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 L45 P02400 133071 A35109 Saccharomyces cerevisiae (Baker's yeast) 110 MKYLAAYLLLVQGGNAAPSAADIKAVVESVGAEVDEARINELLSSLEGKGSLEEIIAEGQKKFATVPTGGASSAAAGAAGAAAGGDAAEEEKEEEAKEESDDDMGFGLFD Disordered 1 110 MKYLAAYLLLVQGGNAAPSAADIKAVVESVGAEVDEARINELLSSLEGKGSLEEIIAEGQKKFATVPTGGASSAAAGAAGAAAGGDAAEEEKEEEAKEESDDDMGFGLFD Native Relationship to function unknown Molecular assembly Protein-protein binding Far-UV circular dichroism (CD) 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 Ordered 332 400 SNTDARCCVHDAACPANQFSGKSCGMFFSEGAKAQVAFKQIKAFMQALYPNAQTGHGHLLMPLRCECNS 1ADTA 1ADVA 1ADVB 1ANVA Paper Ordered 407 452 FLGRQLPKLTPFALSNAEDLDADLISDKSVLASVHHPALIVFQCCN 1ADTA 1ADVA 1ADVB 1ANVA Paper Ordered 465 529 PNCDFKISAPDLLNALVMVRSLWSENFTELPRMVVPEFKWSTKHQYRNVSLPVAHSDARQNPFDF 1ADTA 1ADVA 1ADVB 1ANVA Paper 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 Cytochrome c Apocytochrome c P00004 117995 A00005 Equus caballus (Horse) 104 GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWKEETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE Disordered 1 104 GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWKEETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE Paper 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 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 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 1023-1034 This structure is refered to as 'form II' in Beernink (2001). 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 1023-1034 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 1023-1034 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 1023-1034 The experimental sequence did not contain the N-terminal residues 1-35. This structure is refered to as 'form I' in Beernink (2001). 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 11286553 Beernink PT, Segelke BW, Hadi MZ, Erzberger JP, Wilson DM 3rd, Rupp B 2001 J Mol Biol 307 4 1023-1034 9351835 Gorman MA, Morera S, Rothwell DG, de La Fortelle E, Mol CD, Tainer JA, Hickson ID, Freemont PS 1997 Embo J 16 21 6548-58 This region is not essential for function (Gorman 1997). This structure is refered to as 'form III' in Beernink (2001) Disordered - Extended 124 125 DK Complex Native 1E9NA 1E9NB Relationship to function unknown Unknown 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 11286553 Beernink PT, Segelke BW, Hadi MZ, Erzberger JP, Wilson DM 3rd, Rupp B 2001 J Mol Biol 307 4 1023-1034 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 Alpha-S1 casein [Precursor] P02662 1070620 KABOSB Bos taurus (Bovine) 214 MKLLILTCLVAVALARPKHPIKHQGLPQEVLNENLLRFFVAPFPEVFGKEKVNELSKDIGSESTEDQAMEDIKQMEAESISSSEEIVPNSVEQKHIQKEDVPSERYLGYLEQLLRLKKYKVPQLEIVPNSAEERLHSMKEGIHAQQKEPMIGVNQELAYFYPELFRQFYQLDAYPSGAWYYVPLGTQYTDAPSFSDIPNPIGSENSEKTTMPLW Disordered 16 214 RPKHPIKHQGLPQEVLNENLLRFFVAPFPEVFGKEKVNELSKDIGSESTEDQAMEDIKQMEAESISSSEEIVPNSVEQKHIQKEDVPSERYLGYLEQLLRLKKYKVPQLEIVPNSAEERLHSMKEGIHAQQKEPMIGVNQELAYFYPELFRQFYQLDAYPSGAWYYVPLGTQYTDAPSFSDIPNPIGSENSEKTTMPLW Paper 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 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 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 Disordered 386 445 TVTTHSSDSEVPSRVTEVVVKLFDSDPITVVLPEEVSKDNPKFMDTVAEKALQEYRRKSR Paper 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 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 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 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 Elongation factor G Elongation Factor G Without Nucleotide P13551 1827912 Thermus thermophilus 691 MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERERGITITAAVTTCFWKDHRINIIDTPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSETVWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDVLRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEEELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVEIHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHANHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKADQEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDANVGKPQVAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIPAVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYHEVDSSEMAFKIAGSMAIKEAVQKGDPVILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLRSKTQGRGSFVMFFDHYQEVPKQVQEKLIKGQ Disordered 40 67 HKIGEVHEGAATMDFMEQERERGITITA Paper Disordered 400 475 ESIEVPEPVIDVAIEPKTKADQEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDAN Paper EMB-1 protein Embryonic abundant protein from carrot P17639 119316 JQ2273 Daucus carota (Carrot) 92 MASQQEKKELDARARQGETVVPGGTGGKSLEAQQHLAEGRSKGGQTRKEQLGGEGYHEMGRKGGLSNNDMSGGERAEQEGIDIDESKFRTKK