDTEEDKPKYEQGGNIVDIDFDSVPQIHGQNKGNQSFEEDTEKDKPKYEHGGNIIDIDFDSVPHIHGFNKHTEIIEEDTNKDKPSYQFGGHNSVDFEEDTLPKVSGQNEGQQTIEEDTTPPIVPPTPPTPEVPSEPETPTPPTPEVPSEPETPTPPTPEVPSEPETPTPPTPEVPAEPGKPVPPAKEEPKKPSKPVEQGKVVTPVIEINEKVKAVAPTKKPQSKKSELPETGGEESTNKGMLFGGLFSILGLALLRRNKKNHKA Disordered 745 873 GQNSGNQSFEEDTEEDKPKYEQGGNIVDIDFDSVPQIHGQNKGNQSFEEDTEKDKPKYEHGGNIIDIDFDSVPHIHGFNKHTEIIEEDTNKDKPSYQFGGHNSVDFEEDTLPKVSGQNEGQQTIEEDTT 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 Flagellin FLIC_SALTY Phase-1-I flagellin P06179 FLIC_SALTY 20141325 Salmonella typhimurium 494 AQVINTNSLSLLTQNNLNKSQSALGTAIERLSSGLRINSAKDDAAGQAIANRFTANIKGLTQASRNANDGISIAQTTEGALNEINNNLQRVRELAVQSANSTNSQSDLDSIQAEITQRLNEIDRVSGQTQFNGVKVLAQDNTLTIQVGANDGETIDIDLKQINSQTLGLDTLNVQQKYKVSDTAATVTGYADTTIALDNSTFKASATGLGGTDQKIDGDLKFDDTTGKYYAKVTVTGGTGKDGYYEVSVDKTNGEVTLAGGATSPLTGGLPATATEDVKNVQVANADLTEAKAALTAAGVTGTASVVKMSYTDNNGKTIDGGLAVKVGDDYYSATQNKDGSISINTTKYTADDGTSKTALNKLGGADGKTEVVSIGGKTYAASKAEGHNFKAQPDLAEAAATTTENPLQKIDAALAQVDTLRSDLGAVQNRFNSAITNLGNTVNNLTSARSRIEDSDYATEVSNMSRAQILQQAGTSVLAQANQVPQNVLSLLR Disordered 1 55 AQVINTNSLSLLTQNNLNKSQSALGTAIERLSSGLRINSAKDDAAGQAIANRFTA Paper 2810365 Vonderviszt F, Kanto S, Aizawa S, Namba K 1989 J Mol Biol 209 1 127-33 Disordered 451 494 SRIEDSDYATEVSNMSRAQILQQAGTSVLAQANQVPQNVLSLLR Paper 2810365 Vonderviszt F, Kanto S, Aizawa S, Namba K 1989 J Mol Biol 209 1 127-33 Negative regulator of flagellin synthesis FLGM_SALTY Anti-sigma-28 factor FlgM P26477 FLGM_SALTY 120306 Salmonella typhimurium 97 MSIDRTSPLKPVSTVQTRETSDTPVQKTRQEKTSAATSASVTLSDAQAKLMQPGVSDINMERVEALKTAIRNGELKMDTGKIADSLIREAQSYLQSK Disordered 1 97 MSIDRTSPLKPVSTVQTRETSDTPVQKTRQEKTSAATSASVTLSDAQAKLMQPGVSDINMERVEALKTAIRNGELKMDTGKIADSLIREAQSYLQSK Paper 9095196 Daughdrill GW, Chadsey MS, Karlinsey JE, Hughes KT, Dahlquist FW 1997 Nat Struct Biol 4 4 285-91 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 Paper 9684899 Fletcher CM, Wagner G 1998 Protein Sci 7 7 1639-42 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 Eketjall S, Fainzilber M, Murray-Rust J, Ibanez 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 Eketjall S, Fainzilber M, Murray-Rust J, Ibanez 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 Far-UV circular dichroism (CD) 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 10693-10696 7878043 Dahlman-Wright K, Baumann H, McEwan IJ, Almlof T, Wright AP, Gustafsson JA, Hard 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 Far-UV circular dichroism (CD) 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 10693-10696 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 1 40 VDSVYRTRSLGVAAEGIPDQYADGEAARVWQLYIGDTRSR 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 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 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. Growth hormone receptor 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) 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 1111-1128 This region is likely stabilized upon binding of the second receptor to the growth hormone in the 1:2 complex (Clackson, 1998). 