60S acidic ribosomal protein P1-B CaRP1B Q9HFQ6 Candida albicans 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 L12EIA L45 YL44C YPA1 P02400 133071 A35109 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 Adenovirus ssDNA binding protein Early E2A DNA-binding protein P03265 P03265 118736 W7AD25 Human adenovirus type 5 529 MASREEEQRETTPERGRGAARRPPTMEDVSSPSPSPPPPRAPPKKRMRRRIESEDEEDSSQDALVPRTPSPRPSTSAADLAIAPKKKKKRPSPKPERPPSPEVIVDSEEEREDVALQMVGFSNPPVLIKHGKGGKRTVRRLNEDDPVARGMRTQEEEEEPSEAESEITVMNPLSVPIVSAWEKGMEAARALMDKYHVDNDLKANFKLLPDQVEALAAVCKTWLNEEHRGLQLTFTSNKTFVTMMGRFLQAYLQSFAEVTYKHHEPTGCALWLHRCAEIEGELKCLHGSIMINKEHVIEMDVTSENGQRALKEQSSKAKIVKNRWGRNVVQISNTDARCCVHDAACPANQFSGKSCGMFFSEGAKAQVAFKQIKAFMQALYPNAQTGHGHLLMPLRCECNSKPGHAPFLGRQLPKLTPFALSNAEDLDADLISDKSVLASVHHPALIVFQCCNPVYRNSRAQGGGPNCDFKISAPDLLNALVMVRSLWSENFTELPRMVVPEFKWSTKHQYRNVSLPVAHSDARQNPFDF 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 8039495 Tucker, P., Tsernoglou, D., Tucker, A., Coenjaerts, F., Leenders, H., Vliet, P. 1994 13 13 2994-3002 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 4040872 Tsernoglou, D. Tsugita, A. Tucker, A. D. van der Vliet, P. C. 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. 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 8039495 Tucker, P., Tsernoglou, D., Tucker, A., Coenjaerts, F., Leenders, H., Vliet, P. 1994 13 13 2994-3002 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 4040872 Tsernoglou, D. Tsugita, A. Tucker, A. D. van der Vliet, P. C. 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. 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 8039495 Tucker, P., Tsernoglou, D., Tucker, A., Coenjaerts, F., Leenders, H., Vliet, P. 1994 13 13 2994-3002 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 4040872 Tsernoglou, D. Tsugita, A. Tucker, A. D. van der Vliet, P. C. 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 174 296 SVPIVSAWEKGMEAARALMDKYHVDNDLKANFKLLPDQVEALAAVCKTWLNEEHRGLQLTFTSNKTFVTMMGRFLQAYLQSFAEVTYKHHEPTGCALWLHRCAEIEGELKCLHGSIMINKEHV 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, A. D. van der Vliet, P. C. 1985 FEBS Lett 188 2 248-52 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, A. D. van der Vliet, P. C. 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, A. D. van der Vliet, P. C. 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, A. D. van der Vliet, P. C. 1985 FEBS Lett 188 2 248-52 Antibacterial protein FALL-39 precursor Antibacterial protein LL-37 Antimicrobial protein CAP-18 CAP18 precursor FALL-39 peptide antibiotic hCAP-18 LL-37 P49913 P49913 1706745 I38932 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 magnesium sulfate salt 84 sodium chloride salt 160 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 Antitermination protein N of bacteriophage lambda Nucleocapsid protein PN Regulatory protein N P03045 P03045 132276 P03045 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 Apocytochrome c P00004 117995 A00005 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 APE nuclease APEX nuclease Apurinic/apyrimidinic endonuclease HAP1 Major apurinic/apyrimidinic endonuclease Ref-1 P27695 Hs.73722 P27695 18375505 S23550 Homo sapiens (Human) 318 MPKRGKKGAVAEDGDELRTEPEAKKSKTAAKKNDKEAAGEGPALYEDPPDQKTSPSGKPATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQELPGLSHQYWSAPSDKEGYSGVGLLSRQCPLKVSYGIGDEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQRWDEAFRKFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLPALCDSKIRSKALGSDHCPITLYLAL Disordered - Extended 1 43 MPKRGKKGAVAEDGDELRTEPEAKKSKTAAKKNDKEAAGEGPA Complex Native 1HD7A Relationship to function unknown Unknown Disordered region is not essential for protein function 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 - 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. Disordered - Extended 102 112 NKLPAELQELP 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 - 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) 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 B-cell-specific coactivator BOB.1/OBF.1 B cell-specific transcription co-activator BOB-1 OCA-B OCT binding factor 1 Q64693 1150493 S63588 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 chain TFIIA 13.5 kDa subunit TOA2 P32774 418109 Saccharomyces cerevisiae (Baker's yeast) 122 MAVPGYYELYRRSTIGNSLVDALDTLISDGRIEASLAMRVLETFDKVVAETLKDNTQSKLTVKGNLDTYGFCDDVWTFIVKNCQVTVEDSHRDASQNGSGDSQSVISVDKLRIVACNSKKSE Disordered 89 103 DSHRDASQNGSGDSQ Complex Molecular assembly Protein-protein binding Transactivation (transcriptional activation) X-ray crystallography 103 Paper 8610010 Tan S, Hunziker Y, Sargent DF, Richmond TJ 1996 Nature 381 6578 127-51 Alpha-S1 casein [Precursor] P02662 1070620 KABOSB Bos taurus (Bovine) 214 MKLLILTCLVAVALARPKHPIKHQGLPQEVLNENLLRFFVAPFPEVFGKEKVNELSKDIGSESTEDQAMEDIKQMEAESISSSEEIVPNSVEQKHIQKEDVPSERYLGYLEQLLRLKKYKVPQLEIVPNSAEERLHSMKEGIHAQQKEPMIGVNQELAYFYPELFRQFYQLDAYPSGAWYYVPLGTQYTDAPSFSDIPNPIGSENSEKTTMPLW Disordered 16 214 RPKHPIKHQGLPQEVLNENLLRFFVAPFPEVFGKEKVNELSKDIGSESTEDQAMEDIKQMEAESISSSEEIVPNSVEQKHIQKEDVPSERYLGYLEQLLRLKKYKVPQLEIVPNSAEERLHSMKEGIHAQQKEPMIGVNQELAYFYPELFRQFYQLDAYPSGAWYYVPLGTQYTDAPSFSDIPNPIGSENSEKTTMPLW Paper 10336443 Bhattacharyya J, Das KP 1999 J Biol Chem 274 22 15505-9 Monoamine-sulfating phenol sulfotransferase Catecholamine sulfotransferase EC 2.8.2.1 HAST3 M-PST Placental estrogen sulfotransferase Sulfotransferase, monoamine-preferring Thermolabile phenol sulfotransferase TL-PST P50224 Hs.458369 P50224 10835035 A55451 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 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 1 7 MELIQDT 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 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 cAMP-dependent chloride channel CFTR Cystic fibrosis transmembrane conductance regulator, ATP-binding cassette P13569 1705762 DVHUCF 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. Choriogonadotropin beta chain [Precursor] CG-beta Chorionic gonadotropin beta subunit Hcg Human chorionic gonadotropin P01233 116184 KTHUB 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. Clusterin [Precursor] DAG Dimeric acid glycoprotein SGP-2 Sulfated glycoprotein 2 Testosterone repressed prostate message-2 TRPM-2 P05371 461756 A27205 Rattus norvegicus (Rat) 447 MKILLLCVALLLTWDNGMVLGEQEFSDNELQELSTQGSRYVNKEIQNAVQGVKHIKTLIEKTNAERKSLLNSLEEAKKKKEGALDDTRDSEMKLKAFPEVCNETMMALWEECKPCLKHTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRIDSLLESDRQQSQVLDAMQDSFTRASGIIDTLFQDRFFTHEPQDIHHFSPMGFPHKRPHFLYPKSRLVRSLMPLSHYGPLSFHNMFQPFFDMIHQAQQAMDVQLHSPALQFPDVDFLKEGEDDPTVCKEIRHNSTGCLKMKGQCEKCQEILSVDCSTNNPAQANLRQELNDSLQVAERLTQQYNELLHSLQSKMLNTSSLLEQLNDQFTWVSQLANLTQGDDQYLRVSTVTTHSSDSEVPSRVTEVVVKLFDSDPITVVLPEEVSKDNPKFMDTVAEKALQEYRRKSRME Disordered 66 97 RKSLLNSLEEAKKKKEGALDDTRDSEMKLKAF Paper 14769047 Barghorn S, Davies P, Mandelkow E 2004 Biochemistry 43 6 1694-1703 Disordered 386 445 TVTTHSSDSEVPSRVTEVVVKLFDSDPITVVLPEEVSKDNPKFMDTVAEKALQEYRRKSR Paper 11570883 Bailey RW, Dunker AK, Brown CJ, Garner EC, Griswold MD 2001 Biochemistry 40 39 11828-40 PIR has a mismatch at amino acid 187. cAMP-dependent protein kinase inhibitor, alpha form cAMP-dependent protein kinase inhibitor cAMP-dependent protein kinase inhibitor, muscle/brain isoform PKI-alpha P04541 48428970 A01340 Homo sapiens (Human) 75 TDVETTYADFIASGRTGRRNAIHDILVSSASGNSNELALKLAGLDINKTEGEEDAQRSSTEQSGEAQGEAAKSES Disordered 1 75 TDVETTYADFIASGRTGRRNAIHDILVSSASGNSNELALKLAGLDINKTEGEEDAQRSSTEQSGEAQGEAAKSES 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 7922031 Wu H, Lustbader JW, Liu Y, Canfield RE, Hendrickson WA 1994 Structure 2 6 545-58 Cyclin-dependent kinase inhibitor 1 CDK-interacting protein 1 Cyclin-dependent kinase inhibitor p21 MDA-6 Melanoma differentiation associated protein 6 p21 P38936 Hs.370771 P38936 2134956 I68674 Homo sapiens 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 Cyclin-dependent kinase inhibitor p57 p57KIP2 P49918 Hs.106070 P49918 4557441 G02424 Homo sapiens 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 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 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 Cyclin-dependent kinase inhibitor p27 p27Kip1 P46527 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 Ubiquinol-cytochrome c reductase iron-sulfur subunit, mitochondrial [Precursor] Cytochrome Bc1 Complex Ubiquinol Cytochrome C Oxidoreductase, Complex III P13272 1351360 A34660 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 Repressor/activator site binding protein SBF-E TUF P11938 730473 S50714 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 Elongation Factor G Without Nucleotide P13551 1827912 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 Embryonic abundant protein from carrot P17639 119316 JQ2273 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 17-beta-HSD 1 20-alpha-HSD 20 alpha-hydroxysteroid dehydrogenase E2DH EC 1.1.1.62 Placental 17-beta-hydroxysteroid dehydrogenase P14061 Hs.448861 P14061 4504501 DEHUE7 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&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 Molecular recognition effectors Unknown 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 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 experimental sequence used for PDB ID 1FDV contained a H221L substitution. The 1FDU PDB file gives this protein fragment as complexed with Estradiol and NADP+ and has the mutation H221L. The experimental sequence used for the PDB ID 1FDU contained a H221L substitution. 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. 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 191 198 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. 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. E7 protein E7 protein from HPV16 P03129 6469700 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 [Precursor] Fibronectin binding protein FNBP P14738 120457 Staphylococcus aureus 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 Phase-1-I flagellin P06179 96744 S16121 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 Anti-sigma-28 factor Flagellum specific sigma factor P26477 120306 A41046 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 4E-binding protein 1 4E-BP1 eIF4E-binding protein 1 PHAS-I Phosphorylated heat- and acid-stable protein regulated by insulin 1 Q13541 4758258 S50866 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 Glial cell line-derived neurotrophic factor [Precursor] Q07731 Q07731 729568 A37499 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 benzamidine 0.1 HEPES pH 7.0 50 LiCl 0.8 PEG 6000 20 soduim azide 0.02 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 GR P04150 Hs.126608 P04150 66528611 QRHUGA Homo sapiens (Human) 777 MDSKESLTPGREENPSSVLAQERGDVMDFYKTLRGGATVKVSASSPSLAVASQSDSKQRRLLVDFPKGSVSNAQQPDLSKAVSLSMGLYMGETETKVMGNDLGFPQQGQISLSSGETDLKLLEESIANLNRSTSVPENPKSSASTAVSAAPTEKEFPKTHSDVSSEQQHLKGQTGTNGGNVKLYTTDQSTFDILQDLEFSSGSPGKETNESPWRSDLLIDENCLLSPLAGEDDSFLLEGNSNEDCKPLILPDTKPKIKDNGDLVLSSPSNVTLPQVKTEKEDFIELCTPGVIKQEKLGTVYCQASFPGANIIGNKMSAISVHGVSTSGGQMYHYDMNTASLSQQQDQKPIFNVIPPIPVGSENWNRCQGSGDDNLTSLGTLNFPGRTVFSNGYSSPSMRPDVSSPPSSSSTATTGPPPKLCLVCSDEASGCHYGVLTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRYRKCLQAGMNLEARKTKKKIKGIQQATTGVSQETSENPGNKTIVPATLPQLTPTLVSLLEVIEPEVLYAGYDSSVPDSTWRIMTTLNMLGGRQVIAAVKWAKAIPGFRNLHLDDQMTLLQYSWMFLMAFALGWRSYRQSSANLLCFAPDLIINEQRMTLPCMYDQCKHMLYVSSELHRLQVSYEEYLCMKTLLLLSSVPKDGLKSQELFDEIRMTYIKELGKAIVKREGNSSQNWQRFYQLTKLLDSMHEVVENLLNYCFQTFLDKTMSIEFPEMLAEIITNQIPKYSNGNIKKLLFHQK Disordered - Extended 77 262 DLSKAVSLSMGLYMGETETKVMGNDLGFPQQGQISLSSGETDLKLLEESIANLNRSTSVPENPKSSASTAVSAAPTEKEFPKTHSDVSSEQQHLKGQTGTNGGNVKLYTTDQSTFDILQDLEFSSGSPGKETNESPWRSDLLIDENCLLSPLAGEDDSFLLEGNSNEDCKPLILPDTKPKIKDNGD Engineered 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 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, T. D 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 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 Folate-binding protein P13255 121328 S00112 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 Human growth hormone binding protein hGHbp Human growth hormone receptor binding domain Human growth hormone receptor extracellular domain P10912 Hs.125180 P10912 4503993 A33991 Homo sapiens (Human) 246 FSGSEATAAILSRAPWSLQSVNPGLKTNSSKEPKFTKCRSPERETFSCHWTDEVHHGTKNLGPIQLFYTRRNTQEWTQEWKECPDYVSAGENSCYFNSSFTSIWIPYCIKLTSNGGTVDEKCFSVDEIVQPDPPIALNWTLLNVSLTGIHADIQVRWEAPRNADIQKGWMVLEYELQYKEVNETKWKMMDPILTTSVPVYSLKVDKEYEVRVRSKQRNSGNYGEFSEVLYVTLPQMSQFTCEEDFY 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 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 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. Coat protein A [Precursor] G3P g3p (fd phage minor coat protein) P03661 116658 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 Gia1 G protein Gi Alpha 1 P10824 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 Heat shock transcription factor HSF HSTF P22121 123686 S13365 Kluyveromyces lactis (Yeast) 677 MGHNDSVETMDEISNPNNILLPHDGTGLDATGISGSQEPYGMVDVLNPDSLKDDSNVDEPLIEDIVNPSLDPEGVVSAEPSNEVGTPLLQQPISLDHVITRPASAGGVYSIGNSSTSSAAKLSDGDLTNATDPLLNNAHGHGQPSSESQSHSNGYHKQGQSQQPLLSLNKRKLLAKAHVDKHHSKKKLSTTRARPAFVNKLWSMVNDKSNEKFIHWSTSGESIVVPNRERFVQEVLPKYFKHSNFASFVRQLNMYGWHKVQDVKSGSMLSNNDSRWEFENENFKRGKEYLLENIVRQKSNTNILGGTTNAEVDIHILLNELETVKYNQLAIAEDLKRITKDNEMLWKENMMARERHQSQQQVLEKLLRFLSSVFGPNSAKTIGNGFQPDLIHELSDMQVNHMSNNNHNNTGNINPNAYHNETDDPMANVFGPLTPTDQGKVPLQDYKLRPRLLLKNRSMSSSSSSNLNQRQSPQNRIVGQSPPPQQQQQQQQQQGQPQGQQFSYPIQGGNQMMNQLGSPIGTQVGSPVGSQYGNQYGNQYSNQFGNQLQQQTSRPALHHGSNGEIRELTPSIVSSDSPDPAFFQDLQNNIDKQEESIQEIQDWITKLNPGPGEDGNTPIFPELNMPSYFANTGGSGQSEQPSDYGDSQIEELRNSRLHEPDRSFEEKNNGQKRRRAA 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 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 L1 260 276 VQDVKSGSMLSNNDSRW Fragment Protein-DNA binding Transactivation (transcriptional activation) 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 268 271 MLSN Fragment Protein-DNA binding Transactivation (transcriptional activation) 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) In the Damberger and Harrison papers the sequences listed are one residue off from the referenced sequence. Regions 2 & 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. Peroxiredoxin EC 1.11.1.15 Q9Y9L0 14285795 Aeropyrum pernix 250 MPGSIPLIGERFPEMEVTTDHGVIKLPDHYVSQGKWFVLFSHPADFTPVCTTEFVSFARRYEDFQRLGVDLIGLSVDSVFSHIKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAESATHTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKALKLGDSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARMESGQYRCLDWWFCWDTPASRDDVEEARRYLRRAAEKPAKLLYEEARTHLH Disordered 2 8 PGSIPLI 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 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 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 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 Nonhistone chromosomal protein HMG-14 High-mobility group nucleosome binding domain 1 P02316 P02316 123099 NSBOH4 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 assembly Molecular recognition effectors Acetylation Phosphorylation Protein-DNA binding Protein-protein binding Far-UV circular dichroism (CD) Nuclear magnetic resonance (NMR) Infrared spectroscopy Paper 6273163 Cary PD, Crane-Robinson C, Bradbury EM, Dixon GH 1981 Eur J Biochem 119 3 545-551 Nonhistone chromosomal protein HMG-17 High mobility group - 17 High-mobility group (nonhistone chromosomal) protein 17 High-mobility group nucleosomal binding domain 2 High mobility group protein N2 Bt.1758 P05204 5031749 S03700 Homo sapiens (Human) 89 PKRKAEGDAKGDKAKVKDEPQRRSARLSAKPAPPKPEPKPKKAPAKKGEKVPKGKKGKADAGKEGNNPAENGDAKTDQAQKAEGAGDAK Disordered - Extended 1 89 PKRKAEGDAKGDKAKVKDEPQRRSARLSAKPAPPKPEPKPKKAPAKKGEKVPKGKKGKADAGKEGNNPAENGDAKTDQAQKAEGAGDAK Native Function arises via a disorder to order transition Molecular assembly Molecular recognition effectors Acetylation Phosphorylation Protein-DNA binding Protein-protein binding Far-UV circular dichroism (CD) protien concentration 0.08 Nuclear magnetic resonance (NMR) Small-angle X-ray scattering wavelength: 0.8 nm Infrared spectroscopy 6.8 NaCl salt 1 protien 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 High mobility group - I(Y) HMG-I(Y) P17096 P17096 123377 A32794 Homo sapiens (Human) 107 MSESSSKSSQPLASKQEKDGTEKRGRGRPRKQPPVSPGTALVGSQKEPSEVPTPKRPRGRPKGSKNKGAAKTRKTTTTPGRKPRGRPKKLEKEEEEGISQESSEEEQ Disordered - Extended 1 107 MSESSSKSSQPLASKQEKDGTEKRGRGRPRKQPPVSPGTALVGSQKEPSEVPTPKRPRGRPKGSKNKGAAKTRKTTTTPGRKPRGRPKKLEKEEEEGISQESSEEEQ 2EZDA 2EZEA 2EZFA 2EZGA Function arises from the disordered state Function arises via a disorder to order transition Molecular assembly Protein-DNA binding Protein-protein binding Nuclear magnetic resonance (NMR) Paper 7559428 Wang, D. Z. Ray, P. Boothby, M. 1995 J Biol Chem 270 39 22924-22932 11593421 Pierantoni, G. M. Fedele, M. Pentimalli, F. Benvenuto, G. Pero, R. Viglietto, G. Santoro, M. Chiariotti, L. Fusco, A. 2001 Oncogene 20 43 6132-6141 11498590 Munshi, N. Agalioti, T. Lomvardas, S. Merika, M. Chen, G. Thanos, D. 2001 Science 293 5532 1133-1136 10372360 Reeves, R. Nissen, M. S. 1996 Methods of Enzymology 304 155-188 High mobility group-T protein HMG-T HMG-T1 P07746 Omy.4110 P07746 123382 T01071 Oncorhynchus mykiss (Rainbow trout) 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 Nonhistone chromosomal protein H6 High mobility group - H6 Histone T P02315 462245 Oncorhynchus mykiss (Rainbow trout) 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 TonB P02929 1742041 Escherichia coli 239 MTLDLPRRFPWPTLLSVCIHGAVVAGLLYTSVHQVIELPAPAQPISVTMVTPADLEPPQAVQPPPEPVVEPEPEPEPIPEPPKEAPVVIEKPKPKPKPKPKPVKKVQEQPKRDVKPVESRPASPFENTAPARLTSSTATAATSKPVTSVASGPRALSRNQPQYPARAQALRIEGQVKVKFDVTPDGRVDNVQILSAKPANMFEREVKNAMRRWRYEPGKPGSGIVVNILFKINGTTEIQ Disordered 103 151 VKKVQEQPKRDVKPVESRPASPFENTAPARLTSSTATAATSKPVTSVAS Fragment Monomeric Metal binding Protein-protein binding Nuclear magnetic resonance (NMR) 298 7 NaCl 100 Tris 50 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 Gga.8460 P02259 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 Guanine phosphoribosyltransferase HGPRTase HPRT Hypoxanthine Phosphoribosyltransferase IMP diphosphorylase IMP pyrophosphorylase Transphosphoribosidase Q27796 Q27796 386724 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 Q9QXN1 Q9QXN1 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, J. J. Li, X. Case, D. A. Giese, K. Grosschedl, R. Wright, P. E. 1995 Nature 376 6543 791-795 Myelin basic protein 20 kDa microtubule stabilizing protein MBP Myelin A1 protein Bt.6405 P02687 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 Nef protein 27 kDa protein 3'ORF F-protein Negative factor, HIV1 Q71VG3 P03406 128023 Human immunodeficiency virus type 1 (BRU isolate) (HIV-1) 206 MGGKWSKSSVVGWPTVRERMRRAEPAADGVGAASRDLEKHGAITSSNTAATNAACAWLEAQEEEEVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPGPGVRYPLTFGWCYKLVPVEPDKVEEANKGENTSLLHPVSLHGMDDPEREVLEWRFDSRLAFHHVARELHPEYFKNC Disordered - Extended 1 73 MGGKWSKSSVVGWPTVRERMRRAEPAADGVGAASRDLEKHGAITSSNTAATNAACAWLEAQEEEEVGFPVTPQ 1AVVA 1AVZA 1EFNA 1QA4A Function arises from the disordered state Function arises via a disorder to order transition Fatty acylation (myristolation and palmitoylation) Flexible linkers/spacers Phosphorylation Protein-lipid interaction Protein-protein binding Regulation of proteolysis in vivo Nuclear magnetic resonance (NMR) X-ray crystallography Paper 9351809 Arold, S. Franken, P. Strub, M. P. 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 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, M. P. 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, M. P. 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 1 70 MGGKWSKSSVVGWPTVRERMRRAEPAADGVGAASRDLEKHGAITSSNTAATNAACAWLEAQEEEEVGFPV 1AVVA 1AVZA 1EFNA 1QA4A Function arises from the disordered state Function arises via a disorder to order transition Fatty acylation (myristolation and palmitoylation) Flexible linkers/spacers Phosphorylation Protein-lipid interaction Protein-protein binding Regulation of proteolysis in vivo Nuclear magnetic resonance (NMR) X-ray crystallography Paper 11406408 Arold ST, Baur AS 2001 Trends Biochem Sci 26 6 356-363 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 Neural zinc finger factor-1 NZF-1 Rn.10559 P70475 1511632 T46637 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 triplet H protein 200 kDa neurofilament protein Neurofilament H Neurofilament heavy polypeptide NF-H Mm.298283 P19246 128127 QFMSH Mus musculus (Mouse) 1087 MSFGSADALLGAPFAPLHGGGSLHYSLSRKAGPGGTRSAAGSSSGFHSWARTSVSSVSASPSRFRGAASSTDSLDTLSNGPEGCVVAAVAARSEKEQLQALNDRFAGYIDKVRQLEAHNRSLEGEAAALRQQKGRAAMGELYEREVREMRGAVLRLGAARGQLRLEQEHLLEDIAHVRQRLDEEARQREEAEAAARALAFAQEAEAARVELQKKAQALQEECGYLRRHHQEEVGELLGQIQGCGAAQAQAQAEARDALKCDVTSALREIRAQLEGHAVQSSLQSEEWFRVRLDRLSEAAKVNTDAMRSAQEEITEYRRQLQARTTELEALKSTKESLERQRSELEDRHQADIASYQDAIQQLDSELRNTKWEMAAQLREYQDLLNVKMALDIEIAAYRKLLEGEECRIGFGPSPFSLTEGLPKIPSISTHIKVKSEEMIKVVEKSEKETVIVEGQTEEIRVTEGVTEEEDKEAQGQEGEEAEEGEEKEEEELAAATSPPAEEAASPEKETKSRVKEEAKSPGEAKSPGEAKSPAEAKSPGEAKSPGEAKSPGEAKSPAEPKSPAEPKSPAEAKSPAEPKSPATVKSPGEAKSPSEAKSPAEAKSPAEAKSPAEAKSPAEAKSPAEAKSPAEAKSPATVKSPGEAKSPSEAKSPAEAKSPAEAKSPAEAKSPAEVKSPGEAKSPAEPKSPAEAKSPAEVKSPAEAKSPAEVKSPGEAKSPAAVKSPAEAKSPAAVKSPGEAKSPGEAKSPAEAKSPAEAKSPIEVKSPEKAKTPVKEGAKSPAEAKSPEKAKSPVKEDIKPPAEAKSPEKAKSPVKEGAKPPEKAKPLDVKSPEAQTPVQEEATVPTDIRPPEQVKSPAKEKAKSPEKEEAKTSEKVAPKKEEVKSPVKEEVKAKEPPKKVEEEKTLPTPKTEAKESKKDEAPKEAPKPKVEEKKETPTEKPKDSTAEAKKEEAGEKKKAVASEEETPAKLGVKEEAKPKEKTETTKTEAEDTKAKEPSKPTETEKPKKEEMPAAPEKKDTKEEKTTESRKPEEKPKMEAKVKEDDKSLSKEPSKPKTEKAEKSSSTDQKESQPPEKTTEDKATKGEK Disordered 409 1087 GFGPSPFSLTEGLPKIPSISTHIKVKSEEMIKVVEKSEKETVIVEGQTEEIRVTEGVTEEEDKEAQGQEGEEAEEGEEKEEEELAAATSPPAEEAASPEKETKSRVKEEAKSPGEAKSPGEAKSPAEAKSPGEAKSPGEAKSPGEAKSPAEPKSPAEPKSPAEAKSPAEPKSPATVKSPGEAKSPSEAKSPAEAKSPAEAKSPAEAKSPAEAKSPAEAKSPAEAKSPATVKSPGEAKSPSEAKSPAEAKSPAEAKSPAEAKSPAEVKSPGEAKSPAEPKSPAEAKSPAEVKSPAEAKSPAEVKSPGEAKSPAAVKSPAEAKSPAAVKSPGEAKSPGEAKSPAEAKSPAEAKSPIEVKSPEKAKTPVKEGAKSPAEAKSPEKAKSPVKEDIKPPAEAKSPEKAKSPVKEGAKPPEKAKPLDVKSPEAQTPVQEEATVPTDIRPPEQVKSPAKEKAKSPEKEEAKTSEKVAPKKEEVKSPVKEEVKAKEPPKKVEEEKTLPTPKTEAKESKKDEAPKEAPKPKVEEKKETPTEKPKDSTAEAKKEEAGEKKKAVASEEETPAKLGVKEEAKPKEKTETTKTEAEDTKAKEPSKPTETEKPKKEEMPAAPEKKDTKEEKTTESRKPEEKPKMEAKVKEDDKSLSKEPSKPKTEKAEKSSSTDQKESQPPEKTTEDKATKGEK Aberrant mobility on SDS-PAGE gel Sensitivity to proteolysis Paper 9424114 Brown, H. G. Hoh, J. H. 1997 Biochemistry 36 49 15035-15040 9714161 Hoh, J. H. 1998 Protein Sci 32 2 223-228 3220257 Julien, J. P. Cote, F. Beaudet, L. Sidky, M. Flavell, D. Grosveld, F. Mushynski, W. 1988 Gene 68 2 307-314 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 ODC P07805 7404357 DCUTOB Trypanosoma brucei 425 GAMDIVVNDDLSCRFLEGFNTRDALCKKISMNTCDEGDPFFVADLGDIVRKHETWKKCLPRVTPFYAVACNDDWRVLGTLAALGTGFDCASNTEIQRVRGIGVPPEKIIYANPCKQISHIRYARDSGVDVMTFDCVDELEKVAKTHPKAKMVLRISTDDSLARCRLSVKFGAKVEDCRFILEQAKKLNIDVTGVSFHVGSGSTDASTFAQAISDSRFVFDMGTELGFNMHILDIGGGFPGTRDAPLKFEEIAGVINNALEKHFPPDLKLTIVAEPGRYYVASAFTLAVNVIAKKVTPGVQTDVGAHAESNAQSFMYYVNDGVYGSFNCILYDHAVVRPLPQREPIPNEKLYPSSVWGPTCDGLDQIVERYYLPEMQVGEWLLFEDMGAYTVVGTSSFNGFQSPTIYYVVSGLPDHVVRELKSQKS Disordered - Extended 1 35 GAMDIVVNDDLSCRFLEGFNTRDALCKKISMNTCD Engineered 1QU4A 1QU4B 1QU4C 1QU4D 2TODB Relationship to function unknown Unknown Unknown X-ray crystallography Paper 10563800 Grishin, N. V. Osterman, A. L. Brooks, H. B. Phillips, M. A. Goldsmith, E. J. 1999 Biochemistry 38 46 15174-15184 Jancarik, J. Kim, S.H. 1991 Journal of Applied Crystallography 24 409-411 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 1QU4A 1QU4B 1QU4C 1QU4D 2TODA 2TODB 2TODC 2TODD 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 1QU4A 1QU4B 1QU4C 1QU4D 2TODA 2TODB 2TODC 2TODD 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 1AQ4A 1AQ4B 1AQ4C 1AQ4D 2TODA 2TODB 2TODC 2TODD 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, L. K. Brooks, H. B. Osterman, A. L. Goldsmith, E. J. Phillips, M. A. 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 [Precursor] Basement membrane protein BM-40 ON Osteonectin Secreted protein acidic and rich in cysteine P07214 P07214 129284 GEMSN 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 PheRS P27001 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 PIP5KIIbeta Q8TBP2 Hs.260603 P78356 47605991 Homo sapiens (Human) 416 MSSNCTSTTAVAVAPLSASKTKTKKKHFVCQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVDRAEQEEMEVEERAEDEECENDGVGGNLLCSYGTPPDSPGNLLSFPRFFGPGEFDPSVDVYAMKSHESSPKKEVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSNILT Disordered - Extended N-Terminal 1 33 MSSNCTSTTAVAVAPLSASKTKTKKKHFVCQKV Native 1BO1A Relationship to function unknown Unknown Unknown X-ray crystallography 95 5.6 Lithium acetate 100 MPD 5 PEG 1000 20 Sodium citrate 100 Paper 9753329 Rao, V. D. Misra, S. Boronenkov, I. V. Anderson, R. A. Hurley, J. H. 1998 Cell 94 6 829-839 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 Lithium acetate 100 MPD 5 PEG 1000 20 Sodium citrate 100 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. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta 1 EC 3.1.4.11 Phosphoinositide phospholipase C Phospholipase C Delta-1 PLC-Delta-1 PLC-III P10688 130228 Rattus norvegicus (Rat) 756 MDSGRDFLTLHGLQDDPDLQALLKGSQLLKVKSSSWRRERFYKLQEDCKTIWQESRKVMRSPESQLFSIEDIQEVRMGHRTEGLEKFARDIPEDRCFSIVFKDQRNTLDLIAPSPADAQHWVQGLRKIIHHSGSMDQRQKLQHWIHSCLRKADKNKDNKMNFKELKDFLKELNIQVDDGYARKIFRECDHSQTDSLEDEEIETFYKMLTQRAEIDRAFEEAAGSAETLSVERLVTFLQHQQREEEAGPALALSLIERYEPSETAKAQRQMTKDGFLMYLLSADGNAFSLAHRRVYQDMDQPLSHYLVSSSHNTYLLEDQLTGPSSTEAYIRALCKGCRCLELDCWDGPNQEPIIYHGYTFTSKILFCDVLRAIRDYAFKASPYPVILSLENHCSLEQQRVMARHLRAILGPILLDQPLDGVTTSLPSPEQLKGKILLKGKKLGGLLPAGGENGSEATDVSDEVEAAEMEDEAVRSQVQHKPKEDKLKLVPELSDMIIYCKSVHFGGFSSPGTSGQAFYEMASFSESRALRLLQESGNGFVRHNVSCLSRIYPAGWRTDSSNYSPVEMWNGGCQIVALNFQTPGPEMDVYLGCFQDNGGCGYVLKPAFLRDPNTTFNSRALTQGPWWRPERLRVRIISGQQLPKVNKNKNSIVDPKVIVEIHGVGRDTGSRQTAVITNNGFNPRWDMEFEFEVTVPDLALVRFMVEDYDSSSKNDFIGQSTIPWNSLKQGYRHVHLLSKNGDQHPSATLFVKISIQD 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 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 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 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 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 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 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 Major prion protein [Precursor] PrP PrP27-30 PrP33-35C P04925 200527 Mus musculus (Mouse) 254 MANLGYWLLALFVTMWTDVGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAVSRPMIHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYDGRRSSSTVLFSSPPVILLISFLIFLIVG Disordered 23 119 KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGA Paper 10899999 Lopez Garcia F, Zahn R, Riek R, Wuthrich K 2000 Proc Natl Acad Sci U S A 97 15 8334-9 Sperm histone Galline Protamine P15340 123705 A34320 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 P06302 135836 TNRTA 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 Myc proto-oncogene protein c-myc P01106 127619 Homo sapiens (Human) 439 MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENVKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEEDLLRKRREQLKHKLEQLRNSCA Disordered 1 143 MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAK Paper 8755740 McEwan IJ, Dahlman-Wright K, Ford J, Wright AP 1996 Biochemistry 35 29 9584-93 Disordered - Extended 406 434 VQAEEQKLISEEDLLRKRREQLKHKLEQL Paper 8755740 McEwan IJ, Dahlman-Wright K, Ford J, Wright AP 1996 Biochemistry 35 29 9584-93 Modification methylase PvuII EC 2.1.1.113 M.PvuII N-4 cytosine-specific methyltransferase PvuII P11409 6729995 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 Methylation Protein-DNA binding 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 Replication factor-A protein 1 RF-A RP-A Single-stranded DNA-binding protein P27694 P27694 1350579 A40457 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 Retinoic acid receptor RXR-alpha Retinoid X receptor, alpha P19793 Hs.20084 P19793 S09592 Homo Sapiens 462 MDTKHFLPLDFSTQVNSSLTSPTGRGSMAAPSLHPSLGPGIGSPGQLHSPISTLSSPINGMGPPFSVISSPMGPHSMSVPTTPTLGFSTGSPQLSSPMNPVSSSEDIKPPLGLNGVLKVPAHPSGNMASFTKHICAICGDRSSGKHYGVYSCEGCKGFFKRTVRKDLTYTCRDNKDCLIDKRQRNRCQYCRYQKCLAMGMKREAVQEERQRGKDRNENEVESTSSANEDMPVERILEAELAVEPKTETYVEANMGLNPSSPNDPVTNICQAADKQLFTLVEWAKRIPHFSELPLDDQVILLRAGWNELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGVGAIFDRVLTELVSKMRDMQMDKTELGCLRAIVLFNPDSKGLSNPAEVEALREKVYASLEAYCKHKYPEQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQMT Disordered - Extended D-BOX 172 176 RDNKD Engineered 1RXR1 Molecular assembly Protein-DNA binding Protein-protein binding Nuclear magnetic resonance (NMR) 300 6.6 2H2O 100 KCl 100 KH2PO4 pH 6.7 20 ZnCl2 0.3 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 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 2H2O 100 KCl 100 KH2PO4 pH 6.7 20 ZnCl2 0.3 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 2H2O 100 KCl 100 KH2PO4 pH 6.7 20 ZnCl2 0.3 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. 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 C-terminal helix 202 206 REAVQ Engineered 1RXR1 Function arises via an order to disorder transition Molecular assembly Protein-DNA binding Protein-protein binding Substrate/ligand 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. Regulator of G-protein signaling 4 RGP4 RGS4 Signal transduction inhibitor RGS4 P49799 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 Coat protein [Precursor] Capsid protein Southern bean mosaic virus coat protein P03607 P03607 75662 VCBW Southern bean mosaic virus (SBMV) 260 ATRLTKKQLAQAIQNTLPNPPRRKRRAKRRAAQVPKPTQAGVSMAPIAQGTMVKLRPPMLRSSMDVTILSHCELSTELAVTVTIVVTSELVMPFTVGTWLRGVAQNWSKYAWVAIRYTYLPSCPTTTSGAIHMGFQYDMADTLPVSVNQLSNLKGYVTGPVWEGQSGLCFVNNTKCPDTSRAITIALDTNEVSEKRYPFKTATDYATAVGVNANIGNILVPARLVTAMEGGSSKTAVNTGRLYASYTIRLIEPIAAALNL 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. 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 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 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. 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. 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 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. 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. SdrD protein Serine aspartamine repeat protein D O86488 3550594 T28679 Staphylococcus aureus 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 P130 1942972 Sindbis virus (subtype Ockelbo / strain Edsbyn 82-5) 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 Q57733 2495337 F64335 Methanococcus jannaschii 147 MFGRDPFDSLFERMFKEFFATPMTGTTMIQSSTGIQISGKGFMPISIIEGDQHIKVIAWLPGVNKEDIILNAVGDTLEIRAKRSPLMITESERIIYSEIPEEEEIYRTIKLPATVKEENASAKFENGVLSVILPKAESSIKKGINIE Disordered 1 32 MFGRDPFDSLFERMFKEFFATPMTGTTMIQSS Paper 9707123 Kim KK, Kim R, Kim SH 1998 Nature 394 6693 595-9 SNAP-25 P60881 Rattus norvegicus 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 NaCl salt 100 phosphate buffer 10 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. Synaptobrevin 2 VAMP 2 Vesicle associated membrane protein 2 P63027 Hs.25348 P63027 135094 Homo sapiens 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 NACP Non-A4 component of amyloid precursor Non-A beta component of AD amyloid SNCA P37840 Hs.271771 P37840 586067 A49669 Homo sapiens (Human) 140 MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA Disordered - Extended 1 140 MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA Native Relationship to function unknown Molecular assembly Metal binding Polymerization Protein-protein binding Far-UV circular dichroism (CD) 7.5 Tris buffer 10 Fourier transform infrared spectroscopy calcium fluoride solution cell 0.05 NACP per mL of D2O 4 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 Thyroid transcription factor 1 Homeobox protein Nkx-2.1 Thyroid nuclear factor 1 TTF-1 P23441 136462 S12002 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 elastic titin-skeletal [fragment] Q10465 1017427 I38346 Homo sapiens (Human) 7962 PDQEMPVYPPAIITPLQDTVTSEGQPARFQCRVSGTDLKVSWYSKDKKIKPSRFFRMTQFEDTYQLEIAEAYPEDEGTYTFVANNAVGQVSSTANLSLEAPESILHERIEQEIEMEMKAAPVIKRKIEPLEVALGHLAKFTCEIQSAPNVRFQWFKAGREIYESDKCSIRSSKYISSLEILRTQVVDCGEYTCKASNEYGSVSCTATLTVTEAYPPTFLSRPKSLTTFVGKAAKFICTVTGTPVIETIWQKDGAALSPSPNWRISDAENKHILELSNLTIQDRGVYSCKASNKFGADICQAELIIIDKPHFIKELEPVQSAINKKVHLECQVDEDRKVTVTWSKDGQKLPPGKDYKICFEDKIATLEIPLAKLKDSGTYVCTASNEAGSSSCSATVTVREPPSFVKKVDPSYLMLPGESARLHCKLKGSPVIQVTWFKNNKELSESNTVRMYFVNSEAILDITDVKVEDSGSYSCEAVNDVGSDSCSTEIVIKEPPSFIKTLEPADIVRGTNALLQCEVSGTGPFEISWFKDKKQIRSSKKYRLFSQKSLVCLEIFSFNSADVGEYECVVANEVGKCGCMATHLLKEPPTFVKKVDDLIALGGQTVTLQAAVRGSEPISVTWMKGQEVIREDGKIKMSFSNGVAVLIIPDVQISFGGKYTCLAENEAGSQTSVGELIVKEPAKIIERAELIQVTAGDPATLEYTVAGTPELKPKWYKDGRPLVASKKYRISFKNNVAQLKFYSAELHDSGQYTFEISNEVGSSSCETTFTVLDRDIAPFFTKPLRNVDSVVNGTCRLDCKIAGSLPMRVSWFKDGKEIAASDRYRIAFVEGTASLEIIRVDMNDAGNFTCRATNSVGSKDSSGALIVQEPPSFVTKPGSKDVLPGSAVCLKSTFQGSTPLTIRWFKGNKELVSGGSCYITKEALESSLELYLVKTSDSGTYTCKVSNVAGGVECSANLFVKEPATFVEKLEPSQLLKKGDATQLACKVTGTPPIKITWFANDREIKESSKHRMSFVESTAVLRLTDVGIEDSGEYMCEAQNEAGSDHCSSIVIVKESPYFTKEFKPIEVLKEYDVMLLAEVAGTPPFEITWFKDNTILRSGRKYKTFIQDHLVSLQILKFVAADAGEYQCRVTNEVGSSICSARVTLREPPSFIKKIESTSSLRGGTAAFQATLKGSLPITVTWLKDSDEITEDDNIRMTFENNVASLYLSGIEVKHDGKYVCQAKNDAGIQRCSALLSVKEPATITEEAVSIDVTQGDPATLQVKFSGTKEITAKWFKDGQELTLGSKYKISVTDTVSILKIISTEKKDSGEYTFEVQNDVGRSSCKARINVLDLIIPPSFTKKLKKMDSIKGSFIDLECIVAGSHPISIQWFKDDQEISASEKYKFSFHDNTAFLEISQLEGTDSGTYTCSATNKAGHNQCSGHLTVKEPPYFVEKPQSQDVNPNTRVQLKALVGGTAPMTIKWFKDNKELHSGAARSVWKDDTSTSLELFAAKATDSGTYICQLSNDVGTATSKATLFVKEPPQFIKKPSPVLVLRNGQSTTFECQITGTPKIRVSWYLDGNEITAIQKHGISFIDGLATFQISGARVENSGTYVCEARNDAGTASCSIELKVKEPPTFIRELKPVEVVKYSDVELECEVTGTPPFEVTWLKNNREIRSSKKYTLTDRVSVFNLHITKCDPSDTGEYQCIVSNEGGSCSCSTRVALKEPPSFIKKIENTTTVLKSSATFQSTVAGSPPISITWLKDDQILDEDDNVYISFVDSVATLQIRSVDNGHSGRYTCQAKNESGVERCYAFLLVQEPAQIVEKAKSVDVTEKDPMTLECVVAGTPELKVKWLKDGKQIVPSRYFSMSFENNVASFRIQSVMKQDSGQYTFKVENDFGSSSCDAYLRVLDQNIPPSFTKKLTKMDKVLGSSIHMECKVSGSLPISAQWFKDGKEISTSAKYRLVCHERSVSLEVNNLELEDTANYTCKVSNVAGDDACSGILTVKEPPSFLVKPGRQQAIPDSTVEFKAILKGTPPFKIKWFKDDVELVSGPKCFIGLEGSTSFLNLYSVDASKTGQYTCHVTNDVGSDSCTTMLLVTEPPKFVKKLEASKIVKAGDSSRLECKIAGSPEIRVVWFRNEHELPASDKYRMTFIDSVAVIQMNNLSTEDSGDFICEAQNPAGSTSCSTKVIVKEPPVFSSFPPIVETLKNAEVSLECELSGTPPFEVVWYKDKRQLRSSKKYKIASKNFHTSIHILNVDTSDIGEYHCKAQNEVGSDTCVCTVKLKEPPRFVSKLNSLTVVAGEPAELQASIEGAQPIFVQWLKEKEEVIRESENIRITFVENVATLQFAKAEPANAGKYICQIKNDGGMRENMATLMVLEPAVIVEKAGPMTVTVGETCTLECKVAGTPELSVEWYKDGKLLTSSQKHKFSFYNKISSLRILSVERQDAGTYTFQVQNNVGKSSCTAVVDVSDRAVPPSFTRRLKNTGGVLGASCILECKVAGSSPISVAWFHEKTKIVSGAKYQTTFSDNVCTLQLNSLDSSDMGNYTCVAANVAGSDECRAVLTVQEPPSFVKEPEPLEVLPGKNVTFTSVIRGTPPFKVNWFRGARELVKGDRCNIYFEDTVAELELFNIDISQSGEYTCVVSNNAGQASCTTRLFVKEPAAFLKRLSDHSVEPGKSIILESTYTGTLPISVTWKKDGFNITTSEKCNIVTTEKTCILEILNSTKRDAGQYSCEIENEAGRDVCGALVSTLEPPYFVTELEPLEAAVGDSVSLQCQVAGTPEITVSWYKGDTKLRPTPEYRTYFTNNVATLVFNKVNINDSGEYTCKAENSIGTASSKTVFRIQERQLPPSFARQLKDIEQTVGLPVTLTCRLNGSAPIQVCWYRDGVLLRDHENLQTSFVDNVATLKILQTDLSHSGQYSCSASNPLGTASSSARLTAREPKKSPFFDIKPVSIDVIAGESADFECHVTGAQPMRITWSKDNKEIRPGGNYTITCVGNTPHLRILKVGKGDSGQYTCQATNDVGKDMCSAQLSVKEPPKFVKKLEASKVAKQGESIQLECKISGSPEIKVSWFRNDSELHESWKYNMSFINSVALLTINEASAEDSGDYICEAHNGVGDASCSTALTVKAPPVFTQKPSPVGALKGSDVILQCEISGTPPFEVVWVKDRKQVRNSKKFKITSKHFDTNLHILNLEASDVGEYHCKATNEVGSDTCSCSVKFKEPPRFVKKLSDTSTLIGDAVELRAIVEGFQPISVVWLKDRGEVIRESENTRISFIDNIATLQLGSPEASNSGKYICQIKNDAGMRECSAVLTVLEPARIIEKPEPMTVTTGNPFALECVVTGTPELSAKWFKDGRELSADSKHHITFINKVASLKIPCAEMSDKGLYSFEVKNSVGKSNCTVSVHVSDRIVPPSFIRKLKDVNAILGASVVLECRVSGSAPISVGWFQDGNEIVSGPKCQSSFSENVCTLNLSLLEPSDTGIYTCVAANVAGSDECSAVLTVQEPPSFEQTPDSVEVLPGMSLTFTSVIRGTPPFKVKWFKGSRELVPGESCNISLEDFVTELELFEVQPLESGDYSCLVTNDAGSASCTTHLFVKEPATFVKRLADFSVETGSPIVLEATYTGTPPISVSWIKDEYLISQSERCSITMTEKSTILEILESTIEDYAQYSCLIENEAGQDICEALVSVLEPPYFIEPLEHVEAVIGEPATLQCKVDGTPEIRISWYKEHTKLRSAPAYKMQFKNNVASLVINKVDHSDVGEYSCKADNSVGAVASSAVLVIKARKLPPFFARKLKDVHETLGFPVAFECRINGSEPLQVSWYKDGVLLKDDANLQTSFVHNVATLQILQTDQSHIGQYNCSASNPLGTASSSAKLILSEHEVPPFFDLKPVSVDLALGESGTFKCHVTGTAPIKITWAKDNREIRPGGNYKMTLVENTATLTVLKVGKGDAGQYTCYASNIAGKDSCSAQLGVQEPPRFIKKLEPSRIVKQDEFTRYECKIGGSPEIKVLWYKDETEIQESSKFRMSFVDSVAVLEMHNLSVEDSGDYTCEAHNAAGSASSSTSLKVKEPPIFRKKPHPIETLKGADVHLECELQGTPPFHVSWYKDKRELRSGKKYKIMSENFLTSIHILNVDAADIGEYQCKATNDVGSDTCVGSIALKAPPRFVKKLSDISTVVGKEVQLQTTIEGAEPISVVWFKDKGEIVRESDNIWISYSENIATLQFSRVEPANAGKYTCQIKNDAGMQECFATLSVLEPATIVEKPESIKVTTGDTCTLECTVAGTPELSTKWFKDGKELTSDNKYKISFFNKVSGLKIINVAPSDSGVYSFEVQNPVGKDSCTASLQVSDRTVPPSFTRKLKETNGLSGSSVVMECKVYGSPPISVSWFHEGNEISSGRKYQTTLTDNTCALTVNMLEESDSGDYTCIATNMAGSDECSAPLTVREPPSFVQKPDPMDVLTGTNVTFTSIVKGTPPFSVSWFKGSSELVPGDRCNVSLEDSVAELELFDVDTSQSGEYTCIVSNEAGKASCTTHLYIKAPAKFVKRLNDYSIEKGKPLILEGTFTGTPPISVTWKKNGINVTPSQRCNITTTEKSPILEIPSSTVEDAGQYNCYIENASGKDSCSAQILILEPPYFVKQLEPVKVSVGDSASLQCQLAGTPEIGVSWYKGDTKLRPTTTYKMHFRNNVATLVFNQVDINDSGEYICKAENSVGEVSASTFLTVQEQKLPPSFSRQLRDVQETVGLPVVFDCAISGSEPISVSWYKDGKPLKDSPNVQTSFLDNTATLNIFKTDRSLAGQYSCTATNPIGSASSSARLILTEGKNPPFFDIRLAPVDAVVGESADFECHVTGTQPIKVSWAKDSREIRSGGKYQISYLENSAHLTVLKVDKGDSGQYTCYAVNEVGKDSCTAQLNIKERLIPPSFTKRLSETVEETEGNSFKLEGRVAGSQPITVAWYKNNIEIQPTSNCEITFKNNTLVLQVRKAGMNDAGLYTCKVSNDAGSALCTSSIVIKEPKKPPVFDQHLTPVTVSEGEYVQLSCHVQGSEPIRIQWLKAGREIKPSDRCSFSFASGTAVLELRDVAKADSGDYVCKASNVAGSDTTKSKVTIKDKPAVAPATKKAAVDGRLFFVSEPQSIRVVEKTTATFIAKVGGDPIPNVKWTKGKWRQLNQGGRVFIHQKGDEAKLEIRDTTKTDSGLYRCVAFNEHGEIESNVNLQVDERKKQEKIEGDLRAMLKKTPILKKGAGEEEEIDIMELLKNVDPKEYEKYARMYGITDFRGLLQAFELLKQSQEEETHRLEIEEIERSERDEKEFEELVSFIQQRLSQTEPVTLIKDIENQTVLKDNDAVFEIDIKINYPEIKLSWYKGTEKLEPSDKFEISIDGDRHTLRVKNCQLKDQGNYRLVCGPHIASAKLTVIEPAWERHLQDVTLKEGQTCTMTVQFSVPNVKSEWFRNGRILKPQGRHKTEVEHKVHKLTIADVRAEDQGQYTCKYEDLETSAELRIEAEPIQFTKRIQNIVVSEHQSATFECEVSFDDAIVTWYKGPTELTESQKYNFRNDGRCHYMTIHNVTPDDEGVYSVIARLEPRGEARSTAELYLTTKEIKLELKPPDIPDSRVPIPTMPIRAVPPEEIPPVVAPPVPLLLPTPEEKKPPPKRIEVTKKAVKKDAKKVVAKPKEMTPREEIVKKPPPPTTLIPAKAPEIIDVSSKAEEVKIMTITRKKEVQKEKEAVYEKKQAVHKEKRVFIESFEEPYDELEVEPYTEPFEQPYYEEPDEDYEEIKVEAKKEVHEEWEEDFEEGQEYYEREEGYDEGEEEWEEAYQEREVIQVQKEVYEESHERKVPAKVPEKKAPPPPKVIKKPVIEKIEKTSRRMEEEKVQVTKVPEVSKKIVPQKPSRTPVQEEVIEVKVPAVHTKKMVISEEKMFFASHTEEEVSVTVPEVQKEIVTEEKIHVAVSKRVEPPPKVPELPEKPAPEEVAPVPIPKKVEPPAPKVPEVPKKPVPEEKKPVPVPKKEPAAPPKVPEVPKKPVPEEKIPVPVAKKKEAPPAKVPEVQKGVVTEEKITIVTQREESPPPAVPEIPKKKVPEERKPVPRKEEEVPPPPKVPALPKKPVPEEKVAVPVPVAKKAPPPRAEVSKKTVVEEKRFVAEEKLSFAVPQRVEVTRHEVSAEEEWSYSEEEEGVSISVYREEEREEEEEAEVTEYEVMEEPEEYVVEEKLHIISKRVEAEPAEVTERQEKKIVLKPKIPAKIEEPPPAKVPEAPKKIVPEKKVPAPVPKKEKVPPPKVPEEPKKPVPEKKVPPKVIKMEEPLPAKVTEKHMQITQEEKVLVAVTKKEAPPKARVPEEPKRAVPEEKVLKLKPKREEEPPAKVTEFRKRVVKEEKVSIEAPKREPQPIKEVTIMEEKERAYTLEEEAVSVQREEEYEEYEEYDYKEFEEYEPTEEYDQYEEYEEREYERYEEHEEYITEPEKPIPVKPVPEEPVPTKPKAPPAKVLKKAVPEEKVPVPIPKKLKPPPPKVPEEPKKVFEEKIHISITKREKEQVTEPAAKVPMKPKRVVAEEKVPVPRKEVAPPVRVPEVPKELEPEEVAFEEEVVTHVEEYLVEEEEEYIHEEEEFITEEEVVPVIPVKVPEVPRKPVPEEKKPVPVPKKKEAPPAKVPEVPKKPEEKVPVLIPKKEKPPPAKVPEVPKKPVPEEKVPVPVPKKVEAPPAKVPEVPKKPVPEKKVPVPAPKKVEAPPAKVPEVPKKLIPEEKKPTPVPKKVEAPPPKVPKKREPVPVPVALPQEEEVLFEEEIVPEEEVLPEEEEVLPEEEEVLPEEEEVLPEEEEIPPEEEEVPPEEEYVPEEEEFVPEEEVLPEVKPKVPVPAPVPEIKKKVTEKKVVIPKKEEAPPAKVPEVPKKVEEKRIILPKEEEVLPVEVTEEPEEEPISEEEIPEEPPSIEEVEEVAPPRVPEVIKKAVPEAPTPVPKKVEAPPAKVSKKIPEEKVPVPVQKKEAPPAKVPEVPKKVPEKKVLVPKKEAVPPAKGRTVLEEKVSVAFRQEVVVKERLELEVVEAEVEEIPEEEEFHEVEEYFEEGEFHEVEEFIKLEQHRVEEEHRVEKVHRVIEVFEAEEVEVFEKPKAPPKGPEISEKIIPPKKPPTKVVPRKEPPAKVPEVPKKIVVEEKVRVPEEPRVPPTKVPEVLPPKEVVPEKKVPVPPAKKPEAPPPKVPEAPKEVVPEKKVPVPPPKKPEVPPTKVPEVPKAAVPEKKVPEAIPPKPESPPPEVFEEPEESPSAPPKKPEVPPVRVPEVPKEVVPEKKVPAAPPKKPEVTPVKVPEAPKEVVPEKKVPVPPPKKPEVPPTKVPEVPKVAVPEKKVPEAIPPKPESPPPEVFEEPEEVALEEPPAEVVEEPEPAAPPQVTVPPKNPVPEKKAPAVVAKKPELPPVKVPEVPKEVVPEKKVPLVVPKKPEAPPAKVPEVPKEVVPEKKVAVPKKPEVPPAKVPEVPKKPVLEEKPAVPVPERAESPPPEVYEEPEEIAPEEEIAPEEEKPVPVAEEEEPEVPPPAVPEEPKKIIPEKKVPVIKKPEAPPPKEPEPEKVIEKPKLKPRPPPPPPAPPKEDVKEKIFQLKAIPKKKVPENPQVPEKVELTPLKVPGGEKKVRKLLPERKPEPKEEVVLKSVLRKRPEEEEPKVEPKKLEKVKKPAVPEPPPPKPVEEVEVPTVTKRERKIPEPTKVPEIKPAIPLPAPEPKPKPEAEVKTIKPPPVEPEPTPIAAPVTVPVVGKKAEAKAPKEEAAKPKGPIKGVPKKTPSPIEAERRKLRPGSGGEKPPDEAPFTYQLKAVPLKFVKEIKDIILTESEFVGSSAIFECLVSPSTAITTWMKDGSNIRESPKHRFIADGKDRKLHIIDVQLSDAGEYTCVLRLGNKEKTSTAKLVVEELPVRFVKTLEEEVTVVKGQPLYLSCELNKERDVVWRKDGKIVVEKPGRIVPGVIGLMRALTINDAD Disordered PEVK region 5618 7791 PPEEIPPVVAPPVPLLLPTPEEKKPPPKRIEVTKKAVKKDAKKVVAKPKEMTPREEIVKKPPPPTTLIPAKAPEIIDVSSKAEEVKIMTITRKKEVQKEKEAVYEKKQAVHKEKRVFIESFEEPYDELEVEPYTEPFEQPYYEEPDEDYEEIKVEAKKEVHEEWEEDFEEGQEYYEREEGYDEGEEEWEEAYQEREVIQVQKEVYEESHERKVPAKVPEKKAPPPPKVIKKPVIEKIEKTSRRMEEEKVQVTKVPEVSKKIVPQKPSRTPVQEEVIEVKVPAVHTKKMVISEEKMFFASHTEEEVSVTVPEVQKEIVTEEKIHVAVSKRVEPPPKVPELPEKPAPEEVAPVPIPKKVEPPAPKVPEVPKKPVPEEKKPVPVPKKEPAAPPKVPEVPKKPVPEEKIPVPVAKKKEAPPAKVPEVQKGVVTEEKITIVTQREESPPPAVPEIPKKKVPEERKPVPRKEEEVPPPPKVPALPKKPVPEEKVAVPVPVAKKAPPPRAEVSKKTVVEEKRFVAEEKLSFAVPQRVEVTRHEVSAEEEWSYSEEEEGVSISVYREEEREEEEEAEVTEYEVMEEPEEYVVEEKLHIISKRVEAEPAEVTERQEKKIVLKPKIPAKIEEPPPAKVPEAPKKIVPEKKVPAPVPKKEKVPPPKVPEEPKKPVPEKKVPPKVIKMEEPLPAKVTEKHMQITQEEKVLVAVTKKEAPPKARVPEEPKRAVPEEKVLKLKPKREEEPPAKVTEFRKRVVKEEKVSIEAPKREPQPIKEVTIMEEKERAYTLEEEAVSVQREEEYEEYEEYDYKEFEEYEPTEEYDQYEEYEEREYERYEEHEEYITEPEKPIPVKPVPEEPVPTKPKAPPAKVLKKAVPEEKVPVPIPKKLKPPPPKVPEEPKKVFEEKIHISITKREKEQVTEPAAKVPMKPKRVVAEEKVPVPRKEVAPPVRVPEVPKELEPEEVAFEEEVVTHVEEYLVEEEEEYIHEEEEFITEEEVVPVIPVKVPEVPRKPVPEEKKPVPVPKKKEAPPAKVPEVPKKPEEKVPVLIPKKEKPPPAKVPEVPKKPVPEEKVPVPVPKKVEAPPAKVPEVPKKPVPEKKVPVPAPKKVEAPPAKVPEVPKKLIPEEKKPTPVPKKVEAPPPKVPKKREPVPVPVALPQEEEVLFEEEIVPEEEVLPEEEEVLPEEEEVLPEEEEVLPEEEEIPPEEEEVPPEEEYVPEEEEFVPEEEVLPEVKPKVPVPAPVPEIKKKVTEKKVVIPKKEEAPPAKVPEVPKKVEEKRIILPKEEEVLPVEVTEEPEEEPISEEEIPEEPPSIEEVEEVAPPRVPEVIKKAVPEAPTPVPKKVEAPPAKVSKKIPEEKVPVPVQKKEAPPAKVPEVPKKVPEKKVLVPKKEAVPPAKGRTVLEEKVSVAFRQEVVVKERLELEVVEAEVEEIPEEEEFHEVEEYFEEGEFHEVEEFIKLEQHRVEEEHRVEKVHRVIEVFEAEEVEVFEKPKAPPKGPEISEKIIPPKKPPTKVVPRKEPPAKVPEVPKKIVVEEKVRVPEEPRVPPTKVPEVLPPKEVVPEKKVPVPPAKKPEAPPPKVPEAPKEVVPEKKVPVPPPKKPEVPPTKVPEVPKAAVPEKKVPEAIPPKPESPPPEVFEEPEESPSAPPKKPEVPPVRVPEVPKEVVPEKKVPAAPPKKPEVTPVKVPEAPKEVVPEKKVPVPPPKKPEVPPTKVPEVPKVAVPEKKVPEAIPPKPESPPPEVFEEPEEVALEEPPAEVVEEPEPAAPPQVTVPPKNPVPEKKAPAVVAKKPELPPVKVPEVPKEVVPEKKVPLVVPKKPEAPPAKVPEVPKEVVPEKKVAVPKKPEVPPAKVPEVPKKPVLEEKPAVPVPERAESPPPEVYEEPEEIAPEEEIAPEEEKPVPVAEEEEPEVPPPAVPEEPKKIIPEKKVPVIKKPEAPPPKEPEPEKVIEKPKLKPRPPPPPPAPPKEDVKEKIFQLKAIPKKKVPENPQVPEKVELTPLKVPGGEKKVRKLLPERKPEPKEEVVLKSVLRKRPEEEEPKVEPKKLEKVKKPAVPEPPPPKPVEEVEVPTVTKRERKIPEPTKVPEIKPAIPLPAPEPKPKPEAEVKTIKPPPVEPEPTPIAAPVTVPVVGKKAEAKAPKEEAAKPKGPIKGVPKKTPSPIEAERRKLRPGSGGEKPPDEA Fragment Function arises from the disordered state Entropic chain Entropic spring Paper 7569978 Labeit S, Kolmerer B 1995 Science 270 5234 293-6 9472037 Trombitas K, Greaser M, Labeit S, Jin JP, Kellermayer M, Helmes M, Granzier H 1998 J Cell Biol 140 4 853-9 Thymidylate synthase EC 2.1.1.45 TS TSase Hs.369762 P04818 136611 YXHUT Homo sapiens (Human) 313 MPVAGSELPRRPLPPAAQERDAEPRPPHGELQYLGQIQHILRCGVRKDDRTGTGTLSVFGMQARYSLRDEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKGVKIWDANGSRDFLDSLGFSTREEGDLGPVYGFQWRHFGAEYRDMESDYSGQGVDQLQRVIDTIKTNPDDRRIIMCAWNPRDLPLMALPPCHALCQFYVVNSELSCQLYQRSGDMGLGVPFNIASYALLTYMIAHITGLKPGDFIHTLGDAHIYLNHIEPLKIQLQREPRPFPKLRILRKVEKIDDFKAEDFQIEGYNPHPTIKMEMAV Disordered 1 27 MPVAGSELPRRPLPPAAQERDAEPRPP Native X-ray crystallography 7 Ammonium sulfate 1.5 Beta-Mercaptoethanol pH 6.5-8.0 20 Tris-HCl buffer Paper 8845352 Schiffer CA, Clifton IJ, Davisson VJ, Santi DV, Stroud RM 1995 Biochemistry 34 50 16279-87 Disordered 93 132 KGSTNAKELSSKGVKIWDANGSRDFLDSLGFSTREEGDLG Native X-ray crystallography 7 Ammonium sulfate 1.5 Beta-Mercaptoethanol pH 6.5-8.0 20 Tris-HCl buffer Paper 8845352 Schiffer CA, Clifton IJ, Davisson VJ, Santi DV, Stroud RM 1995 Biochemistry 34 50 16279-87 Disordered 142 157 FGAEYRDMESDYSGQG Native X-ray crystallography 7 Ammonium sulfate 1.5 Beta-Mercaptoethanol pH 6.5-8.0 20 Tris-HCl buffer Paper 8845352 Schiffer CA, Clifton IJ, Davisson VJ, Santi DV, Stroud RM 1995 Biochemistry 34 50 16279-87 Disordered 107 128 KIWDANGSRDFLDSLGFSTREE Engineered X-ray crystallography PEG 4000 15-30%(weight/volume) saturated ammonium sulfate 42-50% Tris-HCL pH 8.5 100 Paper 11278511 Phan J, Steadman DJ, Koli S, Ding WC, Minor W, Dunlap RB, Berger SH, Lebioda L 2001 J Biol Chem 276 17 14170-7 The protein used in the Phan paper had an N-terminal extension of 42 residues. It was noted that these residues have no significant effect on the protein structure. Estrogen receptor alpha ER ER-alpha Estradiol receptor P03372 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-DNA binding Protein-protein 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 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 I Deoxiribonucleate topoisomerase Deoxiribonucleic topoisomerase EC 5.99.1.2 Late protein H6 Nicking-closing enzyme Omega-protein Relaxing enzyme Swivelase TOP1mt Topo I Topoisomerase Topoisomerase I TpI Type I DNA topoisomerase Untwisting enzyme P11387 Hs.253536 P11387 68486 ISHUT1 Homo sapiens (Human) 765 MSGDHLHNDSQIEADFRLNDSHKHKDKHKDREHRHKEHKKEKDREKSKHSNSEHKDSEKKHKEKEKTKHKDGSSEKHKDKHKDRDKEKRKEEKVRASGDAKIKKEKENGFSSPPQIKDEPEDDGYFVPPKEDIKPLKRPRDEDDADYKPKKIKTEDTKKEKKRKLEEEEDGKLKKPKNKDKDKKVPEPDNKKKKPKKEEEQKWKWWEEERYPEGIKWKFLEHKGPVFAPPYEPLPENVKFYYDGKVMKLSPKAEEVATFFAKMLDHEYTTKEIFRKNFFKDWRKEMTNEEKNIITNLSKCDFTQMSQYFKAQTEARKQMSKEEKLKIKEENEKLLKEYGFCIMDNHKERIANFKIEPPGLFRGRGNHPKMGMLKRRIMPEDIIINCSKDAKVPSPPPGHKWKEVRHDNKVTWLVSWTENIQGSIKYIMLNPSSRIKGEKDWQKYETARRLKKCVDKIRNQYREDWKSKEMKVRQRAVALYFIDKLALRAGNEKEEGETADTVGCCSLRVEHINLHPELDGQEYVVEFDFLGKDSIRYYNKVPVEKRVFKNLQLFMENKQPEDDLFDRLNTGILNKHLQDLMEGLTAKVFRTYNASITLQQQLKELTAPDENIPAKILSYNRANRAVAILCNHQRAPPKTFEKSMMNLQTKIDAKKEQLADARRDLKSAKADAKVMKDAKTKKVVESKKKAVQRLEEQLMKLEVQATDREENKQIALGTSKLNYLDPRITVAWCKKWGVPIEKIYNKTQREKFAWAIDMADEDYEF Disordered - Extended 1 174 MSGDHLHNDSQIEADFRLNDSHKHKDKHKDREHRHKEHKKEKDREKSKHSNSEHKDSEKKHKEKEKTKHKDGSSEKHKDKHKDRDKEKRKEEKVRASGDAKIKKEKENGFSSPPQIKDEPEDDGYFVPPKEDIKPLKRPRDEDDADYKPKKIKTEDTKKEKKRKLEEEEDGKLK Function arises from the ordered state Molecular assembly Autoregulatory Disordered region is not essential for protein function Nuclear localization Protein-protein binding 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 Function arises from the disordered state Molecular assembly Autoregulatory Disordered region is not essential for protein function Nuclear localization Phosphorylation Protein-protein binding Paper 8567649 Bharti AK, Olson MO, Kufe DW, Rubin EH 1996 J Biol Chem 271 4 1993-1997 9611241 Labourier E, Rossi F, Gallouzi IE, Allemand E, Divita G, Tazi J 1998 Nucleic Acids Res 26 12 2955-2962 10380229 Shaiu WL, Hu T, Hsieh TS 1999 Pac Symp Biocomput 578-589 8631793 Stewart L, Ireton GC, Parker LH, Madden KR, Champoux JJ 1996 J Biol Chem 271 13 7593-7601 8631794 Stewart L, Ireton GC, Champoux JJ 1996 J Biol Chem 271 13 7602-7608 Charged residues contained within the interacting region of topo I/kinase (139 – 175) make electrostatic interactions with SF2/ASF (splice factor). Topo I/kinase phosphorylates at least six members of the SR protein family on serines contained in the RS domain of these proteins. Binding of SR proteins or other nuclear factors to DNA topoisomerase I may be a mechanism through which DNA topoisomerase I enters the nucleus. The N-terminal domain is highly extended and thereby accessible for specific interaction with other proteins. Human DNA topoisomerase I is a constitutively expressed nuclear phospho-protein that localizes to active transcription sites in which its kinase activity may allow this protein to participate in the coordination between transcription and splicing, since sites of transcription in the nucleus colocalize with sites of splicing. (Labourier, et al., 1998) Proposed functions of N-terminus include regulation of Topo I activity through the phosphorylation of the N-terminal domain, phosphorylation by a number of protein kinases, nuclear targeting (NLS), and possible protein-protein interactions between the Topo I N-terminus and other chromosomal proteins. Since this domain is flexible and extended, it may be proficient in providing an interacting surface to allow for binding with other proteins. A 44-residue segment in the human Topo I N-terminus can bind to an abundant nucleolar protein nucleolin. (Shaiu, et al.) The critical residues involved in nucleolin binding appear to be contained in the region of 166 – 210. Nucleolin binding to topo I may be the mechanism by which topo I enters the nucleus. While the 166 – 210 region of topo I does contain a NLS, the 140 – 167 and 1 – 139 regions of topo I also contain NLSs that do not bind nucleolin. (Bharti AK, et al.) Disordered - Extended 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 174 214 KKPKNKDKDKKVPEPDNKKKKPKKEEEQKWKWWEEERYPEG 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 9488652 Stewart L, Redinbo MR, Qiu X, Hol WG, Champoux JJ 1998 Science 279 5356 1534-1541 Disordered - Extended 627 659 AILCNHQRAPPKTFEKSMMNLQTKIDAKKEQLA Paper 9488652 Stewart L, Redinbo MR, Qiu X, Hol WG, Champoux JJ 1998 Science 279 5356 1534-1541 Disordered - Extended 636 659 PPKTFEKSMMNLQTKIDAKKEQLA Paper 9488644 Redinbo MR, Stewart L, Kuhn P, Champoux JJ, Hol WG 1998 Science 279 5356 1504-1153 Disordered - Extended 634 640 RAPPKTF Paper 10497031 Redinbo MR, Stewart L, Champoux JJ, Hol WG 1999 J Mol Biol 292 3 685-696 9488652 Stewart L, Redinbo MR, Qiu X, Hol WG, Champoux JJ 1998 Science 279 5356 1534-1541 Disordered - Extended 636 640 PPKTF Paper 9488652 Stewart L, Redinbo MR, Qiu X, Hol WG, Champoux JJ 1998 Science 279 5356 1534-1541 Disordered - Extended 628 635 ILCNHQRA Paper 9488644 Redinbo MR, Stewart L, Kuhn P, Champoux JJ, Hol WG 1998 Science 279 5356 1504-1153 Disordered - Extended 713 719 QIALGTS Paper 9488644 Redinbo MR, Stewart L, Kuhn P, Champoux JJ, Hol WG 1998 Science 279 5356 1504-1153 Disordered - Extended 711 716 NKQIAL Paper 9488652 Stewart L, Redinbo MR, Qiu X, Hol WG, Champoux JJ 1998 Science 279 5356 1534-1541 Disordered - Extended 715 719 ALGTS Paper 9488644 Redinbo MR, Stewart L, Kuhn P, Champoux JJ, Hol WG 1998 Science 279 5356 1504-1153 Disordered - Extended 636 712 PPKTFEKSMMNLQTKIDAKKEQLADARRDLKSAKADAKVMKDAKTKKVVESKKKAVQRLEEQLMKLEVQATDREENK Paper 10497031 Redinbo MR, Stewart L, Champoux JJ, Hol WG 1999 J Mol Biol 292 3 685-696 Disordered - Extended 627 632 AILCNH Paper 10497031 Redinbo MR, Stewart L, Champoux JJ, Hol WG 1999 J Mol Biol 292 3 685-696 Disordered - Extended 673 678 KVMKDA Paper 10497031 Redinbo MR, Stewart L, Champoux JJ, Hol WG 1999 J Mol Biol 292 3 685-696 Disordered - Extended 708 721 REENKQIALGTSKL Paper 10497031 Redinbo MR, Stewart L, Champoux JJ, Hol WG 1999 J Mol Biol 292 3 685-696 Disordered - Extended 712 718 KQIALGT Paper 10497031 Redinbo MR, Stewart