Disordered 1 92 MASQQEKKELDARARQGETVVPGGTGGKSLEAQQHLAEGRSKGGQTRKEQLGGEGYHEMGRKGGLSNNDMSGGERAEQEGIDIDESKFRTKK Paper 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 Flagellin Phase-1-I flagellin P06179 96744 S16121 Salmonella typhimurium 494 AQVINTNSLSLLTQNNLNKSQSALGTAIERLSSGLRINSAKDDAAGQAIANRFTANIKGLTQASRNANDGISIAQTTEGALNEINNNLQRVRELAVQSANSTNSQSDLDSIQAEITQRLNEIDRVSGQTQFNGVKVLAQDNTLTIQVGANDGETIDIDLKQINSQTLGLDTLNVQQKYKVSDTAATVTGYADTTIALDNSTFKASATGLGGTDQKIDGDLKFDDTTGKYYAKVTVTGGTGKDGYYEVSVDKTNGEVTLAGGATSPLTGGLPATATEDVKNVQVANADLTEAKAALTAAGVTGTASVVKMSYTDNNGKTIDGGLAVKVGDDYYSATQNKDGSISINTTKYTADDGTSKTALNKLGGADGKTEVVSIGGKTYAASKAEGHNFKAQPDLAEAAATTTENPLQKIDAALAQVDTLRSDLGAVQNRFNSAITNLGNTVNNLTSARSRIEDSDYATEVSNMSRAQILQQAGTSVLAQANQVPQNVLSLLR Disordered 1 55 AQVINTNSLSLLTQNNLNKSQSALGTAIERLSSGLRINSAKDDAAGQAIANRFTA Paper Disordered 451 494 SRIEDSDYATEVSNMSRAQILQQAGTSVLAQANQVPQNVLSLLR Paper 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 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 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 273 7 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 39 in chain A, LYS 38 in chain B, GLY 41 in chain C, and GLY 41 in chain D. This is supported by claims in the Eigenbrot paper as being dependent upon 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 273 7 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 Ordered 174 211 VGQACCRPVAFDDDLSFLDDSLVYHILRKHSAKRCGCI 1AGQA 1AGQB 1AGQC 1AGQD Paper Glucocorticoid receptor GR P04150 Hs.126608 P04150 4758482 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 Glycyl-tRNA synthetase Glycyl-tRNA ligase 1B76_B Thermus thermophilus 442 AASSLDELVALCKRRGFIFQSSEIYGGLQGVYDYGPLGVELKNNLKQAWWRRNVYERDDMEGLDASVLTHRLVLHYSGHEATFADPMVDNAKARYWTPPRYFNMMFQDLRGPRGGRGLLAYLRPETAQGIFVNFKNVLDATSRKLGFGIAQIGKAFRNEITPRNFIFRVREFEQMEIEYFVRPGEDEYWHRYWVEERLKWWQEMGLSRENLVPYQQPPESSAHYAKATVDILYRFPHGSLELEGIAQRTDFDLGSHTKDQEALGITARVLRNEHSTQRLAYRDPETGKWFVPYVIEPSAGVDRGVLALLAEAFTREELPNGEERIVLKLKPQLAPIKVAVIPLVKNRPEITEYAKRLKARLLALGLGRVLYEDTGNIGKAYRRHDEVGTPFAVTVDYDTIGQSKDGTTRLKDTVTVRDRDTMEQIRLHVDELEGFLRERLRW Disordered 96 158 WTPPRYFNMMFQDLRGPRGGRGLLAYLRPETAQGIFVNFKNVLDATSRKLGFGIAQIGKAFRN Paper 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 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 Heat shock factor protein Heat shock transcription factor HSF HSTF P22121 123686 S13365 Kluyveromyces lactis (Yeast) 677 MGHNDSVETMDEISNPNNILLPHDGTGLDATGISGSQEPYGMVDVLNPDSLKDDSNVDEPLIEDIVNPSLDPEGVVSAEPSNEVGTPLLQQPISLDHVITRPASAGGVYSIGNSSTSSAAKLSDGDLTNATDPLLNNAHGHGQPSSESQSHSNGYHKQGQSQQPLLSLNKRKLLAKAHVDKHHSKKKLSTTRARPAFVNKLWSMVNDKSNEKFIHWSTSGESIVVPNRERFVQEVLPKYFKHSNFASFVRQLNMYGWHKVQDVKSGSMLSNNDSRWEFENENFKRGKEYLLENIVRQKSNTNILGGTTNAEVDIHILLNELETVKYNQLAIAEDLKRITKDNEMLWKENMMARERHQSQQQVLEKLLRFLSSVFGPNSAKTIGNGFQPDLIHELSDMQVNHMSNNNHNNTGNINPNAYHNETDDPMANVFGPLTPTDQGKVPLQDYKLRPRLLLKNRSMSSSSSSNLNQRQSPQNRIVGQSPPPQQQQQQQQQQGQPQGQQFSYPIQGGNQMMNQLGSPIGTQVGSPVGSQYGNQYGNQYSNQFGNQLQQQTSRPALHHGSNGEIRELTPSIVSSDSPDPAFFQDLQNNIDKQEESIQEIQDWITKLNPGPGEDGNTPIFPELNMPSYFANTGGSGQSEQPSDYGDSQIEELRNSRLHEPDRSFEEKNNGQKRRRAA Disordered 1 196 MGHNDSVETMDEISNPNNILLPHDGTGLDATGISGSQEPYGMVDVLNPDSLKDDSNVDEPLIEDIVNPSLDPEGVVSAEPSNEVGTPLLQQPISLDHVITRPASAGGVYSIGNSSTSSAAKLSDGDLTNATDPLLNNAHGHGQPSSESQSHSNGYHKQGQSQQPLLSLNKRKLLAKAHVDKHHSKKKLSTTRARPA Paper 8745404 Cho HS, Liu CW, Damberger FF, Pelton JG, Nelson HC, Wemmer DE 1996 Protein Sci 5 2 262-9 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 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 Sensitivity to proteolysis Paper 8384699 Ramakrishnan, V. Finch, J. T. Graziano, V. Lee, P. L. Sweet, R. M. 1993 Nature 362 6417 219-223 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 Sensitivity to proteolysis Paper 8384699 Ramakrishnan, V. Finch, J. T. Graziano, V. Lee, P. L. Sweet, R. M. 1993 Nature 362 6417 219-223 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 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 Negative factor 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 Disordered - Extended 148 178 VEPDKVEEANKGENTSLLHPVSLHGMDDPER 1AVVA 1AVZA 1EFNA 1QA4A Relationship to function unknown Unknown Unknown Nuclear magnetic resonance (NMR) X-ray crystallography Paper Ordered 74 147 VPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPGPGVRYPLTFGWCYKLVP 1AVVA Paper Ordered 179 203 EVLEWRFDSRLAFHHVARELHPEYF 1AVVA Paper 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 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. Major prion protein [Precursor] PrP PrP27-30 PrP33-35C P04925 200527 Mus musculus (Mouse) 254 MANLGYWLLALFVTMWTDVGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAVSRPMIHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYDGRRSSSTVLFSSPPVILLISFLIFLIVG Disordered 23 119 KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGA Paper Sperm histone Galline Protamine P15340 123705 A34320 Gallus gallus (Chicken) 62 MARYRRSRTRSRSPRSRRRRRRSGRRRSPRRRRRYGSARRSRRSVGGRRRRYGSRRRRRRRY Disordered 1 62 MARYRRSRTRSRSPRSRRRRRRSGRRRSPRRRRRYGSARRSRRSVGGRRRRYGSRRRRRRRY Paper Prothymosin alpha P06302 135836 TNRTA Rattus norvegicus (Rat) 112 MSDAAVDTSSEITTKDLKEKKEVVEEAENGRDAPANGNAQNEENGEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGDEDEEAEAPTGKRVAEDDEDDDVETKKQKKTDEDD Disordered 1 112 MSDAAVDTSSEITTKDLKEKKEVVEEAENGRDAPANGNAQNEENGEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGDEDEEAEAPTGKRVAEDDEDDDVETKKQKKTDEDD Paper Myc proto-oncogene protein c-myc P01106 127619 Homo sapiens (Human) 439 MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENVKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEEDLLRKRREQLKHKLEQLRNSCA Disordered 1 143 MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAK Paper Disordered - Extended 406 434 VQAEEQKLISEEDLLRKRREQLKHKLEQL Paper Replication protein A 70 kDa DNA-binding subunit Replication factor-A protein 1 RF-A RP-A Single-stranded DNA-binding protein P27694 1350579 A40457 Homo sapiens (Human) 616 MVGQLSEGAIAAIMQKGDTNIKPILQVINIRPITTGNSPPRYRLLMSDGLNTLSSFMLATQLNPLVEEEQLSSNCVCQIHRFIVNTLKDGRRVVILMELEVLKSAEAVGVKIGNPVPYNEGLGQPQVAPPAPAASPAASSRPQPQNGSSGMGSTVSKAYGASKTFGKAAGPSLSHTSGGTQSKVVPIASLTPYQSKWTICARVTNKSQIRTWSNSRGEGKLFSLELVDESGEIRATAFNEQVDKFFPLIEVNKVYYFSKGTLKIANKQFTAVKNDYEMTFNNETSVMPCEDDHHLPTVQFDFTGIDDLENKSKDSLVDIIGICKSYEDATKITVRSNNREVAKRNIYLMDTSGKVVTATLWGEDADKFDGSRQPVLAIKGARVSDFGGRSLSVLSSSTIIANPDIPEAYKLRGWFDAEGQALDGVSISDLKSGGVGGSNTNWKTLYEVKSENLGQGDKPDYFSSVATVVYLRKENCMYQACPTQDCNKKVIDQQNGLYRCEKCDTEFPNFKYRMILSVNIADFQENQWVTCFQESAEAILGQNAAYLGELKDKNEQAFEEVFQNANFRSFIFRVRVKVETYNDESRIKATVMDVKPVDYREYGRRLVMSIRRSALM Disordered 115 168 PVPYNEGLGQPQVAPPAPAASPAASSRPQPQNGSSGMGSTVSKAYGASKTFGKA Paper Retinoic acid receptor RXR-alpha Retinoid X receptor, alpha [Homo sapiens] 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 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 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 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 6.8 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 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. Ordered 225 462 SANEDMPVERILEAELAVEPKTETYVEANMGLNPSSPNDPVTNICQAADKQLFTLVEWAKRIPHFSELPLDDQVILLRAGWNELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGVGAIFDRVLTELVSKMRDMQMDKTELGCLRAIVLFNPDSKGLSNPAEVEALREKVYASLEAYCKHKYPEQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQMT 1LBDA Paper Regulator of G-protein signaling 4 RGP4 RGS4 Signal transduction inhibitor RGS4 P49799 1710149 Rattus norvegicus (Rat) 205 MCKGLAGLPASCLRSAKDMKHRLGFLLQKSDSCEHSSSHSKKDKVVTCQRVSQEEVKKWAESLENLINHECGLAAFKAFLKSEYSEENIDFWISCEEYKKIKSPSKLSPKAKKIYNEFISVQATKEVNLDSCTREETSRNMLEPTITCFDEAQKKIFNLMEKDSYRRFLKSRFYLDLTNPSSCGAEKQKGAKSSADCTSLVPQCA Disordered 1 50 MCKGLAGLPASCLRSAKDMKHRLGFLLQKSDSCEHSSSHSKKDKVVTCQR Paper Disordered 179 205 NPSSCGAEKQKGAKSSADCTSLVPQCA Paper 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 Structural polyprotein P130 1942972 Sindbis virus (subtype Ockelbo / strain Edsbyn 82-5) 264 MNRGFFNMLGRRPFPAPTAMWRPRRRRQAAPMPARNGLASQIQQLTTAVSALVIGQATRPQNPRPRPPPRQKKQAPKQPPKPKKPKPQEKKKKQPAKTKPGKRQRMALKLEADRLFDVKNEDGDVIGHALAMEGKVMKPLHVKGTIDHPVLSKLKFTKSSAYDMEFAQLPVNMRSEAFTYTSEHPEGFYNWHHGAVQYSGGRFTIPRGVGGRGDSGRPIMDNSGRVVAIVLGGADEGTRTALSVVTWNSKGKTIKTTPEGTEEW Disordered 1 106 MNRGFFNMLGRRPFPAPTAMWRPRRRRQAAPMPARNGLASQIQQLTTAVSALVIGQATRPQNPRPRPPPRQKKQAPKQPPKPKKPKPQEKKKKQPAKTKPGKRQRM Paper This sequence is post processing Small heat shock protein HSP16.5 Q57733 2495337 F64335 Methanococcus jannaschii 147 MFGRDPFDSLFERMFKEFFATPMTGTTMIQSSTGIQISGKGFMPISIIEGDQHIKVIAWLPGVNKEDIILNAVGDTLEIRAKRSPLMITESERIIYSEIPEEEEIYRTIKLPATVKEENASAKFENGVLSVILPKAESSIKKGINIE Disordered 1 32 MFGRDPFDSLFERMFKEFFATPMTGTTMIQSS Paper SNAP-25 206 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 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 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 Function arises via a disorder to order transition 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 [Fragment] Titin, skeletal Q10465 1017427 I38346 Homo sapiens (Human) 7962 