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 1111-1128 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 1111-1128 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 1111-1128 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 1111-1128 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 1111-1128 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 1111-1128 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 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 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 1111-1128 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 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 236 274 GGGSGGGSGGGSEGGGSEGGGSEGGGSEGGGSGGGSGSG 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 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) 353 GCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDAARADDARQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF Disordered 1 31 GCTLSAEDKAAVERSKMIDRNLREDGEKAAR Paper 8073283 Coleman DE, Berghuis AM, Lee E, Linder ME, Gilman AG, Sprang SR 1994 Science 265 5177 1405-12 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 L1 260 276 VQDVKSGSMLSNNDSRW Fragment 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 1806-1821 The fragment used for solution structure determination was the DNA-binding domain.(aa194-aa282) Disordered Omega loop 217 222 STSGES Fragment 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 1806-1821 The fragment used for solution structure determination was the DNA-binding domain.(aa194-aa282) Disordered 1 195 MGHNDSVETMDEISNPNNILLPHDGTGLDATGISGSQEPYGMVDVLNPDSLKDDSNVDEPLIEDIVNPSLDPEGVVSAEPSNEVGTPLLQQPISLDHVITRPASAGGVYSIGNSSTSSAAKLSDGDLTNATDPLLNNAHGHGQPSSESQSHSNGYHKQGQSQQPLLSLNKRKLLAKAHVDKHHSKKKLSTTRARP 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 Far-UV circular dichroism (CD) 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. Probable peroxiredoxin TDXH_AERPE EC 1.11.1.15 Q9Y9L0 TDXH_AERPE 14285795 Aeropyrum pernix 250 MPGSIPLIGERFPEMEVTTDHGVIKLPDHYVSQGKWFVLFSHPADFTPVCTTEFVSFARRYEDFQRLGVDLIGLSVDSVFSHIKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAESATHTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKALKLGDSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARMESGQYRCLDWWFCWDTPASRDDVEEARRYLRRAAEKPAKLLYEEARTHLH Disordered 235 243 EKPAKLLYE Monomeric 2CV4A 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 197 206 RARMESGQYR Monomeric 2CV4A 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 113 125 LGLLHAESATHTV Monomeric 2CV4A 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 104 107 DPQG Monomeric 2CV4A 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 2 8 PGSIPLI Monomeric 2CV4A 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 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 Far-UV circular dichroism (CD) Nuclear magnetic resonance (NMR) Infrared spectroscopy;Fourier transform infrared spectroscopy Paper 6273163 Cary PD, Crane-Robinson C, Bradbury EM, Dixon GH 1981 Eur J Biochem 119 3 545-551 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 Far-UV circular dichroism (CD) protein concentration 0.08 Nuclear magnetic resonance (NMR) Small-angle X-ray scattering wavelength: 0.8 nm Infrared spectroscopy;Fourier transform 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 1 173-177 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-protein binding Protein-DNA binding Nuclear magnetic resonance (NMR) Far-UV circular dichroism (CD) 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 Far-UV circular dichroism (CD) 2 Nuclear magnetic resonance (NMR) Paper 6273163 Cary, P. D. Crane-Robinson, C. Bradbury, E. M. Dixon, G. H. 1981 Eur J Biochem 119 3 545-551 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) 69 PKRKSATKGDEPARRSARLSARPVPKPAAKPKKAAAPKKAVKGKKAAENGDAKAEAKVQAAGDGAGNAK Disordered - Extended 1 69 PKRKSATKGDEPARRSARLSARPVPKPAAKPKKAAAPKKAVKGKKAAENGDAKAEAKVQAAGDGAGNAK Function arises via a disorder to order transition Molecular assembly Protein-DNA binding Far-UV circular dichroism (CD) Nuclear magnetic resonance (NMR) Paper 6273163 