L, Champoux JJ, Hol WG 1999 J Mol Biol 292 3 685-696 Disordered - Extended 620 633 NRANRAVAILCNHQ Paper 10497031 Redinbo MR, Stewart L, Champoux JJ, Hol WG 1999 J Mol Biol 292 3 685-696 Disordered - Extended 642 712 KSMMNLQTKIDAKKEQLADARRDLKSAKADAKVMKDAKTKKVVESKKKAVQRLEEQLMKLEVQATDREENK Paper 10497031 Redinbo MR, Stewart L, Champoux JJ, Hol WG 1999 J Mol Biol 292 3 685-696 Disordered - Extended 713 724 QIALGTSKLNYL Paper 10497031 Redinbo MR, Stewart L, Champoux JJ, Hol WG 1999 J Mol Biol 292 3 685-696 Disordered - Extended 634 641 RAPPKTFE Paper 10497031 Redinbo MR, Stewart L, Champoux JJ, Hol WG 1999 J Mol Biol 292 3 685-696 Disordered - Extended 626 721 VAILCNHQRAPPKTFEKSMMNLQTKIDAKKEQLADARRDLKSAKADAKVMKDAKTKKVVESKKKAVQRLEEQLMKLEVQATDREENKQIALGTSKL Paper 10497031 Redinbo MR, Stewart L, Champoux JJ, Hol WG 1999 J Mol Biol 292 3 685-696 Disordered - Extended 633 641 QRAPPKTFE Paper 10497031 Redinbo MR, Stewart L, Champoux JJ, Hol WG 1999 J Mol Biol 292 3 685-696 Disordered - Extended 626 632 VAILCNH Paper 10497031 Redinbo MR, Stewart L, Champoux JJ, Hol WG 1999 J Mol Biol 292 3 685-696 The loop leading up to His632 (residues 626 – 632) is disordered in four out of five structures A-E. His632 may stabilize the transition state of the scissile phosphorus atom that was exposed through nucleophilic attack by an activated C4-oxygen atom of Tyr723. DNA topoisomerase II EC 5.99.1.3 P06786 1351262 Saccharomyces cerevisiae (Baker's yeast) 1428 MSTEPVSASDKYQKISQLEHILKRPDTYIGSVETQEQLQWIYDEETDCMIEKNVTIVPGLFKIFDEILVNAADNKVRDPSMKRIDVNIHAEEHTIEVKNDGKGIPIEIHNKENIYIPEMIFGHLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTEFILETADLNVGQKYVQKWENNMSICHPPKITSYKKGPSYTKVTFKPDLTRFGMKELDNDILGVMRRRVYDINGSVRDINVYLNGKSLKIRNFKNYVELYLKSLEKKRQLDNGEDGAAKSDIPTILYERINNRWEVAFAVSDISFQQISFVNSIATTMGGTHVNYITDQIVKKISEILKKKKKKSVKSFQIKNNMFIFINCLIENPAFTSQTKEQLTTRVKDFGSRCEIPLEYINKIMKTDLATRMFEIADANEENALKKSDGTRKSRITNYPKLEDANKAGTKEGYKCTLVLTEGDSALSLAVAGLAVVGRDYYGCYPLRGKMLNVREASADQILKNAEIQAIKKIMGLQHRKKYEDTKSLRYGHLMIMTDQDHDGSHIKGLIINFLESSFPGLLDIQGFLLEFITPIIKVSITKPTKNTIAFYNMPDYEKWREEESHKFTWKQKYYKGLGTSLAQEVREYFSNLDRHLKIFHSLQGNDKDYIDLAFSKKKADDRKEWLRQYEPGTVLDPTLKEIPISDFINKELILFSLADNIRSIPNVLDGFKPGQRKVLYGCFKKNLKSELKVAQLAPYVSECTAYHHGEQSLAQTIIGLAQNFVGSNNIYLLLPNGAFGTRATGGKDAAAARYIYTELNKLTRKIFHPADDPLYKYIQEDEKTVEPEWYLPILPMILVNGAEGIGTGWSTYIPPFNPLEIIKNIRHLMNDEELEQMHPWFRGWTGTIEEIEPLRYRMYGRIEQIGDNVLEITELPARTWTSTIKEYLLLGLSGNDKIKPWIKDMEEQHDDNIKFIITLSPEEMAKTRKIGFYERFKLISPISLMNMVAFDPHGKIKKYNSVNEILSEFYYVRLEYYQKRKDHMSERLQWEVEKYSFQVKFIKMIIEKELTVTNKPRNAIIQELENLGFPRFNKEGKPYYGSPNDEIAEQINDVKGATSDEEDEESSHEDTENVINGPEELYGTYEYLLGMRIWSLTKERYQKLLKQKQEKETELENLLKLSAKDIWNTDLKAFEVGYQEFLQRDAEARGGNVPNKGSKTKGKGKRKLVDDEDYDPSKKNKKSTARKGKKIKLEDKNFERILLEQKLVTKSKAPTKIKKEKTPSVSETKTEEEENAPSSTSSSSIFDIKKEDKDEGELSKISNKFKKISTIFDKMGSTSATSKENTPEQDDVATKKNQTTAKKTAVKPKLAKKPVRKQQKVVELSGESDLEILDSYTDREDSNKDEDDAIPQRSRRQRSSRAASVPKKSYVETLELSDDSFIEDDEEENQGSDVSFNEED Disordered 410 420 NALKKSDGTRK Fragment 1BGWA Relationship to function unknown Unknown Unknown X-ray crystallography Paper 8538787 Berger JM, Gamblin SJ, Harrison SC, Wang JC 1996 Nature 379 6562 225-32 DP00076 - The experimental fragment was composed of residues 410 - 1202. Disordered 634 681 DKDYIDLAFSKKKADDRKEWLRQYEPGTVLDPTLKEIPISDFINKELI Fragment 1BGWA Relationship to function unknown Unknown Unknown X-ray crystallography Paper 8538787 Berger JM, Gamblin SJ, Harrison SC, Wang JC 1996 Nature 379 6562 225-32 DP00076 - The experimental fragment was composed of residues 410 - 1202. Disordered 1077 1107 EQINDVKGATSDEEDEESSHEDTENVINGPE Fragment 1BGWA Relationship to function unknown Unknown Unknown X-ray crystallography Paper 8538787 Berger JM, Gamblin SJ, Harrison SC, Wang JC 1996 Nature 379 6562 225-32 DP00076 - The experimental fragment was composed of residues 410 - 1202. Disordered 1179 1202 GNVPNKGSKTKGKGKRKLVDDEDY Fragment 1BGWA Relationship to function unknown Unknown Unknown X-ray crystallography Paper 8538787 Berger JM, Gamblin SJ, Harrison SC, Wang JC 1996 Nature 379 6562 225-32 DP00076 - The experimental fragment was composed of residues 410 - 1202. Disordered 485 489 SADQI Fragment Monomeric Native 1BJTA Function arises from the disordered state Unknown Unknown Paper 8538787 Berger JM, Gamblin SJ, Harrison SC, Wang JC 1996 Nature 379 6562 225-32 DP00076 - The experimental fragment was composed of residues 410 - 1202. Disordered 1072 1106 NDEIAEQINDVKGATSDEEDEESSHEDTENVINGP Fragment Monomeric Native 1BJTA Function arises from the disordered state Unknown Unknown Paper 8538787 Berger JM, Gamblin SJ, Harrison SC, Wang JC 1996 Nature 379 6562 225-32 DP00076 - The experimental fragment was composed of residues 410 - 1202. Disordered 527 531 QDHDG Fragment Monomeric Native 1BJTA Function arises from the disordered state Unknown Unknown Paper 8538787 Berger JM, Gamblin SJ, Harrison SC, Wang JC 1996 Nature 379 6562 225-32 DP00076 - The experimental fragment was composed of residues 410 - 1202. Disordered 631 652 QGNDKDYIDLAFSKKKADDRKE Fragment Monomeric Native 1BJTA Function arises from the disordered state Entropic chain Flexible linkers/spacers Paper 8538787 Berger JM, Gamblin SJ, Harrison SC, Wang JC 1996 Nature 379 6562 225-32 DP00076 - The experimental fragment was composed of residues 410 - 1202. Disordered 660 674 GTVLDPTLKEIPISD Fragment Monomeric Native 1BJTA Function arises from the disordered state Entropic chain Flexible linkers/spacers Unknown Paper 8538787 Berger JM, Gamblin SJ, Harrison SC, Wang JC 1996 Nature 379 6562 225-32 DP00076 - The experimental fragment was composed of residues 410 - 1202. Disordered 1179 1201 GNVPNKGSKTKGKGKRKLVDDED Fragment Monomeric Native 1BJTA Function arises from the disordered state Unknown Unknown Paper 8538787 Berger JM, Gamblin SJ, Harrison SC, Wang JC 1996 Nature 379 6562 225-32 DP00076 - The experimental fragment was composed of residues 410 - 1202. Disordered 1203 1428 DPSKKNKKSTARKGKKIKLEDKNFERILLEQKLVTKSKAPTKIKKEKTPSVSETKTEEEENAPSSTSSSSIFDIKKEDKDEGELSKISNKFKKISTIFDKMGSTSATSKENTPEQDDVATKKNQTTAKKTAVKPKLAKKPVRKQQKVVELSGESDLEILDSYTDREDSNKDEDDAIPQRSRRQRSSRAASVPKKSYVETLELSDDSFIEDDEEENQGSDVSFNEED Monomeric Native Function arises from the disordered state Unknown Unknown Paper Berger, J.M. Regulatory protein ADR1 Transcription factor ADR1 P07248 P07248 113450 A24534 Saccharomyces cerevisiae (Baker's yeast) 1323 MANVEKPNDCSGFPVVDLNSCFSNGFNNEKQEIEMETDDSPILLMSSSASRENSNTFSVIQRTPDGKIITTNNNMNSKINKQLDKLPENLRLNGRTPSGKLRSFVCEVCTRAFARQEHLKRHYRSHTNEKPYPCGLCNRCFTRRDLLIRHAQKIHSGNLGETISHTKKVSRTITKARKNSASSVKFQTPTYGTPDNGNFLNRTTANTRRKASPEANVKRKYLKKLTRRASFSAQSASSYALPDQSSLEQHPKDRVKFSTPELVPLDLKNPELDSSFDLNMNLDLNLNLDSNFNIALNRSDSSGSTMNLDYKLPESANNYTYSSGSPTRAYVGANTNSKNASFNDADLLSSSYWIKAYNDHLFSVSESDETSPMNSELNDTKLIVPDFKSTIHHLKDSRSSSWTVAIDNNSNNNKVSDNQPDFVDFQELLDNDTLGNDLLETTAVLKEFELLHDDSVSATATSNEIDLSHLNLSNSPISPHKLIYKNKEGTNDDMLISFGLDHPSNREDDLDKLCNMTRDVQAIFSQYLKGEESKRSLEDFLSTSNRKEKPDSGNYTFYGLDCLTLSKISRALPASTVNNNQPSHSIESKLFNEPMRNMCIKVLRYYEKFSHDSSESVMDSNPNLLSKELLMPAVSELNEYLDLFKNNFLPHFPIIHPSLLDLDLDSLQRYTNEDGYDDAENAQLFDRLSQGTDKEYDYEHYQILSISKIVCLPLFMATFGSLHKFGYKSQTIELYEMSRRILHSFLETKRRCRSTTVNDSYQNIWLMQSLILSFMFALVADYLEKIDSSLMKRQLSALCSTIRSNCLPTISANSEKSINNNNEPLTFGSPLQYIIFESKIRCTLMAYDFCQFLKCFFHIKFDLSIKEKDVETIYIPDNESKWASESIICNGHVVQKQNFYDFRNFYYSFTYGHLHSIPEFLGSSMIYYEYDLRKGTKSHVFLDRIDTKRLERSLDTSSYGNDNMAATNKNIAILIDDTIILKNNLMSMRFIKQIDRSFTEKVRKGQIAKIYDSFLNSVRLNFLKNYSVEVLCEFLVALNFSIRNISSLYVEEESDCSQRMNSPELPRIHLNNQALSVFNLQGYYYCFILIIKFLLDFEATPNFKLLRIFIELRSLANSILLPTLSRLYPQEFSGFPDVVFTQQFINKDNGMLVPGLSANEHHNGASAAVKTKLAKKINVEGLAMFINEILVNSFNDTSFLNMEDPIRNEFSFDNGHRAVTDLPRSAHFLSDTGLEGINFSGLNDSHQTVSTLNLLRYGENHSSKHKNGGKGQGFAEKYQLSLKYVTIAKLFFTNVKENYIHCHMLDKMASDFHTLENHLKGNS Disordered - Extended 75 104 MNSKINKQLDKLPENLRLNGRTPSGKLRSF Engineered 1ADRA 2ADRA Function arises via a disorder to order transition Molecular assembly Protein-DNA binding Nuclear magnetic resonance (NMR) 310 6.8 Nuclear magnetic resonance (NMR) 288 6.1 Nuclear magnetic resonance (NMR) 290 6.3 Paper 9642072 Hyre, D. E. Klevit, R. E. 1998 Journal of Molecular Biology 279 4 929-943 3515197 Hartshorne, T. A. Blumberg, H. Young, E. T. 1986 Nature 320 6059 283-287 Disordered - Extended 155 161 HSGNLGE Engineered Function arises via a disorder to order transition Molecular assembly Protein-DNA binding Nuclear magnetic resonance (NMR) 310 6.8 Nuclear magnetic resonance (NMR) 288 6.1 Nuclear magnetic resonance (NMR) 290 6.3 Paper 9642072 Hyre, D. E. Klevit, R. E. 1998 Journal of Molecular Biology 279 4 929-943 3515197 Hartshorne, T. A. Blumberg, H. Young, E. T. 1986 Nature 320 6059 283-287 c-fos Cellular oncogene fos G0/G1 switch regulatory protein 7 Proto-oncogene protein c-fos Transcription factor c-Fos P01100 Hs.25647 P01100 4885241 TVHUF1 Homo sapiens (Human) 380 MMFSGFNADYEASSSRCSSASPAGDSLSYYHSPADSFSSMGSPVNAQDFCTDLAVSSANFIPTVTAISTSPDLQWLVQPALVSSVAPSQTRAPHPFGVPAPSAGAYSRAGVVKTMTGGRAQSIGRRGKVEQLSPEEEEKRRIRRERNKMAAAKCRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEKLEFILAAHRPACKIPDDLGFPEEMSVASLDLTGGLPEVATPESEEAFTLPLLNDPEPKPSVEPVKSISSMELKTEPFDDFLFPASSRPSGSETARSVPDMDLSGSFYAADWEPLHSGSLGMGPMATELEPLCTPVVTCTPSCTAYTSSFVFTYPEADSFPSCAAAHRKGSSSNEPSSDSLSSPTLLAL Disordered - Extended FosAD - Fragment 216 380 MSVASLDLTGGLPEVATPESEEAFTLPLLNDPEPKPSVEPVKSISSMELKTEPFDDFLFPASSRPSGSETARSVPDMDLSGSFYAADWEPLHSGSLGMGPMATELEPLCTPVVTCTPSCTAYTSSFVFTYPEADSFPSCAAAHRKGSSSNEPSSDSLSSPTLLAL Fragment Function arises via a disorder to order transition Molecular assembly Autoregulatory Protein-protein binding Near-UV circular dichroism (CD) spectroscopy DTT 1 NaCl 1 sodium phosphate 10 Nuclear magnetic resonance (NMR) 298 d₁₀-DTT 1 NaCl 150 sodium phosphate 10 Gel filtration/size exclusion chromatography DTT 1 NaCl 150 sodium phosphate 10 Paper 10704222 Campbell KM, Terrell AR, Laybourn PJ, Lumb KJ 2000 Biochemistry 39 10 2708-2713 11749217 Flaugh SL, Lumb KJ 2001 Biomacromolecules 2 2 538-540 Helical or beta-sheet structure is not induced in Fos-AD by changes in pH or ionic strength. Chemical shift data indicated that Fos-AD lacked the stable secondary or tertiary structure normally found with globular proteins. Fos-AD has a Stokes’ radius that is twice that of a compact globular protein (35Å compared to 17Å) indicating that Fos-AD is unfolded, and sedimentation equilibrium indicated that Fos-AD is monomeric. Negative amide NOEs indicate that the main chain of Fos-AD is highly flexible and exists in a motional system expected for an unfolded protein.

It has been shown that the active acidic and proline-rich C-terminal activation domain of human c-Fos is structurally disordered and has the properties of an unfolded protein. It was found that disorder was not due to the deletion of a sequence necessary for structure. Structural disorder has also been found with the acidic activation domains from VP16, κB, and p53. Results for c-Fos and for the p53 proline-rich activation domain have indicated that proline-rich activation domains can exhibit structural disorder. Proposed mechanistic advantages of these disordered protein domains include increased binding specificity at the expense of thermodynamic stability, regulation of proteolysis, and the ability to recognize a range of different proteins. The C-terminal activation domain contains a number of phosphorylation sites that moderate Fos activity. The conformational freedom of the structurally disordered C-terminal activation domain contributes to the functional diversity of c-Fos by allowing the formation of numerous protein complexes (with transcription factors and with regulatory kinases).

Estrogen receptor beta ER-beta Q92731 6166154 Homo sapiens (Human) 530 MDIKNSPSSLNSPSSYNCSQSILPLEHGSIYIPSSYVDSHHEYPAMTFYSPAVMNYSIPSNVTNLEGGPGRQTTSPNVLWPTPGHLSPLVVHRQLSHLYAEPQKSPWCEARSLEHTLPVNRETLKRKVSGNRCASPVTGPGSKRDAHFCAVCSDYASGYHYGVWSCEGCKAFFKRSIQGHNDYICPATNQCTIDKNRRKSCQACRLRKCYEVGMVKCGSRRERCGYRLVRRQRSADEQLHCAGKAKRSGGHAPRVRELLLDALSPEQLVLTLLEAEPPHVLISRPSAPFTEASMMMSLTKLADKELVHMISWAKKIPGFVELSLFDQVRLLESCWMEVLMMGLMWRSIDHPGKLIFAPDLVLDRDEGKCVEGILEIFDMLLATTSRFRELKLQHKEYLCVKAMILLNSSMYPLVTATQDADSSRKLAHLLNAVTDALVWVIAKSGISSQQQSMRLANLLMLLSHVRHASNKGMEHLLNMKCKNVVPVYDLLLEMLNAHVLRGCKSSITGSECSPAEDSKSKEGSQNPQSQ Disordered 1 103 MDIKNSPSSLNSPSSYNCSQSILPLEHGSIYIPSSYVDSHHEYPAMTFYSPAVMNYSIPSNVTNLEGGPGRQTTSPNVLWPTPGHLSPLVVHRQLSHLYAEPQ Fragment Relationship to function unknown Protein-protein binding Substrate/ligand binding Nuclear magnetic resonance (NMR) 283 6.5 Sodium azide 0.01% Sodium phosphate 20 Far-UV circular dichroism (CD) 298 6 Sodium azide 15 Sodium phosphate 10 Paper 11595744 Warnmark A, Wikstrom A, Wright AP, Gustafsson JA, Hard T 2001 J Biol Chem 276 49 45939-44 The fragment consisted of residues 1-103. CREB cAMP response element binding Creb-1 P15337 Rn.90061 P15337 117435 Rattus norvegicus 341 MTMESGAENQQSGDAAVTEAENQQMTVQAQPQIATLAQVSMPAAHATSSAPTVTLVQLPNGQTVQVHGVIQAAQPSVIQSPQVQTVQSSCKDLKRLFSGTQISTIAESEDSQESVDSVTDSQKRREILSRRPSYRKILNDLSSDAPGVPRIEEEKSEEETSAPAITTVTVPTPIYQTSSGQYIAITQGGAIQLANNGTDGVQGLQTLTMTNAAATQPGTTILQYAQTTDGQQILVPSNQVVVQAASGDVQTYQIRTAPTSTIAPGVVMASSPALPTQPAEEAARKREVRLMKNREAARECRRKKKEYVKCLENRVAVLENQNKTLIEELKALKDLYCHKSD Disordered pKID 101 120 QISTIAESEDSQESVDSVTD Engineered Fragment 1KDXB Function arises from the disordered state Unknown Unknown Nuclear magnetic resonance (NMR) 315 5.5 acetate-d buffer guanidinium hydrochloride solubilization 0.6 NaCl salt, buffer 50 Tris-d buffer 20 Nuclear magnetic resonance (NMR) 290 5.5 acetate-d buffer guanidinium hydrochloride solubilization 0.6 NaCl salt, buffer 50 Tris-d buffer 20 Paper 9413984 Radhakrishnan I, Perez-Alvarado GC, Parker D, Dyson HJ, Montminy MR, Wright PE 1997 Cell 91 6 741-752 Upon binding to the KIX domain of the CREB binding protein this region remains disordered. The PDB reference 1KDX chain B has the disordered region from residues 101-118. Disordered pKID 119 146 TDSQKRREILSRRPSYRKILNDLSSDAP Engineered Fragment 1KDXB Function arises via a disorder to order transition Molecular assembly Protein-protein binding Nuclear magnetic resonance (NMR) 315 5.5 acetate-d buffer guanidinium hydrochloride solubilization 0.6 NaCl salt, buffer 50 Tris-d buffer 20 Nuclear magnetic resonance (NMR) 290 5.5 acetate-d buffer guanidinium hydrochloride solubilization 0.6 NaCl salt, buffer 50 Tris-d buffer 20 Paper 9413984 Radhakrishnan I, Perez-Alvarado GC, Parker D, Dyson HJ, Montminy MR, Wright PE 1997 Cell 91 6 741-752 9688563 Radhakrishnan I, Perez-Alvarado GC, Dyson HJ, Wright PE 1998 FEBS Lett 430 3 317-322 Upon binding to the KIX domain of the CREB binding protein this region forms two alpha helices, alphaA and alphaB. The two fold into mutually perpendicular helices that run from Asp-120 to Ser-129 and Pro-132 to Asp-144, respectively. Disordered pKID 146 160 PGVPRIEEEKSEEET Engineered Fragment 1KDXB Function arises from the disordered state Unknown Unknown Nuclear magnetic resonance (NMR) 315 5.5 acetate-d buffer guanidinium hydrochloride solubilization 0.6 NaCl salt, buffer 50 Tris-d buffer 20 Nuclear magnetic resonance (NMR) 290 5.5 acetate-d buffer guanidinium hydrochloride solubilization 0.6 NaCl salt, buffer 50 Tris-d buffer 20 Paper 9413984 Radhakrishnan I, Perez-Alvarado GC, Parker D, Dyson HJ, Montminy MR, Wright PE 1997 Cell 91 6 741-752 Upon binding to the KIX domain of the CREB binding protein this region remains unstructured. The PDB reference 1KDX chain B has the disordered region from residues 147-160. Transcription initiation factor TFIID subunit 1 P230 TAFII-230 TAFII250 TBP-associated factor 230 kDa Transcription factor dTAFII230 Transcription initiation factor TFIID 230 kDa subunit P51123 27924000 Drosophila melanogaster (Fruit fly) 2068 MEMESDNSDDEGSIGNGLDLTGILFGNIDSEGRLLQDDDGEGRGGTGFDAELRENIGSLSKLGLDSMLLEVIDLKEAEPPSDDEEEEDARPSAVSASGGMSAFDALKAGVKREEREDGAVKAQDDAIDYSDITELSEDCPRTPPEETSTYDDLEDAIPASKVEAKLTKDDKELMPPPSAPMRSGSGGGIEEPAKSNDASSPSDDSKSTDSKDADRKLDTPLADILPSKYQNVDVRELFPDFRPQKVLRFSRLFGPGKPTSLPQIWRHVRQSRRKRNQSRDQKTTNTGGSDSPSDTEEPRKRGFSLHYAAEPTPAECMSDDEDKLLGDFNSEDVRPEGPDNGENSDQKPKVADWRFGPAQIWYDILEVPDSGEGFNYGFKTKAASTSSQQQLKDERRVKSPEDDVEDPSIADDAFLMVSQLHWEDDVVWDGNDIKAKVLQKLNSKTNAAGWLPSSGSRTAGAFSQPGKPSMPVGSGSSKQGSGASSKKAQQNAQAKPAEAPDDTWYSLFPVENEELIYYKWEDEVIWDAQQVSKVPKPKVLTLDPNDENIILGIPDDIDPSKINKSTGPPPKIKIPHPHVKKSKILLGKAGVINVLAEDTPPPPPKSPDRDPFNISNDTYYTPKTEPTLRLKVGGNLIQHSTPVVELRAPFVPTHMGPMNVRAFHRPPLKKYSHGPMAQSIPHPVFPLLKTIAKKAKQREVERIASGGGDVFFMRNPEDLSGRDGDIVLAEFCEEHPPLINQVGMCSKIKNYYKRKAEKDSGPQDYVYGEVAFAHTSPFLGILHPGQCIQAIENNMYRAPIYPHKMAHNDFLVIRTRNNYWIRSVNSIYTVGQECPLYEVPGPNSKRANNFTRDFLQVFIYRLFWKSRDNPRRIRMDDIKQAFPAHSESSIRKRLKQCADFKRTGMDSNWWVIKPEFRLPSEEEIRAMVSPEQCCAYFSMIAAEQRLKDAGYGEKFLFAPQEDDDEEAQLKLDDEVKVAPWNTTRAYIQAMRGKCLLQLSGPADPTGCGEGFSYVRVPNKPTQTKEEQESQPKRSVTGTDADLRRLPLQRAKELLRQFKVPEEEIKKLSRWEVIDVVRTLSTEKAKAGEEGMDKFSRGNRFSIAEHQERYKEECQRIFDLQNRVLASSEVLSTDEAESSASEESDLEELGKNLENMLSNKKTSTQLSREREELERQELLRQLDEEHGGPSGSGGAKGAKGKDDPGQQMLATNNQGRILRITRTFRGNDGKEYTRVETVRRQPVIDAYIKIRTTKDEQFIKQFATLDEQQKEEMKREKRRIQEQLRRIKRNQERERLAQLAQNQKLQPGGMPTSLGDPKSSGGHSHKERDSGYKEVSPSRKKFKLKPDLKLKCGACGQVGHMRTNKACPLYSGMQSSLSQSNPSLADDFDEQSEKEMTMDDDDLVNVDGTKVTLSSKILKRHGGDDGKRRSGSSSGFTLKVPRDAMGKKKRRVGGDLHCDYLQRHNKTANRRRTDPVVVLSSILEIIHNELRSMPDVSPFLFPVSAKKVPDYYRVVTKPMDLQTMREYIRQRRYTSREMFLEDLKQIVDNSLIYNGPQSAYTLAAQRMFSSCFELLAEREDKLMRLEKAINPLLDDDDQVALSFIFDKLHSQIKQLPESWPFLKPVNKKQVKDYYTVIKRPMDLETIGKNIEAHRYHSRAEYLADIELIATNCEQYNGSDTRYTKFSKKILEYAQTQLIEFSEHCGQLENNIAKTQERARENAPEFDEAWGNDDYNFDRGSRASSPGDDYIDVEGHGGHASSSNSIHRSMGAEAGSSHTAPAVRKPAPPGPGEVKRGRGRPRKQRDPVEEDLQCSTDDEDDDEEEDFQEVSEDENNAASILDQGERINAPADAMDGMFDPKNIKTEIDLEAHQMADESMDVDPNYDPSDFLAMHKQRQSLGEPSSLQGAFTNFLSHEQDDNGPYNPAEASTSAASGADLGMDASMAMQMAPEMPVNTMNNGMGIDDDLDISESDEEDDGSRVRIKKEVFDDGDYALQHQQMGQAASQSQIYMVDSSNEPTTLDYQQPPQLDFQQVQEMEQLQHQVMPPMQSEQLQQQQTPQGDNDYAWTF Disordered 11 77 EGSIGNGLDLTGILFGNIDSEGRLLQDDDGEGRGGTGFDAELRENIGSLSKLGLDSMLLEVIDLKEA Fragment 1TBAA Function arises via a disorder to order transition Protein-protein binding Paper 9741622 Liu D, Ishima R, Tong KI, Bagby S, Kokubo T, Muhandiram DR, Kay LE, Nakatani Y, Ikura M 1998 Cell 94 5 573-583 Eukaryotic initiation factor 4F subunit p150 Cap-binding protein complex TIF4631 eIF-4F p150 eIF4F p150 eIF4 gamma mRNA cap-binding protein complex subunit p150 Protein G7036 Protein YGR162w Translation initiation factor eIF-4F TIF4631 P39935 P39935 6321601 S64473 Saccharomyces cerevisiae (Baker's yeast) 952 MTDETAHPTQSASKQESAALKQTGDDQQESQQQRGYTNYNNGSNYTQKKPYNSNRPHQQRGGKFGPNRYNNRGNYNGGGSFRGGHMGANSSNVPWTGYYNNYPVYYQPQQMAAAGSAPANPIPVEEKSPVPTKIEITTKSGEHLDLKEQHKAKLQSQERSTVSPQPESKLKETSDSTSTSTPTPTPSTNDSKASSEENISEAEKTRRNFIEQVKLRKAALEKKRKEQLEGSSGNNNIPMKTTPENVEEKGSDKPEVTEKTKPAEEKSAEPEVKQETPAEEGEQGEKGQIKEESTPKVLTFAERLKLKKQQKEREEKTEGKENKEVPVQEETKSAIESAPVPPSEQVKEETEVAETEQSNIDESATTPAIPTKSDEAEAEVEAEAGDAGTKIGLEAEIETTTDETDDGTNTVSHILNVLKDATPIEDVFSFNYPEGIEGPDIKYKKEHVKYTYGPTFLLQFKDKLNVKADAEWVQSTASKIVIPPGMGRGNRSRDSGRFGNNSSRGHDFRNTSVRNMDDRANSRTSSKRRSKRMNDDRRSNRSYTSRRDRERGSYRNEEKREDDKPKEEVAPLVPSANRWVPKFKSKKTEKKLAPDGKTELLDKDEVERKMKSLLNKLTLEMFDAISSEILAIANISVWETNGETLKAVIEQIFLKACDEPHWSSMYAQLCGKVVKELNPDITDETNEGKTGPKLVLHYLVARCHAEFDKGWTDKLPTNEDGTPLEPEMMSEEYYAAASAKRRGLGLVRFIGFLYRLNLLTGKMMFECFRRLMKDLTDSPSEETLESVVELLNTVGEQFETDSFRTGQATLEGSQLLDSLFGILDNIIQTAKISSRIKFKLIDIKELRHDKNWNSDKKDNGPKTIQQIHEEEERQRQLKNNSRSNSRRTNNSSNRHSFRRDAPPASKDSFITTRTYSQRNSQRAPPPKEEPAAPTSTATNMFSALMGESDDEE Disordered - Extended 393 490 LEAEIETTTDETDDGTNTVSHILNVLKDATPIEDVFSFNYPEGIEGPDIKYKKEHVKYTYGPTFLLQFKDKLNVKADAEWVQSTASKIVIPPGMGRGN Complex Fragment Function arises via a disorder to order transition Molecular assembly Flexible linkers/spacers Protein-protein binding Aberrant mobility on SDS-PAGE gel Nuclear magnetic resonance (NMR) 299 7.5 Sensitivity to proteolysis Paper 10409688 Hershey PE, McWhirter SM, Gross JD, Wagner G, Alber T, Sachs AB 1999 J Biol Chem 274 30 21297-304 General control protein GCN4 Amino acid biosynthesis regulatory protein Transcription factor GCN4 P03069 121066 RGBYA2 Saccharomyces cerevisiae (Baker's yeast) 281 MSEYQPSLFALNPMGFSPLDGSKSTNENVSASTSTAKPMVGQLIFDKFIKTEEDPIIKQDTPSNLDFDFALPQTATAPDAKTVLPIPELDDAVVESFFSSSTDSTPMFEYENLEDNSKEWTSLFDNDIPVTTDDVSLADKAIESTEEVSLVPSNLEVSTTSFLPTPVLEDAKLTQTRKVKKPNSVVKKSHHVGKDDESRLDHLGVVAYNRKQRSIPLSPIVPESSDPAALKRARNTEAARRSRARKLQRMKQLEDKVEELLSKNYHLENEVARLKKLVGER Disordered 225 281 SDPAALKRARNTEAARRSRARKLQRMKQLEDKVEELLSKNYHLENEVARLKKLVGER Paper 2145515 Weiss MA, Ellenberger T, Wobbe CR, Lee JP, Harrison SC, Struhl K 1990 Nature 347 6293 575-8 Max protein Myc associated factor X P25912 47117704 Homo sapiens (Human) 160 MSDNDDIEVESDEEQPRFQSAADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQVRALEKARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQSRKKLRMEAS Disordered 1 110 MSDNDDIEVESDEEQPRFQSAADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQVRALEKARSSAQ Paper 9399572 Horiuchi M, Kurihara Y, Katahira M, Maeda T, Saito T, Uesugi S 1997 J Biochem (Tokyo) 122 4 711-6 The experimental sequence consisted of the first 110 residues of Max. p21 Max MAX protein, isoform 2 MAX protein isoform b Myc associated factor X 21704263 Homo sapiens (Human) 151 MSDNDDIEVESDADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQVRALEKARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQSRKKLRMEAS Disordered N-terminal 1 12 MSDNDDIEVESD Engineered Function arises from the disordered state Unknown Unknown Nuclear magnetic resonance (NMR) 308 6.8 D2O 10 DSS KCl 100 NaN3 50 Phosphate 50 Far-UV circular dichroism (CD) 293 6.8 KCl 100 Sodium Phosphate 50 Paper 16171389 Naud JF, McDuff FO, Sauve S, Montagne M, Webb BA, Smith SP, Chabot B, Lavigne P 2005 Biochemistry 44 38 12746-12758 Disordered C-terminal 95 151 KARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQSRKKLRMEAS Engineered Function arises from the disordered state Unknown Unknown Nuclear magnetic resonance (NMR) 308 6.8 D2O 10 DSS KCl 100 NaN3 50 Phosphate 50 Far-UV circular dichroism (CD) 293 6.8 KCl 100 Sodium Phosphate 50 Paper 16171389 Naud JF, McDuff FO, Sauve S, Montagne M, Webb BA, Smith SP, Chabot B, Lavigne P 2005 Biochemistry 44 38 12746-12758 This is isoform 2 of MAX protein(SwissProt: P61244). Transcription factor p65 Nuclear factor NF-kappa-B p65 subunit Transcription factor NF-kappa B p65 Q04206 Q04206 46430499 A40851 Homo sapiens 551 MDELFPLIFPAEPAQASGPYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINGYTGPGTVRISLVTKDPPHRPHPHELVGKDCRDGFYEAELCPDRCIHSFQNLGIQCVKKRDLEQAISQRIQTNNNPFQVPIEEQRGDYDLNAVRLCFQVTVRDPSGRPLRLPPVLPHPIFDNRAPNTAELKICRVNRNSGSCLGGDEIFLLCDKVQKEDIEVYFTGPGWEARGSFSQADVHRQVAIVFRTPPYADPSLQAPVRVSMQLRRPSDRELSEPMEFQYLPDTDDRHRIEEKRKRTYETFKSIMKKSPFSGPTDPRPPPRRIAVPSRSSASVPKPAPQPYPFTSSLSTINYDEFPTMVFPSGQISQASALAPAPPQVLPQAPAPAPAPAMVSALAQAPAPVPVLAPGPPQAVAPPAPKPTQAGEGTLSEALLQLQFDDEDLGALLGNSTDPAVFTDLASVDNSEFQQLLNQGIPVAPHTTEPMLMEYPEAITRLVTGAQRPPDPAPAPLGAPGLPNGLLSGDEDFSSIADMDFSALLSQISS Disordered - Extended Transactivation domain 1 (TA1) 522 551 GLPNGLLSGDEDFSSIADMDFSALLSQISS Function arises via a disorder to order transition Modification site Molecular assembly Autoregulatory Protein-protein binding Transactivation (transcriptional activation) Far-UV circular dichroism (CD) 293 quartz cells (1 mm path length) Nuclear magnetic resonance (NMR) 5.5 10% D₂O 90% H₂O NaCl 50 protein 2 sodium phosphate 50 Paper 1935902 Schmitz ML, Baeuerle PA 1991 Embo J 10 12 3805-3817 7929265 Schmitz ML, dos Santos Silva MA, Altmann H, Czisch M, Holak TA, Baeuerle PA 1994 J Biol Chem 269 41 25613-25620 CD and NMR spectra revealed that TA1 exists in aqueous solution at physiological pH in a random coil conformation or is unstructured. The acidic activation domians of p65 TA1 are all capable of forming an alpha-helix in hydrophobic solvents. In an aqueous solution, negatively charged amino acids might prevent formation of a secondary structure due to electrostatic repulsion and/or steric hindrance imposed by hydrate shells. A transition of positively charged random coil sequence into an alpha-helical structure has been reported to occur when leucine zipper proteins contact DNA with their basic domains. (Schmitz 1994) Domains of the p65 molecule required for initiating transcription were subjected to deletion analysis. Removal of only 30 amino acids from the C-terminus of p65 reduced the transactivating potential of p65, whereas removal of 250 amino acids from the C-terminus completely negated the transactivating potential. A feature of TA1 appears to be the clustering of serine residues on one side of an alleged amphipathic helix, in which the serine residues may be involved in a zipper-like structure serving a role in protein-protein interaction as has been proposed for leucine repeats. Ser529 and Ser536 are important for inhibiting NF-κB activation, and phosphorylation of these residues is essential for NF-κB activation. Disordered - Extended Transactivation domain 2 (TA2) 441 518 LQLQFDDEDLGALLGNSTDPAVFTDLASVDNSEFQQLLNQGIPVAPHTTEPMLMEYPEAITRLVTGAQRPPDPAPAPL Function arises via a disorder to order transition Molecular assembly Protein-protein binding Transactivation (transcriptional activation) Nuclear magnetic resonance (NMR) 5.5 10% D₂O 90% H₂O NaCl 50 sodium phosphate 50 Paper 1935902 Schmitz ML, Baeuerle PA 1991 Embo J 10 12 3805-3817 7929265 Schmitz ML, dos Santos Silva MA, Altmann H, Czisch M, Holak TA, Baeuerle PA 1994 J Biol Chem 269 41 25613-25620 NMR spectra revealed that TA2 exists in aqueous solution at physiological pH in a random coil conformation or is unstructured. NMR analysis the C-terminal 123 amino acids showed a random coil conformation, which indicates that the entire transactivating C-terminus is unstructured. C-terminal deletion of the TA2 domain causes a gradual loss in transactivating activity. (Schmitz 1991). A region within TA2 homologous to TA1 is referred to as TA’1. TA’1 is necessary for the activity of TA2 because any deletion affecting the integrity of TA’1 leads to a decrease in the ability of TA2 to stimulate transcription. TA2 activity might also be dependent upon a leucine zipper, but this needs to be studied further. (Schmitz 1995). Disordered - Extended TA1 and TA2 plus mini leucine zipper (C-terminal region) 429 551 TQAGEGTLSEALLQLQFDDEDLGALLGNSTDPAVFTDLASVDNSEFQQLLNQGIPVAPHTTEPMLMEYPEAITRLVTGAQRPPDPAPAPLGAPGLPNGLLSGDEDFSSIADMDFSALLSQISS Fragment Function arises via a disorder to order transition Modification site Molecular assembly Protein-protein binding Transactivation (transcriptional activation) Nuclear magnetic resonance (NMR) 5.5 10% D₂O 90% H₂O NaCl 50 sodium phosphate 50 Paper 7929265 Schmitz ML, dos Santos Silva MA, Altmann H, Czisch M, Holak TA, Baeuerle PA 1994 J Biol Chem 269 41 25613-25620 NMR analysis of a protein corresponding to the C-terminal 123 amino acids showed a random coil conformation, which indicates that the entire transactivating C-terminus is unstructured. Cellular tumor antigen p53 antigen NY-CO-13 cellular phosphoprotein p53 oncoprotein p53 phosphoprotein p53 transformation suppressor tumor suppressor p53 P04637 Hs.408312 P04637 189476 Homo sapiens (Human) 393 MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD Disordered - Extended 1 73 MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPV Engineered Fragment Function arises from the disordered state Molecular recognition effectors Unknown Near-UV circular dichroism (CD) spectroscopy 6.1 Phosphate Buffer TFE Paper 7559631 Chang J, Kim DH, Lee SW, Choi KY, Sung YC 1995 J Biol Chem 270 42 25014-9 This disordered region was discovered in an engineered fragment containing residues 1-73. Disordered - Extended 15 16 SQ Complex Engineered Fragment Function arises from the disordered state Unknown Unknown X-ray crystallography 308 MDM2 Paper 8875929 Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP 1996 Science 274 5289 948-53 This disordered region was discovered in an engineered fragment containing residues 15-29. Disordered - Extended 27 29 PEN Complex Engineered Fragment Function arises from the disordered state Unknown Unknown X-ray crystallography 308 MDM2 Paper 8875929 Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP 1996 Science 274 5289 948-53 The protein studied was an engineered fragment containing residues 15-29. Disordered - Extended 183 188 SDSDGL Engineered Fragment 1GZHA Relationship to function unknown Unknown Unknown X-ray crystallography PDB 12351827 Derbyshire DJ, Basu BP, Date T, Iwabuchi K, Doherty AJ 2002 Acta Crystallogr D Biol Crystallogr 58 Pt 10 Pt 2 1826-9 12110597 Derbyshire DJ, Basu BP, Serpell LC, Joo WS, Date T, Iwabuchi K, Doherty AJ 2002 Embo J 21 14 3863-72 The disordered region characterized was studied in an engineered fragment containing residues 95-292. Disordered - Extended 200 200 N Engineered Fragment 1GZHA Relationship to function unknown Unknown Unknown X-ray crystallography PDB 12351827 Derbyshire DJ, Basu BP, Date T, Iwabuchi K, Doherty AJ 2002 Acta Crystallogr D Biol Crystallogr 58 Pt 10 Pt 2 1826-9 12110597 Derbyshire DJ, Basu BP, Serpell LC, Joo WS, Date T, Iwabuchi K, Doherty AJ 2002 Embo J 21 14 3863-72 The disordered region characterized was studied in an engineered fragment containing residues 95-292. Disordered - Extended 224 227 EVGS Engineered Fragment 1GZHA Relationship to function unknown Unknown Unknown X-ray crystallography PDB 12351827 Derbyshire DJ, Basu BP, Date T, Iwabuchi K, Doherty AJ 2002 Acta Crystallogr D Biol Crystallogr 58 Pt 10 Pt 2 1826-9 12110597 Derbyshire DJ, Basu BP, Serpell LC, Joo WS, Date T, Iwabuchi K, Doherty AJ 2002 Embo J 21 14 3863-72 The disordered region characterized was studied in an engineered fragment containing residues 95-292. Disordered - Extended 291 312 KKGEPHHELPPGSTKRALPNNT Engineered Fragment Mutant 1OULA 1OULB Relationship to function unknown Unknown Unknown X-ray crystallography Paper 14534297 Joerger AC, Allen MD, Fersht AR 2004 J Biol Chem 279 2 1291-6 The disordered region characterized was from an engineered fragment containing residues 94-312 and mutations at M133L, V203A, N239Y, N268D. Disordered - Extended 319 323 KKKPL Engineered Fragment 1OLGA 1OLHA 1SAEA 1SAEB 1SAEC 1SAED 1SAFA 1SAFB 1SAFC 1SAFD 1SAGA 1SAGB 1SAGC 1SAGD 1SAHA 1SAHB 1SAHC 1SAHD 1SAIA 1SAIB 1SAIC 1SAID 1SAKA 1SAKB 1SAKC 1SAKD 1SALA 1SALB 1SALC 1SALD 3SAKA 3SAKB 3SAKC 3SAKD Function arises from the disordered state Unknown Unknown Nuclear magnetic resonance (NMR) Paper Kuszewski J, Gronenborn AM, Clore GM 1999 Journal of the American Chemicial Society 121 10 2337-2338 Disordered - Extended 357 360 KEPG Engineered Fragment 1OLGA 1OLHA 1SAEA 1SAEB 1SAEC 1SAED 1SAFA 1SAFB 1SAFC 1SAFD 1SAGA 1SAGB 1SAGC 1SAGD 1SAHA 1SAHB 1SAHC 1SAHD 1SAIA 1SAIB 1SAIC 1SAID 1SAKA 1SAKB 1SAKC 1SAKD 1SALA 1SALB 1SALC 1SALD 3SAKA 3SAKB 3SAKC 3SAKD Function arises from the disordered state Unknown Unknown Nuclear magnetic resonance (NMR) Paper Kuszewski J, Gronenborn AM, Clore GM 1999 Journal of the American Chemicial Society 121 10 2337-2338 This disordered region was located in an engineered fragment containing residues 319-360. Alpha trans-inducing protein ALPHA-TIF ICP25 Transcription factor VP16 VMW65 VP16 PROTEIN P23990 55584017 Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2) 490 MDLLVDDLFADADGVSPPPPRPAGGPKNTPAAPPLYATGRLSQAQLMPSPPMPVPPAALFNRLLDDLGFSAGPALCTMLDTWNEDLFSGFPTNADMYRECKFLSTLPSDVIDWGDAHVPERSPIDIRAHGDVAFPTLPATRDELPSYYEAMAQFFRGELRAREESYRTVLANFCSALYRYLRASVRQLHRQAHMRGRNRDLREMLRTTIADRYYRETARLARVLFLHLYLFLSREILWAAYAEQMMRPDLFDGLCCDLESWRQLACLFQPLMFINGSLTVRGVPVEARRLRELNHIREHLNLPLVRSAAAEEPGAPLTTPPVLQGNQARSSGYFMLLIRAKLDSYSSVATSEGESVMREHAYSRGRTRNNYGSTIEGLLDLPDDDDAPAEAGLVAPRMSFLSAGQRPRRLSTTAPITDVSLGDELRLDGEEVDMTPADALDDFDLEMLGDVESPSPGMTHDPVSYGALDVDDFEFEQMFTDAMGIDDFGG Disordered 350 394 TSEGESVMREHAYSRGRTRNNYGSTIEGLLDLPDDDDAPAEAGLV Paper 10398682 Liu Y, Gong W, Huang CC, Herr W, Cheng X 1999 Genes Dev 13 13 1692-703 Disordered 403 490 AGQRPRRLSTTAPITDVSLGDELRLDGEEVDMTPADALDDFDLEMLGDVESPSPGMTHDPVSYGALDVDDFEFEQMFTDAMGIDDFGG Paper 10398682 Liu Y, Gong W, Huang CC, Herr W, Cheng X 1999 Genes Dev 13 13 1692-703 Ubiquinol oxidase polypeptide I Cytochrome O subunit 1 Cytochrome O ubiquinol oxidase subunit 1 Oxidase BO(3) subunit 1 Ubiquinol oxidase chain A P18401 P18401 118072 A85540 Escherichia coli 663 MFGKLSLDAVPFHEPIVMVTIAGIILGGLALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQALASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDPQFHTMLMIAASGAVLIALGILCLVIQMYVSIRDRDQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHVHERDAFWEMKEKGEAYKKPDHYEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVPVAEIEKLENQHFDEITKAGLKNGN Disordered 1 51 MFGKLSLDAVPFHEPIVMVTIAGIILGGLALVGLITYFGKWTYLWKEWLTS Engineered 1FFTA 1FFTF Relationship to function unknown Unknown Unknown X-ray crystallography ethanol (v/v) 5 MgCl2 100 NaCl 100 PEG 1500 approximately (w/v) 9 Paper 11017202 Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikstrom M 2000 Nat Struct Biol 7 10 910-7 2162835 Chepuri V, Lemieux L, Au DC, Gennis RB 1990 J Biol Chem 265 19 11185-92 Disordered 553 663 AVVPHVHERDAFWEMKEKGEAYKKPDHYEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVPVAEIEKLENQHFDEITKAGLKNGN Engineered 1FFTA 1FFTF Relationship to function unknown Unknown Unknown X-ray crystallography ethanol (v/v) 5 MgCl2 100 NaCl 100 PEG 1500 approximately (w/v) 9 Paper 11017202 Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikstrom M 2000 Nat Struct Biol 7 10 910-7 2162835 Chepuri V, Lemieux L, Au DC, Gennis RB 1990 J Biol Chem 265 19 11185-92 Disordered 82 95 QQALASAGEAGFLP Engineered Relationship to function unknown Unknown Unknown X-ray crystallography ethanol (v/v) 5 MgCl2 100 NaCl 100 PEG 1500 approximately (w/v) 9 Paper 11017202 Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikstrom M 2000 Nat Struct Biol 7 10 910-7 2162835 Chepuri V, Lemieux L, Au DC, Gennis RB 1990 J Biol Chem 265 19 11185-92 Disordered 180 185 EYSPGV Engineered Relationship to function unknown Unknown Unknown X-ray crystallography ethanol (v/v) 5 MgCl2 100 NaCl 100 PEG 1500 approximately (w/v) 9 Paper 11017202 Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikstrom M 2000 Nat Struct Biol 7 10 910-7 2162835 Chepuri V, Lemieux L, Au DC, Gennis RB 1990 J Biol Chem 265 19 11185-92 Disordered 521 540 RDRDQNRDLTGDPWGGRTLE Engineered Relationship to function unknown Unknown Unknown X-ray crystallography ethanol (v/v) 5 MgCl2 100 NaCl 100 PEG 1500 approximately (w/v) 9 Paper 11017202 Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikstrom M 2000 Nat Struct Biol 7 10 910-7 2162835 Chepuri V, Lemieux L, Au DC, Gennis RB 1990 J Biol Chem 265 19 11185-92 Ubiquinol oxidase polypeptide II [Precursor] CyoA Cytochrome O subunit 2 Cytochrome O ubiquinol oxidase subunit 2 EC 1.10.3.- Oxidase BO(3) subunit 2 Ubiquinol oxidase chain B P18400 P18400 118071 A42226 Escherichia coli 315 MRLRKYNKSLGWLSLFAGTVLLSGCNSALLDPKGQIGLEQRSLILTAFGLMLIVVIPAILMAVGFAWKYRASNKDAKYSPNWSHSNKVEAVVWTVPILIIIFLAVLTWKTTHALEPSKPLAHDEKPITIEVVSMDWKWFFIYPEQGIATVNEIAFPANTPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKAIATPDRAAFDQWVAKAKQSPNTMSDMAAFEKLAAPSEYNQVEYFSNVKPDLFADVINKFMAHGKSMDMTQPEGEHSAHEGMEGMDMSHAESAH Disordered 1 26 MRLRKYNKSLGWLSLFAGTVLLSGCN Engineered 1FFTB 1FFTG Relationship to function unknown Unknown Unknown X-ray crystallography ethanol (v/v) 5 magnesium chloride 100 PEG 1500 approximate (w/v) 9 sodium chloride 100 Paper 11017202 Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikstrom M 2000 Nat Struct Biol 7 10 910-7 This region is located in the periplasmic space. Abramson et al. could not assign a sequence for residues 1-36 or 113-124. However the PDB file locates electron density for residues 27-283. Disordered 284 315 HGKSMDMTQPEGEHSAHEGMEGMDMSHAESAH Engineered 1FFTB 1FFTG Relationship to function unknown Unknown Unknown X-ray crystallography ethanol (v/v) 5 magnesium chloride 100 PEG 1500 approximate (w/v) 9 sodium chloride 100 Paper 11017202 Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikstrom M 2000 Nat Struct Biol 7 10 910-7 This region is located in the periplasmic space. Disordered 1 14 MRLRKYNKSLGWLS Fragment 1FFTB 1FFTG Relationship to function unknown Unknown Unknown X-ray crystallography 277 ammonium sulfate precipitant 35 citrate/bis-Tris-propane (pH 9.0-9.5) 100 dimethylsulphoxide (to obtain sharp edges) v/v 2 DTT buffer 1 EDTA buffer 1 NaN3 buffer 1 Paper 1324168 van der Oost J, Lappalainen P, Musacchio A, Warne A, Lemieux L, Rumbley J, Gennis RB, Aasa R, Pascher T, Malmstrom BG, et al 1992 Embo J 11 9 3209-17 8433374 van der Oost J, Musacchio A, Pauptit RA, Ceska TA, Wierenga RK, Saraste M 1993 J Mol Biol 229 3 794-6 8618822 Wilmanns M, Lappalainen P, Kelly M, Sauer-Eriksson E, Saraste M 1995 Proc Natl Acad Sci U S A 92 26 11955-9 This region is located in the periplasmic space. Disordered 283 315 AHGKSMDMTQPEGEHSAHEGMEGMDMSHAESAH Fragment 1FFTB 1FFTG Relationship to function unknown Unknown Unknown X-ray crystallography 277 ammonium sulfphate precipitant 35 citrate/bis-Tris-propane (pH 9.0-9.5) 100 dimethylsuphoxide (to obtain sharp edges) v/v 2 DTT buffer 1 EDTA buffer 1 NaN3 buffer 1 Paper 1324168 van der Oost J, Lappalainen P, Musacchio A, Warne A, Lemieux L, Rumbley J, Gennis RB, Aasa R, Pascher T, Malmstrom BG, et al 1992 Embo J 11 9 3209-17 8433374 van der Oost J, Musacchio A, Pauptit RA, Ceska TA, Wierenga RK, Saraste M 1993 J Mol Biol 229 3 794-6 8618822 Wilmanns M, Lappalainen P, Kelly M, Sauer-Eriksson E, Saraste M 1995 Proc Natl Acad Sci U S A 92 26 11955-9 This region is located in the periplasmic space. A periplasmic fragment of subunit II is located under the PDB identification of 1CYW. It is residues 125-283 of subunit II as described by Abramson et. al. Potassium voltage-gated channel, shaker-related subfamily, beta member 1, isoform 3 potassium channel shaker chain beta 1a Q6PI60 NP_751891 S66503 Homo sapiens (Human) 401 MQVSIACTEHNLKSRNGEDRLLSKQSSTAPNVVNAARAKFRTVAIIARSLGTFTPQHHISLKESTAKQTGMKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNKPYSKKDYRS Disordered 1 62 MQVSIACTEHNLKSRNGEDRLLSKQSSTAPNVVNAARAKFRTVAIIARSLGTFTPQHHISLK Fragment Native Function arises from the disordered state Entropic chain Flexible linkers/spacers Nuclear magnetic resonance (NMR) Paper 10585425 Wissmann R, Baukrowitz T, Kalbacher H, Kalbitzer HR, Ruppersberg JP, Pongs O, Antz C, Fakler B 1999 J Biol Chem 274 50 35521-5 DNA-repair protein complementing XP-A cells homolog DNA repair protein XPAC Xeroderma pigmentosum group A complementing protein homolog P27088 P27088 139817 JQ1324 Xenopus laevis (African clawed frog) 267 MEPEPEPEQEANKEEEKILSAAVRAKIERNRQRALMLRQARLACRPYPTGEGISTVKAPPKVIDSGGGFFIEEEEAEEQHVENVVRQPGPVLECDYLICEECGKDFMDSYLSNHFDLAVCDSCRDAEEKHKLITRTEAKQEYLLKDCDIDKREPVLKFILKKNPHNTHWGDMKLYLKAQVIKRSLEVWGSEEALEEAKEVRKDNRDKMKQKKFDKKVKELRRTVRSSLWKKEASGHQHEYGPEEHVEEDSYKKTCITCGYEMNYEKM Disordered - Extended 1 84 MEPEPEPEQEANKEEEKILSAAVRAKIERNRQRALMLRQARLACRPYPTGEGISTVKAPPKVIDSGGGFFIEEEEAEEQHVENV Engineered Function arises from the disordered state Molecular assembly Protein-protein binding Mass spectrometry-based high resolution hydrogen-deuterium exchange Sensitivity to proteolysis 310 7.5 Hepes-KOH 25 KCl 100 trypsin Second Concentration 0.05 trypsin First Concentration 0.5 Paper 11344324 Iakoucheva LM, Kimzey AL, Masselon CD, Bruce JE, Garner EC, Brown CJ, Dunker AK, Smith RD, Ackerman EJ 2001 Protein Sci 10 3 560-71 The results from the laboratory experiments were compared to PONDR predictions and found to be identical. Disordered - Extended 181 265 IKRSLEVWGSEEALEEAKEVRKDNRDKMKQKKFDKKVKELRRTVRSSLWKKEASGHQHEYGPEEHVEEDSYKKTCITCGYEMNYE Engineered Function arises from the disordered state Molecular assembly Protein-protein binding Mass spectrometry-based high resolution hydrogen-deuterium exchange Sensitivity to proteolysis 310 7.5 Hepes-KOH 25 KCl 100 trypsin First Concentration 0.5 trypsin Second Concentration 0.05 Paper 11344324 Iakoucheva LM, Kimzey AL, Masselon CD, Bruce JE, Garner EC, Brown CJ, Dunker AK, Smith RD, Ackerman EJ 2001 Protein Sci 10 3 560-71 The results from the laboratory experiments were compared to PONDR predictions and found to be identical. Calcineurin Calmodulin-dependent calcineurin A subunit, alpha isoform CAM-PRP catalytic subunit CaNA Dual specificity phosphatase EC 3.1.3.16 KAP Kinase associated phosphatase Phosphoprotein phosphatase PP7 Serine/threonine protein phosphatase 2B catalytic subunit, alpha isoform Serine/threonine specific protein phosphatase Q08209 Hs.272458 Q08209 6715568 S35067 Homo sapiens 521 MSEPKAIDPKLSTTDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKEGRLEESVALRIITEGASILRQEKNLLDIDAPVTVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHGGLSPEINTLDDIRKLDRFKEPPAYGPMCDILWSDPLEDFGNEKTQEHFTHNTVRGCSYFYSYPAVCEFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLNICSDDELGSEEDGFDGATAAARKEVIRNKIRAIGKMARVFSVLREESESVLTLKGLTPTGMLPSGVLSGGKQTLQSATVEAIEADEAIKGFSPQHKITSFEEAKGLDRINERMPPRRDAMPSDANLNSINKALTSETNGTDSNGSNSSNIQ Disordered - Extended 1 13 MSEPKAIDPKLST 1AUIA Relationship to function unknown Unknown Unknown X-ray crystallography CaCl2 polyethylene glycol (PEG) 6000 Paper 8524402 Kissinger CR, Parge HE, Knighton DR, Lewis CT, Pelletier LA, Tempczyk A, Kalish VJ, Tucker KD, Showalter RE, Moomaw EW, et al 1995 Nature 378 6557 641-4 Mass spectrometry combined with enzymatic digestion showed that the N-terminal residues were sensitive to proteolysis. (Jin and Harrison, 2002) Disordered - Extended 374 468 DDELGSEEDGFDGATAAARKEVIRNKIRAIGKMARVFSVLREESESVLTLKGLTPTGMLPSGVLSGGKQTLQSATVEAIEADEAIKGFSPQHKIT 1AUIA Function arises via a disorder to order transition Molecular assembly Autoregulatory Protein-protein binding X-ray crystallography CaCl2 polyethylene glycol (PEG) 6000 Paper 8524402 Kissinger CR, Parge HE, Knighton DR, Lewis CT, Pelletier LA, Tempczyk A, Kalish VJ, Tucker KD, Showalter RE, Moomaw EW, et al 1995 Nature 378 6557 641-4 The disordered region from 374 – 468 includes the CaM-binding domain predicted to lie between residues 390 – 414. As in the crystal structure of native CaN, the C-terminal portion of CaNA is disordered beyond the CaNB-binding helix (343 – 373), and electron density for the CaM-binding domain of CaNA is not visible. (Kissinger CR, et al.) Mass spectrometry combined with enzymatic digestion showed that the calmodulin-binding region was removed by trypsin, indicating that this disordered region is sensitive to proteolysis. Calmodulin binds to this disordered region between the CnB-binding site and the autoinhibitory helix, and this segment takes on an α-helical conformation to pull the AI helix away from the catalytic site in order to activate the phosphatase activity. (Jin and Harrison) Calmodulin is a protein that wraps around a target helix in calcineurin upon binding. The ~20-residue target helix is located within a 95-residue disordered region that is not observed in crystal structures. The disorder allows the target helix to separate from the rest of the protein, thus permitting access for binding. For the calmodulin/target helix interaction, it is unknown whether the other ~75 disordered residues become ordered upon binding, but it is thought that this region takes on an α-helical conformation when calmodulin binds (Jin and Harrison). The function of the disordered region is to make the helix accessible for calmodulin binding, and this region of disorder is essential to the regulation of calcineurin by calcium/calmodulin. Binding of calcium/calcineurin activates calcineurin’s serine/threonine phosphatase activity. (Dunker et al., 2001) Disordered - Extended CaM-binding domain 390 414 AARKEVIRNKIRAIGKMARVFSVLR 1AUIA Function arises via a disorder to order transition Molecular assembly Autoregulatory Protein-protein binding X-ray crystallography CaCl2 polyethylene glycol (PEG) 6000 Paper 8524402 Kissinger CR, Parge HE, Knighton DR, Lewis CT, Pelletier LA, Tempczyk A, Kalish VJ, Tucker KD, Showalter RE, Moomaw EW, et al 1995 Nature 378 6557 641-4 Disordered - Extended Autoinhibitory region 469 486 SFEEAKGLDRINERMPPR 1AUIA Function arises via an order to disorder transition Function arises via a disorder to order transition Molecular assembly Autoregulatory Protein-protein binding X-ray crystallography CaCl2 polyethylene glycol (PEG) 6000 Paper 8524402 Kissinger CR, Parge HE, Knighton DR, Lewis CT, Pelletier LA, Tempczyk A, Kalish VJ, Tucker KD, Showalter RE, Moomaw EW, et al 1995 Nature 378 6557 641-4 As in the crystal structure of native CaN, the C-terminal portion of CaNA is disordered beyond the CaNB-binding helix (343 – 373), which indicates that the autoinhibitory domain is disordered. However, this disordered region is present for PDB 1AUI. Unlike the native CaN crystal structure, the AI segment of CaN is not seen in the crystal structure of the FKBP12-FK506-CaN complex. This might indicate that the autoinhibitory complex is ordered when CaNA is in a complex with CaNB, but other evidence suggests that when the AI domain is either not in contact with the catalytic domain (as is the case with immunosuppressants) or when CaNA exists as a monomer, the AI domain may not be structured. Calmodulin binds to the disordered region between the CnB-binding site and the autoinhibitory helix, and this segment takes on an α-helical conformation to pull the AI helix away from the catalytic site in order to activate the phosphatase activity according to Jin and Harrison. When this occurs, the structure of the AI helix may change as well, leading to disorder. Further evidence needs to be found in order to indicate the state of the AI domain. For now, the AI domain will be considered disordered based on the statement made by Kissinger above and the information provided by Jin and Harrison in regards to proteolytic sensitivity. The autoinhibitory domain lies over the substrate-binding cleft in the catalytic domain and consists of two short α-helical regions plus five residues in an extended conformation. The helical regions restrict interaction with the substrate-binding cleft when the AI segment contacts the cleft. (Kissinger CR, et al.) Mass spectrometry combined with enzymatic digestion showed that the autoinhibitory helix was removed by trypsin, indicating that this disordered region is sensitive to proteolysis. (Jin and Harrison, 2002) Disordered - Extended 487 521 RDAMPSDANLNSINKALTSETNGTDSNGSNSSNIQ 1AUIA Relationship to function unknown Unknown Unknown X-ray crystallography CaCl2 polyethylene glycol (PEG) 6000 Paper 8524402 Kissinger CR, Parge HE, Knighton DR, Lewis CT, Pelletier LA, Tempczyk A, Kalish VJ, Tucker KD, Showalter RE, Moomaw EW, et al 1995 Nature 378 6557 641-4 CaNA residues 487 – 521 are not visible in the electron density map of the crystal structure and are disordered. Ordered 14 373 TDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKEGRLEESVALRIITEGASILRQEKNLLDIDAPVTVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHGGLSPEINTLDDIRKLDRFKEPPAYGPMCDILWSDPLEDFGNEKTQEHFTHNTVRGCSYFYSYPAVCEFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLNICS 1AUIA X-ray crystallography CaCl2 polyethylene glycol (PEG) 6000 Paper 8524402 Kissinger CR, Parge HE, Knighton DR, Lewis CT, Pelletier LA, Tempczyk A, Kalish VJ, Tucker KD, Showalter RE, Moomaw EW, et al 1995 Nature 378 6557 641-4 Calcineurin B subunit isoform 1 Protein phosphatase 2B regulatory subunit 1 Protein phosphatase 3 regulatory subunit B alpha isoform 1 P63098 Homo sapiens 169 GNEASYPLEMCSHFDADEIKRLGKRFKKLDLDNSGSLSVEEFMSLPELQQNPLVQRVIDIFDTDGNGEVDFKEFIEGVSQFSVKGDKEQKLRFAFRIYDMDKDGYISNGELFQVLKMMVGNNLKDTQLQQIVDKTIINADKDGDGRISFEEFCAVVGGLDIHKKMVVDV Disordered 1 4 GNEA Complex Native 1AUIB Relationship to function unknown Unknown Unknown Paper 12357034 Jin L, Harrison SC 2002 Proc Natl Acad Sci U S A 99 21 13522-6 8524402 Kissinger CR, Parge HE, Knighton DR, Lewis CT, Pelletier LA, Tempczyk A, Kalish VJ, Tucker KD, Showalter RE, Moomaw EW, et al 1995 Nature 378 6557 641-4 Disordered 169 169 V Complex Native 1MF8B Relationship to function unknown Unknown Unknown Paper 12357034 Jin L, Harrison SC 2002 Proc Natl Acad Sci U S A 99 21 13522-6 Chain D, Complex Between Human T-Cell Receptor, Viral Peptide (Tax), And Hla-A 0201 2554793 Homo sapiens (Human) 204 KEVEQNSGPLSVPEGAIASLNCTYSDRGSQSFFWYRQYSGKSPELIMSIYSNGDKEDGRFTAQLNKASQYVSLLIRDSQPSDSATYLCAVTTDSWGKLQFGAGTQVVVTPDIQNPDPAVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKTVLDMRSMDFKSNSAVAWSNKSDFACANAFNNSIIPEDTFFPSPESS Disordered 125 204 SKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKTVLDMRSMDFKSNSAVAWSNKSDFACANAFNNSIIPEDTFFPSPESS Paper 8906788 Garboczi DN, Ghosh P, Utz U, Fan QR, Biddison WE, Wiley DC 1996 Nature 384 6605 134-41 Tyrosine 3-monooxygenase TH Tyrosine 3-hydroxylase P04177 136577 Rattus norvegicus (Rat) 498 MPTPSAPSPQPKGFRRAVSEQDAKQAEAVTSPRFIGRRQSLIEDARKEREAAAAAAAAAVASSEPGNPLEAVVFEERDGNAVLNLLFSLRGTKPSSLSRAVKVFETFEAKIHHLETRPAQRPLAGSPHLEYFVRFEVPSGDLAALLSSVRRVSDDVRSAREDKVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQYKHGEPIPHVEYTAEEIATWKEVYVTLKGLYATHACREHLEGFQLLERYCGYREDSIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTVYWFTVEFGLCKQNGELKAYGAGLLSSYGELLHSLSEEPEVRAFDPDTAAVQPYQDQTYQPVYFVSESFNDAKDKLRNYASRIQRPFSVKFDPYTLAIDVLDSPHTIQRSLEGVQDELHTLAHALSAIS Disordered 1 155 MPTPSAPSPQPKGFRRAVSEQDAKQAEAVTSPRFIGRRQSLIEDARKEREAAAAAAAAAVASSEPGNPLEAVVFEERDGNAVLNLLFSLRGTKPSSLSRAVKVFETFEAKIHHLETRPAQRPLAGSPHLEYFVRFEVPSGDLAALLSSVRRVSDD Paper 8104613 Daubner SC, Lohse DL, Fitzpatrick PF 1993 Protein Sci 2 9 1452-60 Tyrosyl-tRNA synthetase Tyrosine translase Tyrosine--tRNA ligase Tyrosyl-tRNA ligase TyrRS P00952 P00952 135197 SYBSYF Bacillus stearothermophilus 419 MDLLAELQWRGLVNQTTDEDGLRKLLNEERVTLYCGFDPTADSLHIGHLATILTMRRFQQAGHRPIALVGGATGLIGDPSGKKSERTLNAKETVEAWSARIKEQLGRFLDFEADGNPAKIKNNYDWIGPLDVITFLRDVGKHFSVNYMMAKESVQSRIETGISFTEFSYMMLQAYDFLRLYETEGCRLQIGGSDQWGNITAGLELIRKTKGEARAFGLTIPLVTKADGTKFGKTESGTIWLDKEKTSPYEFYQFWINTDDRDVIRYLKYFTFLSKEEIEALEQELREAPEKRAAQKTLAEEVTKLVHGEEALRQAIRISEALFSGDIANLTAAEIEQGFKDVPSFVHEGGDVPLVELLVSAGISPSKRQAREDIQNGAIYVNGERLQDVGAILTAEHRLEGRFTVIRRGKKKYYLIRYA Disordered 321 419 ALFSGDIANLTAAEIEQGFKDVPSFVHEGGDVPLVELLVSAGISPSKRQAREDIQNGAIYVNGERLQDVGAILTAEHRLEGRFTVIRRGKKKYYLIRYA Substrate/ligand binding X-ray crystallography 2.3 A Nuclear magnetic resonance (NMR) Paper 2504923 Brick P, Bhat TN, Blow DM 1989 J Mol Biol 208 1 83-98 12005430 Guijarro JI, Pintar A, Prochnicka-Chalufour A, Guez V, Gilquin B, Bedouelle H, Delepierre M 2002 Structure (Camb) 10 3 311-7 H1 histone family, member 0 H1.0 H1(0) Histone H1' P10922 P10922 31560697 Mus musculus (Mouse) 193 