PDQEMPVYPPAIITPLQDTVTSEGQPARFQCRVSGTDLKVSWYSKDKKIKPSRFFRMTQFEDTYQLEIAEAYPEDEGTYTFVANNAVGQVSSTANLSLEAPESILHERIEQEIEMEMKAAPVIKRKIEPLEVALGHLAKFTCEIQSAPNVRFQWFKAGREIYESDKCSIRSSKYISSLEILRTQVVDCGEYTCKASNEYGSVSCTATLTVTEAYPPTFLSRPKSLTTFVGKAAKFICTVTGTPVIETIWQKDGAALSPSPNWRISDAENKHILELSNLTIQDRGVYSCKASNKFGADICQAELIIIDKPHFIKELEPVQSAINKKVHLECQVDEDRKVTVTWSKDGQKLPPGKDYKICFEDKIATLEIPLAKLKDSGTYVCTASNEAGSSSCSATVTVREPPSFVKKVDPSYLMLPGESARLHCKLKGSPVIQVTWFKNNKELSESNTVRMYFVNSEAILDITDVKVEDSGSYSCEAVNDVGSDSCSTEIVIKEPPSFIKTLEPADIVRGTNALLQCEVSGTGPFEISWFKDKKQIRSSKKYRLFSQKSLVCLEIFSFNSADVGEYECVVANEVGKCGCMATHLLKEPPTFVKKVDDLIALGGQTVTLQAAVRGSEPISVTWMKGQEVIREDGKIKMSFSNGVAVLIIPDVQISFGGKYTCLAENEAGSQTSVGELIVKEPAKIIERAELIQVTAGDPATLEYTVAGTPELKPKWYKDGRPLVASKKYRISFKNNVAQLKFYSAELHDSGQYTFEISNEVGSSSCETTFTVLDRDIAPFFTKPLRNVDSVVNGTCRLDCKIAGSLPMRVSWFKDGKEIAASDRYRIAFVEGTASLEIIRVDMNDAGNFTCRATNSVGSKDSSGALIVQEPPSFVTKPGSKDVLPGSAVCLKSTFQGSTPLTIRWFKGNKELVSGGSCYITKEALESSLELYLVKTSDSGTYTCKVSNVAGGVECSANLFVKEPATFVEKLEPSQLLKKGDATQLACKVTGTPPIKITWFANDREIKESSKHRMSFVESTAVLRLTDVGIEDSGEYMCEAQNEAGSDHCSSIVIVKESPYFTKEFKPIEVLKEYDVMLLAEVAGTPPFEITWFKDNTILRSGRKYKTFIQDHLVSLQILKFVAADAGEYQCRVTNEVGSSICSARVTLREPPSFIKKIESTSSLRGGTAAFQATLKGSLPITVTWLKDSDEITEDDNIRMTFENNVASLYLSGIEVKHDGKYVCQAKNDAGIQRCSALLSVKEPATITEEAVSIDVTQGDPATLQVKFSGTKEITAKWFKDGQELTLGSKYKISVTDTVSILKIISTEKKDSGEYTFEVQNDVGRSSCKARINVLDLIIPPSFTKKLKKMDSIKGSFIDLECIVAGSHPISIQWFKDDQEISASEKYKFSFHDNTAFLEISQLEGTDSGTYTCSATNKAGHNQCSGHLTVKEPPYFVEKPQSQDVNPNTRVQLKALVGGTAPMTIKWFKDNKELHSGAARSVWKDDTSTSLELFAAKATDSGTYICQLSNDVGTATSKATLFVKEPPQFIKKPSPVLVLRNGQSTTFECQITGTPKIRVSWYLDGNEITAIQKHGISFIDGLATFQISGARVENSGTYVCEARNDAGTASCSIELKVKEPPTFIRELKPVEVVKYSDVELECEVTGTPPFEVTWLKNNREIRSSKKYTLTDRVSVFNLHITKCDPSDTGEYQCIVSNEGGSCSCSTRVALKEPPSFIKKIENTTTVLKSSATFQSTVAGSPPISITWLKDDQILDEDDNVYISFVDSVATLQIRSVDNGHSGRYTCQAKNESGVERCYAFLLVQEPAQIVEKAKSVDVTEKDPMTLECVVAGTPELKVKWLKDGKQIVPSRYFSMSFENNVASFRIQSVMKQDSGQYTFKVENDFGSSSCDAYLRVLDQNIPPSFTKKLTKMDKVLGSSIHMECKVSGSLPISAQWFKDGKEISTSAKYRLVCHERSVSLEVNNLELEDTANYTCKVSNVAGDDACSGILTVKEPPSFLVKPGRQQAIPDSTVEFKAILKGTPPFKIKWFKDDVELVSGPKCFIGLEGSTSFLNLYSVDASKTGQYTCHVTNDVGSDSCTTMLLVTEPPKFVKKLEASKIVKAGDSSRLECKIAGSPEIRVVWFRNEHELPASDKYRMTFIDSVAVIQMNNLSTEDSGDFICEAQNPAGSTSCSTKVIVKEPPVFSSFPPIVETLKNAEVSLECELSGTPPFEVVWYKDKRQLRSSKKYKIASKNFHTSIHILNVDTSDIGEYHCKAQNEVGSDTCVCTVKLKEPPRFVSKLNSLTVVAGEPAELQASIEGAQPIFVQWLKEKEEVIRESENIRITFVENVATLQFAKAEPANAGKYICQIKNDGGMRENMATLMVLEPAVIVEKAGPMTVTVGETCTLECKVAGTPELSVEWYKDGKLLTSSQKHKFSFYNKISSLRILSVERQDAGTYTFQVQNNVGKSSCTAVVDVSDRAVPPSFTRRLKNTGGVLGASCILECKVAGSSPISVAWFHEKTKIVSGAKYQTTFSDNVCTLQLNSLDSSDMGNYTCVAANVAGSDECRAVLTVQEPPSFVKEPEPLEVLPGKNVTFTSVIRGTPPFKVNWFRGARELVKGDRCNIYFEDTVAELELFNIDISQSGEYTCVVSNNAGQASCTTRLFVKEPAAFLKRLSDHSVEPGKSIILESTYTGTLPISVTWKKDGFNITTSEKCNIVTTEKTCILEILNSTKRDAGQYSCEIENEAGRDVCGALVSTLEPPYFVTELEPLEAAVGDSVSLQCQVAGTPEITVSWYKGDTKLRPTPEYRTYFTNNVATLVFNKVNINDSGEYTCKAENSIGTASSKTVFRIQERQLPPSFARQLKDIEQTVGLPVTLTCRLNGSAPIQVCWYRDGVLLRDHENLQTSFVDNVATLKILQTDLSHSGQYSCSASNPLGTASSSARLTAREPKKSPFFDIKPVSIDVIAGESADFECHVTGAQPMRITWSKDNKEIRPGGNYTITCVGNTPHLRILKVGKGDSGQYTCQATNDVGKDMCSAQLSVKEPPKFVKKLEASKVAKQGESIQLECKISGSPEIKVSWFRNDSELHESWKYNMSFINSVALLTINEASAEDSGDYICEAHNGVGDASCSTALTVKAPPVFTQKPSPVGALKGSDVILQCEISGTPPFEVVWVKDRKQVRNSKKFKITSKHFDTNLHILNLEASDVGEYHCKATNEVGSDTCSCSVKFKEPPRFVKKLSDTSTLIGDAVELRAIVEGFQPISVVWLKDRGEVIRESENTRISFIDNIATLQLGSPEASNSGKYICQIKNDAGMRECSAVLTVLEPARIIEKPEPMTVTTGNPFALECVVTGTPELSAKWFKDGRELSADSKHHITFINKVASLKIPCAEMSDKGLYSFEVKNSVGKSNCTVSVHVSDRIVPPSFIRKLKDVNAILGASVVLECRVSGSAPISVGWFQDGNEIVSGPKCQSSFSENVCTLNLSLLEPSDTGIYTCVAANVAGSDECSAVLTVQEPPSFEQTPDSVEVLPGMSLTFTSVIRGTPPFKVKWFKGSRELVPGESCNISLEDFVTELELFEVQPLESGDYSCLVTNDAGSASCTTHLFVKEPATFVKRLADFSVETGSPIVLEATYTGTPPISVSWIKDEYLISQSERCSITMTEKSTILEILESTIEDYAQYSCLIENEAGQDICEALVSVLEPPYFIEPLEHVEAVIGEPATLQCKVDGTPEIRISWYKEHTKLRSAPAYKMQFKNNVASLVINKVDHSDVGEYSCKADNSVGAVASSAVLVIKARKLPPFFARKLKDVHETLGFPVAFECRINGSEPLQVSWYKDGVLLKDDANLQTSFVHNVATLQILQTDQSHIGQYNCSASNPLGTASSSAKLILSEHEVPPFFDLKPVSVDLALGESGTFKCHVTGTAPIKITWAKDNREIRPGGNYKMTLVENTATLTVLKVGKGDAGQYTCYASNIAGKDSCSAQLGVQEPPRFIKKLEPSRIVKQDEFTRYECKIGGSPEIKVLWYKDETEIQESSKFRMSFVDSVAVLEMHNLSVEDSGDYTCEAHNAAGSASSSTSLKVKEPPIFRKKPHPIETLKGADVHLECELQGTPPFHVSWYKDKRELRSGKKYKIMSENFLTSIHILNVDAADIGEYQCKATNDVGSDTCVGSIALKAPPRFVKKLSDISTVVGKEVQLQTTIEGAEPISVVWFKDKGEIVRESDNIWISYSENIATLQFSRVEPANAGKYTCQIKNDAGMQECFATLSVLEPATIVEKPESIKVTTGDTCTLECTVAGTPELSTKWFKDGKELTSDNKYKISFFNKVSGLKIINVAPSDSGVYSFEVQNPVGKDSCTASLQVSDRTVPPSFTRKLKETNGLSGSSVVMECKVYGSPPISVSWFHEGNEISSGRKYQTTLTDNTCALTVNMLEESDSGDYTCIATNMAGSDECSAPLTVREPPSFVQKPDPMDVLTGTNVTFTSIVKGTPPFSVSWFKGSSELVPGDRCNVSLEDSVAELELFDVDTSQSGEYTCIVSNEAGKASCTTHLYIKAPAKFVKRLNDYSIEKGKPLILEGTFTGTPPISVTWKKNGINVTPSQRCNITTTEKSPILEIPSSTVEDAGQYNCYIENASGKDSCSAQILILEPPYFVKQLEPVKVSVGDSASLQCQLAGTPEIGVSWYKGDTKLRPTTTYKMHFRNNVATLVFNQVDINDSGEYICKAENSVGEVSASTFLTVQEQKLPPSFSRQLRDVQETVGLPVVFDCAISGSEPISVSWYKDGKPLKDSPNVQTSFLDNTATLNIFKTDRSLAGQYSCTATNPIGSASSSARLILTEGKNPPFFDIRLAPVDAVVGESADFECHVTGTQPIKVSWAKDSREIRSGGKYQISYLENSAHLTVLKVDKGDSGQYTCYAVNEVGKDSCTAQLNIKERLIPPSFTKRLSETVEETEGNSFKLEGRVAGSQPITVAWYKNNIEIQPTSNCEITFKNNTLVLQVRKAGMNDAGLYTCKVSNDAGSALCTSSIVIKEPKKPPVFDQHLTPVTVSEGEYVQLSCHVQGSEPIRIQWLKAGREIKPSDRCSFSFASGTAVLELRDVAKADSGDYVCKASNVAGSDTTKSKVTIKDKPAVAPATKKAAVDGRLFFVSEPQSIRVVEKTTATFIAKVGGDPIPNVKWTKGKWRQLNQGGRVFIHQKGDEAKLEIRDTTKTDSGLYRCVAFNEHGEIESNVNLQVDERKKQEKIEGDLRAMLKKTPILKKGAGEEEEIDIMELLKNVDPKEYEKYARMYGITDFRGLLQAFELLKQSQEEETHRLEIEEIERSERDEKEFEELVSFIQQRLSQTEPVTLIKDIENQTVLKDNDAVFEIDIKINYPEIKLSWYKGTEKLEPSDKFEISIDGDRHTLRVKNCQLKDQGNYRLVCGPHIASAKLTVIEPAWERHLQDVTLKEGQTCTMTVQFSVPNVKSEWFRNGRILKPQGRHKTEVEHKVHKLTIADVRAEDQGQYTCKYEDLETSAELRIEAEPIQFTKRIQNIVVSEHQSATFECEVSFDDAIVTWYKGPTELTESQKYNFRNDGRCHYMTIHNVTPDDEGVYSVIARLEPRGEARSTAELYLTTKEIKLELKPPDIPDSRVPIPTMPIRAVPPEEIPPVVAPPVPLLLPTPEEKKPPPKRIEVTKKAVKKDAKKVVAKPKEMTPREEIVKKPPPPTTLIPAKAPEIIDVSSKAEEVKIMTITRKKEVQKEKEAVYEKKQAVHKEKRVFIESFEEPYDELEVEPYTEPFEQPYYEEPDEDYEEIKVEAKKEVHEEWEEDFEEGQEYYEREEGYDEGEEEWEEAYQEREVIQVQKEVYEESHERKVPAKVPEKKAPPPPKVIKKPVIEKIEKTSRRMEEEKVQVTKVPEVSKKIVPQKPSRTPVQEEVIEVKVPAVHTKKMVISEEKMFFASHTEEEVSVTVPEVQKEIVTEEKIHVAVSKRVEPPPKVPELPEKPAPEEVAPVPIPKKVEPPAPKVPEVPKKPVPEEKKPVPVPKKEPAAPPKVPEVPKKPVPEEKIPVPVAKKKEAPPAKVPEVQKGVVTEEKITIVTQREESPPPAVPEIPKKKVPEERKPVPRKEEEVPPPPKVPALPKKPVPEEKVAVPVPVAKKAPPPRAEVSKKTVVEEKRFVAEEKLSFAVPQRVEVTRHEVSAEEEWSYSEEEEGVSISVYREEEREEEEEAEVTEYEVMEEPEEYVVEEKLHIISKRVEAEPAEVTERQEKKIVLKPKIPAKIEEPPPAKVPEAPKKIVPEKKVPAPVPKKEKVPPPKVPEEPKKPVPEKKVPPKVIKMEEPLPAKVTEKHMQITQEEKVLVAVTKKEAPPKARVPEEPKRAVPEEKVLKLKPKREEEPPAKVTEFRKRVVKEEKVSIEAPKREPQPIKEVTIMEEKERAYTLEEEAVSVQREEEYEEYEEYDYKEFEEYEPTEEYDQYEEYEEREYERYEEHEEYITEPEKPIPVKPVPEEPVPTKPKAPPAKVLKKAVPEEKVPVPIPKKLKPPPPKVPEEPKKVFEEKIHISITKREKEQVTEPAAKVPMKPKRVVAEEKVPVPRKEVAPPVRVPEVPKELEPEEVAFEEEVVTHVEEYLVEEEEEYIHEEEEFITEEEVVPVIPVKVPEVPRKPVPEEKKPVPVPKKKEAPPAKVPEVPKKPEEKVPVLIPKKEKPPPAKVPEVPKKPVPEEKVPVPVPKKVEAPPAKVPEVPKKPVPEKKVPVPAPKKVEAPPAKVPEVPKKLIPEEKKPTPVPKKVEAPPPKVPKKREPVPVPVALPQEEEVLFEEEIVPEEEVLPEEEEVLPEEEEVLPEEEEVLPEEEEIPPEEEEVPPEEEYVPEEEEFVPEEEVLPEVKPKVPVPAPVPEIKKKVTEKKVVIPKKEEAPPAKVPEVPKKVEEKRIILPKEEEVLPVEVTEEPEEEPISEEEIPEEPPSIEEVEEVAPPRVPEVIKKAVPEAPTPVPKKVEAPPAKVSKKIPEEKVPVPVQKKEAPPAKVPEVPKKVPEKKVLVPKKEAVPPAKGRTVLEEKVSVAFRQEVVVKERLELEVVEAEVEEIPEEEEFHEVEEYFEEGEFHEVEEFIKLEQHRVEEEHRVEKVHRVIEVFEAEEVEVFEKPKAPPKGPEISEKIIPPKKPPTKVVPRKEPPAKVPEVPKKIVVEEKVRVPEEPRVPPTKVPEVLPPKEVVPEKKVPVPPAKKPEAPPPKVPEAPKEVVPEKKVPVPPPKKPEVPPTKVPEVPKAAVPEKKVPEAIPPKPESPPPEVFEEPEESPSAPPKKPEVPPVRVPEVPKEVVPEKKVPAAPPKKPEVTPVKVPEAPKEVVPEKKVPVPPPKKPEVPPTKVPEVPKVAVPEKKVPEAIPPKPESPPPEVFEEPEEVALEEPPAEVVEEPEPAAPPQVTVPPKNPVPEKKAPAVVAKKPELPPVKVPEVPKEVVPEKKVPLVVPKKPEAPPAKVPEVPKEVVPEKKVAVPKKPEVPPAKVPEVPKKPVLEEKPAVPVPERAESPPPEVYEEPEEIAPEEEIAPEEEKPVPVAEEEEPEVPPPAVPEEPKKIIPEKKVPVIKKPEAPPPKEPEPEKVIEKPKLKPRPPPPPPAPPKEDVKEKIFQLKAIPKKKVPENPQVPEKVELTPLKVPGGEKKVRKLLPERKPEPKEEVVLKSVLRKRPEEEEPKVEPKKLEKVKKPAVPEPPPPKPVEEVEVPTVTKRERKIPEPTKVPEIKPAIPLPAPEPKPKPEAEVKTIKPPPVEPEPTPIAAPVTVPVVGKKAEAKAPKEEAAKPKGPIKGVPKKTPSPIEAERRKLRPGSGGEKPPDEAPFTYQLKAVPLKFVKEIKDIILTESEFVGSSAIFECLVSPSTAITTWMKDGSNIRESPKHRFIADGKDRKLHIIDVQLSDAGEYTCVLRLGNKEKTSTAKLVVEELPVRFVKTLEEEVTVVKGQPLYLSCELNKERDVVWRKDGKIVVEKPGRIVPGVIGLMRALTINDAD Disordered 5618 7791 PPEEIPPVVAPPVPLLLPTPEEKKPPPKRIEVTKKAVKKDAKKVVAKPKEMTPREEIVKKPPPPTTLIPAKAPEIIDVSSKAEEVKIMTITRKKEVQKEKEAVYEKKQAVHKEKRVFIESFEEPYDELEVEPYTEPFEQPYYEEPDEDYEEIKVEAKKEVHEEWEEDFEEGQEYYEREEGYDEGEEEWEEAYQEREVIQVQKEVYEESHERKVPAKVPEKKAPPPPKVIKKPVIEKIEKTSRRMEEEKVQVTKVPEVSKKIVPQKPSRTPVQEEVIEVKVPAVHTKKMVISEEKMFFASHTEEEVSVTVPEVQKEIVTEEKIHVAVSKRVEPPPKVPELPEKPAPEEVAPVPIPKKVEPPAPKVPEVPKKPVPEEKKPVPVPKKEPAAPPKVPEVPKKPVPEEKIPVPVAKKKEAPPAKVPEVQKGVVTEEKITIVTQREESPPPAVPEIPKKKVPEERKPVPRKEEEVPPPPKVPALPKKPVPEEKVAVPVPVAKKAPPPRAEVSKKTVVEEKRFVAEEKLSFAVPQRVEVTRHEVSAEEEWSYSEEEEGVSISVYREEEREEEEEAEVTEYEVMEEPEEYVVEEKLHIISKRVEAEPAEVTERQEKKIVLKPKIPAKIEEPPPAKVPEAPKKIVPEKKVPAPVPKKEKVPPPKVPEEPKKPVPEKKVPPKVIKMEEPLPAKVTEKHMQITQEEKVLVAVTKKEAPPKARVPEEPKRAVPEEKVLKLKPKREEEPPAKVTEFRKRVVKEEKVSIEAPKREPQPIKEVTIMEEKERAYTLEEEAVSVQREEEYEEYEEYDYKEFEEYEPTEEYDQYEEYEEREYERYEEHEEYITEPEKPIPVKPVPEEPVPTKPKAPPAKVLKKAVPEEKVPVPIPKKLKPPPPKVPEEPKKVFEEKIHISITKREKEQVTEPAAKVPMKPKRVVAEEKVPVPRKEVAPPVRVPEVPKELEPEEVAFEEEVVTHVEEYLVEEEEEYIHEEEEFITEEEVVPVIPVKVPEVPRKPVPEEKKPVPVPKKKEAPPAKVPEVPKKPEEKVPVLIPKKEKPPPAKVPEVPKKPVPEEKVPVPVPKKVEAPPAKVPEVPKKPVPEKKVPVPAPKKVEAPPAKVPEVPKKLIPEEKKPTPVPKKVEAPPPKVPKKREPVPVPVALPQEEEVLFEEEIVPEEEVLPEEEEVLPEEEEVLPEEEEVLPEEEEIPPEEEEVPPEEEYVPEEEEFVPEEEVLPEVKPKVPVPAPVPEIKKKVTEKKVVIPKKEEAPPAKVPEVPKKVEEKRIILPKEEEVLPVEVTEEPEEEPISEEEIPEEPPSIEEVEEVAPPRVPEVIKKAVPEAPTPVPKKVEAPPAKVSKKIPEEKVPVPVQKKEAPPAKVPEVPKKVPEKKVLVPKKEAVPPAKGRTVLEEKVSVAFRQEVVVKERLELEVVEAEVEEIPEEEEFHEVEEYFEEGEFHEVEEFIKLEQHRVEEEHRVEKVHRVIEVFEAEEVEVFEKPKAPPKGPEISEKIIPPKKPPTKVVPRKEPPAKVPEVPKKIVVEEKVRVPEEPRVPPTKVPEVLPPKEVVPEKKVPVPPAKKPEAPPPKVPEAPKEVVPEKKVPVPPPKKPEVPPTKVPEVPKAAVPEKKVPEAIPPKPESPPPEVFEEPEESPSAPPKKPEVPPVRVPEVPKEVVPEKKVPAAPPKKPEVTPVKVPEAPKEVVPEKKVPVPPPKKPEVPPTKVPEVPKVAVPEKKVPEAIPPKPESPPPEVFEEPEEVALEEPPAEVVEEPEPAAPPQVTVPPKNPVPEKKAPAVVAKKPELPPVKVPEVPKEVVPEKKVPLVVPKKPEAPPAKVPEVPKEVVPEKKVAVPKKPEVPPAKVPEVPKKPVLEEKPAVPVPERAESPPPEVYEEPEEIAPEEEIAPEEEKPVPVAEEEEPEVPPPAVPEEPKKIIPEKKVPVIKKPEAPPPKEPEPEKVIEKPKLKPRPPPPPPAPPKEDVKEKIFQLKAIPKKKVPENPQVPEKVELTPLKVPGGEKKVRKLLPERKPEPKEEVVLKSVLRKRPEEEEPKVEPKKLEKVKKPAVPEPPPPKPVEEVEVPTVTKRERKIPEPTKVPEIKPAIPLPAPEPKPKPEAEVKTIKPPPVEPEPTPIAAPVTVPVVGKKAEAKAPKEEAAKPKGPIKGVPKKTPSPIEAERRKLRPGSGGEKPPDEA