Cary PD, Crane-Robinson C, Bradbury EM, Dixon GH 1981 Eur J Biochem 119 3 545-551 Protein tonB TONB_ECOLI P02929 TONB_ECOLI 401196 Escherichia coli (strain K12) 239 MTLDLPRRFPWPTLLSVCIHGAVVAGLLYTSVHQVIELPAPAQPISVTMVTPADLEPPQAVQPPPEPVVEPEPEPEPIPEPPKEAPVVIEKPKPKPKPKPKPVKKVQEQPKRDVKPVESRPASPFENTAPARLTSSTATAATSKPVTSVASGPRALSRNQPQYPARAQALRIEGQVKVKFDVTPDGRVDNVQILSAKPANMFEREVKNAMRRWRYEPGKPGSGIVVNILFKINGTTEIQ Disordered 103 151 VKKVQEQPKRDVKPVESRPASPFENTAPARLTSSTATAATSKPVTSVAS Fragment Monomeric 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 1185-1197 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. 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 Far-UV circular dichroism (CD) 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 (Camb) 5 10 1361-1372 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 (Camb) 5 10 1361-1372 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 6 356-363 Ordered 71 147 TPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPGPGVRYPLTFGWCYKLVP 1AVVA Nuclear magnetic resonance (NMR) X-ray crystallography Paper 11406408 Arold ST, Baur AS 2001 Trends Biochem Sci 26 6 356-363 Ordered 179 203 EVLEWRFDSRLAFHHVARELHPEYF 1AVVA Nuclear magnetic resonance (NMR) X-ray crystallography Paper 11406408 Arold ST, Baur AS 2001 Trends Biochem Sci 26 6 356-363 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 6 356-363 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 (Camb) 5 10 1361-1372 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) Aberrant mobility on SDS-PAGE gel +/- Zn Paper 10606515 Berkovits, H. J. Berg, J. M. 1999 Biochemistry 38 51 16826-16830 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 Aberrant mobility on SDS-PAGE gel 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, H. G. Hoh, J. H. 1997 Biochemistry 36 49 15035-15040 9714161 Hoh, J. H. 1998 Protein Sci 32 2 223-228 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, S.H. 1991 Journal of Applied Crystallography 24 409-411 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, S.H. 1991 Journal of Applied Crystallography 24 409-411 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, S.H. 1991 Journal of Applied Crystallography 24 409-411 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, S.H. 1991 Journal of Applied Crystallography 24 409-411 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 Far-UV circular dichroism (CD) 293 Paper 3427055 Engel J, Taylor W, Paulsson M, Sage H, Hogan B 1987 Biochemistry 26 22 6958-6965 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 1 85 MLEEALAAIQNARDLEELKALKARYLGKKGLLTQEMKGLSALPLEERRKRGQELNAIKAALEAALEAREKALEEAALKEALERER 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 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, V. D. Misra, S. Boronenkov, I. V. Anderson, R. A. Hurley, J. H. 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, V. D. Misra, S. Boronenkov, I. V. Anderson, R. A. Hurley, J. H. 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 446 488 LPAGGENGSEATDVSDEVEAAEMEDEAVRSQVQHKPKEDKLKL Fragment X-ray crystallography Paper 8602259 Essen LO, Perisic O, Cheung R, Katan M, Williams RL 1996 Nature 380 6575 595-602 Disordered 502 517 VHFGGFSSPGTSGQAF Fragment X-ray crystallography Paper 8602259 Essen LO, Perisic O, Cheung R, Katan M, Williams RL 1996 Nature 380 6575 595-602 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 8602259 Essen LO, Perisic O, Cheung R, Katan M, Williams RL 1996 Nature 380 6575 595-602 8784353 Grobler JA, Essen LO, Williams RL, Hurley JH 1996 Nat Struct Biol 3 9 788-95 Sperm histone HSP1_CHICK Protamine