TENSTSAPAAKPKRAKASKKSTDHPKYSDMIVAAIQAEKNRAGSSRQSIQKYIKSHYKVGENADSQIKLSIKRLVTTGVLKQTKGVGASGSFRLAKGDEPKRSVAFKKTKKEVKKVATPKKAAKPKKAASKAPSKKPKATPVKKAKKKPAATPKKAKKPKVVKVKPVKASKPKKAKTVKPKAKSSAKRASKKK Disordered 1 20 TENSTSAPAAKPKRAKASKK Fragment Function arises via a disorder to order transition Protein-DNA binding Far-UV circular dichroism (CD) 293 3.5 H2O NaCl 10 Sodium phosphate buffer 5 Far-UV circular dichroism (CD) 293 3.5 H2O 10% NaCl 10 Sodium phosphate buffer 5 TFE 90% Nuclear magnetic resonance (NMR) 298 3.5 deuterated TFE 90% H2O 10% NaCl 10 peptide 2.7 Phosphate buffer 5 Fourier transform infrared spectroscopy D2O HEPES pH 7.0 10 NaCl 10 mM or 70 mM peptide 4.6 Fourier transform infrared spectroscopy HEPES pH 7.0 10 mouse DNA 6.7 NaCl 10 mM or 70 mM TFE Paper 11584004 Vila R, Ponte I, Collado M, Arrondo JL, Jimenez MA, Rico M, Suau P 2001 J Biol Chem 276 49 46429-35 The fragment used consisted of residues 1-20. Disordered 8 30 PAAKPKRAKASKKSTDHPKYSDM Fragment Function arises via a disorder to order transition Protein-DNA binding Far-UV circular dichroism (CD) 293 3.5 H2O NaCl 10 Sodium phosphate buffer 5 Far-UV circular dichroism (CD) 293 3.5 H2O 10% NaCl 10 Sodium phosphate buffer 5 TFE 90% Nuclear magnetic resonance (NMR) 298 3.5 deuterated TFE 90% H2O 10% NaCl 10 peptide 2.7 Phosphate buffer 5 Fourier transform infrared spectroscopy D2O HEPES pH 7.0 10 NaCl 10 mM or 70 mM peptide 4.6 Fourier transform infrared spectroscopy HEPES pH 7.0 10 mouse DNA 6.7 NaCl 10 mM or 70 mM TFE Paper 11584004 Vila R, Ponte I, Collado M, Arrondo JL, Jimenez MA, Rico M, Suau P 2001 J Biol Chem 276 49 46429-35 The fragment used consisted of residues 8-30. Disordered 96 193 KGDEPKRSVAFKKTKKEVKKVATPKKAAKPKKAASKAPSKKPKATPVKKAKKKPAATPKKAKKPKVVKVKPVKASKPKKAKTVKPKAKSSAKRASKKK Fragment Function arises via a disorder to order transition Protein-DNA binding Far-UV circular dichroism (CD) 293 Phosphate buffer pH 7.0 10 Far-UV circular dichroism (CD) 293 Phosphate buffer pH 7.0 10 TFE 60% (v/v) Fourier transform infrared spectroscopy 295 HEPES 10 NaCl 10 mM or 140 mM peptide 5 Fourier transform infrared spectroscopy 295 HEPES 10 mouse DNA 7 NaCl 10 mM or 140 mM peptide 5 Paper 16006555 Roque A, Iloro I, Ponte I, Arrondo JL, Suau P 2005 J Biol Chem 280 37 32141-7 The fragment used consisted of residues 96-193. Disordered 99 121 EPKRSVAFKKTKKEVKKVATPKK Fragment Function arises via a disorder to order transition Protein-DNA binding Infrared spectroscopy 295 HEPES pD 7.0 10 NaCl 10 mM or 70 mM peptide 4.6 Infrared spectroscopy 295 HEPES pD 7.0 10 mouse DNA 6.7 NaCl 10 mM or 70 mM Far-UV circular dichroism (CD) 278 3.5 H2O Phosphate buffer 5 Far-UV circular dichroism (CD) 278 3.5 H2O 50% Phosphate buffer 5 TFE 50% Far-UV circular dichroism (CD) 278 3.5 H2O 10% Phosphate buffer 5 TFE 90% Nuclear magnetic resonance (NMR) 298 3.5 TFE 50% Nuclear magnetic resonance (NMR) 298 3.5 TFE 90% Paper 10794405 Vila R, Ponte I, Jimenez MA, Rico M, Suau P 2000 Protein Sci 9 4 627-36 11413144 Vila R, Ponte I, Collado M, Arrondo JL, Suau P 2001 J Biol Chem 276 33 30898-903 The fragment used consisted of residues 99-121. Collagen adhesin [Precursor] Q53654 3913259 1183 MNKNVLKFMVFIMLLNIITPLFNKNEAFAARDISSTNVTDLTVSPSKIEDGGKTTVKMTFDDKNGKIQNGDMIKVAWPTSGTVKIEGYSKTVPLTVKGEQVGQAVITPDGATITFNDKVEKLSDVSGFAEFEVQGRNLTQTNTSDDKVATITSGNKSTNVTVHKSEAGTSSVFYYKTGDMLPEDTTHVRWFLNINNEKSYVSKDITIKDQIQGGQQLDLSTLNINVTGTHSNYYSGQSAITDFEKAFPGSKITVDNTKNTIDVTIPQGYGSYNSFSINYKTKITNEQQKEFVNNSQAWYQEHGKEEVNGKSFNHTVHNINANAGIEGTVKGELKVLKQDKDTKAPIANVKFKLSKKDGSVVKDNQKEIEIITDANGIANIKALPSGDYILKEIEAPRPYTFDKDKEYPFTMKDTDNQGYFTTIENAKAIEKTKDVSAQKVWEGTQKVKPTIYFKLYKQDDNQNTTPVDKAEIKKLEDGTTKVTWSNLPENDKNGKAIKYLVKEVNAQGEDTTPEGYTKKENGLVVTNTEKPIETTSISGEKVWDDKDNQDGKRPEKVSVNLLANGEKVKTLDVTSETNWKYEFKDLPKYDEGKKIEYTVTEDHVKDYTTDINGTTITNKYTPGETSATVTKNWDDNNNQDGKRPTEIKVELYQDGKATGKTAILNESNNWTHTWTGLDEKAKGQQVKYTVEELTKVKGYTTHVDNNDMGNLIVTNKYTPETTSISGEKVWDDKDNQDGKRPEKVSVNLLADGEKVKTLDVTSETNWKYEFKDLPKYDEGKKIEYTVTEDHVKDYTTDINGTTITNKYTPGETSATVTKNWDDNNNQDGKRPTEIKVELYQDGKATGKTAILNESNNWTHTWTGLDEKAKGQQVKYTVEELTKVKGYTTHVDNNDMGNLIVTNKYTPETTSISGEKVWDDKDNQDGKRPEKVSVNLLANGEKVKTLDVTSETNWKYEFKDLPKYDEGKKIEYTVTEDHVKDYTTDINGTTITNKYTPGETSATVTKNWDDNNNQDGKRPTEIKVELYQDGKATGKTAILNESNNWTHTWTGLDEKAKGQQVKYTVDELTKVNGYTTHVDNNDMGNLIVTNKYTPKKPNKPIYPEKPKDKTPPTKPDHSNKVKPTPPDKPSKVDKDDQPKDNKTKPENPLKELPKTGMKIITSWITWVFIGILGLYLILRKRFNS Disordered 151 168 ITSGNKSTNVTVHKSEAG Fragment 1AMXA Relationship to function unknown Unknown Protein-protein binding Far-UV circular dichroism (CD) 298 Near-UV circular dichroism (CD) spectroscopy 298 Paper 9334749 Symersky J, Patti JM, Carson M, House-Pompeo K, Teale M, Moore D, Jin L, Schneider A, DeLucas LJ, Hook M, Narayana SV 1997 Nat Struct Biol 4 10 833-8 8218209 Patti JM, Boles JO, Hook M 1993 Biochemistry 32 42 11428-35 Glycine amidinotransferase, mitochondrial [Precursor] AT EC 2.1.4.1 L-Arginine: Glycine Amidinotransferase Transamidinase P50440 Hs.75335 P50440 1730201 S41734 Homo sapiens (Human) 423 MLRVRCLRGGSRGAEAVHYIGSRLGRTLTGWVQRTFQSTQAATASSRNSCAADDKATEPLPKDCPVSSYNEWDPLEEVIVGRAENACVPPFTIEVKANTYEKYWPFYQKQGGHYFPKDHLKKAVAEIEEMCNILKTEGVTVRRPDPIDWSLKYKTPDFESTGLYSAMPRDILIVVGNEIIEAPMAWRSRFFEYRAYRSIIKDYFHRGAKWTTAPKPTMADELYNQDYPIHSVEDRHKLAAQGKFVTTEFEPCFDAADFIRAGRDIFAQRSQVTNYLGIEWMRRHLAPDYRVHIISFKDPNPMHIDATFNIIGPGIVLSNPDRPCHQIDLFKKAGWTIITPPTPIIPDDHPLWMSSKWLSMNVLMLDEKRVMVDANEVPIQKMFEKLGITTIKVNIRNANSLGGGFHCWTCDVRRRGTLQSYLD Disordered - Extended 38 63 STQAATASSRNSCAADDKATEPLPKD Engineered 1JDWA 2JDXA Relationship to function unknown Unknown Unknown X-ray crystallography 295 7 Beta-ME buffer 2 HEPES buffer 40 PEG 6000 buffer 3 protein solution approximately 2 Paper 9218780 1997 Embo J 16 12 3373-3385 9165070 Humm A, Fritsche E, Steinbacher S 1997 Biol Chem 378 3-4 193-7 ATP-dependent hsl protease ATP-binding subunit hslU Heat Shock Locus U Heat shock protein hslU P32168 12518837 B86083 Escherichia coli 442 SEMTPREIVSELDKHIIGQDNAKRSVAIALRNRWRRMQLNEELRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVGYVGKEVDSIIRDLTDAAVKMVRVQAIEKNRYRAEELAEERILDVLIPPAKNNWGQTEQQQEPSAARQAFRKKLREGQLDDKEIEIDLAAAPMGVEIMAPPGMEEMTSQLQSMFQNLGGQKQKARKLKIKDAMKLLIEEEAAKLVNPEELKQDAIDAVEQHGIVFIDEIDKICKRGESSGPDVSREGVQRDLLPLVEGCTVSTKHGMVKTDHILFIASGAFQIAKPSDLIPELQGRLPIRVELQALTTSDFERILTEPNASITVQYKALMATEGVNIEFTDSGIKRIAEAAWQVNESTENIGARRLHTVLERLMEEISYDASDLSGQNITIDADYVSKHLDALVADEDLSRFIL Disordered 176 211 LAAAPMGVEIMAPPGMEEMTSQLQSMFQNLGGQKQK Paper 10693812 Bochtler M, Hartmann C, Song HK, Bourenkov GP, Bartunik HD, Huber R 2000 Nature 403 6771 800-5 HIV Type 1 p6 Protein P12493 120839 Human immunodeficiency virus type 1 499 GARASVLSGGELDKWEKIRLRPGGKKQYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTIAVLYCVHQRIDVKDTKEALDKIEEEQNKSKKKAQQAAADTGNNSQVSQNYPIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTHNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPGATLEEMMTACQGVGGPGHKARVLAEAMSQVTNPATIMIQKGNFRNQRKTVKCFNCGKEGHIAKNCRAPRKKGCWKCGKEGHQMKDCTERQANFLGKIWPSHKGRPGNFLQSRPEPTAPPEESFRFGEETTTPSQKQEPIDKELYPLASLRSLFGSDPSSQ Disordered 448 460 LQSRPEPTAPPEE Engineered Far-UV circular dichroism (CD) 7.2 Phosphate buffer protein 0.2 Nuclear magnetic resonance (NMR) 308 3 H2O super distilled TFE-d2 Paper 16234236 Fossen T, Wray V, Bruns K, Rachmat J, Henklein P, Tessmer U, Maczurek A, Klinger P, Schubert U 2005 J Biol Chem Disordered flexible hinge region 466 479 EETTTPSQKQEPID Engineered Far-UV circular dichroism (CD) 7.2 Phosphate buffer protein 0.2 Nuclear magnetic resonance (NMR) 308 3 H2O super distilled TFE-d2 Paper 16234236 Fossen T, Wray V, Bruns K, Rachmat J, Henklein P, Tessmer U, Maczurek A, Klinger P, Schubert U 2005 J Biol Chem Disordered 491 499 LFGSDPSSQ Engineered Far-UV circular dichroism (CD) 7.2 Phosphate buffer protein 0.2 Nuclear magnetic resonance (NMR) 308 3 H2O super distilled TFE-d2 Paper 16234236 Fossen T, Wray V, Bruns K, Rachmat J, Henklein P, Tessmer U, Maczurek A, Klinger P, Schubert U 2005 J Biol Chem The sequence given is the sequence of the Pr55 Gag polyprotein from HIV Type 1. p6 protein is the C-terminal part of Pr55. In its mature state p6 protein is free from Pr55. This entry is for the mature free state of p6. Myosin Gizzard smooth muscle Myosin heavy chain P10587 Gga.103 P10587 3915778 S03166 Gallus gallus (Chicken) 1979 MSQKPLSDDEKFLFVDKNFVNNPLAQADWSAKKLVWVPSEKHGFEAASIKEEKGDEVTVELQENGKKVTLSKDDIQKMNPPKFSKVEDMAELTCLNEASVLHNLRERYFSGLIYTYSGLFCVVINPYKQLPIYSEKIIDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDTSITQGPSFSYGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHIFYYLIAGASEQMRNDLLLEGFNNYTFLSNGHVPIPAQQDDEMFQETLEAMTIMGFTEEEQTSILRVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADFAIEALAKAKFERLFRWILTRVNKALDKTKRQGASFLGILDIAGFEIFEINSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPTNPPGVLALLDEECWFPKATDTSFVEKLIQEQQNHAKFQKSKQLKDKTEFCILHYAGKVTYNASAWLTKNMDPLNDNVTSLLNQSSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYKEQLTKLMTTLRNTNPNFVRCIIPNHEKRAGKLDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFRTGVLAHLEEERDLKITDVIIAFQAQCRGYLARKAFAKRQQQLTAMLVIQRNCAAYLKLRNWQWWRLFTKVKPLLQVTRQEEEMQAKDEELQRTKERQQKAEAELKELEQKHTQLCEEKNLLQEKLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARIEEEEERSQQLQAEKKKMQQQMLDLEEQLEEEEAARQKLQLEKVTADGKIKKMEDDILIMEDQNNKLTKERKLLEERVSDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKIKRKLEGESSDLHEQIAELQAQIAELKAQLAKKEEELQAALARLEDETSQKNNALKKIRELESHISDLQEDLESEKAARNKAEKQKRDLSEELEALKTELEDTLDTTATQQELRAKREQEVTVLKRALEEETRTHGAQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKTKQTLEKDNADLANEIRSLSQAKQDVEHKKKKLEVQLQDLQSKYSDGERVRTELNEKVHKLQIEVENVTSLLNEAESKNIKLTKDVATLGSQLQDTQELLQEETRQKLNVTTKLRQLEDDKNSLQEQLDEEVEAKQNLERHISTLTIQLSDSKKKLQEFTATVETMEEGKKKLQREIESLTQQFEEKAASYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQMLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRTLEQQVEEMKTQLEELEDELQAAEDAKLRLEVNMQAMKSQFERDLQARDEQNEEKRRQLLKQLHEHETELEDERKQRALAAAAKKKLEVDVKDLESQVDSANKAREEAIKQLRKLQAQMKDYQRDLDDARAAREEIFATARENEKKAKNLEAELIQLQEDLAAAERARKQADLEKEEMAEELASANSGRTSLQDEKRRLEARIAQLEEELDEEHSNIETMSDRMRKAVQQAEQLNNELATERATAQKNENARQQLERQNKELRSKLQEMEGAVKSKFKSTIAALEAKIASLEEQLEQEAREKQAAAKTLRQKDKKLKDALLQVEDERKQAEQYKDQAEKGNLRLKQLKRQLEEAEEESQRINANRRKLQRELDEATESNDALGREVAALKSKLRRGNEPVSFAPPRRSGGRRVIENATDGGEEEIDGRDGDFNGKASE Disordered 1 33 MSQKPLSDDEKFLFVDKNFVNNPLAQADWSAKK Engineered 1BR2A 1BR2B 1BR2C 1BR2D 1BR2E 1BR2F Relationship to function unknown Unknown Unknown X-ray crystallography 100 6.8 cryoprotectant 25% polyethylene glydol 200 Paper 9741621 Dominguez, R. Freyzon, Y. Trybus, K. M. Cohen, C. 1998 Cell 94 5 559-571 Disordered 50 55 KEEKGD Engineered 1BR2A 1BR2B 1BR2C 1BR2D 1BR2E 1BR2F Relationship to function unknown Unknown Unknown X-ray crystallography 100 6.8 cryoprotectant 25% polyethylene glycol 200 Paper 9741621 Dominguez, R. Freyzon, Y. Trybus, K. M. Cohen, C. 1998 Cell 94 5 559-571 Disordered 200 217 SHKGKKDTSITQGPSFSY Engineered 1BR2A 1BR2B 1BR2C 1BR2D 1BR2E 1BR2F Relationship to function unknown Unknown Unknown X-ray crystallography 100 6.8 cryoprotectant 25% polyethylene glycol 200 Paper 9147986 Rovner, A. S. Freyzon, Y. Trybus, K. M. 1997 Journal of Muscle Research and Cell Motility 18 1 103-110 The sequence information for this region came from Rovner et. al. (1997). It is a deviation from the Yanagisawa et. al sequence. This region is part of a 7 AA insert that helps to differentiate between fast and slow smooth muscle. The insert increases the protein’s enzymatic capabilities, as well as its ability to bind and move actin filaments. Disordered 371 374 RNTD Engineered 1BR2A 1BR2B 1BR2C 1BR2D 1BR2E 1BR2F Relationship to function unknown Unknown Unknown X-ray crystallography 100 6.8 cryoprotectant 25% polyethylene glycol 200 Paper 9741621 Dominguez, R. Freyzon, Y. Trybus, K. M. Cohen, C. 1998 Cell 94 5 559-571 Disordered 406 415 RIKVGRDVVQ Engineered 1BR2A 1BR2B 1BR2C 1BR2D 1BR2E 1BR2F Relationship to function unknown Unknown Unknown X-ray crystallography 100 6.8 cryoprotectant 25% polyethylene glycol 200 Paper 9741621 Dominguez, R. Freyzon, Y. Trybus, K. M. Cohen, C. 1998 Cell 94 5 559-571 Disordered 452 457 KTKRQG Engineered 1BR2A 1BR2B 1BR2C 1BR2D 1BR2E 1BR2F Relationship to function unknown Unknown Unknown X-ray crystallography 100 6.8 cryoprotectant 25% polyethylene glycol 200 Paper 9741621 Dominguez, R. Freyzon, Y. Trybus, K. M. Cohen, C. 1998 Cell 94 5 559-571 Disordered 546 549 WFPK Engineered 1BR2A 1BR2B 1BR2C 1BR2D 1BR2E 1BR2F Relationship to function unknown Unknown Unknown X-ray crystallography 100 6.8 cryoprotectant 25% polyethylene glycol 200 Paper 9741621 Dominguez, R. Freyzon, Y. Trybus, K. M. Cohen, C. 1998 Cell 94 5 559-571 The PDB file 1BR2 shows the disordered region ending at amino acid PRO-548. Disordered 573 577 KQLKD Engineered 1BR2A 1BR2B 1BR2C 1BR2D 1BR2E 1BR2F Relationship to function unknown Unknown Unknown X-ray crystallography 100 6.8 cryoprotectant 25% polyethylene glycol 200 Paper 9741621 Dominguez, R. Freyzon, Y. Trybus, K. M. Cohen, C. 1998 Cell 94 5 559-571 Disordered 627 656 DVDRIVGLDQMAKMTESSLPSASKTKKGMF Engineered 1BR2A 1BR2B 1BR2C 1BR2D 1BR2E 1BR2F Relationship to function unknown Unknown Unknown X-ray crystallography 100 6.8 cryoprotectant 25% polyethylene glycol 200 Paper 9741621 Dominguez, R. Freyzon, Y. Trybus, K. M. Cohen, C. 1998 Cell 94 5 559-571 Disordered 790 791 LK Engineered 1BR2A 1BR2B 1BR2C 1BR2D 1BR2E 1BR2F Relationship to function unknown Unknown Unknown X-ray crystallography 100 6.8 cryoprotectant 25% polyethylene glycol 200 Paper 9741621 Dominguez, R. Freyzon, Y. Trybus, K. M. Cohen, C. 1998 Cell 94 5 559-571 GrpE protein Nucleotide Exchange Factor Grpe P09372 Escherichia coli 197 MSSKEQKTPEGQAPEEIIMDQHEEIEAVEPEASAEQVDPRDEKVANLEAQLAEAQTRERDGILRVKAEMENLRRRTELDIEKAHKFALEKFINELLPVIDSLDRALEVADKANPDMSAMVEDIELTLKSMLDVVRKFGVEVIAETNVPLDPNVHQAIAMVESDDVAPGNVLGIMQKGYTLNGRTIRAAMVTVAKAKA Disordered 1 37 MSSKEQKTPEGQAPEEIIMDQHEEIEAVEPEASAEQV Paper 9103205 Harrison CJ, Hayer-Hartl M, Di Liberto M, Hartl F, Kuriyan J 1997 Science 276 5311 431-5 Transcription initiation factor IIA large chain TFIIA 32 kDa subunit P32773 418108 Saccharomyces cerevisiae (Baker's yeast) 286 MSNAEASRVYEIIVESVVNEVREDFENAGIDEQTLQDLKNIWQKKLTETKVTTFSWDNQFNEGNINGVQNDLNFNLATPGVNSSEFNIKEENTGNEGLILPNINSNNNIPHSGETNINTNTVEATNNSGATLNTNTSGNTNADVTSQPKIEVKPEIELTINNANITTVENIDDESEKKDDEEKEEDVEKTRKEKEQIEQVKLQAKKEKRSALLDTDEVGSELDDSDDDYLISEGEEDGPDENLMLCLYDKVTRTKARWKCSLKDGVVTINRNDYTFQKAQVEAEWV Disordered 210 240 SALLDTDEVGSELDDSDDDYLISEGEEDGPD Complex Fragment Protein-protein binding Transactivation (transcriptional activation) X-ray crystallography 103 Paper 8610010 Tan S, Hunziker Y, Sargent DF, Richmond TJ 1996 Nature 381 6578 127-51 The fragment used for structure determination consisted of the C-terminal 76 residues.(aa210-aa286) Diol Dehydratase Beta Subunit 10835671 Klebsiella oxytoca 224 MEINEKLLRQIIEDVLSEMKGSDKPVSFNAPAASAAPQATPPAGDGFLTEVGEARQGTQQDEVIIAVGPAFGLAQTVNIVGIPHKSILREVIAGIEEEGIKARVIRCFKSSDVAFVAVEGNRLSGSGISIGIQSKGTTVIHQQGLPPLSNLELFPQAPLLTLETYRQIGKNAARYAKRESPQPVPTLNDQMARPKYQAKSAILHIKETKYVVTGKNPQELRVAL Disordered 1 45 MEINEKLLRQIIEDVLSEMKGSDKPVSFNAPAASAAPQATPPAGD Complex 1EGMB X-ray crystallography 1,2-propanediol 2.0% Cyanocobalamin 2.5 lauryldimethylamine oxide (LDAO) 0.10% Potassium phosphate buffer pH 8.0 10 Paper 10467140 Shibata N, Masuda J, Tobimatsu T, Toraya T, Suto K, Morimoto Y, Yasuoka N 1999 Structure Fold Des 7 8 997-1008 Diol Dehydratase Gamma Subunit 10835672 Klebsiella oxytoca 173 MNTDAIESMVRDVLSRMNSLQGEAPAAAPAAGGASRSARVSDYPLANKHPEWVKTATNKTLDDFTLENVLSNKVTAQDMRITPETLRLQASIAKDAGRDRLAMNFERAAELTAVPDDRILEIYNALRPYRSTKEELLAIADDLESRYQAKICAAFVREAATLYVERKKLKGDD Disordered 1 36 MNTDAIESMVRDVLSRMNSLQGEAPAAAPAAGGASR Complex 1EGMG X-ray crystallography 1,2-propanediol 2.0% Cyanocobalamin 2.5 lauryldimethylamine oxide (LDAO) 0.10% Potassium phosphate buffer pH 8.0 10 Paper 10467140 Shibata N, Masuda J, Tobimatsu T, Toraya T, Suto K, Morimoto Y, Yasuoka N 1999 Structure Fold Des 7 8 997-1008 Protein R2 of ribonucleotide reductase P00453 Escherichia coli 375 AYTTFSQTKNDQLKEPMFFGQPVNVARYDQQKYDIFEKLIEKQLSFFWRPEEVDVSRDRIDYQALPEHEKHIFISNLKYQTLLDSIQGRSPNVALLPLISIPELETWVETWAFSETIHSRSYTHIIRNIVNDPSVVFDDIVTNEQIQKRAEGISSYYDELIEMTSYWHLLGEGTHTVNGKTVTVSLRELKKKLYLCLMSVNALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLNLLRSGADDPEMAEIAEECKQECYDLFVQAAQQEKDWADYLFRDGSMIGLNKDILCQYVEYITNIRMQAVGLDLPFQTRSNPIPWINTWLVSDNVQVAPQEVEVSSYLVGQIDSEVDTDDLSNFQL Disordered 341 375 SDNVQVAPQEVEVSSYLVGQIDSEVDTDDLSNFQL Paper 8805591 Logan DT, Su XD, Aberg A, Regnstrom K, Hajdu J, Eklund H, Nordlund P 1996 Structure 4 9 1053-64 Fe-Only Hydrogenase (Larger Subunit) P07598 Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303) 421 MSRTVMERIEYEMHTPDPKADPDKLHFVQIDEAKCIGCDTCSQYCPTAAIFGEMGEPHSIPHIEACINCGQCLTHCPENAIYEAQSWVPEVEKKLKDGKVKCIAMPAPAVRYALGDAFGMPVGSVTTGKMLAALQKLGFAHCWDTEFTADVTIWEEGSEFVERLTKKSDMPLPQFTSCCPGWQKYAETYYPELLPHFSTCKSPIGMNGALAKTYGAERMKYDPKQVYTVSIMPCIAKKYEGLRPELKSSGMRDIDATLTTRELAYMIKKAGIDFAKLPDGKRDSLMGESTGGATIFGVTGGVMEAALRFAYEAVTGKKPDSWDFKAVRGLDGIKEATVNVGGTDVKVAVVHGAKRFKQVCDDVKAGKSPYHFIEYMACPGGCVCGGGQPVMPGVLEAMDRTTTRLYAGLKKRLAMASANKA Disordered 398 421 MDRTTTRLYAGLKKRLAMASANKA Paper 10368269 Nicolet Y, Piras C, Legrand P, Hatchikian CE, Fontecilla-Camps JC 1999 Structure Fold Des 7 1 13-23 Carbonic Anhydrase P40881 Methanosarcina thermophila 247 MMFNKQIFTILILSLSLALAGSGCISEGAEDNVAQEITVDEFSNIRENPVTPWNPEPSAPVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGMPIFVGDRSNVQDGVVLHALETINEEGEPIEDNIVEVDGKEYAVYIGNNVSLAHQSQVHGPAAVGDDTFIGMQAFVFKSKVGNNCVLEPRSAAIGVTIPDGRYIPAGMVVTSQAEADKLPEVTDDYAYSHTNEAVVYVNVHLAEGYKETS Disordered 1 37 MMFNKQIFTILILSLSLALAGSGCISEGAEDNVAQEI Paper 10924115 Iverson TM, Alber BE, Kisker C, Ferry JG, Rees DC 2000 Biochemistry 39 31 9222-31 C-ets-1 protein EGF receptor-related protein Ets-1 Ets1 protein p54 proto-oncogene Q540Q5 P27577 Q540Q5 296023 A35875 Mus musculus (Mouse) 440 MKAAVDLKPTLTIIKTEKVDLELFPSPDMECADVPLLTPSSKEMMSQALKATFSGFTKEQQRLGIPKDPRQWTETHVRDWVMWAVNEFSLKGVDFQKFCMSGAALCALGKECFLELAPDFVGDILWEHLEILQKEDVKPYQVNGANPTYPESCYTSDYFISYGIEHAQCVPPSEFSEPSFITESYQTLHPISSEELLSLKYENDYPSVILQDPLQTDTLQTDYFAIKQEVLTPDNMCLGRASRGKLGGQDSFESVESYDSCDRLTQSWSSQSSFNSLQRVPSYDSFDYEDYPAALPNHKPKGTFKDYVRDRADLNKDKPVIPAAALAGYTGSGPIQLWQFLLELLTDKSCQSFISWTGDGWEFKLSDPDEVARRWGKRKNKPKMNYEKLSRGLRYYYDKNIIHKTAGKRYVYRFVCDLQSLLGYTPEELHAMLDVKPDAD Disordered N-terminal region 1 49 MKAAVDLKPTLTIIKTEKVDLELFPSPDMECADVPLLTPSSKEMMSQAL Fragment Native 1BQVA Nuclear magnetic resonance (NMR) 303 6.5 10% D2O 10 mM KCl, 10 mM KH2PO4, 10 mM DTT 1.2 mM Ets-1 amide 1HN and 15N chemical shifts Sensitivity to proteolysis 296 6 200 ng trypsin 20mMcitrate, 150mMKCl, 1mMDTT 2.75 microg protein Paper 9770451 Slupsky CM, Gentile LN, Donaldson LW, Mackereth CD, Seidel JJ, Graves BJ, McIntosh LP 1998 Proc Natl Acad Sci U S A 95 21 12129-34 Dessication-related protein CDET6-19 Desiccation-related protein clone PCC6-19 P22239 P22239 167473 S43775 Craterostigma plantagineum 155 MAQFGGEKYGGRHTDEYGNPIQQGAGAHRGGGIMGGGQQAGQHGTTGVLGHGTAGQHGTTGGGLGHGTAGTGGALGGQHRRSGSSSSSSSSESDGEGGRRKKGMKDKMKEKLPGGHGTTTDQQQYGTAATHGQAQQHEKKGIMDKIKEKLPGGQH Disordered - Molten Globule 1 155 MAQFGGEKYGGRHTDEYGNPIQQGAGAHRGGGIMGGGQQAGQHGTTGVLGHGTAGQHGTTGGGLGHGTAGTGGALGGQHRRSGSSSSSSSSESDGEGGRRKKGMKDKMKEKLPGGHGTTTDQQQYGTAATHGQAQQHEKKGIMDKIKEKLPGGQH Native Function arises via a molten globule to order transition Molecular recognition effectors Substrate/ligand binding Far-UV circular dichroism (CD) Nuclear magnetic resonance (NMR) 283 D2O 50 Dsp16 protein 11.6 EDTA 1 KCl 100 phosphate buffer 10 water 450 Nuclear magnetic resonance (NMR) 308 D2O 50 Dsp16 protein 11.6 EDTA 1 KCl 100 phosphate buffer 10 water 450 Paper 9067253 Lisse T, Bartels D, Kalbitzer HR, Jaenicke R 1996 Biol Chem 377 9 555-61 Piatkowski D Schneider K Salamini F Bartels D 1990 Plant Physiol 94 1682-1688 Synaptobrevin homolog 1 P31109 P31109 6319289 Saccharomyces cerevisiae 117 MSSSTPFDPYALSEHDEERPQNVQSKSRTAELQAEIDDTVGIMRDNINKVAERGERLTSIEDKADNLAVSAQGFKRGANRVRKAMWYKDLKMKMCLALVIIILLVVIIVPIAVHFSR Disordered 1 93 MSSSTPFDPYALSEHDEERPQNVQSKSRTAELQAEIDDTVGIMRDNINKVAERGERLTSIEDKADNLAVSAQGFKRGANRVRKAMWYKDLKMK Fragment Paper 9326367 Rice LM, Brennwald P, Brunger AT 1997 FEBS Lett 415 1 49-55 Tubulin beta-4 chain Tubulin 5 beta Tubulin beta-4 P04350 21361322 Homo sapiens (Human) 444 MREIVHLQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLERINVYYNEATGGNYVPRAVLVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDAVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKMREEFPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPAFAPLTSRGSQQYRGLTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGRMSMKEVDEQMLSVQSKNSSYFVEWIPNNVKTAVCDIPPRGLKMAVTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEQGEFEEEAEEEVA Disordered 394 444 FLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEQGEFEEEAEEEVA Fragment Native Relationship to function unknown Unknown Unknown Far-UV circular dichroism (CD) Paper 10211825 Jimenez MA, Evangelio JA, Aranda C, Lopez-Brauet A, Andreu D, Rico M, Lagos R, Andreu JM, Monasterio O 1999 Protein Sci 8 4 788-799 Tubulin, alpha, ubiquitous alpha-tubulin hk alpha 1 tubulin alpha-1 chain Hs.524390 57013276 I77403 Homo sapiens (Human) 451 MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTRLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVADITNACFEPANQMVKCDPGHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY Disordered - Extended 404 417 FVHWYVGEGMEEGE Engineered Fragment Function arises via a disorder to order transition Molecular assembly Protein-protein binding Far-UV circular dichroism (CD) 298 Nuclear magnetic resonance (NMR) 7 X-ray crystallography Paper 10211825 Jimenez MA, Evangelio JA, Aranda C, Lopez-Brauet A, Andreu D, Rico M, Lagos R, Andreu JM, Monasterio O 1999 Protein Sci 8 4 788-799 The disordered region characterized was studied in an engineered fragment containing residues 404-451. Disordered - Extended 433 451 EEVGVDSVEGEGEEEGEEY Engineered Fragment Function arises via a disorder to order transition Molecular assembly Protein-protein binding Substrate/ligand binding Far-UV circular dichroism (CD) 298 Nuclear magnetic resonance (NMR) 7 X-ray crystallography Paper 10211825 Jimenez MA, Evangelio JA, Aranda C, Lopez-Brauet A, Andreu D, Rico M, Lagos R, Andreu JM, Monasterio O 1999 Protein Sci 8 4 788-799 The disordered region characterized was studied in an engineered fragment containing residues 404-451. Osteocalcin BGP Bone Gla-protein Gamma-carboxyglutamic acid-containing protein P81455 Cfa.3627 P81455 386624 Canis familiaris (dog) 49 YLDSGLGAPVPYPDPLEPKREVCELNPNCDELADHIGFQEAYQRFYGPV Disordered - Extended 1 49 YLDSGLGAPVPYPDPLEPKREVCELNPNCDELADHIGFQEAYQRFYGPV Native Function arises via a disorder to order transition Molecular assembly Substrate/ligand binding Nuclear magnetic resonance (NMR) 298 6.8 calcium chloride buffer 5 imidazole buffer 30 sodium chloride buffer 20 Gel filtration/size exclusion chromatography 298 6.8 calcium chloride buffer 5 imidazole buffer 30 sodium chloride buffer 20 Paper 8101026 Colombo G, Fanti P, Yao C, Malluche HH 1993 J Bone Miner Res 8 6 733-743 8218200 Isbell DT, Du S, Schroering AG, Colombo G, Shelling JG 1993 Biochemistry 32 42 11352-11362 This protein is only disordered in the absence of calcium. When calcium is present, the conformation dramatically changes to a more ordered state. Protein transport protein SEC61 gamma subunit P60058 P60058 38503385 S42412 Canis familiaris (dog) 68 MDQVMQFVEPSRQFVKDSIRLVKRCTKPDRKEFQKIAMATAIGFAIMGFIGFFVKLIHIPINNIIVGG Disordered - Extended 1 9 MDQVMQFVE Engineered Fragment Mutant Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 274 5 Paper 8942632 Beswick V, Baleux F, Huynh-Dinh T, Kepes F, Neumann JM, Sanson A 1996 Biochemistry 35 47 14717-14724 This disordered region was characterized by the study of an engineered fragment containing residues 1-43. This fragment was synthesized via the Merrifield solid-phase method with a mutation at Cys24Ser. This mutation was inserted to prevent dimerization. Disordered - Extended 18 43 SIRLVKRCTKPDRKEFQKIAMATAIG Engineered Fragment Mutant Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 274 5 Paper 8942632 Beswick V, Baleux F, Huynh-Dinh T, Kepes F, Neumann JM, Sanson A 1996 Biochemistry 35 47 14717-14724 This disordered region was characterized by the study of an engineered fragment containing residues 1-43. This fragment was synthesized via the Merrifield solid-phase method with a mutation at Cys24Ser. This mutation was inserted to prevent dimerization. Disordered - Extended 1 4 MDQV Engineered Fragment Mutant Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 311 6 perdeuterated DPC Paper 8942632 Beswick V, Baleux F, Huynh-Dinh T, Kepes F, Neumann JM, Sanson A 1996 Biochemistry 35 47 14717-14724 This disordered region was characterized by the study of an engineered fragment containing residues 1-43. This fragment was synthesized via the Merrifield solid-phase method with a mutation at Cys24Ser. This mutation was inserted to prevent dimerization. Disordered - Extended 40 43 TAIG Engineered Fragment Mutant Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 311 5 perdeuterated DPC Paper 8942632 Beswick V, Baleux F, Huynh-Dinh T, Kepes F, Neumann JM, Sanson A 1996 Biochemistry 35 47 14717-14724 This disordered region was characterized by the study of an engineered fragment containing residues 1-43. This fragment was synthesized via the Merrifield solid-phase method with a mutation at Cys24Ser. This mutation was inserted to prevent dimerization. Chromogranin A Precursor CgA Chromacin Chromogranin A Chromostatin Pituitary secretory protein I secretory protein I SP-I P05059 P05059 89468 A41520 Bos taurus (Cow) 449 MRSAAVLALLLCAGQVIALPVNSPMNKGDTEVMKCIVEVISDTLSKPSPMPVSKECFETLRGDERILSILRHQNLLKELQDLALQGAKERTHQQKKHSSYEDELSEVLEKPNDQAEPKEVTEEVSSKDAAEKRDDFKEVEKSDEDSDGDRPQASPGLGPGPKVEEDNQAPGEEEEAPSNAHPLASLPSPKHPGPQAKEDSEGPSQGPASREKGLSAEQGRQTEREEEEEKWEEAEAREKAVPEEESPPTAAFKAPPSLGNKETQRAAPGWPEDGAGKMGAEEAKPPEGKGEWAHSRQEEEEMARAPQVLFRGGKSGEPEQEEQLSKEWEDAKRWSKMDQLAKELTAEKRLEGEEEEEEDPDRSMRLSFRARGYGFRGPGLQLRRGWRPNSREDSVEAGLPLQVRGYPEEKKEEEGSANRRPEDQELESLSAIEAELEKVAHQLEELRRG Disordered - Extended 407 431 PEEKKEEEGSANRRPEDQELESLSA Engineered Fragment Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Aberrant mobility on SDS-PAGE gel 310 7.5 Tris-HCl 0.2 Near-UV circular dichroism (CD) spectroscopy 295 5.5 sodium acetate salt 15 Near-UV circular dichroism (CD) spectroscopy 295 7.5 Tris-HCl 15 Sensitivity to proteolysis Paper 3473966 Grimes M, Iacangelo A, Eiden LE, Godfrey B, Herbert E 1987 Ann N Y Acad Sci 493 351-378 8243650 Yoo SH, Ferretti JA 1993 FEBS Lett 334 3 373-377 Salivary proline-rich glycoprotein precursor PRB4 2144912 Homo sapiens (Human) 310 MLLILLSVALLALSSAESSSEDVSQEESLFLISGKPQGRRPQGGNQPQRPPPPPGKPQGPPPQGGNQSQGPPPPPGKPEGRPPQGGNQSQGPPPHPGKPERPPPQGGNQSQGPPPHPGKPESRPPQGGHQSQGPPPTPGKPEGPPPQGGNQSQGTPPPPGKPEGRPPQGGNQSQGPPPHPGKPERPPPQGGNQSHRPPPPPGKPERPPPQGGNQSQGPPPHPGKPEGPPPQEGNKSRSARSPPGKPQGPPQQEGNKPQGPPPPGKPQGPPPPGGNPQQPQAPPAGKPQGPPPPPQGGRPPRPAQGQQPPQ Disordered 17 310 ESSSEDVSQEESLFLISGKPQGRRPQGGNQPQRPPPPPGKPQGPPPQGGNQSQGPPPPPGKPEGRPPQGGNQSQGPPPHPGKPERPPPQGGNQSQGPPPHPGKPESRPPQGGHQSQGPPPTPGKPEGPPPQGGNQSQGTPPPPGKPEGRPPQGGNQSQGPPPHPGKPERPPPQGGNQSHRPPPPPGKPERPPPQGGNQSQGPPPHPGKPEGPPPQEGNKSRSARSPPGKPQGPPQQEGNKPQGPPPPGKPQGPPPPGGNPQQPQAPPAGKPQGPPPPPQGGRPPRPAQGQQPPQ Paper 4093242 Loomis RE, Bergey EJ, Levine MJ, Tabak LA 1985 Int J Pept Protein Res 26 6 621-9 Loomis RE, Tseng Ching-Chung, Levine MJ 1986 Int. J. Biol. Macromol. 8 149-152 Caldesmon CaD CDM h-caldesmon high molecular weight caldesmon P12957 Gga.4988 P12957 211896 A33430 Gallus gallus (Chicken) 771 MDDFERRRELRRQKREEMRLEAERLSYQRNDDDEEEAARERRRRARQERLRQKEEGDVSGEVTEKSEVNAQNSVAEEETKRSTDDEAALLERLARREERRQKRLQEALERQKEFDPTITDGSLSVPSRREVNNVEENEITGKEEKVETRQGRCEIEETETVTKSYQRNNWRQDGEEEGKKEEKDSEEEKPKEVPTEENQVDVAVEKSTDKEEVVETKTLAVNAENDTNAMLEGEQSITDAADKEKEEAEKEREKLEAEEKERLKAEEEKKAAEEKQKAEEEKKAAEERERAKAEEEKRAAEERERAKAEEERKAAEERERAKAEEERKAAEERAKAEEERKAAEERAKAEEERKAAEERAKAEKERKAAEERERAKAEEEKRAAEEKARLEAEKLKEKKKMEEKKAQEEKAQANLLRKQEEDKEAKVEAKKESLPEKLQPTSKKDQVKDNKDKEKAPKEEMKSVWDRKRGVPEQKAQNGERELTTPKLKSTENAFGRSNLKGAANAEAGSEKLKEKQQEAAVELDELKKRREERRKILEEEEQKKKQEEAERKIREEEEKKRMKEEIERRRAEAAEKRQKVPEDGVSEEKKPFKCFSPKGSSLKIEERAEFLNKSAQKSGMKPAHTTAVVSKIDSRLEQYTSAVVGNKAAKPAKPAASDLPVPAEGVRNIKSMWEKGNVFSSPGGTGTPNKETAGLKVGVSSRINEWLTKTPEGNKSPAPKPSDLRPGDVSGKRNLWEKQSVEKPAASSSKVTATGKKSETNGLRQFEKEP Disordered - Extended 636 771 RLEQYTSAVVGNKAAKPAKPAASDLPVPAEGVRNIKSMWEKGNVFSSPGGTGTPNKETAGLKVGVSSRINEWLTKTPEGNKSPAPKPSDLRPGDVSGKRNLWEKQSVEKPAASSSKVTATGKKSETNGLRQFEKEP Complex Engineered Fragment Isoform Function arises via a pre-molten globule to order transition Molecular recognition effectors Phosphorylation Protein-protein binding Aberrant mobility on SDS-PAGE gel 293 Calcium Calmodulin Far-UV circular dichroism (CD) 293 Calcium Calmodulin Gel filtration/size exclusion chromatography 293 Calcium Calmodulin Small-angle X-ray scattering 293 Calcium Calmodulin Thermal stability 293 Calcium Calmodulin Paper 2803315 Hayashi K, Kanda K, Kimizuka F, Kato I, Sobue K 1989 Biochem Biophys Res Commun 164 1 503-511 14635127 Permyakov SE, Millett IS, Doniach S, Permyakov EA, Uversky VN 2003 Proteins 53 4 855-862 Protein L precursor Ig light chain-binding protein precursor Q51912 Q51912 150672 A42808 Peptostreptococcus magnus (Finegoldia magna) 719 MAALAGAIVVTGGVGSYAADEPIDLEKLEEKRDKENVGNLPKFDNEVKDGSENPMAKYPDFDDEASTRFETENNEFEEKKVVSDNFFDQSEHPFVENKEETPETPETDSEEEVTIKANLIFANGSTQTAEFKGTFEKATSEAYAYADTLKKDNGEYTVDVADKGYTLNIKFAGKEKTPEEPKEEVTIKANLIYADGKTQTAEFKGTFEEATAEAYRYADALKKDNGEYTVDVADKGYTLNIKFAGKEKTPEEPKEEVTIKANLIYADGKTQTAEFKGTFEEATAEAYRYADLLAKENGKYTVDVADKGYTLNIKFAGKEKTPEEPKEEVTIKANLIYADGKTQTAEFKGTFAEATAEAYRYADLLAKENGKYTADLEDGGYTINIRFAGKKVDEKPEEKEQVTIKENIYFEDGTVQTATFKGTFAEATAEAYRYADLLSKEHGKYTADLEDGGYTINIRFAGKEEPEETPEKPEVQDGYASYEEAEAAAKEALKNDDVNKSYTIRQGADGRYYYVLSPVEAEEEKPEAQNGYATYEEAEAAAKKALENDPINKSYSIRQGADGRYYYVLSPVEAETPEKPVEPSEPSTPDVPSNPSNPSTPDVPSTPDVPSNPSTPEVPSNPSTPGNEEKPGNEQKPGNEQKPGNEQKPGNEQKPGNEQKPDQPSKPEKEENGKGGVDSPKKKEKAALPKAGSEAEILTLAAASLSSVAGAFISLKKRK Disordered - Extended 1 17 MAALAGAIVVTGGVGSY Engineered Fragment 2PTLA Function arises from the disordered state Unknown Unknown Nuclear magnetic resonance (NMR) PDB Wikstroem M, Sjoebring U, Kastern W, Bjoerck L 1993 32 3381 Disordered - Extended 95 115 VENKEETPETPETDSEEEVTI Engineered Fragment Function arises via a disorder to order transition Unknown Unknown Far-UV circular dichroism (CD) 4.1 Paper 9007989 Ramirez-Alvarado M, Serrano L, Blanco FJ 1997 Protein Sci 6 1 162-174 Disordered - Extended 114 123 TIKANLIFAN Engineered Fragment Function arises from the disordered state Unknown Unknown Nuclear magnetic resonance (NMR) TFE Paper 9007989 Ramirez-Alvarado M, Serrano L, Blanco FJ 1997 Protein Sci 6 1 162-174 Disordered - Extended 114 138 TIKANLIFANGSTQTAEFKGTFEKA Engineered Fragment Function arises via a disorder to order transition Unknown Unknown Far-UV circular dichroism (CD) Nuclear magnetic resonance (NMR) Paper 9007989 Ramirez-Alvarado M, Serrano L, Blanco FJ 1997 Protein Sci 6 1 162-174 Disordered - Extended 135 138 FEKA Engineered Fragment Function arises from the disordered state Unknown Unknown Nuclear magnetic resonance (NMR) TFE Paper 9007989 Ramirez-Alvarado M, Serrano L, Blanco FJ 1997 Protein Sci 6 1 162-174 Disordered - Extended 136 155 EKATSEAYAYADTLKKDNGE Engineered Fragment Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Far-UV circular dichroism (CD) Nuclear magnetic resonance (NMR) 295 Paper 9007989 Ramirez-Alvarado M, Serrano L, Blanco FJ 1997 Protein Sci 6 1 162-174 Microtubule-associated protein 2 MAP2 MAP-2 P15146 Rattus norvegicus 1861 MADERKDEGKAPHWTSASLTEAAAHPHSPEMKDQGGSGEGLSRSANGFPYREEEEGAFGEHGSQGTYSDTKENGINGELTSADRETAEEVSARIVQVVTAEAVAVLKGEQEKEAQHKDQPAALPLAAEETVNLPPSPPPSPASEQTAALEEDLLTASKMEFPEQQKLPSSFAEPLDKEETEFKMQSKPGEDFEHAALVPQPDTSKTPQDKKDPQDMEGEKSPASPFAQTFGTNLEDIKQITEPSITVPSIGLSAEPLAPKDQKDWFIEMPVESKKDEWGLAAPISPGPLTPMREKDVLEDIPRWEGKQFDSPMPSPFHGGSFTLPLDTVKDERVTEGSQPFAPVFFQSDDKMSLQDTSGSATSKESSKDEEPQKDKADKVADVPVSEATTVLGDVHSPAVEGFVGENISGEEKGTTDQEKKETSTPSVQEPTLTETEPQTKLEETSKVSIEETVAKEEESLKLKDDKAGVIQTSTEQSFSKEDQKGQEQTIEALKQDSFPISLEQAVTDAAMATKTLEKVTSEPEAVSEKREIQGLFEEDIADKSKLEGAGSATVAEVEMPFYEDKSGMSKYFETSALKEDVTRSTGLGSDYYELSDSRGNAQESLDTVSPKNQQDEKELLAKASQPSPPAHEAGYSTLAQSYTSDHPSELPEEPSSPQERMFTIDPKVYGEKRDLHSKNKDDLTLSRSLGLGGRSAIEQRSMSINLPMSCLDSIALGFNFGRGHDLSPLASDILTNTSGSMDEGDDYLPPTTPAVEKIPCFPIESKEEEDKTEQAKVTGGQTTQVETSSESPFPAKEYYKNGTVMAPDLPEMLDLAGTRSRLASVSADAEVARRKSVPSEAVVAESSTGLPPVADDSQPVKPDSQLEDMGYCVFNKYTVPLPSPVQDSENLSGESGSFYEGTDDKVRRDLATDLSLIEVKLAAAGRVKDEFTAEKEASPPSSADKSGLSREFDQDRKANDKLDTVLEKSEEHVDSKEHAKESEEVGDKVELFGLGVTYEQTSAKELITTKETAPERAEKGLSSVPEVAEVETTTKADQGLDVAAKKDDQSPLDIKVSDFGQMASGMSVDAGKTIELKFEVDQQLTLSSEAPQETDSFMGIESSHVKDGAKVSETEVKEKVAKPDLVHQEAVDKEESYESSGEHESLTMESLKPDEGKKETSPETSLIQDEVALKLSVEIPCPPPVSEADSSIDEKAEVQMEFIQLPKEESTETPDIPAIPSDVTQPQPEAVVSEPAEVRGEEEEIEAEGEYDKLLFRSDTLQITDLLVPGSREEFVETCPGEHKGVVESVVTIEDDFITVVQTTTDEGELGSHSVRFAAPVQPEEERRPYPHDEELEVLMAAEAQAEPKDGSPDAPATPEKEEVPFSEYKTETYDDYKDETTIDDSIMDADSLWVDTQDDDRSILTEQLETIPKEERAEKEARRPSLEKHRKEKPFKTGRGRISTPERREVAKKEPSTVSRDEVRRKKAVYKKAELAKESEVQAHSPSRKLILKPAIKYTRPTHLSCVKRKTTATSGESAQAPSAFKQAKDKVTDGITKSPEKRSSLPRPSSILPPRRGVSGDREENSFSLNSSISSARRTTRSEPIRRAGKSGTSTPTTPGSTAITPGTPPSYSSRTPGTPGTPSYPRTPGTPKSGILVPSEKKVAIIRTPPKSPATPKQLRLINQPLPDLKNVKSKIGSTDNIKYQPKGGQVRILNKKMDFSKVQSRCGSKDNIKHSAGGGNVQIVTKKIDLSHVTSKCGSLKNIRHRPGGGRVKIESVKLDFKEKAQAKVGSLDNAHHVPGGGNVKIDSQKLNFREHAKARVDHGAEIITQSPSRSSVASPRRLSNVSSSGSINLLESPQLATLAEDVTAALAKQGL Disordered 1 1861 MADERKDEGKAPHWTSASLTEAAAHPHSPEMKDQGGSGEGLSRSANGFPYREEEEGAFGEHGSQGTYSDTKENGINGELTSADRETAEEVSARIVQVVTAEAVAVLKGEQEKEAQHKDQPAALPLAAEETVNLPPSPPPSPASEQTAALEEDLLTASKMEFPEQQKLPSSFAEPLDKEETEFKMQSKPGEDFEHAALVPQPDTSKTPQDKKDPQDMEGEKSPASPFAQTFGTNLEDIKQITEPSITVPSIGLSAEPLAPKDQKDWFIEMPVESKKDEWGLAAPISPGPLTPMREKDVLEDIPRWEGKQFDSPMPSPFHGGSFTLPLDTVKDERVTEGSQPFAPVFFQSDDKMSLQDTSGSATSKESSKDEEPQKDKADKVADVPVSEATTVLGDVHSPAVEGFVGENISGEEKGTTDQEKKETSTPSVQEPTLTETEPQTKLEETSKVSIEETVAKEEESLKLKDDKAGVIQTSTEQSFSKEDQKGQEQTIEALKQDSFPISLEQAVTDAAMATKTLEKVTSEPEAVSEKREIQGLFEEDIADKSKLEGAGSATVAEVEMPFYEDKSGMSKYFETSALKEDVTRSTGLGSDYYELSDSRGNAQESLDTVSPKNQQDEKELLAKASQPSPPAHEAGYSTLAQSYTSDHPSELPEEPSSPQERMFTIDPKVYGEKRDLHSKNKDDLTLSRSLGLGGRSAIEQRSMSINLPMSCLDSIALGFNFGRGHDLSPLASDILTNTSGSMDEGDDYLPPTTPAVEKIPCFPIESKEEEDKTEQAKVTGGQTTQVETSSESPFPAKEYYKNGTVMAPDLPEMLDLAGTRSRLASVSADAEVARRKSVPSEAVVAESSTGLPPVADDSQPVKPDSQLEDMGYCVFNKYTVPLPSPVQDSENLSGESGSFYEGTDDKVRRDLATDLSLIEVKLAAAGRVKDEFTAEKEASPPSSADKSGLSREFDQDRKANDKLDTVLEKSEEHVDSKEHAKESEEVGDKVELFGLGVTYEQTSAKELITTKETAPERAEKGLSSVPEVAEVETTTKADQGLDVAAKKDDQSPLDIKVSDFGQMASGMSVDAGKTIELKFEVDQQLTLSSEAPQETDSFMGIESSHVKDGAKVSETEVKEKVAKPDLVHQEAVDKEESYESSGEHESLTMESLKPDEGKKETSPETSLIQDEVALKLSVEIPCPPPVSEADSSIDEKAEVQMEFIQLPKEESTETPDIPAIPSDVTQPQPEAVVSEPAEVRGEEEEIEAEGEYDKLLFRSDTLQITDLLVPGSREEFVETCPGEHKGVVESVVTIEDDFITVVQTTTDEGELGSHSVRFAAPVQPEEERRPYPHDEELEVLMAAEAQAEPKDGSPDAPATPEKEEVPFSEYKTETYDDYKDETTIDDSIMDADSLWVDTQDDDRSILTEQLETIPKEERAEKEARRPSLEKHRKEKPFKTGRGRISTPERREVAKKEPSTVSRDEVRRKKAVYKKAELAKESEVQAHSPSRKLILKPAIKYTRPTHLSCVKRKTTATSGESAQAPSAFKQAKDKVTDGITKSPEKRSSLPRPSSILPPRRGVSGDREENSFSLNSSISSARRTTRSEPIRRAGKSGTSTPTTPGSTAITPGTPPSYSSRTPGTPGTPSYPRTPGTPKSGILVPSEKKVAIIRTPPKSPATPKQLRLINQPLPDLKNVKSKIGSTDNIKYQPKGGQVRILNKKMDFSKVQSRCGSKDNIKHSAGGGNVQIVTKKIDLSHVTSKCGSLKNIRHRPGGGRVKIESVKLDFKEKAQAKVGSLDNAHHVPGGGNVKIDSQKLNFREHAKARVDHGAEIITQSPSRSSVASPRRLSNVSSSGSINLLESPQLATLAEDVTAALAKQGL Native Paper 15751971 Csizmok V, Bokor M, Banki P, Klement E, Medzihradszky KF, Friedrich P, Tompa K, Tompa P 2005 Biochemistry 44 10 3955-64 CD4 glycoprotein (Precursor) T-cell surface antigen T4/Leu-3 T-cell surface glycoprotein CD4 P01730 P01730 179142 RWHUT4 Homo sapiens (Human) 458 MNRGVPFRHLLLVLQLALLPAATQGKKVVLGKKGDTVELTCTASQKKSIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRADSRRSLWDQGNFPLIIKNLKIEDSDTYICEVEDQKEEVQLLVFGLTANSDTHLLQGQSLTLTLESPPGSSPSVQCRSPRGKNIQGGKTLSVSQLELQDSGTWTCTVLQNQKKVEFKIDIVVLAFQKASSIVYKKEGEQVEFSFPLAFTVEKLTGSGELWWQAERASSSKSWITFDLKNKEVSVKRVTQDPKLQMGKKLPLHLTLPQALPQYAGSGNLTLALEAKTGKLHQEVNLVVMRATQLQKNLTCEVWGPTSPKLMLSLKLENKEAKVSKREKAVWVLNPEAGMWQCLLSDSGQVLLESNIKVLPTWSTPVQPMALIVLGGVAGLLLFIGLGIFFCVRCRHRRRQAERMSQIKRLLSEKKTCQCPHRFQKTCSPI Disordered cytoplasmic tail 421 458 RCRHRRRQAERMSQIKRLLSEKKTCQCPHRFQKTCSPI Fragment Native Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Far-UV circular dichroism (CD) 298 Nuclear magnetic resonance (NMR) 300 1.9 0.3 mg 1,4-dithiothreitol 9 mg peptide in 600 microl 50% TFE-d2 Paper 9622505 Wray V, Mertins D, Kiess M, Henklein P, Trowitzsch-Kienast W, Schubert U. 1998 Biochemistry 37 23 8527-38 CD and NMR results in aqueous solution were characteristic of a disordered peptide conformation with very little evidence of stable secondary structure. However, both the qualitative and quantitative NMR data provide convincing evidence for the presence of predominantly alfa-helical secondary structure upon increasing the content of TFE, but only a fraction of the complete CD4CYTO tail (from Gln-428 to Arg-437) has the ability of adopting stabilized helical structure in this environment. The N- and C-terminal regions, which are inherently nonstructured, destabilize the alfa-helical core structure. Addition of TFE causes a stabilization of the helical region in the molecule that already has a tendency for such a structure when this helical region of CD4CYTO was studied in water alone. However, in the context of full-length CD4CYTO, the helical core structure requires stabilizing factors which could be provided either by the membrane itself or by other CD4 interacting factors such as Vpu, Nef, or p56lck. Chromogranin B 2052401 Bos taurus (Bovine) 646 MQPAALLGLLGATVVAAVSSMPVDIRNHNEEVVTHCIIEVLSNALLKSSAPPITPECRQVLKKNGKELKDEEKSENENTRFEVRLLRDPADTSEAPGLSSREDSGEGDAQVPTVADTESGGHSRERAGEPPGSQVAKEAKTRYSKSEGQNREEEMVKYQKRERGEVGSEERLSEGPGKAQMAFLNQRNQTPAKKEELVSRYDTQSARGLEKSHSRERSSQESGEETKSQENWPQELQRHPEGQEAPGESEEDASPEVDKRRSRPRHHHGRSRPDRSSQEGNPPLEEESHVGTGNSDEEKARHPAHFRALEEGAEYGEEVRRHSAAQAPGDLQGARFGGRGRGEHQALRRPSEESLEQENKRHGLSPDLNMAQGYSEESEEERGPARGPSYRARGGEAAAYSTLGQTDEKRFLGETHHRVQESQRDKARRRLPGELRNYLDYGEEKGEEAARGKWQPQGDPRDADENREEARLRGKQYAPHHITEKRLGELLNPFYDPSQWKSSRFERKDPMDDSFLEGEEENGLTLNEKNFFPEYNYDWWEKKPFEEDVNWGYEKRNPVPKLDLKRQYDRVAELDQLLHYRKKSAEFPDFYDSEEQVSPQHTAENEEEKAGQGVLTEEEEKELENLAAMDLELQKIAEKFSGTRRG Disordered 1 646 MQPAALLGLLGATVVAAVSSMPVDIRNHNEEVVTHCIIEVLSNALLKSSAPPITPECRQVLKKNGKELKDEEKSENENTRFEVRLLRDPADTSEAPGLSSREDSGEGDAQVPTVADTESGGHSRERAGEPPGSQVAKEAKTRYSKSEGQNREEEMVKYQKRERGEVGSEERLSEGPGKAQMAFLNQRNQTPAKKEELVSRYDTQSARGLEKSHSRERSSQESGEETKSQENWPQELQRHPEGQEAPGESEEDASPEVDKRRSRPRHHHGRSRPDRSSQEGNPPLEEESHVGTGNSDEEKARHPAHFRALEEGAEYGEEVRRHSAAQAPGDLQGARFGGRGRGEHQALRRPSEESLEQENKRHGLSPDLNMAQGYSEESEEERGPARGPSYRARGGEAAAYSTLGQTDEKRFLGETHHRVQESQRDKARRRLPGELRNYLDYGEEKGEEAARGKWQPQGDPRDADENREEARLRGKQYAPHHITEKRLGELLNPFYDPSQWKSSRFERKDPMDDSFLEGEEENGLTLNEKNFFPEYNYDWWEKKPFEEDVNWGYEKRNPVPKLDLKRQYDRVAELDQLLHYRKKSAEFPDFYDSEEQVSPQHTAENEEEKAGQGVLTEEEEKELENLAAMDLELQKIAEKFSGTRRG Paper Somatoliberin [Precursor] GHRH GRF Growth hormone-releasing factor Growth hormone-releasing hormone P63292 54039610 Bos taurus (Bovine) 106 MLLWVFFLVTLTLSSGSHGSLPSQPLRIPRYADAIFTNSYRKVLGQLSARKLLQDIMNRQQGERNQEQGAKVRLGRQVDGVWTDQQQMALESTLVSLLQERRNSQG Disordered U-90600F 31 59 YIDAIFTSSYRKVLAQLSARKLLQDILSR Engineered Fragment Mutant Function arises via a disorder to order transition Infrared spectroscopy 323 5.6 protein per ml 100 Infrared spectroscopy 513 5.6 protein per ml 100 Infrared spectroscopy 297 5.6 protein per ml 100 Infrared spectroscopy 278 5.6 protein per ml 100 Raman optical activity 313 Paper 9375414 Sarver RW Jr, Friedman AR, Thamann TJ 1997 Spectrochim Acta A Mol Biomol Spectrosc 53A 11 1889-900 U-90699F is an analog of the bovine growth hormone releasing factor. It is a fragment that contains the following substitutions: Ile2, Ser8, Ala15, Leu27, and Ser28. It also has a C-terminal tag of Hse-NH-ethyl x Ch3COOH. Microtubule-associated protein tau isoform Tau-F htau40 Microtubule-associated protein tau isoform Tau-4 Neurofibrillary tangle protein Paired helical filament-tau PHF-tau tau-4 P10636 Hs.101174 P10636-8 6754638 Homo sapiens (Human) 441 MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL Disordered - Extended 1 243 MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRL Engineered Isoform Relationship to function unknown Molecular assembly Protein-protein binding Near-UV circular dichroism (CD) spectroscopy 295 7 Fourier transform infrared spectroscopy Small-angle X-ray scattering Thermal stability Rotory shadowing electron microscopy Paper 14769047 Barghorn S, Davies P, Mandelkow E 2004 Biochemistry 43 6 1694-1703 2484340 Goedert M, Spillantini MG, Jakes R, Rutherford D, Crowther RA 1989 Neuron 3 4 519-526 15147841 Santarella RA, Skiniotis G, Goldie KN, Tittmann P, Gross H, Mandelkow EM, Mandelkow E, Hoenger A 2004 J Mol Biol 339 3 539-553 7929085 Schweers O, Schonbrunn-Hanebeck E, Marx A, Mandelkow E 1994 J Biol Chem 269 39 24290-24297 Disordered - Extended Core Domain/Binding Domain 244 368 QTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGN Engineered Isoform Function arises via a disorder to order transition Molecular assembly Protein-protein binding Thermal stability Rotory shadowing electron microscopy Paper 2484340 Goedert M, Spillantini MG, Jakes R, Rutherford D, Crowther RA 1989 Neuron 3 4 519-526 15147841 Santarella RA, Skiniotis G, Goldie KN, Tittmann P, Gross H, Mandelkow EM, Mandelkow E, Hoenger A 2004 J Mol Biol 339 3 539-553 7929085 Schweers O, Schonbrunn-Hanebeck E, Marx A, Mandelkow E 1994 J Biol Chem 269 39 24290-24297 Disordered - Extended Core Domain/Binding Domain 244 369 QTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNK Engineered Isoform Function arises via a disorder to order transition Molecular assembly Protein-protein binding Near-UV circular dichroism (CD) spectroscopy 295 7 Rotory shadowing electron microscopy Fourier transform infrared spectroscopy Small-angle X-ray scattering Thermal stability Paper 14769047 Barghorn S, Davies P, Mandelkow E 2004 Biochemistry 43 6 1694-1703 2484340 Goedert M, Spillantini MG, Jakes R, Rutherford D, Crowther RA 1989 Neuron 3 4 519-526 7929085 Schweers O, Schonbrunn-Hanebeck E, Marx A, Mandelkow E 1994 J Biol Chem 269 39 24290-24297 This the microtubule binding domain. Disordered - Extended 369 441 KKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL Engineered Isoform Relationship to function unknown Molecular assembly Protein-protein binding Rotory shadowing electron microscopy Thermal stability Paper 2484340 Goedert M, Spillantini MG, Jakes R, Rutherford D, Crowther RA 1989 Neuron 3 4 519-526 15147841 Santarella RA, Skiniotis G, Goldie KN, Tittmann P, Gross H, Mandelkow EM, Mandelkow E, Hoenger A 2004 J Mol Biol 339 3 539-553 7929085 Schweers O, Schonbrunn-Hanebeck E, Marx A, Mandelkow E 1994 J Biol Chem 269 39 24290-24297 Disordered - Extended 370 441 KIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL Engineered Isoform Function arises via a disorder to order transition Molecular assembly Protein-protein binding Near-UV circular dichroism (CD) spectroscopy 295 7 Rotory shadowing electron microscopy Fourier transform infrared spectroscopy Small-angle X-ray scattering Thermal stability Paper 14769047 Barghorn S, Davies P, Mandelkow E 2004 Biochemistry 43 6 1694-1703 2484340 Goedert M, Spillantini MG, Jakes R, Rutherford D, Crowther RA 1989 Neuron 3 4 519-526 7929085 Schweers O, Schonbrunn-Hanebeck E, Marx A, Mandelkow E 1994 J Biol Chem 269 39 24290-24297 PHF-tau is generally found as dimers but can also form larger complexes. Fibronecin binding protein 288969 Streptococcus dysgalactiae 1091 MTNCKYKLRKLSIGLVSVGTMFMAAPVMGEDASQPTASVTTESPAIQTEEDQGSQAEALEEPTPAPQTSPSTVSAVPAEAAAMADEKGIAEAPAHEPAPKASVQAEAASPAGKAEATTNTGQPTNTEQARSRSKRAAEIAPQTIEVEKLEVDKENSSLTVKDGEKDKQLIKHRDGNQRDIFDISRDVKVNQDGTMDVTLTVKPKQIDEGAEVIVLLDTSQKMTETDFNTAKENIKKLVTTLTGTTDKEGKNVSHYNNRNSVRLIDFYRKVGESTDLSGWDAKKIDEKLNEVWKKAKDDYNGWGVDLQGAIHKAREIFNLDKEKRSGKRQHIVLFSQGESTFSYDIKDKSKMDKVAVEEPVTYSNPLFPWPFYFDTTTRTHNVVNDAKKLIDFLNKLGISQFNGAVDNVATVGNTLLGLGSFFGLKNPLDYISLADLETSKLNSEKFDYSRRVGEGYNFRSYFDREVDKVGFKKILVEKIKGNLKKFQPKQTDTWLSSLGLNSIKEKIQDWMIDKALDNLFYRRQYQFYNHNLSAQAEARMAREEGIKFYAVDVTEPERIAKEINSQKYSEAYTNHLKKKAEEARELAKKRNEKFDKYLKEMSESQKFFKDVEDPEKFKDILTELKVTETFEEKVSVNNSEQRKSNKEVEYKKASSNSSFLSFIFSSSTNESITWTLSKDKLQKALQSGETLTLEYKLKIHKDKFKLAPQTRSKRSLDTSENKKSVTEKVITSDVKYKINDKEVKGKELDDVSLTYSKETVRKPQVEPNVPDTPQEKPLTPLAPSEPSQPSIPETPLIPSEPSVPETSTPEGPTEGENNLGGQSEEITITEDSQSGMSGQNPGSGNETVVEDTQTSQEDIVLGGPGQVIDFTEDSQPGMSGNNSHTITEDSKPSQEDEVIIGGQGQVIDFTEDTQSGMSGDNSHTDGTVLEEDSKPSQEDEVIIGGQGQVIDFTEDTQTGMSGAGQVESPTITEETHKPEIIMGGQSDPIDMVEDTLPGMSGSNEATVVEEDTRPKLQFHFDNEEPVPATVPTVSQTPIAQVESKVPHAKAESALPQTGDTNKLETFFTITALTVIGAAGLLGKKRRNNQTD Disordered 810 969 EGPTEGENNLGGQSEEITITEDSQSGMSGQNPGSGNETVVEDTQTSQEDIVLGGPGQVIDFTEDSQPGMSGNNSHTITEDSKPSQEDEVIIGGQGQVIDFTEDTQSGMSGDNSHTDGTVLEEDSKPSQEDEVIIGGQGQVIDFTEDTQTGMSGAGQVESP Paper 8576127 House-Pompeo K, Xu Y, Joh D, Speziale P, Hook M 1996 J Biol Chem 271 3 1379-84 Protein transport protein SEC9 protein G3860 protein YGR009c Putative t-SNARE of the plasma membrane Sec9p SEC9 protein P40357 P40357 6321446 A55100 Saccharomyces cerevisiae (Baker's yeast) 651 MGLKKFFKIKPPEEATPEQNKDTLMELGISVKNPSKKRKEKFAAYGKFANDKAEDKVYAPPGYEQYARPQDELEDLNASPLDANANEATAGSNRGSSGTQDLGNGAESNSMQDPYAIENDDYRYDDDPYARFQANKSNGRGSVNAAPYGDYGGGYNGTSLNSYNNDGPYSNQNTSNSWVNANGRNSLNHSNSTLNVGPSRQTRQPPVSTSTNSLSLDQRSPLANPMQEKRNPYADMNSYGGAYDSNTNRSSGTRQGSSKNANPYASMANDSYSNGNLNRSANPYSSRSVRQPQSQQAPMTYTPSFIASDEAARNSEVDLNEEPRTGEFDFEEVYADKSAENRAALDEPDLNAVMTNEDSIDLNASEVDHSSRQQQQQQWFMDEQQQQQQHFNATNNQYGDQRGYKTFEEIQKEEEARQQQEEDEAVDEIKQEIKFTKQSSVASTRNTLKMAQDAERAGMNTLGMLGHQSEQLNNVEGNLDLMKVQNKVADEKVAELKKLNRSILAVHVSNPFNSKRRRREREEQLKNRKIEEKLMREQTSQQLSQSTQRIEGAMNANNNISEVRERYQRKNVLEKAKRYQFENDEEDDEMELEIDRNLDQIQQVSNRLKKMALTTGKELDSQQKRLNNIEESTDDLDINLHMNTNRLAGIR Disordered - Extended 1 651 MGLKKFFKIKPPEEATPEQNKDTLMELGISVKNPSKKRKEKFAAYGKFANDKAEDKVYAPPGYEQYARPQDELEDLNASPLDANANEATAGSNRGSSGTQDLGNGAESNSMQDPYAIENDDYRYDDDPYARFQANKSNGRGSVNAAPYGDYGGGYNGTSLNSYNNDGPYSNQNTSNSWVNANGRNSLNHSNSTLNVGPSRQTRQPPVSTSTNSLSLDQRSPLANPMQEKRNPYADMNSYGGAYDSNTNRSSGTRQGSSKNANPYASMANDSYSNGNLNRSANPYSSRSVRQPQSQQAPMTYTPSFIASDEAARNSEVDLNEEPRTGEFDFEEVYADKSAENRAALDEPDLNAVMTNEDSIDLNASEVDHSSRQQQQQQWFMDEQQQQQQHFNATNNQYGDQRGYKTFEEIQKEEEARQQQEEDEAVDEIKQEIKFTKQSSVASTRNTLKMAQDAERAGMNTLGMLGHQSEQLNNVEGNLDLMKVQNKVADEKVAELKKLNRSILAVHVSNPFNSKRRRREREEQLKNRKIEEKLMREQTSQQLSQSTQRIEGAMNANNNISEVRERYQRKNVLEKAKRYQFENDEEDDEMELEIDRNLDQIQQVSNRLKKMALTTGKELDSQQKRLNNIEESTDDLDINLHMNTNRLAGIR Native Function arises via a disorder to order transition Molecular assembly Protein-protein binding Paper 10048921 Fiebig KM, Rice LM, Pollock E, Brunger AT 1999 Nat Struct Biol 6 2 117-23 Sec9 is completely disordered in isolation, but acquires some structure when forming a complex with Sso1. Disordered 401 651 QRGYKTFEEIQKEEEARQQQEEDEAVDEIKQEIKFTKQSSVASTRNTLKMAQDAERAGMNTLGMLGHQSEQLNNVEGNLDLMKVQNKVADEKVAELKKLNRSILAVHVSNPFNSKRRRREREEQLKNRKIEEKLMREQTSQQLSQSTQRIEGAMNANNNISEVRERYQRKNVLEKAKRYQFENDEEDDEMELEIDRNLDQIQQVSNRLKKMALTTGKELDSQQKRLNNIEESTDDLDINLHMNTNRLAGIR Complex Engineered Fragment Function arises via a disorder to order transition Molecular assembly Protein-protein binding Far-UV circular dichroism (CD) 298 8.4 phosphate buffer 10 sodium chloride 300 Fluorescent probes 298 8.4 Sncl 2.5 sodium chloride 300 sodium phosphate 10 Aberrant mobility on SDS-PAGE gel Paper 9326367 Rice LM, Brennwald P, Brunger AT 1997 FEBS Lett 415 1 49-55 Transcription factor p65 Nuclear factor NF-kappa-B p65 subunit Q04207 Mus musculus (Mouse) 549 MDDLFPLIFPSEPAQASGPYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINGYTGPGTVRISLVTKDPPHRPHPHELVGKDCRDGYYEADLCPDRSIHSFQNLGIQCVKKRDLEQAISQRIQTNNNPFHVPIEEQRGDYDLNAVRLCFQVTVRDPAGRPLLLTPVLSHPIFDNRAPNTAELKICRVNRNSGSCLGGDEIFLLCDKVQKEDIEVYFTGPGWEARGSFSQADVHRQVAIVFRTPPYADPSLQAPVRVSMQLRRPSDRELSEPMEFQYLPDTDDRHRIEEKRKRTYETFKSIMKKSPFNGPTEPRPPTRRIAVPTRNSTSVPKPAPQPYTFPASLSTINFDEFSPMLLPSGQISNQALALAPSSAPVLAQTMVPSSAMVPLAQPPAPAPVLTPGPPQSLSAPVPKSTQAGEGTLSEALLHLQFDADEDLGALLGNSTDPGVFTDLASVDNSEFQQLLNQGVSMSHSTAEPMLMEYPEAITRLVTGSQRPPDPAPTPLGTSGLPNGLSGDEDFSSIADMDFSALLSQISS Disordered 321 326 PTEPRP Complex Engineered Fragment 1K3ZA Relationship to function unknown Unknown Unknown X-ray crystallography Paper 12686541 Malek S, Huang DB, Huxford T, Ghosh S, Ghosh G 2003 J Biol Chem 278 25 23094-100 Disordered 309 326 FKSIMKKSPFNGPTEPRP Complex Engineered Fragment 1K3ZB Relationship to function unknown Unknown Unknown X-ray crystallography Paper 12686541 Malek S, Huang DB, Huxford T, Ghosh S, Ghosh G 2003 J Biol Chem 278 25 23094-100 Small proline-rich protein 2E Small proline rich protein Small proline-rich protein II SPR-2E SPR-II P22531 P22531 338423 B27725 Homo sapiens (Human) 72 MSYQQQQCKQPCQPPPVCPTPKCPEPCPPPKCPEPCPPPKCPQPSPPQQCQQKCPPVTPSPPCQPKCPPKSK Disordered - Extended 1 20 MSYQQQQCKQPCQPPPVCPT Native Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Aberrant mobility on SDS-PAGE gel 310 TGase 1 or 3 trypsin Near-UV circular dichroism (CD) spectroscopy Phosphate Buffer Sensitivity to proteolysis 310 TGase 1 or 3 trypsin Thermal stability 293 Paper 3133554 Kartasova T, van de Putte P 1988 Mol Cell Biol 8 5 2195-2203 9722562 Tarcsa E, Candi E, Kartasova T, Idler WW, Marekov LN, Steinert PM 1998 J Biol Chem 273 36 23297-23303 Disordered - Extended 48 72 QQCQQKCPPVTPSPPCQPKCPPKSK Native Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Aberrant mobility on SDS-PAGE gel 310 TGase 1 or 3 trypsin Near-UV circular dichroism (CD) spectroscopy 293 Phosphate Buffer Sensitivity to proteolysis 310 TGase 1 or 2 trypsin Thermal stability 293 Paper 3133554 Kartasova T, van de Putte P 1988 Mol Cell Biol 8 5 2195-2203 9722562 Tarcsa E, Candi E, Kartasova T, Idler WW, Marekov LN, Steinert PM 1998 J Biol Chem 273 36 23297-23303 tropomodulin Q91006 Q91006 562263 A55463 Gallus gallus (Chicken) 359 MSYRKELEKYRDLDEDKILGALTEEELRKLENELEELDPDNALLPAGLRQRDQTQKPPTGPFKREELMAHLEQQAKDIKDREDLVPFTGEKRGKAWIPKQKPMDPVLESVTLEPELEEALANASDAELCDIAAILGMHTLMSNQQYYEALGSSTIVNKEGLNSVIKPTKYKPVPDEEPNSTDVEETLKRIQNNDPDLEEVNLNNIMNIPVPTLKALAEALKTNTYVKKFSIVGTRSNDPVAFALAEMLKVNNTLKSLNVESNFISGSGILALVEALQSNTSLIELRIDNQSQPLGNNVEMEIANMLEKNTTLLKFGYHFTQQGPRLRASNAMMNNNDLVRKRRLAELNGPIFPKCRTGV Disordered N-terminal capping domain 1 92 MSYRKELEKYRDLDEDKILGALTEEELRKLENELEELDPDNALLPAGLRQRDQTQKPPTGPFKREELMAHLEQQAKDIKDREDLVPFTGEKR Fragment Function arises via a disorder to order transition Molecular assembly Protein-protein binding Far-UV circular dichroism (CD) 6.5 100 mM NaCl, 