Paper Elastic titin Q10465 Homo sapiens (Human) 7962 PDQEMPVYPPAIITPLQDTVTSEGQPARFQCRVSGTDLKVSWYSKDKKIKPSRFFRMTQFEDTYQLEIAEAYPEDEGTYTFVANNAVGQVSSTANLSLEAPESILHERIEQEIEMEMKAAPVIKRKIEPLEVALGHLAKFTCEIQSAPNVRFQWFKAGREIYESDKCSIRSSKYISSLEILRTQVVDCGEYTCKASNEYGSVSCTATLTVTEAYPPTFLSRPKSLTTFVGKAAKFICTVTGTPVIETIWQKDGAALSPSPNWRISDAENKHILELSNLTIQDRGVYSCKASNKFGADICQAELIIIDKPHFIKELEPVQSAINKKVHLECQVDEDRKVTVTWSKDGQKLPPGKDYKICFEDKIATLEIPLAKLKDSGTYVCTASNEAGSSSCSATVTVREPPSFVKKVDPSYLMLPGESARLHCKLKGSPVIQVTWFKNNKELSESNTVRMYFVNSEAILDITDVKVEDSGSYSCEAVNDVGSDSCSTEIVIKEPPSFIKTLEPADIVRGTNALLQCEVSGTGPFEISWFKDKKQIRSSKKYRLFSQKSLVCLEIFSFNSADVGEYECVVANEVGKCGCMATHLLKEPPTFVKKVDDLIALGGQTVTLQAAVRGSEPISVTWMKGQEVIREDGKIKMSFSNGVAVLIIPDVQISFGGKYTCLAENEAGSQTSVGELIVKEPAKIIERAELIQVTAGDPATLEYTVAGTPELKPKWYKDGRPLVASKKYRISFKNNVAQLKFYSAELHDSGQYTFEISNEVGSSSCETTFTVLDRDIAPFFTKPLRNVDSVVNGTCRLDCKIAGSLPMRVSWFKDGKEIAASDRYRIAFVEGTASLEIIRVDMNDAGNFTCRATNSVGSKDSSGALIVQEPPSFVTKPGSKDVLPGSAVCLKSTFQGSTPLTIRWFKGNKELVSGGSCYITKEALESSLELYLVKTSDSGTYTCKVSNVAGGVECSANLFVKEPATFVEKLEPSQLLKKGDATQLACKVTGTPPIKITWFANDREIKESSKHRMSFVESTAVLRLTDVGIEDSGEYMCEAQNEAGSDHCSSIVIVKESPYFTKEFKPIEVLKEYDVMLLAEVAGTPPFEITWFKDNTILRSGRKYKTFIQDHLVSLQILKFVAADAGEYQCRVTNEVGSSICSARVTLREPPSFIKKIESTSSLRGGTAAFQATLKGSLPITVTWLKDSDEITEDDNIRMTFENNVASLYLSGIEVKHDGKYVCQAKNDAGIQRCSALLSVKEPATITEEAVSIDVTQGDPATLQVKFSGTKEITAKWFKDGQELTLGSKYKISVTDTVSILKIISTEKKDSGEYTFEVQNDVGRSSCKARINVLDLIIPPSFTKKLKKMDSIKGSFIDLECIVAGSHPISIQWFKDDQEISASEKYKFSFHDNTAFLEISQLEGTDSGTYTCSATNKAGHNQCSGHLTVKEPPYFVEKPQSQDVNPNTRVQLKALVGGTAPMTIKWFKDNKELHSGAARSVWKDDTSTSLELFAAKATDSGTYICQLSNDVGTATSKATLFVKEPPQFIKKPSPVLVLRNGQSTTFECQITGTPKIRVSWYLDGNEITAIQKHGISFIDGLATFQISGARVENSGTYVCEARNDAGTASCSIELKVKEPPTFIRELKPVEVVKYSDVELECEVTGTPPFEVTWLKNNREIRSSKKYTLTDRVSVFNLHITKCDPSDTGEYQCIVSNEGGSCSCSTRVALKEPPSFIKKIENTTTVLKSSATFQSTVAGSPPISITWLKDDQILDEDDNVYISFVDSVATLQIRSVDNGHSGRYTCQAKNESGVERCYAFLLVQEPAQIVEKAKSVDVTEKDPMTLECVVAGTPELKVKWLKDGKQIVPSRYFSMSFENNVASFRIQSVMKQDSGQYTFKVENDFGSSSCDAYLRVLDQNIPPSFTKKLTKMDKVLGSSIHMECKVSGSLPISAQWFKDGKEISTSAKYRLVCHERSVSLEVNNLELEDTANYTCKVSNVAGDDACSGILTVKEPPSFLVKPGRQQAIPDSTVEFKAILKGTPPFKIKWFKDDVELVSGPKCFIGLEGSTSFLNLYSVDASKTGQYTCHVTNDVGSDSCTTMLLVTEPPKFVKKLEASKIVKAGDSSRLECKIAGSPEIRVVWFRNEHELPASDKYRMTFIDSVAVIQMNNLSTEDSGDFICEAQNPAGSTSCSTKVIVKEPPVFSSFPPIVETLKNAEVSLECELSGTPPFEVVWYKDKRQLRSSKKYKIASKNFHTSIHILNVDTSDIGEYHCKAQNEVGSDTCVCTVKLKEPPRFVSKLNSLTVVAGEPAELQASIEGAQPIFVQWLKEKEEVIRESENIRITFVENVATLQFAKAEPANAGKYICQIKNDGGMRENMATLMVLEPAVIVEKAGPMTVTVGETCTLECKVAGTPELSVEWYKDGKLLTSSQKHKFSFYNKISSLRILSVERQDAGTYTFQVQNNVGKSSCTAVVDVSDRAVPPSFTRRLKNTGGVLGASCILECKVAGSSPISVAWFHEKTKIVSGAKYQTTFSDNVCTLQLNSLDSSDMGNYTCVAANVAGSDECRAVLTVQEPPSFVKEPEPLEVLPGKNVTFTSVIRGTPPFKVNWFRGARELVKGDRCNIYFEDTVAELELFNIDISQSGEYTCVVSNNAGQASCTTRLFVKEPAAFLKRLSDHSVEPGKSIILESTYTGTLPISVTWKKDGFNITTSEKCNIVTTEKTCILEILNSTKRDAGQYSCEIENEAGRDVCGALVSTLEPPYFVTELEPLEAAVGDSVSLQCQVAGTPEITVSWYKGDTKLRPTPEYRTYFTNNVATLVFNKVNINDSGEYTCKAENSIGTASSKTVFRIQERQLPPSFARQLKDIEQTVGLPVTLTCRLNGSAPIQVCWYRDGVLLRDHENLQTSFVDNVATLKILQTDLSHSGQYSCSASNPLGTASSSARLTAREPKKSPFFDIKPVSIDVIAGESADFECHVTGAQPMRITWSKDNKEIRPGGNYTITCVGNTPHLRILKVGKGDSGQYTCQATNDVGKDMCSAQLSVKEPPKFVKKLEASKVAKQGESIQLECKISGSPEIKVSWFRNDSELHESWKYNMSFINSVALLTINEASAEDSGDYICEAHNGVGDASCSTALTVKAPPVFTQKPSPVGALKGSDVILQCEISGTPPFEVVWVKDRKQVRNSKKFKITSKHFDTNLHILNLEASDVGEYHCKATNEVGSDTCSCSVKFKEPPRFVKKLSDTSTLIGDAVELRAIVEGFQPISVVWLKDRGEVIRESENTRISFIDNIATLQLGSPEASNSGKYICQIKNDAGMRECSAVLTVLEPARIIEKPEPMTVTTGNPFALECVVTGTPELSAKWFKDGRELSADSKHHITFINKVASLKIPCAEMSDKGLYSFEVKNSVGKSNCTVSVHVSDRIVPPSFIRKLKDVNAILGASVVLECRVSGSAPISVGWFQDGNEIVSGPKCQSSFSENVCTLNLSLLEPSDTGIYTCVAANVAGSDECSAVLTVQEPPSFEQTPDSVEVLPGMSLTFTSVIRGTPPFKVKWFKGSRELVPGESCNISLEDFVTELELFEVQPLESGDYSCLVTNDAGSASCTTHLFVKEPATFVKRLADFSVETGSPIVLEATYTGTPPISVSWIKDEYLISQSERCSITMTEKSTILEILESTIEDYAQYSCLIENEAGQDICEALVSVLEPPYFIEPLEHVEAVIGEPATLQCKVDGTPEIRISWYKEHTKLRSAPAYKMQFKNNVASLVINKVDHSDVGEYSCKADNSVGAVASSAVLVIKARKLPPFFARKLKDVHETLGFPVAFECRINGSEPLQVSWYKDGVLLKDDANLQTSFVHNVATLQILQTDQSHIGQYNCSASNPLGTASSSAKLILSEHEVPPFFDLKPVSVDLALGESGTFKCHVTGTAPIKITWAKDNREIRPGGNYKMTLVENTATLTVLKVGKGDAGQYTCYASNIAGKDSCSAQLGVQEPPRFIKKLEPSRIVKQDEFTRYECKIGGSPEIKVLWYKDETEIQESSKFRMSFVDSVAVLEMHNLSVEDSGDYTCEAHNAAGSASSSTSLKVKEPPIFRKKPHPIETLKGADVHLECELQGTPPFHVSWYKDKRELRSGKKYKIMSENFLTSIHILNVDAADIGEYQCKATNDVGSDTCVGSIALKAPPRFVKKLSDISTVVGKEVQLQTTIEGAEPISVVWFKDKGEIVRESDNIWISYSENIATLQFSRVEPANAGKYTCQIKNDAGMQECFATLSVLEPATIVEKPESIKVTTGDTCTLECTVAGTPELSTKWFKDGKELTSDNKYKISFFNKVSGLKIINVAPSDSGVYSFEVQNPVGKDSCTASLQVSDRTVPPSFTRKLKETNGLSGSSVVMECKVYGSPPISVSWFHEGNEISSGRKYQTTLTDNTCALTVNMLEESDSGDYTCIATNMAGSDECSAPLTVREPPSFVQKPDPMDVLTGTNVTFTSIVKGTPPFSVSWFKGSSELVPGDRCNVSLEDSVAELELFDVDTSQSGEYTCIVSNEAGKASCTTHLYIKAPAKFVKRLNDYSIEKGKPLILEGTFTGTPPISVTWKKNGINVTPSQRCNITTTEKSPILEIPSSTVEDAGQYNCYIENASGKDSCSAQILILEPPYFVKQLEPVKVSVGDSASLQCQLAGTPEIGVSWYKGDTKLRPTTTYKMHFRNNVATLVFNQVDINDSGEYICKAENSVGEVSASTFLTVQEQKLPPSFSRQLRDVQETVGLPVVFDCAISGSEPISVSWYKDGKPLKDSPNVQTSFLDNTATLNIFKTDRSLAGQYSCTATNPIGSASSSARLILTEGKNPPFFDIRLAPVDAVVGESADFECHVTGTQPIKVSWAKDSREIRSGGKYQISYLENSAHLTVLKVDKGDSGQYTCYAVNEVGKDSCTAQLNIKERLIPPSFTKRLSETVEETEGNSFKLEGRVAGSQPITVAWYKNNIEIQPTSNCEITFKNNTLVLQVRKAGMNDAGLYTCKVSNDAGSALCTSSIVIKEPKKPPVFDQHLTPVTVSEGEYVQLSCHVQGSEPIRIQWLKAGREIKPSDRCSFSFASGTAVLELRDVAKADSGDYVCKASNVAGSDTTKSKVTIKDKPAVAPATKKAAVDGRLFFVSEPQSIRVVEKTTATFIAKVGGDPIPNVKWTKGKWRQLNQGGRVFIHQKGDEAKLEIRDTTKTDSGLYRCVAFNEHGEIESNVNLQVDERKKQEKIEGDLRAMLKKTPILKKGAGEEEEIDIMELLKNVDPKEYEKYARMYGITDFRGLLQAFELLKQSQEEETHRLEIEEIERSERDEKEFEELVSFIQQRLSQTEPVTLIKDIENQTVLKDNDAVFEIDIKINYPEIKLSWYKGTEKLEPSDKFEISIDGDRHTLRVKNCQLKDQGNYRLVCGPHIASAKLTVIEPAWERHLQDVTLKEGQTCTMTVQFSVPNVKSEWFRNGRILKPQGRHKTEVEHKVHKLTIADVRAEDQGQYTCKYEDLETSAELRIEAEPIQFTKRIQNIVVSEHQSATFECEVSFDDAIVTWYKGPTELTESQKYNFRNDGRCHYMTIHNVTPDDEGVYSVIARLEPRGEARSTAELYLTTKEIKLELKPPDIPDSRVPIPTMPIRAVPPEEIPPVVAPPVPLLLPTPEEKKPPPKRIEVTKKAVKKDAKKVVAKPKEMTPREEIVKKPPPPTTLIPAKAPEIIDVSSKAEEVKIMTITRKKEVQKEKEAVYEKKQAVHKEKRVFIESFEEPYDELEVEPYTEPFEQPYYEEPDEDYEEIKVEAKKEVHEEWEEDFEEGQEYYEREEGYDEGEEEWEEAYQEREVIQVQKEVYEESHERKVPAKVPEKKAPPPPKVIKKPVIEKIEKTSRRMEEEKVQVTKVPEVSKKIVPQKPSRTPVQEEVIEVKVPAVHTKKMVISEEKMFFASHTEEEVSVTVPEVQKEIVTEEKIHVAVSKRVEPPPKVPELPEKPAPEEVAPVPIPKKVEPPAPKVPEVPKKPVPEEKKPVPVPKKEPAAPPKVPEVPKKPVPEEKIPVPVAKKKEAPPAKVPEVQKGVVTEEKITIVTQREESPPPAVPEIPKKKVPEERKPVPRKEEEVPPPPKVPALPKKPVPEEKVAVPVPVAKKAPPPRAEVSKKTVVEEKRFVAEEKLSFAVPQRVEVTRHEVSAEEEWSYSEEEEGVSISVYREEEREEEEEAEVTEYEVMEEPEEYVVEEKLHIISKRVEAEPAEVTERQEKKIVLKPKIPAKIEEPPPAKVPEAPKKIVPEKKVPAPVPKKEKVPPPKVPEEPKKPVPEKKVPPKVIKMEEPLPAKVTEKHMQITQEEKVLVAVTKKEAPPKARVPEEPKRAVPEEKVLKLKPKREEEPPAKVTEFRKRVVKEEKVSIEAPKREPQPIKEVTIMEEKERAYTLEEEAVSVQREEEYEEYEEYDYKEFEEYEPTEEYDQYEEYEEREYERYEEHEEYITEPEKPIPVKPVPEEPVPTKPKAPPAKVLKKAVPEEKVPVPIPKKLKPPPPKVPEEPKKVFEEKIHISITKREKEQVTEPAAKVPMKPKRVVAEEKVPVPRKEVAPPVRVPEVPKELEPEEVAFEEEVVTHVEEYLVEEEEEYIHEEEEFITEEEVVPVIPVKVPEVPRKPVPEEKKPVPVPKKKEAPPAKVPEVPKKPEEKVPVLIPKKEKPPPAKVPEVPKKPVPEEKVPVPVPKKVEAPPAKVPEVPKKPVPEKKVPVPAPKKVEAPPAKVPEVPKKLIPEEKKPTPVPKKVEAPPPKVPKKREPVPVPVALPQEEEVLFEEEIVPEEEVLPEEEEVLPEEEEVLPEEEEVLPEEEEIPPEEEEVPPEEEYVPEEEEFVPEEEVLPEVKPKVPVPAPVPEIKKKVTEKKVVIPKKEEAPPAKVPEVPKKVEEKRIILPKEEEVLPVEVTEEPEEEPISEEEIPEEPPSIEEVEEVAPPRVPEVIKKAVPEAPTPVPKKVEAPPAKVSKKIPEEKVPVPVQKKEAPPAKVPEVPKKVPEKKVLVPKKEAVPPAKGRTVLEEKVSVAFRQEVVVKERLELEVVEAEVEEIPEEEEFHEVEEYFEEGEFHEVEEFIKLEQHRVEEEHRVEKVHRVIEVFEAEEVEVFEKPKAPPKGPEISEKIIPPKKPPTKVVPRKEPPAKVPEVPKKIVVEEKVRVPEEPRVPPTKVPEVLPPKEVVPEKKVPVPPAKKPEAPPPKVPEAPKEVVPEKKVPVPPPKKPEVPPTKVPEVPKAAVPEKKVPEAIPPKPESPPPEVFEEPEESPSAPPKKPEVPPVRVPEVPKEVVPEKKVPAAPPKKPEVTPVKVPEAPKEVVPEKKVPVPPPKKPEVPPTKVPEVPKVAVPEKKVPEAIPPKPESPPPEVFEEPEEVALEEPPAEVVEEPEPAAPPQVTVPPKNPVPEKKAPAVVAKKPELPPVKVPEVPKEVVPEKKVPLVVPKKPEAPPAKVPEVPKEVVPEKKVAVPKKPEVPPAKVPEVPKKPVLEEKPAVPVPERAESPPPEVYEEPEEIAPEEEIAPEEEKPVPVAEEEEPEVPPPAVPEEPKKIIPEKKVPVIKKPEAPPPKEPEPEKVIEKPKLKPRPPPPPPAPPKEDVKEKIFQLKAIPKKKVPENPQVPEKVELTPLKVPGGEKKVRKLLPERKPEPKEEVVLKSVLRKRPEEEEPKVEPKKLEKVKKPAVPEPPPPKPVEEVEVPTVTKRERKIPEPTKVPEIKPAIPLPAPEPKPKPEAEVKTIKPPPVEPEPTPIAAPVTVPVVGKKAEAKAPKEEAAKPKGPIKGVPKKTPSPIEAERRKLRPGSGGEKPPDEAPFTYQLKAVPLKFVKEIKDIILTESEFVGSSAIFECLVSPSTAITTWMKDGSNIRESPKHRFIADGKDRKLHIIDVQLSDAGEYTCVLRLGNKEKTSTAKLVVEELPVRFVKTLEEEVTVVKGQPLYLSCELNKERDVVWRKDGKIVVEKPGRIVPGVIGLMRALTINDAD Disordered 5746 6215 EVEPYTEPFEQPYYEEPDEDYEEIKVEAKKEVHEEWEEDFEEGQEYYEREEGYDEGEEEWEEAYQEREVIQVQKEVYEESHERKVPAKVPEKKAPPPPKVIKKPVIEKIEKTSRRMEEEKVQVTKVPEVSKKIVPQKPSRTPVQEEVIEVKVPAVHTKKMVISEEKMFFASHTEEEVSVTVPEVQKEIVTEEKIHVAVSKRVEPPPKVPELPEKPAPEEVAPVPIPKKVEPPAPKVPEVPKKPVPEEKKPVPVPKKEPAAPPKVPEVPKKPVPEEKIPVPVAKKKEAPPAKVPEVQKGVVTEEKITIVTQREESPPPAVPEIPKKKVPEERKPVPRKEEEVPPPPKVPALPKKPVPEEKVAVPVPVAKKAPPPRAEVSKKTVVEEKRFVAEEKLSFAVPQRVEVTRHEVSAEEEWSYSEEEEGVSISVYREEEREEEEEAEVTEYEVMEEPEEYVVEEKLHIISKRVEAE Fragment Native Function arises from the disordered