Galline P15340 HSP1_CHICK 123705 Gallus gallus (Chicken) 62 MARYRRSRTRSRSPRSRRRRRRSGRRRSPRRRRRYGSARRSRRSVGGRRRRYGSRRRRRRRY Disordered 1 62 MARYRRSRTRSRSPRSRRRRRRSGRRRSPRRRRRYGSARRSRRSVGGRRRRYGSRRRRRRRY 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 Prothymosin alpha PTMA_RAT Thymosin alpha [cleavage chain 1] P06302 Rn.817 PTMA_RAT 135836 Rattus norvegicus (Rat) 112 MSDAAVDTSSEITTKDLKEKKEVVEEAENGRDAPANGNAQNEENGEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGDEDEEAEAPTGKRVAEDDEDDDVETKKQKKTDEDD Disordered 1 112 MSDAAVDTSSEITTKDLKEKKEVVEEAENGRDAPANGNAQNEENGEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGDEDEEAEAPTGKRVAEDDEDDDVETKKQKKTDEDD 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 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 Methylation X-ray crystallography 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 Function arises via a disorder to order transition Protein-DNA binding Methylation X-ray crystallography 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. 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 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 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 Paper 9108480 Tesmer JJ, Berman DM, Gilman AG, Sprang SR 1997 Cell 89 2 251-61 Disordered 179 205 NPSSCGAEKQKGAKSSADCTSLVPQCA 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 569 1123 VYKIGNYVWEDTNKNGVQELGEKGVGNVTVTVFDNNTNTKVGEAVTKEDGSYLIPNLPNGDYRVEFSNLPKGYEVTPSKQGNNEELDSNGLSSVITVNGKDNLSADLGIYKPKYNLGDYVWEDTNKNGIQDQDEKGISGVTVTLKDENGNVLKTVTTDADGKYKFTDLDNGNYKVEFTTPEGYTPTTVTSGSDIEKDSNGLTTTGVINGADNMTLDSGFYKTPKYNLGNYVWEDTNKDGKQDSTEKGISGVTVTLKNENGEVLQTTKTDKDGKYQFTGLENGTYKVEFETPSGYTPTQVGSGTDEGIDSNGTSTTGVIKDKDNDTIDSGFYKPTYNLGDYVWEDTNKNGVQDKDEKGISGVTVTLKDENDKVLKTVTTDENGKYQFTDLNNGTYKVEFETPSGYTPTSVTSGNDTEKDSNGLTTTGVIKDADNMTLDSGFYKTPKYSLGDYVWYDSNKDGKQDSTEKGIKDVKVTLLNEKGEVIGTTKTDENGKYCFDNLDSGKYKVIFEKPAGLTQTGTNTTEDDKDADGGEVDVTITDHDDFTLDNGYYEEET Paper 9813018 Josefsson E, O'Connell D, Foster TJ, Durussel I, Cox JA 1998 J Biol Chem 273 47 31145-52 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) 264 MNRGFFNMLGRRPFPAPTAMWRPRRRRQAAPMPARNGLASQIQQLTTAVSALVIGQATRPQNPRPRPPPRQKKQAPKQPPKPKKPKPQEKKKKQPAKTKPGKRQRMALKLEADRLFDVKNEDGDVIGHALAMEGKVMKPLHVKGTIDHPVLSKLKFTKSSAYDMEFAQLPVNMRSEAFTYTSEHPEGFYNWHHGAVQYSGGRFTIPRGVGGRGDSGRPIMDNSGRVVAIVLGGADEGTRTALSVVTWNSKGKTIKTTPEGTEEW Disordered 1 106 MNRGFFNMLGRRPFPAPTAMWRPRRRRQAAPMPARNGLASQIQQLTTAVSALVIGQATRPQNPRPRPPPRQKKQAPKQPPKPKKPKPQEKKKKQPAKTKPGKRQRM Paper 1944569 Choi HK, Tong L, Minor W, Dumas P, Boege U, Rossmann MG, Wengler G 1991 Nature 354 6348 37-43 This sequence is post processing Small heat shock protein HSP16.5 HSPS_METJA Q57733 HSPS_METJA 2495337 Methanocaldococcus jannaschii (Methanococcus jannaschii) 147 MFGRDPFDSLFERMFKEFFATPMTGTTMIQSSTGIQISGKGFMPISIIEGDQHIKVIAWLPGVNKEDIILNAVGDTLEIRAKRSPLMITESERIIYSEIPEEEEIYRTIKLPATVKEENASAKFENGVLSVILPKAESSIKKGINIE Disordered 1 32 MFGRDPFDSLFERMFKEFFATPMTGTTMIQSS Paper 9707123 Kim KK, Kim R, Kim SH 1998 Nature 394 6693 595-9 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 Far-UV circular dichroism (CD) 277 7.4 phosphate buffer 10 NaCl salt 100 Nuclear magnetic resonance (NMR) Sensitivity to proteolysis 298 chymotrypsin NaCl salt 100 proteinase K trypsin Gel filtration/size exclusion chromatography 368 6.8 betamercaptoethanol buffer 3 glycerol buffer 10 SDS buffer 2 Tris buffer 60 Gel filtration/size exclusion chromatography 298 6.8 betamercaptoethanol buffer 3 glycerol buffer 10 SDS buffer 2 Tris buffer 60 Paper 9671503 Fasshauer, D. Eliason, W. K. Brunger, A. T. Jahn, R. 1998 