The exchangeable yeast ribosomal acidic protein YP2beta shows characteristics of a partly folded state under physiological conditions

60S acidic ribosomal protein P1-beta Acidic ribosomal stalk protein P1 133069 P10622 C28104 106 MSDSIISFAAFILADAGLEITSDNLLTITKAAGANVDNVWADVYAKALEGKDLKEILSGFHNAGPVAGAGAASGAAAAGGDAAAEEEKEEEAAEESDDDMGFGLFD Circular dichroism Limited proteolysis Nuclear magnetic resonance spectroscopy Thermal Stability 1 106 Disordered Function arises from the disordered (extended) state Function arises from the molten globule (collapsed) state Phosphorylation Protein-protein binding Protein-rRNA binding Regulation of proteolysis in vivo Substrate/ligand binding Zurdo, J., Sanz, J. M., Gonzalez, C., Rico, M., and Ballesta, J. P. The exchangeable yeast ribosomal acidic protein YP2beta shows characteristics of a partly folded state under physiological conditions 1997 Biochemistry 36 9625 9635 9236009 Zurdo, J., Gonzalez, C., Sanz, J. M., Rico, M., Remacha, M., and Ballesta, J. P. Structural differences between Saccharomyces cerevisiae ribosomal stalk proteins P1 and P2 support their functional diversity 2000 Biochemistry 39 8935 8943 10913306 Nusspaumer, G., Remacha, M., and Ballesta, J. P. Phosphorylation and N-terminal region of yeast ribosomal protein P1 mediate its degradation, which is prevented by protein P2 2000 EMBO J. 19 6075 6084 11080154 Ballesta, J. P. Personal communication 60S acidic ribosomal protein P2-beta Acidic ribosomal stalk protein P2 133071 P02400 A35109 110 MKYLAAYLLLVQGGNAAPSAADIKAVVESVGAEVDEARINELLSSLEGKGSLEEIIAEGQKKFATVPTGGASSAAAGAAGAAAGGDAAEEEKEEEAKEESDDDMGFGLFD Circular dichroism Limited proteolysis Nuclear magnetic resonance spectroscopy Thermal Stability 1 110 Disordered Function arises from the disordered (extended) state Function arises from the molten globule (collapsed) state Phosphorylation Protein-protein binding Protein-rRNA binding Regulation of proteolysis in vivo Substrate/ligand binding Zurdo, J., Sanz, J. M., Gonzalez, C., Rico, M., and Ballesta, J. P. The exchangeable yeast ribosomal acidic protein YP2beta shows characteristics of a partly folded state under physiological conditions 1997 Biochemistry 36 9625 9635 9236009 Zurdo, J., Gonzalez, C., Sanz, J. M., Rico, M., Remacha, M., and Ballesta, J. P. Structural differences between Saccharomyces cerevisiae ribosomal stalk proteins P1 and P2 support their functional diversity 2000 Biochemistry 39 8935 8943 10913306 Nusspaumer, G., Remacha, M., and Ballesta, J. P. Phosphorylation and N-terminal region of yeast ribosomal protein P1 mediate its degradation, which is prevented by protein P2 2000 EMBO J. 19 6075 6084 11080154 Ballesta, J. P. Personal communication Early E2a Dna-Binding Protein Adenovirus ssDNA binding protein 1633461 P03265 1ADT A03833 356 SVPIVSAWEKGMEAARALMDKYHVDNDLKANFKLLPDQVEALAAVCKTWLNEEHRGLQLTFTSNKTFVTMMGRFLQAYLQSFAEVTYKHHEPTGCALWLHRCAEIEGELKCLHGSIMINKEHVIEMDVTSENGQRALKEQSSKAKIVKNRWGRNVVQISNTDARCCVHDAACPANQFSGKSCGMFFSEGAKAQVAFKQIKAFMQALYPNAQTGHGHLLMPLRCECNSKPGHAPFLGRQLPKLTPFALSNAEDLDADLISDKSVLASVHHPALIVFQCCNPVYRNSRAQGGGPNCDFKISAPDLLNALVMVRSLWSENFTELPRMVVPQFKWSTKHQYRNVSLPVAHSDARQNPFDF X-ray crystallography 124 158 Disordered Function arises via a disorder to order transition DNA unwinding Flexible linkers/spacers Protein-DNA binding