10 mM sodium phosphate 5 to 20 microM peptide Nuclear magnetic resonance (NMR) 283 6.5 0.8 mM 13C15N labeled peptide 100 mM NaCl, 10 mM sodium phosphate, 5% D2O 1.1 mM 15N labeled peptide Paper 11423419 Kostyukova AS, Tiktopulo EI, Maeda Y. 2001 Biophys J 81 1 345-51 15475586 Greenfield NJ, Kostyukova AS, Hitchcock-DeGregori SE. 2005 Biophys J 88 1 372-83 Calsequestrin, skeletal muscle isoform precursor 58K dihydropyridine-binding protein Aspartactin Calmitine Calsequestrin 1 Calsequestrin precursor, fast skeletal muscle Laminin-binding protein P07221 P07221 164842 A25887 Oryctolagus cuniculus (Rabbit) 395 MNAADRMGARVALLLLLVLGSPQSGVHGEEGLDFPEYDGVDRVINVNAKNYKNVFKKYEVLALLYHEPPEDDKASQRQFEMEELILELAAQVLEDKGVGFGLVDSEKDAAVAKKLGLTEEDSIYVFKEDEVIEYDGEFSADTLVEFLLDVLEDPVELIEGERELQAFENIEDEIKLIGYFKNKDSEHYKAFKEAAEEFHPYIPFFATFDSKVAKKLTLKLNEIDFYEAFMEEPVTIPDKPNSEEEIVNFVEEHRRSTLRKLKPESMYETWEDDMDGIHIVAFAEEADPDGYEFLEILKSVAQDNTDNPDLSIIWIDPDDFPLLVPYWEKTFDIDLSAPQIGVVNVTDADSVWMEMDDEEDLPSAEELEDWLEDVLEGEINTEDDDDEDDDDDDDD Disordered - Extended 1 395 MNAADRMGARVALLLLLVLGSPQSGVHGEEGLDFPEYDGVDRVINVNAKNYKNVFKKYEVLALLYHEPPEDDKASQRQFEMEELILELAAQVLEDKGVGFGLVDSEKDAAVAKKLGLTEEDSIYVFKEDEVIEYDGEFSADTLVEFLLDVLEDPVELIEGERELQAFENIEDEIKLIGYFKNKDSEHYKAFKEAAEEFHPYIPFFATFDSKVAKKLTLKLNEIDFYEAFMEEPVTIPDKPNSEEEIVNFVEEHRRSTLRKLKPESMYETWEDDMDGIHIVAFAEEADPDGYEFLEILKSVAQDNTDNPDLSIIWIDPDDFPLLVPYWEKTFDIDLSAPQIGVVNVTDADSVWMEMDDEEDLPSAEELEDWLEDVLEGEINTEDDDDEDDDDDDDD Isoform Native Function arises via a disorder to order transition Molecular assembly Protein-protein binding Substrate/ligand binding Near-UV circular dichroism (CD) spectroscopy 7.5 Nuclear magnetic resonance (NMR) 278 7.5 Analytical ultracentrifugation Aberrant mobility on SDS-PAGE gel 7.5 Paper 4472093 Ostwald TJ, MacLennan DH, Dorrington KJ 1974 J Biol Chem 249 18 5867-71 6725251 Cozens B, Reithmeier RA 1984 J Biol Chem 259 10 6248-52 6480588 Aaron BM, Oikawa K, Reithmeier RA, Sykes BD 1984 J Biol Chem 259 19 11876-81 Disordered 1 4 MNAA Isoform Native 1A8YA Function arises via a disorder to order transition Unknown Protein-protein binding Substrate/ligand binding X-ray crystallography 277 6.5 Paper 9628486 Wang S, Trumble WR, Liao H, Wesson CR, Dunker AK, Kang CH 1998 Nat Struct Biol 5 6 476-83 Disordered 328 333 EKTFDI Isoform Native 1A8YA Function arises via a disorder to order transition Unknown Protein-protein binding Substrate/ligand binding X-ray crystallography 277 6.5 Paper 9628486 Wang S, Trumble WR, Liao H, Wesson CR, Dunker AK, Kang CH 1998 Nat Struct Biol 5 6 476-83 Disordered 352 367 WMEMDDEEDLPSAEEL Isoform Native 1A8YA Function arises via a disorder to order transition Unknown Protein-protein binding Substrate/ligand binding X-ray crystallography 277 6.5 Paper 9628486 Wang S, Trumble WR, Liao H, Wesson CR, Dunker AK, Kang CH 1998 Nat Struct Biol 5 6 476-83 Measles virus phosphoprotein polymerase-associated nucleocapsid phosphoprotein P protein P03422 P03422 P03422 331804 RRNZM Measles virus (strain Edmonston) (Subacute sclerose panencephalitis virus) 507 MAEEQARHVKNGLECIRALKAEPIGSLAIEEAMAAWSEISDNPGQERATCREEKAGSSGLSKPCLSAIGSTEGGAPRIRGQGPGESDDDAETLGIPPRNLQASSTGLQCYYVYDHSGEAVKGIQDADSIMVQSGLDGDSTLSGGDNESENSDVDIGEPDTEGYAITDRGSAPISMGFRASDVETAEGGEIHELLRLQSRGNNFPKLGKTLNVPPPPDPGRASTSGTPIKKGTERRLASFGTEIASLLTGGATQCARKSPSEPSGPGAPAGNVPECVSNAALIQEWTPESGTTISPRSQNNEEGGDYYDDELFSDVQDIKTALAKIHEDNQKIISKLESLLLLKGEVESIKKQINRQNISISTLEGHLSSIMIAIPGLGKDPNDPTADVEINPDLKPIIGRDSGRALAEVLKKPVASRQLQGMTNGRTSSRGQLLKEFQLKPIGKKMSSAVGFVPDTGPASRSVIRSIIKSSRLEEDRKRYLMTLLDDIKGANDLAKFHQMLMKIIMK Disordered region within the PCT domain 304 376 GDYYDDELFSDVQDIKTALAKIHEDNQKIISKLESLLLLKGEVESIKKQINRQNISISTLEGHLSSIMIAIPG Native Function arises from the disordered state Molecular assembly Protein-protein binding Protein-tRNA binding Far-UV circular dichroism (CD) 293 7 10 mM sodium phosphate buffer 1-mm-thick quartz cells Sensitivity to proteolysis 298 7.8 1 mg/ml protein in 20 mM Tris/HCl Horse heart cytochrome c (type VI) and thermolysin protease:protein substrate ratio 1:100 Dynamic light scattering 293 8 1 mg/ml protein in 100 mM NaCl Gel filtration/size exclusion chromatography 7 100 mM NaCl 50 mM sodium phosphate buffer Superdex 200 column Nuclear magnetic resonance (NMR) 300 5.6 0.3 mM protein 30 mM NaCl 50 mM sodium acetate Paper 12069524 Karlin D, Longhi S, Receveur V, Canard B. 2002 Virology 296 2 251-62 The detection methods were carried out on the full PCT domain of measles virus phosphoprotein. The PONDR program was used to predict the location of intrinsically disordered regions within this domain. Disordered region within PCT domain 432 507 QLLKEFQLKPIGKKMSSAVGFVPDTGPASRSVIRSIIKSSRLEEDRKRYLMTLLDDIKGANDLAKFHQMLMKIIMK Native Function arises from the disordered state Molecular assembly Protein-protein binding Protein-tRNA binding Far-UV circular dichroism (CD) 293 7 10 mM sodium phosphate buffer 1-mm-thick quartz cells Sensitivity to proteolysis 298 7.8 1 mg/ml protein in 20 mM Tris/HCl Horse heart cytochrome c (type VI) and thermolysin protease:protein substrate ratio 1:100 Dynamic light scattering 293 8 1 mg/ml protein in 100 mM NaCl Gel filtration/size exclusion chromatography 7 100 mM NaCl 50 mM sodium phosphate buffer Superdex 200 column Nuclear magnetic resonance (NMR) 300 5.6 0.3 mM protein 30 mM NaCl 50 mM sodium acetate Paper 12069524 Karlin D, Longhi S, Receveur V, Canard B. 2002 Virology 296 2 251-62 The detection methods were carried out on the full PCT domain of measles virus phosphoprotein. The PONDR program was used to predict the location of intrinsically disordered regions within this domain. Fragile X mental retardation 1 protein FMR1 FMRP fragile X mental retardation syndrome protein Protein FMR-1 Q99054 Q06787 457235 A40724 Homo sapiens (Human) 632 MEELVVEVRGSNGAFYKAFVKDVHEDSITVAFENNWQPDRQIPFHDVRFPPPVGYNKDINESDEVEVYSRANEKEPCCWWLAKVRMIKGEFYVIEYAACDATYNEIVTIERLRSVNPNKPATKDTFHKIKLDVPEDLRQMCAKEAAHKDFKKAVGAFSVTYDPENYQLVILSINEVTSKRAHMLIDMHFRSLRTKLSLIMRNEEASKQLESSRQLASRFHEQFIVREDLMGLAIGTHGANIQQARKVPGVTAIDLDEDTCTFHIYGEDQDAVKKARSFLEFAEDVIQVPRNLVGKVIGKNGKLIQEIVDKSGVVRVRIEAENEKNVPQEEEIMPPNSLPSNNSRVGPNAPEEKKHLDIKENSTHFSQPNSTKVQRVLVASSVVAGESQKPELKAWQGMVPFVFVGTKDSIANATVLLDYHLNYLKEVDQLRLERLQIDEQLRQIGASSRPPPNRTDKEKSYVTDDGQGMGRGSRPYRNRGHGRRGPGYTSGTNSEASNASETESDHRDELSDWSLAPTEEERESFLRRGDGRRRGGGGRGQGGRGRGGGFKGNDDHSRTDNRPRNPREAKGRTTDGSLQIRVDCNNERSVHTKTLQNTSSEGSRLRTGKDRNQKKEKPDSVDGQQPLVNGVP Disordered KH2 domain 281 422 FAEDVIQVPRNLVGKVIGKNGKLIQEIVDKSGVVRVRIEAENEKNVPQEEEIMPPNSLPSNNSRVGPNAPEEKKHLDIKENSTHFSQPNSTKVQRVLVASSVVAGESQKPELKAWQGMVPFVFVGTKDSIANATVLLDYHLN Fragment Function arises via an order to disorder transition Protein-mRNA binding Far-UV circular dichroism (CD) 298 0.1 cm pathlength 17 microM protein Nuclear magnetic resonance (NMR) 300 0.5–1.0 mM samples in 90% H2O/10% D2O Paper 10496225 Adinolfi S, Bagni C, Musco G, Gibson T, Mazzarella L, Pastore A 1999 5 9 1248-58 Disordered FCT domain 516 632 APTEEERESFLRRGDGRRRGGGGRGQGGRGRGGGFKGNDDHSRTDNRPRNPREAKGRTTDGSLQIRVDCNNERSVHTKTLQNTSSEGSRLRTGKDRNQKKEKPDSVDGQQPLVNGVP Fragment Function arises from the disordered state Protein-mRNA binding Far-UV circular dichroism (CD) 298 10 microM protein Paper 10496225 Adinolfi S, Bagni C, Musco G, Gibson T, Mazzarella L, Pastore A 1999 5 9 1248-58 Heat shock transcription factor Heat shock factor protein HSF HSTF P11529 P10961 171708 A31593 Saccharomyces cerevisiae (Baker's yeast) 833 MNNAANTGTTNESNVSDAPRIEPLPSLNDDDIEKILQPNDIFTTDRTDASTTSSTAIEDIINPSLDPQSAASPVPSSSFFHDSRKPSTSTHLVRRGTPLGIYQTNLYGHNSRENTNPNSTLLSSKLLAHPPVPYGQNPDLLQHAVYRAQPSSGTTNAQPRQTTRRYQSHKSRPAFVNKLWSMLNDDSNTKLIQWAEDGKSFIVTNREEFVHQILPKYFKHSNFASFVRQLNMYGWHKVQDVKSGSIQSSSDDKWQFENENFIRGREDLLEKIIRQKGSSNNHNSPSGNGNPANGSNIPLDNAAGSNNSNNNISSSNSFFNNGHLLQGKTLRLMNEANLGDKNDVTAILGELEQIKYNQIAISKDLLRINKDNELLWQENMMARERHRTQQQALEKMFRFLTSIVPHLDPKMIMDGLGDPKVNNEKLNSANNIGLNRDNTGTIDELKSNDSFINDDRNSFTNATTNARNNMSPNNDDNSIDTASTNTTNRKKNIDENIKNNNDIINDIIFNTNLANNLSNYNSNNNAGSPIRPYKQRYLLKNRANSSTSSENPSLTPFDIESNNDRKISEIPFDDEEEEETDFRPFTSRDPNNQTSENTFDPNRFTMLSDDDLKKDSHTNDNKHNESDLFWDNVHRNIDEQDARLQNLENMVHILSPGYPNKSFNNKTSSTNTNSNMESAVNVNSPGFNLQDYLTGESNSPNSVHSVPSNGSGSTPLPMPNDNDTEHASTSVNQGENGSGLTPFLTVDDHTLNDNNTSEGSTRVSPDIKFSATENTKVSDNLPSFNDHSYSTQADTAPENAKKRFVEEIPEPAIVEIQDPTEYNDHRLPKRAKK Disordered N-terminal activation domain 1 167 MNNAANTGTTNESNVSDAPRIEPLPSLNDDDIEKILQPNDIFTTDRTDASTTSSTAIEDIINPSLDPQSAASPVPSSSFFHDSRKPSTSTHLVRRGTPLGIYQTNLYGHNSRENTNPNSTLLSSKLLAHPPVPYGQNPDLLQHAVYRAQPSSGTTNAQPRQTTRRYQ Native Function arises from the disordered state Molecular assembly Protein-protein binding Transactivation (transcriptional activation) Nuclear magnetic resonance (NMR) heteronuclear NOE spectrum pH 3.4 and 5.75 Far-UV circular dichroism (CD) 298 7 1 mg/mL protein solutions in 25 mM sodium phosphate buffer Paper 8745404 Cho HS, Liu CW, Damberger FF, Pelton JG, Nelson HC, Wemmer DE 1996 Protein Sci 5 2 262-9 Histone H1.2 H1d Histone H1d P15865 P15865 204595 JH0159 Rattus norvegicus (Rat) 217 MSETAPAAPAAPAPAEKTPIKKKARKAAGGAKRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPKAKKAGAAKAKKPAGAAKKPKKATGTATPKKSTKKTPKKAKKPAAGAKKAKSPKKAKATKAKKAPKSPAKARAVKPKAAKPKTSKPKAAKPKKTAAKKK Disordered - Extended 1 30 MSETAPAAPAAPAPAEKTPIKKKARKAAGG Complex Engineered Function arises via a disorder to order transition Molecular assembly Protein-DNA binding Protein-protein binding Near-UV circular dichroism (CD) spectroscopy 7.5 Paper 9109385 Tarkka T, Oikarinen J, Grundstrom T 1997 FEBS Lett 406 1-2 56-60 2373370 Cole KD, Kandala JC, Kremer E, Kistler WS 1990 Gene 89 2 265-9 Disordered - Molten Globule 31 119 AKRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPK Complex Engineered Function arises via a molten globule to order transition Molecular assembly Protein-DNA binding Protein-protein binding Near-UV circular dichroism (CD) spectroscopy 7.5 Paper 9109385 Tarkka T, Oikarinen J, Grundstrom T 1997 FEBS Lett 406 1-2 56-60 2373370 Cole KD, Kandala JC, Kremer E, Kistler WS 1990 Gene 89 2 265-9 Disordered - Extended 120 217 AKKAGAAKAKKPAGAAKKPKKATGTATPKKSTKKTPKKAKKPAAGAKKAKSPKKAKATKAKKAPKSPAKARAVKPKAAKPKTSKPKAAKPKKTAAKKK Complex Engineered Function arises via a disorder to order transition Molecular assembly Protein-DNA binding Protein-protein binding Near-UV circular dichroism (CD) spectroscopy 7.5 Paper 9109385 Tarkka T, Oikarinen J, Grundstrom T 1997 FEBS Lett 406 1-2 56-60 2373370 Cole KD, Kandala JC, Kremer E, Kistler WS 1990 Gene 89 2 265-9 Hirudin variant-1 Lepirudin Thrombin inhibitor P01050 P01050 124981 HULXH Hirudo medicinalis (Medicinal leech) 65 VVYTDCTESGQNLCLCEGSNVCGQGNKCILGSDGEKNQCVTGEGTPKPQSHNDGDFEEIPEEYLQ Disordered - Extended C-Terminal Tail 50 65 SHNDGDFEEIPEEYLQ Native 1HRTA 2HIRA 5HIRA Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 300 D20 H20 Paper 2567183 Folkers PJ, Clore GM, Driscoll PC, Dodt J, Kohler S, Gronenborn AM 1989 Biochemistry 28 6 2601-17 3013692 Dodt J, Schmitz T, Schafer T, Bergmann C 1986 FEBS Lett 202 2 373-7 Parathyroid hormone-related protein precursor PTHrP PTH-rP P12272 Hs.89626 P12272 39995091 PTHU2L Homo sapiens (Human) 177 MQRRLVQQWSVAVFLLSYAVPSCGRSVEGLSRRLKRAVSEHQLLHDKGKSIQDLRRRFFLHHLIAEIHTAEIRATSEVSPNSKPSPNTKNHPVRFGSDDEGRYLTQETNKVETYKEQPLKTPGKKKKGKPGKRKEQEKKKRRTRSAWLDSGVTGSGLEGDHLSDTSTTSLELDSRRH Disordered - Extended 1 4 MQRR Engineered Fragment Relationship to function unknown Molecular assembly Molecular recognition effectors Protein-protein binding Substrate/ligand binding Far-UV circular dichroism (CD) 298 5.1 Nuclear magnetic resonance (NMR) 277 5.1 Paper 10050767 Weidler M, Marx UC, Seidel G, Schafer W, Hoffmann E, Esswein A, Rosch P 1999 FEBS Lett 444 2-3 239-244 8138348 Willis KJ 1994 Int J Pept Protein Res 43 1 23-28 Disordered - Extended 9 15 WSVAVFL Engineered Fragment Function arises via a disorder to order transition Molecular assembly Molecular recognition effectors Flexible linkers/spacers Far-UV circular dichroism (CD) 298 5.1 Nuclear magnetic resonance (NMR) 277 5.1 Paper 10050767 Weidler M, Marx UC, Seidel G, Schafer W, Hoffmann E, Esswein A, Rosch P 1999 FEBS Lett 444 2-3 239-244 8138348 Willis KJ 1994 Int J Pept Protein Res 43 1 23-28 Disordered - Extended 28 34 EGLSRRL Engineered Fragment Relationship to function unknown Molecular assembly Molecular recognition effectors Protein-protein binding Substrate/ligand binding Far-UV circular dichroism (CD) 298 5.1 Nuclear magnetic resonance (NMR) 277 5.1 Paper 10050767 Weidler M, Marx UC, Seidel G, Schafer W, Hoffmann E, Esswein A, Rosch P 1999 FEBS Lett 444 2-3 239-244 8138348 Willis KJ 1994 Int J Pept Protein Res 43 1 23-28 50S ribosomal protein L2 P02387 26249909 B85997 Escherichia coli 273 MAVVKCKPTSPGRRHVVKVVNPELHKGKPFAPLLEKNSKSGGRNNNGRITTRHIGGGHKQAYRIVDFKRNKDGIPAVVERLEYDPNRSANIALVLYKDGERRYILAPKGLKAGDQIQSGVDAAIKPGNTLPMRNIPVGSTVHNVEMKPGKGGQLARSAGTYVQIVARDGAYVTLRLRSGEMRKVEADCRATLGEVGNAEHMLRVLGKAGAARWRGVRPTVRGTAMNPVDHPHGGGEGRNFGKHPVTPWGVQTKGKKTRSNKRTDKFIVRRRSK Disordered 1 273 MAVVKCKPTSPGRRHVVKVVNPELHKGKPFAPLLEKNSKSGGRNNNGRITTRHIGGGHKQAYRIVDFKRNKDGIPAVVERLEYDPNRSANIALVLYKDGERRYILAPKGLKAGDQIQSGVDAAIKPGNTLPMRNIPVGSTVHNVEMKPGKGGQLARSAGTYVQIVARDGAYVTLRLRSGEMRKVEADCRATLGEVGNAEHMLRVLGKAGAARWRGVRPTVRGTAMNPVDHPHGGGEGRNFGKHPVTPWGVQTKGKKTRSNKRTDKFIVRRRSK Paper 3297162 Littlechild J, Malcolm A, Paterakis K, Ackermann I, Dijk J 1987 Biochim Biophys Acta 913 2 245-55 50S ribosomal protein L27 50S ribosomal subunit protein L27 Ribosomal protein L27 P02427 P02427 16131075 R5EC27 Escherichia coli 85 MAHKKAGGSTRNGRDSEAKRLGVKRFGGESVLAGSIIVRQRGTKFHAGANVGCGRDHTLFAKADGKVKFEVKGPKNRKFISIEAE Disordered 1 85 MAHKKAGGSTRNGRDSEAKRLGVKRFGGESVLAGSIIVRQRGTKFHAGANVGCGRDHTLFAKADGKVKFEVKGPKNRKFISIEAE Native Relationship to function unknown Molecular assembly Protein-protein binding Near-UV circular dichroism (CD) spectroscopy 277 7 beta-mercaptoethanol 1 sodium phosphate 1 Nuclear magnetic resonance (NMR) 293 7 2D heteronuclear NMR M9 medium with 15NH4SO4 supplement beta-mercaptoethanol 1 sodium phosphate 1 Tetramethylsilane phosphate as internal chemical shift standard Nuclear magnetic resonance (NMR) 353 7 2D heteronuclear NMR M9 medium with 15NH4SO4 supplement beta-mercaptoethanol 1 sodium phosphate 1 Tetramethylsilane phosphate as internal chemical shift standard Paper 11673426 Maguire BA, Manuilov AV, Zimmermann RA 2001 J Bacteriol 183 22 6565-72 3297162 Littlechild J, Malcolm A, Paterakis K, Ackermann I, Dijk J 1987 Biochim Biophys Acta 913 2 245-55 Smad anchor for receptor activation hSARA Madh-interacting protein Mothers against decapentaplegic homolog interacting protein Novel serine protease NSP Receptor activation anchor zinc finger, FYVE domain containing 9 isoform 3 O95405 O95405 O95405 47717106 Homo sapiens (Human) 1425 MENYFQAEAYNLDKVLDEFEQNEDETVSSTLLDTKWNKILDPPSHRLSFNPTLASVNESAVSNESQPQLKVFSLAHSAPLTTEEEDHCANGQDCNLNPEIATMWIDENAVAEDQLIKRNYSWDDQCSAVEVGEKKCGNLACLPDEKNVLVVAVMHNCDKRTLQNDLQDCNNYNSQSLMDAFSCSLDNENRQTDQFSFSINESTEKDMNSEKQMDPLNRPKTEGRSVNHLCPTSSDSLASVCSPSQLKDDGSIGRDPSMSAITSLTVDSVISSQGTDGCPAVKKQENYIPDEDLTGKISSPRTDLGSPNSFSHMSEGILMKKEPAEESTTEESLRSGLPLLLKPDMPNGSGRNNDCERCSDCLVPNEVRADENEGYEHEETLGTTEFLNMTEHFSESQDMTNWKLTKLNEMNDSQVNEEKEKFLQISQPEDTNGDSGGQCVGLADAGLDLKGTCISESEECDFSTVIDTPAANYLSNGCDSYGMQDPGVSFVPKTLPSKEDSVTEEKEIEESKSECYSNIYEQRGNEATEGSGLLLNSTGDLMKKNYLHNFCSQVPSVLGQSSPKVVASLPSISVPFGGARPKQPSNLKLQIPKPLSDHLQNDFPANSGNNTKNKNDILGKAKLGENSATNVCSPSLGNISNVDTNGEHLESYEAEISTRPCLALAPDSPDNDLRAGQFGISARKPFTTLGEVAPVWVPDSQAPNCMKCEARFTFTKRRHHCRACGKVFCASCCSLKCKLLYMDRKEARVCVICHSVLMNAQAWENMMSASSQSPNPNNPAEYCSTIPPLQQAQASGALSSPPPTVMVPVGVLKHPGAEVAQPREQRRVWFADGILPNGEVADAAKLTMNGTSSAGTLAVSHDPVKPVTTSPLPAETDICLFSGSITQVGSPVGSAMNLIPEDGLPPILISTGVKGDYAVEEKPSQISVMQQLEDGGPDPLVFVLNANLLSMVKIVNYVNRKCWCFTTKGMHAVGQSEIVILLQCLPDEKCLPKDIFNHFVQLYRDALAGNVVSNLGHSFFSQSFLGSKEHGGFLYVTSTYQSLQDLVLPTPPYLFGILIQKWETPWAKVFPIRLMLRLGAEYRLYPCPLFSVRFRKPLFGETGHTIMNLLADFRNYQYTLPVVQGLVVDMEVRKTSIKIPSNRYNEMMKAMNKSNEHVLAGGACFNEKADSHLVCVQNDDGNYQTQAISIHNQPRKVTGASFFVFSGALKSSSGYLAKSSIVEDGVMVQITAENMDSLRQALREMKDFTITCGKADAEEPQEHIHIQWVDDDKNVSKGVVSPIDGKSMETITNVKIFHGSEYKANGKVIRWTEVFFLENDDQHNCLSDPADHSRLTEHVAKAFCLALCPHLKLLKEDGMTKLGLRVTLDSDQVGYQAGSNGQPLPSQYMNDLDSALVPVIHGGACQLSEGPVVMELIFYILENIV Disordered Smad binding domain 663 751 ALAPDSPDNDLRAGQFGISARKPFTTLGEVAPVWVPDSQAPNCMKCEARFTFTKRRHHCRACGKVFCASCCSLKCKLLYMDRKEARVCV Native Function arises via a disorder to order transition Molecular assembly Protein-protein binding Nuclear magnetic resonance (NMR) Paper 15231848 Chong PA, Ozdamar B, Wrana JL, Forman-Kay JD 2004 J Biol Chem 279 39 40707-14 Hsp25 Growth-related 25 kDa protein Heat shock 27 kDa protein Heat-shock protein beta-1 HSP 27 HspB1 P25 P14602 Mm.13849 P14602 194012 JN0679 Mus musculus (Mouse) 209 MTERRVPFSLLRSPSWEPFRDWYPAHSRLFDQAFGVPRLPDEWSQWFSAAGWPGYVRPLPAATAEGPAAVTLAAPAFSRALNRQLSSGVSEIRQTADRWRVSLDVNHFAPEELTVKTKEGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTLVSSSLSPEGTLTVEAPLPKAVTQSAEITIPVTFEARAQIGGPEAGKSEQSGAK Disordered C-terminal extension 192 209 RAQIGGPEAGKSEQSGAK Native Function arises from the disordered state Chaperones Nuclear magnetic resonance (NMR) Paper 7649277 Carver JA, Esposito G, Schwedersky G, Gaestel M. 1995 FEBS Lett 369 2-3 305-10 50S ribosomal protein L33 P02436 132895 G91192 Escherichia coli 55 MAKGIREKIKLVSSAGTGHFYTTTKNKRTKPEKLELKKFDPVVRQHVIYKEAKIK Disordered 1 55 MAKGIREKIKLVSSAGTGHFYTTTKNKRTKPEKLELKKFDPVVRQHVIYKEAKIK Paper 3297162 Littlechild J, Malcolm A, Paterakis K, Ackermann I, Dijk J 1987 Biochim Biophys Acta 913 2 245-55 Histone mRNA Binding Protein Histone RNA hairpin-binding protein SLBP Stem-loop binding protein Q9VAN6 Q9VAN6 9789800 Drosophila melanogaster (Fruit fly) 276 MLCEDQHMSVENTPQKGSGSLNSSASSISIDVKPTMQSWAQEVRAEFGHSDEASSSLNSSAASCGSLAKKETADGNLESKDGEGREMAFEFLDGVNEVKFERLVKEEKLKTPYKRRHSFTPPSNENSRSNSPNSSNSSANGDAAAPKGGNNPHSRNSKKSGNFRAHKEEKRVRHNSYTSSTSSSSSYTEADPAILSRRQKQIDYGKNTAAYERYVEMVPKDERTRDHPRTPNKYGKYSRRAFDGLVKIWRKSLHIYDPPTQARDTAKDSNSDSDSD Disordered N-terminal domain 1 175 MLCEDQHMSVENTPQKGSGSLNSSASSISIDVKPTMQSWAQEVRAEFGHSDEASSSLNSSAASCGSLAKKETADGNLESKDGEGREMAFEFLDGVNEVKFERLVKEEKLKTPYKRRHSFTPPSNENSRSNSPNSSNSSANGDAAAPKGGNNPHSRNSKKSGNFRAHKEEKRVRHN Fragment Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 298 7 2D (15N,1H) HSQC and 3D HNCA 3D (13C, 1H) NOESY-HSQC (mixing time of 100 ms) 3D (15N,1H) NOESY-HSQC (mixing time of 75 ms) 3D HNHA 600 MHz Far-UV circular dichroism (CD) 298 7 20 mM sodium phosphate 50 microM protein Paper 15260482 Thapar R, Mueller GA, Marzluff WF 2004 43 29 9390-400 The N-terminal domain of SLBP is intrinsically or natively unfolded but it has transient helical structure in four regions. The N-terminal domain of SLBP gives one cross-peak per residue indicating that, although unfolded, the different conformations are in fast exchange on the NMR time scale. 30S ribosomal protein S12 P02367 133737 A98153 Escherichia coli 124 MATVNQLVRKPRARKVAKSNVPALEACPQKRGVCTRVYTTTPKKPNSALRKVCRVRLTNGFEVTSYIGGEGHNLQEHSVILIRGGRVKDLPGVRYHTVRGALDCSGVKDRKQARSKYGVKRPKA Disordered 1 124 MATVNQLVRKPRARKVAKSNVPALEACPQKRGVCTRVYTTTPKKPNSALRKVCRVRLTNGFEVTSYIGGEGHNLQEHSVILIRGGRVKDLPGVRYHTVRGALDCSGVKDRKQARSKYGVKRPKA Paper 6751823 Venyaminov SY, Gogia ZV 1982 Eur J Biochem 126 2 299-309 30S ribosomal protein S18 P02374 133836 B86117 Escherichia coli 75 MARYFRRRKFCRFTAEGVQEIDYKDIATLKNYITESGKIVPSRITGTRAKYQRQLARAIKRARYLSLLPYTDRHQ Disordered 1 75 MARYFRRRKFCRFTAEGVQEIDYKDIATLKNYITESGKIVPSRITGTRAKYQRQLARAIKRARYLSLLPYTDRHQ Paper 6751823 Venyaminov SY, Gogia ZV 1982 Eur J Biochem 126 2 299-309 30S ribosomal protein S19 P02375 133848 A85997 Escherichia coli 92 MPRSLKKGPFIDLHLLKKVEKAVESGDKKPLRTWSRRSTIFPNMIGLTIAVHNGRQHVPVFVTDEMVGHKLGEFAPTRTYRGHAADKKAKKK Disordered 1 92 MPRSLKKGPFIDLHLLKKVEKAVESGDKKPLRTWSRRSTIFPNMIGLTIAVHNGRQHVPVFVTDEMVGHKLGEFAPTRTYRGHAADKKAKKK Paper 6751823 Venyaminov SY, Gogia ZV 1982 Eur J Biochem 126 2 299-309 NCp7 NC71 nucleocapsid protein Q9PY17 Q9PY17 247852 Human immunodeficiency virus 1 (HIV-1) 71 MQRGNFRNQRKMVKCFNCGKEGHTARNCRAPRKKGCWKCGKEGHQMKDCTERQANFLGKIWPSYKGRPGNF Disordered - Extended 1 71 MQRGNFRNQRKMVKCFNCGKEGHTARNCRAPRKKGCWKCGKEGHQMKDCTERQANFLGKIWPSYKGRPGNF Native Function arises from the disordered state Chaperones DNA unwinding Protein-tRNA binding Nuclear magnetic resonance (NMR) 293 5.5 100% D20 5.0 mM protein 600 MHz 'H frequency Paper 1304355 Summers MF, Henderson LE, Chance MR, Bess JW Jr, South TL, Blake PR, Sagi I, Perez-Alvarado G, Sowder RC 3rd, Hare DR, et al. 1992 1 5 563-74 1639074 Morellet N, Jullian N, De Rocquigny H, Maigret B, Darlix JL, Roques BP 1992 11 8 3059-65 Cardiac phospholamban Phospholamban PLB P26678 P26678 4505887 A40424 Homo sapiens (Human) 52 MEKVQYLTRSAIRRASTIEMPQQARQKLQNLFINFCLILICLLLICIIVMLL Disordered - Extended 1 25 MEKVQYLTRSAIRRASTIEMPQQAR Engineered Fragment Function arises from the disordered state Molecular recognition effectors Phosphorylation Substrate/ligand binding Near-UV circular dichroism (CD) spectroscopy 283 7 peptide 60 sodium phosphate 10 Nuclear magnetic resonance (NMR) 3 H2O/D2O 90 protein varying concentrations between 1.8 and 4.0 mM Nuclear magnetic resonance (NMR) 3 protein varying concentrations between 1.8 and 4.0 mM TFE-d3/H2O 30 Nuclear magnetic resonance (NMR) 3 H2O/300 mM SDS-d25(MSD isotopes) 90 protein varying concentrations between 1.8 and 4.0 mM Paper 7779806 Mortishire-Smith RJ, Pitzenberger SM, Burke CJ, Middaugh CR, Garsky VM, Johnson RG 1995 Biochemistry 34 23 7603-13 Disordered - Extended 17 25 TIEMPQQAR Engineered Fragment Function arises via a disorder to order transition Molecular recognition effectors Phosphorylation Protein-protein binding Near-UV circular dichroism (CD) spectroscopy 283 7 peptide 60 sodium phosphate 10 Nuclear magnetic resonance (NMR) 3 H2O/D2O 90 protein varying concentrations between 1.8 and 4.0 mM Nuclear magnetic resonance (NMR) 3 protein varying concentrations between 1.8 and 4.0 mM TFE-d3/H2O 90 Nuclear magnetic resonance (NMR) 3 H2O/300 mM SDS-d25(MSD isotopes) 90 protein varying concentrations between 1.8 and 4.0 mM Paper 7779806 Mortishire-Smith RJ, Pitzenberger SM, Burke CJ, Middaugh CR, Garsky VM, Johnson RG 1995 Biochemistry 34 23 7603-13 This region adopts a helical structure in aqueous trifluoroethanol. Growth factor receptor-bound protein 14 GRB14 adapter protein Q14449 Q14449 59802920 Homo sapiens 540 MTTSLQDGQSAASRAAARDSPLAAQVCGAAQGRGDAHDLAPAPWLHARALLPLPDGTRGCAADRRKKKDLDVPEMPSIPNPFPELCCSPFTSVLSADLFPKANSRKKQVIKVYSEDETSRALDVPSDITARDVCQLLILKNHYIDDHSWTLFEHLPHIGVERTIEDHELVIEVLSNWGIEEENKLYFRKNYAKYEFFKNPMYFFPEHMVSFATETNGEISPTQILQMFLSSSTYPEIHGFLHAKEQGKKSWKKIYFFLRRSGLYFSTKGTSKEPRHLQFFSEFGNSDIYVSLAGKKKHGAPTNYGFCFKPNKAGGPRDLKMLCAEEEQSRTCWVTAIRLLKYGMQLYQNYMHPYQGRSGCSSQSISPMRSISENSLVAMDFSGQKSRVIENPTEALSVAVEEGLAWRKKGCLRLGTHGSPTASSQSSATNMAIHRSQPWFHHKISRDEAQRLIIQQGLVDGVFLVRDSQSNPKTFVLSMSHGQKIKHFQIIPVEDDGEMFHTLDDGHTRFTDLIQLVEFYQLNKGVLPCKLKHYCARIAL Disordered PIR domain 361 435 SSQSISPMRSISENSLVAMDFSGQKSRVIENPTEALSVAVEEGLAWRKKGCLRLGTHGSPTASSQSSATNMAIHR Native Function arises via a disorder to order transition Protein-protein binding Nuclear magnetic resonance (NMR) 300 Paper 14623073 Moncoq K, Broutin I, Larue V, Perdereau D, Cailliau K, Browaeys-Poly E, Burnol AF, Ducruix A. 2003 FEBS Lett 554 3 240-246 Neurofilament triplet L protein 68 kDa neurofilament protein Neurofilament light polypeptide NF-L P02547 P02547 71551 QFPGL Sus scrofa (Pig) 548 SSFYSEPYYSTSYKRRYVETPRVHISSVRSGYSTARSAYSSYSAPVSSSLSVRRSYSSSSGLMPSLENLDLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAQLLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLKKVHEEEIAELQAQIQYAQISVEMDVSSKPDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELEDKQNADISAMQDTINKLENELRTTKSEMARYLKEYQDLLNVKMALDIEIAAYRKLLEGEETRLSFTSVGSLTTGYSQSSQVFGRSAYGGLQTSSYLMSTRSFPSYYTSHVQEEQIEVEETIEAAKAEEAKDEPPSEGEAEEEGKEKEEAEAEAEAEEEGAQEEEEAAEKEESEEAKEEEGGEGEQGEETKEAEEEEKKDEGAGEEQATKKKD Disordered - Extended 443 548 TSHVQEEQIEVEETIEAAKAEEAKDEPPSEGEAEEEGKEKEEAEAEAEAEEEGAQEEEEAAEKEESEEAKEEEGGEGEQGEETKEAEEEEKKDEGAGEEQATKKKD Native Function arises from the disordered state Entropic chain Entropic bristle Fourier transform infrared spectroscopy 277 7.5 Paper 8634266 Heimburg T, Schuenemann J, Weber K, Geisler N 1996 Biochemistry 35 5 1375-82 3920075 Geisler N, Plessmann U, Weber K 1985 FEBS Lett 182 2 475-8 DNA repair protein XRCC4 X-ray repair cross-complementing protein 4 XRCC4 Q13426 Hs.171190 Q13426 5706611 Homo sapiens (Human) 336 MERKISRIHLVSEPSITHFLQVSWEKTLESGFVITLTDGHSAWTGTVSESEISQEADDMAMEKGKYVGELRKALLSGAGPADVYTFNFSKESCYFFFEKNLKDVSFRLGSFNLEKVENPAEVIRELICYCLDTIAENQAKNEHLQKENERLLRDWNDVQGRFEKCVSAKEALETDLYKRFILVLNEKKTKIRSLHNKLLNAAQEREKDIKQEGETAICSEMTADRDPVYDESTDEESENQTDLSGLASAAVSKDDSIISSLDVTDIAPSRKRRQRMQRNLGTEPKMAPQENQLQEKENSRPDSSLPETSKKEHISAENMSLETLRNSSPEDLFDEI Disordered 212 213 EG Engineered Fragment 1IK9A Relationship to function unknown Molecular assembly Protein-DNA binding X-ray crystallography 6 2-(N-morpholino)ethanesulfonic acid 0.1 NaCl buffer 150 PEG 6000 (w/v) 3 protein 100 Tris-HCl pH 8.0 20 xylitol precipitant solution (w/v) 3 Paper 11702069 Sibanda BL, Critchlow SE, Begun J, Pei XY, Jackson SP, Blundell TL, Pellegrini L 2001 Nat Struct Biol 8 12 1015-9 The experiments were conducted using a fragment of Xrcc4 spanning residues 1 - 213. Disordered 77 80 GAGP Engineered Fragment 1IK9A Relationship to function unknown Unknown Unknown X-ray crystallography 6 2-(N-morpholino)ethanesulfonic acid 0.1 NaCl buffer 150 PEG 6000 (w/v) 3 protein 100 Tris-HCl pH 8.0 20 xylitol precipitant solution (w/v) 3 Paper 11702069 Sibanda BL, Critchlow SE, Begun J, Pei XY, Jackson SP, Blundell TL, Pellegrini L 2001 Nat Struct Biol 8 12 1015-9 The experiments were conducted using a fragment of Xrcc4 spanning residues 1 - 213. Disordered 77 82 GAGPAD Engineered Fragment 1IK9B Relationship to function unknown Unknown Unknown X-ray crystallography 6 2-(N-morpholino)ethanesulfonic acid 0.1 NaCl buffer 150 PEG 6000 (w/v) 3 protein 100 Tris-HCl pH 8.0 20 xylitol precipitant solution (w/v) 3 Paper 11702069 Sibanda BL, Critchlow SE, Begun J, Pei XY, Jackson SP, Blundell TL, Pellegrini L 2001 Nat Struct Biol 8 12 1015-9 The experiments were conducted using a fragment of Xrcc4 spanning residues 1 - 213. Disordered 202 213 AQEREKDIKQEG Engineered Fragment 1IK9B Relationship to function unknown Molecular assembly Protein-DNA binding X-ray crystallography 6 2-(N-morpholino)ethanesulfonic acid 0.1 NaCl buffer 150 PEG 6000 (w/v) 3 protein 100 Tris-HCl pH 8.0 20 xylitol precipitant solution (w/v) 3 Paper 11702069 Sibanda BL, Critchlow SE, Begun J, Pei XY, Jackson SP, Blundell TL, Pellegrini L 2001 Nat Struct Biol 8 12 1015-9 The experiments were conducted using a fragment of Xrcc4 spanning residues 1 - 213. Disordered 204 265 EREKDIKQEGETAICSEMTADRDPVYDESTDEESENQTDLSGLASAAVSKDDSIISSLDVTD Fragment 1FU1A Relationship to function unknown Unknown Unknown X-ray crystallography 293 6.5 ammonium sulfate well solution 1.2 DTT well solution 10 magnesium acetate well solution 10 protein per mL 8 sodium cacodylate well solution 100 Paper 11080143 Junop MS, Modesti M, Guarne A, Ghirlando R, Gellert M, Yang W 2000 Embo J 19 22 5962-70 The experiments were conducted using a fragment of Xrcc4 spanning residues 1 - 265. Disordered - Extended 179 203 RFILVLNEKKTKIRSLHNKLLNAAQ Fragment 1FU1A Function arises via a disorder to order transition Molecular assembly Protein-DNA binding X-ray crystallography 293 6.5 ammonium sulfate well solution 1.2 DTT well solution 10 magnesium acetate well solution 10 protein per mL 8 sodium cacodylate well solution 100 Paper 11080143 Junop MS, Modesti M, Guarne A, Ghirlando R, Gellert M, Yang W 2000 Embo J 19 22 5962-70 This region is disordered in the S subunit. The experiments were conducted using a fragment of Xrcc4 spanning residues 1 - 213. Ras GTPase c-bas/has oncogene c-Ha-ras protein c-Harvey-ras protein c-H-p21 Ras c-H-ras protein H-ras H-ras oncogene Transforming protein p21/H-Ras-1 (c-H-ras) P01112 Hs.37003 P01112 131869 TVHUH Homo sapiens (Human) 189 MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPGCMSCKCVLS Disordered - Extended 10 13 GAGG Complex Engineered Fragment Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Nuclear magnetic resonance (NMR) 5.5 1H2O 90 2H2O 10 MgCl2 10 Na2HPO4-NaH2PO4 20 NaCl 150 Paper 9230043 Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T 1997 Biochemistry 36 30 9109-9119 Disordered - Extended 10 16 GAGGVGK Complex Engineered Fragment Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Nuclear magnetic resonance (NMR) 5.5 1H2O 90 2H2O 10 MgCl2 10 Na2HPO4-NaH2PO4 20 NaCl 150 Paper 9230043 Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T 1997 Biochemistry 36 30 9109-9119 Disordered 21 21 I Complex Engineered Fragment Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Nuclear magnetic resonance (NMR) 5.5 1H2O 90 2H2O 10 MgCl2 10 Na2HPO4-NaH2PO4 20 NaCl 150 Paper 9230043 Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T 1997 Biochemistry 36 30 9109-9119 Disordered 27 32 HFVDEY Complex Engineered Fragment Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Nuclear magnetic resonance (NMR) 5.5 1H2O 90 2H2O 10 MgCl2 10 Na2HPO4-NaH2PO4 20 NaCl 150 Nuclear magnetic resonance (NMR) 303 D2O 10 DTT 5 GDP 30 H2O 90 MgCl2 5 NaCl 40 sodium azide 0.01 Tris-maleate-d15 pH 6.5 20 Nuclear magnetic resonance (NMR) 303 D2O 100 DTT 5 GDP 30 MgCl2 5 NaCl 40 sodium azide 0.01 Tris-maleate-d15 pH 6.5 20 Paper 9230043 Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T 1997 Biochemistry 36 30 9109-9119 8142349 Kraulis PJ, Domaille PJ, Campbell-Burk SL, Van Aken T, Laue ED 1994 Biochemistry 33 12 3515-3531 Disordered 30 38 DEYDPTIED Complex Engineered Fragment 1CRPA 1CRQA 1CRRA 1Q21A Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 303 6.5 D2O 10 DTT 5 GDP 30 H2O 90 MgCl2 5 NaCl 40 sodium azide 0.01 Tris-maleate-d15 20 Nuclear magnetic resonance (NMR) 303 6.5 D2O 100 DTT 5 GDP 30 MgCl2 5 NaCl 40 sodium azide 0.01 Tris-maleate-d15 20 X-ray crystallography Paper 8142349 Kraulis PJ, Domaille PJ, Campbell-Burk SL, Van Aken T, Laue ED 1994 Biochemistry 33 12 3515-3531 2406906 Milburn MV, Tong L, deVos AM, Brunger A, Yamaizumi Z, Nishimura S, Kim SH 1990 Science 247 4945 939-945 Disordered 31 39 EYDPTIEDS Complex Engineered Fragment 1AA9A Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Nuclear magnetic resonance (NMR) 5.5 1H2O 90 2H2O 10 MgCl2 10 Na2HPO4-NaH2PO4 20 NaCl 150 Paper 9230043 Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T 1997 Biochemistry 36 30 9109-9119 Disordered 32 38 YDPTIED Complex Engineered Fragment Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding X-ray crystallography 298 1,6-hexanediol 60 2,2,2-trifluoroethanol 50 isopropanol 50 Paper 12842038 Buhrman G, de Serrano V, Mattos C 2003 Structure (Camb) 11 7 747-751 Disordered 32 40 YDPTIEDSY Complex Engineered Fragment Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Nuclear magnetic resonance (NMR) 5.5 1H2O 90 2H2O 10 MgCl2 10 Na2HPO4-NaH2PO4 20 NaCl 150 Paper 9230043 Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T 1997 Biochemistry 36 30 9109-9119 Disordered 57 61 DTAGQ Complex Engineered Fragment Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Nuclear magnetic resonance (NMR) 5.5 1H2O 90 2H2O 10 MgCl2 10 Na2HPO4-NaH2PO4 20 NaCl 150 Paper 9230043 Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T 1997 Biochemistry 36 30 9109-9119 Disordered 57 64 DTAGQEEY Complex Engineered Fragment 1AA9A 1IOZA Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Nuclear magnetic resonance (NMR) 5.5 1H2O 90 2H2O 10 MgCl2 10 Na2HPO4-NaH2PO4 20 NaCl 150 Paper 9230043 Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T 1997 Biochemistry 36 30 9109-9119 Disordered 58 66 TAGQEEYSA Complex Engineered Fragment 1AA9A 1CRPA 1CRQA 1CRRA 1IOZA Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Nuclear magnetic resonance (NMR) 303 D2O 10 DTT 5 GDP 30 H2O 90 MgCl2 5 NaCl 40 sodium azide 0.01 Tris-maleate-d15 pH 6.5 20 Nuclear magnetic resonance (NMR) 303 5.5 D2O 100 DTT 5 GDP 30 MgCl2 5 NaCl 40 sodium azide 0.01 Tris-maleate-d15 pH 6.5 20 Nuclear magnetic resonance (NMR) 5.5 1H2O 90 2H2O 10 MgCl2 10 Na2-HPO4-NaH2PO4 20 NaCl 150 X-ray crystallography Paper 9230043 Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T 1997 Biochemistry 36 30 9109-9119 8142349 Kraulis PJ, Domaille PJ, Campbell-Burk SL, Van Aken T, Laue ED 1994 Biochemistry 33 12 3515-3531 2406906 Milburn MV, Tong L, deVos AM, Brunger A, Yamaizumi Z, Nishimura S, Kim SH 1990 Science 247 4945 939-945 Disordered 59 72 AGQEEYSAMRDQYM Complex Engineered Fragment 121PA 1P2UA Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding X-ray crystallography 298 1,6-hexanediol 60 2,2,2-trifluoroethanol 50 isopropanol 50 Paper 12842038 Buhrman G, de Serrano V, Mattos C 2003 Structure (Camb) 11 7 747-751 Disordered 60 64 GQEEY Complex Engineered Fragment 4Q21A Relationship to function unknown Unknown Unknown X-ray crystallography PDB 2406906 Milburn MV, Tong L, deVos AM, Brunger A, Yamaizumi Z, Nishimura S, Kim SH 1990 Science 247 4945 939-945 Disordered 60 68 GQEEYSAMR Complex Engineered Fragment 1Q21A 6Q21A Relationship to function unknown Unknown Unknown X-ray crystallography Paper 2406906 Milburn MV, Tong L, deVos AM, Brunger A, Yamaizumi Z, Nishimura S, Kim SH 1990 Science 247 4945 939-945 Disordered 61 65 QEEYS Complex Engineered Fragment 1Q21A 6Q21A Relationship to function unknown Unknown Unknown X-ray crystallography Paper 2406906 Milburn MV, Tong L, deVos AM, Brunger A, Yamaizumi Z, Nishimura S, Kim SH 1990 Science 247 4945 939-945 Disordered 62 65 EEYS Complex Engineered Fragment 1Q21A 6Q21A Relationship to function unknown Unknown Unknown X-ray crystallography Paper 2406906 Milburn MV, Tong L, deVos AM, Brunger A, Yamaizumi Z, Nishimura S, Kim SH 1990 Science 247 4945 939-945 Disordered 71 71 Y Complex Engineered Fragment Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Nuclear magnetic resonance (NMR) 5.5 1H2O 90 2H2O 10 MgCl2 10 Na2HPO4-NaH2PO4 20 NaCl 150 Paper 9230043 Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T 1997 Biochemistry 36 30 9109-9119 Disordered 107 109 DDV Complex Engineered Fragment Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Nuclear magnetic resonance (NMR) 303 6.5 D2O 10 DTT 5 GDP 30 H2O 90 MgCl2 5 NaCl 40 sodium azide 0.01 Tris-maleate-d15 20 Nuclear magnetic resonance (NMR) 303 6.5 D2O 100 DTT 5 GDP 30 MgCl2 5 NaCl 40 sodium azide 0.01 Tris-maleate-d15 20 Nuclear magnetic resonance (NMR) 5.5 1H2O 90 2H2O 10 MgCl2 10 Na2-HPO4-NaH2PO4 20 NaCl 150 Paper 9230043 Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T 1997 Biochemistry 36 30 9109-9119 8142349 Kraulis PJ, Domaille PJ, Campbell-Burk SL, Van Aken T, Laue ED 1994 Biochemistry 33 12 3515-3531 Disordered 168 189 LRKLNPPDESGPGCMSCKCVLS Complex Engineered Fragment 4Q21A Relationship to function unknown Unknown Unknown X-ray crystallography Paper 2406906 Milburn MV, Tong L, deVos AM, Brunger A, Yamaizumi Z, Nishimura S, Kim SH 1990 Science 247 4945 939-945 Disordered 172 189 NPPDESGPGCMSCKCVLS Complex Engineered Fragment Relationship to function unknown Unknown Unknown X-ray crystallography Paper 2406906 Milburn MV, Tong L, deVos AM, Brunger A, Yamaizumi Z, Nishimura S, Kim SH 1990 Science 247 4945 939-945 SHC transforming protein 1 SH2 domain protein C1 Src homology 2 domain containing transforming protein C1 P29353 Hs.433795 P29353 52693921 Homo sapiens (Human) 583 MDLLPPKPKYNPLRNESLSSLEEGASGSTPPEELPSPSASSLGPILPPLPGDDSPTTLCSFFPRMSNLRLANPAGGRPGSKGEPGRAADDGEGIDGAAMPESGPLPLLQDMNKLSGGGGRRTRVEGGQLGGEEWTRHGSFVNKPTRGWLHPNDKVMGPGVSYLVRYMGCVEVLQSMRALDFNTRTQVTREAISLVCEAVPGAKGATRRRKPCSRPLSSILGRSNLKFAGMPITLTVSTSSLNLMAADCKQIIANHHMQSISFASGGDPDTAEYVAYVAKDPVNQRACHILECPEGLAQDVISTIGQAFELRFKQYLRNPPKLVTPHDRMAGFDGSAWDEEEEEPPDHQYYNDFPGKEPPLGGVVDMRLREGAAPGAARPTAPNAQTPSHLGATLPVGQPVGGDPEVRKQMPPPPPCPGRELFDDPSYVNVQNLDKARQAVGGAGPPNPAINGSAPRDLFDMKPFEDALRVPPPPQSVSMAEQLRGEPWFHGKLSRREAEALLQLNGDFLVRESTTTPGQYVLTGLQSGQPKHLLLVDPEGVVRTKDHRFESVSHLISYHMDNHLPIISAGSELCLQQPVERKL Disordered - Extended 128 166 QLGGEEWTRHGSFVNKPTRGWLHPNDKVMGPGVSYLVRY Complex Engineered Fragment Isoform Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Substrate/ligand binding Nuclear magnetic resonance (NMR) 308 6.5 Paper 12906822 Farooq A, Zeng L, Yan KS, Ravichandran KS, Zhou MM 2003 Structure (Camb) 11 8 905-13 This entry is from the characterization of the experimental fragment in complex with a 12 residue tyrosine-phosphated peptide. The experimental fragment consisted of residues 128 - 318 of the Swiss-Prot sequence. Disordered - Extended 128 152 QLGGEEWTRHGSFVNKPTRGWLHPN Engineered Fragment Isoform Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Substrate/ligand binding Nuclear magnetic resonance (NMR) 308 6.5 Paper 12906822 Farooq A, Zeng L, Yan KS, Ravichandran KS, Zhou MM 2003 Structure (Camb) 11 8 905-13 This entry is from the characterization of a fragment containing residues 17-207 in solution. The experimental fragment consisted of residues 128 - 318 of the Swiss-Prot sequence. Disordered 303 318 TIGQAFELRFKQYLRN Engineered Fragment Isoform Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Substrate/ligand binding Nuclear magnetic resonance (NMR) 308 6.5 Paper 12906822 Farooq A, Zeng L, Yan KS, Ravichandran KS, Zhou MM 2003 Structure (Camb) 11 8 905-13 This entry is from the characterization of a fragment containing residues 17-207 in solution. The experimental fragment consisted of residues 128 - 318 of the Swiss-Prot sequence. Disordered 311 318 RFKQYLRN Complex Engineered Fragment Isoform Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Substrate/ligand binding Nuclear magnetic resonance (NMR) 308 6.5 Paper 12906822 Farooq A, Zeng L, Yan KS, Ravichandran KS, Zhou MM 2003 Structure (Camb) 11 8 905-13 This entry is from the characterization of the experimental fragment in complex with a 12 residue tyrosine-phosphated peptide. The experimental fragment consisted of residues 128 - 318 of the Swiss-Prot sequence. Syntaxin 1A Neuron-specific antigen HPC-1 P35A Synaptotagmin associated 35 kDa protein P32851 Rn.9943 P32851 417842 A38141 Rattus norvegicus (Rat) 288 MKDRTQELRTAKDSDDDDDVTVTVDRDRFMDEFFEQVEEIRGFIDKIAENVEEVKRKHSAILASPNPDEKTKEELEELMSDIKKTANKVRSKLKSIEQSIEQEEGLNRSSADLRIRKTQHSTLSRKFVEVMSEYNATQSDYRERCKGRIQRQLEITGRTTTSEELEDMLESGNPAIFASGIIMDSSISKQALSEIETRHSEIIKLENSIRELHDMFMDMAMLVESQGEMIDRIEYNVEHAVDYVERAVSDTKKAVKYQSKARRKKIMIIICCVILGIIIASTIGGIFG Disordered - Extended 149 182 IQRQLEITGRTTTSEELEDMLESGNPAIFASGII Engineered Fragment Function arises via a disorder to order transition Molecular assembly Protein-protein binding X-ray crystallography Paper 12680753 Margittai M, Fasshauer D, Jahn R, Langen R 2003 Biochemistry 42 14 4009-4014 The sequence was cited in Fasshauer (1998) and confirmed to match Swiss-Prot ST1A_RAT (P32851) for residues 1-206 which are characterized in this entry. DNA-repair protein hHR23A UV excision repair protein RAD23 homolog A P54725 Hs.440960 P54725 1709983 S44443 Homo sapiens (Human) 363 MAVTITLKTLQQQTFKIRMEPDETVKVLKEKIEAEKGRDAFPVAGQKLIYAGKILSDDVPIRDYRIDEKNFVVVMVTKTKAGQGTSAPPEASPTAAPESSTSFPPAPTSGMSHPPPAAREDKSPSEESAPTTSPESVSGSVPSSGSSGREEDAASTLVTGSEYETMLTEIMSMGYERERVVAALRASYNNPHRAVEYLLTGIPGSPEPEHGSVQESQVSEQPATEAAGENPLEFLRDQPQFQNMRQVIQQNPALLPALLQQLGQENPQLLQQISRHQEQFIQMLNEPPGELADISDVEGEVGAIGEEAPQMNYIQVTPQEKEAIERLKALGFPESLVIQAYFACEKNENLAANFLLSQNFDDE Disordered - Extended 79 160 TKAGQGTSAPPEASPTAAPESSTSFPPAPTSGMSHPPPAAREDKSPSEESAPTTSPESVSGSVPSSGSSGREEDAASTLVTG Function arises from the disordered state Molecular assembly Flexible linkers/spacers Nuclear magnetic resonance (NMR) Paper 14557549 Walters, K. J. Lech, P. J. Goh, A. M. Wang, Q. Howley, P. M. 2003 Proc Natl Acad Sci U S A 100 22 12694-12699 Disordered - Extended 201 231 GIPGSPEPEHGSVQESQVSEQPATEAAGENP Function arises from the disordered state Molecular assembly Flexible linkers/spacers Nuclear magnetic resonance (NMR) Paper 14557549 Walters KJ, Lech PJ, Goh AM, Wang Q, Howley PM 2003 Proc Natl Acad Sci U S A 100 22 12694-12699 Disordered - Extended 283 316 MLNEPPGELADISDVEGEVGAIGEEAPQMNYIQV Function arises from the disordered state Molecular assembly Flexible linkers/spacers Nuclear magnetic resonance (NMR) Paper 14557549 Walters KJ, Lech PJ, Goh AM, Wang Q, Howley PM 2003 Proc Natl Acad Sci U S A 100 22 12694-12699 Ordered UBL 3 78 VTITLKTLQQQTFKIRMEPDETVKVLKEKIEAEKGRDAFPVAGQKLIYAGKILSDDVPIRDYRIDEKNFVVVMVTK Engineered Function arises from the ordered state Molecular assembly Protein-protein binding Nuclear magnetic resonance (NMR) Paper 14557549 Walters KJ, Lech PJ, Goh AM, Wang Q, Howley PM 2003 Proc Natl Acad Sci U S A 100 22 12694-12699 The UBL region interacts with UBA domains of the same protein. It is unable to bind to both simultaneously, but does so in equilibrium with each. Ordered UBA1 161 200 SEYETMLTEIMSMGYERERVVAALRASYNNPHRAVEYLLT Engineered Function arises from the ordered state Relationship to function unknown Molecular assembly Protein-protein binding Nuclear magnetic resonance (NMR) Paper 14557549 Walters KJ, Lech PJ, Goh AM, Wang Q, Howley PM 2003 Proc Natl Acad Sci U S A 100 22 12694-12699 The UBA1 domain binds with the UBL domain of the same protein. It does so at equilibrium with UBA2. Ordered XBC-binding 232 282 LEFLRDQPQFQNMRQVIQQNPALLPALLQQLGQENPQLLQQISRHQEQFIQ Engineered Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) Paper 14557549 Walters KJ, Lech PJ, Goh AM, Wang Q, Howley PM 2003 Proc Natl Acad Sci U S A 100 22 12694-12699 Ordered UBA2 317 359 TPQEKEAIERLKALGFPESLVIQAYFACEKNENLAANFLLSQN Engineered Function arises from the ordered state Molecular assembly Protein-protein binding Nuclear magnetic resonance (NMR) Paper 14557549 Walters KJ, Lech PJ, Goh AM, Wang Q, Howley PM 2003 Proc Natl Acad Sci U S A 100 22 12694-12699 The UBA2 domain binds with the UBL domain of the same protein. It does so at equilibrium with UBA1. SipA Salmonella invasion protein A Q56034 Q56034 1172128 Q56034 Salmonella typhimurium 684 MVTSVRTQPPVIMPGMQTEIKTQATNLAANLSAVRAKCHSDAVREIKGPQLEDFPALIKQASLDALFKCGKDAEALKEVFTNSNNVAGKKAIMEFAGLFRSALNATSDSPEAKTLLMKVGAEYAAQIIKDGLKEKSAFGPWLPETKKAEAKLENLEKQLLDIIKNNTGGELSKLSTNLVMQEVMPYIASCIEHNFGCTLDPLTRSNLTHLVDKAAAKAVEALDMCPQKLTQEQGTSVGREARHLEMQTLIPLLLRNVFAQIPADKLPDPKIPEPAAGPVPDGGKKAEPTGINININIDSSNHSVDNSKHINNAEPVDNGQRHIDNSNHDNSRKTIDNSRTFIDNSQRNGESHHSTNSSNVSHSHSRVDSTTHQTETAHSASTGAIDHGIAGKIDVTAHATAEAVTNASSESKDGKVVTSEKGTTGETTSFDEVDGVTSKSIIGKPVQATVHGVDDNKQQSQTAEIVNVKPLASQLAGVENVKTDTLQSDTTVITGNKAGTTDNDNSQTDKTGPFSGLKFKQNSFLSTVPSVTNMHSMHFDARETFLGVIRKALEPDTSTPFPVRRAFDGLRAEILPNDTIKSAALKAQCSDIDKHPELKAKMETLKEVITHHPQKEKLAEIALQFAREAGLTRLKGETDYVLSNVLDGLIGDGSWRAGPAYESYLNKPGVDRVITTVDGLHMQR Disordered - Extended 425 512 GETTSFDEVDGVTSKSIIGKPVQATVHGVDDNKQQSQTAEIVNVKPLASQLAGVENVKTDTLQSDTTVITGNKAGTTDNDNSQTDKTG Engineered Fragment 1Q5ZA Function arises from the disordered state Molecular assembly Protein-protein binding X-ray crystallography Rotory shadowing electron microscopy Sensitivity to proteolysis Paper 14512630 Lilic M, Galkin VE, Orlova A, VanLoock MS, Egelman EH, Stebbins CE 2003 Science 301 5641 1918-1921 Ordered 513 657 PFSGLKFKQNSFLSTVPSVTNMHSMHFDARETFLGVIRKALEPDTSTPFPVRRAFDGLRAEILPNDTIKSAALKAQCSDIDKHPELKAKMETLKEVITHHPQKEKLAEIALQFAREAGLTRLKGETDYVLSNVLDGLIGDGSWRA Engineered Fragment 1Q5ZA Function arises from the ordered state Molecular assembly Polymerization X-ray crystallography Rotory shadowing electron microscopy Sensitivity to proteolysis Paper 14512630 Lilic M, Galkin VE, Orlova A, VanLoock MS, Egelman EH, Stebbins CE 2003 Science 301 5641 1918-1921 Disordered - Extended 658 684 GPAYESYLNKPGVDRVITTVDGLHMQR Engineered Fragment 1Q5ZA Function arises from the disordered state Molecular assembly Protein-protein binding X-ray crystallography Rotory shadowing electron microscopy Sensitivity to proteolysis Paper 14512630 Lilic M, Galkin VE, Orlova A, VanLoock MS, Egelman EH, Stebbins CE 2003 Science 301 5641 1918-1921 IF7 Ssl1911 protein P73124 7469343 S75236 Synechocystis sp. 65 MSTQQQARALMMRHHQFIKNRQQSMLSRAAAEIGVEAEKDFWTTVQGKPQSSFRTTYDRSNASLS Disordered 1 65 MSTQQQARALMMRHHQFIKNRQQSMLSRAAAEIGVEAEKDFWTTVQGKPQSSFRTTYDRSNASLS Native Relationship to function unknown Protein-protein binding Fourier transform infrared spectroscopy 283 NaCl pH 6.5 0.1 Tris 10 Nuclear magnetic resonance (NMR) 298 Phosphate buffer pH 6.5 10 Nuclear magnetic resonance (NMR) 278 Phosphate buffer pH 6.5 10 Gel filtration/size exclusion chromatography 298 NaCl 150 Far-UV circular dichroism (CD) 298 Near-UV circular dichroism (CD) spectroscopy Thermal stability 298K-363 K Paper 12824490 Muro-Pastor MI, Barrera FN, Reyes JC, Florencio FJ, Neira JL 2003 Protein Sci 12 7 1443-1454 Epithelial-cadherin precursor ARC-1 Cadherin-1 E-cadherin Uvomorulin P09803 P09803 115419 IJMSCE Mus musculus (Mouse) 884 MGARCRSFSALLLLLQVSSWLCQELEPESCSPGFSSEVYTFPVPERHLERGHVLGRVRFEGCTGRPRTAFFSEDSRFKVATDGTITVKRHLKLHKLETSFLVRARDSSHRELSTKVTLKSMGHHHHRHHHRDPASESNPELLMFPSVYPGLRRQKRDWVIPPISCPENEKGEFPKNLVQIKSNRDKETKVFYSITGQGADKPPVGVFIIERETGWLKVTQPLDREAIAKYILYSHAVSSNGEAVEDPMEIVITVTDQNDNRPEFTQEVFEGSVAEGAVPGTSVMKVSATDADDDVNTYNAAIAYTIVSQDPELPHKNMFTVNRDTGVISVLTSGLDRESYPTYTLVVQAADLQGEGLSTTAKAVITVKDINDNAPVFNPSTYQGQVPENEVNARIATLKVTDDDAPNTPAWKAVYTVVNDPDQQFVVVTDPTTNDGILKTAKGLDFEAKQQYILHVRVENEEPFEGSLVPSTATVTVDVVDVNEAPIFMPAERRVEVPEDFGVGQEITSYTAREPDTFMDQKITYRIWRDTANWLEINPETGAIFTRAEMDREDAEHVKNSTYVALIIATDDGSPIATGTGTLLLVLLDVNDNAPIPEPRNMQFCQRNPQPHIITILDPDLPPNTSPFTAELTHGASVNWTIEYNDAAQESLILQPRKDLEIGEYKIHLKLADNQNKDQVTTLDVHVCDCEGTVNNCMKAGIVAAGLQVPAILGILGGILALLILILLLLLFLRRRTVVKEPLLPPDDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTLMSVPQYRPRPANPDEIGNFIDENLKAADSDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDQDQDYDYLNEWGNRFKKLADMYGGGEDD Disordered 580 728 TGTLLLVLLDVNDNAPIPEPRNMQFCQRNPQPHIITILDPDLPPNTSPFTAELTHGASVNWTIEYNDAAQESLILQPRKDLEIGEYKIHLKLADNQNKDQVTTLDVHVCDCEGTVNNCMKAGIVAAGLQVPAILGILGGILALLILILL Engineered Function arises via a disorder to order transition Molecular assembly Protein-protein binding Far-UV circular dichroism (CD) 273 7 phosphate 10 Fluorescence anisotropy DTT 1 NaCl buffer 20 protein 12 Tris-HCl or HEPES pH 7.0 to 8.5 (10 to 100 mM) Fluorescence anisotropy B-mercaptoethanol 10 NaCl buffer 20 protein 12 Tris-HCl or HEPES pH 7.0 to 8.5 (10 to 100 mM) Fluorescence anisotropy 7 guanidine HCl 6 protein 12 Tris-HCl 100 Nuclear magnetic resonance (NMR) 323 8 D2O 50 NaCl 10 trimethyl silyl propionate 0.35 Tris-HCl 5 Nuclear magnetic resonance (NMR) 298 8 D2O 50 NaCl 10 trimethyl silyl propionate 0.35 Tris-HCl 5 Nuclear magnetic resonance (NMR) 276 8 D2O 50 NaCl 10 trimethyl silyl propionate 0.35 Tris-HCl 5 Sensitivity to proteolysis 298 CaCl2 2 CHES pH 9.2 100 DTT 5 Paper 11121423 Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI 2001 J Biol Chem 276 15 12301-12309 Measles virus nucleocapsid protein P04851 127901 Measles virus 525 MATLLRSLALFKRNKDKPPITSGSGGAIRGIKHIIIVPIPGDSSITTRSRLLDRLVRLIGNPDVSGPKLTGALIGILSLFVESPGQLIQRITDDPDVSIRLLEVVQSDQSQSGLTFASRGTNMEDEADQYFSHDDPISSDQSRFGWFENKEISDIEVQDPEGFNMILGTILAQIWVLVAKAVTAPDTAADSELRRWIKYTQQRRVVGEFRLERKWLDVVRNRIAEDLSLRRFMVALILDIKRTPGNKPRIAEMICNIDTYIVEAGLASFILTIKFGIETMYPALGLHEFDGELSTLESLMNLYQQMGETAPYMVILENSIQNKFSAGSYPLLWSYAMGVGVELENSMGGLNFGRSYFDPAYFRLGQEMVRRSAGKVSSTLASELGITAEDARLVSEIAMHTTEDKISRAVGPRQAQVSFLHGDQSENELPRLGGKEDRRVKQSRGEARESYRETGPSRASDARAAHLPTGTPLDIDTASESSQDPQDSRRSADALLRLQAMAGISEEQGSDTDTPIVYNDRNLLD Disordered - Pre-Molten Globule N Tail 400 525 HTTEDKISRAVGPRQAQVSFLHGDQSENELPRLGGKEDRRVKQSRGEARESYRETGPSRASDARAAHLPTGTPLDIDTASESSQDPQDSRRSADALLRLQAMAGISEEQGSDTDTPIVYNDRNLLD Engineered Function arises via a disorder to order transition Molecular assembly Protein-protein binding Nuclear magnetic resonance (NMR) 7 protein 0.5 sodium phosphate 10 Far-UV circular dichroism (CD) 293 7 sodium phosphate 10 TFE increasing concentrations (0,10,20,30) 30 Small-angle X-ray scattering 281 EDTA buffer 5 glycerol radiation scavenger 10 Tris/HCl buffer 10 Dynamic light scattering 7 sodium phosphate 10 Dynamic light scattering 8 NaCl concentrated at 1.25mg/ml. 75 Tris/HCl 10 Gel filtration/size exclusion chromatography Sensitivity to proteolysis Mass spectrometry-based high resolution hydrogen-deuterium exchange N tail purified 1 SDS-PAGE 12 trypsin 0.25 Paper 12621042 Longhi, S. Receveur-Brechot, V. Karlin, D. Johansson, K. Darbon, H. Bhella, D. Yeo, R. Finet, S. Canard, B. 2003 J Biol Chem 278 20 18638-18648 3211755 Buckland, R. Gerald, C. Barker, D. Wild, F. 1988 Nucleic Acids Res 16 24 11821 The experimental NTAIL sequence in the Longhi et al. article contained four additional amino acids plus a 6X Histidine tag fused to the N-terminus of amino acids 399-523 of the SwissProt sequence. The experimental sequence was obtained through direct correspondence with Longhi. The secondary structure predictor, JPRED, predicts an alpha-helix at amino acids 489-504. Cell division protein zipA P77173 P77173 C65015 Escherichia coli 328 MMQDLRLILIIVGAIAIIALLVHGFWTSRKERSSMFRDRPLKRMKSKRDDDSYDEDVEDDEGVGEVRVHRVNHAPANAQEHEAARPSPQHQYQPPYASAQPRQPVQQPPEAQVPPQHAPHPAQPVQQPAYQPQPEQPLQQPVSPQVAPAPQPVHSAPQPAQQAFQPAEPVAAPQPEPVAEPAPVMDKPKRKEAVIIMNVAAHHGSELNGELLLNSIQQAGFIFGDMNIYHRHLSPDGSGPALFSLANMVKPGTFDPEMKDFTTPGVTIFMQVPSYGDELQNFKLMLQSAQHIADEVGGVVLDDQRRMMTPQKLREYQDIIREVKDANA Disordered 29 85 RKERSSMFRDRPLKRMKSKRDDDSYDEDVEDDEGVGEVRVHRVNHAPANAQEHEAAR Paper 12107152 Ohashi T, Hale CA, de Boer PA, Erickson HP 2002 J Bacteriol 184 15 4313-4315 Disordered 86 185 PSPQHQYQPPYASAQPRQPVQQPPEAQVPPQHAPHPAQPVQQPAYQPQPEQPLQQPVSPQVAPAPQPVHSAPQPAQQAFQPAEPVAAPQPEPVAEPAPVM Analytical ultracentrifugation Paper 12107152 Ohashi T, Hale CA, de Boer PA, Erickson HP 2002 J Bacteriol 184 15 4313-4315 Stannin AG8_1 SNN O75324 6094313 Homo sapiens (Human) 88 MSIMDHSPTTGVVTVIVILIAIAALGALILGCWCYLRLQRISQSEDEESIVGDGETKEPFLLVQYSAKGPCVERKAKLMTPNGPEVHG Disordered 36 58 LRLQRISQSEDEESIVGDGETKE Monomeric Flexible linkers/spacers Nuclear magnetic resonance (NMR) 333 d25-SDS 600 DTT 0.05-1 mM H2O 10% NaN3 0.02% Phosphate-buffered saline pH 4.0 20 Paper 16246365 Buck-Koehntop BA, Mascioni A, Buffy JJ, Veglia G 2005 J Mol Biol Gir2 Q03768 Q03768 30913066 Saccharomyces cerevisiae (Baker's yeast) 265 MDYKEEQKQELEVLESIYPDELRIINDEYPKIKFEVAIKLELDTGDSTSVLTKEHTIIAEFKLPENYPDEPCLISLEAQEVALNDNEEDNEEDEDEVEYDDHGNKVLKKFENLPDLISFKGYLPELTVQLESQIETDMLLGMQMCFALISSIKERCEQWYSEQLNKLEKQYELEAQEREKKEQAKFHGTKVTRESYLEWRSKFRQELKLDERDQVRRMKAHHGKLTGKQMFEQGVVGTGDEYMEEDDASVDDVAKGLAKTEIANQ Disordered 1 265 MDYKEEQKQELEVLESIYPDELRIINDEYPKIKFEVAIKLELDTGDSTSVLTKEHTIIAEFKLPENYPDEPCLISLEAQEVALNDNEEDNEEDEDEVEYDDHGNKVLKKFENLPDLISFKGYLPELTVQLESQIETDMLLGMQMCFALISSIKERCEQWYSEQLNKLEKQYELEAQEREKKEQAKFHGTKVTRESYLEWRSKFRQELKLDERDQVRRMKAHHGKLTGKQMFEQGVVGTGDEYMEEDDASVDDVAKGLAKTEIANQ Native Relationship to function unknown Unknown Unknown Aberrant mobility on SDS-PAGE gel Thermal stability Sensitivity to proteolysis Paper 15896712 Alves VS, Castilho BA 2005 Biochem Biophys Res Commun 332 2 450-5. 