Biochemistry 37 29 10354-10362 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 Far-UV circular dichroism (CD) 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 28036-28041 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 Far-UV circular dichroism (CD) 298 7.4 NaCl salt 100 sodium phosphate 10 Experimental 9852083 Canaves JM, Montal M 1998 J Biol Chem 273 51 34214-34221 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 Far-UV circular dichroism (CD) 7.5 Tris buffer 10 Infrared spectroscopy;Fourier transform 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 8901511 Weinreb, P. H. Zhen, W. Poon, A. W. Conway, K. A. Lansbury, P. T., Jr. 1996 Biochemistry 35 43 13709-13715 11312271 Nielsen, M. S. Vorum, H. Lindersson, E. Jensen, P. H. 2001 J Biol Chem 276 25 22680-22684 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 1 166 MSMSPKHTTPFSVSDILSPLEESYKKVGMEGGGLGAPLAAYRQGQAAPPAAAMQQHAVGHHGAVTAAYHMTAAGVPQLSHSAVGGYCNGNLGNMSELPPYQDTMRNSASGPGWYGANPDPRFPAISRFMGPASGMNMSGMGGLGSLGDVSKNMAPLPSAPRRKRRV Far-UV circular dichroism (CD) 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 217 226 KRQAKDKAAQ Far-UV circular dichroism (CD) 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 Function arises via a disorder to order transition Far-UV circular dichroism (CD) 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 Estrogen receptor [Isoform long] ESR1_HUMAN ER Estradiol receptor Estrogen receptor alpha ER-alpha Nuclear receptor subfamily 3 group A member 1 P03372-1 Hs.208124 ESR1_HUMAN 544257 Homo sapiens (Human) 595 MTMTLHTKASGMALLHQIQGNELEPLNRPQLKIPLERPLGEVYLDSSKPAVYNYPEGAAYEFNAAAAANAQVYGQTGLPYGPGSEAAAFGSNGLGGFPPLNSVSPSPLMLLHPPPQLSPFLQPHGQQVPYYLENEPSGYTVREAGPPAFYRPNSDNRRQGGRERLASTNDKGSMAMESAKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGRMLKHKRQRDDGEGRGEVGSAGDMRAANLWPSPLMIKRSKKNSLALSLTADQMVSALLDAEPPILYSEYDPTRPFSEASMMGLLTNLADRELVHMINWAKRVPGFVDLTLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHQRLAQLLLILSHIRHMSNKGMEHLYSMKCKNVVPLYDLLLEMLDAHRLHAPTSRGGASVEETDQSHLATAGSTSSHSLQKYYITGEAEGFPATV Disordered 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 Far-UV circular dichroism (CD) 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-protein binding Protein-DNA 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 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 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 175 214 KPKNKDKDKKVPEPDNKKKKPKKEEEQKWKWWEEERYPEG Complex Engineered Fragment 1A31A 1A35A X-ray crystallography Paper 8567649 Bharti AK, Olson MO, Kufe DW, Rubin EH 1996 J Biol Chem 271 4 1993-1997 14654701 Christensen MO, Barthelmes HU, Boege F, Mielke C 2003 Nucleic Acids Res 31 24 7255-7263 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 Disordered - Extended 1 174 MSGDHLHNDSQIEADFRLNDSHKHKDKHKDREHRHKEHKKEKDREKSKHSNSEHKDSEKKHKEKEKTKHKDGSSEKHKDKHKDRDKEKRKEEKVRASGDAKIKKEKENGFSSPPQIKDEPEDDGYFVPPKEDIKPLKRPRDEDDADYKPKKIKTEDTKKEKKRKLEEEEDGKLK Function arises from the ordered state Molecular assembly Nuclear localization Autoregulatory Protein-protein binding Disordered region is not essential for protein function Far-UV circular dichroism (CD) 310 KPO₄ (pH 7.4) 10 Gel filtration/size exclusion chromatography 298 DTT 1 EDTA 1 KPO₄ (pH 7.4) 200 Paper 8567649 Bharti AK, Olson MO, Kufe DW, Rubin EH 1996 J Biol Chem 271 4 1993-1997 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 1 197 MSGDHLHNDSQIEADFRLNDSHKHKDKHKDREHRHKEHKKEKDREKSKHSNSEHKDSEKKHKEKEKTKHKDGSSEKHKDKHKDRDKEKRKEEKVRASGDAKIKKEKENGFSSPPQIKDEPEDDGYFVPPKEDIKPLKRPRDEDDADYKPKKIKTEDTKKEKKRKLEEEEDGKLKKPKNKDKDKKVPEPDNKKKKPKK