Tucker, P. A., Tsernoglou, D., Tucker, A. D., Coenjaerts, F. E., Leenders, H., and van der Vliet, P. C. Crystal structure of the adenovirus DNA binding protein reveals a hook-on model for cooperative DNA binding 1994 EMBO J. 13 2994 3002 8039495 Dekker, J., Kanellopoulos, P. N., van Oosterhout, J. A., Stier, G., Tucker, P. A., and van der Vliet, P. C. ATP-independent DNA unwinding by the adenovirus single-stranded DNA binding protein requires a flexible DNA binding loop 1998 J. Mol. Biol. 277 825 838 9545375 van Breukelen, B., Kanellopoulos, P. N., Tucker, P. A., and van der Vliet, P. C. The formation of a flexible DNA-binding protein chain is required for efficient DNA unwinding and adenovirus DNA chain elongation 2000 J. Biol. Chem. 275 40897 40903 11016931 Antibacterial protein FALL-39 precursor Antibacterial protein LL-37 FALL-39 peptide antibiotic Antimicrobial protein CAP-18 hCAP-18 LL-37 1706745 P49913 I38932 170 MKTQRDGHSLGRWSLVLLLLGLVMPLAIIAQVLSYKEAVLRAIDGINQRSSDANLYRLLDLDPRPTMDGDPDTPKPVSFTVKETVCPRTTQQSPEDCDFKKDGLVKRCMGTVTLNQARGSFDISCDKDNKRFALLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES Circular dichroism 134 170 Disordered Function arises via a disorder to order transition Polymerization Protein-protein binding Johansson, J., Gudmundsson, G. H., Rottenberg, M. E., Berndt, K. D., and Agerberth, B. Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37 1998 J. Biol. Chem. 273 3718 3724 9452503 Antitermination protein N Nucleocapsid protein PN Regulatory protein N Antitermination protein N of bacteriophage lambda 132276 P03045 107 MDAQTRRRERRAEKQAQWKAANPLLVGVSAKPVNLPILSLNRKPKSRVESALNPIDLTVLAEYHKQIESNLQRIERKNQRTWYSKPGERGITCSGRQKIKGKSIPLI Circular dichroism Nuclear magnetic resonance spectroscopy 1 107 Disordered Function arises via a disorder to order transition Protein-mRNA binding Protein-protein binding Mogridge, J., Legault, P., Li, J., Van Oene, M. D., Kay, L. E., and Greenblatt, J. Independent ligand-induced folding of the RNA-binding domain and two functionally distinct antitermination regions in the phage lambda N protein 1998 Mol. Cell 1 265 275 9659923 Legault, P., Li, L., Mogridge, J., Kay, L. E., and Greenblatt, J. NMR structure of the bacteriophage lambda N peptide/boxB RNA complex: recognition of a GNRA fold by an arginine-rich motif 1998 Cell 93 289 299 9568720 Cytochrome c Apocytochrome c 117995 P00004 1CRC 1WEJ A00005 104 GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWKEETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE Circular dichroism 1 104 Disordered Function arises via a disorder to order transition Cofactor/heme binding Stellwagen, E., Rysavy, R., and Babul, G. The conformation of horse heart apocytochrome c 1972 J. Biol. Chem. 247 8074 8077 4344990 APEX nuclease Major apurinic/apyrimidinic endonuclease Apurinic/apyrimidinic endonuclease 299037 P27695 S23550 317 PKRGKKGAVAEDGDELRTEPEAKKSKTAAKKNDKEAAGEGPALYEDPPDHKTSPSGKPATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQELPGLSHQYWSAPSDKEGYSGVGLLSRQCPLKVSYGIGDEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQRWDEAFRKFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLPALCDSKIRSKALGSDHCPITLYLAL Limited proteolysis X-ray crystallography 1 40 Disordered Relationship to function unknown Unknown Strauss, P. R., and Holt, C. M. Domain mapping of