state Entropic chain Entropic spring Far-UV circular dichroism (CD) Paper 11084039 Gutierrez-Cruz G, Van Heerden AH, Wang K 2001 J Biol Chem 276 10 7442-9 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 PSYLMLPGESA Fragment 1GBWA 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 Disordered 634 681 KIKMSFSNGVAVLIIPDVQISFGGKYTCLAENEAGSQTSVGELIVKEP Fragment 1GBWA 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 Disordered 1077 1107 LLAEVAGTPPFEITWFKDNTILRSGRKYKTF Fragment 1GBWA 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 Disordered 1179 1202 PITVTWLKDSDEITEDDNIRMTFE Fragment 1GBWA 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 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).

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. 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 Max protein Transcription factor MAX P25912 57619109 Felis silvestris catus (Cat) 160 MSDNDDIEVESDEEQPRFQSAADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQVRALEKARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQSRKKLRMEAS Disordered 1 110 MSDNDDIEVESDEEQPRFQSAADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQVRALEKARSSAQ Paper 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) 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 14711835 Takada Y, Singh S, Aggarwal BB 2004 J Biol Chem 279 15 15096-15104 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) 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 7797554 Schmitz ML, dos Santos Silva MA, Baeuerle PA 1995 J Biol Chem 270 26 15576-15584 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 TA'1 458 483 TDPAVFTDLASVDNSEFQQLLNQGIP Function arises via a disorder to order transition Molecular assembly Protein-protein binding Transactivation (transcriptional activation) Nuclear magnetic resonance (NMR) 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 7797554 Schmitz ML, dos Santos Silva MA, Baeuerle PA 1995 J Biol Chem 270 26 15576-15584 NMR spectra revealed that TA’1 exists in aqueous solution at physiological pH in a random coil conformation or is unstructured. (See region 2) Disordered - Extended TA1 and TA2 (C-terminal region) 429 551 TQAGEGTLSEALLQLQFDDEDLGALLGNSTDPAVFTDLASVDNSEFQQLLNQGIPVAPHTTEPMLMEYPEAITRLVTGAQRPPDPAPAPLGAPGLPNGLLSGDEDFSSIADMDFSALLSQISS Function arises via a disorder to order transition Modification site Molecular assembly Protein-protein binding Transactivation (transcriptional activation) Nuclear magnetic resonance (NMR) 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. Ordered 20 320 YVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINGYTGPGTVRISLVTKDPPHRPHPHELVGKDCRDGFYEAELCPDRCIHSFQNLGIQCVKKRDLEQAISQRIQTNNNPFQVPIEEQRGDYDLNAVRLCFQVTVRDPSGRPLRLPPVLPHPIFDNRAPNTAELKICRVNRNSGSCLGGDEIFLLCDKVQKEDIEVYFTGPGWEARGSFSQADVHRQVAIVFRTPPYADPSLQAPVRVSMQLRRPSDRELSEPMEFQYLPDTDDRHRIEEKRKRTYETFKSIMKKSPFSG 1NFLA Paper 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 Disordered 403 490 AGQRPRRLSTTAPITDVSLGDELRLDGEEVDMTPADALDDFDLEMLGDVESPSPGMTHDPVSYGALDVDDFEFEQMFTDAMGIDDFGG Paper 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 This protein also matches the PIR references of B42226 and E90689. 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 subfamily A member 1 Voltage-gated potassium channel Q09470 4557685 I57680 Homo sapiens (Human) 495 MTVMSGENVDEASAAPGHPQDGSYPRQADHDDHECCERVVINISGLRFETQLKTLAQFPNTLLGNPKKRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDMFSEEIKFYELGEEAMEKFREDEGFIKEEERPLPEKEYQRQVWLLFEYPESSGPARVIAIVSVMVILISIVIFCLETLPELKDDKDFTGTVHRIDNTTVIYNSNIFTDPFFIVETLCIIWFSFELVVRFFACPSKTDFFKNIMNFIDIVAIIPYFITLGTEIAEQEGNQKGEQATSLAILRVIRLVRVFRIFKLSRHSKGLQILGQTLKASMRELGLLIFFLFIGVILFSSAVYFAEAEEAESHFSSIPDAFWWAVVSMTTVGYGDMYPVTIGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETEGEEQAQLLHVSSPNLASDSDLSRRSSSTMSKYEYMEIEEDMNNSIAHYRQVNIRTANCTTANQNCVNKSKLLTDV Disordered 1 62 MTVMSGENVDEASAAPGHPQDGSYPRQADHDDHECCERVVINISGLRFETQLKTLAQFPNTL Paper 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. Human 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 Mass spectrometry-based high resolution hydrogen-deuterium exchange Sensitivity to proteolysis CaCl₂ 5 NaCl 50 Tris-HCl 10 Trypsin (10 mg/ml) in HCl (1 mM) X-ray crystallography 92 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 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 an order to disorder transition Function arises via a disorder to order transition Molecular assembly Autoregulatory Protein-protein binding Mass spectrometry-based high resolution hydrogen-deuterium exchange Sensitivity to proteolysis CaCl₂ 5 NaCl 50 Tris-HCl 10 Trypsin (10 mg/ml