60S acidic ribosomal protein P1-alpha P05318 Saccharomyces cerevisiae (Baker's yeast) 106 MSTESALSYAALILADSEIEISSEKLLTLTNAANVPDENIWADIFAKALDGQNLKDLLVNFSAGAAAPAGVAGGVAGGEAGEAEAEKEEEEAKEESDDDMGFGLFD Disordered 1 106 MSTESALSYAALILADSEIEISSEKLLTLTNAANVPDENIWADIFAKALDGQNLKDLLVNFSAGAAAPAGVAGGVAGGEAGEAEAEKEEEEAKEESDDDMGFGLFD Native Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Far-UV circular dichroism (CD) Nuclear magnetic resonance (NMR) Intrinsic fluorescence Thermal stability Sensitivity to proteolysis Paper 10913306 Zurdo J, Gonzalez C, Sanz JM, Rico M, Remacha M, Ballesta JP 2000 Biochemistry 39 30 8935-43 Pyridoxamine 5'-phosphate oxidase EC 1.4.3.5 PNPOx PNP/PMP oxidase P28225 129736 Escherichia coli 218 MSDNDELQQIAHLRREYTKGGLRRRDLPADPLTLFERWLSQACEAKLADPTAMVVATVDEHGQPYQRIVLLKHYDEKGMVFYTNLGSRKAHQIENNPRVSLLFPWHTLERQVMVIGKAERLSTLEVMKYFHSRPRDSQIGAWVSKQSSRISARGILESKFLELKQKFQQGEVPLPSFWGGFRVSLEQIEFWQGGEHRLHDRFLYQRENDAWKIDRLAP Disordered 1 10 MSDNDELQQI Complex Native Function arises via a disorder to order transition Modification site Protein-protein binding X-ray crystallography 100 2-mercaptoethanol 5 HEPES pH 6.8 60 K2PO4 pH 7.5 100 KH2PO4/NH4H2PO4 0.65 protein 5 Paper 15858270 Safo MK, Musayev FN, Schirch V 2005 Acta Crystallogr D Biol Crystallogr 61 Pt 5 599-604 Disorder in this region is found in monomer A of the tetragonal unit cell. Disordered 1 16 MSDNDELQQIAHLRRE Complex Native Function arises via a disorder to order transition Modification site Protein-protein binding X-ray crystallography 100 2-mercaptoethanol 5 HEPES pH 6.8 60 K2PO4 pH 7.5 100 KH2PO4/NH4H2PO4 0.65 protein 5 Paper 15858270 Safo MK, Musayev FN, Schirch V 2005 Acta Crystallogr D Biol Crystallogr 61 Pt 5 599-604 Disorder in this region is found in monomer B of the tetragonal unit cell. Disordered domain 2 130 175 FHSRPRDSQIGAWVSKQSSRISARGILESKFLELKQKFQQGEVPLP Complex Native Function arises from the disordered state Modification site X-ray crystallography 100 2-mercaptoethanol 5 HEPES pH 6.8 60 K2PO4 pH 7.5 100 KH2PO4/NH4H2PO4 0.65 protein 5 Paper 15858270 Safo MK, Musayev FN, Schirch V 2005 Acta Crystallogr D Biol Crystallogr 61 Pt 5 599-604 Disorder in this region is found in monomer A of the tetragonal unit cell. Disordered domain 2 128 175 KYFHSRPRDSQIGAWVSKQSSRISARGILESKFLELKQKFQQGEVPLP Complex Native Function arises from the disordered state Modification site X-ray crystallography 100 2-mercaptoethanol 5 HEPES pH 6.8 60 K2PO4 pH 7.5 100 KH2PO4/NH4H2PO4 0.65 protein 5 Paper 15858270 Safo MK, Musayev FN, Schirch V 2005 Acta Crystallogr D Biol Crystallogr 61 Pt 5 599-604 Disorder in this region is found in monomer B of the tetragonal unit cell. The sequence referenced in the paper has an M at position 1. However, the SwissProt sequence does not include this M. Troponin I, cardiac muscle cardiac troponin I Troponin inhibitory subunit P19429 Hs.512709 P19429 1524066 TPHUIC Homo sapiens (Human) 210 MADGSSDAAREPRPAPAPIRRRSSNYRAYATEPHAKKKSKISASRKLQLKTLLLQIAKQELEREAEERRGEKGRALSTRCQPLELAGLGFAELQDLCRQLHARVDKVDEERYDIEAKVTKNITEIADLTQKIFDLRGKFKRPTLRRVRISADAMMQALLGARAKESLDLRAHLKQVKKEDTEKENREVGDWRKNIDALSGMEGRKKKFES Disordered - Extended 31 34 TEPH Complex Engineered Fragment Mutant 1J1DC 1J1EC Function arises from the disordered state Unknown Unknown X-ray crystallography 293 8 CaCl2 5 glycerol 15% LiCl 0.1 PEG 3350 20% protein 10 Tris-HCl 50 Paper 12840750 Takeda S, Yamashita A, Maeda K, Maeda Y 2003 Nature 424 6944 35-41 Disordered - Extended 66 89 EERRGEKGRALSTRCQPLELAGLG Complex Engineered Fragment Mutant Function arises via a disorder to order transition Molecular assembly Flexible linkers/spacers Protein-protein binding X-ray crystallography 293 8 CaCl2 5 glycerol 15% LiCl 0.1 PEG3350 20% protein 10 Tris-HCl 50 Paper 12840750 Takeda S, Yamashita A, Maeda K, Maeda Y 2003 Nature 424 6944 35-41 This disordered region becomes ordered when in complex with Troponin T. Disordered - Extended TnI Inhibitory Region 137 148 GKFKRPTLRRVR Complex Engineered Fragment Mutant Relationship to function unknown Molecular recognition effectors Flexible linkers/spacers Protein-protein binding X-ray crystallography 293 8 CaCl2 5 glycerol 15% LiCl 0.1 PEG3350 20% protein 10 Tris-HCl 50 Paper 12840750 Takeda S, Yamashita A, Maeda K, Maeda Y 2003 Nature 424 6944 35-41 This disordered region is thought to be the binding sites for actin and tropomyosin. Disordered - Extended C-Terminus 163 210 AKESLDLRAHLKQVKKEDTEKENREVGDWRKNIDALSGMEGRKKKFES Complex Engineered Fragment Mutant 1J1EC Function arises via a disorder to order transition Molecular assembly Molecular recognition effectors Flexible linkers/spacers Protein-protein binding X-ray crystallography 293 8 CaCl2 5 glycerol 15% LiCl 0.1 PEG3350 20% protein 10 Tris-HCl 50 Paper 12840750 Takeda S, Yamashita A, Maeda K, Maeda Y 2003 Nature 424 6944 35-41 Residues 163-191 were disordered in one of the two Troponin I molecules that were obtained through crystallization. Disordered - Extended 189 191 GDW Complex Engineered Fragment Mutant Function arises via a disorder to order transition Molecular assembly Molecular recognition effectors Flexible linkers/spacers Protein-protein binding X-ray crystallography 293 8 CaCl2 5 glycerol 15% LiCl 0.1 PEG3350 20% Tris-HCl 50 Paper 12840750 Takeda S, Yamashita A, Maeda K, Maeda Y 2003 Nature 424 6944 35-41 This disordered region undergoes a conformational change when interacting with other Troponin moledules. Disordered - Extended C-terminus 192 210 RKNIDALSGMEGRKKKFES Complex Engineered Fragment Mutant 1J1EF Function arises via a disorder to order transition Molecular assembly Protein-protein binding X-ray crystallography 293 8 CaCl2 5 glycerol 15% LiCl 0.1 PEG3350 20% protein 10 Tris-HCl 50 Paper 12840750 Takeda S, Yamashita A, Maeda K, Maeda Y 2003 Nature 424 6944 35-41 Ras-related protein Rap-2a K-REV member of RAS oncogene family RAP2 RAP2A ras-related protein rap2 RbBP-30 transforming protein rap2 P10114 Hs.165636 P10114 10518344 S03180 Homo sapiens (Human) 183 MREYKVVVLGSGGVGKSALTVQFVTGTFIEKYDPTIEDFYRKEIEVDSSPSVLEILDTAGTEQFASMRDLYIKNGQGFILVYSLVNQQSFQDIKPMRDQIIRVKRYEKVPVILVGNKVDLESEREVSSSEGRALAEEWGCPFMETSAKSKTMVDELFAEIVRQMNYAAQPDKDDPCCSACNIQ Disordered - Extended Switch I 32 36 YDPTI Complex Fragment 1KAOA 2RAPA 3RAPR 3RAPS Function arises via a disorder to order transition Molecular assembly Molecular recognition effectors Protein-protein binding X-ray crystallography 7.5 magnesium chloride 100 PEG 4000 19 protein per mL 10 Tris 100 Paper 9312017 Cherfils J, Menetrey J, Le Bras G, Janoueix-Lerosey I, de Gunzburg J, Garel JR, Auzat I 1997 Embo J 16 18 5582-5591 Disordered - Extended L3 Loop 45 55 EVDSSPSVLEI Complex Fragment Native 1KAOA 2RAPA 3RAPR 3RAPS Function arises from the disordered state Entropic chain Flexible linkers/spacers X-ray crystallography 8 LiSO4 100 PEG 8000 20-25% Tris/HCl 100 X-ray crystallography 8 MgCl2 100 PEG 8000 20-25% Tris/HCl 100 Paper 10591105 Menetrey J, Cherfils J 1999 Proteins 37 3 465-473 Disordered - Extended Switch II 60 63 GTEQ Complex Fragment 1KAOA 2RAPA 3RAPR 3RAPS Function arises via a disorder to order transition Molecular assembly Protein-protein binding X-ray crystallography 7.5 magnesium chloride 100 PEG 4000 19 protein per mL 10 Tris 100 Paper 9312017 Cherfils J, Menetrey J, Le Bras G, Janoueix-Lerosey I, de Gunzburg J, Garel JR, Auzat I 1997 Embo J 16 18 5582-5591 Disordered - Extended Switch II 62 63 EQ Complex Fragment Native 1KAOA 2RAPA 3RAPR 3RAPS Function arises via a disorder to order transition Molecular assembly Protein-protein binding X-ray crystallography 8 LiSO4 100 PEG 8000 20-25% Tris/HCl 100 X-ray crystallography 8 MgCl2 100 PEG 8000 20-25% Tris/HCl 100 Paper 10591105 Menetrey J, Cherfils J 1999 Proteins 37 3 465-473 Disordered - Extended Switch II 62 66 EQFAS Complex Fragment Native 1KAOA 2RAPA 3RAPR 3RAPS Function arises via a disorder to order transition Molecular assembly Protein-protein binding X-ray crystallography 8 LiSO4 100 PEG 8000 20-25% Tris/HCl 100 X-ray crystallography 8 MgCl2 100 PEG 8000 20-25% Tris/HCl 100 Paper 10591105 Menetrey J, Cherfils J 1999 Proteins 37 3 465-473 Pyridoxine-5'-phosphate oxidase EC 1.4.3.5 Pyridoxamine-phosphate oxidase Q9NVS9 Q9NVS9 37082126 Homo sapiens (Human) 261 MTCWLRGVTATFGRPAEWPGYLSHLCGRSAAMDLGPMRKSYRGDREAFEETHLTSLDPVKQFAAWFEEAVQCPDIGEANAMCLATCTRDGKPSARMLLLKGFGKDGFRFFTNFESRKGKELDSNPFASLVFYWEPLNRQVRVEGPVKKLPEEEAECYFHSRPKSSQIGAVVSHQSSVIPDREYLRKKNEELEQLYQDQEVPKPKSWGGYVLYPQVMEFWQGQTNRLHDRIVFRRGLPTGDSPLGPMTHRGEEDWLYERLAP Disordered 1 48 MTCWLRGVTATFGRPAEWPGYLSHLCGRSAAMDLGPMRKSYRGDREAF Engineered Relationship to function unknown Modification site Protein-protein binding X-ray crystallography 100 Beta-mercaptoethanol 2.5 NaCl 250 polyethyleneimine 1.5% potassium phosphate pH 7.5 50 protein 7 Sodium citrate 20 Paper 12824491 Musayev FN, Di Salvo ML, Ko TP, Schirch V, Safo MK 2003 Protein Sci 12 7 1455-63 Tubulin beta-2 chain beta-2 tubulin beta-tubulin class-II tubulin beta-2 tubulin beta chain P32882 P32882 212844 UBCHB Gallus gallus (Chicken, Embryonic) 445 MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEGEEDEA Disordered - Extended 394 407 FLHWYTGEGMDEME Engineered Fragment Function arises via a disorder to order transition Molecular assembly Protein-protein binding Substrate/ligand binding Nuclear magnetic resonance (NMR) 298 7 TFE Paper 10211825 Jimenez MA, Evangelio JA, Aranda C, Lopez-Brauet A, Andreu D, Rico M, Lagos R, Andreu JM, Monasterio O 1999 Protein Sci 8 4 788-799 Disordered - Extended 394 404 FLHWYTGEGMD Engineered Fragment Function arises via a disorder to order transition Molecular assembly Protein-protein binding Substrate/ligand binding Near-UV circular dichroism (CD) spectroscopy 298 Paper 10211825 Jimenez MA, Evangelio JA, Aranda C, Lopez-Brauet A, Andreu D, Rico M, Lagos R, Andreu JM, Monasterio O 1999 Protein Sci 8 4 788-799 Disordered - Extended 412 414 ESN Engineered Fragment Function arises via a disorder to order transition Molecular assembly Protein-protein binding Substrate/ligand binding Near-UV circular dichroism (CD) spectroscopy 298 TFE Paper 10211825 Jimenez MA, Evangelio JA, Aranda C, Lopez-Brauet A, Andreu D, Rico M, Lagos R, Andreu JM, Monasterio O 1999 Protein Sci 8 4 788-799 Disorder may be caused by the truncation of this fragment Disordered - Extended 431 431 D Engineered Fragment Function arises via a disorder to order transition Molecular assembly Protein-protein binding Substrate/ligand binding Near-UV circular dichroism (CD) spectroscopy 298 TFE Paper 10211825 Jimenez MA, Evangelio JA, Aranda C, Lopez-Brauet A, Andreu D, Rico M, Lagos R, Andreu JM, Monasterio O 1999 Protein Sci 8 4 788-799 Disorder may be caused by the truncation of this fragment Disordered - Extended 432 445 EQGEFEEEGEEDEA Engineered Fragment Function arises via a disorder to order transition Molecular assembly Protein-protein binding Substrate/ligand binding Nuclear magnetic resonance (NMR) 298 7 TFE Near-UV circular dichroism (CD) spectroscopy 298 Paper 10211825 Jimenez MA, Evangelio JA, Aranda C, Lopez-Brauet A, Andreu D, Rico M, Lagos R, Andreu JM, Monasterio O 1999 Protein Sci 8 4 788-799 Dehydrin-like protein Q39805 Q39805 11056061 PC4381 Glycine max (Soybean) 226 MASYQKHYDDQGRKVDEYGNVEKQTDEYGNPVHAASVTYVATRTAAGGYSDDINKQHDTTNAYGVDTGRQHSSGGYDGDTNKHHGTTGGYNDDTNRHHGTTGVYGIDTDRQQHGTTGGYAGDTGRQHGNIGGPYYGTNTADTGTGPRSGTTGGTGYGGTGGTDYGTTGGTGYGSGTGYGVNTGGAHTEAGYRKEHRQHDQSHGDQNEKKGIMDKIKEKLPGGHSDK Disordered - Extended 1 226 MASYQKHYDDQGRKVDEYGNVEKQTDEYGNPVHAASVTYVATRTAAGGYSDDINKQHDTTNAYGVDTGRQHSSGGYDGDTNKHHGTTGGYNDDTNRHHGTTGVYGIDTDRQQHGTTGGYAGDTGRQHGNIGGPYYGTNTADTGTGPRSGTTGGTGYGGTGGTDYGTTGGTGYGSGTGYGVNTGGAHTEAGYRKEHRQHDQSHGDQNEKKGIMDKIKEKLPGGHSDK Native Function arises from the disordered state Unknown Unknown Thermal stability from 0°C to 100°C Far-UV circular dichroism (CD) 7 buffer sodium phosphate increasing temperatures from 12 to 80°C Paper 12644649 Soulages JL, Kim K, Arrese EL, Walters C, Cushman JC 2003 Plant Physiol 131 3 963-75 RAF proto-oncogene serine/threonine-protein kinase cRaf C-RAF kinase-related transforming protein raf-1 protein kinase raf-1 proto-oncogene protein-serine/threonine kinase Raf-1 P04049 Hs.257266 P04049 4506401 TVHUF6 Homo sapiens (Human) 648 MEHIQGAWKTISNGFGFKDAVFDGSSCISPTIVQQFGYQRRASDDGKLTDPSKTSNTIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKKARLDWNTDAASLIGEELQVDFLDHVPLTTHNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMCVDWSNIRQLLLFPNSTIGDSGVPALPSLTMRRMRESVSRMPVSSQHRYSTPHAFTFNTSSPSSEGSLSQRQRSTSTPNVHMVSTTLPVDSRMIEDAIRSHSESASPSALSSSPNNLSPTGWSQPKTPVPAQRERAPVSGTQEKNKIRPRGQRDSSYYWEIEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTGSVLWMAPEVIRMQDNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMVGRGYASPDLSKLYKNCPKAMKRLVADCVKKVKEERPLFPQILSSIELLQHSLPKINRSASEPSLHRAAHTEDINACTLTTSPRLPVF Disordered 51 54 PSKT Engineered Fragment Relationship to function unknown Unknown Unknown X-ray crystallography 298 7.6 ammonium sulphate 50 CaCl2 5 Dithioerythritol (DTE) 0.5 MgCl2 2.5 monomethylether PEG 5000 (Fluka) 10 Tris-HCl 32.2 Paper 7791872 Nassar N, Horn G, Herrmann C, Scherer A, McCormick F, Wittinghofer A 1995 Nature 375 6532 554-560 Disordered region may be present due to the fragmentation of the sequence. Disordered 55 55 S Engineered Fragment Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 298 5.3 15N labeled protein 1.4 dithiothreitol 0.1 sodium acetate-d3 10 sodium azide in 100%D2O or 94% H2O/6% D2O 0.05 Nuclear magnetic resonance (NMR) 298 5.3 13C/15N labeled protein 1.4 dithiolthreitol 0.1 sodium acetate-d3 10 sodium azide in 100%D2O or 94% H2O/6% D2O 0.05 Paper 7766599 Emerson SD, Madison VS, Palermo RE, Waugh DS, Scheffler JE, Tsao KL, Kiefer SE, Liu SP, Fry DC 1995 Biochemistry 34 21 6911-8 Disordered region may be present due to the fragmentation of the sequence. Disordered 64 64 N Engineered Fragment Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 298 5.3 15N labeled protein 1.4 dithiothreitol 1 sodium acetate-d3 10 sodium azide in 100%D2O or 94% H2O/6% D2O 0.05 Nuclear magnetic resonance (NMR) 298 5.3 13C/15N labeled protein 1.4 dithiolthreitol 0.1 sodium acetate-d3 10 sodium azide in 100%D2O or 94% H2O/6% D2O 0.05 Paper 7766599 Emerson SD, Madison VS, Palermo RE, Waugh DS, Scheffler JE, Tsao KL, Kiefer SE, Liu SP, Fry DC 1995 Biochemistry 34 21 6911-8 Disordered region may be present due to the fragmentation of the sequence. Disordered 73 76 RNGM Engineered Fragment Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 298 5.3 15N labeled protein 1.4 dithiothreitol 0.1 sodium acetate-d3 10 sodium azide in 100%D2O or 94% H2O/6% D2O 0.05 Nuclear magnetic resonance (NMR) 298 5.3 13C/15N labeled protein 1.4 dithiolthreitol 0.1 sodium acetate-d3 10 sodium azide in 100%D2O or 94% H2O/6% D2O 0.05 Paper 7766599 Emerson SD, Madison VS, Palermo RE, Waugh DS, Scheffler JE, Tsao KL, Kiefer SE, Liu SP, Fry DC 1995 Biochemistry 34 21 6911-8 Disordered region may be present due to the fragmentation of the sequence. Disordered 102 108 LHEHKGK Engineered Fragment Relationship to function unknown Unknown Unknown X-ray crystallography 298 7.6 ammonium sulphate 50 CaCl2 5 Dithioerythritol (DTE) 0.5 MgCl2 2.5 monomethylether PEG 5000 (Fluka) 10 Tris-HCl 32.2 Paper 7791872 Nassar N, Horn G, Herrmann C, Scherer A, McCormick F, Wittinghofer A 1995 Nature 375 6532 554-560 Disordered region may be present due to the fragmentation of the sequence. Disordered - Extended 104 107 EHKG Engineered Fragment 1GUAB Relationship to function unknown Unknown Unknown X-ray crystallography 292 calcium acetate 20-50 mM dithiothreitol 2 MgCl2 5 PEG 4000 11 Tris-HCl pH 7.6 80 PDB 8756332 Nassar N, Horn G, Herrmann C, Block C, Janknecht R, Wittinghofer A 1996 Nat Struct Biol 3 8 723-729 Disordered 113 117 DWNTD Engineered Fragment Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 298 5.3 15N labeled protein 1.4 dithiothreitol 0.1 sodium acetate-d3 10 sodium azide in 100%D2O or 94% H2O/6% D2O 0.05 Nuclear magnetic resonance (NMR) 298 5.3 13C/15N labeled protein 1.4 dithiolthreitol 0.1 sodium acetate-d3 10 sodium azide in 100%D2O or 94% H2O/6% D2O 0.05 Paper 7766599 Emerson SD, Madison VS, Palermo RE, Waugh DS, Scheffler JE, Tsao KL, Kiefer SE, Liu SP, Fry DC 1995 Biochemistry 34 21 6911-8 Disordered region may be present due to the fragmentation of the sequence. Disordered 132 132 D Engineered Fragment Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 298 5.3 15N labeled protein 1.4 dithiothreitol 0.1 sodium acetate-d3 10 sodium azide in 100%D2O or 94% H2O/6% D2O 0.05 Nuclear magnetic resonance (NMR) 298 5.3 13C/15N labeled protein 1.4 dithiolthreitol 0.1 sodium acetate-d3 10 sodium azide in 100%D2O or 94% H2O/6% D2O 0.05 Paper 7766599 Emerson SD, Madison VS, Palermo RE, Waugh DS, Scheffler JE, Tsao KL, Kiefer SE, Liu SP, Fry DC 1995 Biochemistry 34 21 6911-8 Disordered region may be present due to the fragmentation of the sequence. Disordered 136 138 LTT Engineered Fragment 1FAQA 1FARA Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 298 6.2 d10-DTT 1 d11-Tris d3-acetate 30 D2O 10 Na2SO4 75 NaN3 0.01 ZnCl2 10 Paper 8710867 Mott HR, Carpenter JW, Zhong S, Ghosh S, Bell RM, Campbell SL 1996 Proc Natl Acad Sci U S A 93 16 8312-8317 Disordered region may be present due to the fragmentation of the sequence. Disordered 146 150 FLKLA Engineered Fragment Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 298 6.2 d10-DTT 1 d11-Tris d3-acetate 30 D2O 10 Na2SO4 75 NaN3 0.01 ZnCl2 10 Paper 8710867 Mott HR, Carpenter JW, Zhong S, Ghosh S, Bell RM, Campbell SL 1996 Proc Natl Acad Sci U S A 93 16 8312-8317 Disordered region may be present due to the fragmentation of the sequence. Disordered 185 187 VDW Engineered Fragment 1FAQA 1FARA Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 298 6.2 d10-DTT 1 d11-Tris d3-acetate 30 D2O 10 Na2SO4 75 NaN3 0.01 ZnCl2 10 Paper 8710867 Mott HR, Carpenter JW, Zhong S, Ghosh S, Bell RM, Campbell SL 1996 Proc Natl Acad Sci U S A 93 16 8312-8317 Disordered region may be present due to the fragmentation of the sequence. POU domain class 2, associating factor 1 B-cell-specific coactivator OBF-1 B-cell specific coactivator protein BOB-1 OBF-1 OCA-B octamer binding factor 1 OCT binding factor 1 Q16633 Hs.2407 Q16633 732793 A55652 Homo sapiens (Human) 256 MLWQKPTAPEQAPAPARPYQGVRVKEPVKELLRRKRGHASSGAAPAPTAVVLPHQPLATYTTVGPSCLDMEGSVSAVTEEAALCAGWLSQPTPATLQPLAPWTPYTEYVPHEAVSCPYSADMYVQPVCPSYTVVGPSSVLTYASPPLITNVTTRSSATPAVGPPLEGPEHQAPLTYFPWPQPLSTLPTSTLQYQPPAPALPGPQFVQLPISIPEPVLQDMEDPRRAASSLTIDKLLLEEEDSDAYALNHTLSVEGF Disordered - Extended 1 15 MLWQKPTAPEQAPAP Complex Engineered Fragment 1CQTI Function arises from the disordered state Molecular assembly Protein-DNA binding Protein-protein binding X-ray crystallography Paper 10541551 Chasman D, Cepek K, Sharp PA, Pabo CO 1999 Genes Dev 13 20 2650-2657 Disordered - Extended 1 16 MLWQKPTAPEQAPAPA Complex Engineered Fragment 1CQTJ Function arises from the disordered state Molecular assembly Protein-DNA binding Protein-protein binding X-ray crystallography PDB 10541551 Chasman D, Cepek K, Sharp PA, Pabo CO 1999 Genes Dev 13 20 2650-2657 Disordered - Extended 38 44 HASSGAA Complex Engineered Fragment 1CQTI Function arises from the disordered state Molecular assembly Protein-DNA binding Protein-protein binding X-ray crystallography Paper 10541551 Chasman D, Cepek K, Sharp PA, Pabo CO 1999 Genes Dev 13 20 2650-2657 Disordered - Extended 39 44 ASSGAA Complex Engineered Fragment 1CQTJ Function arises from the disordered state Molecular assembly Protein-DNA binding Protein-protein binding X-ray crystallography Paper 10541551 Chasman D, Cepek K, Sharp PA, Pabo CO 1999 Genes Dev 13 20 2650-2657 DNA fragmentation factor alpha subunit 45kDa, alpha polypeptide isoform 1 45 kD, alpha polypeptide 45 kD, alpha subunit DNA fragmentation factor DFF45 DFF-45 DNA fragmentation factor DNA fragmentation factor 45 kDa subunit ICAD Inhibitor of CAD O00273 O00273 4758148 Homo sapiens (Human) 331 MEVTGDAGVPESGEIRTLKPCLLRRNYSREQHGVAASCLEDLRSKACDILAIDKSLTPVTLVLAEDGTIVDDDDYFLCLPSNTKFVALASNEKWAYNNSDGGTAWISQESFDVDETDSGAGLKWKNVARQLKEDLSSIILLSEEDLQMLVDAPCSDLAQELRQSCATVQRLQHTLQQVLDQREEVRQSKQLLQLYLQALEKEGSLLSKQEESKAAFGEEVDAVDTGISRETSSDVALASHILTALREKQAPELSLSSQDLELVTKEDPKALAVALNWDIKKTETVQEACERELALRLQQTQSLHSLRSISASKASPPGDLQNPKRARQDPT Disordered 1 116 MEVTGDAGVPESGEIRTLKPCLLRRNYSREQHGVAASCLEDLRSKACDILAIDKSLTPVTLVLAEDGTIVDDDDYFLCLPSNTKFVALASNEKWAYNNSDGGTAWISQESFDVDET Fragment Function arises via a disorder to order transition Molecular assembly Protein-protein binding Near-UV circular dichroism (CD) spectroscopy 6 phosphate buffer 20 sodium chloride 50 Nuclear magnetic resonance (NMR) 296 6 DTT 5 phosphate buffer 20 sodium chloride in D2O ( 1 vol/vol) 50 sodium chloride in water (9 vol/vol) 50 Paper 11371636 Zhou P, Lugovskoy AA, McCarty JS, Li P, Wagner G 2001 Proc Natl Acad Sci U S A 98 11 6051-6055 This fragment is disordered in solution and becomes ordered when it interacts with DFF40. Stathmin Leukemia-associated phosphoprotein p18 Metablastin Oncoprotein 18 Op18 Phosphoprotein p19 pp17 pp19 Pr22 protein proliferation-related phosphoprotein p18 Prosolin stathmin 1 P16949 Hs.209983 P16949 5031851 A40936 Homo sapiens (Human) 149 MASSDIQVKELEKRASGQAFELILSPRSKESVPEFPLSPPKKKDLSLEEIQKKLEAAEERRKSHEAEVLKQLAEKREHEKEVLQKAIEENNNFSKMAEEKLTHKMEANKENREAQMAAKLERLREKDKHIEEVRKNKESKDPADETEAD Disordered 1 149 MASSDIQVKELEKRASGQAFELILSPRSKESVPEFPLSPPKKKDLSLEEIQKKLEAAEERRKSHEAEVLKQLAEKREHEKEVLQKAIEENNNFSKMAEEKLTHKMEANKENREAQMAAKLERLREKDKHIEEVRKNKESKDPADETEAD Native Function arises via a disorder to order transition Molecular assembly Protein-protein binding Nuclear magnetic resonance (NMR) 296 6.8 Far-UV circular dichroism (CD) 6.8 EGTA 1 GTP 1 MgCl2 1 PIPES-KOH 8 Nuclear magnetic resonance (NMR) 296 7.5 Far-UV circular dichroism (CD) 7.5 EGTA 1 GTP 1 MgCl2 1 PIPES-KOH 8 Paper 12860982 Honnappa S, Cutting B, Jahnke W, Seelig J, Steinmetz MO 2003 J Biol Chem 278 40 38926-38934 pH had little to no effect upon the disordered regions of this protein. Temperature however, did play a factor in measurement of the disordered regions. At lower temperatures, such as 5◦C, this protein was found to be nearly completely helical. Transcription factor 7-like 2 T7L2 T-cell factor 4 Tcf-4 Q9NQB0 Hs.501080 Q9NQB0 29337146 Q9NQB0 Homo sapiens (Human) 619 MPQLNGGGGDDLGANDELISFKDEGEQEEKSSENSSAERDLADVKSSLVNESETNQNSSSDSEAERRPPPRSESFRDKSRESLEEAAKRQDGGLFKGPPYPGYPFIMIPDLTSPYLPNGSLSPTARTLHFQSGSTHYSAYKTIEHQIAVQYLQMKWPLLDVQAGSLQSRQALKDARSPSPAHIVSNKVPVVQHPHHVHPLTPLITYSNEHFTPGNPPPHLPADVDPKTGIPRPPHPPDISPYYPLSPGTVGQIPHPLGWLVPQQGQPVYPITTGGFRHPYPTALTVNASMSRFPPHMVPPHHTLHTTGIPHPAIVTPTVKQESSQSDVGSLHSSKHQDSKKEEEKKKPHIKKPLNAFMLYMKEMRAKVVAECTLKESAAINQILGRRWHALSREEQAKYYELARKERQLHMQLYPGWSARDNYGKKKKRKRDKQPGETNEHSECFLNPCLSLPPITDLSAPKKCRARFGLDQQNNWCGPCRRKKKCVRYIQGEGSCLSPPSSDGSLLDSPPPSPNLLGSPPRDAKSQTEQTQPLSLSLKPDPLAHLSMMPPPPALLLAEATHKASALCPNGALDLPPAALQPAAPSSSIAQPSTSSLHSHSSLAGTQPQPLSLVTKSLE Disordered catenin-binding domain 1 56 MPQLNGGGGDDLGANDELISFKDEGEQEEKSSENSSAERDLADVKSSLVNESETNQ Native 1JPWD Function arises via a disorder to order transition Molecular assembly Molecular recognition effectors Protein-protein binding Transactivation (transcriptional activation) Far-UV circular dichroism (CD) Paper 11237626 Knapp S, Zamai M, Volpi D, Nardese V, Avanzi N, Breton J, Plyte S, Flocco M, Marconi M, Isacchi A, Caiolfa VR 2001 J Mol Biol 306 5 1179-1189 11713476 Poy F, Lepourcelet M, Shivdasani RA, Eck MJ 2001 Nat Struct Biol 8 12 1053-1057 In the PDB file, the disorder to order transition upon binding with beta-catenin can be seen: residues 13-25 and 40-50 form alpha helicies upon binding to the armadillo repeats of catenin. Fe(III)-pyochelin receptor [Precursor] FptA P42512 1169730 Pseudomonas aeruginosa 720 MKTETKVIKGRQGIARNRHTPLCLGLLLALSPLAAAVADARKDGETELPDMVISGESTSATQPPGVTTLGKVPLKPRELPQSASVIDHERLEQQNLFSLDEAMQQATGVTVQPFQLLTTAYYVRGFKVDSFELDGVPALLGNTASSPQDMAIYERVEILRGSNGLLHGTGNPAATVNLVRKRPQREFAASTTLSAGRWDRYRAEVDVGGPLSASGNVRGRAVAAYEDRDYFYDVADQGTRLLYGVTEFDLSPDTLLTVGAQYQHIDSITNMAGVPMAKDGSNLGLSRDTYLDVDWDRFKWDTYRAFGSLEQQLGGGWKGKVSAEYQEADSRLRYAGSFGAIDPQTGDGGQLMGAAYKFKSIQRSLDANLNGPVRLFGLTHELLGGVTYAQGETRQDTARFLNLPNTPVNVYRWDPHGVPRPQIGQYTSPGTTTTTQKGLYALGRIKLAEPLTLVVGGRESWWDQDTPATRFKPGRQFTPYGGLIWDFARDWSWYVSYAEVYQPQADRQTWNSEPLSPVEGKTYETGIKGELADGRLNLSLAAFRIDLENNPQEDPDHPGPPNNPFYISGGKVRSQGFELEGTGYLTPYWSLSAGYTYTSTEYLKDSQNDSGTRYSTFTPRHLLRLWSNYDLPWQDRRWSVGGGLQAQSDYSVDYRGVSMRQGGYALVNMRLGYKIDEHWTAAVNVNNLFDRTYYQSLSNPNWNNRYGEPRSFNVSLRGAF Disordered 38 55 ADARKDGETELPDMVISG Complex Function arises from the disordered state Molecular assembly Substrate/ligand binding X-ray crystallography ethylene glycol 25% (v/v) (NH4)2SO4 0.15 PEG 10,000 6% (w/v) Sodium acetate buffer pH 4.6 0.1 Paper 16139844 Cobessi D, Celia H, Pattus F 2005 J Mol Biol 352 4 893-904 Disordered Loop L8 551 568 PQEDPDHPGPPNNPFYIS Complex Substrate/ligand binding X-ray crystallography ethylene glycol 25% (v/v) (NH4)2SO4 0.15 PEG 10,000 6% (w/v) Sodium acetate buffer pH 4.6 0.1 Paper 16139844 Cobessi D, Celia H, Pattus F 2005 J Mol Biol 352 4 893-904 Disordered Loop L7 504 513 QADRQTWNSE Complex Substrate/ligand binding X-ray crystallography ethylene glycol 25% (v/v) (NH4)2SO4 0.15 PEG 10,000 6% (w/v) Sodium acetate buffer pH 4.6 0.1 Paper 16139844 Cobessi D, Celia H, Pattus F 2005 J Mol Biol 352 4 893-904 RNA polymerase II subunit A C-terminal domain phosphatase Q9Y5B0 Homo sapiens 961 MEVPAAGRVPAEGAPTAAVAEVRCPGPAPLRLLEWRVAAGAAVRIGSVLAVFEAAASAQSAGASQSRVASGGCVRPARPERRLRSERAGVVRELCAQPGQVVAPGAVLVRLEGCSHPVVMKGLCAECGQDLTQLQSKNGKQQVPLSTATVSMVHSVPELMVSSEQAEQLGREDQQRLHRNRKLVLMVDLDQTLIHTTEQHCQQMSNKGIFHFQLGRGEPMLHTRLRPHCKDFLEKIAKLYELHVFTFGSRLYAHTIAGFLDPEKKLFSHRILSRDECIDPFSKTGNLRNLFPCGDSMVCIIDDREDVWKFAPNLITVKKYVYFQGTGDMNAPPGSRESQTRKKVNHSRGTEVSEPSPPVRDPEGVTQAPGVEPSNGLEKPARELNGSEAATPRDSPRPGKPDERDIWPPAQAPTSSQELAGAPEPQGSCAQGGRVAPGQRPAQGATGTDLDFDLSSDSESSSESEGTKSSSSASDGESEGKRGRQKPKAAPEGAGALAQGSSLEPGRPAAPSLPGEAEPGAHAPDKEPELGGQEEGERDGLCGLGNGCADRKEAETESQNSELSGVTAGESLDQSMEEEEEEDTDEDDHLIYLEEILVRVHTDYYAKYDRYLNKEIEEAPDIRKIVPELKSKVLADVAIIFSGLHPTNFPIEKTREHYHATALGAKILTRLVLSPDAPDRATHLIAARAGTEKVLQAQECGHLHVVNPDWLWSCLERWDKVEEQLFPLRDDHTKAQRENSPAAFPDREGVPPTALFHPMPVLPKAQPGPEVRIYDSNTGKLIRTGARGPPAPSSSLPIRQEPSSFRAVPPPQPQMFGEELPDAQDGEQPGPSRRKRQPSMSETMPLYTLCKEDLESMDKEVDDILGEGSDDSDSEKRRPEEQEEEPQPRKPGTRRGADARAPASSERSAAGGRGPRGHKRKLNEEDAASESSRESSNEDEGSSSEADEMAKALEAELNDLM Disordered cterFCP 879 961 PEEQEEEPQPRKPGTRRGADARAPASSERSAAGGRGPRGHKRKLNEEDAASESSRESSNEDEGSSSEADEMAKALEAELNDLM Engineered Fragment Function arises via a disorder to order transition Molecular assembly Protein-protein binding Paper 12732728 Nguyen BD, Abbott KL, Potempa K, Kobor MS, Archambault J, Greenblatt J, Legault P, Omichinski JG 2003 Proc Natl Acad Sci U S A 100 10 5688-93 Tubulin beta-1 chain Q71U36 Homo sapiens 451 MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY Disordered RL52alpha3 404 451 FVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY Complex Engineered Fragment Function arises via a disorder to order transition Molecular assembly Protein-protein binding Far-UV circular dichroism (CD) Paper 10211825 Jimenez MA, Evangelio JA, Aranda C, Lopez-Brauet A, Andreu D, Rico M, Lagos R, Andreu JM, Monasterio O 1999 Protein Sci 8 4 788-799 Protease A inhibitor 3 Proteinase inhibitor I(A)3 Proteinase yscA-inhibitor Saccharopepsin inhibitor P01094 124811 Saccharomyces cerevisiae (Baker's yeast) 68 MNTDQQKVSEIFQSSKEKLQGDAKVVSDAFKKMASQDKDGKTTDADESEKHNYQEQYNKLKGAGHKKE Disordered - Extended 33 68 MASQDKDGKTTDADESEKHNYQEQYNKLKGAGHKKE 1DP5B Paper 10655612 Li M, Phylip LH, Lees WE, Winther JR, Dunn BM, Wlodawer A, Kay J, Gustchina A 2000 Nat Struct Biol 7 2 113-7 Salt-mediated killer protoxin 1 [Precursor] P19972 Pichia farinosa (Yeast) 222 MRKETLIGLAFITANVIAWSLRWRMQKSTTIAAIAGCSGAATFGGLAGGIVGCIAAGILAILQGFEVNWHNGGGGDRSNPVKRSSDSFSIVNHNGEKVDSYAHLVPGKVGKVIIDNIELSAIRYANNHTSLGYHFTSDGSGPAARGEATTIWGVGADEAIDKGTPSKNDLQNMSADLAKNGFKGHQGVACSTVKDGNKDVYMIKFSLAGGSNDPGGSPCSDD Disordered beta subunit of SMK toxin 146 222 GEATTIWGVGADEAIDKGTPSKNDLQNMSADLAKNGFKGHQGVACSTVKDGNKDVYMIKFSLAGGSNDPGGSPCSDD Native Function arises via a disorder to order transition Molecular assembly Protein-protein binding Far-UV circular dichroism (CD) 298 7 Paper 9089808 Suzuki C, Kashiwagi T, Tsuchiya F, Kunishima N, Morikawa K, Nikkuni S, Arata Y 1997 Protein Eng 10 2 99-101 DNA-directed RNA polymerase II largest subunit B220 EC 2.7.7.6 RNA polymerase II subunit 1 P08775 Mus musculus (Mouse) 1970 MHGGGPPSGDSACPLRTIKRVQFGVLSPDELKRMSVTEGGIKYPETTEGGRPKLGGLMDPRQGVIERTGRCQTCAGNMTECPGHFGHIELAKPVFHVGFLVKTMKVLRCVCFFCSKLLVDSNNPKIKDILAKSKGQPKKRLTHVYDLCKGKNICEGGEEMDNKFGVEQPEGDEDLTKEKGHGGCGRYQPRIRRSGLELYAEWKHVNEDSQEKKILLSPERVHEIFKRISDEECFVLGMEPRYARPEWMIVTVLPVPPLSVRPAVVMQGSARNQDDLTHKLADIVKINNQLRRNEQNGAAAHVIAEDVKLLQFHVATMVDNELPGLPRAMQKSGRPLKSLKQRLKGKEGRVRGNLMGKRVDFSARTVITPDPNLSIDQVGVPRSIAANMTFAEIVTPFNIDRLQELVRRGNSQYPGAKYIIRDNGDRIDLRFHPKPSDLHLQTGYKVERHMCDGDIVIFNRQPTLHKMSMMGHRVRILPWSTFRLNLSVTTPYNADFDGDEMNLHLPQSLETRAEIQELAMVPRMIVTPQSNRPVMGIVQDTLTAVRKFTKRDVFLERGEVMNLLMFLSTWDGKVPQPAILKPRPLWTGKQIFSLIIPGHINCIRTHSTHPDDEDSGPYKHISPGDTKVVVENGELIMGILCKKSLGTSAGSLVHISYLEMGHDITRLFYSNIQTVINNWLLIEGHTIGIGDSIADSKTYQDIQNTIKKAKQDVIEVIEKAHNNELEPTPGNTLRQTFENQVNRILNDARDKTGSSAQKSLSEYNNFKSMVVSGAKGSKINISQVIAVVGQQNVEGKRIPFGFKHRTLPHFIKDDYGPESRGFVENSYLAGLTPTEFFFHAMGGREGLIDTAVKTAETGYIQRRLIKSMESVMVKYDATVRNSINQVVQLRYGEDGLAGESVEFQNLATLKPSNKAFEKKFRFDYTNERALRRTLQEDLVKDVLSNAHIQNELEREFERMREDREVLRVIFPTGDSKVVLPCNLLRMIWNAQKIFHINPRLPSDLHPIKVVEGVKELSKKLVIVNGDDPLSRQAQENATLLFNIHLRSTLCSRRMAEEFRLSGEAFDWLLGEIESKFNQAIAHPGEMVGALAAQSLGEPATQMTLNTFHYAGVSAKNVTLGVPRLKELINISKKPKTPSLTVFLLGQSARDAERAKDILCRLEHTTLRKVTANTAIYYDPNPQSTVVAEDQEWVNVYYEMPDFDVARISPWLLRVELDRKHMTDRKLTMEQIAEKINAGFGDDLNCIFNDDNAEKLVLRIRIMNSDENKMQEEEEVVDKMDDDVFLRCIESNMLTDMTLQGIEQISKVYMHLPQTDNKKKIIITEDGEFKALQEWILETDGVSLMRVLSEKDVDPVRTTSNDIVEIFTVLGIEAVRKALERELYHVISFDGSYVNYRHLALLCDTMTCRGHLMAITRHGVNRQDTGPLMKCSFEETVDVLMEAAAHGESDPMKGVSENIMLGQLAPAGTGCFDLLLDAEKCKYGMEIPTNIPGLGAAGPTGMFFGSAPSPMGGISPAMTPWNQGATPAYGAWSPSVGSGMTPGAAGFSPSAASDASGFSPGYSPAWSPTPGSPGSPGPSSPYIPSPGGAMSPSYSPTSPAYEPRSPGGYTPQSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPNYTPTSPSYSPTSPSYSPTSPNYTPTSPNYSPTSPSYSPTSPSYSPTSPSYSPSSPRYTPQSPTYTPSSPSYSPSSPSYSPTSPKYTPTSPSYSPSSPEYTPASPKYSPTSPKYSPTSPKYSPTSPTYSPTTPKYSPTSPTYSPTSPVYTPTSPKYSPTSPTYSPTSPKYSPTSPTYSPTSPKGSTYSPTSPGYSPTSPTYSLTSPAISPDDSDEEN Disordered 1686 1741 SPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSY Fragment Native Relationship to function unknown Unknown Unknown Far-UV circular dichroism (CD) water Paper 10704311 Bienkiewicz EA, Moon Woody A, Woody RW 2000 J Mol Biol 297 1 119-33 The first 8 repeats of SPTSPSY that make up this region are essential. Disordered CTD 1592 1959 SYSPTSPAYEPRSPGGYTPQSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPNYTPTSPSYSPTSPSYSPTSPNYTPTSPNYSPTSPSYSPTSPSYSPTSPSYSPSSPRYTPQSPTYTPSSPSYSPSSPSYSPTSPKYTPTSPSYSPSSPEYTPASPKYSPTSPKYSPTSPKYSPTSPTYSPTTPKYSPTSPTYSPTSPVYTPTSPKYSPTSPTYSPTSPKYSPTSPTYSPTSPKGSTYSPTSPGYSPTSPTYSLTSP Far-UV circular dichroism (CD) water Paper 10704311 Bienkiewicz EA, Moon Woody A, Woody RW 2000 J Mol Biol 297 1 119-33 Coat protein VP1 P03087 Simian virus 40 (SV40) 364 MKMAPTKRKGSCPGAAPKKPKEPVQVPKLVIKGGIEVLGVKTGVDSFTEVECFLNPQMGNPDEHQKGLSKSLAAEKQFTDDSPDKEQLPCYSVARIPLPNINEDLTCGNILMWEAVTVKTEVIGVTAMLNLHSGTQKTHENGAGKPIQGSNFHFFAVGGEPLELQGVLANYRTKYPAQTVTPKNATVDSQQMNTDHKAVLDKDNAYPVECWVPDPSKNENTRYFGTYTGGENVPPVLHITNTATTVLLDEQGVGPLCKADSLYVSAVDICGLFTNTSGTQQWKGLPRYFKITLRKRSVKNPYPISFLLSDLINRRTQRVDGQPMIGMSSQVEEVRVYEDTEELPGDPDMIRYIDEFGQTTTRMQ Disordered 304 331 ISFLLSDLINRRTQRVDGQPMIGMSSQV Complex Native 1SVA1 1SVA2 1SVA3 1SVA4 1SVA5 1SVA6 Function arises from the disordered state Molecular assembly Protein-protein binding Structural mortar X-ray crystallography Paper 1659663 Liddington RC, Yan Y, Moulai J, Sahli R, Benjamin TL, Harrison SC 1991 Nature 354 6351 278-84 8805523 Stehle T, Gamblin SJ, Yan Y, Harrison SC 1996 Structure 4 2 165-82 Disordered 339 364 DTEELPGDPDMIRYIDEFGQTTTRMQ Complex Native 1SVA1 1SVA2 1SVA3 1SVA4 1SVA5 1SVA6 Function arises from the disordered state Molecular assembly Protein-protein binding Structural mortar X-ray crystallography Paper 1659663 Liddington RC, Yan Y, Moulai J, Sahli R, Benjamin TL, Harrison SC 1991 Nature 354 6351 278-84 8805523 Stehle T, Gamblin SJ, Yan Y, Harrison SC 1996 Structure 4 2 165-82 Ferripyoverdine receptor [Precursor] FpvA P48632 12230910 Pseudomonas aeruginosa 815 MPAPHGLSPLSKAFLMRRAFQRRILPHSLAMALSLPLAGYVQAQEVEFDIPPQALGSALQEFGRQADIQVLYRPEEVRNKRSSAIKGKLEPNQAITELLRGTGASVDFQGNAITISVAEAADSSVDLGATMITSNQLGTITEDSGSYTPGTIATATRLVLTPRETPQSITVVTRQNMDDFGLNNIDDVMRHTPGITVSAYDTDRNNYYARGFSINNFQYDGIPSTARNVGYSAGNTLSDMAIYDRVEVLKGATGLLTGAGSLGATINLIRKKPTHEFKGHVELGAGSWDNYRSELDVSGPLTESGNVRGRAVAAYQDKHSFMDHYERKTSVYYGILEFDLNPDTMLTVGADYQDNDPKGSGWSGSFPLFDSQGNRNDVSRSFNNGAKWSSWEQYTRTVFANLEHNFANGWVGKVQLDHKINGYHAPLGAIMGDWPAPDNSAKIVAQKYTGETKSNSLDIYLTGPFQFLGREHELVVGTSASFSHWEGKSYWNLRNYDNTTDDFINWDGDIGKPDWGTPSQYIDDKTRQLGSYMTARFNVTDDLNLFLGGRVVDYRVTGLNPTIRESGRFIPYVGAVYDLNDTYSVYASYTDIFMPQDSWYRDSSNKLLEPDEGQNYEIGIKGEYLDGRLNTSLAYFEIHEENRAEEDALYNSKPTNPAITYAYKGIKAKTKGYEAEISGELAPGWQVQAGYTHKIIRDDSGKKVSTWEPQDQLSLYTSYKFKGALDKLTVGGGARWQGKSWQMVYNNPRSRWEKFSQEDYWLVDLMARYQITDKLSASVNVNNVFDKTYYTNIGFYTSASYGDPRNLMFSTRWDF Disordered - Extended TonB box 129 134 ATMITS Complex Function arises from the disordered state Molecular assembly Protein-protein binding X-ray crystallography C8E5 0.75% ethylene glycol 20-25% Magnesium sulfate 50 PEG 4000 13-16% (w/v) protein 1-4 ul 5 Sodium citrate buffer pH 5.6 0.1 Paper 15733922 Cobessi D, Celia H, Folschweiller N, Schalk IJ, Abdallah MA, Pattus F 2005 J Mol Biol 347 1 121-34 1,25-dihydroxyvitamin D3 receptor VDR Vitamin D3 receptor P11473 Homo sapiens (Human) 427 MEAMAASTSLPDPGDFDRNVPRICGVCGDRATGFHFNAMTCEGCKGFFRRSMKRKALFTCPFNGDCRITKDNRRHCQACRLKRCVDIGMMKEFILTDEEVQRKREMILKRKEEEALKDSLRPKLSEEQQRIIAILLDAHHKTYDPTYSDFCQFRPPVRVNDGGGSHPSRPNSRHTPSFSGDSSSSCSDHCITSSDMMDSSSFSNLDLSEEDSDDPSVTLELSQLSMLPHLADLVSYSIQKVIGFAKMIPGFRDLTSEDQIVLLKSSAIEVIMLRSNESFTMDDMSWTCGNQDYKYRVSDVTKAGHSLELIEPLIKFQVGLKKLNLHEEEHVLLMAICIVSPDRPGVQDAALIEAIQDRLSNTLQTYIRCRHPPPGSHLLYAKMIQKLADLRSLNEEHSKQYRCLSFQPECSMKLTPLVLEVFGNEIS Disordered 424 427 NEIS Fragment Native Relationship to function unknown Unknown Unknown Paper 10678179 Rochel N, Wurtz JM, Mitschler A, Klaholz B, Moras D 2000 Mol Cell 5 1 173-9 Experimental sequence extended from 410 to 1202 of the SwissProt sequence. Late embryogenesis-abundant protein [Glycine max] embryonic abundant protein Em protein P93165 P93165 1762955 T07087 Glycine max (soybean) 105 MASRQNNKQELDERARQGETVVPGGTGGKSLEAQQHLAEGRSKGGQTRKEQLGTEGYQEMGRKGGLSTVDKSGEERAQEEGIGIDESKFRTGNNKNQNQNEDQDK Disordered - Extended 1 105 MASRQNNKQELDERARQGETVVPGGTGGKSLEAQQHLAEGRSKGGQTRKEQLGTEGYQEMGRKGGLSTVDKSGEERAQEEGIGIDESKFRTGNNKNQNQNEDQDK Native Function arises from the disordered state Unknown Unknown Far-UV circular dichroism (CD) 0.1-cm path-length 7.7 microM protein solution in 50 mM buffer Na-phosphate pH 5, 8, and 9 temperature from 10°C to 80°C Paper 11891239 Soulages JL, Kim K, Walters C, Cushman JC 2002 Plant Physiol 128 3 822-32 Late embryogenesis abundant protein 1 AavLea1 Q95V77 Q95V77 24418520 Aphelenchus avenae (Mycophagous nematode worm) 143 MSSQQNQNRQGEQQEQGYMEAAKEKVVNAWESTKETLSSTAQAAAEKTAEFRDSAGETIRDLTGQAQEKGQEFKERAGEKAEETKQRAGEKMDETKQRAGEMRENAGQKMEEYKQQGKGKAEELRDTAAEKLHQAGEKVKGRD Disordered 1 143 MSSQQNQNRQGEQQEQGYMEAAKEKVVNAWESTKETLSSTAQAAAEKTAEFRDSAGETIRDLTGQAQEKGQEFKERAGEKAEETKQRAGEKMDETKQRAGEMRENAGQKMEEYKQQGKGKAEELRDTAAEKLHQAGEKVKGRD Native Function arises from the disordered state Unknown Unknown Far-UV circular dichroism (CD) 7 0.1 and 2 mg/ml of AavLEA1 in 50 mM phosphate buffer 0.1-cm path length temperature range of 4 to 75 °C Fluorescence anisotropy 0.1 and 0.5 mg/ml AavLEA1 excitation wavelength of 280 nm scan rate of 60 nm/min slit widths of 2.5 nm Fourier transform infrared spectroscopy 298 15 mg/ml protein Paper 12569097 Goyal K, Tisi L, Basran A, Browne J, Burnell A, Zurdo J, Tunnacliffe A 2003 J Biol Chem 278 15 12977-84 Major prion protein precursor PrP PrP27-30 PrP33-35C P04273 P04273 130913 Mesocricetus auratus (golden hamster) 254 MANLSYWLLALFVAMWTDVGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGTWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMMHFGNDWEDRYYRENMNRYPNQVYYRPVDQYNNQNNFVHDCVNITIKQHTVTTTTKGENFTETDIKIMERVVEQMCTTQYQKESQAYYDGRRSSAVLFSSPPVILLISFLIFLMVG Disordered - Extended 90 124 GQGGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGG Fragment Native Function arises from the disordered state Unknown Unknown Nuclear magnetic resonance (NMR) Paper 9391046 Donne DG, Viles JH, Groth D, Mehlhorn I, James TL, Cohen FE, Prusiner SB, Wright PE, Dyson HJ 1997 Proc Natl Acad Sci U S A 94 25 13452-7 Disordered PrP(29-231) 29 124 GGWNTGGSRYPGQGSPGGNRYPPQGGGTWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGG Fragment Native Function arises from the disordered state Unknown Unknown Nuclear magnetic resonance (NMR) Paper 9391046 Donne DG, Viles JH, Groth D, Mehlhorn I, James TL, Cohen FE, Prusiner SB, Wright PE, Dyson HJ 1997 Proc Natl Acad Sci U S A 94 25 13452-7 Manganese stabilizing protein 224916 Spinacea oleracea 248 EGGKRLTYDEIQSKTYLEVKGTGTANQCPTVEGGVDSFAFKPGKYTAKKFCLEPTKFAVKAEGISKNSGPDFQNTKLMTRLTYTLDEIEGPFEVSSDGTVKFEEKDGIDYAAVTVQLPGGERVPFLFTIKQLVASGKPESFSGDFLVPSYRGSSFLDPKGRGGSTGYDNAVALPAGGRGDEEELQKENNKNVASSKGTITLSVTSSKPETGEVIGVFQSLQPSDTDLGAKVPKDVKIEGVWYAQLEQQ Disordered 1 248 EGGKRLTYDEIQSKTYLEVKGTGTANQCPTVEGGVDSFAFKPGKYTAKKFCLEPTKFAVKAEGISKNSGPDFQNTKLMTRLTYTLDEIEGPFEVSSDGTVKFEEKDGIDYAAVTVQLPGGERVPFLFTIKQLVASGKPESFSGDFLVPSYRGSSFLDPKGRGGSTGYDNAVALPAGGRGDEEELQKENNKNVASSKGTITLSVTSSKPETGEVIGVFQSLQPSDTDLGAKVPKDVKIEGVWYAQLEQQ Function arises from the disordered state Molecular assembly Protein-protein binding Far-UV circular dichroism (CD) 6 KH2PO4 10 Paper 9890923 Lydakis-Simantiris N, Hutchison RS, Betts SD, Barry BA, Yocum CF 1999 Biochemistry 38 1 404-14 10569936 Lydakis-Simantiris N, Betts SD, Yocum CF 1999 Biochemistry 38 47 15528-35 Nef protein 3'ORF F-protein Negative factor P04324 Human immunodeficiency virus type 1 206 MGGKWSKSSVVGWPAVRERMRRAEPAADGVGAASRDLEKHGAITSSNTAANNAACAWLEAQEEEKVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPGPGIRYPLTFGWCYKLVPVEPEKLEEANKGENTSLLHPVSLHGMDDPEREVLEWRFDSRLAFHHVARELHPEYFKNC Disordered 2 16 GGKWSKSSVVGWPAV Fragment Native Relationship to function unknown Unknown Unknown Paper 10339411 Geyer M, Munte CE, Schorr J, Kellner R, Kalbitzer HR 1999 J Mol Biol 289 1 123-38 The experimental protein consisted of residues 2 - 57 of SwissProt entry P04324. Ordered 17 22 RERMRR Fragment Native Paper 10339411 Geyer M, Munte CE, Schorr J, Kellner R, Kalbitzer HR 1999 J Mol Biol 289 1 123-38 The experimental protein consisted of residues 2 - 57 of SwissProt entry P04324. Disordered 23 34 AEPAADGVGAAS Fragment Native Relationship to function unknown Unknown Unknown Paper 10339411 Geyer M, Munte CE, Schorr J, Kellner R, Kalbitzer HR 1999 J Mol Biol 289 1 123-38 The experimental protein consisted of residues 2 - 57 of SwissProt entry P04324. Ordered 35 41 RDLEKHG Fragment Native Paper 10339411 Geyer M, Munte CE, Schorr J, Kellner R, Kalbitzer HR 1999 J Mol Biol 289 1 123-38 The experimental protein consisted of residues 2 - 57 of SwissProt entry P04324. Disordered 42 57 AITSSNTAANNAACAW Fragment Native Relationship to function unknown Unknown Unknown Paper 10339411 Geyer M, Munte CE, Schorr J, Kellner R, Kalbitzer HR 1999 J Mol Biol 289 1 123-38 The experimental protein consisted of residues 2 - 57 of SwissProt entry P04324. Sulfite reductase [NADPH] flavoprotein alpha-component CYSJ_ECOLI EC 1.8.1.2 SIR-FP P38038 1706269 Escherichia coli 598 TTQVPPSALLPLNPEQLARLQAATTDLTPTQLAWVSGYFWGVLNQQPAALAATPAPAAEMPGITIISASQTGNARRVAEALRDDLLAAKLNVKLVNAGDYKFKQIASEKLLIVVTSTQGEGEPPEEAVALHKFLFSKKAPKLENTAFAVFSLGDTSYEFFCQSGKDFDSKLAELGGERLLDRVDADVEYQAAASEWRARVVDALKSRAPVAAPSQSVATGAVNEIHTSPYSKDAPLVASLSVNQKITGRNSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPALVKELVELLWLKGDEPVTVEGKTLPLNEALQWHFELTVNTANIVENYATLTRSETLLPLVGDKAKLQHYAATTPIVDMVRFSPAQLDAEALINLLRPLTPRLYSIASSQAEVENEVHVTVGVVRYDVEGRARAGGASSFLADRVEEEGEVRVFIEHNDNFRLPANPETPVIMIGPGTGIAPFRAFMQQRAADEAPGKNWLFFGNPHFTEDFLYQVEWQRYVKEGVLTRIDLAWSRDQKEKVYVQDKLREQGAELWRWINDGAHIYVCGDANRMAKDVEQALLEVIAEFGGMDTEAADEFLSELRVERRYQRDVY Disordered FMN binding domain 52 224 ATPAPAAEMPGITIISASQTGNARRVAEALRDDLLAAKLNVKLVNAGDYKFKQIASEKLLIVVTSTQGEGEPPEEAVALHKFLFSKKAPKLENTAFAVFSLGDTSYEFFCQSGKDFDSKLAELGGERLLDRVDADVEYQAAASEWRARVVDALKSRAPVAAPSQSVATGAVNE Fragment 1DDGA 1DDGB 1DDIA Function arises from the disordered state Molecular recognition effectors Cofactor/heme binding X-ray crystallography 277 1-4 methyl-pentane-diol 10 ammonium sulfate 2 NADP+ (5mM) 2 SiR-FP60 (15 g/mL) protein 2 Tris-HCl pH 7.0 50 Paper 10860732 Gruez A, Pignol D, Zeghouf M, Coves J, Fontecave M, Ferrer JL, Fontecilla-Camps JC 2000 J Mol Biol 299 1 199-212 This is the FMN binding domain of this protein. It transfers electrons from the ferredoxin NADP+ reductase (FNR) module to the beta subunit, which contains Fe4S4 and siroheme. The FMN of one molecule binds to the FNR of an adjacent molecule. The flexibility of this region is believed to be important in optimal molecular arrangment during electron transfer. Ordered FAD-binding domain 225 279 IHTSPYSKDAPLVASLSVNQKITGRNSEKDVRHIEIDLGDSGLRYQPGDALGVWY Fragment 1DDGA 1DDGB 1DDIA Function arises from the ordered state Molecular recognition effectors Cofactor/heme binding X-ray crystallography 277 1-4 methyl-pentane-diol 10 ammonium sulfate 2 NADP+ (5mM) 2 SiR-FP60 (15 g/mL) protein 2 Tris-HCl pH 7.0 50 Paper 10860732 Gruez A, Pignol D, Zeghouf M, Coves J, Fontecave M, Ferrer JL, Fontecilla-Camps JC 2000 J Mol Biol 299 1 199-212 Ordered connecting domain 280 384 QNDPALVKELVELLWLKGDEPVTVEGKTLPLNEALQWHFELTVNTANIVENYATLTRSETLLPLVGDKAKLQHYAATTPIVDMVRFSPAQLDAEALINLLRPLTP Fragment 1DDGA 1DDGB 1DDIA Relationship to function unknown Molecular assembly Protein-protein binding X-ray crystallography 277 1-4 methyl-pentane-diol 10 ammonium sulfate 2 NADP+ (5mM) 2 SiR-FP60 (15 g/mL) protein 2 Tris-HCl pH 7.0 50 Paper 10860732 Gruez A, Pignol D, Zeghouf M, Coves J, Fontecave M, Ferrer JL, Fontecilla-Camps JC 2000 J Mol Biol 299 1 199-212 Ordered FAD-binding domain 385 444 RLYSIASSQAEVENEVHVTVGVVRYDVEGRARAGGASSFLADRVEEEGEVRVFIEHNDNF Fragment 1DDGA 1DDGB 1DDIA Function arises from the ordered state Molecular recognition effectors Cofactor/heme binding X-ray crystallography 277 1-4 methyl-pentane-diol 10 ammonium sulfate 2 NADP+ (5mM) 2 SiR-FP60 (15 g/mL) protein 2 Tris-HCl pH 7.0 50 Paper 10860732 Gruez A, Pignol D, Zeghouf M, Coves J, Fontecave M, Ferrer JL, Fontecilla-Camps JC 2000 J Mol Biol 299 1 199-212 Ordered NADP(H)-binding domain 445 598 RLPANPETPVIMIGPGTGIAPFRAFMQQRAADEAPGKNWLFFGNPHFTEDFLYQVEWQRYVKEGVLTRIDLAWSRDQKEKVYVQDKLREQGAELWRWINDGAHIYVCGDANRMAKDVEQALLEVIAEFGGMDTEAADEFLSELRVERRYQRDVY Fragment 1DDGA 1DDGB 1DDIA Relationship to function unknown Unknown Unknown X-ray crystallography 277 1-4 methyl-pentane-diol 10 ammonium sulfate 2 NADP+ (5mM) 2 SiR-FP60 (15 g/mL) protein 2 Tris-HCl pH 7.0 50 Paper 10860732 Gruez A, Pignol D, Zeghouf M, Coves J, Fontecave M, Ferrer JL, Fontecilla-Camps JC 2000 J Mol Biol 299 1 199-212 Disordered 55 255 APAAEMPGITIISASQTGNARRVAEALRDDLLAAKLNVKLVNAGDYKFKQIASEKLLIVVTSTQGEGEPPEEAVALHKFLFSKKAPKLENTAFAVFSLGDTSYEFFCQSGKDFDSKLAELGGERLLDRVDADVEYQAAASEWRARVVDALKSRAPVAAPSQSVATGAVNEIHTSPYSKDAPLVASLSVNQKITGRNSEKDV Fragment 1DDGA 1DDGB 1DDIA Function arises from the disordered state Molecular recognition effectors Cofactor/heme binding X-ray crystallography 277 1-4 methyl-pentane-diol 10 ammonium sulfate 2 NADP+ (5mM) 2 SiR-FP60 (15mg/ml) protein 2 Tris-HCl pH 7.0 50 Paper 10860732 Gruez A, Pignol D, Zeghouf M, Coves J, Fontecave M, Ferrer JL, Fontecilla-Camps JC 2000 J Mol Biol 299 1 199-212 Four polymorphs were created for this protein. #1 was used to determine the structure, and was thus used for this entry. Polymorphs 2-4 were analyzed and their structures were also determined. They had no regions of electron density from residues 55-255, and were assumed to be disordered in these regions. The paper by Ostrowski et al. contains the full protein sequence. Plasminogen EC.3.4.21.7 P00747 130316 Homo sapiens (Human) 810 MEHKEVVLLLLLFLKSGQGEPLDDYVNTQGASLFSVTKKQLGAGSIEECAAKCEEDEEFTCRAFQYHSKEQQCVIMAENRKSSIIIRMRDVVLFEKKVYLSECKTGNGKNYRGTMSKTKNGITCQKWSSTSPHRPRFSPATHPSEGLEENYCRNPDNDPQGPWCYTTDPEKRYDYCDILECEEECMHCSGENYDGKISKTMSGLECQAWDSQSPHAHGYIPSKFPNKNLKKNYCRNPDRELRPWCFTTDPNKRWELCDIPRCTTPPPSSGPTYQCLKGTGENYRGNVAVTVSGHTCQHWSAQTPHTHNRTPENFPCKNLDENYCRNPDGKRAPWCHTTNSQVRWEYCKIPSCDSSPVSTEQLAPTAPPELTPVVQDCYHGDGQSYRGTSSTTTTGKKCQSWSSMTPHRHQKTPENYPNAGLTMNYCRNPDADKGPWCFTTDPSVRWEYCNLKKCSGTEASVVAPPPVVLLPDVETPSEEDCMFGNGKGYRGKRATTVTGTPCQDWAAQEPHRHSIFTPETNPRAGLEKNYCRNPDGDVGGPWCYTTNPRKLYDYCDVPQCAAPSFDCGKPQVEPKKCPGRVVGGCVAHPHSWPWQVSLRTRFGMHFCGGTLISPEWVLTAAHCLEKSPRPSSYKVILGAHQEVNLEPHVQEIEVSRLFLEPTRKDIALLKLSSPAVITDKVIPACLPSPNYVVADRTECFITGWGETQGTFGAGLLKEAQLPVIENKVCNRYEFLNGRVQSTELCAGHLAGGTDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRFVTWIEGVMRNN Disordered 384 384 S Fragment 1KRNA X-ray crystallography 277 6 1.68 Angstroms 22% PEG in reservoir equilibrated against CAC Buffer 50 PEG 10% concentration stabilized at 10% BASA Paper 15299951 Stec B, Yamano A, Whitlow M, Teeter MM 1997 Acta Crystallogr D Biol Crystallogr 53 Pt 2 169-178 Disordered 389 389 S Fragment 1KRNA X-ray crystallography 277 6 1.68 Angstroms 22% PEG in reservoir equilibrated against CAC Buffer 50 PEG 10% concentration stabilized at 10% BASA Paper 15299951 Stec B, Yamano A, Whitlow M, Teeter MM 1997 Acta Crystallogr D Biol Crystallogr 53 Pt 2 169-178 Disordered 391 391 T Fragment 1KRNA X-ray crystallography 277 6 1.68 Angstroms 22% PEG in reservoir equilibrated against CAC Buffer 50 PEG 10% concentration stabilized at 10% BASA Paper 15299951 Stec B, Yamano A, Whitlow M, Teeter MM 1997 Acta Crystallogr D Biol Crystallogr 53 Pt 2 169-178 This residue is part of the first disordered residue patch on the surface of the protein. Disordered 400 400 S Fragment 1KRNA X-ray crystallography 277 6 1.68 Angstroms 22% PEG in reservoir equilibrated against CAC Buffer 50 PEG 10% concentration stabilized at 10% BASA Paper 15299951 Stec B, Yamano A, Whitlow M, Teeter MM 1997 Acta Crystallogr D Biol Crystallogr 53 Pt 2 169-178 This residue is part of the second disordered residue patch on the surface of the protein. Disordered 402 402 S Fragment 1KRNA X-ray crystallography 277 6 1.68 Angstroms 22% PEG in reservoir equilibrated against CAC Buffer 50 PEG 10% concentration stabilized at 10% BASA Paper 15299951 Stec B, Yamano A, Whitlow M, Teeter MM 1997 Acta Crystallogr D Biol Crystallogr 53 Pt 2 169-178 This residue is part of the second disordered residue patch on the surface of the protein. Disordered 403 403 S Fragment 1KRNA X-ray crystallography 277 6 1.68 Angstroms 22% PEG in reservoir equilibrated against CAC Buffer 50 PEG 10% concentration stabilized at 10% BASA Paper 15299951 Stec B, Yamano A, Whitlow M, Teeter MM 1997 Acta Crystallogr D Biol Crystallogr 53 Pt 2 169-178 This residue is part of the second disordered residue patch on the surface of the protein. Disordered 423 423 M Fragment 1KRNA Function arises via a disorder to order transition X-ray crystallography 277 6 1.68 Angstroms 22% PEG in reservoir equilibrated against CAC Buffer 50 PEG 10% concentration stabilized at 10% BASA Paper 15299951 Stec B, Yamano A, Whitlow M, Teeter MM 1997 Acta Crystallogr D Biol Crystallogr 53 Pt 2 169-178 The carbonyl group of this residue is associated with serine 91 via a strong water-mediated hydrogen bond to the nitrogen atom of the amide group. This residue is part of the second disordered residue patch on the surface of the protein. Disordered 449 449 C Fragment 1KRNA X-ray crystallography 277 6 1.68 Angstroms 22% PEG in reservoir equilibrated against CAC Buffer 50 PEG 10% concentration stabilized at 10% BASA Paper 15299951 Stec B, Yamano A, Whitlow M, Teeter MM 1997 Acta Crystallogr D Biol Crystallogr 53 Pt 2 169-178 Part of a disordered disulfide bridge (with residue 426). Disordered 453 453 K Fragment 1KRNA X-ray crystallography 277 6 1.68 Angstroms 22% PEG in reservoir equilibrated against CAC Buffer 50 PEG 10% concentration stabilized at 10% BASA Paper 15299951 Stec B, Yamano A, Whitlow M, Teeter MM 1997 Acta Crystallogr D Biol Crystallogr 53 Pt 2 169-178 Disordered 443 443 S Fragment 1KRNA X-ray crystallography 277 6 1.68 Angstroms 22% PEG in reservoir equilibrated against CAC Buffer 50 PEG 10% concentration stabilized at 10% BASA Paper 15299951 Stec B, Yamano A, Whitlow M, Teeter MM 1997 Acta Crystallogr D Biol Crystallogr 53 Pt 2 169-178 Disordered 426 426 C Fragment 1KRNA Relationship to function unknown Unknown Unknown Paper 15299951 Stec B, Yamano A, Whitlow M, Teeter MM 1997 Acta Crystallogr D Biol Crystallogr 53 Pt 2 169-178 Part of a disordered disulfide bridge (with residue 449). Some of the disordered residues combine together, forming patches on the surface of the protein, which may be relevant to quaternary assemblage of proteins with kringle domains. Kappa casein [precursor] P02668 115667 KKBOB Bos taurus (Bovine) 190 MMKSFFLVVTILALTLPFLGAQEQNQEQPIRCEKDERFFSDKIAKYIPIQYVLSRYPSYGLNYYQQKPVALINNQFLPYPYYAKPAAVRSPAQILQWQVLSNTVPAKSCQAQPTTMARHPHPHLSFMAIPPKKNQDKTEIPTINTIASGEPTSTPTTEAVESTVATLEDSPEVIESPPEINTVQVTSTAV Disordered 1 182 MMKSFFLVVTILALTLPFLGAQEQNQEQPIRCEKDERFFSDKIAKYIPIQYVLSRYPSYGLNYYQQKPVALINNQFLPYPYYAKPAAVRSPAQILQWQVLSNTVPAKSCQAQPTTMARHPHPHLSFMAIPPKKNQDKTEIPTINTIASGEPTSTPTTEAVESTVATLEDSPEVIESPPEINT Native Relationship to function unknown Molecular assembly Unknown Raman optical activity Thermal stability Paper 11784308 Syme CD, Blanch EW, Holt C, Jakes R, Goedert M, Hecht L, Barron LD 2002 Eur J Biochem 269 1 148-56 Beta-lactoglobulin Allergen Bos d 5 Beta-LG P02754 Bos taurus (Cow) 178 MKCLLLALALTCGAQALIVTQTMKGLDIQKVAGTWYSLAMAASDISLLDAQSAPLRVYVEELKPTPEGDLEILLQKWENGECAQKKIIAEKTKIPAVFKIDALNENKVLVLDTDYKKYLLFCMENSAEPEQSLACQCLVRTPEVDDEALEKFDKALKALPMHIRLSFNPTQLEEQCHI