human apurinic/apyrimidinic endonuclease. Structural and functional evidence for a disordered amino terminus and a tight globular carboxyl domain 1998 J. Biol. Chem. 273 14435 14441 9603956 Gorman, M. A., Morera, S., Rothwell, D. G., de La Fortelle, E., Mol, C. D., Tainer, J. A., Hickson, I. D., and Freemont, P. S. The crystal structure of the human DNA repair endonuclease HAP1 suggests the recognition of extra-helical deoxyribose at DNA abasic sites 1997 EMBO J. 16 6548 6558 9351835 Mol, C. D., Izumi, T., Mitra, S., and Tainer, J. A. DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination 2000 Nature 403 451 456 10667800 GenBank AAB26054.1 B-cell-specific coactivator BOB.1/OBF.1 B cell-specific transcription co-activator POU domain class 2, associating factor 1 OCT binding factor 1 BOB-1 OCA-B 1150493 Q64693 S63588 256 MLWQKSTAPEQAPAPPRPYQGVRVKEPVKELLRRKRGHTSVGAAGPPTAGVLPHQPLATYSTVGPSCLDMEVSASTVTEEGTLCAGWLSQPAPATLHALAPWTPYTEYVSHEAVSCPYSTDMYVQPVCPSYTVVGPSSVLTYASPPLITNVTPRSTATPAVGPQLEGPEHQAPLTYFPWPQPLSTLPTSSLQYQPPAPTLSGPQFVQLPISIPEPVLQDMDDPRRAISSLTIDKLLLEEEESNTYELNHTLSVEGF Circular dichroism Limited proteolysis 1 256 Disordered Function arises via a disorder to order transition Protein-DNA binding Protein-protein binding Chang, J. F., Phillips, K., Lundback, T., Gstaiger, M., Ladbury, J. E., and Luisi, B. Oct-1 POU and octamer DNA co-operate to recognise the Bob-1 transcription co-activator via induced folding 1999 J. Mol. Biol. 288 941 952 10329190 Rat Bcl-Xl An Apoptosis Inhibitory Protein Bcl-xL antiapoptotic protein Apoptosis regulator Bcl-X Bcl-2-like 1 protein 2392082 P53563 1AF3 I67431 196 MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEETEPERETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIASWMATYLNDHLEPWIQENGGWDTFVDLYG Limited proteolysis X-ray crystallography 31 80 Disordered Function arises from the disordered (extended) state Phosphorylation Regulation of proteolysis in vivo Yamamoto, K., Ichijo, H., and Korsmeyer, S. J. BCL-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal protein kinase pathway normally activated at G(2)/M 1999 Mol. Cell. Biol. 19 8469 8478 10567572 Cheng, E. H., Kirsch, D. G., Clem, R. 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Chem. 274 15505 15509 10336443 Monoamine-sulfating phenol sulfotransferase Sulfotransferase, monoamine-preferring Catecholamine sulfotransferase EC 2.8.2.1 M-PST Thermolabile phenol sulfotransferase TL-PST Placental estrogen sulfotransferase HAST3 1711609 P50224 1CJM A55451 295 MELIQDTSRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLINTYPKSGTTWVSQILDMIYQGGDLEKCNRAPIYVRVPFLEVNDPGEPSGLETLKDTPPPRLIKSHLPLALLPQTLLDQKVKVVYVARNPKDVAVSYYHFHRMEKAHPEPGTWDSFLEKFMAGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETMDFMVQHTSFKEMKKNPMTNYTTVPQELMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL X-ray crystallography 216 261 Disordered Function arises via a disorder to order transition Substrate/ligand binding Bidwell, L. M., McManus, M. E., Gaedigk, A., Kakuta, Y., Negishi, M., Pedersen, L., and Martin, J. L. Crystal structure of human catecholamine sulfotransferase 1999 J. Mol. Biol. 293 521 530 10543947 Dajani, R., Cleasby, A., Neu, M., Wonacott, A. J., Jhoti, H., Hood, A. 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Chem. 274 37862 37868 10608851 Cystic fibrosis transmembrane conductance regulator, ATP-binding cassette CFTR cAMP-dependent chloride channel 14753227 P13569 A39069 1480 MQRSPLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEKLEREWDRELASKKNPKLINALRRCFFWRFMFYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGLGRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVFLSVLPYALIKGIILRKIFTTISFCIVLRMAVTRQFPWAVQTWYDSLGAINKIQDFLQKQEYKTLEYNLTTTEVVMENVTAFWEEGFGELFEKAKQNNNNRKTSNGDDSLFFSNFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPDFSSKLMGCDSFDQFSAERRNSILTETLHRFSLEGDAPVSWTETKKQSFKQTGEFGEKRKNSILNPINSIRKFSIVQKTPLQMNGIEEDSDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSVNQGQNIHRKTTASTRKVSLAPQANLTELDIYSRRLSQETGLEISEEINEEDLKECFFDDMESIPAVTTWNTYLRYITVHKSLIFVLIWCLVIFLAEVAASLVVLWLLGNTPLQDKGNSTHSRNNSYAVIITSTSSYYVFYIYVGVADTLLAMGFFRGLPLVHTLITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFISILTTGEGEGRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFIDMPTEGKPTKSTKPYKNGQLSKVMIIENSHVKKDDIWPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQAISPSDRVKLFPHRNSSKCKSKPQIAALKEETEEEVQDTRL Circular dichroism Limited proteolysis 1 707 Undetermined Relationship to function unknown Unknown 708 831 Disordered Function arises from the disordered (extended) state Autoregulatory Phosphorylation 832 1480 Undetermined Relationship to function unknown Unknown Ostedgaard, L. 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Intrinsic structural disorder and sequence features of the cell cycle inhibitor p57Kip2 2002 Proteins 46 1 7 11746698 Cyclin-dependent kinase inhibitor 1B Cyclin-dependent kinase inhibitor p27 p27Kip1 1168871 P46527 1JSU 198 MSNVRVSNGSPSLERMDARQAEHPKPSACRNLFGPVDHEELTRDLEKHCRDMEEASQRKWNFDFQNHKPLEGKYEWQEVEKGSLPEFYYRPPRPPKGACKVPAQESQDVSGSRPAAPLIGAPANSEDTHLVDPKTDPSDSQTGLAEQCAGIRKRPATDDSSTQNKRANRTEENVSDGSPNAGSVEQTPKKPGLRRRQT Circular dichroism Intrinsic Fluorescence X-ray crystallography 1 21 Undetermined Relationship to function unknown Unknown 22 106 Disordered Function arises via a disorder to order transition Protein-protein binding 107 198 Undetermined Relationship to function unknown Unknown Russo, A. A., Jeffrey, P. D., Patten, A. K., Massague, J., and Pavletich, N. P. Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex 1996 Nature 381 325 331 8684460 Flaugh, S. L., and Lumb, K. J. 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Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex 1998 Science 281 64 71 9651245 DNA-binding protein RAP1 SBF-E Repressor/activator site binding protein TUF 730473 P11938 1IGN S50714 827 MSSPDDFETAPAEYVDALDPSMVVVDSGSAAVTAPSDSAAEVKANQNEENTGATAAETSEKVDQTEVEKKDDDDTTEVGVTTTTPSIADTAATANIASTSGASVTEPTTDDTAADEKKEQVSGPPLSNMKFYLNRDADAHDSLNDIDQLARLIRANGGEVLDSKPRESKENVFIVSPYNHTNLPTVTPTYIKACCQSNSLLNMENYLVPYDNFREVVDSRLQEESHSNGVDNSNSNSDNKDSIRPKTEIISTNTNGATEDSTSEKVMVDAEQQARLQEQAQLLRQHVSSTASITSGGHNDLVQIEQPQKDTSNNNNSNVNDEDNDLLTQDNNPQTADEGNASFQAQRSMISRGALPSHNKASFTDEEDEFILDVVRKNPTRRTTHTLYDEISHYVPNHTGNSIRHRFRVYLSKRLEYVYEVDKFGKLVRDDDGNLIKTKVLPPSIKRKFSADEDYTLAIAVKKQFYRDLFQIDPDTGRSLITDEDTPTAIARRNMTMDPNHVPGSEPNFAAYRTQSRRGPIAREFFKHFAEEHAAHTENAWRDRFRKFLLAYGIDDYISYYEAEKAQNREPEPMKNLTNRPKRPGVPTPGNYNSAAKRARNYSSQRNVQPTANAASANAAAAAAAAASNSYAIPENELLDEDTMNFISSLKNDLSNISNSLPFEYPHEIAEAIRSDFSNEDIYDNIDPDTISFPPKIATTDLFLPLFFHFGSTRQFMDKLHEVISGDYEPSQAEKLVQDLCDETGIRKNFSTSILTCLSGDLMVFPRYFLNMFKDNVNPPPNVPGIWTHDDDESLKSNDQEQIRKLVKKHGTGRMEMRKRFFEKDLL