Disordered - Molten Globule 1 178 MKCLLLALALTCGAQALIVTQTMKGLDIQKVAGTWYSLAMAASDISLLDAQSAPLRVYVEELKPTPEGDLEILLQKWENGECAQKKIIAEKTKIPAVFKIDALNENKVLVLDTDYKKYLLFCMENSAEPEQSLACQCLVRTPEVDDEALEKFDKALKALPMHIRLSFNPTQLEEQCHI Native Relationship to function unknown Unknown Unknown Far-UV circular dichroism (CD) 298 1.5 potasium cirate buffer 10 Gel filtration/size exclusion chromatography 277 1.5 HCl-KCl buffer 100 Analytical ultracentrifugation 1.5 HCl-KCl buffer 100 Paper 9141136 Ikeguchi M, Kato S, Shimizu A, Sugai S 1997 Proteins 27 4 567-75 Beta-lactoglobulin has a compact globular structure at neutral pH. Stringent starvation protein B SspB Q3YX20 P25663 Q3YX20 134929 E91141 Escherichia coli 165 MDLSQLTPRRPYLLRAFYEWLLDNQLTPHLVVDVTLPGVQVPMEYARDGQIVLNIAPRAVGNLELANDEVRFNARFGGIPRQVSVPLAAVLAIYARENGAGTMFEPEAAYDEDTSIMNDEEASADNETVMSVIDGDKPDHDDDTHPDDEPPQPPRGGRPALRVVK Disordered 111 165 DEDTSIMNDEEASADNETVMSVIDGDKPDHDDDTHPDDEPPQPPRGGRPALRVVK Native Function arises from the disordered state Molecular assembly Flexible linkers/spacers Protein-protein binding Substrate/ligand binding Far-UV circular dichroism (CD) 298 7.5 1 mm pathlenght 20 microM SspB in 10 mM potassium phosphate Paper 14536075 Wah DA, Levchenko I, Rieckhof GE, Bolon DN, Baker TA, Sauer RT 2003 Mol Cell 12 2 355-63 HMG-17 HG17_BOVIN High-mobility group nucleosome binding domain 2 Nonhistone chromosomal protein HMG-17 P02313 123104 NSBOH7 Bos taurus (Bovine) 89 PKRKAEGDAKGDKAKVKDEPQRRSARLSAKPAPPKPEPKPKKAPAKKGEKVPKGKKGKADAGKBGBBPAZBGBAKTBZAZKAEGAGDAK Disordered 1 89 PKRKAEGDAKGDKAKVKDEPQRRSARLSAKPAPPKPEPKPKKAPAKKGEKVPKGKKGKADAGKBGBBPAZBGBAKTBZAZKAEGAGDAK Monomeric Mutant Function arises via a disorder to order transition Molecular assembly Protein-DNA binding Infrared spectroscopy 6.8 NaCl 1 Small-angle neutron scattering 7 phosphate buffer 50 Far-UV circular dichroism (CD) 7.9 NaCl 1 Tris-HCl buffer 20 Paper 565710 Abercrombie BD, Kneale GG, Crane-Robinson C, Bradbury EM, Goodwin GH, Walker JM, Johns EW 1978 Eur J Biochem 84 1 173-177 Calpastatin Calpain inhibitor Sperm BS-17 component P20810 Homo sapiens (Human) 708 MNPTETKAIPVSQQMEGPHLPNKKKHKKQAVKTEPEKKSQSTKLSVVHEKKSQEGKPKEHTEPKSLPKQASDTGSNDAHNKKAVSRSAEQQPSEKSTEPKTKPQDMISAGGESVAGITAISGKPGDKKKEKKSLTPAVPVESKPDKPSGKSGMDAALDDLIDTLGGPEETEEENTTYTGPEVSDPMSSTYIEELGKREVTIPPKYRELLAKKEGITGPPADSSKPIGPDDAIDALSSDFTCGSPTAAGKKTEKEESTEVLKAQSAGTVRSAAPPQEKKRKVEKDTMSDQALEALSASLGTRQAEPELDLRSIKEVDEAKAKEEKLEKCGEDDETIPSEYRLKPATDKDGKPLLPEPEEKPKPRSESELIDELSEDFDRSECKEKPSKPTEKTEESKAAAPAPVSEAVSRTSMCSIQSAPPEPATLKGTVPDDAVEALADSLGKKEADPEDGKPVMDKVKEKAKEEDREKLGEKEETIPPDYRLEEVKDKDGKPLLPKESKEQLPPMSEDFLLDALSEDFSGPQNASSLKFEDAKLAAAISEVVSQTPASTTQAGAPPRDTSQSDKDLDDALDKLSDSLGQRQPDPDENKPMGDKVKEKAKAEHRDKLGERDDTIPPEYRHLLDDNGQDKPVKPPTKKSEDSKKPADDQDPIDALSGDLDSCPSTTETSQNTAKDKCKKAASSSKAPKNGGKAKDSAKTTEETSKPKDD Disordered 137 277 AVPVESKPDKPSGKSGMDAALDDLIDTLGGPEETEEENTTYTGPEVSDPMSSTYIEELGKREVTIPPKYRELLAKKEGITGPPADSSKPIGPDDAIDALSSDFTCGSPTAAGKKTEKEESTEVLKAQSAGTVRSAAPPQEK Fragment Far-UV circular dichroism (CD) 298 Na2HPO4 pH 7.5 10 NaCl 150 Sensitivity to proteolysis 298 EDTA 1 mercaptoethanol 5 NaCl 150 Tris pH 7.5 20 Nuclear magnetic resonance (NMR) EDTA 1 mercaptoethanol 5 NaCl 150 protein 50 Tris pH 7.5 20 Paper 15751971 Csizmok V, Bokor M, Banki P, Klement E, Medzihradszky KF, Friedrich P, Tompa K, Tompa P 2005 Biochemistry 44 10 3955-64 Translation initiation factor IF-3 IF3_ECOLI P02999 P02999 A90932 Escherichia coli 180 MKGGKRVQTARPNRINGEIRAQEVRLTGLEGEQLGIVSLREALEKAEEAGVDLVEISPNAEPPVCRIMDYGKFLYEKSKSSKEQKKKQKVIQVKEIKFRPGTDEGDYQVKLRSLIRFLEEGDKAKITLRFRGREMAHQQIGMEVLNRVKDDLQELAVVESFPTKIEGRQMIMVLAPKKKQ Disordered inter-domain linker 78 89 SKSSKEQKKKQK Native Relationship to function unknown Entropic chain Flexible linkers/spacers Nuclear magnetic resonance (NMR) 6.5 20mM potassium phosphate Paper 9054966 Moreau M, de Cock E, Fortier PL, Garcia C, Albaret C, Blanquet S, Lallemand JY, Dardel F 1997 J Mol Biol 266 1 15-22 Transcriptional activator protein traR TraR P33905 Agrobacterium tumefaciens 234 MQHWLDKLTDLAAIEGDECILKTGLADIADHFGFTGYAYLHIQHRHITAVTNYHRQWQSTYFDKKFEALDPVVKRARSRKHIFTWSGEHERPTLSKDERAFYDHASDFGIRSGITIPIKTANGFMSMFTMASDKPVIDLDREIDAVAAAATIGQIHARISFLRTTPTAEDAAWLDPKEATYLRWIAVGKTMEEIADVEGVKYNSVRVKLREAMKRFDVRSKAHLTALAIRRKLI Disordered 1 234 MQHWLDKLTDLAAIEGDECILKTGLADIADHFGFTGYAYLHIQHRHITAVTNYHRQWQSTYFDKKFEALDPVVKRARSRKHIFTWSGEHERPTLSKDERAFYDHASDFGIRSGITIPIKTANGFMSMFTMASDKPVIDLDREIDAVAAAATIGQIHARISFLRTTPTAEDAAWLDPKEATYLRWIAVGKTMEEIADVEGVKYNSVRVKLREAMKRFDVRSKAHLTALAIRRKLI Native Function arises via a disorder to order transition Molecular recognition effectors Substrate/ligand binding Transactivation (transcriptional activation) Sensitivity to proteolysis Paper 11171981 Zhu J, Winans SC 2001 Proc Natl Acad Sci U S A 98 4 1507-12 Beta casein [Precursor] P05814 P05814 115661 KBHU Homo sapiens 226 MKVLILACLVALALARETIESLSSSEESITEYKQKVEKVKHEDQQQGEDEHQDKIYPSFQPQPLIYPFVEPIPYGFLPQNILPLAQPAVVLPVPQPEIMEVPKAKDTVYTKGRVMPVLKSPTIPFFDPQIPKLTDLENLHLPLPLLQPLMQQVPQPIPQTLALPPQPLWSVPQPKVLPIPQQVVPYPQRAVPVQALLLNQELLLNPTHQIYPVTQPLAPVHNPISV Disordered - Extended 1 226 MKVLILACLVALALARETIESLSSSEESITEYKQKVEKVKHEDQQQGEDEHQDKIYPSFQPQPLIYPFVEPIPYGFLPQNILPLAQPAVVLPVPQPEIMEVPKAKDTVYTKGRVMPVLKSPTIPFFDPQIPKLTDLENLHLPLPLLQPLMQQVPQPIPQTLALPPQPLWSVPQPKVLPIPQQVVPYPQRAVPVQALLLNQELLLNPTHQIYPVTQPLAPVHNPISV Native Function arises from the disordered state Molecular recognition scavengers Metal binding Phosphorylation X-ray crystallography Near-UV circular dichroism (CD) spectroscopy 298 7 protein solution 0.04 Near-UV circular dichroism (CD) spectroscopy 283 7 protein solution 0.04 Near-UV circular dichroism (CD) spectroscopy 277 7 protein solution 0.04 Paper 3074304 Holt C, Sawyer L 1988 Protein Eng 2 4 251-9 4624541 Toyoda M, Yamauchi K 1972 Biochim Biophys Acta 263 3 555-63 T-cell surface glycoprotein CD3 zeta chain [Precursor] T-cell receptor T3 zeta chain T-cell receptor zeta chain isoform 1 precursor T-cell receptor zeta chain precursor P20963 P20963 37595565 A31768 Homo sapiens (Human) 164 MKWKALFTAAILQAQLPITEAQSFGLLDPKLCYLLDGILFIYGVILTALFLRVKFSRSADAPAYQQGQNQLYNELNLGRREEYDVLDKRRGRDPEMGGKPQRRKNPQEGLYNELQKDKMAEAYSEIGMKGERRRGKGHDGLYQGLSTATKDTYDALHMQALPPR Disordered cytoplasmic domain 50 164 FLRVKFSRSADAPAYQQGQNQLYNELNLGRREEYDVLDKRRGRDPEMGGKPQRRKNPQEGLYNELQKDKMAEAYSEIGMKGERRRGKGHDGLYQGLSTATKDTYDALHMQALPPR Native Function arises from the disordered state Molecular assembly Polymerization Protein-protein binding Substrate/ligand binding Far-UV circular dichroism (CD) 298 7 0.01 and 1.0 mM protein in PBS 1.0 and 0.01 mm path-length Nuclear magnetic resonance (NMR) 293 6.2 0.9 mM protein in 20 mM sodium phosphate buffer 600 MHz Paper 14967045 Sigalov A, Aivazian D, Stern L. 2004 Biochemistry 43 7 2049-61 F6 subunit of ATP synthase, mitochondrial precursor ATP synthase coupling factor 6, mitochondrial EC 3.6.3.14 F6 P02721 JLBO6 Bos taurus 108 MILQRLFRLSSAVQSAISVSWRRNIGITAVAFNKELDPVQKLFVDKIREYRTKRQTSGGPVDAGPEYQQDLDRELFKLKQMYGKADMNTFPNFTFEDPKFEVVEKPQS Disordered - Extended ATP synthase coupling factor 6 33 108 NKELDPVQKLFVDKIREYRTKRQTSGGPVDAGPEYQQDLDRELFKLKQMYGKADMNTFPNFTFEDPKFEVVEKPQS Native 1VZSA Relationship to function unknown Molecular assembly Protein-protein binding Nuclear magnetic resonance (NMR) 300 6.5 sodium chloride 50 sodium phosphate 20 Paper 15327958 Carbajo RJ, Silvester JA, Runswick MJ, Walker JE, Neuhaus D 2004 J Mol Biol 342 2 593-603 The SwissProt sequence includes a signal sequence that spans from residue 1 to 32 and was not included in the experimental sequence. Disordered 56 66 TSGGPVDAGPE Native Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 300 6.5 sodium chloride 50 sodium phosphate 20 Paper 15327958 Carbajo RJ, Silvester JA, Runswick MJ, Walker JE, Neuhaus D 2004 J Mol Biol 342 2 593-603 The SwissProt sequence includes a signal sequence that spans from residue 1 to 32 and was not included in the experimental sequence. Disordered 84 108 KADMNTFPNFTFEDPKFEVVEKPQS Native Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 300 6.5 sodium chloride 50 sodium phosphate 20 Paper 15327958 Carbajo RJ, Silvester JA, Runswick MJ, Walker JE, Neuhaus D 2004 J Mol Biol 342 2 593-603 The SwissProt sequence includes a signal sequence that spans from residue 1 to 32 and was not included in the experimental sequence. The ATP synthase is embedded in the inner membranes of mitochondria where it uses the proton motive force generated across the membrane by respiration to make ATP from ADP and inorganic phosphate. The enzyme has two major domains, a globular catalytic domain known as F1 that extends into the mitochondrial matrix, and a membrane domain known as Fo. The two domains are linked together by a central stalk and a peripheral stalk. The central stalk consists of subunits gamma, delta, and epsilon and its foot is intimately associated with a ring of c-subunits in the Fo domain. The peripheral stalk in bovine mitochondria consists of one copy of each of subunits OSCP, F6, b and d. F6 subunit was described first almost 40 years ago and shown to be required for restoration of ATP-Pi exchange and oligomycin-sensitive ATPase activity to F6-depleted ATP synthase. Subunit F6 or coupling factor 6 is a 9 kDa (76 residues) acidic protein that is soluble and heat stable over a broad pH range. It is derived from the precursor protein (108 residues), deposited in Swiss-Prot as P02721 (ATPR_BOVIN). UPF0234 zinc-binding protein yacG P0A8H9 67476023 Escherichia coli 65 MSETITVNCPTCGKTVVWGEISPFRPFCSKRCQLIDLGEWAAEEKRIPSSGDLSESDDWSEEPKQ Disordered 1 3 MSE Engineered Function arises from the disordered state Molecular assembly Metal binding Protein-protein binding Nuclear magnetic resonance (NMR) 298 6.5 benzamidine 1 DTT 10 inhibitor cocktail Na2HPO4 25 NaN3 in 10% v/v D2O/H2O 0.01 sodium chloride 450 Zn 2+ 20 Paper 12211008 Ramelot TA, Cort JR, Yee AA, Semesi A, Edwards AM, Arrowsmith CH, Kennedy MA 2002 Proteins 49 2 289-293 Disordered 40 65 WAAEEKRIPSSGDLSESDDWSEEPKQ Engineered Function arises from the disordered state Molecular assembly Metal binding Protein-protein binding Nuclear magnetic resonance (NMR) 298 6.5 benzamidine 1 DTT 10 inhibitor cocktail Na2HPO4 25 NaN3 in 10% v/v D2O/H2O 0.01 sodium chloride 450 Zn 2+ 20 Paper 12211008 Ramelot TA, Cort JR, Yee AA, Semesi A, Edwards AM, Arrowsmith CH, Kennedy MA 2002 Proteins 49 2 289-293 Thermonuclease precursor EC 3.1.31.1 Micrococcal nuclease Staphylococcal nuclease TNase P00644 P00644 11514489 NCSAF Staphylococcus aureus Foggi strain 149 ATSTKKLHKEPATLIKAIDGDTVKLMYKGQPMTFRLLLVDTPETKHPKKGVEKYGPEASAFTKKMVENAKKIEVEFDKGQRTDKYGRGLAYIYADGKMVNEALVRQGLAKVAYVYKPNNTHEQHLRKSEAQAKKEKLNIWSEDNADSGQ Disordered 1 6 ATSTKK Engineered 1EY0A Function arises from the disordered state X-ray crystallography 277 8.15 calcium chloride 10 pdTp 1.1 potassium citrate 20 potassium phosphate 10.5 protein per mL 20 Paper 2780539 Loll PJ, Lattman EE 1989 Proteins 5 3 183-201 Disordered 1 5 ATSTK Native 1EY0A Function arises from the disordered state X-ray crystallography 278 MPD precipitant (w/w) 22 potassium phosphate pH 8.15, 25 C 10.5 Paper 1896431 Hynes TR, Fox RO 1991 Proteins 10 2 92-105 Disordered 44 50 TKHPKKG Engineered 1EY0A Function arises from the disordered state X-ray crystallography 277 8.15 calcium chloride 10 pdTp 1.1 potassium citrate 20 potassium phosphate 10.5 protein per mL 20 Paper 2780539 Loll PJ, Lattman EE 1989 Proteins 5 3 183-201 Disordered 45 52 KHPKKGVE Native 1EY0A Function arises from the disordered state X-ray crystallography 278 MPD precipitant (w/w) 22 potassium phosphate pH 8.15, 25 C 10.5 Paper 1896431 Hynes TR, Fox RO 1991 Proteins 10 2 92-105 Disordered 141 149 SEDNADSGQ Native 1EY0A Function arises from the disordered state X-ray crystallography MPD precipitant (w/w) 22 potassium phosphate pH 8.15, 25 C 10.5 Paper 1896431 Hynes TR, Fox RO 1991 Proteins 10 2 92-105 Note: Accession numbers for PIR, Swiss-Prot, and UniProt all reference the precursor. Phosphoprotein P protein P23055 P23055 RRNZP2 Human parainfluenza 2 virus (HPIV-2) 395 MAEEPTYTTEQVDELIHAGLGTVDFFLSRPIDAQSSLGKGSIPPGVTAVLTSAAEAKSKPVAAGPVKPRRKKVISNTTPYTIADNIPPEKLPINTPIPNPLLPLARPHGKMTDIDIVTGNITEGSYKGVELAKLGKQTLLTRFTSNEPVSSAGSAQDPNFKRGGELIEKEQEATIGENGVLHGSEIRSKSSSGVIPGVPQSRPQLASSPAHADPAPASAENVKEIIELLKGLDLRLQTVEGKVDKILATSATIINLKNEMTSLKASVATVEGMITTIKIMDPSTPTNVPVEEIRKSLHNVPVVIAGPTSGGFTAEGSDMISMDELARPTLSSTKRITRKPESKKDLTGIKLTLMQLANDCISRPDTKTEFVTKIQAATTESQLNEIKRSIIRSAI Disordered 1 219 MAEEPTYTTEQVDELIHAGLGTVDFFLSRPIDAQSSLGKGSIPPGVTAVLTSAAEAKSKPVAAGPVKPRRKKVISNTTPYTIADNIPPEKLPINTPIPNPLLPLARPHGKMTDIDIVTGNITEGSYKGVELAKLGKQTLLTRFTSNEPVSSAGSAQDPNFKRGGELIEKEQEATIGENGVLHGSEIRSKSSSGVIPGVPQSRPQLASSPAHADPAPASA Native Function arises via a disorder to order transition Protein-protein binding Protein-tRNA binding Paper 14645906 Karlin D, Ferron F, Canard B, Longhi S 2003 84 Pt 12 3239-52 Disordered 309 353 SGGFTAEGSDMISMDELARPTLSSTKRITRKPESKKDLTGIKLTL Native Function arises via a disorder to order transition Protein-protein binding Paper 14645906 Karlin D, Ferron F, Canard B, Longhi S 2003 84 Pt 12 3239-52 Small metal binding protein SmbP 30250382 Nitrosomonas europaea 117 MKTTLIKVIAASVTALFLSMQVYASGHTAHVDEAVKHAEEAVAHGKEGHTDQLLEHAKESLTHAKAASEAGGNTHVGHGIKHLEDAIKHGEEGHVGVATKHAQEAIEHLRASEHKSH Disordered - Extended Small metal binding protein 1 117 MKTTLIKVIAASVTALFLSMQVYASGHTAHVDEAVKHAEEAVAHGKEGHTDQLLEHAKESLTHAKAASEAGGNTHVGHGIKHLEDAIKHGEEGHVGVATKHAQEAIEHLRASEHKSH Monomeric Native Function arises via a disorder to order transition Metal sponge Metal binding Gel filtration/size exclusion chromatography 7.5 Far-UV circular dichroism (CD) 7.5 Paper 15366930 Barney BM, LoBrutto R, Francisco WA 2004 Biochemistry 43 35 11206-11213 SmbP is characterized by an unusually high number of histidine residues (17%). The apoprotein has negligible absorbance between 260 and 280 nm resulting from the lack of tryptophan, tyrosine, and phenylalanine residues. The protein also does not contain any methionine or cysteine residues. Besides histidine, the protein is primarily an assembly of alanine (16%), glutamate (14%), glycine (11%), and lysine (9%), accounting for 67% of the amino acid composition. The percentage of nonpolar amino acids is also very low, although a nonpolar residue is the predominant amino acid for the second position of the seven-unit repeat and likely contributes to the stabilization of a hydrophobic core. This unique protein is distinguished by 10 sequential repeats of a seven amino acid motif characterized by an absolutely conserved histidine residue in the fourth position and conserved residues at each of the other six positions. Extensive searches of the current databases did not identify any proteins with significant homology. The protein, as isolated from N. europaea, had approximately one copper atom bound per protein molecule. Fimbrial protein, precursor Pilin P17838 A31105 Pseudomonas aeruginosa 157 MKAAQKGFTLIELMIVVAIIGILAAIAIPAYQDYTARAQLSERMTLASGLKTKVSDIFSQDGSCPANTAATAGIEKDTDINGKYVAKVTTGGTAAASGGCTIVATMKASDVATPLRGKTLTLTLGNADKGSYTWACTSNADNKYLPKTCQTATTTTP Disordered - Extended 35 37 TAR Engineered Fragment 1HPWA Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 303 7.2 sodium chloride 100 sodium phosphate 20 Paper 11294863 Keizer DW, Slupsky CM, Kalisiak M, Campbell AP, Crump MP, Sastry PA, Hazes B, Irvin RT, Sykes BD 2001 J Biol Chem 276 26 24186-24193 The experimental sequence consisted of seven residues from the cloning vector followed by residues 8 through 157 of SwissProt sequence P17838. Disordered - Extended 62 64 GSC Engineered Fragment 1HBWA Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 303 7.2 sodium chloride 100 sodium phosphate 20 Paper 11294863 Keizer DW, Slupsky CM, Kalisiak M, Campbell AP, Crump MP, Sastry PA, Hazes B, Irvin RT, Sykes BD 2001 J Biol Chem 276 26 24186-24193 The experimental sequence consisted of seven residues from the cloning vector followed by residues 8 through 157 of SwissProt sequence P17838. Disordered - Extended 95 97 AAS Engineered Fragment 1HBWA Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 303 7.2 sodium chloride 100 sodium phosphate 20 Paper 11294863 Keizer DW, Slupsky CM, Kalisiak M, Campbell AP, Crump MP, Sastry PA, Hazes B, Irvin RT, Sykes BD 2001 J Biol Chem 276 26 24186-24193 The experimental sequence consisted of seven residues from the cloning vector followed by residues 8 through 157 of SwissProt sequence P17838. Disordered - Extended 108 116 ASDVATPLR Engineered Fragment 1HBWA Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 303 7.2 sodium chloride 100 sodium phosphate 20 Paper 11294863 Keizer DW, Slupsky CM, Kalisiak M, Campbell AP, Crump MP, Sastry PA, Hazes B, Irvin RT, Sykes BD 2001 J Biol Chem 276 26 24186-24193 The experimental sequence consisted of seven residues from the cloning vector followed by residues 8 through 157 of SwissProt sequence P17838. Disordered - Extended 127 132 ADKGSY Engineered Fragment 1HBWA Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 303 7.2 sodium chloride 100 sodium phosphate 20 Paper 11294863 Keizer DW, Slupsky CM, Kalisiak M, Campbell AP, Crump MP, Sastry PA, Hazes B, Irvin RT, Sykes BD 2001 J Biol Chem 276 26 24186-24193 The experimental sequence consisted of seven residues from the cloning vector followed by residues 8 through 157 of SwissProt sequence P17838. Disordered - Extended 141 157 DNKYLPKTCQTATTTTP Engineered Fragment Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 303 7.2 sodium chloride 100 sodium phosphate 20 Paper 11294863 Keizer DW, Slupsky CM, Kalisiak M, Campbell AP, Crump MP, Sastry PA, Hazes B, Irvin RT, Sykes BD 2001 J Biol Chem 276 26 24186-24193 The experimental sequence consisted of seven residues from the cloning vector followed by residues 8 through 157 of SwissProt sequence P17838. Ribonuclease E RNase E RNE_ECOLI P21513 P21513 1787325 S27311 Escherichia coli 1061 MKRMLINATQQEELRVALVDGQRLYDLDIESPGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPLKEIAREYFPANYSAHGRPNIKDVLREGQEVIVQIDKEERGNKGAALTTFISLAGSYLVLMPNNPRAGGISRRIEGDDRTELKEALASLELPEGMGLIVRTAGVGKSAEALQWDLSFRLKHWEAIKKAAESRPAPFLIHQESNVIVRAFRDYLRQDIGEILIDNPKVLELARQHIAALGRPDFSSKIKLYTGEIPLFSHYQIESQIESAFQREVRLPSGGSIVIDSTEALTAIDINSARATRGGDIEETAFNTNLEAADEIARQLRLRDLGGLIVIDFIDMTPVRHQRAVENRLREAVRQDRARIQISHISRFGLLEMSRQRLSPSLGESSHHVCPRCSGTGTVRDNESLSLSILRLIEEEALKENTQEVHAIVPVPIASYLLNEKRSAVNAIETRQDGVRCVIVPNDQMETPHYHVLRVRKGEETPTLSYMLPKLHEEAMALPSEEEFAERKRPEQPALATFAMPDVPPAPTPAEPAAPVVAPAPKAAPATPAAPAQPGLLSRFFGALKALFSGGEETKPTEQPAPKAEAKPERQQDRRKPRQNNRRDRNERRDTRSERTEGSDNREENRRNRRQAQQQTAETRESRQQAEVTEKARTADEQQAPRRERSRRRNDDKRQAQQEAKALNVEEQSVQETEQEERVRPVQPRRKQRQLNQKVRYEQSVAEEAVVAPVVEETVAAEPIVQEAPAPRTELVKVPLPVVAQTAPEQQEENNADNRDNGGMPRRSRRSPRHLRVSGQRRRRYRDERYPTQSPMPLTVACASPELASGKVWIRYPIVRPQDVQVEEQREQEEVHVQPMVTEVPVAAAIEPVVSAPVVEEVAGVVEAPVQVAEPQPEVVETTHPEVIAAAVTEQPQVITESDVAVAQEVAEQAEPVVEPQEETADIEEVVETAEVVVAEPEVVAQPAAPVVAEVAAEVETVAAVEPEVTVEHNHATAPMTRAPAPEYVPEAPRHSDWQRPTFAFEGKGAAGGHTATHHASAAPARPQPVE Disordered CTD (C-terminal domain) 499 1061 SYMLPKLHEEAMALPSEEEFAERKRPEQPALATFAMPDVPPAPTPAEPAAPVVAPAPKAAPATPAAPAQPGLLSRFFGALKALFSGGEETKPTEQPAPKAEAKPERQQDRRKPRQNNRRDRNERRDTRSERTEGSDNREENRRNRRQAQQQTAETRESRQQAEVTEKARTADEQQAPRRERSRRRNDDKRQAQQEAKALNVEEQSVQETEQEERVRPVQPRRKQRQLNQKVRYEQSVAEEAVVAPVVEETVAAEPIVQEAPAPRTELVKVPLPVVAQTAPEQQEENNADNRDNGGMPRRSRRSPRHLRVSGQRRRRYRDERYPTQSPMPLTVACASPELASGKVWIRYPIVRPQDVQVEEQREQEEVHVQPMVTEVPVAAAIEPVVSAPVVEEVAGVVEAPVQVAEPQPEVVETTHPEVIAAAVTEQPQVITESDVAVAQEVAEQAEPVVEPQEETADIEEVVETAEVVVAEPEVVAQPAAPVVAEVAAEVETVAAVEPEVTVEHNHATAPMTRAPAPEYVPEAPRHSDWQRPTFAFEGKGAAGGHTATHHASAAPARPQPVE Fragment Native Function arises from the disordered state Function arises via a disorder to order transition Unknown Autoregulatory Protein-protein binding Protein-rRNA binding Sensitivity to proteolysis Far-UV circular dichroism (CD) 275 collected between 185 nm and 260 nm 1 nm steps Far-UV circular dichroism (CD) 295 collected between 185 nm and 260 nm 1 nm steps Far-UV circular dichroism (CD) 315 collected between 185 nm and 260 nm 1 nm steps Far-UV circular dichroism (CD) 335 collected between 185 nm and 260 nm 1 nm steps Far-UV circular dichroism (CD) 355 collected between 185 nm and 260 nm 1 nm steps Small-angle X-ray scattering Paper 15236960 Callaghan AJ, Aurikko JP, Ilag LL, Gunter Grossmann J, Chandran V, Kuhnel K, Poljak L, Carpousis AJ, Robinson CV, Symmons MF, Luisi BF 2004 J Mol Biol 340 5 965-979 CTD can be cross-linked to itself, thus forming dimers. The region that can self-interact is from 500-752 residues. Within the disordered CTD, there are four regions that have predicted structural propensity. These segments are called RISPs (regions of increased structural propensity). The RISPs are; segment A- residues 565-585, segment B- residues 633-712, segment C- residues 839-850 and segment D- residues 1021-1061. Disordered R-domain 628 843 ERTEGSDNREENRRNRRQAQQQTAETRESRQQAEVTEKARTADEQQAPRRERSRRRNDDKRQAQQEAKALNVEEQSVQETEQEERVRPVQPRRKQRQLNQKVRYEQSVAEEAVVAPVVEETVAAEPIVQEAPAPRTELVKVPLPVVAQTAPEQQEENNADNRDNGGMPRRSRRSPRHLRVSGQRRRRYRDERYPTQSPMPLTVACASPELASGKVW Engineered Fragment Function arises from the disordered state Unknown Protein-protein binding Protein-rRNA binding Far-UV circular dichroism (CD) Gel filtration/size exclusion chromatography Paper 15236960 Callaghan AJ, Aurikko JP, Ilag LL, Gunter Grossmann J, Chandran V, Kuhnel K, Poljak L, Carpousis AJ, Robinson CV, Symmons MF, Luisi BF 2004 J Mol Biol 340 5 965-979 The experimental domain included the coiled coil segment B region. The 7SrRNA binding region is within this domain. There is an arginine-rich region within this domain, residues 796-819, that may gain some structure upon the binding to RNA. This domain contains the portion of the disordered CTD that binds helicase RhlB. It binds helicase RhlB in a 1:1 ratio. The binding of helicase RhlB to this domain stimulates the ATPase activity of the helicase. Binding to the helicase protein does not induce folding of the R-domain. Disordered - Extended 796 819 RRSRRSPRHLRVSGQRRRRYRDER Fragment Function arises via a disorder to order transition Unknown Protein-rRNA binding Paper 15236960 Callaghan AJ, Aurikko JP, Ilag LL, Gunter Grossmann J, Chandran V, Kuhnel K, Poljak L, Carpousis AJ, Robinson CV, Symmons MF, Luisi BF 2004 J Mol Biol 340 5 965-979 This region is completely contained within the R-domain. This region is disordered because it is within the CTD domain of the protein but it is thought to gain structure upon the binding of RNA. Disordered - Extended native-CTD 580 1038 ALFSGGEETKPTEQPAPKAEAKPERQQDRRKPRQNNRRDRNERRDTRSERTEGSDNREENRRNRRQAQQQTAETRESRQQAEVTEKARTADEQQAPRRERSRRRNDDKRQAQQEAKALNVEEQSVQETEQEERVRPVQPRRKQRQLNQKVRYEQSVAEEAVVAPVVEETVAAEPIVQEAPAPRTELVKVPLPVVAQTAPEQQEENNADNRDNGGMPRRSRRSPRHLRVSGQRRRRYRDERYPTQSPMPLTVACASPELASGKVWIRYPIVRPQDVQVEEQREQEEVHVQPMVTEVPVAAAIEPVVSAPVVEEVAGVVEAPVQVAEPQPEVVETTHPEVIAAAVTEQPQVITESDVAVAQEVAEQAEPVVEPQEETADIEEVVETAEVVVAEPEVVAQPAAPVVAEVAAEVETVAAVEPEVTVEHNHATAPMTRAPAPEYVPEAPRHSDWQRPTFAFEGK Complex Fragment Function arises from the disordered state Unknown Protein-protein binding Sensitivity to proteolysis Complex, (native-CTD-enolase) less sensitive to chymotrypsin Complex, (native-CTD-enolase) very sensitive to Protease K Paper 15236960 Callaghan AJ, Aurikko JP, Ilag LL, Gunter Grossmann J, Chandran V, Kuhnel K, Poljak L, Carpousis AJ, Robinson CV, Symmons MF, Luisi BF 2004 J Mol Biol 340 5 965-979 This domain contains the entire C segment, residues 839-850. This fragment is a version of CTD isolated under native conditions without affinity tags. This domain was co-purified with enolase. The binding region included residues 816-1038. PDB entries 1SLJ:A, 1SMX:A, B, and 1SN8:A, B pertain to the ordered region of RNase E. These entries are related to amino acid residues 35-125. Sortase A SrtA Q9S446 Q9S446 5726436 NF00431099 Staphylococcus aureus 206 MKKWTNRLMTIAGVVLILVAAYLFAKPHIDNYLHDKDKDEKIEQYDKNVKEQASKDKKQQAKPQIPKDKSKVAGYIEIPDADIKEPVYPGPATPEQLNRGVSFAEENESLDDQNISIAGHTFIDRPNYQFTNLKAAKKGSMVYFKVGNETRKYKMTSIRDVKPTDVGVLDEQKGKDKQLTLITCDDYNEKTGVWEKRKIFVATEVK Disordered - Extended disordered loop 162 174 KPTDVGVLDEQKG Engineered 1IJAA Function arises from the disordered state Molecular assembly Substrate/ligand binding Nuclear magnetic resonance (NMR) 306 6.7 CaCl2 20 DTT 3 H2O 7 NaCl 100 NaN3 0.01 SrtAN59 protein 2.5 Tris-HCl 50 Paper 11371637 Ilangovan U, Ton-That H, Iwahara J, Schneewind O, Clubb RT 2001 Proc Natl Acad Sci U S A 98 11 6056-61 15117963 Zong Y, Bice TW, Ton-That H, Schneewind O, Narayana SV 2004 J Biol Chem 279 30 31383-9 The PDB file does not contain the first 59 amino acids of the sequence (Zhong 2004). It was shown that the removal of this N terminal region had no effect on the enzymatic activity of the protein. The disordered region is part of the “catalytic core” of the protein (Ilangovan 2001). Beta-defensin 12 BNDB-12 P46170 1168638 Bos taurus (Bovine) 38 GPLSCGRNGGVCIPIRCPVPMRQIGTCFGRPVKCCRSW Disordered 1 4 GPLS Native 1BNBA Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) Paper 7577957 Zimmermann GR, Legault P, Selsted ME, Pardi A 1995 Biochemistry 34 41 13663-71 Growth factor receptor-bound protein 2 Ash protein GRB2 adapter protein SH2/SH3 adapter GRB2 P62993 Homo sapiens 217 MEAIAKYDFKATADDELSFKRGDILKVLNEECDQNWYKAELNGKDGFIPKNYIEMKPHPWFFGKIPRAKAEEMLSKQRHDGAFLIRESESAPGDFSLSVKFGNDVQHFKVLRDGAGKYFLWVVKFNSLNELVDYHRSTSVSRNQQIFLRDIEQVPQQPTYVQALFDFDPQEDGELGFRRGDFIHVMDNSDPNWWKGACHGQTGMFPRNYVTPVNRNV Disordered 58 59 HP Native Function arises from the disordered state Entropic chain Flexible linkers/spacers Nuclear magnetic resonance (NMR) Paper 11178911 Yuzawa S, Yokochi M, Hatanaka H, Ogura K, Kataoka M, Miura K, Mandiyan V, Schlessinger J, Inagaki F 2001 J Mol Biol 306 3 527-37 Disordered 153 159 QVPQQPT Native Function arises from the disordered state Entropic chain Flexible linkers/spacers Nuclear magnetic resonance (NMR) Paper 11178911 Yuzawa S, Yokochi M, Hatanaka H, Ogura K, Kataoka M, Miura K, Mandiyan V, Schlessinger J, Inagaki F 2001 J Mol Biol 306 3 527-37 Insulin-like growth factor binding protein 6 IBP-6 IGF-binding protein 6 IGFBP-6 P24592 A39842 Homo sapiens (Human) 240 MTPHRLLPPLLLLLALLLAASPGGALARCPGCGQGVQAGCPGGCVEEEDGGSPAEGCAEAEGCLRREGQECGVYTPNCAPGLQCHPPKDDEAPLRALLLGRGRCLPARAPAVAEENPKESKPQAGTARPQDVNRRDQQRNPGTSTTPSQPNSAGVQDTEMGPCRRHLDSVLQQLQTEVYRGAQTLYVPNCDHRGFYRKRQCRSSQGQRRGPCWCVDRMGKSLPGSPDGNGSSSCPTGSSG Disordered - Extended Loop 177 184 EVYRGAQT Fragment Native 1RMJA Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 298 4.5 D2O 5 H2O 95 sodium acetate 10 sodium azide 0.02 Paper 15308688 Headey SJ, Keizer DW, Yao S, Brasier G, Kantharidis P, Bach LA, Norton RS 2004 Mol Endocrinol 18 11 2740-2750 Disordered - Extended Loop 205 211 QGQRRGP Fragment Native 1RMJA Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 298 4.5 D2O 5 H2O 95 sodium acetate 10 sodium azide 0.02 Paper 15308688 Headey SJ, Keizer DW, Yao S, Brasier G, Kantharidis P, Bach LA, Norton RS 2004 Mol Endocrinol 18 11 2740-2750 Disordered - Extended 223 240 PGSPDGNGSSSCPTGSSG Fragment Native 1RMJA Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 298 4.5 D2O 5 H2O 95 sodium acetate 10 sodium azide 0.02 Paper 15308688 Headey SJ, Keizer DW, Yao S, Brasier G, Kantharidis P, Bach LA, Norton RS 2004 Mol Endocrinol 18 11 2740-2750 The experimental fragment was the C-terminal domain of human IGFHB-6. Transcription factor p65 Nuclear factor NF-kappa-B p65 subunit Q04207 Mus musculus (Mouse) 549 MDDLFPLIFPSEPAQASGPYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINGYTGPGTVRISLVTKDPPHRPHPHELVGKDCRDGYYEADLCPDRSIHSFQNLGIQCVKKRDLEQAISQRIQTNNNPFHVPIEEQRGDYDLNAVRLCFQVTVRDPAGRPLLLTPVLSHPIFDNRAPNTAELKICRVNRNSGSCLGGDEIFLLCDKVQKEDIEVYFTGPGWEARGSFSQADVHRQVAIVFRTPPYADPSLQAPVRVSMQLRRPSDRELSEPMEFQYLPDTDDRHRIEEKRKRTYETFKSIMKKSPFNGPTEPRPPTRRIAVPTRNSTSVPKPAPQPYTFPASLSTINFDEFSPMLLPSGQISNQALALAPSSAPVLAQTMVPSSAMVPLAQPPAPAPVLTPGPPQSLSAPVPKSTQAGEGTLSEALLHLQFDADEDLGALLGNSTDPGVFTDLASVDNSEFQQLLNQGVSMSHSTAEPMLMEYPEAITRLVTGSQRPPDPAPTPLGTSGLPNGLSGDEDFSSIADMDFSALLSQISS Disordered 19 304 PYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINGYTGPGTVRISLVTKDPPHRPHPHELVGKDCRDGYYEADLCPDRSIHSFQNLGIQCVKKRDLEQAISQRIQTNNNPFHVPIEEQRGDYDLNAVRLCFQVTVRDPAGRPLLLTPVLSHPIFDNRAPNTAELKICRVNRNSGSCLGGDEIFLLCDKVQKEDIEVYFTGPGWEARGSFSQADVHRQVAIVFRTPPYADPSLQAPVRVSMQLRRPSDRELSEPMEFQYLPDTDDRHRIEEKRKR Fragment Native 1IKNA Relationship to function unknown Molecular recognition effectors Nuclear localization Paper 9384558 Huang DB, Huxford T, Chen YQ, Ghosh G 1997 Structure 5 11 1427-36 Histone binding protein N1/N2 P06180 Xenopus laevis (African clawed frog) 589 AEETAALSTEKTEDTSTAPSTSAEKADGIDIDTEAKRLMGAGQKHLVMKDVRSAVNLFQEASSLLAKQYGETADECAEAFYSYGMSLLELARLENGVLGNALEGMPEDDEEEAEKEEDPNIPSADNLDEKEREQLREQVYDAMAEDQRAPDDTSESEAKGKPEGDSKDKEADEKMKNGQKETEKVTDDLKIDSASRDVPMDKSGKGEPPESKDAETLVEQKESKPETLKEKSIETKEKDLSKEKTDAKETANQSPDSTEVAEEKMDSEASESKESTSIPPTENEANKPDDPEKMEEEEEGEDSEENEDGTEENEGTEEKETEEEDVGNLQLAWEMLDLCKTIFKRQQSKEAQLKAAQAHQKLGEVCIESENYSQAVEDFLACLNIQKEHLEEHDRLLAETHYHLGLAYQYSSKHEEAISHFTQSIGVIEKRMDVLTKQLEASVGELVDEVKKEMDELKDLLPDIKEKIEDSKEAQKNATVTEKALKETLVGGSSGFSKENGSTSSSSAVEKSGDSTVPVTNCVSDISHLVRKKRKTEEESPLKDKDAKKSKQEPVANGAGNGDAVVPTNEEAEKAEEASMETATVESTA This protein shows aberrant migration on SDS-PAGE gels and is heat stable. These two properties strongly suggest that the protein is totally disordered but are not considered definitive evidence that it is, in fact, disordered. Osteopontin Bone sialoprotein 1 Nephropontin Secreted phosphoprotein 1 SPP-1 Urinary stone protein Uropontin P10451 Hs.313 P10451 129260 S09575 Homo sapiens (Human) 314 MRIAVICFCLLGITCAIPVKQADSGSSEEKQLYNKYPDAVATWLNPDPSQKQNLLAPQNAVSSEETNDFKQETLPSKSNESHDHMDDMDDEDDDDHVDSQDSIDSNDSDDVDDTDDSHQSDESHHSDESDELVTDFPTDLPATEVFTPVVPTVDTYDGRGDSVVYGLRSKSKKFRRPDIQYPDATDEDITSHMESEELNGAYKAIPVAQDLNAPSDWDSRGKDSYETSQLDDQSAETHSHKQSRLYKRKANDESNEHSDVIDSQELSKVSREFHSHEFHSHEDMLVVDPKSKEEDKHLKFRISHELDSASSEVN Disordered 1 314 MRIAVICFCLLGITCAIPVKQADSGSSEEKQLYNKYPDAVATWLNPDPSQKQNLLAPQNAVSSEETNDFKQETLPSKSNESHDHMDDMDDEDDDDHVDSQDSIDSNDSDDVDDTDDSHQSDESHHSDESDELVTDFPTDLPATEVFTPVVPTVDTYDGRGDSVVYGLRSKSKKFRRPDIQYPDATDEDITSHMESEELNGAYKAIPVAQDLNAPSDWDSRGKDSYETSQLDDQSAETHSHKQSRLYKRKANDESNEHSDVIDSQELSKVSREFHSHEFHSHEDMLVVDPKSKEEDKHLKFRISHELDSASSEVN Native Function arises via a disorder to order transition Molecular assembly Protein-protein binding Substrate/ligand binding Nuclear magnetic resonance (NMR) 303 6 protein per mL water (BSP) 15 Nuclear magnetic resonance (NMR) 303 6 protein 15 sodium phosphate 10 Paper 11162539 Fisher LW, Torchia DA, Fohr B, Young MF, Fedarko NS 2001 Biochem Biophys Res Commun 280 2 460-5 Wiskott-Aldrich syndrome protein WASp P42768 Homo sapiens (Human) 501 SGGPMGGRPGGRGAPAVQQNIPSTLLQDHENQRLFEMLGRKCLTLATAVVQLYLALPPGAEHWTKEHCGAVCFVKDNPQKSYFIRLYGLQAGRLLWEQELYSQLVYSTPTPFFHTFAGDDCQAGLNFADEDEAQAFRALVQEKIQKRNQRQSGDRRQLPPPPTPANEERRGGLPPLPLHPGGDQGGPPVGPLSLGLATVDIQNPDITSSRYRGLPAPGPSPADKKRSGKKKISKADIGAPSGFKHVSHVGWDPQNGFDVNNLDPDLRSLFSRAGISEAQLTDAETSKLIYDFIEDQGGLEAVRQEMRRQEPLPPPPPPSRGGNQLPRPPIVGGNKGRSGPLPPVPLGIAPPPPTPRGPPPPGRGGPPPPPPPATGRSGPLPPPPPGAGGPPMPPPPPPPPPPPSSGNGPAPPPLPPALVPAGGLAPGGGRGALLDQIRQGIQLNKTPGAPESSALQPPPQSSEGLVGALMHVMQKRSRAIHSSDEGEDQAGDEDEDDEWDD Disordered 230 249 KKISKADIGAPSGFKHVSHV Engineered Fragment Native Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Paper 10724160 Kim AS, Kakalis LT, Abdul-Manan N, Liu GA, Rosen MK 2000 Nature 404 6774 151-8 Experimental sequence was KKISKADIGAPSGFKHVSHVGWDPQNGFDVNNLDPDLRSLFSRAGISEAQLTDAETSKLI YDFIEDQGGLEAVRQEMRRQ. Disordered 241 249 SGFKHVSHV Engineered Fragment Mutant Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Paper 10724160 Kim AS, Kakalis LT, Abdul-Manan N, Liu GA, Rosen MK 2000 Nature 404 6774 151-8 Experimental sequence was a fusion of two fragments of WASp joined by a short GS linker. The experimental sequence was K KISKADIGAP SGFKHVSHVG WDPQNGFDVN NLDPDLRSLF SRAGISEAQL TDAETSKLIY DFIEDQGGLE AVRQEMRRQE ggsggs SSEGLVGALM HVMQKRSRAI HSSDEGEDQA GD. Disordered 480 492 IHSSDEGEDQAGD Engineered Fragment Mutant Relationship to function unknown Unknown Unknown Paper 10724160 Kim AS, Kakalis LT, Abdul-Manan N, Liu GA, Rosen MK 2000 Nature 404 6774 151-8 Experimental sequence was a fusion of two fragments of WASp joined by a short GS linker. The experimental sequence was K KISKADIGAP SGFKHVSHVG WDPQNGFDVN NLDPDLRSLF SRAGISEAQL TDAETSKLIY DFIEDQGGLE AVRQEMRRQE ggsggs SSEGLVGALM HVMQKRSRAI HSSDEGEDQA GD. BN28a Q9FUM5 Brassica napus 65 MADNKQSFQAGQAAGRAEEKGNVLMDKVKDAATAAGASAQTAGQKITEAAGGAVNLVKEKTGMNK Disordered 1 65 MADNKQSFQAGQAAGRAEEKGNVLMDKVKDAATAAGASAQTAGQKITEAAGGAVNLVKEKTGMNK Native Relationship to function unknown Unknown Unknown Far-UV circular dichroism (CD) Nuclear magnetic resonance (NMR) Paper 9046590 Boothe JG, Sonnichsen FD, de Beus MD, Johnson-Flanagan AM 1997 Plant Physiol 113 2 367-76 Nucleoplasmin P05221 Xenopus laevis (African clawed frog) 200 MASTVSNTSKLEKPVSLIWGCELNEQDKTFEFKVEDDEEKCEHQLALRTVCLGDKAKDEFNIVEIVTQEEGAEKSVPIATLKPSILPMATMVGIELTPPVTFRLKAGSGPLYISGQHVAMEEDYSWAEEEDEGEAEGEEEEEEEEDQESPPKAVKRPAATKKAGQAKKKKLDKEDESSEEDSPTKKGKGAGRGRKPAAKK Disordered 120 200 MEEDYSWAEEEDEGEAEGEEEEEEEEDQESPPKAVKRPAATKKAGQAKKKKLDKEDESSEEDSPTKKGKGAGRGRKPAAKK Fragment Native Relationship to function unknown Unknown Unknown Far-UV circular dichroism (CD) Fourier transform infrared spectroscopy Sensitivity to proteolysis Paper 11248694 Hierro A, Arizmendi JM, De Las Rivas J, Urbaneja MA, Prado A, Muga A 2001 Eur J Biochem 268 6 1739-48 130 kDa myosin-binding subunit of smooth muscle myosin phophatase M130 Q90624 Gallus gallus (Chicken) 963 MKMADAKQKRNEQLKRWIGSETDLEPPVVKRKKTKVKFDDGAVFLAACSSGDTEEVLRLLERGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEYLISQGAHVGAVNSEGDTPLDIAEEEAMEELLQNEVNRQGVDIEAARKEEERIMLRDARQWLNSGHINDVRHAKSGGTALHVAAAKGYTEVLKLLIQARYDVNIKDYDGWTPLHAAAHWGKEEACRILVENLCDMEAVNKVGQTAFDVADEDILGYLEELQKKQNLLHSEKREKKSPLIESTANLDNNQTQKTFKNKETLIMEQEKNASSIESLEHEKADEEEEGKKDESSCSSEEEEDDDSESEAETDKAKTLANANTTSTQSASMTAPSVAGGQGTPTSPLKKFPTSTTKVSPKEEERKDESPASWRLGLRKTGSYGALAEITASKEAQKEKDSAGVIRSASSPRLSSSLDNKEKEKDGKGTRLAYVAPTIPRRLASTSDIDEKENSGSFGRRQDDLVSSNVPSTASTVTSSAGLQKTLPASANTTTKSTTGSTSAGVQSSTSNRLWAEDSTEKEKDSVPTAVTVPVAPSVVNAAATTTAMTTATSGTVSSTSEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRSRSTRTREQENEEKEKEEKEKQDKEKQEEKKESETKDDDYRQRYSRTVEEPYHRYRPTSTSTSTSSTSSLSTSTSSLSSSSQLNRPNSLIGITSAYSRSGTKESEREGGKKEEEKEEDKSQPKSIRERRRPREKRRSTGVSFWTQDSDENEQEHQSDSEEGTNKKETQSDSLSRYDTGSLSVSSGDRYDSAQGRSGSQSYLEDRKPYCSRLEKEDSTDFKKLYEQILAENEKLKAQLHDTNMELTDLKLQLEKTTQRQERFADRSLLEMEKRVSGKSQYLLGGKKSSRKKDI Disordered 1 299 MKMADAKQKRNEQLKRWIGSETDLEPPVVKRKKTKVKFDDGAVFLAACSSGDTEEVLRLLERGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEYLISQGAHVGAVNSEGDTPLDIAEEEAMEELLQNEVNRQGVDIEAARKEEERIMLRDARQWLNSGHINDVRHAKSGGTALHVAAAKGYTEVLKLLIQARYDVNIKDYDGWTPLHAAAHWGKEEACRILVENLCDMEAVNKVGQTAFDVADEDILGYLEELQKKQNLLHSEKREKKS Fragment Native 1S70B Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Paper 15164081 Terrak M, Kerff F, Langsetmo K, Tao T, Dominguez R 2004 Nature 429 6993 780-4 protein phosphatase 1, regulatory (inhibitor) subunit 11 isoform 1 11386175 Homo sapiens (Human) 126 MAEAGAGLSETVTETTVTVTTEPENRSLTIKLRKRKPEKKVEWTSDTVDNEHMGRRSSKCCCIYEKPRAFGESSTESDEEEEEGCGHTHCVRGHRKGRRRATLGPTPTTPPQPPDPSQPPPGPMQH Disordered 1 126 MAEAGAGLSETVTETTVTVTTEPENRSLTIKLRKRKPEKKVEWTSDTVDNEHMGRRSSKCCCIYEKPRAFGESSTESDEEEEEGCGHTHCVRGHRKGRRRATLGPTPTTPPQPPDPSQPPPGPMQH Native Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Thermal stability Aberrant mobility on SDS-PAGE gel Gel filtration/size exclusion chromatography Paper 9843442 Zhang J, Zhang L, Zhao S, Lee EY 1998 Biochemistry 37 47 16728-34 Peripherin Peripherin/rds peripherin/retinal degeneration slow P/rds Retinal degeneration slow protein P17810 P17810 132211 A34608 Bos taurus (Bovine) 345 ALLKVKFDQKKRVKLAQGLWLMNWFSVLAGIIIFGLGLFLKIELRKRSDVMNNSESHFVPNSLIGVGVLSCVFNSLAGKICYDALDPAKYAKWKPWLKPYLAVCVLFNVVLFLVALCCFLLRGSLESTLAHGLKNGMKFYRDTDTPGRCFMKKTIDMLQIEFKCCGNNGFRDWFEIQWISNRYLDFSSKEVKDRIKSNVDGRYLVDGVPFSCCNPNSPRPCIQYQLTNNSAHYSYDHQTEELNLWLRGCRAALLSYYSNLMNTTGAVTLLVWLFEVTITVGLRYLHTALEGMANPEDPECESEGWLLEKSVPETWKAFLESVKKLGKGNQVEAEGEDAGQAPAAG Disordered - Extended C-terminal domain 283 345 RYLHTALEGMANPEDPECESEGWLLEKSVPETWKAFLESVKKLGKGNQVEAEGEDAGQAPAAG Fragment Native Function arises from the disordered state Unknown Unknown Sensitivity to proteolysis 310 7.5 0.4 mg/ml protein 2 microg/ml Proteinase K 50 mM Tris-HCl, 150 mM NaCl Intrinsic fluorescence 298 7.5 50 mM Tris-HCl, 150 mM NaCl, 1 mM TCEP 5 microg/ml protein excitation at 295nm, emission scan from 295 to 430nm Far-UV circular dichroism (CD) 283 7.5 0.1 cm cell 0.3 mg/ml protein 50 mM Tris-HCl, 150 mM NaCl, 1 mM TCEP Gel filtration/size exclusion chromatography 298 7.5 0.2 ml/min flow rate 0.5 to 1.5 mg protein 1 cm x 46 cm Sephacryl S-100HR column 50 mM Tris-HCl, 150 mM NaCl, 1 mM TCEP Analytical ultracentrifugation 293 7.5 1.0, 0.3 and 0.1 mg/ml protein 500 microl aliquots 50k rpm 50 mM Tris-HCl, 150 mM NaCl, 1 mM TCEP Paper L.M. Ritter, T. Arakawa and A.F.X. Goldberg 2005 Protein and Peptide Letters 12 7 677-686 Involucrin P07476 Homo sapiens (Human) 585 MSQQHTLPVTLSPALSQELLKTVPPPVNTHQEQMKQPTPLPPPCQKVPVELPVEVPSKQEEKHMTAVKGLPEQECEQQQKEPQEQELQQQHWEQHEEYQKAENPEQQLKQEKTQRDQQLNKQLEEEKKLLDQQLDQELVKRDEQLGMKKEQLLELPEQQEGHLKHLEQQEGQLKHPEQQEGQLELPEQQEGQLELPEQQEGQLELPEQQEGQLELPEQQEGQLELPQQQEGQLELSEQQEGQLELSEQQEGQLELSEQQEGQLKHLEHQEGQLEVPEEQMGQLKYLEQQEGQLKHLDQQEKQPELPEQQMGQLKHLEQQEGQPKHLEQQEGQLEQLEEQEGQLKHLEQQEGQLEHLEHQEGQLGLPEQQVLQLKQLEKQQGQPKHLEEEEGQLKHLVQQEGQLKHLVQQEGQLEQQERQVEHLEQQVGQLKHLEEQEGQLKHLEQQQGQLEVPEQQVGQPKNLEQEEKQLELPEQQEGQVKHLEKQEAQLELPEQQVGQPKHLEQQEKHLEHPEQQDGQLKHLEQQEGQLKDLEQQKGQLEQPVFAPAPGQVQDIQPALPTKGEVLLPVEHQQQKQEVQWPPKHK Disordered 336 365 LEQQEGQLEHLEQQEGQLEHLEQQEGQLEH Engineered Mutant Relationship to function unknown Unknown Unknown Paper 10601302 Lazo ND, Downing DT 1999 J Biol Chem 274 52 37340-4 Experimental fragment was three repeats of LEQQEGQLEH. This consensus repeat sequence had the following deviations from the native sequence; E248Q and E354K. Note that there are several LEQQEGQLEH repeats in native sequence. Disordered 336 365 PEQQEGQLELPEQQEGQLELPEQQEGQLEL Engineered Fragment Native Relationship to function unknown Unknown Unknown Paper 10601302 Lazo ND, Downing DT 1999 J Biol Chem 274 52 37340-4 The experimental sequence consisted of three repeats of PEQQEGQLEL. Note that there are several PEQQEGQLEL repeats in the native sequence. Nucleoporin NUP2 Nuclear pore protein NUP2 p95 P32499 Saccharomyces cerevisiae (Baker's yeast) 720 MAKRVADAQIQRETYDSNESDDDVTPSTKVASSAVMNRRKIAMPKRRMAFKPFGSAKSDETKQASSFSFLNRADGTGEAQVDNSPTTESNSRLKALNLQFKAKVDDLVLGKPLADLRPLFTRYELYIKNILEAPVKSIENPTQTKGNDAKPAKVEDVQKSSDSSSEDEVKVEGPKFTIDAKPPISDSVFSFGPKKENRKKDESDSENDIEIKGPEFKFSGTVSSDVFKLNPSTDKNEKKTETNAKPFSFSSATSTTEQTKSKNPLSLTEATKTNVDNNSKAEASFTFGTKHAADSQNNKPSFVFGQAAAKPSLEKSSFTFGSTTIEKKNDENSTSNSKPEKSSDSNDSNPSFSFSIPSKNTPDASKPSFSFGVPNSSKNETSKPVFSFGAATPSAKEASQEDDNNNVEKPSSKPAFNLISNAGTEKEKESKKDSKPAFSFGISNGSESKDSDKPSLPSAVDGENDKKEATKPAFSFGINTNTTKTADTKAPTFTFGSSALADNKEDVKKPFSFGTSQPNNTPSFSFGKTTANLPANSSTSPAPSIPSTGFKFSLPFEQKGSQTTTNDSKEESTTEATGNESQDATKVDATPEESKPINLQNGEEDEVALFSQKAKLMTFNAETKSYDSRGVGEMKLLKKKDDPSKVRLLCRSDGMGNVLLNATVVDSFKYEPLAPGNDNLIKAPTVAADGKLVTYIVKFKQKEEGRSFTKAIEDAKKEMK Disordered 1 720 MAKRVADAQIQRETYDSNESDDDVTPSTKVASSAVMNRRKIAMPKRRMAFKPFGSAKSDETKQASSFSFLNRADGTGEAQVDNSPTTESNSRLKALNLQFKAKVDDLVLGKPLADLRPLFTRYELYIKNILEAPVKSIENPTQTKGNDAKPAKVEDVQKSSDSSSEDEVKVEGPKFTIDAKPPISDSVFSFGPKKENRKKDESDSENDIEIKGPEFKFSGTVSSDVFKLNPSTDKNEKKTETNAKPFSFSSATSTTEQTKSKNPLSLTEATKTNVDNNSKAEASFTFGTKHAADSQNNKPSFVFGQAAAKPSLEKSSFTFGSTTIEKKNDENSTSNSKPEKSSDSNDSNPSFSFSIPSKNTPDASKPSFSFGVPNSSKNETSKPVFSFGAATPSAKEASQEDDNNNVEKPSSKPAFNLISNAGTEKEKESKKDSKPAFSFGISNGSESKDSDKPSLPSAVDGENDKKEATKPAFSFGINTNTTKTADTKAPTFTFGSSALADNKEDVKKPFSFGTSQPNNTPSFSFGKTTANLPANSSTSPAPSIPSTGFKFSLPFEQKGSQTTTNDSKEESTTEATGNESQDATKVDATPEESKPINLQNGEEDEVALFSQKAKLMTFNAETKSYDSRGVGEMKLLKKKDDPSKVRLLCRSDGMGNVLLNATVVDSFKYEPLAPGNDNLIKAPTVAADGKLVTYIVKFKQKEEGRSFTKAIEDAKKEMK Monomeric Native Relationship to function unknown Unknown Unknown Far-UV circular dichroism (CD) Fourier transform infrared spectroscopy Sensitivity to proteolysis Gel filtration/size exclusion chromatography Analytical ultracentrifugation Paper 12065587 Denning DP, Uversky V, Patel SS, Fink AL, Rexach M 2002 J Biol Chem 277 36 33447-55 G2/mitotic-specific cyclin B1 P14635 Homo sapiens (Human) 433 MALRVTRNSKINAENKAKINMAGAKRVPTAPAATSKPGLRPRTALGDIGNKVSEQLQAKMPMKKEAKPSATGKVIDKKLPKPLEKVPMLVPVPVSEPVPEPEPEPEPEPVKEEKLSPEPILVDTASPSPMETSGCAPAEEDLCQAFSDVILAVNDVDAEDGADPNLCSEYVKDIYAYLRQLEEEQAVRPKYLLGREVTGNMRAILIDWLVQVQMKFRLLQETMYMTVSIIDRFMQNNCVPKKMLQLVGVTAMFIASKYEEMYPPEIGDFAFVTDNTYTKHQIRQMEMKILRALNFGLGRPLPLHFLRRASKIGEVDVEQHTLAKYLMELTMLDYDMVHFPPSQIAAGAFCLALKILDNGEWTPTLQHYLSYTEESLLPVMQHLAKNVVMVNQGLTKHMTVKNKYATSKHAKISTLPQLNSALVQDLAKAVAKV Disordered ND-cycB 1 78 MALRVTRNSKINAENKAKINMAGAKRVPTAPAATSKPGLRPRTALGDIGNKVSEQLQAKMPMKKEAKPSATGKVIDKK Fragment Native Function arises from the disordered state Molecular recognition effectors Protein-protein binding Far-UV circular dichroism (CD) Nuclear magnetic resonance (NMR) Paper 12220679 Cox CJ, Dutta K, Petri ET, Hwang WC, Lin Y, Pascal SM, Basavappa R 2002 FEBS Lett 527 1-3 303-8 Transcription factor 4 Immunoglobulin transcription factor 2 ITF-2 SEF-2 SL3-3 enhancer factor 2 P15884 Hs.200285 P15884 3915747 A41311 Homo sapiens (Human) 667 MHHQQRMAALGTDKELSDLLDFSAMFSPPVSSGKNGPTSLASGHFTGSNVEDRSSSGSWGNGGHPSPSRNYGDGTPYDHMTSRDLGSHDNLSPPFVNSRIQSKTERGSYSSYGRESNLQGCHQQSLLGGDMDMGNPGTLSPTKPGSQYYQYSSNNPRRRPLHSSAMEVQTKKVRKVPPGLPSSVYAPSASTADYNRDSPGYPSSKPATSTFPSSFFMQDGHHSSDPWSSSSGMNQPGYAGMLGNSSHIPQSSSYCSLHPHERLSYPSHSSADINSSLPPMSTFHRSGTNHYSTSSCTPPANGTDSIMANRGSGAAGSSQTGDALGKALASIYSPDHTNNSFSSNPSTPVGSPPSLSAGTAVWSRNGGQASSSPNYEGPLHSLQSRIEDRLERLDDAIHVLRNHAVGPSTAMPGGHGDMHGIIGPSHNGAMGGLGSGYGTGLLSANRHSLMVGTHREDGVALRGSHSLLPNQVPVPQLPVQSATSPDLNPPQDPYRGMPPGLQGQSVSSGSSEIKSDDEGDENLQDTKSSEDKKLDDDKKDIKSITSNNDDEDLTPEQKAEREKERRMANNARERLRVRDINEAFKELGRMVQLHLKSDKPQTKLLILHQAVAVILSLEQQVRERNLNPKAACLKRREEEKVSSEPPPLSLAGPHPGMGDASNHMGQM Disordered 1 53 MHHQQRMAALGTDKELSDLLDFSAMFSPPVSSGKNGPTSLASGHFTGSNVEDR Fragment Native Function arises via a disorder to order transition Molecular assembly Protein-DNA binding Protein-protein binding Far-UV circular dichroism (CD) Intrinsic fluorescence 7.4 DTT 2 sodium chloride 100 sodium phosphate buffer 50 Paper 11237626 Knapp S, Zamai M, Volpi D, Nardese V, Avanzi N, Breton J, Plyte S, Flocco M, Marconi M, Isacchi A, Caiolfa VR 2001 J Mol Biol 306 5 1179-1189 Disordered 1 56 MHHQQRMAALGTDKELSDLLDFSAMFSPPVSSGKNGPTSLASGHFTGSNVEDRSSS Fragment Native Function arises via a disorder to order transition Molecular assembly Protein-DNA binding Protein-protein binding Far-UV circular dichroism (CD) Intrinsic fluorescence 7.4 DTT 2 sodium chloride 100 sodium phosphate buffer 50 Paper 11237626 Knapp S, Zamai M, Volpi D, Nardese V, Avanzi N, Breton J, Plyte S, Flocco M, Marconi M, Isacchi A, Caiolfa VR 2001 J Mol Biol 306 5 1179-1189 Disordered 1 130 MHHQQRMAALGTDKELSDLLDFSAMFSPPVSSGKNGPTSLASGHFTGSNVEDRSSSGSWGNGGHPSPSRNYGDGTPYDHMTSRDLGSHDNLSPPFVNSRIQSKTERGSYSSYGRESNLQGCHQQSLLGGD Fragment Native Function arises via a disorder to order transition Molecular assembly Protein-DNA binding Protein-protein binding Far-UV circular dichroism (CD) Intrinsic fluorescence 7.4 DTT 2 sodium chloride 100 sodium phosphate buffer 50 Paper 11237626 Knapp S, Zamai M, Volpi D, Nardese V, Avanzi N, Breton J, Plyte S, Flocco M, Marconi M, Isacchi A, Caiolfa VR 2001 J Mol Biol 306 5 1179-1189 Three constructs of TCF4 were used in the Knapp paper. They extended from residues 1-53, 1-56, and 1-130. Each was found to be disordered in solution. Clathrin coat assembly protein AP180 91 kDa synaptosomal-associated protein Clathrin coat associated protein AP180 Q05140 Rattus norvegicus 915 MSGQTLTDRIAAAQYSVTGSAVARAVCKATTHEVMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLASRNTLFNLSNFLDKSGSHGYDMSTFIRRYSRYLNEKAFSYRQMAFDFARVKKGADGVMRTMVPEKLLKSMPILQGQIDALLEFDVHPNELTNGVINAAFMLLFKDLIKLFACYNDGVINLLEKFFEMKKGQCKDALEIYKRFLTRMTRVSEFLKVADEVGIDKGDIPDLTQAPSSLMETLEQHLNTLEGKKPGNNEGSGAPSPLSKSSPATTVTSPNSTPAKTIDTSPPVDIFATASAAAPVSSAKPSSDLLDLQPDFSGARAGAAAPVPPPTGGATAWGDLLGEDSLAALSSVPSEAPISDPFAPEPSPPTTTTEPASASASATTAVTAATTEVDLFGDAFAASPGEAPAASEGATAPATPAPVAAALDACSGNDPFAPSEGSAEAAPELDLFAMKPPETSAPVVTPTASTAPPVPATAPSPAPTAVAATAATTTAAAAATTTATTSAAAATTAAAPPALDIFGDLFDSAPEVAAASKPDVAPSIDLFGTDAFSSPPRGASPVPESSLTADLLSGSGFHCAEDDRHVPLFFTAVDAFAAPSPASTASPAKAESSGVIDLFGDAFGSSASETQPAPQAVSSSSASADLLAGFGGSFMAPSTTPVTPAQNNLLQPNFEAAFGTTPSTSSSSSFDPSGDLLMPTMAPSGQPAPVSMVPPSPAMSASKGLGSDLDSSLASLVGNLGISGTTSKKGDLQWNAGEKKLTGGANWQPKVTPATWSAGVPPQGTVPPTSSVPPGAGAPSVGQPGAGYGMPPAGTGMTMMPQQPVMFAQPMMRPPFGAAAVPGTQLSPSPTPATQSPKKPPAKDPLADLNIKDFL Disordered 328 896 VDIFATASAAAPVSSAKPSSDLLDLQPDFSGARAGAAAPVPPPTGGATAWGDLLGEDSLAALSSVPSEAPISDPFAPEPSPPTTTTEPASASASATTAVTAATTEVDLFGDAFAASPGEAPAASEGATAPATPAPVAAALDACSGNDPFAPSEGSAEAAPELDLFAMKPPETSAPVVTPTASTAPPVPATAPSPAPTAVAATAATTTAAAAATTTATTSAAAATTAAAPPALDIFGDLFDSAPEVAAASKPDVAPSIDLFGTDAFSSPPRGASPVPESSLTADLLSGSGFHCAEDDRHVPLFFTAVDAFAAPSPASTASPAKAESSGVIDLFGDAFGSSASETQPAPQAVSSSSASADLLAGFGGSFMAPSTTPVTPAQNNLLQPNFEAAFGTTPSTSSSSSFDPSGDLLMPTMAPSGQPAPVSMVPPSPAMSASKGLGSDLDSSLASLVGNLGISGTTSKKGDLQWNAGEKKLTGGANWQPKVTPATWSAGVPPQGTVPPTSSVPPGAGAPSVGQPGAGYGMPPAGTGMTMMPQQPVMFAQPMMRPPFGAAAVPGTQLSPSPTPATQS Fragment Monomeric Native Relationship to function unknown Unknown Unknown Far-UV circular dichroism (CD) Analytical ultracentrifugation Gel filtration/size exclusion chromatography Paper 11756460 Kalthoff C, Alves J, Urbanke C, Knorr R, Ungewickell EJ 2002 J Biol Chem 277 10 8209-16 Siah-interacting protein CacyBP Calcyclin-binding protein SIP Q9CXW3 Q9CXW3 46576641 Mus musculus (Mouse) 229 MASVLEELQKDLEEVKVLLEKSTRKRLRDTLTSEKSKIETELKNKMQQKSQKKPELDNEKPAAVVAPLTTGYTVKISNYGWDQSDKFVKIYITLTGVHQVPTENVQVHFTERSFDLLVKNLNGKNYSMIVNNLLKPISVESSSKKVKTDTVIILCRKKAENTRWDYLTQVEKECKEKEKPSYDTEADPSEGLMNVLKKIYEDGDDDMKRTINKAWVESREKQAREDTEF Ordered SIPN Domain 1 47 MASVLEELQKDLEEVKVLLEKSTRKRLRDTLTSEKSKIETELKNKMQ Native Function arises from the ordered state Nuclear magnetic resonance (NMR) 303 7 NaCl 50 NaPi 20 Paper 15996101 Bhattacharya S, Lee YT, Michowski W, Jastrzebska B, Filipek A, Kuznicki J, Chazin WJ. 2005 Biochemistry 44 27 9462-71 Disordered 48 73 QKSQKKPELDNEKPAAVVAPLTTGYT Native Function arises from the disordered state Molecular assembly Protein-protein binding Nuclear magnetic resonance (NMR) 303 7 NaCl 50 NaPi 20 Paper 15996101 Bhattacharya S, Lee YT, Michowski W, Jastrzebska B, Filipek A, Kuznicki J, Chazin WJ. 2005 Biochemistry 44 27 9462-71 Ordered CS Domain 74 177 VKISNYGWDQSDKFVKIYITLTGVHQVPTENVQVHFTERSFDLLVKNLNGKNYSMIVNNLLKPISVESSSKKVKTDTVIILCRKKAENTRWDYLTQVEKECKEK Native Function arises from the ordered state Protein-protein binding Nuclear magnetic resonance (NMR) 303 7 NaCl 50 NaPi 20 Paper 15996101 Bhattacharya S, Lee YT, Michowski W, Jastrzebska B, Filipek A, Kuznicki J, Chazin WJ. 2005 Biochemistry 44 27 9462-71 Disordered SGS Domain 178 229 EKPSYDTEADPSEGLMNVLKKIYEDGDDDMKRTINKAWVESREKQAREDTEF Native Function arises from the disordered state Molecular assembly Protein-protein binding Nuclear magnetic resonance (NMR) 303 7 NaCl 50 NaPi 20 Paper 15996101 Bhattacharya S, Lee YT, Michowski W, Jastrzebska B, Filipek A, Kuznicki J, Chazin WJ. 2005 Biochemistry 44 27 9462-71 Omega-gliadin 10444084 Triticum aestivum (Wheat) 280 MKTFLIFVLLAMAMKIATAARELNPSNKELQSPQQSFSYQQQPFPQQPYPQQPYPSQQPYPSQQPFPTPQQQFPEQSQQPFTQPQQPTPIQPQQPFPQQPQQPQQPFPQPQQPFPWQPQQPFPQTQQSFPLQPQQPFPQQPQQPFPQPQLPFPQQSEQIIPQQLQQPFPLQPQQPFPQQPQQPFPQPQQPIPVQPQQSFPQQSQQSQQPFAQPQQLFPELQQPIPQQPQQPFPLQPQQPFPQQPQQPFPQQPQQSFPQQPQQPYPQQQPYGSSLTSIGGQ Disordered 1 280 MKTFLIFVLLAMAMKIATAARELNPSNKELQSPQQSFSYQQQPFPQQPYPQQPYPSQQPYPSQQPFPTPQQQFPEQSQQPFTQPQQPTPIQPQQPFPQQPQQPQQPFPQPQQPFPWQPQQPFPQTQQSFPLQPQQPFPQQPQQPFPQPQLPFPQQSEQIIPQQLQQPFPLQPQQPFPQQPQQPFPQPQQPIPVQPQQSFPQQSQQSQQPFAQPQQLFPELQQPIPQQPQQPFPLQPQQPFPQQPQQPFPQQPQQSFPQQPQQPYPQQQPYGSSLTSIGGQ Native Relationship to function unknown Unknown Unknown Raman optical activity Paper 12741823 Blanch EW, Kasarda DD, Hecht L, Nielsen K, Barron LD 2003 Biochemistry 42 19 5665-73 Voltage-dependent L-type calcium channel alpha-1S subunit Calcium channel, L type, alpha-1 polypeptide, isoform 3, skeletal muscle Voltage-gated calcium channel alpha subunit Cav1.1 P07293 P07293 Oryctolagus cuniculus (Rabbit) 1873 MEPSSPQDEGLRKKQPKKPLPEVLPRPPRALFCLTLQNPLRKACISIVEWKPFETIILLTIFANCVALAVYLPMPEDDNNSLNLGLEKLEYFFLTVFSIEAAMKIIAYGFLFHQDAYLRSGWNVLDFIIVFLGVFTAILEQVNVIQSNTAPMSSKGAGLDVKALRAFRVLRPLRLVSGVPSLQVVLNSIFKAMLPLFHIALLVLFMVIIYAIIGLELFKGKMHKTCYYIGTDIVATVENEKPSPCARTGSGRPCTINGSECRGGWPGPNHGITHFDNFGFSMLTVYQCITMEGWTDVLYWVNDAIGNEWPWIYFVTLILLGSFFILNLVLGVLSGEFTKEREKAKSRGTFQKLREKQQLEEDLRGYMSWITQGEVMDVEDLREGKLSLEEGGSDTESLYEIEGLNKIIQFIRHWRQWNRVFRWKCHDLVKSRVFYWLVILIVALNTLSIASEHHNQPLWLTHLQDIANRVLLSLFTIEMLLKMYGLGLRQYFMSIFNRFDCFVVCSGILELLLVESGAMTPLGISVLRCIRLLRLFKITKYWTSLSNLVASLLNSIRSIASLLLLLFLFIIIFALLGMQLFGGRYDFEDTEVRRSNFDNFPQALISVFQVLTGEDWNSVMYNGIMAYGGPSYPGVLVCIYFIILFVCGNYILLNVFLAIAVDNLAEAESLTSAQKAKAEERKRRKMSRGLPDKTEEEKSVMAKKLEQKPKGEGIPTTAKLKVDEFESNVNEVKDPYPSADFPGDDEEDEPEIPVSPRPRPLAELQLKEKAVPIPEASSFFIFSPTNKVRVLCHRIVNATWFTNFILLFILLSSAALAAEDPIRAESVRNQILGYFDIAFTSVFTVEIVLKMTTYGAFLHKGSFCRNYFNILDLLVVAVSLISMGLESSTISVVKILRVLRVLRPLRAINRAKGLKHVVQCVFVAIRTIGNIVLVTTLLQFMFACIGVQLFKGKFFSCNDLSKMTEEECRGYYYVYKDGDPTQMELRPRQWIHNDFHFDNVLSAMMSLFTVSTFEGWPQLLYRAIDSNEEDMGPVYNNRVEMAIFFIIYIILIAFFMMNIFVGFVIVTFQEQGETEYKNCELDKNQRQCVQYALKARPLRCYIPKNPYQYQVWYVVTSSYFEYLMFALIMLNTICLGMQHYHQSEEMNHISDILNVAFTIIFTLEMILKLLAFKARGYFGDPWNVFDFLIVIGSIIDVILSEIDTFLASSGGLYCLGGGCGNVDPDESARISSAFFRLFRVMRLIKLLSRAEGVRTLLWTFIKSFQALPYVALLIVMLFFIYAVIGMQMFGKIALVDGTQINRNNNFQTFPQAVLLLFRCATGEAWQEILLACSYGKLCDPESDYAPGEEYTCGTNFAYYYFISFYMLCAFLIINLFVAVIMDNFDYLTRDWSILGPHHLDEFKAIWAEYDPEAKGRIKHLDVVTLLRRIQPPLGFGKFCPHRVACKRLVGMNMPLNSDGTVTFNATLFALVRTALKIKTEGNFEQANEELRAIIKKIWKRTSMKLLDQVIPPIGDDEVTVGKFYATFLIQEHFRKFMKRQEEYYGYRPKKDTVQIQAGLRTIEEEAAPEIRRTISGDLTAEEELERAMVEAAMEERIFRRTGGLFGQVDTFLERTNSLPPVMANQRPLQFAEIEMEELESPVFLEDFPQDARTNPLARANTNNANANVAYGNSNHSNNQMFSSVHCEREFPGEAETPAAGRGALSHSHRALGPHSKPCAGKLNGQLVQPGMPINQAPPAPCQQPSTDPPERGQRRTSLTGSLQDEAPQRRSSEGSTPRRPAPATALLIQEALVRGGLDTLAADAGFVTATSQALADACQMEPEEVEVAATELLKARESVQGMASVPGSLSRRSSLGSLDQVQGSQETLIPPRP Disordered peptide C 724 760 EFESNVNEVKDPYPSADFPGDDEEDEPEIPVSPRPRP Fragment Native Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Far-UV circular dichroism (CD) Nuclear magnetic resonance (NMR) Analytical