Limited proteolysis X-ray crystallography 482 512 Disordered Relationship to function unknown Unknown Konig, P., Giraldo, R., Chapman, L., and Rhodes, D. The crystal structure of the DNA-binding domain of yeast RAP1 in complex with telomeric DNA 1996 Cell 85 125 136 8620531 Elongation Factor G Without Nucleotide Elongation factor G 1827912 P13551 1ELO S15928 691 MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERERGITITAAVTTCFWKDHRINIIDTPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSETVWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDVLRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEEELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVEIHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHANHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKADQEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDANVGKPQVAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIPAVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYHEVDSSEMAFKIAGSMAIKEAVQKGDPVILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLRSKTQGRGSFVMFFDHYQEVPKQVQEKLIKGQ X-ray crystallography 40 67 Disordered Relationship to function unknown Unknown 400 475 Disordered Relationship to function unknown Autoregulatory Flexible linkers/spacers Protein-rRNA binding AEvarsson, A., Brazhnikov, E., Garber, M., Zheltonosova, J., Chirgadze, Y., al-Karadaghi, S., Svensson, L. A., and Liljas, A. Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus 1994 EMBO Journal 13 3669 3677 8070397 Laurberg, M., Kristensen, O., Martemyanov, K., Gudkov, A. T., Nagaev, I., Hughes, D., and Liljas, A. Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site 2000 J. Mol. Biol. 303 593 603 11054294 Martemyanov, K. A., and Gudkov, A. T Domain III of elongation factor G from Thermus thermophilus is essential for induction of GTP hydrolysis on the ribosome 2000 J. Biol. Chem. 275 35820 35824 10940297 EMB-1 PROTEIN Embryonic abundant protein from carrot 119316 P17639 JQ2273 92 MASQQEKKELDARARQGETVVPGGTGGKSLEAQQHLAEGRSKGGQTRKEQLGGEGYHEMGRKGGLSNNDMSGGERAEQEGIDIDESKFRTKK Nuclear magnetic resonance spectroscopy 1 92 Disordered Relationship to function unknown Substrate/ligand binding Eom, J., Baker, W., Kintanar, A., and Wurtele, E. The embryo-specific EMB-1 protein of Daucus Carota is flexible and unstructured in solution 1996 Plant Science 115 17 24 Estradiol 17 beta-dehydrogenase 1 EC 1.1.1.62 17-beta-HSD 1 Placental 17-beta-hydroxysteroid dehydrogenase 20 alpha-hydroxysteroid dehydrogenase 20-alpha-HSD E2DH Estrogenic 17-Beta Hydroxysteroid Dehydrogenase Complexed 17-Beta-Estradiol 2392375 P14061 1IOL A36081 327 ARTVVLITGCSSGIGLHLAVRLASDPSQSFKVYATLRDLKTQGRLWEAARALACPPGSLETLQLDVRDSKSVAAARERVTEGRVDVLVCNAGLGLLGPLEALGEDAVASVLEVNVVGTVRMLQAFLPDMKRRGSGRVLVTGSVGGLMGLPFNDVYCASKFALEGLCESLAVLLLPFGVHLSLIECGPVHTAFMEKVLGSPEEVLDRTDIHTFHRFYQYLAHSKQVFREAAQNPEEVAEVFLTALRAPKPTLRYFTTERFLPLLRMRLDDPSGSNYVTAMHREVFGDVPAKAEAGAEAGGGAGPGAEDEAGRSAVGDPELGDPPAAPQ X-ray crystallography 285 327 Disordered Relationship to function unknown Disordered region is not essential for protein function Protein-lipid interaction Ghosh, D., Pletnev, V. Z., Zhu, D. W., Wawrzak, Z., Duax, W. L., Pangborn, W., Labrie, F., and Lin, S. X. Structure of human estrogenic 17 beta-hydroxysteroid dehydrogenase at 2.20 A resolution 1995 Structure 3 503 513 7663947 E7 protein E7 protein from HPV16 6469700 P03129 A03688 93 MHGDTPTLHEYMLDLQPETTDLYCYEQLSDSSEEEDEIDGPAGQAEPDRAHYNIVTFCCKCDSTLRLCVQSTHVDIRTLEDLLMGTLGIVCPI Circular dichroism 1 93 Disordered Function arises via a disorder to order transition Metal binding Protein-protein binding Pahel, G., Aulabaugh, A., Short, S. A., Barnes, J. A., Painter, G. R., Ray, P., and Phelps, W. C. Structural and functional characterization of the HPV16 E7 protein expressed in bacteria 1993 J. Biol. Chem. 268 26018 26025 8245034 Fibronectin-binding protein precursor FNBP Fibronectin binding protein 120457 P14738 1018 MKNNLRYGIRKHKLGAASVFLGTMIVVGMGQDKEAAASEQKTTTVEENGNSATDNKTSETQTTATNVNHIEETQSYNATVTEQPSNATQVTTEEAPKAVQAPQTAQPANIETVKEEVVKEEAKPQVKETTQSQDNSGDQRQVDLTPKKATQNQVAETQVEVAQPRTASESKPRVTRSADVAEAKEASNAKVETGTDVTSKVTVEIGSIEGHNNTNKVEPHAGQRAVLKYKLKFENGLHQGDYFDFTLSNNVNTHGVSTARKVPEIKNGSVVMATGEVLEGGKIRYTFTNDIEDKVDVTAELEINLFIDPKTVQTNGNQTITSTLNEEQTSKELDVKYKDGIGNYYANLNGSIETFNKANNRFSHVAFIKPNNGKTTSVTVTGTLMKGSNQNGNQPKVRIFEYLGNNEDIAKSVYANTTDTSKFKEVTSNMSGNLNLQNNGSYSLNIENLDKTYVVHYDGEYLNGTDEVDFRTQMVGHPEQLYKYYYDRGYTLTWDNGLVLYSNKANGNEKNGPIIQNNKFEYKEDTIKETLTGQYDKNLVTTVEEEYDSSTLDIDYHTAIDGGGGYVDGYIETIEETDSSAIDIDYHTAVDSEAGHVGGYTESSEESNPIDFEESTHENSKHHADVVEYEEDTNPGGGQVTTESNLVEFDEESTKGIVTGAVSDHTTVEDTKEYTTESNLIELVDELPEEHGQAQGPVEEITKNNHHISHSGLGTENGHGNYDVIEEIEENSHVDIKSELGYEGGQNSGNQSFEEDTEEDKPKYEQGGNIVDIDFDSVPQIHGQNKGNQSFEEDTEKDKPKYEHGGNIIDIDFDSVPHIHGFNKHTEIIEEDTNKDKPSYQFGGHNSVDFEEDTLPKVSGQNEGQQTIEEDTTPPIVPPTPPTPEVPSEPETPTPPTPEVPSEPETPTPPTPEVPSEPETPTPPTPEVPAEPGKPVPPAKEEPKKPSKPVEQGKVVTPVIEINEKVKAVAPTKKPQSKKSELPETGGEESTNKGMLFGGLFSILGLALLRRNKKNHKA Nuclear magnetic resonance spectroscopy 1 744 Undetermined Relationship to function unknown Unknown 745 873 Disordered Function arises via a disorder to order transition Protein-protein binding 874 1018 Undetermined Relationship to function unknown Unknown Penkett, C. J., Redfield, C., Dodd, I., Hubbard, J., McBay, D. L., Mossakowska, D. E., Smith, R. A., Dobson, C. M., and Smith, L. J. NMR analysis of main-chain conformational preferences in an unfolded fibronectin-binding protein 1997 J. Mol. Biol. 274 152 159 9398523 Penkett, C. J., Redfield, C., Jones, J. A., Dodd, I., Hubbard, J., Smith, R. A., Smith, L. J., and Dobson, C. M. Structural and dynamical characterization of a biologically active unfolded fibronectin-binding protein from Staphylococcus aureus 1998 Biochemistry 37 17054 17067 9836601 Penkett, C. J., Dobson, C. M., Smith, L. J., Bright, J. R., Pickford, A. R., Campbell, I. D., and Potts, J. R. Identification of residues involved in the interaction of Staphylococcus aureus fibronectin-binding protein with the (4)F1(5)F1 module pair of human fibronectin using heteronuclear NMR spectroscopy 2000 Biochemistry 39 2887 2893 10715108 Flagellin - Salmonella typhimurium Flagellin 96744 P06179 S16121 494 AQVINTNSLSLLTQNNLNKSQSALGTAIERLSSGLRINSAKDDAAGQAIANRFTANIKGLTQASRNANDGISIAQTTEGALNEINNNLQRVRELAVQSANSTNSQSDLDSIQAEITQRLNEIDRVSGQTQFNGVKVLAQDNTLTIQVGANDGETIDIDLKQINSQTLGLDTLNVQQKYKVSDTAATVTGYADTTIALDNSTFKASATGLGGTDQKIDGDLKFDDTTGKYYAKVTVTGGTGKDGYYEVSVDKTNGEVTLAGGATSPLTGGLPATATEDVKNVQVANADLTEAKAALTAAGVTGTASVVKMSYTDNNGKTIDGGLAVKVGDDYYSATQNKDGSISINTTKYTADDGTSKTALNKLGGADGKTEVVSIGGKTYAASKAEGHNFKAQPDLAEAAATTTENPLQKIDAALAQVDTLRSDLGAVQNRFNSAITNLGNTVNNLTSARSRIEDSDYATEVSNMSRAQILQQAGTSVLAQANQVPQNVLSLLR