ultracentrifugation Paper 12620094 Haarmann CS, Green D, Casarotto MG, Laver DR, Dulhunty AF 2003 Biochem J 372 Pt 2 305-16 Peptide C is sufficient to activate the ryanodine receptor at physiological concentrations. Structure determination experiments were conducted on isolated peptide C. Lupus La protein La autoantigen La ribonucleoprotein Sjogren syndrome type B antigen SS-B P05455 Homo sapiens (Human) 408 MAENGDNEKMAALEAKICHQIEYYFGDFNLPRDKFLKEQIKLDEGWVPLEIMIKFNRLNRLTTDFNVIVEALSKSKAELMEISEDKTKIRRSPSKPLPEVTDEYKNDVKNRSVYIKGFPTDATLDDIKEWLEDKGQVLNIQMRRTLHKAFKGSIFVVFDSIESAKKFVETPGQKYKETDLLILFKDDYFAKKNEERKQNKVEAKLRAKQEQEAKQKLEEDAEMKSLEEKIGCLLKFSGDLDDQTCREDLHILFSNHGEIKWIDFVRGAKEGIILFKEKAKEALGKAKDANNGNLQLRNKEVTWEVLEGEVEKEALKKIIEDQQESLNKWKSKGRRFKGKGKGNKAAQPGSGKGKVQFQGKKTKFASDDEHDEHDENGATGPVKRAREETDKEEPASKQQKTENGAGDQ Disordered 326 408 LNKWKSKGRRFKGKGKGNKAAQPGSGKGKVQFQGKKTKFASDDEHDEHDENGATGPVKRAREETDKEEPASKQQKTENGAGDQ Fragment Native Relationship to function unknown Unknown Unknown Analytical ultracentrifugation Nuclear magnetic resonance (NMR) Paper 12842046 Jacks A, Babon J, Kelly G, Manolaridis I, Cary PD, Curry S, Conte MR 2003 Structure (Camb) 11 7 833-43 Growth factor receptor-bound protein 14 Q14449 Homo sapiens (Human) 540 MTTSLQDGQSAASRAAARDSPLAAQVCGAAQGRGDAHDLAPAPWLHARALLPLPDGTRGCAADRRKKKDLDVPEMPSIPNPFPELCCSPITSVLSADLFPKANSRKKQVIKVYSEDETSRALDVPSDITARDVCQLLILKNHYIDDHSWTLFEHLPHIGVERTIEDHELVIEVLSNWGIEEENKLYFRKNYAKYEFFKNPMYFFPEHMVSFATETNGEISPTQILQMFLSSSTYPEIHGFLHAKEQGKKSWKKIYFFLRRSGLYFSTKGTSKEPRHLQFFSEFGNSDIYVSLAGKKKHGAPTNYGFCFKPNKAGGPRDLKMLCAEEEQSRTCWVTAIRLLKYGMQLYQNYMHPYQGRSGCSSQSISPMRSISENSLVAMDFSGQKSRVIENPTEALSVAVEEGLAWRKKGCLRLGTHGSPTASSQSSATNMAIHRSQPWFHHKISRDEAQRLIIQQGLVDGVFLVRDSQSNPKTFVLSMSHGQKIKHFQIIPVEDDGEMFHTLDDGHTRFTDLIQLVEFYQLNKGVLPCKLKHYCARIAL Disordered 361 435 SSQSISPMRSISENSLVAMDFSGQKSRVIENPTEALSVAVEEGLAWRKKGCLRLGTHGSPTASSQSSATNMAIHR Fragment Native Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) Thermal stability Paper 14623073 Moncoq K, Broutin I, Larue V, Perdereau D, Cailliau K, Browaeys-Poly E, Burnol AF, Ducruix A 2003 FEBS Lett 554 3 240-6 POU domain, class 2, transcription factor 1 NF-A1 Oct-1 Octamer-binding transcription factor 1 OTF-1 P14859 Homo sapiens (Human) 743 MNNPSETSKPSMESGDGNTGTQTNGLDFQKQPVPVGGAISTAQAQAFLGHLHQVQLAGTSLQAAAQSLNVQSKSNEESGDSQQPSQPSQQPSVQAAIPQTQLMLAGGQITGLTLTPAQQQLLLQQAQAQAQLLAAAVQQHSASQQHSAAGATISASAATPMTQIPLSQPIQIAQDLQQLQQLQQQNLNLQQFVLVHPTTNLQPAQFIISQTPQGQQGLLQAQNLLTQLPQQSQANLLQSQPSITLTSQPATPTRTIAATPIQTLPQSQSTPKRIDTPSLEEPSDLEELEQFAKTFKQRRIKLGFTQGDVGLAMGKLYGNDFSQTTISRFEALNLSFKNMCKLKPLLEKWLNDAENLSSDSSLSSPSALNSPGIEGLSRRRKKRTSIETNIRVALEKSFLENQKPTSEEITMIADQLNMEKEVIRVWFCNRRQKEKRINPPSSGGTSSSPIKAIFPSPTSLVATTPSLVTSSAATTLTVSPVLPLTSAAVTNLSVTGTSDTTSNNTATVISTAPPASSAVTSPSLSPSPSASASTSEASSASETSTTQTTSTPLSSPLGTSQVMVTASGLQTAAAAALQGAAQLPANASLAAMAAAAGLNPSLMAPSQFAAGGALLSLNPGTLSGALSPALMSNSTLATIQALASGGSLPITSLDATGNLVFANAGGAPNIVTAPLFLNPQNLSLLTSNPVSLVSAAAASAGNSAPVASLHATSTSAESIQNSLFTVASASGAASTTTTASKAQ Disordered activation domain 1 200 MNNPSETSKPSMESGDGNTGTQTNGLDFQKQPVPVGGAISTAQAQAFLGHLHQVQLAGTSLQAAAQSLNVQSKSNEESGDSQQPSQPSQQPSVQAAIPQTQLMLAGGQITGLTLTPAQQQLLLQQAQAQAQLLAAAVQQHSASQQHSAAGATISASAATPMTQIPLSQPIQIAQDLQQLQQLQQQNLNLQQFVLVHPTTN Fragment Monomeric Native Function arises from the disordered state Molecular recognition effectors Protein-protein binding Small-angle X-ray scattering Nuclear magnetic resonance (NMR) Far-UV circular dichroism (CD) Intrinsic fluorescence Paper 11380252 Lee L, Stollar E, Chang J, Grossmann JG, O'Brien R, Ladbury J, Carpenter B, Roberts S, Luisi B 2001 Biochemistry 40 22 6580-8 Disordered activation domain 1 200 MNNPSETSKPSMESGDGNTGTQTNGLDFQKQPVPVGGAISTAQAQAFLGHLHQVQLAGTSLQAAAQSLNVQSKSNEESGDSQQPSQPSQQPSVQAAIPQTQLMLAGGQITGLTLTPAQQQLLLQQAQAQAQLLAAAVQQHSASQQHSAAGATISASAATPMTQIPLSQPIQIAQDLQQLQQLQQQNLNLQQFVLVHPTTN Complex Fragment Native Function arises from the disordered state Molecular recognition effectors Protein-protein binding Far-UV circular dichroism (CD) Paper 11380252 Lee L, Stollar E, Chang J, Grossmann JG, O'Brien R, Ladbury J, Carpenter B, Roberts S, Luisi B 2001 Biochemistry 40 22 6580-8 There was no increase in structure when a fragment of Oct-1 containing the activation domain was incubated with the binding partner, Bob-1. Disordered 355 378 NLSSDSSLSSPSALNSPGIEGLSR X-ray crystallography Paper 8156594 Klemm JD, Rould MA, Aurora R, Herr W, Pabo CO 1994 Cell 77 1 21-32 Disordered 355 359 NLSSD Fragment Native Function arises from the disordered state Entropic chain Flexible linkers/spacers Nuclear magnetic resonance (NMR) Paper 8479524 Dekker N, Cox M, Boelens R, Verrijzer CP, van der Vliet PC, Kaptein R 1993 Nature 362 6423 852-5 Protein phosphatase inhibitor 2 IPP-2 P11845 1170582 Oryctolagus cuniculus (Rabbit) 205 MAASTASHRPIKGILKNKTSSTSSRVASAEQPRGSVDEELSKKSQKWDEMNILATYHPADKDYGLMKIDEPSTPYHSMIGDDDDAYSDTETTEAMTPDTLAKKLAAAEGSEPKYRIREQESSGEEDSDLSPEEREKKRQFEMKRKLHYNEGLNIKLARQLISKDLHDDEEDEEMSETADGESMNTEESNQGSTPSDQRQNKSQSS Disordered 1 205 MAASTASHRPIKGILKNKTSSTSSRVASAEQPRGSVDEELSKKSQKWDEMNILATYHPADKDYGLMKIDEPSTPYHSMIGDDDDAYSDTETTEAMTPDTLAKKLAAAEGSEPKYRIREQESSGEEDSDLSPEEREKKRQFEMKRKLHYNEGLNIKLARQLISKDLHDDEEDEEMSETADGESMNTEESNQGSTPSDQRQNKSQSS Monomeric Native Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Analytical ultracentrifugation Gel filtration/size exclusion chromatography Thermal stability Aberrant mobility on SDS-PAGE gel Insensitivity to pH extremes Paper 6245879 Foulkes JG, Cohen P 1980 Eur J Biochem 105 1 195-203 10807923 Yang J, Hurley TD, DePaoli-Roach AA 2000 J Biol Chem 275 30 22635-44 Fibrinogen alpha/alpha-E chain P14448 Gallus gallus (Chicken) 741 MIPVTILCVLLCLNLAWAQDGKTTFEKEGGGGRGPRILENMHESSCKYEKNWPICVDDDWGTKCPSCCRMQGIIDDTDQNYSQRIDNIRQQLADSQNKYKTSNRVIVETINILKPGLEGAQQLDENYGHVSTELRRRIVTLKQRVATQVNRIKALQNSIQEQVVEMKRLEVDIDIKIRACKGSCARSFDYQVDKEGYDNIQKHLTQASSIDMHPDFQTTTLSTLKMRPLKDSNVPEHFKLKPSPEMQAMSAFNNIKQMQVVLERPETDHVAEARGDSSPSHTGKLITSSHRRESPSLVDKTSSASSVHRCTRTVTKKVISGPDGPREEIVEKMVSSDGSDCSHLQGGREGSTYHFSGTGDFHKLDRLLPDLESFFTHDSVSTSSRHSIGSSTSSHVTGAGSSHLGTGGKDKFTDLGEEEEDDFGGLQPSGFAAGSASHSKTVLTSSSSSFNKGGSTFETKSLKTRETSEQLGGVQHDQSAEDTPDFKARSFRPAAMSTRRSYNGKDCDDIRQKHTSGAKSGIFKIKPEGSNKVLSVYCDQETTLGGWLLIQQRMDGSVNFNRTWQDYRRGFGSVDGKGQGELWLGNENIHLLTQNDTLLRVELEDWDGNAAYAEYIVQVGTEAEGYALTVSSYEGTAGDALVAGWLEEGSEYTSHAQMQFSTFDRDQDHWEESCAEVYGGGWWYNSCQAANLNGIYYPGGHYDPRYNVPYEIENGVVWIPFRASDYSLKVVRMKIRPLETL Disordered 19 44 QDGKTTFEKEGGGGRGPRILENMHES Fragment Native 1M1JA X-ray crystallography Paper 11601975 Yang Z, Kollman JM, Pandi L, Doolittle RF 2001 Biochemistry 40 42 12515-23 Disordered 237 509 HFKLKPSPEMQAMSAFNNIKQMQVVLERPETDHVAEARGDSSPSHTGKLITSSHRRESPSLVDKTSSASSVHRCTRTVTKKVISGPDGPREEIVEKMVSSDGSDCSHLQGGREGSTYHFSGTGDFHKLDRLLPDLESFFTHDSVSTSSRHSIGSSTSSHVTGAGSSHLGTGGKDKFTDLGEEEEDDFGGLQPSGFAAGSASHSKTVLTSSSSSFNKGGSTFETKSLKTRETSEQLGGVQHDQSAEDTPDFKARSFRPAAMSTRRSYNGKDCDD Fragment Native 1M1JA Paper 11601975 Yang Z, Kollman JM, Pandi L, Doolittle RF 2001 Biochemistry 40 42 12515-23 Fibrinogen beta chain [Fragment] Q02020 Gallus gallus (Chicken) 463 ASVEYDNEEDSPQIDARAHRPLDKRQEAAPTLRPVAPPISGTGYQPRPPKQDKQAMKKGPIIYPDAGGCKHPLDELGVLCPTGCELQTTLLKQEKTVKPVLRDLKDRVAKFSDTSTTMYQYVNMIDNKLVKTQKQRKDNDIILSEYNTEMELHYNYIKDNLDNNIPSSLRVLRAVIDSLHKKIQKLENAIATQTDYCRSPCVASCNIPVVSGRECEDIYRKGGETSEMYIIQPDPFTTPYRVYCDMETDNGGWTLIQNRQDGSVNFGRAWDEYKRGFGNIAKSGGKKYCDTPGEYWLGNDKISQLTKIGPTKVLIEMEDWNGDKVSALYGGFTIHNEGNKYQLSVSNYKGNAGNALMEGASQLYGENRTMTIHNGMYFSTYDRDNDGWLTTDPRKQCSKEDGGGWWYNRCHAANPNGRYYWGGTYSWDMAKHGTDDGIVWMNWKGSWYSMKKMSMKIKPYFPD Disordered 1 62 ASVEYDNEEDSPQIDARAHRPLDKRQEAAPTLRPVAPPISGTGYQPRPPKQDKQAMKKGPII Fragment Native 1M1JB X-ray crystallography Paper 11601975 Yang Z, Kollman JM, Pandi L, Doolittle RF 2001 Biochemistry 40 42 12515-23 Fibrinogen gamma chain 45384500 Gallus gallus (Chicken) 435 MMGVKSVTSRLAVGDLLSLLFSTSMAYIATRENCCILDERFGSYCPTTCGIADFFNKYRLTTDGELLEIEGLLQQATNSTGSIEYLIQHIKTIYPSEKQTLPQSIEQLTQKSKKIIEEIIRYENTILAHENTIQQLTDMHIMNSNKITQLKQKIAQLESHCQEPCKDTAEIQETTGRDCQDIANKGARKSGLYFIKPQKAKQSFLVYCEIDTYGNGWTVLQRRLDGSEDFRRNWVQYKEGFGHLSPDDTTEFWLGNEKIHLITTQSTLPYALRIELEDWSGKKGTADYAVFKVGTEEDKYRLTYAYFIGGERGDAFDGFNFGDDPSDKSYTYHNGMRFSTFDNDNDNFEGNCAEQDGSGWWMNRCHAGHLNGPYYIGGVYSRDTGTNSYDNGIIWATWRDRWYSMKKTTMKIIPFNRLSIDGQQHSGGLKQVGDS Disordered 27 29 YIA Fragment Native 1M1JC X-ray crystallography Paper 11601975 Yang Z, Kollman JM, Pandi L, Doolittle RF 2001 Biochemistry 40 42 12515-23 Disordered 420 435 IDGQQHSGGLKQVGDS Fragment Native 1M1JC X-ray crystallography Paper 11601975 Yang Z, Kollman JM, Pandi L, Doolittle RF 2001 Biochemistry 40 42 12515-23 Myelin basic protein MBP Myelin A1 protein Myelin membrane encephalitogenic protein P02686 Homo sapiens 304 MGNHAGKRELNAEKASTNSETNRGESEKKRNLGELSRTTSEDNEVFGEADANQNNGTSSQDTAVTDSKRTADPKNAWQDAHPADPGSRPHLIRLFSRDAPGREDNTFKDRPSESDELQTIQEDSAATSESLDVMASQKRPSQRHGSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFGGDRGAPKRGSGKDSHHPARTAHYGSLPQKSHGRTQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQRPGFGYGGRASDYKSAHKGFKGVDAQGTLSKIFKLGGRDSRSGSPMARR Disordered 134 304 MASQKRPSQRHGSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFGGDRGAPKRGSGKDSHHPARTAHYGSLPQKSHGRTQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQRPGFGYGGRASDYKSAHKGFKGVDAQGTLSKIFKLGGRDSRSGSPMARR Isoform Mutant Relationship to function unknown Molecular assembly Protein-protein binding Far-UV circular dichroism (CD) 294 7.2 Tris buffer 0.3 Paper 7500383 Deibler GE, Burlin TV, Stone AL 1995 J Neurosci Res 41 6 819-27 The experimental sequence was the 18.5 kDa isoform and therefore did not include residues 1 - 133 of the sequence listed in SwissProt. Myelin basic protein MBP Myelin A1 protein P04370 Mus musculus (Mouse) 169 MASQKRPSQRSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFSGDRGAPKRGSGKDSHTRTTHYGSLPQKSQHGRTQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQKPGFGYGGRASDYKSAHKGFKGAYDAQGTLSKIFKLGGRDSRSGSPMARR Disordered 1 169 MASQKRPSQRSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFSGDRGAPKRGSGKDSHTRTTHYGSLPQKSQHGRTQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQKPGFGYGGRASDYKSAHKGFKGAYDAQGTLSKIFKLGGRDSRSGSPMARR Engineered Isoform Mutant Relationship to function unknown Molecular assembly Protein-protein binding Far-UV circular dichroism (CD) Paper 12372316 Hill CM, Bates IR, White GF, Hallett FR, Harauz G 2002 J Struct Biol 139 1 13-26 The experimental sequence was the 18.5 kDa isoform. The experimental sequence had a C-terminal hexahistidine tagged. Breast cancer type 1 susceptibility protein BRCA1 RING finger protein 53 P38398 Homo sapiens 1863 MDLSALRVEEVQNVINAMQKILECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCKNDITKRSLQESTRFSQLVEELLKIICAFQLDTGLEYANSYNFAKKENNSPEHLKDEVSIIQSMGYRNRAKRLLQSEPENPSLQETSLSVQLSNLGTVRTLRTKQRIQPQKTSVYIELGSDSSEDTVNKATYCSVGDQELLQITPQGTRDEISLDSAKKAACEFSETDVTNTEHHQPSNNDLNTTEKRAAERHPEKYQGSSVSNLHVEPCGTNTHASSLQHENSSLLLTKDRMNVEKAEFCNKSKQPGLARSQHNRWAGSKETCNDRRTPSTEKKVDLNADPLCERKEWNKQKLPCSENPRDTEDVPWITLNSSIQKVNEWFSRSDELLGSDDSHDGESESNAKVADVLDVLNEVDEYSGSSEKIDLLASDPHEALICKSERVHSKSVESNIEDKIFGKTYRKKASLPNLSHVTENLIIGAFVTEPQIIQERPLTNKLKRKRRPTSGLHPEDFIKKADLAVQKTPEMINQGTNQTEQNGQVMNITNSGHENKTKGDSIQNEKNPNPIESLEKESAFKTKAEPISSSISNMELELNIHNSKAPKKNRLRRKSSTRHIHALELVVSRNLSPPNCTELQIDSCSSSEEIKKKKYNQMPVRHSRNLQLMEGKEPATGAKKSNKPNEQTSKRHDSDTFPELKLTNAPGSFTKCSNTSELKEFVNPSLPREEKEEKLETVKVSNNAEDPKDLMLSGERVLQTERSVESSSISLVPGTDYGTQESISLLEVSTLGKAKTEPNKCVSQCAAFENPKGLIHGCSKDNRNDTEGFKYPLGHEVNHSRETSIEMEESELDAQYLQNTFKVSKRQSFAPFSNPGNAEEECATFSAHSGSLKKQSPKVTFECEQKEENQGKNESNIKPVQTVNITAGFPVVGQKDKPVDNAKCSIKGGSRFCLSSQFRGNETGLITPNKHGLLQNPYRIPPLFPIKSFVKTKCKKNLLEENFEEHSMSPEREMGNENIPSTVSTISRNNIRENVFKEASSSNINEVGSSTNEVGSSINEIGSSDENIQAELGRNRGPKLNAMLRLGVLQPEVYKQSLPGSNCKHPEIKKQEYEEVVQTVNTDFSPYLISDNLEQPMGSSHASQVCSETPDDLLDDGEIKEDTSFAENDIKESSAVFSKSVQKGELSRSPSPFTHTHLAQGYRRGAKKLESSEENLSSEDEELPCFQHLLFGKVNNIPSQSTRHSTVATECLSKNTEENLLSLKNSLNDCSNQVILAKASQEHHLSEETKCSASLFSSQCSELEDLTANTNTQDPFLIGSSKQMRHQSESQGVGLSDKELVSDDEERGTGLEENNQEEQSMDSNLGEAASGCESETSVSEDCSGLSSQSDILTTQQRDTMQHNLIKLQQEMAELEAVLEQHGSQPSNSYPSIISDSSALEDLRNPEQSTSEKAVLTSQKSSEYPISQNPEGLSADKFEVSADSSTSKNKEPGVERSSPSKCPSLDDRWYMHSCSGSLQNRNYPSQEELIKVVDVEEQQLEESGPHDLTETSYLPRQDLEGTPYLESGISLFSDDPESDPSEDRAPESARVGNIPSSTSALKVPQLKVAESAQSPAAAHTTDTAGYNAMEESVSREKPELTASTERVNKRMSMVVSGLTPEEFMLVYKFARKHHITLTNLITEETTHVVMKTDAEFVCERTLKYFLGIAGGKWVVSYFWVTQSIKERKMLNEHDFEVRGDVVNGRNHQGPKRARESQDRKIFRGLEICCYGPFTNMPTDQLEWMVQLCGASVVKELSSFTLGTGVHPIVVVQPDAWTEDNGFHAIGQMCEAPVVTREWVLDSVALYQCQELDTYLIPQIPHSHY Disordered 170 1649 RIQPQKTSVYIELGSDSSEDTVNKATYCSVGDQELLQITPQGTRDEISLDSAKKAACEFSETDVTNTEHHQPSNNDLNTTEKRAAERHPEKYQGSSVSNLHVEPCGTNTHASSLQHENSSLLLTKDRMNVEKAEFCNKSKQPGLARSQHNRWAGSKETCNDRRTPSTEKKVDLNADPLCERKEWNKQKLPCSENPRDTEDVPWITLNSSIQKVNEWFSRSDELLGSDDSHDGESESNAKVADVLDVLNEVDEYSGSSEKIDLLASDPHEALICKSERVHSKSVESNIEDKIFGKTYRKKASLPNLSHVTENLIIGAFVTEPQIIQERPLTNKLKRKRRPTSGLHPEDFIKKADLAVQKTPEMINQGTNQTEQNGQVMNITNSGHENKTKGDSIQNEKNPNPIESLEKESAFKTKAEPISSSISNMELELNIHNSKAPKKNRLRRKSSTRHIHALELVVSRNLSPPNCTELQIDSCSSSEEIKKKKYNQMPVRHSRNLQLMEGKEPATGAKKSNKPNEQTSKRHDSDTFPELKLTNAPGSFTKCSNTSELKEFVNPSLPREEKEEKLETVKVSNNAEDPKDLMLSGERVLQTERSVESSSISLVPGTDYGTQESISLLEVSTLGKAKTEPNKCVSQCAAFENPKGLIHGCSKDNRNDTEGFKYPLGHEVNHSRETSIEMEESELDAQYLQNTFKVSKRQSFAPFSNPGNAEEECATFSAHSGSLKKQSPKVTFECEQKEENQGKNESNIKPVQTVNITAGFPVVGQKDKPVDNAKCSIKGGSRFCLSSQFRGNETGLITPNKHGLLQNPYRIPPLFPIKSFVKTKCKKNLLEENFEEHSMSPEREMGNENIPSTVSTISRNNIRENVFKEASSSNINEVGSSTNEVGSSINEIGSSDENIQAELGRNRGPKLNAMLRLGVLQPEVYKQSLPGSNCKHPEIKKQEYEEVVQTVNTDFSPYLISDNLEQPMGSSHASQVCSETPDDLLDDGEIKEDTSFAENDIKESSAVFSKSVQKGELSRSPSPFTHTHLAQGYRRGAKKLESSEENLSSEDEELPCFQHLLFGKVNNIPSQSTRHSTVATECLSKNTEENLLSLKNSLNDCSNQVILAKASQEHHLSEETKCSASLFSSQCSELEDLTANTNTQDPFLIGSSKQMRHQSESQGVGLSDKELVSDDEERGTGLEENNQEEQSMDSNLGEAASGCESETSVSEDCSGLSSQSDILTTQQRDTMQHNLIKLQQEMAELEAVLEQHGSQPSNSYPSIISDSSALEDLRNPEQSTSEKAVLTSQKSSEYPISQNPEGLSADKFEVSADSSTSKNKEPGVERSSPSKCPSLDDRWYMHSCSGSLQNRNYPSQEELIKVVDVEEQQLEESGPHDLTETSYLPRQDLEGTPYLESGISLFSDDPESDPSEDRAPESARVGNIPSSTSALKVPQLKVAESAQSPAAAHTTDTAGYNAMEESVSREKPELTASTERVNKR Fragment Native Relationship to function unknown Molecular recognition effectors Protein-protein binding Far-UV circular dichroism (CD) Nuclear magnetic resonance (NMR) Paper 15571721 Mark WY, Liao JC, Lu Y, Ayed A, Laister R, Szymczyna B, Chakrabartty A, Arrowsmith CH 2005 J Mol Biol 345 2 275-87 The structure of the 1480 residue central region was investigated by characterizing 21 different fragments. Disordered 1755 1758 SQDR Nuclear magnetic resonance (NMR) 296 6.8 DTT 10 K2HPO4 10 KCl 5 KH2PO4 10 Paper 15609993 Gaiser OJ, Ball LJ, Schmieder P, Leitner D, Strauss H, Wahl M, Kuhne R, Oschkinat H, Heinemann U 2004 Biochemistry 43 51 15983-95 Disordered 1773 1777 TNMPT Nuclear magnetic resonance (NMR) 296 6.8 DTT 10 K2HPO4 10 KCl 5 KH2PO4 10 Paper 15609993 Gaiser OJ, Ball LJ, Schmieder P, Leitner D, Strauss H, Wahl M, Kuhne R, Oschkinat H, Heinemann U 2004 Biochemistry 43 51 15983-95 Disordered 1799 1804 TLGTGV Nuclear magnetic resonance (NMR) 296 6.8 DTT 10 K2HPO4 10 KCl 5 KH2PO4 10 Paper 15609993 Gaiser OJ, Ball LJ, Schmieder P, Leitner D, Strauss H, Wahl M, Kuhne R, Oschkinat H, Heinemann U 2004 Biochemistry 43 51 15983-95 Disordered 1812 1823 PDAWTEDNGFHA Nuclear magnetic resonance (NMR) 296 6.8 DTT 10 K2HPO4 10 KCl 5 KH2PO4 10 Paper 15609993 Gaiser OJ, Ball LJ, Schmieder P, Leitner D, Strauss H, Wahl M, Kuhne R, Oschkinat H, Heinemann U 2004 Biochemistry 43 51 15983-95 Alpha adducin Erythrocyte adducin alpha subunit P35611 Homo sapiens 737 MNGDSRAAVVTSPPPTTAPHKERYFDRVDENNPEYLRERNMAPDLRQDFNMMEQKKRVSMILQSPAFCEELESMIQEQFKKGKNPTGLLALQQIADFMTTNVPNVYPAAPQGGMAALNMSLGMVTPVNDLRGSDSIAYDKGEKLLRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDRGSTNLGVNQAGFTLHSAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSLGEVAYHDYHGILVDEEEKVLIQKNLGPKSKVLILRNHGLVSVGESVEEAFYYIHNLVVACEIQVRTLASAGGPDNLVLLNPEKYKAKSRSPGSPVGEGTGSPPKWQIGEQEFEALMRMLDNLGYRTGYPYRYPALREKSKKYSDVEVPASVTGYSFASDGDSGTCSPLRHSFQKQQREKTRWLNSGRGDEASEEGQNGSSPKSKTKWTKEDGHRTSTSAVPNLFVPLNTNPKEVQEMRNKIREQNLQDIKTAGPQSQVLCGVVMDRSLVQGELVTASKAIIEKEYQPHVIVSTTGPNPFTTLTDRELEEYRREVERKQKGSEENLDEAREQKEKSPPDQPAVPHPPPSTPIKLEEDLVPEPTTGDDSDAATFKPTLPDLSPDEPSEALGFPMLEKEEEAHRPPSPTEAPTEASPEPAPDPAPVAEEAAPSAVEEGAAADPGSDGSPGKSPSKKKKKFRTPSFLKKSKKKSDS Disordered tail 430 737 CSPLRHSFQKQQREKTRWLNSGRGDEASEEGQNGSSPKSKTKWTKEDGHRTSTSAVPNLFVPLNTNPKEVQEMRNKIREQNLQDIKTAGPQSQVLCGVVMDRSLVQGELVTASKAIIEKEYQPHVIVSTTGPNPFTTLTDRELEEYRREVERKQKGSEENLDEAREQKEKSPPDQPAVPHPPPSTPIKLEEDLVPEPTTGDDSDAATFKPTLPDLSPDEPSEALGFPMLEKEEEAHRPPSPTEAPTEASPEPAPDPAPVAEEAAPSAVEEGAAADPGSDGSPGKSPSKKKKKFRTPSFLKKSKKKSDS Fragment Monomeric Native Relationship to function unknown Molecular assembly Protein-protein binding Far-UV circular dichroism (CD) Aberrant mobility on SDS-PAGE gel Sensitivity to proteolysis Paper 7642559 Hughes CA, Bennett V 1995 J Biol Chem 270 32 18990-6 Beta adducin Erythrocyte adducin beta subunit P35612 Homo sapiens 726 MSEETVPEAASPPPPQGQPYFDRFSEDDPEYMRLRNRAADLRQDFNLMEQKKRVTMILQSPSFREELEGLIQEQMKKGNNSSNIWALRQIADFMASTSHAVFPTSSMNVSMMTPINDLHTADSLNLAKGERLMRCKISSVYRLLDLYGWAQLSDTYVTLRVSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKGSSCFPVDTTGFCLHSAIYAARPDVRCIIHLHTPATAAVSAMKWGLLPVSHNALLVGDMAYYDFNGEMEQEADRINLQKCLGPTCKILVLRNHGVVALGDTVEEAFYKIFHLQAACEIQVSALSSAGGVENLILLEQEKHRPHEVGSVQWAGSTFGPMQKSRLGEHEFEALMRMLDNLGYRTGYTYRHPFVQEKTKHKSEVEIPATVTAFVFEEDGAPVPALRQHAQKQQKEKTRWLNTPNTYLRVNVADEVQRSMGSPRPKTTWMKADEVEKSSSGMPIRIENPNQFVPLYTDPQEVLEMRNKIREQNRQDVKSAGPQSQLLASVIAEKSRSPSTESQLMSKGDEDTKDDSEETVPNPFSQLTDQELEEYKKEVERKKLELDGEKETAPEEPGSPAKSAPASPVQSPAKEAETKSPLVSPSKSLEEGTKKTETSKAATTEPETTQPEGVVVNGREEEQTAEEILSKGLSQMTTSADTDVDTSKDKTESVTSGPMSPEGSPSKSPSKKKKKFRTPSFLKKSKKKEKVES Disordered tail 409 726 FEEDGAPVPALRQHAQKQQKEKTRWLNTPNTYLRVNVADEVQRSMGSPRPKTTWMKADEVEKSSSGMPIRIENPNQFVPLYTDPQEVLEMRNKIREQNRQDVKSAGPQSQLLASVIAEKSRSPSTESQLMSKGDEDTKDDSEETVPNPFSQLTDQELEEYKKEVERKKLELDGEKETAPEEPGSPAKSAPASPVQSPAKEAETKSPLVSPSKSLEEGTKKTETSKAATTEPETTQPEGVVVNGREEEQTAEEILSKGLSQMTTSADTDVDTSKDKTESVTSGPMSPEGSPSKSPSKKKKKFRTPSFLKKSKKKEKVES Fragment Monomeric Native Relationship to function unknown Molecular assembly Protein-protein binding Far-UV circular dichroism (CD) Aberrant mobility on SDS-PAGE gel Sensitivity to proteolysis Paper 7642559 Hughes CA, Bennett V 1995 J Biol Chem 270 32 18990-6 30S ribosomal protein S17 P02373 Escherichia coli 83 TDKIRTLQGRVVSDKMEKSIVVAIERFVKHPIYGKFIKRTTKLHVHDENNECGIGDVVEIRECRPLSKTKSWTLVRVVEKAVL Disordered 1 83 TDKIRTLQGRVVSDKMEKSIVVAIERFVKHPIYGKFIKRTTKLHVHDENNECGIGDVVEIRECRPLSKTKSWTLVRVVEKAVL Monomeric Native Relationship to function unknown Molecular assembly Unknown Far-UV circular dichroism (CD) Paper 6751823 Venyaminov SY, Gogia ZV 1982 Eur J Biochem 126 2 299-309 DNA-repair protein complementing XP-A cells Xeroderma pigmentosum group A complementing protein P23025 P23025 Homo sapiens (Human) 273 MAAADGALPEAAALEQPAELPASVRASIERKRQRALMLRQARLAARPYSATAAAATGGMANVKAAPKIIDTGGGFILEEEEEEEQKIGKVVHQPGPVMEFDYVICEECGKEFMDSYLMNHFDLPTCDNCRDADDKHKLITKTEAKQEYLLKDCDLEKREPPLKFIVKKNPHHSQWGDMKLYLKLQIVKRSLEVWGSQEALEEAKEVRQENREKMKQKKFDKKVKELRRAVRSSVWKRETIVHQHEYGPEENLEDDMYRKTCTMCGHELTYEKM Disordered 158 158 R Fragment 1XPAA Nuclear magnetic resonance (NMR) 303 6.5 Paper 9699634 Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M 1998 Nat Struct Biol 5 8 701-706 10050037 Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M 1999 J Biochem (Tokyo) 125 3 495-506 Disordered 168 179 KNPHHSQWGDMK Fragment 1XPAA Nuclear magnetic resonance (NMR) 303 6.5 Paper 9699634 Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M 1998 Nat Struct Biol 5 8 701-706 10050037 Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M 1999 J Biochem (Tokyo) 125 3 495-506 Disordered 206 219 VRQENREKMKQKKF Fragment 1XPAA Nuclear magnetic resonance (NMR) 303 6.5 Paper 9699634 Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M 1998 Nat Struct Biol 5 8 701-706 10050037 Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M 1999 J Biochem (Tokyo) 125 3 495-506 Ordered 10 157 EAAALEQPAELPASVRASIERKRQRALMLRQARLAARPYSATAAAATGGMANVKAAPKIIDTGGGFILEEEEEEEQKIGKVVHQPGPVMEFDYVICEECGKEFMDSYLMNHFDLPTCDNCRDADDKHKLITKTEAKQEYLLKDCDLEK 1XPAA Nuclear magnetic resonance (NMR) 303 6.5 Paper 9699634 Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M 1998 Nat Struct Biol 5 8 701-706 10050037 Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M 1999 J Biochem (Tokyo) 125 3 495-506 Ordered 159 167 EPPLKFIVK 1XPAA Nuclear magnetic resonance (NMR) 303 6.5 Paper 9699634 Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M 1998 Nat Struct Biol 5 8 701-706 10050037 Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M 1999 J Biochem (Tokyo) 125 3 495-506 Ordered 180 205 LYLKLQIVKRSLEVWGSQEALEEAKE 1XPAA Nuclear magnetic resonance (NMR) 303 6.5 Paper 9699634 Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M 1998 Nat Struct Biol 5 8 701-706 10050037 Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M 1999 J Biochem (Tokyo) 125 3 495-506 Thyroid cancer 1 TC-1 Q9NR00 Hs.283683 Homo sapiens (Human) 106 MKAKRSHQAIIMSTSLRVSPSIHGYHFDTASRKKAVGNIFENTDQESLERLFRNSGDKKAEERAKIIFAIDQDVEEKTRALMALKKRTKDKLFQFLKLRKYSIKVH Disordered 1 106 MKAKRSHQAIIMSTSLRVSPSIHGYHFDTASRKKAVGNIFENTDQESLERLFRNSGDKKAEERAKIIFAIDQDVEEKTRALMALKKRTKDKLFQFLKLRKYSIKVH Far-UV circular dichroism (CD) NaF varying concentrations protein per ml 0.21 sodium acetate 10 Nuclear magnetic resonance (NMR) 6.8 NaCl 150 protein 120 sodium acetate 10 Paper 15087392 Sunde M, McGrath KC, Young L, Matthews JM, Chua EL, Mackay JP, Death AK 2004 Cancer Res 64 8 2766-73 PKA Regulatory Subunit RI alpha P00514 Bos taurus (Bovine) 379 ASGTTASEEERSLRECELYVQKHNIQALLKDSIVQLCTARPERPMAFLREYFEKLEKEEAKQIQNLQKAGSRADSREDEISPPPPNPVVKGRRRRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFDAMFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNEWATSVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGSAAVLQRRSENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCVKLDRPRFERVLGPCSDILKRNIQQYNSFVSLSV Disordered 91 112 GRRRRGAISAEVYTEEDAASYV Complex Function arises via a disorder to order transition X-ray crystallography Paper 15692043 Kim C, Xuong NH, Taylor SS 2005 Science 307 5710 690-6 6487597 Titani K, Sasagawa T, Ericsson LH, Kumar S, Smith SB, Krebs EG, Walsh KA 1984 Biochemistry 23 18 4193-9 Macrophage scavenger receptor types I and II Macrophage acetylated LDL receptor I and II MSR P21758 S08278 Bos taurus (Bovine) 453 MAQWDDFPDQQEDTDSCTESVKFDARSVTALLPPHPKNGPTLQERMKSYKTALITLYLIVFVVLVPIIGIVAAQLLKWETKNCTVGSVNADISPSPEGKGNGSEDEMRFREAVMERMSNMESRIQYLSDNEANLLDAKNFQNFSITTDQRFNDVLFQLNSLLSSIQEHENIIGDISKSLVGLNTTVLDLQFSIETLNGRVQENAFKQQEEMRKLEERIYNASAEIKSLDEKQVYLEQEIKGEMKLLNNITNDLRLKDWEHSQTLKNITLLQGPPGPPGEKGDRGPPGQNGIPGFPGLIGTPGLKGDRGISGLPGVRGFPGPMGKTGKPGLNGQKGQKGEKGSGSMQRQSNTVRLVGGSGPHEGRVEIFHEGQWGTVCDDRWELRGGLVVCRSLGYKGVQSVHKRAYFGKGTGPIWLNEVFCFGKESSIEECRIRQWGVRACSHDEDAGVTCTT Disordered cytoplasmic domain 1 50 MAQWDDFPDQQEDTDSCTESVKFDARSVTALLPPHPKNGPTLQERMKSYK Engineered Fragment Protein-protein binding Far-UV circular dichroism (CD) 7 peptide monomer or trimer (10 or 25 uM) sodium phosphate 0.1 Paper 11785981 Nakamura T, Hinagata J, Tanaka T, Imanishi T, Wada Y, Kodama T, Doi T 2002 Biochem Biophys Res Commun 290 2 858-64 The experimental sequence consisted of the first 50 residues of bovine MSR with a C17A substitution and a GC appended to the C-terminus. The C17A substitution has been shown to have no affect on the cell surface expression and endocytosis of MSR. Probable two-component system transcriptional regulator gene product of Rv1626 O06143 H70558 Mycobacterium tuberculosis 205 MTGPTTDADAAVPRRVLIAEDEALIRMDLAEMLREEGYEIVGEAGDGQEAVELAELHKPDLVIMDVKMPRRDGIDAASEIASKRIAPIVVLTAFSQRDLVERARDAGAMAYLVKPFSISDLIPAIELAVSRFREITALEGEVATLSERLETRKLVERAKGLLQTKHGMTEPDAFKWIQRAAMDRRTTMKRVAEVVLETLGTPKDT Disordered 21 21 D Engineered Monomeric X-ray crystallography PEG 1.5K 14-18% Paper 15341725 Morth JP, Feng V, Perry LJ, Svergun DI, Tucker PA 2004 Structure (Camb) 12 9 1595-605 Disordered 68 73 MPRRDG Engineered Monomeric X-ray crystallography PEG 1.5K 14-18% Paper 15341725 Morth JP, Feng V, Perry LJ, Svergun DI, Tucker PA 2004 Structure (Camb) 12 9 1595-605 Disordered 103 107 ARDAG Monomeric Native X-ray crystallography BaCl2 10 PEG 1.5K 15 sodium iodide soak 0.5 Paper 15341725 Morth JP, Feng V, Perry LJ, Svergun DI, Tucker PA 2004 Structure (Camb) 12 9 1595-605 Acylamino-acid-releasing enzyme AARE Acylaminoacyl-peptidase Acyl-peptide hydrolase APH EC 3.4.19.1 Q9YBQ2 Aeropyrum pernix K1 582 MRIIMPVEFSRIVRDVERLIAVEKYSLQGVVDGDKLLVVGFSEGSVNAYLYDGGETVKLNREPINSVLDPHYGVGRVILVRDVSKGAEQHALFKVNTSRPGEEQRLEAVKPMRILSGVDTGEAVVFTGATEDRVALYALDGGGLRELARLPGFGFVSDIRGDLIAGLGFFGGGRVSLFTSNLSSGGLRVFDSGEGSFSSASISPGMKVTAGLETAREARLVTVDPRDGSVEDLELPSKDFSSYRPTAITWLGYLPDGRLAVVARREGRSAVFIDGERVEAPQGNHGRVVLWRGKLVTSHTSLSTPPRIVSLPSGEPLLEGGLPEDLRRSIAGSRLVWVESFDGSRVPTYVLESGRAPTPGPTVVLVHGGPFAEDSDSWDTFAASLAAAGFHVVMPNYRGSTGYGEEWRLKIIGDPCGGELEDVSAAARWARESGLASELYIMGYSYGGYMTLCALTMKPGLFKAGVAGASVVDWEEMYELSDAAFRNFIEQLTGGSREIMRSRSPINHVDRIKEPLALIHPQNDSRTPLKPLLRLMGELLARGKTFEAHIIPDAGHAINTMEDAVKILLPAVFFLATQRERR Disordered 1 7 MRIIMPV 1VE6A X-ray crystallography 291 4.6 DTT per l 15 EDTA per l 0.2 NaAC per l 50 PEG4000 6 Paper 15296741 Bartlam M, Wang G, Yang H, Gao R, Zhao X, Xie G, Cao S, Feng Y, Rao Z 2004 Structure (Camb) 12 8 1481-8 Disordered 582 582 R 1VE6A 1VE7A X-ray crystallography 291 4.6 DTT per l 15 EDTA per l 0.2 NaAC per l 50 PEG4000 6 Paper 15296741 Bartlam M, Wang G, Yang H, Gao R, Zhao X, Xie G, Cao S, Feng Y, Rao Z 2004 Structure (Camb) 12 8 1481-8 Disordered 1 8 MRIIMPVE Complex 1VE7A X-ray crystallography 291 4.6 DTT per l 15 EDTA per l 0.2 NaAC per l 50 PEG4000 6 Paper 15296741 Bartlam M, Wang G, Yang H, Gao R, Zhao X, Xie G, Cao S, Feng Y, Rao Z 2004 Structure (Camb) 12 8 1481-8 This region is disordered when in a complex with p-nitrophenyl phosphate (pNP). Troponin C, slow skeletal and cardiac muscles TN-C P63315 Bos taurus (Bovine) 161 MDDIYKAAVEQLTEEQKNEFKAAFDIFVLGAEDGCISTKELGKVMRMLGQNPTPEELQEMIDEVDEDGSGTVDFDEFLVMMVRCMKDDSKGKSEEELSDLFRMFDKNADGYIDLEELKIMLQATGETITEDDIEELMKDGDKNNDGRIDYDEFLEFMKGVE Disordered 103 158 MFDKNADGYIDLEELKIMLQATGETITEDDIEELMKDGDKNNDGRIDYDEFLEFMK Function arises via a disorder to order transition Metal binding Protein-protein binding Far-UV circular dichroism (CD) 298 Near-UV circular dichroism (CD) spectroscopy 298 Paper 2933134 McCubbin WD, Kay CM 1985 Can J Biochem Cell Biol 63 8 812-23 Cholera enterotoxin, A chain [Precursor] Cholera enterotoxin A subunit EC 2.4.2.36 NAD(+)--diphthamide ADP-ribosyltransferase P01555 Vibrio cholerae 258 MVKIIFVFFIFLSSFSYANDDKLYRADSRPPDEIKQSGGLMPRGQSEYFDRGTQMNINLYDHARGTQTGFVRHDDGYVSTSISLRSAHLVGQTILSGHSTYYIYVIATAPNMFNVNDVLGAYSPHPDEQEVSALGGIPYSQIYGWYRVHFGVLDEQLHRNRGYRDRYYSNLDIAPAADGYGLAGFPPEHRAWREEPWIHHAPPGCGNAPRSSMSNTCDEKTQSLGVKFLDEYQSKVKRQIFSGYQSDIDTHNRIKDEL Disordered Activation Loop 44 54 GQSEYFDRGTQ Engineered Fragment Mutant Function arises via a disorder to order transition X-ray crystallography 7 MES pH 6 to 7 100 PEG 2000 monomethylether 14% to 20% protein solution in PBS 1.5 Paper 15049684 O'Neal CJ, Amaya EI, Jobling MG, Holmes RK, Hol WG 2004 Biochemistry 43 13 3772-82 This region is disordered in crystal form 1. Disordered Activation Loop 47 54 EYFDRGTQ Engineered Fragment Mutant Function arises via a disorder to order transition X-ray crystallography D-Galactose 0.5 uL 300 PEG 3350 20 protein in buffer 1.5 sodium citrate 100 Paper 15049684 O'Neal CJ, Amaya EI, Jobling MG, Holmes RK, Hol WG 2004 Biochemistry 43 13 3772-82 This region is disordered in crystal form 2. Disordered Activation Loop 44 54 GQSEYFDRGTQ Engineered Fragment Mutant Function arises via a disorder to order transition X-ray crystallography 7 kemptide solution (250 mM kemptide) 0.5 MES pH 6 to 7 100 PEG 2000 monomethylether 14% to 20% protein solution in PBS 1.5 Paper 15049684 O'Neal CJ, Amaya EI, Jobling MG, Holmes RK, Hol WG 2004 Biochemistry 43 13 3772-82 This region is disordered in crystal form 3. Epsin-1 EPS-15 interacting protein 1 O88339 Rattus norvegicus (Rat) 575 MSTSSLRRQMKNIVHNYSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREERAHALKTKEKLAQTATASSAAVGSGPPPEAEQAWPQSSGEEELQLQLALAMSKEEADQPPSCGPEDDVQLQLALSLSREEHDKEERIRRGDDLRLQMAIEESKRETGGKEESSLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGAPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTSDPWGSADGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGAKASNPFLPSGAPATGPSVTNPFQPAPPATLTLNQLRLSPVPPVPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNPFLL Disordered 144 575 RAHALKTKEKLAQTATASSAAVGSGPPPEAEQAWPQSSGEEELQLQLALAMSKEEADQPPSCGPEDDVQLQLALSLSREEHDKEERIRRGDDLRLQMAIEESKRETGGKEESSLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGAPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTSDPWGSADGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGAKASNPFLPSGAPATGPSVTNPFQPAPPATLTLNQLRLSPVPPVPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNPFLL Fragment Monomeric Function arises from the disordered state Molecular assembly Protein-protein binding Far-UV circular dichroism (CD) Gel filtration/size exclusion chromatography cytosol 500 Analytical ultracentrifugation 293 Paper 11756460 Kalthoff C, Alves J, Urbanke C, Knorr R, Ungewickell EJ 2002 J Biol Chem 277 10 8209-16 Tryptophan synthase alpha chain EC 4.2.1.20 P0A877 Escherichia coli 268 MERYESLFAQLKERKEGAFVPFVTLGDPGIEQSLKIIDTLIEAGADALELGIPFSDPLADGPTIQNATLRAFAAGVTPAQCFEMLALIRQKHPTIPIGLLMYANLVFNKGIDEFYAQCEKVGVDSVLVADVPVEESAPFRQAALRHNVAPIFICPPNADDDLLRQIASYGRGYTYLLSRAGVTGAENRAALPLNHLVAKLKEYNAAPPLQGFGISAPDQVKAAIDAGAAGAISGSAIVKIIEQHINEPEKMLAALKVFVQPMKAATRS Disordered 57 64 PLADGPTI Function arises via an order to disorder transition Molecular assembly Protein-protein binding X-ray crystallography 288 ammonium sulfate 1.8 potassium phosphate buffer (pH 7.0) 5 protein solution (20 mg/mL) 1 sodium cacodylate pH 6.5 0.1 Paper 15667212 Nishio K, Morimoto Y, Ishizuka M, Ogasahara K, Tsukihara T, Yutani K 2005 Biochemistry 44 4 1184-92 These densities were unclear in molecule A only. The region stayed disordered when in a complex with molecule B. Disordered 184 185 GA Relationship to function unknown Unknown Unknown X-ray crystallography 288 ammonium sulfate 1.8 potassium phosphate buffer (pH 7.0) 5 protein solution (20 mg/mL) 1 sodium cacodylate pH 6.5 0.1 Paper 15667212 Nishio K, Morimoto Y, Ishizuka M, Ogasahara K, Tsukihara T, Yutani K 2005 Biochemistry 44 4 1184-92 These densities were unclear in molecules A and B. Disordered 59 63 ADGPT Function arises via an order to disorder transition Molecular assembly Protein-protein binding X-ray crystallography 288 ammonium sulfate 1.8 potassium phosphate buffer (pH 7.0) 5 protein solution (20 mg/mL) 1 sodium cacodylate pH 6.5 0.1 Paper 15667212 Nishio K, Morimoto Y, Ishizuka M, Ogasahara K, Tsukihara T, Yutani K 2005 Biochemistry 44 4 1184-92 These densities are unclear in molecule B only. The region stayed disordered when in complex with molecule A. Myristoylated alanine-rich C-kinase substrate MARCKS P26645 Mus musculus (Mouse) 309 MGAQFSKTAAKGEATAERPGEAAVASSPSKANGQENGHVKVNGDASPAAAEPGAKEELQANGSAPAADKEEPASGSAATPAAAEKDEAAAATEPGAGAADKEAAEAEPAEPSSPAAEAEGASASSTSSPKAEDGAAPSPSSETPKKKKKRFSFKKSFKLSGFSFKKSKKESGEGAEAEGATAEGAKDEAAAAAGGEGAAAPGEQAGGAGAEGAAGGEPREAEAAEPEQPEQPEQPAAEEPQAEEQSEAAGEKAEEPAPGATAGDASSAAGPEQEAPAATDEAAASAAPAASPEPQPECSPEAPPAPTAE Disordered 1 309 MGAQFSKTAAKGEATAERPGEAAVASSPSKANGQENGHVKVNGDASPAAAEPGAKEELQANGSAPAADKEEPASGSAATPAAAEKDEAAAATEPGAGAADKEAAEAEPAEPSSPAAEAEGASASSTSSPKAEDGAAPSPSSETPKKKKKRFSFKKSFKLSGFSFKKSKKESGEGAEAEGATAEGAKDEAAAAAGGEGAAAPGEQAGGAGAEGAAGGEPREAEAAEPEQPEQPEQPAAEEPQAEEQSEAAGEKAEEPAPGATAGDASSAAGPEQEAPAATDEAAASAAPAASPEPQPECSPEAPPAPTAE Function arises from the disordered state Phosphorylation Substrate/ligand binding Far-UV circular dichroism (CD) 298 CaCl2 0.5 NaCl 0.1 protein 1 Tris-HCl buffer (pH 7.5) 20 Paper 9468306 Matsubara M, Yamauchi E, Hayashi N, Taniguchi H 1998 FEBS Lett 421 3 203-7 15640140 Tapp H, Al-Naggar IM, Yarmola EG, Harrison A, Shaw G, Edison AS, Bubb MR 2005 J Biol Chem 280 11 9946-56 Disordered 1 309 MGAQFSKTAAKGEATAERPGEAAVASSPSKANGQENGHVKVNGDASPAAAEPGAKEELQANGSAPAADKEEPASGSAATPAAAEKDEAAAATEPGAGAADKEAAEAEPAEPSSPAAEAEGASASSTSSPKAEDGAAPSPSSETPKKKKKRFSFKKSFKLSGFSFKKSKKESGEGAEAEGATAEGAKDEAAAAAGGEGAAAPGEQAGGAGAEGAAGGEPREAEAAEPEQPEQPEQPAAEEPQAEEQSEAAGEKAEEPAPGATAGDASSAAGPEQEAPAATDEAAASAAPAASPEPQPECSPEAPPAPTAE Complex Function arises from the disordered state Phosphorylation Substrate/ligand binding Far-UV circular dichroism (CD) 298 CaCl2 0.5 calmodulin 1 NaCl 0.1 protein 1 Tris-HCl buffer (pH 7.5) 20 Paper 9468306 Matsubara M, Yamauchi E, Hayashi N, Taniguchi H 1998 FEBS Lett 421 3 203-7 15640140 Tapp H, Al-Naggar IM, Yarmola EG, Harrison A, Shaw G, Edison AS, Bubb MR 2005 J Biol Chem 280 11 9946-56 This protein was found to be disordered while in a complex with calmodulin. protein tyrosine phosphatase type IVA, member 3 isoform 1 PRL-3 14589856 Homo sapiens (Human) 173 MARMNRPAPVEVSYKHMRFLITHNPTNATLSTFIEDLKKYGATTVVRVCEVTYDKTPLEKDGITVVDWPFDDGAPPPGKVVEDWLSLVKAKFCEAPGSCVAVHCVAGLGRAPVLVALALIESGMKYEDAIQFIRQKRRGAINSKQLTYLEKYRPKQRLRFKDPHTHKTRCCVM Disordered 1 7 MARMNRP Nuclear magnetic resonance (NMR) 308 6.8 DTT 10 to 12 mM NaCl 100 phosphate buffer 50 protein 3 sodium azide 0.1 Paper 14704153 Kozlov G, Cheng J, Ziomek E, Banville D, Gehring K, Ekiel I 2004 J Biol Chem 279 12 11882-9 Disordered 157 173 RLRFKDPHTHKTRCCVM Nuclear magnetic resonance (NMR) 308 6.8 DTT 10 to 12 mM NaCl 100 phosphate buffer 50 protein 3 sodium azide 0.1 Paper 14704153 Kozlov G, Cheng J, Ziomek E, Banville D, Gehring K, Ekiel I 2004 J Biol Chem 279 12 11882-9 Disordered acid loop 69 78 PFDDGAPPPG Nuclear magnetic resonance (NMR) 308 6.8 DTT 10 to 12 mM NaCl 100 phosphate buffer 50 protein 3 sodium azide 0.1 Paper 14704153 Kozlov G, Cheng J, Ziomek E, Banville D, Gehring K, Ekiel I 2004 J Biol Chem 279 12 11882-9 protein tyrosine phosphatase type IVA, member 1 PRL-1 4506283 Homo sapiens (Human) 173 MARMNRPAPVEVTYKNMRFLITHNPTNATLNKFIEELKKYGVTTIVRVCEATYDTTLVEKEGIHVLDWPFDDGAPPSNQIVDDWLSLVKIKFREEPGCCIAVHCVAGLGRAPVLVALALIEGGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRFKDSNGHRNNCCIQ Disordered 1 6 MARMNR Nuclear magnetic resonance (NMR) 310 D2O 5 Paper 15213447 Laurence JS, Hallenga K, Stauffacher CV 2004 J Biomol NMR 29 3 417-8 Disordered P-loop 25 29 PTNAT Nuclear magnetic resonance (NMR) 310 D2O 5 Paper 15213447 Laurence JS, Hallenga K, Stauffacher CV 2004 J Biomol NMR 29 3 417-8 Disordered 136 173 KRRGAFNSKQLLYLEKYRPKMRLRFKDSNGHRNNCCIQ Nuclear magnetic resonance (NMR) 310 D2O 5 Paper 15213447 Laurence JS, Hallenga K, Stauffacher CV 2004 J Biomol NMR 29 3 417-8 Securin P40316 730288 Saccharomyces cerevisiae (Baker's yeast) 373 MMPANEDKENNIVYTGNESSGINFPQTPAHLLKRSHSNILKPPVRLDQLKRDANSNNGNTLKYIQGGKEVSPTKRLHTHAQQQGRLPLAAKDNNRSKSFIFPETSNQSKDADLPQLQNTLSIRKNDQLRKLSQISRSRSRANHNDLLSNSRKLQKYGSVLGYNALPKMKSLVLKDLADSGKNEESSDDDEGNEDSESKLGKKLQSALLKQDSSDGENELNGGLGLFNEQGGLQQLIKNSTKNEQKTKNDKSDKTDDYDIEIAPQRQEPLPYVPEGYSPFQQDDIEKLKTFNSPYKLDLEDEDDTPDKVDLLPLEQIDEEGEKDETECITRNQEEGAALPLLSKNFKEVAAVPTMELVYSEEGLDPEELEDLVT Disordered 1 110 MMPANEDKENNIVYTGNESSGINFPQTPAHLLKRSHSNILKPPVRLDQLKRDANSNNGNTLKYIQGGKEVSPTKRLHTHAQQQGRLPLAAKDNNRSKSFIFPETSNQSKD Engineered Fragment Near-UV circular dichroism (CD) spectroscopy 7 ND-Pds1 per ml 0.05 sodium phosphate 10 Nuclear magnetic resonance (NMR) 298 7.2 D2O v/v 5 NaCl 140 NaN3 50 NaPi 12 ND-Pds1 1 Paper 12220679 Cox CJ, Dutta K, Petri ET, Hwang WC, Lin Y, Pascal SM, Basavappa R 2002 FEBS Lett 527 1-3 303-8 The destruction of securin facilitates sister chromatid segregation by releasing the binding partner of securin, separase, which then cleaves the protein complexes that bind together the sister chromatids. Hypothetical superoxide dismutase-like protein yojM [Precursor] O31851 Bacillus subtilis 196 MHRLLLLMMLTALGVAGCGQKKPPDPPNRVPEKKVVETSAFGHHVQLVNREGKAVGFIEIKESDDEGLDIHISANSLRPGASLGFHIYEKGSCVRPDFESAGGPFNPLNKEHGFNNPMGHHAGDLPNLEVGADGKVDVIMNAPDTSLKKGSKLNILDEDGSAFIIHEQADDYLTNPSGNSGARIVCGALLGNNEKQ Disordered 35 39 VVETS Fragment Monomeric Function arises via a disorder to order transition Metal binding Nuclear magnetic resonance (NMR) 298 X-ray crystallography 100 Paper 15897454 Banci L, Bertini I, Calderone V, Cramaro F, Del Conte R, Fantoni A, Mangani S, Quattrone A, Viezzoli MS 2005 Proc Natl Acad Sci U S A 102 21 7541-6 Disordered Long loop IV 89 125 EKGSCVRPDFESAGGPFNPLNKEHGFNNPMGHHAGDL Fragment Monomeric Function arises via a disorder to order transition Metal binding Nuclear magnetic resonance (NMR) 298 X-ray crystallography 100 Paper 15897454 Banci L, Bertini I, Calderone V, Cramaro F, Del Conte R, Fantoni A, Mangani S, Quattrone A, Viezzoli MS 2005 Proc Natl Acad Sci U S A 102 21 7541-6 Disordered Electrostatic loop VII 172 177 YLTNPS Fragment Monomeric Function arises via a disorder to order transition Metal binding Nuclear magnetic resonance (NMR) 298 X-ray crystallography 100 Paper 15897454 Banci L, Bertini I, Calderone V, Cramaro F, Del Conte R, Fantoni A, Mangani S, Quattrone A, Viezzoli MS 2005 Proc Natl Acad Sci U S A 102 21 7541-6 Disordered 191 196 GNNEKQ Fragment Monomeric Function arises via a disorder to order transition Metal binding Nuclear magnetic resonance (NMR) 298 X-ray crystallography 100 Paper 15897454 Banci L, Bertini I, Calderone V, Cramaro F, Del Conte R, Fantoni A, Mangani S, Quattrone A, Viezzoli MS 2005 Proc Natl Acad Sci U S A 102 21 7541-6 Lupus La protein La autoantigen La ribonucleoprotein Sjogren syndrome type B antigen SS-B P05455 Homo sapiens (Human) 408 MAENGDNEKMAALEAKICHQIEYYFGDFNLPRDKFLKEQIKLDEGWVPLEIMIKFNRLNRLTTDFNVIVEALSKSKAELMEISEDKTKIRRSPSKPLPEVTDEYKNDVKNRSVYIKGFPTDATLDDIKEWLEDKGQVLNIQMRRTLHKAFKGSIFVVFDSIESAKKFVETPGQKYKETDLLILFKDDYFAKKNEERKQNKVEAKLRAKQEQEAKQKLEEDAEMKSLEEKIGCLLKFSGDLDDQTCREDLHILFSNHGEIKWIDFVRGAKEGIILFKEKAKEALGKAKDANNGNLQLRNKEVTWEVLEGEVEKEALKKIIEDQQESLNKWKSKGRRFKGKGKGNKAAQPGSGKGKVQFQGKKTKFASDDEHDEHDENGATGPVKRAREETDKEEPASKQQKTENGAGDQ Disordered 326 408 LNKWKSKGRRFKGKGKGNKAAQPGSGKGKVQFQGKKTKFASDDEHDEHDENGATGPVKRAREETDKEEPASKQQKTENGAGDQ Fragment Nuclear magnetic resonance (NMR) DTT pH 7.0 1 KCl buffer 100 protein concen. to 0.2 to 0.5 mM 700 Tris-HCl buffer 20 Nuclear magnetic resonance (NMR) DTT pH 5.8 to 6.5 1 KCl buffer 100 protein concen. to 0.2 to 0.5 mM 700 sodium acetate buffer 20 Analytical ultracentrifugation 293 DTT pH 7.0 0.5 KCl 100 protein 0.5 to 30 uM Tris-HCl 20 Far-UV circular dichroism (CD) 295 KF pH 7 100 NaH2PO4 10 protein per ml 0.5 Far-UV circular dichroism (CD) 295 KF pH 7 100 NaH2PO4 10 protein per ml 45 Paper 12842046 Jacks A, Babon J, Kelly G, Manolaridis I, Cary PD, Curry S, Conte MR 2003 Structure (Camb) 11 7 833-43 Lysozyme C [Precursor] 1,4-beta-N-acetylmuramidase C EC 3.2.1.17 TEWL P00703 126619 Meleagris gallopavo (Common turkey) 147 MRSLLILVLCFLPLAALGKVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKFESNFNTHATNRNTDGSTDYGILQINSRWWCNDGRTPGSKNLCNIPCSALLSSDITASVNCAKKIASGGNGMNAWVAWRNRCKGTDVHAWIRGCRL Disordered beta-hairpin 47 49 NTD Fragment X-ray crystallography 8 ammonium acetate buffer 100 NaCl 9% w/v 50 protein 6 mg per ml 50 Paper 15805597 Margiolaki I, Wright JP, Fitch AN, Fox GC, Von Dreele RB 2005 Acta Crystallogr D Biol Crystallogr 61 Pt 4 423-32 1515108 Howell PL, Almo SC, Parsons MR, Hajdu J, Petsko GA 1992 Acta Crystallogr B 48 ( Pt 2) 200-7 Disordered 60 62 SRW Fragment X-ray crystallography 295 6 NaCl 0.5 M 200 protein per ml 100 Paper 15805597 Margiolaki I, Wright JP, Fitch AN, Fox GC, Von Dreele RB 2005 Acta Crystallogr D Biol Crystallogr 61 Pt 4 423-32 Disordered 70 74 PGSKN Fragment X-ray crystallography 295 6 NaCl 0.5 M 200 protein per ml 100 Paper 15805597 Margiolaki I, Wright JP, Fitch AN, Fox GC, Von Dreele RB 2005 Acta Crystallogr D Biol Crystallogr 61 Pt 4 423-32 Disordered 101 107 GGNGMNA Fragment X-ray crystallography 295 6 NaCl 0.5 M 200 protein per ml 100 Paper 15805597 Margiolaki I, Wright JP, Fitch AN, Fox GC, Von Dreele RB 2005 Acta Crystallogr D Biol Crystallogr 61 Pt 4 423-32 Disordered 129 129 L Fragment X-ray crystallography 295 6 NaCl 0.5 M 200 protein per ml 100 Paper 15805597 Margiolaki I, Wright JP, Fitch AN, Fox GC, Von Dreele RB 2005 Acta Crystallogr D Biol Crystallogr 61 Pt 4 423-32 The sequence for this protein was obtained from LaRue et al. SwissProt has a Asn instead of a Asp at postion 103 of the fragment. Myc proto-oncogene protein c-myc Transcription factor p64 P01106 Homo sapiens (Human) 439 MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENVKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEEDLLRKRREQLKHKLEQLRNSCA Disordered 1 88 MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDG Fragment Transactivation (transcriptional activation) Far-UV circular dichroism (CD) 278 Far-UV circular dichroism (CD) 298 Far-UV circular dichroism (CD) 343 Fluorescence resonance energy transfer 298 8 ANS 20 GuHCl 6 NaCl 100 NaH2PO4 20 Fluorescence resonance energy transfer 298 8 ANS 20 NaCl 100 NaH2PO4 20 Sensitivity to proteolysis 298 2-mercaptoethanol 0.02 bromophenol blue w/v 0.002 glycerol v/v 35 SDS w/v 3 Tris-HCl pH 6.8 80 Paper 15663936 Fladvad M, Zhou K, Moshref A, Pursglove S, Safsten P, Sunnerhagen M 2005 J Mol Biol 346 1 175-89 Disordered - Molten Globule 1 167 MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARG Fragment Function arises from the molten globule state Protein-protein binding Transactivation (transcriptional activation) Thermal stability Far-UV circular dichroism (CD) 278 Far-UV circular dichroism (CD) 298 Far-UV circular dichroism (CD) 343 Fluorescence resonance energy transfer 298 8 ANS 20 GuHCl 6 NaCl 100 NaH2PO4 20 Fluorescence resonance energy transfer 298 8 ANS 20 NaCl 100 NaH2PO4 20 Sensitivity to proteolysis 298 2-mercaptoethanol 0.02 bromophenol blue w/v 0.002 glycerol v/v 35 SDS w/v 3 Tris-HCl pH 6.8 80 Paper 15663936 Fladvad M, Zhou K, Moshref A, Pursglove S, Safsten P, Sunnerhagen M 2005 J Mol Biol 346 1 175-89 Disordered transactivation domain (TAD) 1 143 MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAK Engineered Fragment Function arises via a disorder to order transition Modification site Molecular assembly Protein-protein binding Transactivation (transcriptional activation) Far-UV circular dichroism (CD) phosphate buffer 3 Far-UV circular dichroism (CD) phosphate buffer 10 Paper 8755740 McEwan IJ, Dahlman-Wright K, Ford J, Wright AP 1996 Biochemistry 35 29 9584-93 15663936 Fladvad M, Zhou K, Moshref A, Pursglove S, Safsten P, Sunnerhagen M 2005 J Mol Biol 346 1 175-89 Sialidase 2 Cytosolic sialidase EC 3.2.1.18 N-acetyl-alpha-neuraminidase 2 Q9Y3R4 17369917 Homo sapiens (Human) 380 MASLPVLQKESVFQSGAHAYRIPALLYLPGQQSLLAFAEQRASKKDEHAELIVLRRGDYDAPTHQVQWQAQEVVAQARLDGHRSMNPCPLYDAQTGTLFLFFIAIPGQVTEQQQLQTRANVTRLCQVTSTDHGRTWSSPRDLTDAAIGPAYREWSTFAVGPGHCLQLNDRARSLVVPAYAYRKLHPIQRPIPSAFCFLSHDHGRTWARGHFVAQDTLECQVAEVETGEQRVVTLNARSHLRARVQAQSTNDGLDFQESQLVKKLVEPPPQGCQGSVISFPSPRSGPGSPAQWLLYTHPTHSWQRADLGAYLNPRPPAPEAWSEPVLLAKGSCAYSDLQSMGTGPDGSPLFGCLYEANDYEEIVFLMFTLKQAFPAEYLPQ Disordered alpha-1 helix 42 48 ASKKDEH Function arises via a disorder to order transition X-ray crystallography 298 6.2 NaCl 2.5 protein per ml 10 sodium/potassium phosphate buffer 100 Paper 15501818 Chavas LM, Tringali C, Fusi P, Venerando B, Tettamanti G, Kato R, Monti E, Wakatsuki S 2005 J Biol Chem 280 1 469-75 Disordered alpha-2 helix 107 118 GQVTEQQQLQTR Function arises via a disorder to order transition Substrate/ligand binding X-ray crystallography 298 6.2 NaCl 2.5 protein per ml 10 sodium/potassium phosphate buffer 100 Paper 15501818 Chavas LM, Tringali C, Fusi P, Venerando B, Tettamanti G, Kato R, Monti E, Wakatsuki S 2005 J Biol Chem 280 1 469-75 Hypoxia-inducible factor 1 alpha ARNT interacting protein HIF-1 alpha HIF1 alpha Member of PAS protein 1 MOP1 Q16665 Homo sapiens (Human) 826 MEGAGGANDKKKISSERRKEKSRDAARSRRSKESEVFYELAHQLPLPHNVSSHLDKASVMRLTISYLRVRKLLDAGDLDIEDDMKAQMNCFYLKALDGFVMVLTDDGDMIYISDNVNKYMGLTQFELTGHSVFDFTHPCDHEEMREMLTHRNGLVKKGKEQNTQRSFFLRMKCTLTSRGRTMNIKSATWKVLHCTGHIHVYDTNSNQPQCGYKKPPMTCLVLICEPIPHPSNIEIPLDSKTFLSRHSLDMKFSYCDERITELMGYEPEELLGRSIYEYYHALDSDHLTKTHHDMFTKGQVTTGQYRMLAKRGGYVWVETQATVIYNTKNSQPQCIVCVNYVVSGIIQHDLIFSLQQTECVLKPVESSDMKMTQLFTKVESEDTSSLFDKLKKEPDALTLLAPAAGDTIISLDFGSNDTETDDQQLEEVPLYNDVMLPSPNEKLQNINLAMSPLPTAETPKPLRSSADPALNQEVALKLEPNPESLELSFTMPQIQDQTPSPSDGSTRQSSPEPNSPSEYCFYVDSDMVNEFKLELVEKLFAEDTEAKNPFSTQDTDLDLEMLAPYIPMDDDFQLRSFDQLSPLESSSASPESASPQSTVTVFQQTQIQEPTANATTTTATTDELKTVTKDRMEDIKILIASPSPTHIHKETTSATSSPYRDTQSRTASPNRAGKGVIEQTEKSHPRSPNVLSVALSQRTTVPEEELNPKILALQNAQRKRKMEHDGSLFQAVGIGTLLQQPDDHAATTSLSWKRVKGCKSSEQNGMEQKTIILIPSDLACRLLGQSMDESGLPQLTSYDCEVNAPIQGSRNLLQGEELLRALDQVN Disordered - Extended N-TAD and inhibitory domain 530 698 EFKLELVEKLFAEDTEAKNPFSTQDTDLDLEMLAPYIPMDDDFQLRSFDQLSPLESSSASPESASPQSTVTVFQQTQIQEPTANATTTTATTDELKTVTKDRMEDIKILIASPSPTHIHKETTSATSSPYRDTQSRTASPNRAGKGVIEQTEKSHPRSPNVLSVALSQR Fragment Far-UV circular dichroism (CD) DTE buffer 1 KCl buffer 150 NaPi buffer (pH 7.2) 25 protein 30 Analytical ultracentrifugation 283 DTT buffer 1 KCl buffer 150 NaPi buffer (pH 7.2) 25 Fluorescence anisotropy 283 DTT buffer 1 HEPES pH 7.2 50 Fluorescence anisotropy 283 DTT 1 NaCl buffer (0, 90, and 150 mM) NaPi pH 7.2 25 Paper 15629713 Sanchez-Puig N, Veprintsev DB, Fersht AR 2005 Mol Cell 17 1 11-21 Disordered - Extended ODD domain 403 603 AAGDTIISLDFGSNDTETDDQQLEEVPLYNDVMLPSPNEKLQNINLAMSPLPTAETPKPLRSSADPALNQEVALKLEPNPESLELSFTMPQIQDQTPSPSDGSTRQSSPEPNSPSEYCFYVDSDMVNEFKLELVEKLFAEDTEAKNPFSTQDTDLDLEMLAPYIPMDDDFQLRSFDQLSPLESSSASPESASPQSTVTVFQ Fragment Far-UV circular dichroism (CD) DTE buffer 1 KCl buffer 150 NaPi buffer (pH 7.2) 25 protein 10 Analytical ultracentrifugation 283 DTT buffer 1 KCl buffer 150 NaPi buffer (7.2) 25 Fluorescence anisotropy 283 DTT buffer 1 HEPES pH 7.2 50 Fluorescence anisotropy 283 DTT 1 NaCl buffer (0, 90, 150 mM) NaPi pH 7.2 25 Paper 15629713 Sanchez-Puig N, Veprintsev DB, Fersht AR 2005 Mol Cell 17 1 11-21 Disordered C-terminal activation domain 776 826 SDLACRLLGQSMDESGLPQLTSYDCEVNAPIQGSRNLLQGEELLRALDQVN Native Function arises via a disorder to order transition Transactivation (transcriptional activation) Nuclear magnetic resonance (NMR) 298 Paper 11959977 Dames SA, Martinez-Yamout M, De Guzman RN, Dyson HJ, Wright PE. 2002 Proc Natl Acad Sci U S A 99 8 5271-6. Fatty acid-binding protein, intestinal FABPI I-FABP P02693 1345948 Rattus norvegicus (Rat) 131 AFDGTWKVDRNENYEKFMEKMGINVVKRKLGAHDNLKLTITQEGNKFTVKESSNFRNIDVVFELGVDFAYSLADGTELTGTWTMEGNKLVGKFKRVDNGKELIAVREISGNELIQTYTYEGVEAKRIFKKE Disordered 29 36 KLGAHDNL Nuclear magnetic resonance (NMR) 306 7.2 X-ray crystallography Paper 9063893 Hodsdon ME, Cistola DP 1997 Biochemistry 36 6 1450-60 Disordered 54 57 NFRN Optical rotatory dispersion 306 7.2 X-ray crystallography Paper 9063893 Hodsdon ME, Cistola DP 1997 Biochemistry 36 6 1450-60 Major prion protein [Precursor] PrP PrP27-30 PrP33-35C P04273 130913 Mesocricetus auratus (golden hamster) 254 MANLSYWLLALFVAMWTDVGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGTWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMMHFGNDWEDRYYRENMNRYPNQVYYRPVDQYNNQNNFVHDCVNITIKQHTVTTTTKGENFTETDIKIMERVVEQMCTTQYQKESQAYYDGRRSSAVLFSSPPVILLISFLIFLMVG Disordered 29 124 GGWNTGGSRYPGQGSPGGNRYPPQGGGTWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGG Monomeric Function arises via a disorder to order transition Nuclear magnetic resonance (NMR) 5.2 1H2O 90 2H2O 10 sodium acetate-d5 buffer 20 sodium azide 0.005 Paper 9391046 Donne DG, Viles JH, Groth D, Mehlhorn I, James TL, Cohen FE, Prusiner SB, Wright PE, Dyson HJ 1997 Proc Natl Acad Sci U S A 94 25 13452-7 Major prion protein [Precursor] PrP PrP27-30 PrP33-35C P04925 130914 Mus musculus (Mouse) 254 MANLGYWLLALFVTMWTDVGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYDGRRSSSTVLFSSPPVILLISFLIFLIVG Disordered 23 120 KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAV Fragment Nuclear magnetic resonance (NMR) 293 4.5 COMPLETE protease inhibitor cocktail D2O 10 EDTA 0.01 H2O 90 Pepstatin 0.1 PMSF 0.01 protein 0.8 Paper 9280298 Riek R, Hornemann S, Wider G, Glockshuber R, Wuthrich K 1997 FEBS Lett 413 2 282-8 Thymosin beta-4 Fx T beta 4 P62328 14594937 A38682 Homo sapiens (Human) 43 SDKPDMAEIEKFDKSKLKKTETQEKNPLPSKETIEQEKQAGES Disordered 1 43 SDKPDMAEIEKFDKSKLKKTETQEKNPLPSKETIEQEKQAGES Monomeric Native Function arises via a disorder to order transition Autoregulatory Substrate/ligand binding Gel filtration/size exclusion chromatography Paper 12852258 Bubb MR 2003 Vitam Horm 66 297-316 Potassium voltage-gated channel protein Shaker P08510 13432103 Drosophila melanogaster (Fruit fly) 656 MAAVAGLYGLGEDRQHRKKQQQQQQHQKEQLEQKEEQKKIAERKLQLREQQLQRNSLDGYGSLPKLSSQDEEGGAGHGFGGGPQHFEPIPHDHDFCERVVINVSGLRFETQLRTLNQFPDTLLGDPARRLRYFDPLRNEYFFDRSRPSFDAILYYYQSGGRLRRPVNVPLDVFSEEIKFYELGDQAINKFREDEGFIKEEERPLPDNEKQRKVWLLFEYPESSQAARVVAIISVFVILLSIVIFCLETLPEFKHYKVFNTTTNGTKIEEDEVPDITDPFFLIETLCIIWFTFELTVRFLACPNKLNFCRDVMNVIDIIAIIPYFITLATVVAEEEDTLNLPKAPVSPQDKSSNQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGRTLKASMRELGLLIFFLFIGVVLFSSAVYFAEAGSENSFFKSIPDAFWWAVVTMTTVGYGDMTPVGVWGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETDQEEMQSQNFNHVTSCPYLPGTLGQHMKKSSLSESSSDMMDLDDGVESTPGLTETHPGRSAVAPFLGAQQQQQQQPVASSLSMSIDKQLQHPLQHVTQTQLYQQQQQQQQQQQNGFKQQQQQTQQQLQQQQSHTINASAAAATSGSGSSGLTMRHNNALAVSIETDV Disordered 20 83 QQQQQQHQKEQLEQKEEQKKIAERKLQLREQQLQRNSLDGYGSLPKLSSQDEEGGAGHGFGGGP Mutant Native Function arises from the disordered state Entropic chain Entropic clock Flexible linkers/spacers Paper 2122519 Hoshi T, Zagotta WN, Aldrich RW 1990 Science 250 4980 533-8 Coat protein Protein gp5 P26747 137894 Bacteriophage P22 429 ALNEGQIVTLAVDEIIETISAITPMAQKAKKYTPPAASMQRSSNTIWMPVEQESPTQEGWDLTDKATGLLELNVAVNMGEPDNDFFQLRADDLRDETAYRRRIQSAARKLANNVELKVANMAAEMGSLVITSPDAIGTNTADAWNFVADAEEIMFSRELNRDMGTSYFFNPQDYKKAGYDLTKRDIFGRIPEEAYRDGTIQRQVAGFDDVLRSPKLPVLTKSTATGITVSGAQSFKPVAWQLDNDGNKVNVDNRFATVTLSATTGMKRGDKISFAGVKFLGQMAKNVLAQDATFSVVRVVDGTHVEITPKPVALDDVSLSPEQRAYANVNTSLADAMAVNILNVKDARTNVFWADDAIRIVSQPIPANHELFAGMKTTSFSIPDVGLNGIFATQGDISTLSGLCRIALWYGVNATRPEAIGVGLPGQTA Disordered N-terminal domain 1 190 ALNEGQIVTLAVDEIIETISAITPMAQKAKKYTPPAASMQRSSNTIWMPVEQESPTQEGWDLTDKATGLLELNVAVNMGEPDNDFFQLRADDLRDETAYRRRIQSAARKLANNVELKVANMAAEMGSLVITSPDAIGTNTADAWNFVADAEEIMFSRELNRDMGTSYFFNPQDYKKAGYDLTKRDIFGRI Engineered Fragment Function arises via a disorder to molten globule transition Molecular assembly Protein-protein binding Near-UV circular dichroism (CD) spectroscopy 293 NaCl pH 7.6 25 PO4 25 Hydrogen-deuterium Exchange 294 7.6 2H2O 90 Paper 15784254 Kang S, Prevelige PE Jr 2005 J Mol Biol 347 5 935-48 The N-terminal domain adopts additional structure