Circular dichroism Nuclear magnetic resonance spectroscopy Thermal Stability X-ray crystallography 1 55 Disordered Function arises from the disordered (extended) state Function arises via a disorder to order transition Polymerization Protein-protein binding Self-transport through channel 451 494 Disordered Function arises from the disordered (extended) state Function arises via a disorder to order transition Polymerization Protein-protein binding Self-transport through channel Vonderviszt, F., Kanto, S., Aizawa, S., and Namba, K. Terminal regions of flagellin are disordered in solution 1989 J. Mol. Biol. 209 127 133 2810365 Aizawa, S. I., Vonderviszt, F., Ishima, R., and Akasaka, K. Termini of Salmonella flagellin are disordered and become organized upon polymerization into flagellar filament 1990 J. Mol. Biol. 211 673 677 2313691 Mimori-Kiyosue, Y., Yamashita, I., Fujiyoshi, Y., Yamaguchi, S., and Namba, K. Role of the outermost subdomain of Salmonella flagellin in the filament structure revealed by electron cryomicroscopy 1998 J. Mol. Biol. 284 521 530 9813134 Mimori-Kiyosue, Y., Vonderviszt, F., and Namba, K. Locations of terminal segments of flagellin in the filament structure and their roles in polymerization and polymorphism 1997 J. Mol. Biol. 270 (2) 222 237 9236124 Samatey, F. A., Imada, K., Nagashima, S., Vonderviszt, F., Kumasaka, T., Yamamoto, M., and Namba, K. Structure of the bacterial flagellar protofilament and implications for a switch for supercoiling 2001 Nature 410 331 337 11268201 Negative regulator of flagellin synthesis Anti-sigma-28 factor Flagellum specific sigma factor 120306 P26477 A41046 97 MSIDRTSPLKPVSTVQTRETSDTPVQKTRQEKTSAATSASVTLSDAQAKLMQPGVSDINMERVEALKTAIRNGELKMDTGKIADSLIREAQSYLQSK Nuclear magnetic resonance spectroscopy 1 97 Disordered Function arises from the disordered (extended) state Function arises via a disorder to order transition Protein-protein binding Self-transport through channel Daughdrill, G. W., Chadsey, M. S., Karlinsey, J. E., Hughes, K. T., and Dahlquist, F. W. The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, sigma 28 1997 Nat. Struct. Biol. 4 285 291 9095196 Daughdrill, G. W., Hanely, L. J., and Dahlquist, F. W. The C-terminal half of the anti-sigma factor FlgM contains a dynamic equilibrium solution structure favoring helical conformations 1998 Biochemistry 37 1076 1082 9454599 Eukaryotic translation initiation factor 4E binding protein 1 4E-binding protein 1 4758258 Q13541 S50866 118 MSGGSSCSQTPSRAIPATRRVVLGDGVQLPPGDYSTTPGGTLFSTTPGGTRIIYDRKFLMECRNSPVTKTPPRDLPTIPGVTSPSSDEPPMEASQSHLRNSPEDKRAGGEESQFEMDI Circular dichroism Nuclear magnetic resonance spectroscopy X-ray crystallography 1 118 Disordered Function arises from the disordered (extended) state Function arises via a disorder to order transition Phosphorylation Protein-protein binding Fletcher, C. M., McGuire, A. M., Gingras, A. C., Li, H., Matsuo, H., Sonenberg, N., and Wagner, G. 4E binding proteins inhibit the translation factor eIF4E without folded structure 1998 Biochemistry 37 9 15 9453748 Fletcher, C. M., and Wagner, G. The interaction of eIF4E with 4E-BP1 is an induced fit to a completely disordered protein 1998 Protein Sci. 7 