in the context of the C-terminal domain but retains some flexibility. DE-cadherin 517102 Drosophila melanogaster (Fruit fly) 1507 MSTSVQRMSRSYHCINMSATPQAGHLNPAQQQTHQQHKRKCRDLGRRLIPARLLLGVIVAISLLSPALALHSPPDKNFSGDNRKPAFKNCAGYAPKVKEEQPENTYVLTVEAVDPDPDQVIRYSIVQSPFERPKFFINPSTGVIFTTHTFDRDEPIHEKFVFVTVQATDNGLPPLDDVCTFNVTIEDINDNAPAFNKARYDESMSENAQPDAVVMTISASDFDDGNNSLVEYEILRERDFQYFKIDKESGIIYLKRPIDKRPGQSYAIIVRAYNVVPDPPQDAQIEVRIRVVESSIKPPSFVNPIDTPIYLKENLKNFTHPIATLRAVSNMPDKPEVIFELNTGRTEQTNSKNTFVFNQIGNEVTISLGKTLDYEAITDYTLTMIVRNTHELGTEHQIKIQVEDVNDNIPYYTEVKSGTILENEPPGTPVMQVRAFDMDGTSANNIVSFELADNREYFTIDPNTGNITALTTFDREERDFYNVKVIASDNSPSSLFDNGEPNRGHQVFRISIGDKNDHKPHFQQDKYLAERLLEDANTNTEVIEVKAEDEDNASQILYSIESGNVGDAFKIGLKTGKITVNQKLDYETITEYELKVRAFDGIYDDYTTVVIKIEDVNDNPPVFKQDYSVTILEETTYDDCILTVEAYDPDIKDRNADQHIVYSIHQNDGNRWTIDNSGCLRLVKTLDRDPPNGHKNWQVLIKANDEDGVGTTVSTVKEVTVTLKDINDNAPFLINEMPVYWQENRNPGHVVQLQANDYDDTPGAGNFTFGIDSEATPDIKTKFSMDGDYLHANVQFDREAQKEYFIPIRISDSGVPRQSAVSILHLVIGDVNDNAMSEGSSRIFIYNYKGEAPETDIGRVFVDDLDDWDLEDKYFEWKDLPHDQFRLNPSTGMITMLVHTAEGEYDLSFVVTEDSMFVPRHSVDAYVTVVVRELPEEAVDKSGSIRFINVTKEEFISVPRDFQSPDALSLKDRFQLSLAKLFNTSVSNVDVFTVLQNENHTLDVRFSAHGSPYYAPEKLNGIVAQNQQRLENELDLQMLMVNIDECLIEKFKCEESCTNELHKSSVPYMIYSNTTSFVGVNAFVQAQCVCEAPLMRRCLNGGSPRYGENDVCDCIDGFTGPHCELVSVAFYGSGYAFYEPIAACNNTKISLEITPQIDQGLIMYLGPLNFNPLLAISDFLALELDNGYPVLTVDYGSGAIRIRHQHIKMVADRTYQLDIILQRTSIEMTVDNCRLSTCQTLGAPIGPNEFLNVNAPLQLGGTPVDLEQLGRQLNWTHVPNQKGFFGCIRNLTINEQTYNLGMPSVFRNIDSGCQQSVAVAFSFGIDRNFIIAIIVCLALLLIILLAVVVQKKQKNGWHEKDIDDIRETIINYEDEGGGERDTDYDLNVLRTQPFYEEKLYKDPHALQGNMRDPNDIPDIADFLGDKKENCDRDVGATTVDDVRHYAYEGDGNSDGSLSSLASCTDDGDLNFDYLSNFGPRFRKLADMYGEEPSDTDSNVDDDQGWRI Disordered cytoplasmic domain 1350 1507 QKKQKNGWHEKDIDDIRETIINYEDEGGGERDTDYDLNVLRTQPFYEEKLYKDPHALQGNMRDPNDIPDIADFLGDKKENCDRDVGATTVDDVRHYAYEGDGNSDGSLSSLASCTDDGDLNFDYLSNFGPRFRKLADMYGEEPSDTDSNVDDDQGWRI Fragment Fluorescence anisotropy beta76 2 beta-catenin 3.5 bovin serum albumin 3 protein 6,3, or 1.5 mM tryptophan 12 or 14 mM Near-UV circular dichroism (CD) spectroscopy 273 7 phosphate 10 Paper 11121423 Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI 2001 J Biol Chem 276 15 12301-12309 7958432 Oda H, Uemura T, Harada Y, Iwai Y, Takeichi M 1994 Dev Biol 165 2 716-26 This sequence has 99% homology with SwissProt ID Q24298. SwissProt has a leucine at position 974 instead of a phenylalanine. antibody heavy chain FAB 3399661 Mus musculus (Mouse) 220 LESGPELVKPGASVKMSCKASGYTFTSYVMHWVKQKPGQGLEWIGYINPYNDGTKYNEKFKGKATLTSDKSSSTAYMELSSLTSEDSAVYYCVRGGYRPYYAMDYWGQGTSVTVSSAKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSTWPSETVTCNVAHPASSTKVDKKIVPRDCTS Disordered apical residues of HCDR3 97 100 YRPY Function arises via a disorder to order transition Protein-DNA binding Substrate/ligand binding X-ray crystallography 298 isopranol 20 PEG4000 w/v 14 sodium citrate pH 5.5 0.1 Paper 15784256 Schuermann JP, Prewitt SP, Davies C, Deutscher SL, Tanner JJ 2005 J Mol Biol 347 5 965-78 Disordered HCDR3 95 105 GGYRPYYAMDY Function arises via a disorder to order transition Molecular assembly Substrate/ligand binding X-ray crystallography isopropanol 20 PEG4000 w/v 14 sodium citrate pH 5.5 0.1 Paper 7506692 Calcutt MJ, Kremer MT, Giblin MF, Quinn TP, Deutscher SL 1993 Gene 137 1 77-83 15784256 Schuermann JP, Prewitt SP, Davies C, Deutscher SL, Tanner JJ 2005 J Mol Biol 347 5 965-78 Rhodopsin P02699 129204 Bos taurus (Bovine) 348 MNGTEGPNFYVPFSNKTGVVRSPFEAPQYYLAEPWQFSMLAAYMFLLIMLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVFGGFTTTLYTSLHGYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLVGWSRYIPEGMQCSCGIDYYTPHEETNNESFVIYMFVVHFIIPLIVIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVIAFLICWLPYAGVAFYIFTHQGSDFGPIFMTIPAFFAKTSAVYNPVIYIMMNKQFRNCMVTTLCCGKNPLGDDEASTTVSKTETSQVAPA Disordered 236 239 QQQE Relationship to function unknown X-ray crystallography Paper 10926528 Palczewski K, Kumasaka T, Hori T, Behnke CA, Motoshima H, Fox BA, Le Trong I, Teller DC, Okada T, Stenkamp RE, Yamamoto M, Miyano M 2000 Science 289 5480 739-45 Disordered 328 333 LGDDEA X-ray crystallography Paper 10926528 Palczewski K, Kumasaka T, Hori T, Behnke CA, Motoshima H, Fox BA, Le Trong I, Teller DC, Okada T, Stenkamp RE, Yamamoto M, Miyano M 2000 Science 289 5480 739-45 Disordered 133 137 IERYV X-ray crystallography Paper 10926528 Palczewski K, Kumasaka T, Hori T, Behnke CA, Motoshima H, Fox BA, Le Trong I, Teller DC, Okada T, Stenkamp RE, Yamamoto M, Miyano M 2000 Science 289 5480 739-45 Disordered 207 222 MFVVHFIIPLIVIFFC X-ray crystallography Paper 10926528 Palczewski K, Kumasaka T, Hori T, Behnke CA, Motoshima H, Fox BA, Le Trong I, Teller DC, Okada T, Stenkamp RE, Yamamoto M, Miyano M 2000 Science 289 5480 739-45 Disordered 327 348 PLGDDEASTTVSKTETSQVAPA X-ray crystallography Paper 10926528 Palczewski K, Kumasaka T, Hori T, Behnke CA, Motoshima H, Fox BA, Le Trong I, Teller DC, Okada T, Stenkamp RE, Yamamoto M, Miyano M 2000 Science 289 5480 739-45 Mu-type opioid receptor MOR-1 P35372 2851402 Homo sapiens (Human) 400 MDSSAAPTNASNCTDALAYSSCSPAPSPGSWVNLSHLDGNLSDPCGPNRTDLGGRDSLCPPTGSPSMITAITIMALYSIVCVVGLFGNFLVMYVIVRYTKMKTATNIYIFNLALADALATSTLPFQSVNYLMGTWPFGTILCKIVISIDYYNMFTSIFTLCTMSVDRYIAVCHPVKALDFRTPRNAKIINVCNWILSSAIGLPVMFMATTKYRQGSIDCTLTFSHPTWYWENLLKICVFIFAFIMPVLIITVCYGLMILRLKSVRMLSGSKEKDRNLRRITRMVLVVVAVFIVCWTPIHIYVIIKALVTIPETTFQTVSWHFCIALGYTNSCLNPVLYAFLDENFKRCFREFCIPTSSNIEQQNSTRIRQNTRDHPSTANTVDRTNHQLENLEAETAPLP Disordered 128 143 VNYLMGTWPFGTILSK Fragment Mutant Molecular recognition effectors Near-UV circular dichroism (CD) spectroscopy 7 NaCl buffer 50 protein 15 Tris-HCl buffer 10 Paper 15680247 Kerman A, Ananthanarayanan VS 2005 Biochim Biophys Acta 1747 1 133-40 The fragment used for structure determination contained residues 97-176 of the human µR. Guanine nucleotide-binding protein G(t), alpha-1 subunit Transducin alpha-1 chain P04695 121031 Bos taurus (Bovine) 350 MGAGASAEEKHSRELEKKLKEDAEKDARTVKLLLLGAGESGKSTIVKQMKIIHQDGYSLEECLEFIAIIYGNTLQSILAIVRAMTTLNIQYGDSARQDDARKLMHMADTIEEGTMPKEMSDIIQRLWKDSGIQACFDRASEYQLNDSAGYYLSDLERLVTPGYVPTEQDVLRSRVKTTGIIETQFSFKDLNFRMFDVGGQRSERKKWIHCFEGVTCIIFIAALSAYDMVLVEDDEVNRMHESLHLFNSICNHRYFATTSIVLFLNKKDVFSEKIKKAHLSICFPDYNGPNTYEDAGNYIKVQFLELNMRRDVKEIYSHMTCATDTQNVKFVFDAVTDIIIKENLKDCGLF Disordered Gt alpha 340 350 IKENLKDCGLF Function arises via an order to disorder transition Nuclear magnetic resonance (NMR) 274 2H2O 10 DTT 1 EDTA 0.1 KCl 100 sodium phosphate pH 7.5 20 Paper 9539726 Kisselev OG, Kao J, Ponder JW, Fann YC, Gautam N, Marshall GR 1998 Proc Natl Acad Sci U S A 95 8 4270-5 Alpha-1 type II collagen Homo sapiens (Human) 1487 MIRLGAPQSLVLLTLLVAAVLRCQGQDVQEAGSCVQDGQRYNDKDVWKPEPCRICVCDTGTVLCDDIICEDVKDCLSPEIPFGECCPICPTDLATASGQPGPKGQKGEPGDIKDIVGPKGPPGPQGPAGEQGPRGDRGDKGEKGAPGPRGRDGEPGTPGNPGPPGPPGPPGPPGLGGNFAAQMAGGFDEKAGGAQLGVMQGPMGPMGPRGPPGPAGAPGPQGFQGNPGEPGEPGVSGPMGPRGPPGPPGKPGDDGEAGKPGKAGERGPPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGENGSPGPMGPRGLPGERGRTGPAGAAGARGNDGQPGPAGPPGPVGPAGGPGFPGAPGAKGEAGPTGARGPEGAQGPRGEPGTPGSPGPAGASGNPGTDGIPGAKGSAGAPGIAGAPGFPGPRGPPGPQGATGPLGPKGQTGEPGIAGFKGEQGPKGEPGPAGPQGAPGPAGEEGKRGARGEPGGVGPIGPPGERGAPGNRGFPGQDGLAGPKGAPGERGPSGLAGPKGANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQGARGQPGVMGFPGPKGANGEPGKAGEKGLPGAPGLRGLPGKDGETGAAGPPGPAGPAGERGEQGAPGPSGFQGLPGPPGPPGEGGKPGDQGVPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDGPKGASGPAGPPGAQGPPGLQGMPGERGAAGIAGPKGDRGDVGEKGPEGAPGKDGGRGLTGPIGPPGPAGANGEKGEVGPPGPAGSAGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGEQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGRVGPPGSNGNPGPPGPPGPSGKDGPKGARGDSGPPGRAGEPGLQGPAGPPGEKGEPGDDGPSGAEGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGASGDRGPPGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGVKGDRGETGAVGAPGAPGPPGSPGPAGPTGKQGDRGEAGAQGPMGPSGPAGARGIQGPQGPRGDKGEAGEPGERGLKGHRGFTGLQGLPGPPGPSGDQGASGPAGPSGPRGPPGPVGPSGKDGANGIPGPIGPPGPRGRSGETGPAGPPGNPGPPGPPGPPGPGIDMSAFAGLGPREKGPDPLQYMRADQAAGGLRQHDAEVDATLKSLNNQIESIRSPEGSRKNPARTCRDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMETGETCVYPNPANVPKKNWWSSKSKEKKHIWFGETINGGFHFSYGDDNLAPNTANVQMTFLRLLSTEGSQNITYHCKNSIAYLDEAAGNLKKALLIQGSNDVEIRAEGNSRFTYTALKDGCTKHTGKWGKTVIEYRSQKTSRLPIIDIAPMDIGGPEQEFGVDIGPVCFL Disordered linker region 71 75 DVKDC Engineered Fragment 1U5MA Function arises via a disorder to order transition Substrate/ligand binding Nuclear magnetic resonance (NMR) 298 6 2H2O v/v 10 potassium phosphate buffer (90% v/v) 50 protein 0.8 sodium azide v/v 0.02 Paper 15466413 O'Leary JM, Hamilton JM, Deane CM, Valeyev NV, Sandell LJ, Downing AK 2004 J Biol Chem 279 51 53857-66 hypothetical protein YPO2884 Q8ZCT1 16123076 AD0351 Yersinia pestis 806 MRYNRNHMLTLMFSLLIFDAYANEPKVCFYMDDDYNGESLCAAQGNSVASIPDKWNDRISSISIPHGLVVTVYEDVDFLGASRSFEADVDLVSDKDLIYLNDNISAFKIKKAVCFYGESNFTGDSLCLSSGEQFDLYRGNYPERKQSHLVNPLNDEVYSIKIPPGMQTTVYEDDDYNGKYFVLTEDYTPDDLLIIRMNNKISSMRVSQDEDFICDRFCSIKKSIKFKIQKSFGSYWIDPRIKYRDILLDFQLSDTDDYSIKFFDEGLIKVKNYKLFFFDGNEKHGEGFLFNLSDKSSNLSFLLRFNGGFFQIQFVESLNNEIVYSSPLIGTLFDDANSDVIFDINNVDANSPIVIDKMVLTVGKEHNRAERSTLGLATCWAIPILSIYNYIVQGHCNQADKFVHNAADFFGSPADKILQIFGSSLPLPPKNSNETLDDESALINFMSDVKGTLTYITTNMGEHALTVPATALACKASMREKILPHLRNRRDLAPGCIDWTLSILTDFTLLFGASIEYWNSKNFGRVIENIVREGEIGSAVADVDTASRLIESVQAHVAEATEVADIIHLKTAFDFSQLSYVSYVRHTEEEVVSPQSAQALPLGRYELALVDYHFIETVPRIRQDGRWVERPDLHFDIEVISGVPEETDASRQVLLPIIEAWQHSYSQQELLFHASDILPESSLARYEIEPLLEASRLTSEVAISWLRTSRDDFVYVVVRLEGEVISLTMAVDININDVGVAGSLTNPDYVITPNAEGAVRGAGTAAIRALADHFKRKGKISLVSSVISQPSAIVKKKVGFRFIEEL Disordered Domain 1 21 112 YANEPKVCFYMDDDYNGESLCAAQGNSVASIPDKWNDRISSISIPHGLVVTVYEDVDFLGASRSFEADVDLVSDKDLIYLNDNISAFKIKKA Engineered Function arises via a disorder to order transition Substrate/ligand binding Far-UV circular dichroism (CD) 298 Paper 15536081 Jobby MK, Sharma Y 2005 J Biol Chem 280 2 1209-16 Disordered Domain 2 110 215 KKAVCFYGESNFTGDSLCLSSGEQFDLYRGNYPERKQSHLVNPLNDEVYSIKIPPGMQTTVYEDDDYNGKYFVLTEDYTPDDLLIIRMNNKISSMRVSQDEDFICD Engineered Relationship to function unknown Substrate/ligand binding Far-UV circular dichroism (CD) 298 Paper 15536081 Jobby MK, Sharma Y 2005 J Biol Chem 280 2 1209-16 membrane fusion protein p14 29888078 Reptilian orthoreovirus 125 MGSGPSNFVNHAPGEAIVTGLEKGADKVAGTISHTIWEVIAGLVALLTFLAFGFWLFKYLQKRRERRRQLTEFQKRYLRNSYRLSEIQRPISQHEYEDPYEPPSRRKPPPPPYSTYVNIDNVSAI Disordered 2 14 GSGPSNFVNHAPG Function arises via a disorder to order transition Far-UV circular dichroism (CD) 298 protein 10-80 uM in water Nuclear magnetic resonance (NMR) 278 7.2 1H2O 90 2H2O 10 lyophilized acetyl-p14 peptide 5 potassium phosphate buffer 50 Nuclear magnetic resonance (NMR) 278 7.2 1H2O 90 2H2O 10 myristoylated p14 peptide 0.5 potassium phosphate buffer 50 Paper 15448165 Corcoran JA, Syvitski R, Top D, Epand RM, Epand RF, Jakeman D, Duncan R 2004 J Biol Chem 279 49 51386-94 This region contains an extended "loop structure" comprising residues Pro5 to Pro13. Disordered 15 31 EAIVTGLEKGADKVAGT Function arises via a disorder to order transition Flexible linkers/spacers Far-UV circular dichroism (CD) 298 protein 10-80 uM in water Nuclear magnetic resonance (NMR) 278 7.2 1H2O 90 2H2O 10 lyophilized acetyl-p14 peptide 5 potassium phosphate buffer 50 Nuclear magnetic resonance (NMR) 278 7.2 1H2O 90 2H2O 10 myristoylated p14 peptide 0.5 potassium phosphate buffer 50 Paper 15448165 Corcoran JA, Syvitski R, Top D, Epand RM, Epand RF, Jakeman D, Duncan R 2004 J Biol Chem 279 49 51386-94 Cytochrome c oxidase copper chaperone Cox17 Q12287 2493874 Saccharomyces cerevisiae (Baker's yeast) 69 MTETDKKQEQENHAECEDKPKPCCVCKPEKEERDTCILFNGQDSEKCKEFIEKYKECMKGYGFEVPSAN Disordered 1 26 MTETDKKQEQENHAECEDKPKPCCVC Function arises from the disordered state Metal binding Protein-protein binding Nuclear magnetic resonance (NMR) 298 6 D2O v/v 7 potassium phosphate 20 protein 1 TCEP 1 Paper 15465825 Abajian C, Yatsunyk LA, Ramirez BE, Rosenzweig AC 2004 J Biol Chem 279 51 53584-92 This is the Cox17 protein in the apo form Disordered 1 22 MTETDKKQEQENHAECEDKPKP Complex Function arises from the disordered state Metal binding Protein-protein binding Nuclear magnetic resonance (NMR) 298 6 CuCl anaerobic solution 6.1 HCl anaerobic solution 10 NaCl 100 potassium phosphate 100 protein 1 sodium chloride anaerobic solution 1 Paper 15465825 Abajian C, Yatsunyk LA, Ramirez BE, Rosenzweig AC 2004 J Biol Chem 279 51 53584-92 This is the Cox17 protein in complex with copper. Disordered 64 69 EVPSAN Function arises from the disordered state Metal binding Protein-protein binding Nuclear magnetic resonance (NMR) 298 6 D2O v/v 7 potassium phosphate 20 protein 1 TCEP 1 Paper 15465825 Abajian C, Yatsunyk LA, Ramirez BE, Rosenzweig AC 2004 J Biol Chem 279 51 53584-92 This is the Cox17 protein is its apo form. Disordered 64 69 EVPSAN Complex Function arises from the disordered state Metal binding Protein-protein binding Nuclear magnetic resonance (NMR) 298 6 CuCl anaerobic solution 6.1 HCl anaerobic solution 10 NaCl 100 potassium phosphate 100 protein 1 sodium chloride anaerobic solution 1 Paper 15465825 Abajian C, Yatsunyk LA, Ramirez BE, Rosenzweig AC 2004 J Biol Chem 279 51 53584-92 This is the Cox17 protein in complex with copper. Gap junction alpha-1 protein Connexin 43 Cx43 Gap junction 43 kDa heart protein P08050 117708 Rattus norvegicus (Rat) 381 GDWSALGKLLDKVQAYSTAGGKVWLSVLFIFRILLLGTAVESAWGDEQSAFRCNTQQPGCENVCYDKSFPISHVRFWVLQIIFVSVPTLLYLAHVFYVMRKEEKLNKKEEELKVAQTDGVNVEMHLKQIEIKKFKYGIEEHGKVKMRGGLLRTYIISILFKSVFEVAFLLIQWYIYGFSLSAVYTCKRDPCPHQVDCFLSRPTEKTIFIIFMLVVSLVSLALNIIELFYVFFKGVKDRVKGRSDPYHATTGPLSPSKDCGSPKYAYFNGCSSPTAPLSPMSPPGYKLVTGDRNNSSCRNYNKQASEQNWANYSAEQNRMGQAGSTISNSHAQPFDFPDDNQNAKKVAAGHELQPLAIVDQRPSSRASSRASSRPRPDDLEI Disordered 254 313 SPSKDCGSPKYAYFNGCSSPTAPLSPMSPPGYKLVTGDRNNSSCRNYNKQASEQNWANYS Fragment Function arises via a disorder to order transition Flexible linkers/spacers Phosphorylation Protein-protein binding Nuclear magnetic resonance (NMR) 280 5.8 phosphate saline buffer Paper 15492000 Sorgen PL, Duffy HS, Sahoo P, Coombs W, Delmar M, Spray DC 2004 J Biol Chem 279 52 54695-701 Disordered 326 338 ISNSHAQPFDFPD Fragment Function arises via a disorder to order transition Flexible linkers/spacers Phosphorylation Protein-protein binding Nuclear magnetic resonance (NMR) 280 5.8 phosphate saline buffer Paper 15492000 Sorgen PL, Duffy HS, Sahoo P, Coombs W, Delmar M, Spray DC 2004 J Biol Chem 279 52 54695-701 Disordered 347 382 AGHELQPLAIVDQRPSSRASSRASSRPRPDDLEI Fragment Function arises via a disorder to order transition Flexible linkers/spacers Phosphorylation Protein-protein binding Nuclear magnetic resonance (NMR) 280 5.8 phosphate saline buffer Paper 15492000 Sorgen PL, Duffy HS, Sahoo P, Coombs W, Delmar M, Spray DC 2004 J Biol Chem 279 52 54695-701 Olfactory marker protein Olfactory neuronal specific protein P08523 129096 Rattus norvegicus (Rat) 163 MAEDGPQKQQLDMPLVLDQDLTKQMRLRVESLKQRGEKKQDGEKLLRPAESVYRLDFIQQQKLQFDHWNVVLDKPGKVTITGTSQNWTPDLTNLMTRQLLDPAAIFWRKEDSDAMDWNEADALEFGERLSDLAKIRKVMYFLITFGEGVEPANLKASVVFNQL Disordered Loop 1 35 49 RGEKKQDGEKLLRPA Nuclear magnetic resonance (NMR) 310 D2O 5 H2O 95 Na2EDTA 0.1 Na2HPO4 pH 6.6 5 NaN3 0.3 Paper 16008352 Gitti RK, Wright NT, Margolis JW, Varney KM, Weber DJ, Margolis FL 2005 Biochemistry 44 28 9673-9679 Disordered Loop 2 57 68 FIQQQKLQFDHW Nuclear magnetic resonance (NMR) D2O 5 H2O 95 Na2EDTA 0.1 Na2HPO4 pH 6.6 5 NaN3 0.3 Paper 16008352 Gitti RK, Wright NT, Margolis JW, Varney KM, Weber DJ, Margolis FL 2005 Biochemistry 44 28 9673-9679 Disordered Omega Loop 84 99 SQNWTPDLTNLMTRQL Nuclear magnetic resonance (NMR) D2O 5 H2O 95 Na2EDTA 0.1 Na2HPO4 pH 6.6 5 NaN3 0.3 Paper 16008352 Gitti RK, Wright NT, Margolis JW, Varney KM, Weber DJ, Margolis FL 2005 Biochemistry 44 28 9673-9679 Perfringolysin O [Precursor] Theta-toxin Thiol-activated cytolysin P19995 20141696 Clostridium perfringens 500 MIRFKKTKLIASIAMALCLFSQPVISFSKDITDKNQSIDSGISSLSYNRNEVLASNGDKIESFVPKEGKKTGNKFIVVERQKRSLTTSPVDISIIDSVNDRTYPGALQLADKAFVENRPTILMVKRKPININIDLPGLKGENSIKVDDPTYGKVSGAIDELVSKWNEKYSSTHTLPARTQYSESMVYSKSQISSALNVNAKVLENSLGVDFNAVANNEKKVMILAYKQIFYTVSADLPKNPSDLFDDSVTFNDLKQKGVSNEAPPLMVSNVAYGRTIYVKLETTSSSKDVQAAFKALIKNTDIKNSQQYKDIYENSSFTAVVLGGDAQEHNKVVTKDFDEIRKVIKDNATFSTKNPAYPISYTSVFLKDNSVAAVHNKTDYIETTSTEYSKGKINLDHSGAYVAQFEVAWDEVSYDKEGNEVLTHKTWDGNYQDKTAHYSTVIPLEANARNIRIKARECTGLAWEWWRDVISEYDVPLTNNINVSIWGTTLYPGSSITYN Disordered TMH1 190 217 SQISSALNVNAKVLENSLGVDFNAVANN Monomeric Mutant Fluorescent probes 298 HEPES pH 7.5 50 NaCl 100 Paper 15797734 Dang TX, Hotze EM, Rouiller I, Tweten RK, Wilson-Kubalek EM 2005 J Struct Biol 150 1 100-8 10555145 Shatursky O, Heuck AP, Shepard LA, Rossjohn J, Parker MW, Johnson AE, Tweten RK 1999 Cell 99 3 293-9 The six alpha-helices in domain 3 undergo a conformational change into two beta-hairpins that span the membrane. This order to order transition proceeds through a disordered intermediate. Disordered TMH2 288 311 KDVQAAFKALIKNTDIKNSQQYKD Monomeric Mutant Fluorescent probes 298 HEPES pH 7.5 50 NaCl 100 Paper 15797734 Dang TX, Hotze EM, Rouiller I, Tweten RK, Wilson-Kubalek EM 2005 J Struct Biol 150 1 100-8 10555145 Shatursky O, Heuck AP, Shepard LA, Rossjohn J, Parker MW, Johnson AE, Tweten RK 1999 Cell 99 3 293-9 The six alpha-helices in domain 3 undergo a conformational change into two beta-hairpins that span the membrane. This order to order transition proceeds through a disordered intermediate. yefM protein 7467161 H64966 Escherichia coli 92 MNCTKEEIDMRTISYSEARQNLSATMMKAVEDHAPILITRQNGEACVLMSLEEYNSLEETAYLLRSPANARRLMDSIDSLKSGKGTEKDIIE Disordered 1 92 MNCTKEEIDMRTISYSEARQNLSATMMKAVEDHAPILITRQNGEACVLMSLEEYNSLEETAYLLRSPANARRLMDSIDSLKSGKGTEKDIIE Engineered Function arises from the disordered state Protein-protein binding Far-UV circular dichroism (CD) 298 7.3 PBS protein 10 Far-UV circular dichroism (CD) 310 7.3 PBS protein 10 Far-UV circular dichroism (CD) 315 7.3 PBS protein 10 Paper 14672926 Cherny I, Gazit E 2004 J Biol Chem 279 9 8252-61 Copper-transporting ATPase 1 Copper pump 1 EC 3.6.3.4 Menkes disease-associated protein Q04656 1351993 Homo sapiens (Human) 1500 MDPSMGVNSVTISVEGMTCNSCVWTIEQQIGKVNGVHHIKVSLEEKNATIIYDPKLQTPKTLQEAIDDMGFDAVIHNPDPLPVLTDTLFLTVTASLTLPWDHIQSTLLKTKGVTDIKIYPQKRTVAVTIIPSIVNANQIKELVPELSLDTGTLEKKSGACEDHSMAQAGEVVLKMKVEGMTCHSCTSTIEGKIGKLQGVQRIKVSLDNQEATIVYQPHLISVEEMKKQIEAMGFPAFVKKQPKYLKLGAIDVERLKNTPVKSSEGSQQRSPSYTNDSTATFIIDGMHCKSCVSNIESTLSALQYVSSIVVSLENRSAIVKYNASSVTPESLRKAIEAVSPGLYRVSITSEVESTSNSPSSSSLQKIPLNVVSQPLTQETVINIDGMTCNSCVQSIEGVISKKPGVKSIRVSLANSNGTVEYDPLLTSPETLRGAIEDMGFDATLSDTNEPLVVIAQPSSEMPLLTSTNEFYTKGMTPVQDKEEGKNSSKCYIQVTGMTCASCVANIERNLRREEGIYSILVALMAGKAEVRYNPAVIQPPMIAEFIRELGFGATVIENADEGDGVLELVVRGMTCASCVHKIESSLTKHRGILYCSVALATNKAHIKYDPEIIGPRDIIHTIESLGFEASLVKKDRSASHLDHKREIRQWRRSFLVSLFFCIPVMGLMTYMMVMDHHFATLHHNQNMSKEEMINLHSSMFLERQILPGLSVMNLLSFLLCVPVQFFGGWYFYIQAYKALKHKTANMDVLIVLATTIAFAYSLIILLVAMYERAKVNPITFFDTPPMLFVFIALGRWLEHIAKGKTSEALAKLISLQATEATIVTLDSDNILLSEEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKPGSTVIAGSINQNGSLLICATHVGADTTLSQIVKLVEEAQTSKAPIQQFADKLSGYFVPFIVFVSIATLLVWIVIGFLNFEIVETYFPGYNRSISRTETIIRFAFQASITVLCIACPCSLGLATPTAVMVGTGVGAQNGILIKGGEPLEMAHKVKVVVFDKTGTITHGTPVVNQVKVLTESNRISHHKILAIVGTAESNSEHPLGTAITKYCKQELDTETLGTCIDFQVVPGCGISCKVTNIEGLLHKNNWNIEDNNIKNASLVQIDASNEQSSTSSSMIIDAQISNALNAQQHKVLIGNREWMIRNGLVINNDVNDFMTEHERKGRTAVLVAVDDELCGLIAIADTVKPEAELAIHILKSMGLEVVLMTGDNSKTARSIASQVGITKVFAEVLPSHKVAKVKQLQEEGKRVAMVGDGINDSPALAMANVGIAIGTGTDVAIEAADVVLIRNDLLDVVASIDLSRKTVKRIRINFVFALIYNLVGIPIAAGVFMPIGLVLQPWMGSAAMAASSVSVVLSSLFLKLYRKPTYESYELPARSQIGQKSPSEISVHVGIDDTSRNSPKLGLLDRIVNYSRASINSLLSDKRSLNSVVTSEPDKHSLLVGDFREDDDTAL Disordered 164 168 SMAQA Fragment Mutant Nuclear magnetic resonance (NMR) 298 Paper 14572476 Jones CE, Daly NL, Cobine PA, Craik DJ, Dameron CT 2003 J Struct Biol 143 3 209-18 A single point mutation of MNKr2 was created with a F72I substitution, as discussed in the Jones et al. article. Disordered Loop 1 171 180 VVLKMKVEGM Monomeric Function arises via a disorder to order transition Substrate/ligand binding Nuclear magnetic resonance (NMR) 298 Nuclear magnetic resonance (NMR) 298 7 2H2O v/v 10 DTT excess protein 1 sodium phsophate buffer 100 Paper 15035611 Banci L, Bertini I, Del Conte R, D'Onofrio M, Rosato A 2004 Biochemistry 43 12 3396-403 14572476 Jones CE, Daly NL, Cobine PA, Craik DJ, Dameron CT 2003 J Struct Biol 143 3 209-18 Disordered 239 246 KKQPKYLK Fragment Mutant Nuclear magnetic resonance (NMR) 298 Paper 14572476 Jones CE, Daly NL, Cobine PA, Craik DJ, Dameron CT 2003 J Struct Biol 143 3 209-18 A single point mutation of MNKr2 was created with a F72I substitution, as discussed in the Jones et al. article. Chimeric Double Cellulase Cel6BA Humicola insolens 796 QSGNPFSGRTLLVNSDYSSKLDQTRQAFLSRGDQTNAAKVKYVQEKVGTFYWISNIFLLRDIDVAIQNARAAKARGENPIVGLVLYNLPDRDCSAGESSGELKLSQNGLNRYKNEYVNPFAQKLKAASDVQFAVILEPDAIGNMVTGTSAFCRNARGPQQEAIGYAISQLQASHIHLYLDVANGGWLGWADKLEPTAQEVATILQKAGNNAKIRGFSSNVSNYNPYSTSNPPPYTSGSPSPDESRYATNIANAMRQRGLPTQFIIDQSRVALSGARSEWGQWCNVNPAGFGQPFTTNTNNPNVDAIVWVKPGGESDGQCGMGGAPAAGMWFDAYAQMLTQNAHDEIARAGAAGSGGGNNGGGNNPNPTPTNPTNPGPTSNPGGGNPGQVTTSTTSSSSTTSRATSTTSAGGVTSITTAPTRTVTIPGGASTTASYNGNPFEGVQLWANNYYRSEVHTLAIPQITDPALRAAASAVAEVPSFQWLDRNVTVDTLLVQTLSEIREANQAGANPQYAAQIVVYDLPDRDCAAAASNGEWAIANNGVNNYKAYINRIREILISFSDVRTILVIEPDSLANMVTNMNVPKCSGAASTYRELTIYALKQLDLPHVAMYMDAGHAGWLGWPANIQPAAELFAKIYEDAGKPRAVRGLATNVANYNAWSVSSPPPYTSPNPNYDEKHYIEAFRPLLEARGFPAQFIVDQGRSGKQPTGQKEWGHWCNAIGTGFGMRPTANTGHQYVDAFVWVKPGGECDGTSDTTAARYDYHCGLEDALKPAPEAGQWFNEYFIQLLRNANPPF Disordered - Extended Linker 349 436 AGAAGSGGGNNGGGNNPNPTPTNPTNPGPTSNPGGGNPGQVTTSTTSSSSTTSRATSTTSAGGVTSITTAPTRTVTIPGGASTTASYN Engineered Function arises from the disordered state Unknown Flexible linkers/spacers Small-angle X-ray scattering 293 7.5 sodium phosphate buffer 50 Paper 15653742 von Ossowski I, Eaton JT, Czjzek M, Perkins SJ, Frandsen TP, Schulein M, Panine P, Henrissat B, Receveur-Brechot V 2005 Biophys J 88 4 2823-32 The conformation of the disordered linker was studied by means of an artificial fusion protein, Cel6BA, in which the 88-residue linker connects the large catalytic modules of the cellulases Cel6A and Cel6B. Therefore, there are no accession numbers pertaining to this experiment sequence. Tail-associated lysozyme EC 3.2.1.17 Protein Gp5 P16009 137895 Bacteriophage T4 575 MEMISNNLNWFVGVVEDRMDPLKLGRVRVRVVGLHPPQRAQGDVMGIPTEKLPWMSVIQPITSAAMSGIGGSVTGPVEGTRVYGHFLDKWKTNGIVLGTYGGIVREKPNRLEGFSDPTGQYPRRLGNDTNVLNQGGEVGYDSSSNVIQDSNLDTAINPDDRPLSEIPTDDNPNMSMAEMLRRDEGLRLKVYWDTEGYPTIGIGHLIMKQPVRDMAQINKVLSKQVGREITGNPGSITMEEATTLFERDLADMQRDIKSHSKVGPVWQAVNRSRQMALENMAFQMGVGGVAKFNTMLTAMLAGDWEKAYKAGRDSLWYQQTKGRASRVTMIILTGNLESYGVEVKTPARSLSAMAATVAKSSDPADPPIPNDSRILFKEPVSSYKGEYPYVHTMETESGHIQEFDDTPGQERYRLVHPTGTYEEVSPSGRRTRKTVDNLYDITNADGNFLVAGDKKTNVGGSEIYYNMDNRLHQIDGSNTIFVRGDETKTVEGNGTILVKGNVTIIVEGNADITVKGDATTLVEGNQTNTVNGNLSWKVAGTVDWDVGGDWTEKMASMSSISSGQYTIDGSRIDIG Disordered 343 361 VKTPARSLSAMAATVAKSS Complex Native Substrate/ligand binding X-ray crystallography 285 glycerol v/v 35 PEG 8000 5.2 to 5.6%(w/v) Tris-HCl pH 7.2 to 8.0 0.65 Paper 15701513 Kanamaru S, Ishiwata Y, Suzuki T, Rossmann MG, Arisaka F 2005 J Mol Biol 346 4 1013-20 glutenin high molecular weight chain Dx5 82602 S02262 Triticum aestivum (Bread Wheat) 848 MAKRLVLFVAVVVALVALTVAEGEASEQLQCERELQELQERELKACQQVMDQQLRDISPECHPVVVSPVAGQYEQQIVVPPKGGSFYPGETTPPQQLQQRIFWGIPALLKRYYPSVTCPQQVSYYPGQASPQRPGQGQQPGQGQQGYYPTSPQQPGQWQQPEQGQPRYYPTSPQQSGQLQQPAQGQQPGQGQQGQQPGQGQPGYYPTSSQLQPGQLQQPAQGQQGQQPGQAQQGQQPGQGQQPGQGQQGQQPGQGQQPGQGQQGQQLGQGQQGYYPTSLQQSGQGQPGYYPTSLQQLGQGQSGYYPTSPQQPGQGQQPGQLQQPAQGQQPGQGQQGQQPGQGQQGQQPGQGQQPGQGQPGYYPTSPQQSGQGQPGYYPTSSQQPTQSQQPGQGQQGQQVGQGQQAQQPGQGQQPGQGQPGYYPTSPQQSGQGQPGYYLTSPQQSGQGQQPGQLQQSAQGQKGQQPGQGQQPGQGQQGQQPGQGQQGQQPGQGQPGYYPTSPQQSGQGQQPGQWQQPGQGQPGYYPTSPLQPGQGQPGYDPTSPQQPGQGQQPGQLQQPAQGQQGQQLAQGQQGQQPAQVQQGQRPAQGQQGQQPGQGQQGQQLGQGQQGQQPGQGQQGQQPAQGQQGQQPGQGQQGQQPGQGQQGQQPGQGQQPGQGQPWYYPTSPQESGQGQQPGQWQQPGQGQPGYYLTSPLQLGQGQQGYYPTSLQQPGQGQQPGQWQQSGQGQHWYYPTSPQLSGQGQRPGQWLQPGQGQQGYYPTSPQQPGQGQQLGQWLQPGQGQQGYYPTSLQQTGQGQQSGQGQQGYYSSYHVSVEHQAASLKVAKAQQLAAQLPAMCRLEGGDALSASQ Disordered - Pre-Molten Globule T-A-1 147 440 YYPTSPQQPGQWQQPEQGQPRYYPTSPQQSGQLQQPAQGQQPGQGQQGQQPGQGQPGYYPTSSQLQPGQLQQPAQGQQGQQPGQAQQGQQPGQGQQPGQGQQGQQPGQGQQPGQGQQGQQLGQGQQGYYPTSLQQSGQGQPGYYPTSLQQLGQGQSGYYPTSPQQPGQGQQPGQLQQPAQGQQPGQGQQGQQPGQGQQGQQPGQGQQPGQGQPGYYPTSPQQSGQGQPGYYPTSSQQPTQSQQPGQGQQGQQVGQGQQAQQPGQGQQPGQGQPGYYPTSPQQSGQGQPGYYLTS Fragment Raman optical activity Dynamic light scattering protein 3 to 4 mg/mL Paper 12741823 Blanch EW, Kasarda DD, Hecht L, Nielsen K, Barron LD 2003 Biochemistry 42 19 5665-73 KH-QUA2 Region Of The Xenopus Star-Gsg Quaking Protein 66361554 Xenopus laevis (African clawed frog) 140 QLQEKLYVPVKEYPDFNFVGRILGPRGLTAKQLEAETGCKIMVRGKGSMRDKKKEEQNRGKPNWEHLNEDLHVLITVEDAQNRAELKLKRAVEEVKKLLVPAAEGEDSLKKMKLMELAILNGTYRDANLKSPALHHHHHH Disordered flexible linker 103 108 AEGEDS Fragment Flexible linkers/spacers Nuclear magnetic resonance (NMR) 298 6.5 2H2O v/v 10 3,3,3-trimethylsilylpropionate 20 dithio-1,4-threitol 5 pXqua KH-QUA2 protein 1 sodium azide w/v 0.05 sodium phosphate 50 Paper 15811367 Maguire ML, Guler-Gane G, Nietlispach D, Raine AR, Zorn AM, Standart N, Broadhurst RW 2005 J Mol Biol 348 2 265-79 Disordered 122 134 GTYRDLNLKSPAL Fragment Nuclear magnetic resonance (NMR) 298 6.5 2H2O v/v 10 3,3,3-trimethysilylpropionate 20 dithio-1,4-threitol 5 pXqua KH-QUA2 protein 1 sodium azide w/v 0.05 sodium phosphate 50 Paper 15811367 Maguire ML, Guler-Gane G, Nietlispach D, Raine AR, Zorn AM, Standart N, Broadhurst RW 2005 J Mol Biol 348 2 265-79 The Maguire et. al paper has a leucine instead of an alanine at position 127, as determined by the NCBI ID. The sequence taken from the Maguire et al. article matches 99% (139/140 amino acids) with the NCBI reference. The paper has a leucine instead of an alanine at position 127. von Hippel-Lindau Tumor Suppressor G7 protein pVHL P40337 Hs.421597 P40337 4507891 P40337 Homo sapiens 213 MPRRAENWDEAEVGAEEAGVEEYGPEEDGGEESGAEESGPEESGPEELGAEEEMEAGRPRPVLRSVNSREPSQVIFCNRSPRVVLPVWLNFDGEPQPYPTLPPGTGRRIHSYRGHLWLFRDAGTHDGLLVNQTELFVPSLNVDGQPIFANITLPVYTLKERCLQVVRSLVKPENYRRLDIVRSLYEDLEDHPNVQKDLERLTQERIAHQRMGD Disordered - Molten Globule 1 213 MPRRAENWDEAEVGAEEAGVEEYGPEEDGGEESGAEESGPEESGPEELGAEEEMEAGRPRPVLRSVNSREPSQVIFCNRSPRVVLPVWLNFDGEPQPYPTLPPGTGRRIHSYRGHLWLFRDAGTHDGLLVNQTELFVPSLNVDGQPIFANITLPVYTLKERCLQVVRSLVKPENYRRLDIVRSLYEDLEDHPNVQKDLERLTQERIAHQRMGD Native Function arises from the molten globule state Unknown Unknown Near-UV circular dichroism (CD) spectroscopy 298 8 NaCl buffer 200 Tris-HCl buffer 50 Dynamic light scattering Paper 14963040 Sutovsky H, Gazit E 2004 J Biol Chem 279 17 17190-6 The physiological role of pVHL is not fully understood. However, it is suggested to play a role in protein degradation in the ubiquitin pathway and to be a regulator of multiple transcription pathways. Prevent host death protein Phd Q06253 730320 S40015 Enterobacteria phage P1 73 MQSINFRTARGNLSEVLNNVEAGEEVEITRRGREPAVIVSKATFEAYKKAALDAEFASLFDTLDSTNKELVNR Disordered 1 73 MQSINFRTARGNLSEVLNNVEAGEEVEITRRGREPAVIVSKATFEAYKKAALDAEFASLFDTLDSTNKELVNR Engineered Monomeric Function arises via a disorder to order transition Molecular assembly Protein-DNA binding Near-UV circular dichroism (CD) spectroscopy 310 EDTA buffer 0.1 NaCl buffer 100 Tris-HCl buffer (pH 7.4) 50 Paper 9915794 Gazit E, Sauer RT 1999 J Biol Chem 274 5 2652-7 EntA-im probable immunity protein 68195490 Enterococcus faecium DO 103 MKKNAKQIVHELYNDISISKDPKYSDILEVLQKVYLKLEKQKYELDPSPLINRLVNYLYFTAYTNKIRFTEYQEELIRNLSEIGRTAGINGLYRADYGDKSQF Disordered 1 3 MKK Native 2BL8A Relationship to function unknown Unknown Unknown X-ray crystallography 110 diammonium hydrogen citrate 200 PEG 3350 15 to 25% Paper 12832790 Dalhus B, Johnsen L, Nissen-Meyer J 2003 Acta Crystallogr D Biol Crystallogr 59 Pt 7 1291-3 15753083 Johnsen L, Dalhus B, Leiros I, Nissen-Meyer J 2005 J Biol Chem 280 19 19045-50 This region was disordered in chain A of the native molecule. Disordered 40 46 KQKYELD Native 2BL8A Flexible linkers/spacers X-ray crystallography 110 diammonium hydrogen citrate 200 PEG 3350 15 to 25% Paper 12832790 Dalhus B, Johnsen L, Nissen-Meyer J 2003 Acta Crystallogr D Biol Crystallogr 59 Pt 7 1291-3 15753083 Johnsen L, Dalhus B, Leiros I, Nissen-Meyer J 2005 J Biol Chem 280 19 19045-50 This region was disordered in chain A of the native molecule. Disordered 1 3 MKK Native 2BL8B Relationship to function unknown Unknown Unknown X-ray crystallography 110 diammonium hydrogen citrate 200 PEG 3350 15 to 25% Paper 12832790 Dalhus B, Johnsen L, Nissen-Meyer J 2003 Acta Crystallogr D Biol Crystallogr 59 Pt 7 1291-3 15753083 Johnsen L, Dalhus B, Leiros I, Nissen-Meyer J 2005 J Biol Chem 280 19 19045-50 This region was disordered in chain B of the native molecule. Disordered 86 103 TAGINGLYRADYGDKSQF Native 2BL8B X-ray crystallography 110 diammonium hydrogen citrate 200 PEG 3350 15 to 25% Paper 12832790 Dalhus B, Johnsen L, Nissen-Meyer J 2003 Acta Crystallogr D Biol Crystallogr 59 Pt 7 1291-3 15753083 Johnsen L, Dalhus B, Leiros I, Nissen-Meyer J 2005 J Biol Chem 280 19 19045-50 This region was disordered in chain B of the native molecule. Disordered 1 3 MKK Native 2BL8C Relationship to function unknown Unknown Unknown X-ray crystallography 110 diammonium hydrogen citrate 200 PEG 3350 15 to 25% Paper 12832790 Dalhus B, Johnsen L, Nissen-Meyer J 2003 Acta Crystallogr D Biol Crystallogr 59 Pt 7 1291-3 15753083 Johnsen L, Dalhus B, Leiros I, Nissen-Meyer J 2005 J Biol Chem 280 19 19045-50 This region was disordered in chain C of the native molecule. Disordered 82 91 EIGRTAGING Native 2BL8C Flexible linkers/spacers X-ray crystallography 110 diammonium hydrogen citrate 200 PEG 3350 15 to 25% Paper 12832790 Dalhus B, Johnsen L, Nissen-Meyer J 2003 Acta Crystallogr D Biol Crystallogr 59 Pt 7 1291-3 15753083 Johnsen L, Dalhus B, Leiros I, Nissen-Meyer J 2005 J Biol Chem 280 19 19045-50 This region was disordered in chain C of the native molecule. Disordered 1 2 MK Mutant 2BL7A Relationship to function unknown Unknown Unknown X-ray crystallography 298 PEG 3350 15 to 30% (w/v) protein 3 to 5 mg/ml 2 sodium tartrate 200 Paper 15753083 Johnsen L, Dalhus B, Leiros I, Nissen-Meyer J 2005 J Biol Chem 280 19 19045-50 This region was disordered in chain A of the mutant molecule. The mutations included two methionines being inserted in place of lysine 31 and lysine 80. Disordered 83 103 IGRTAGINGLYRADYGDKSQF Mutant 2BL7A X-ray crystallography 298 PEG 3350 15 to 30% (w/v) protein 3 to 5 mg/ml 2 sodium tartrate 200 Paper 15753083 Johnsen L, Dalhus B, Leiros I, Nissen-Meyer J 2005 J Biol Chem 280 19 19045-50 This region was disordered in chain A of the mutant molecule. The mutations included two methionines being inserted in place of lysine 31 and lysine 80. type III secretion system EscJ protein 81707043 E91200 Escherichia coli 190 MKKHIKNLFLLAAICLTVACKEQLYTGLTEKEANQMQALLLSNDVNVSKEMDKSGNMTLSVEKEDFVRAITILNNNGFPKKKFADIEVIFPPSQLVASPSQENAKINYLKEQDIERLLSKIPGVIDCSVSLNVNNNESQPSSAAVLVISSPEVNLAPSVIQIKNLVKNSVDDLKLENISVVIKSSSGQDG Disordered 60 85 SVEKEDFVRAITILNNNGFPKKKFAD Relationship to function unknown Flexible linkers/spacers Nuclear magnetic resonance (NMR) protein 250 sodium phosphate buffer (pH 7.2) Paper 15752191 Crepin VF, Prasannan S, Shaw RK, Wilson RK, Creasey E, Abe CM, Knutton S, Frankel G, Matthews S 2005 Mol Microbiol 55 6 1658-70 Dream/calsenilin DREAM 8347913 Mus musculus (Mouse) 256 MQRTKEAVKASDGSLLGDPGRIPLSKRESIKWQRPRFTRQALMRCCLIKWILSSAAPQGSDSSDSELELSTVRHQPEGLDQLQAQTKFTKKELQSLYRGFKNECPTGLVDEDTFKLIYSQFFPQGDATTYAHFLFNAFDADGNGAIHFEDFVVGLSILLRGTVHEKLKWAFNLYDINKDGCITKEEMLAIMKSIYDMMGRHTYPILREDAPLEHVERFFQKMDRNQDGVVTIDEFLETCQKDENIMNSMQLFENVI Disordered - Molten Globule DREAM-C 65 256 SELELSTVRHQPEGLDQLQAQTKFTKKELQSLYRGFKNECPTGLVDEDTFKLIYSQFFPQGDATTYAHFLFNAFDADGNGAIHFENFVVGLSILLRGTVHEKLKWAFNLYDINKDGCITKEQMLAIMKSIYDMMGRHTYPILREDAPLEHVERFFQKMDRNQDGVVTIDQFLETCQKDENIMNSMQLFENVI Fragment Mutant Function arises via a disorder to order transition Molecular assembly Protein-DNA binding Protein-protein binding Substrate/ligand binding Nuclear magnetic resonance (NMR) 305 [2H10]dithiothreitol 5 [2H11]Tris pH 7.4 10 EDTA 5 H2O/2H2O 5%/95% 0.3 KCl 50 protein 0.2 to 0.5 mM Paper 15746104 Osawa M, Dace A, Tong KI, Valiveti A, Ikura M, Ames JB 2005 J Biol Chem 280 18 18008-14 DREAM-C is a mutant containing residues 65-256 of the full length protein, and contains the mutant residues D150N, E186Q, and E234Q. Phosphorelay protein luxU Q9ZBB6 50401212 Vibrio harveyi 114 MNTDVLNQQKIEELSAEIGSDNVPVLLDIFLGEMDSYIGTLTELQGSEQLLYLKEISHALKSSAASFGADRLCERAIAIDKKAKANQLQEQGMETSEMLALLHITRDAYRSWTN Disordered 17 25 EIGSDNVPV Engineered Nuclear magnetic resonance (NMR) 294 6.4 2H2O 10 leupeptin protease inhibitor NaCl 300 pepstatin protease inhibitor Paper 15740742 Ulrich DL, Kojetin D, Bassler BL, Cavanagh J, Loria JP 2005 J Mol Biol 347 2 297-307 Disordered 86 92 NQLQEQG Engineered Nuclear magnetic resonance (NMR) 294 6.4 2H2O 10 leupeptin protease inhibitor NaCl 300 pepstatin protease inhibitor Paper 15740742 Ulrich DL, Kojetin D, Bassler BL, Cavanagh J, Loria JP 2005 J Mol Biol 347 2 297-307 Disordered 45 46 QG Engineered Nuclear magnetic resonance (NMR) 294 6.4 2H2O 10 leupeptin protease inhibitor NaCl 300 pepstatin protease inhibitor Paper 15740742 Ulrich DL, Kojetin D, Bassler BL, Cavanagh J, Loria JP 2005 J Mol Biol 347 2 297-307 Disordered 112 114 WTN Engineered Nuclear magnetic resonance (NMR) 294 6.4 2H2O 10 leupeptin protease inhibitor NaCl 300 pepstatin protease inhibitor Paper 15740742 Ulrich DL, Kojetin D, Bassler BL, Cavanagh J, Loria JP 2005 J Mol Biol 347 2 297-307 Major prion protein ASCR CD230 antigen PrP PrP27-30 PrP33-35C P04156 Homo sapiens 253 MANLGCWMLVLFVATWSDLGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGSSMVLFSSPPVILLISFLIFLIVG Disordered 23 121 KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAV Fragment Monomeric Native 1QLXA 1QLZA 1QM0A 1QM1A 1QM2A 1QM3A Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 293 4.5 H2O/D2O 90%/10% sodium acetate 10 sodium azide 0.05 Nuclear magnetic resonance (NMR) 293 4.5 D2O 99.9 sodium acetate 10 sodium azide 0.05 Paper 10618385 Zahn R, Liu A, Luhrs T, Riek R, von Schroetter C, Lopez Garcia F, Billeter M, Calzolai L, Wider G, Wuthrich K 2000 Proc Natl Acad Sci U S A 97 1 145-50 Disordered disordered loop 167 171 DEYSN Fragment Monomeric Native 1QLXA 1QLZA 1QM0A 1QM1A 1QM2A 1QM3A Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 293 4.5 H2O/D2O 90%/10% sodium acetate 10 sodium azide 0.05 Nuclear magnetic resonance (NMR) 293 4.5 D2O 99.9 sodium acetate 10 sodium azide 0.05 Paper 10618385 Zahn R, Liu A, Luhrs T, Riek R, von Schroetter C, Lopez Garcia F, Billeter M, Calzolai L, Wider G, Wuthrich K 2000 Proc Natl Acad Sci U S A 97 1 145-50 Methyl-accepting chemotaxis protein II Aspartate chemoreceptor protein MCP-II Tar P07017 Escherichia coli 553 MINRIRVVTLLVMVLGVFALLQLISGSLFFSSLHHSQKSFVVSNQLREQQGELTSTWDLMLQTRINLSRSAVRMMMDSSNQQSNAKVELLDSARKTLAQAATHYKKFKSMAPLPEMVATSRNIDEKYKNYYTALTELIDYLDYGNTGAYFAQPTQGMQNAMGEAFAQYALSSEKLYRDIVTDNADDYRFAQWQLAVIALVVVLILLVAWYGIRRMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRLAASPLTNKPQTPSRPASEQPPAQPRLRIAEQDPNWETF Disordered 524 553 PQTPSRPASEQPPAQPRLRIAEQDPNWETF Function arises from the disordered state Molecular recognition effectors Protein-protein binding Paper 15774032 Bray D 2005 Genome Biol 6 3 106 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase BPG-dependent PGAM dPGM EC 5.4.2.1 PGAM Phosphoglyceromutase P0A5R6 61225470 Mycobacterium tuberculosis 249 MANTGSLVLLRHGESDWNALNLFTGWVDVGLTDKGQAEAVRSGELIAEHDLLPDVLYTSLLRRAITTAHLALDSADRLWIPVRRSWRLNERHYGALQGLDKAETKARYGEEQFMAWRRSYDTPPPPIERGSQFSQDADPRYADIGGGPLTECLADVVARFLPYFTDVIVGDLRVGKTVLIVAHGNSLRALVKHLDQMSDDEIVGLNIPTGIPLRYDLDSAMRPLVRGGTYLDPEAAAAGAAAVAGQGRG Disordered 245 249 GQGRG Engineered Monomeric 1RIIA Function arises via a disorder to order transition Molecular recognition effectors Intraprotein interaction X-ray crystallography 298 MgCl2 0.2 PEG 3350 20 Paper 15735341 Muller P, Sawaya MR, Pashkov I, Chan S, Nguyen C, Wu Y, Perry LJ, Eisenberg D 2005 Acta Crystallogr D Biol Crystallogr 61 Pt 3 309-15 This region was disordered in chain A. This region contained an additional C-terminal His tag that was composed of the following residues: GVPRGAAALEHHHHHH. These residues were also found to be disordered in the experiment. Disordered 240 249 AAAVAGQGRG Engineered Monomeric 1RIIB Function arises via a disorder to order transition Molecular recognition effectors Intraprotein interaction X-ray crystallography 298 MgCl2 0.2 PEG 3350 20 Paper 15735341 Muller P, Sawaya MR, Pashkov I, Chan S, Nguyen C, Wu Y, Perry LJ, Eisenberg D 2005 Acta Crystallogr D Biol Crystallogr 61 Pt 3 309-15 This region was disordered in chain B. This region contained an additional C-terminal His tag that was composed of the following residues: GVPRGAAALEHHHHHH. These residues were also found to be disordered in the experiment. Disordered 239 249 GAAAVAGQGRG Engineered Monomeric 1RIIC Function arises via a disorder to order transition Molecular recognition effectors Intraprotein interaction X-ray crystallography 298 MgCl2 0.2 PEG 3350 20 Paper 15735341 Muller P, Sawaya MR, Pashkov I, Chan S, Nguyen C, Wu Y, Perry LJ, Eisenberg D 2005 Acta Crystallogr D Biol Crystallogr 61 Pt 3 309-15 This region was disordered in chain C. This region contained an additional C-terminal His tag that was composed of the following residues: GVPRGAAALEHHHHHH. These residues were also found to be disordered in the experiment. Disordered 234 249 EAAAAGAAAVAGQGRG Engineered Monomeric 1RIID Function arises via a disorder to order transition Molecular recognition effectors Intraprotein interaction X-ray crystallography 298 MgCl2 0.2 PEG 3350 20 Paper 15735341 Muller P, Sawaya MR, Pashkov I, Chan S, Nguyen C, Wu Y, Perry LJ, Eisenberg D 2005 Acta Crystallogr D Biol Crystallogr 61 Pt 3 309-15 This region was disordered in chain D. This region contained an additional C-terminal His tag that was composed of the following residues: GVPRGAAALEHHHHHH. These residues were also found to be disordered in the experiment. PemI-like protein 1 MazE protein P0AE73 882677 Escherichia coli 82 MIHSSVKRWGNSPAVRIPATLMQALNLNIDDEVKIDLVDGKLIIEPVRKEPVFTLAELVNDITPENLHENIDWGEPKDKEVW Disordered 1 3 MIH Complex 1MVFD 1MVFE Relationship to function unknown Unknown Unknown X-ray crystallography 6.5 magnesium acetate 0.2 PBS PEG 8000 20 protein 9 mg/ml sodium cacodylate 0.1 Paper 15735309 Lah J, Simic M, Vesnaver G, Marianovsky I, Glaser G, Engelberg-Kulka H, Loris R 2005 J Biol Chem 280 17 17397-407 12743116 Loris R, Marianovsky I, Lah J, Laeremans T, Engelberg-Kulka H, Glaser G, Muyldermans S, Wyns L 2003 J Biol Chem 278 30 28252-7 This region is disordered while complexed with the protein fragment VHH. Disordered 45 82 EPVRKEPVFTLAELVNDITPENLHENIDWGEPKDKEVW Complex 1MVFD 1MVFE Function arises via a disorder to molten globule transition Molecular assembly Protein-protein binding X-ray crystallography 6.5 magnesium acetate 0.2 PBS PEG 8000 20 protein 9 mg/ml sodium cacodylate 0.1 Paper 15735309 Lah J, Simic M, Vesnaver G, Marianovsky I, Glaser G, Engelberg-Kulka H, Loris R 2005 J Biol Chem 280 17 17397-407 12743116 Loris R, Marianovsky I, Lah J, Laeremans T, Engelberg-Kulka H, Glaser G, Muyldermans S, Wyns L 2003 J Biol Chem 278 30 28252-7 The PDB files have this region starting at R48. This region is disordered while complexed with the protein fragment VHH. Disordered 77 82 KDKEVW Complex 1UB4C Function arises via a disorder to molten globule transition Molecular assembly Protein-protein binding X-ray crystallography 277 4.5 DTT 10 glycerol v/v 15 NaAcetate 100 NaCl 2 protein 40 mg/ml Paper 12718874 Kamada K, Hanaoka F, Burley SK 2003 Mol Cell 11 4 875-84 15735309 Lah J, Simic M, Vesnaver G, Marianovsky I, Glaser G, Engelberg-Kulka H, Loris R 2005 J Biol Chem 280 17 17397-407 This region is disordered while complexed with the protein MazF. Apoptosis regulator Bcl-2 P10415 231632 Homo sapiens (Human) 239 MAHAGRTGYDNREIVMKYIHYKLSQRGYEWDAGDVGAAPPGAAPAPGIFSSQPGHTPHPAASRDPVARTSPLQTPAAPGAAAGPALSPVPPVVHLTLRQAGDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACITLGAYLGHK Disordered flexible loop 31 92 DAGDVGAAPPGAAPAPGIFSSQPGHTPHPAASRDPVARTSPLQTPAAPGAAAGPALSPVPPV Function arises from the disordered state Molecular assembly Protein-protein binding X-ray crystallography Nuclear magnetic resonance (NMR) Paper 15733859 Kang CB, Tai J, Chia J, Yoon HS 2005 FEBS Lett 579 6 1469-76 BCLX_HUMAN Q07817 728955 Homo sapiens (Human) 233 MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEGTESEMETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIAAWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK Disordered 28 80 SDVEENRTEAPEGTESEMETPSAINGNPSWHLADSPAVNGATGHSSSLDAREV Engineered Fragment Monomeric 1LXLA 1R2GA X-ray crystallography ammonium acetate 0.2 PEG 4000 28-31% (w/v) protein 25 mg/ml sodium citrate pH 7.5 0.1 Tris pH 7.4 50 Nuclear magnetic resonance (NMR) 303 H2O/2H2O 9/1 perdeuterated DTT 5 perdeuterated EDTA 1 protein 1-3 nM sodium phosphate pH 7.3 20 Nuclear magnetic resonance (NMR) 303 2H2O perdeuterated DTT 5 perdeuterated EDTA 1 protein 1-3 nM sodium phosphate pH 7.3 20 Paper 8692274 Muchmore SW, Sattler M, Liang H, Meadows RP, Harlan JE, Yoon HS, Nettesheim D, Chang BS, Thompson CB, Wong SL, Ng SL, Fesik SW 1996 Nature 381 6580 335-41 The PDB file 1R2G has this region being disordered from S28 to I81. Disordered 101 103 YRR Engineered Fragment Monomeric 1LXLA 1MAZA 1R2DA Relationship to function unknown Unknown Unknown X-ray crystallography ammonium acetate 0.2 PEG 4000 28-31% (w/v) protein 25 mg/ml sodium citrate pH 7.5 0.1 Tris pH 7.4 50 Nuclear magnetic resonance (NMR) 303 H2O/2H2O 9/1 perdeuterated DTT 5 perdeuterated EDTA 1 protein 1-3 nM sodium phosphate pH 7.3 20 Nuclear magnetic resonance (NMR) 303 2H2O perdeuterated DTT 5 perdeuterated EDTA 1 protein 1-3 nM sodium phosphate pH 7.3 20 Paper 8692274 Muchmore SW, Sattler M, Liang H, Meadows RP, Harlan JE, Yoon HS, Nettesheim D, Chang BS, Thompson CB, Wong SL, Ng SL, Fesik SW 1996 Nature 381 6580 335-41 Disordered 28 81 SDVEENRTEAPEGTESEMETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVI 1MAZA 1R2DA 1R2HA 1R2IA Paper 14534311 Manion MK, O'Neill JW, Giedt CD, Kim KM, Zhang KY, Hockenbery DM 2004 J Biol Chem 279 3 2159-65 Disordered 197 209 NNAAAESRKGQER 1R2DA Paper 14534311 Manion MK, O'Neill JW, Giedt CD, Kim KM, Zhang KY, Hockenbery DM 2004 J Biol Chem 279 3 2159-65 Disordered 197 218 NNAAAESRKGQERLEHHHHHH Engineered Fragment 1R2DA 1R2GA 1R2HA 1RDEA Paper 14534311 Manion MK, O'Neill JW, Giedt CD, Kim KM, Zhang KY, Hockenbery DM 2004 J Biol Chem 279 3 2159-65 This disordered region contains an extra poly-histine tail at the C-terminus of the fragment that was added in the experiment to facilitate purification. Disordered 28 79 SDVEENRTEAPEGTESEMETPSAINGNPSWHLADSPAVNGATGHSSSLDARE 1R2EA Paper 14534311 Manion MK, O'Neill JW, Giedt CD, Kim KM, Zhang KY, Hockenbery DM 2004 J Biol Chem 279 3 2159-65 Disordered 198 218 NAAAESRKGQERLEHHHHHH Engineered Fragment 1R2IA Paper 14534311 Manion MK, O'Neill JW, Giedt CD, Kim KM, Zhang KY, Hockenbery DM 2004 J Biol Chem 279 3 2159-65 This disordered region contains an extra poly-histine tail at the C-terminus of the fragment that was added in the experiment to facilitate purification. PemK-like protein 1 MazF protein P33645 464357 Escherichia coli 111 MVSRYVPDMGDLIWVDFDPTKGSEQAGHRPAVVLSPFMYNNKTGMCLCVPCTTQSKGYPFEVVLSGQERDGVALADQVKSIAWRARGATKKGTVAPEELQLIKAKINVLIG Disordered S1-S2 loop 20 26 TKGSEQA Complex 1UB4B Function arises from the disordered state Molecular assembly Protein-protein binding X-ray crystallography 277 4.5 DTT 10 glycerol v/v 15 NaAcetate 100 NaCl 2 protein complex 40 mg/ml Paper 12718874 Kamada K, Hanaoka F, Burley SK 2003 Mol Cell 11 4 875-84 Molecule B Disordered S1-S2 loop 18 27 DPTKGSEQAG Complex 1UB4A Function arises from the disordered state Molecular assembly Protein-protein binding X-ray crystallography 277 4.5 DTT 10 glycerol v/v 15 NaAcetate 100 NaCl 2 protein complex 40 mg/ml Paper 12718874 Kamada K, Hanaoka F, Burley SK 2003 Mol Cell 11 4 875-84 Molecule A Disordered 67 71 QERDG Complex Relationship to function unknown Unknown Unknown X-ray crystallography 277 4.5 DTT 10 glycerol v/v 15 NaAcetate 100 NaCl 2 protein complex 40 mg/ml Paper 12718874 Kamada K, Hanaoka F, Burley SK 2003 Mol Cell 11 4 875-84 methyl-accepting chemotaxis protein I MCP-I Serine chemoreceptor protein tsr P02942 16132176 Escherichia coli 551 MLKRIKIVTSLLLVLAVFGLLQLTSGGLFFNALKNDKENFTVLQTIRQQQSTLNGSWVALLQTRNTLNRAGIRYMMDQNNIGSGSTVAELMESASISLKQAEKNWADYEALPRDPRQSTAAAAEIKRNYDIYHNALAELIQLLGAGKINEFFDQPTQGYQDGFEKQYVAYMEQNDRLHDIAVSDNNASYSQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIQQQQRETSAVVKTVTPAAPRKMAVADSEENWETF Disordered 521 551 QRETSAVVKTVTPAAPRKMAVADSEENWETF Function arises from the disordered state Molecular recognition effectors Protein-protein binding Paper 15774032 Bray D 2005 Genome Biol 6 3 106 Dihydrofolate reductase DHFR EC 1.5.1.3 P0ABQ5 Escherichia coli 159 MISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPGTDDRVTWVKSVDEAIAACGDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILERR Disordered Met20 loop 9 24 AVDRVIGMENAMPWNL Complex 1DDRA 1DDRB 1DDSA 1DDSB Function arises via a disorder to order transition Substrate/ligand binding X-ray crystallography Paper 9012674 Sawaya MR, Kraut J 1997 Biochemistry 36 3 586-603 14717591 Schnell JR, Dyson HJ, Wright PE 2004 Biochemistry 43 2 374-83 Disordered F-G loop 116 132 DAEVEGDTHFPDYEPDD Complex 1DDRA 1DDRB 1DDSA 1DDSB Function arises via a disorder to order transition Substrate/ligand binding X-ray crystallography Paper 9012674 Sawaya MR, Kraut J 1997 Biochemistry 36 3 586-603 14717591 Schnell JR, Dyson HJ, Wright PE 2004 Biochemistry 43 2 374-83 Disordered G-H loop 142 150 DADAQNSHS Complex 1DDRA 1DDRB 1DDSA 1DDSB Function arises via a disorder to order transition Substrate/ligand binding X-ray crystallography Paper 9012674 Sawaya MR, Kraut J 1997 Biochemistry 36 3 586-603 14717591 Schnell JR, Dyson HJ, Wright PE 2004 Biochemistry 43 2 374-83 Disordered 63 72 SSQPGTDDRV Complex 1DDRA 1DDRB 1DDSA 1DDSB Function arises via a disorder to order transition Unknown Unknown X-ray crystallography Paper 9012674 Sawaya MR, Kraut J 1997 Biochemistry 36 3 586-603 14717591 Schnell JR, Dyson HJ, Wright PE 2004 Biochemistry 43 2 374-83 Disordered Met20 loop 16 20 MENAM Complex 5DFRA 6DFRA Function arises via a disorder to order transition Molecular assembly Substrate/ligand binding X-ray crystallography 277 DHFR 40 to 50 mg/ml X-ray crystallography 298 CaCl2 50 imidazole pH 7.0 20 imidazole (second aliquot) pH 7.2 60 PEG 6000 (w/v) 25 Paper 9012674 Sawaya MR, Kraut J 1997 Biochemistry 36 3 586-603 14717591 Schnell JR, Dyson HJ, Wright PE 2004 Biochemistry 43 2 374-83 PDB ID 5DFR had V10, L28, E120, D122, and D127 containing disordered side chains. PDB ID 6DFR had the side chains beyond the CB of E120 and D127 being disordered. Disordered 95 96 GG Complex 5DFRA Relationship to function unknown Unknown Unknown X-ray crystallography 277 Paper 9012674 Sawaya MR, Kraut J 1997 Biochemistry 36 3 586-603 14717591 Schnell JR, Dyson HJ, Wright PE 2004 Biochemistry 43 2 374-83 Disordered Met20 loop 16 22 MENAMPW Complex 1RG7A Function arises via a disorder to order transition Molecular assembly Substrate/ligand binding X-ray crystallography CaCl2 50 imidazole pH 7.0 20 imidazole (second aliquot) pH 7.2 60 PEG 6000 w/v 25 Paper 9012674 Sawaya MR, Kraut J 1997 Biochemistry 36 3 586-603 14717591 Schnell JR, Dyson HJ, Wright PE 2004 Biochemistry 43 2 374-83 Stringent starvation protein A SspA 22124052 Yersinia pestis 213 MAVAANKRSVMTLFSGPTDIFSHQVRIVLAEKGVSVEIEQVEADNLPQDLIDLNPYRTVPTLVDRELTLYESRIIMEYLDERFPHPPLMPVYPVARGSSRLMMHRIEHDWYSLLYKIEQGNAQEAEAARKQLREELLSIAPVFNETPFFMSEEFSLVDCYLAPLLWRLPVLGIEFTGAGSKELKGYMTRVFERDAFLASLTEAEREMHLKTRS Disordered 1 9 MAVAANKRS 1YY7B Relationship to function unknown Unknown Transactivation (transcriptional activation) X-ray crystallography Paper 15735307 Hansen AM, Gu Y, Li M, Andrykovitch M, Waugh DS, Jin DJ, Ji X 2005 J Biol Chem 280 17 17380-91 Disordered alpha-2 helix 48 53 QDLIDL Function arises from the disordered state Molecular recognition effectors Transactivation (transcriptional activation) X-ray crystallography Paper 15735307 Hansen AM, Gu Y, Li M, Andrykovitch M, Waugh DS, Jin DJ, Ji X 2005 J Biol Chem 280 17 17380-91 Disordered 204 212 EREMHLKTR 1YY7A Relationship to function unknown Unknown Transactivation (transcriptional activation) X-ray crystallography Paper 15735307 Hansen AM, Gu Y, Li M, Andrykovitch M, Waugh DS, Jin DJ, Ji X 2005 J Biol Chem 280 17 17380-91 Myoglobin P02185 127687 Physeter catodon (Sperm whale) 153 VLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETLEKFDRFKHLKTEAEMKASEDLKKHGVTVLTALGAILKKKGHHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHPGDFGADAQGAMNKALELFRKDIAAKYKELGYQG Disordered C Helix 36 42 HPETLEK Engineered Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 308 6 1H2O 95 2H2O 5 Mes buffer 20 Paper 12079388 Kitahara R, Yamada H, Akasaka K, Wright PE 2002 J Mol Biol 320 2 311-9 8844864 Lecomte JT, Kao YH, Cocco MJ 1996 Proteins 25 3 267-85 This region becomes disordered between a pressure change of 500 and 1200 bar. Disordered CD loop 43 49 FDRFKHL Engineered Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 308 6 1H2O 95 2H2O 5 Mes buffer 20 Paper 12079388 Kitahara R, Yamada H, Akasaka K, Wright PE 2002 J Mol Biol 320 2 311-9 8844864 Lecomte JT, Kao YH, Cocco MJ 1996 Proteins 25 3 267-85 This region becomes disordered between a pressure change of 500 and 1200 bar. Disordered F Helix 86 94 LKPLAQSHA Engineered Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 308 6 1H2O 95 2H2O 5 Mes buffer 20 Paper 12079388 Kitahara R, Yamada H, Akasaka K, Wright PE 2002 J Mol Biol 320 2 311-9 8844864 Lecomte JT, Kao YH, Cocco MJ 1996 Proteins 25 3 267-85 This region is the only disordered region for the natively folded protein when at a pressure of 30 bar. Disordered G Helix 100 118 PIKYLEFISEAIIHVLHSR Engineered Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) 308 6 1H2O 95 2H2O 5 Mes buffer 20 Paper 12079388 Kitahara R, Yamada H, Akasaka K, Wright PE 2002 J Mol Biol 320 2 311-9 8844864 Lecomte JT, Kao YH, Cocco MJ 1996 Proteins 25 3 267-85 This region becomes disordered between a pressure change of 500 and 1200 bar. Disordered 82 101 HEAELKPLAQSHATKHKIPI Engi