1639 1642 9684899 Gingras, A. C., Gygi, S. P., Raught, B., Polakiewicz, R. D., Abraham, R. T., Hoekstra, M. F., Aebersold, R., and Sonenberg, N. Regulation of 4E-BP1 phosphorylation: a novel two-step mechanism 1999 Genes Dev. 13 1422 1437 10364159 Glycine N-Methyltransferase Glial cell-derived neurotrophic factor 729568 Q07731 1AGQ A37499 135 MSPDKQAAALPRRERNRQAAAASPENSRGKGRRGQRGKNRGCVLTAIHLNVTDLGLGYETKEELIFRYCSGSCEAAETMYDKILKNLSRSRRLTSDKVGQACCRPVAFDDDLSFLDDSLVYHILRKHSAKRCGCI X-ray crystallography 1 38 Disordered Function arises via a disorder to order transition Protein-protein binding Eigenbrot, C., and Gerber, N. X-ray structure of glial cell-derived neurotrophic factor at 1.9 A resolution and implications for receptor binding 1997 Nat. Struct. Biol. 4 435 438 9187648 Eketjall, S., Fainzilber, M., Murray-Rust, J., and Ibanez, C. F. Distinct structural elements in GDNF mediate binding to GFRalpha1 and activation of the GFRalpha1-c-Ret receptor complex 1999 EMBO Journal 18 5901 5910 10545102 Ibanez, C. F. Personal communication Part of GI: 729568 Part of SP: Q07731 glucocorticoid receptor DNA binding factor 1 [Homo sapiens] Glucocorticoid receptor 4758482 835 MDATSHIDNMENERIPFDLMDTVPAEALYEAHLEKLRNERKRVEMRRAFKENLETSPFITPGKPWEEARSFIMNEDFYQWLEESVYTDIYGKHQKQIIDKAKEEFQELLLEYSELFYELELDAKPSKEKMGVIQDVLGEEQRFKAIYKSSKQSVDALILKHIHFVYHPTKETCPSCPACVDAKIEHLISSRFIRPSDRNQKNSLSDPNIDRINLVILGKDALPESWPMEIRALCTNDDKYVIDGKMYELSLRPIEGNVRLPVNSFQTPTFQPHGCLCLYNSKESLSYVVESIEKSRESTLGRRDNHLVHLPLTLILVNKRGDTSGETLHSLIQQGQQIASKLQCVFLDPASAGIGYGRNINEKQISQVLKGLLDSKRNLNLVSSTASIKDLADVDLRIVMCLMCGDPFSADDILFPVLQSQTCKSSHCGSNNSVLLELPIGLHKKRIELSVLSYHSSFSIRKSRLVHGYIVFYSAKRKASLAMLRAFLCEVQDIIPIQLVALTDGAVDVLDNDLSREQLTEGEEIAQEIDGRFTSIPCSQPQHKLEIFHPFFKDVVEKKNIIEATHMYDNAAEACSTTEEVFNSPRAGSPLCNSNLQDSEEDIEPSYSLFREDTSLPSLSKDHSKLSMELEGNDGLSFIMSNFESKLNNKVPPPVKPKPPVHFEITKGDLSYLDQGHRDGQRKSVSSSPWLPQDGFDPSDYAEPMDAVVKPRNEEENIYSVPHDSTQGKIITIRNINKAQSNGSGNGSDSEMDTSSLERGRKVSIVSKPVLYRTRCTRLGGLLVTGPASAWGVMMSWGPSGRKRRIRHPRVIKGTMLSFHTKQTKTRGGGIFFAA Circular dichroism Intrinsic Fluorescence 1 76 Undetermined Relationship to function unknown Unknown 77 262 Disordered Function arises via a disorder to order transition Protein-protein binding 263 835 Undetermined Relationship to function unknown Unknown Baskakov, I. V., Kumar, R., Srinivasan, G., Ji, Y. S., Bolen, D. W., and Thompson, E. B. Trimethylamine N-oxide-induced cooperative folding of an intrinsically unfolded transcription-activating fragment of human glucocorticoid receptor 1999 J. Biol. Chem. 274 10693 10696 10196139 121328 P13255 1D2H S00112 292 VDSVYRTRSLGVAAEGIPDQYADGEAARVWQLYIGDTRSRTAEYKAWLLGLLRQHGCHRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYALKERWNRRKEPAFDKWVIEEANWLTLDKDVPAGDGFDAVICLGNSFAHLPDSKGDQSEHRLALKNIASMVRPGGLLVIDHKNYDYILSTGCAPPGKNIYYKSDLTKDITTSVLTVNNKAHMVTLDYTVQVPGAGRDGAPGFSKFRLSYYPHCLASFTELVQEAFGGRCQHSVLGDFKPYRPGQAYVPCYFIHVLKKTG X-ray crystallography 1 40 Disordered Function arises via a disorder to order transition Relationship to function unknown Substrate/ligand binding Huang, Y., Komoto, J., Konishi, K., Takata, Y., Ogawa, H., Gomi, T., Fujioka, M., and Takusagawa, F. Mechanisms for auto-inhibition and forced product release in glycine N-methyltransferase: crystal structures of wild-type, mutant R175K and S-adenosylhomocysteine-bound R175K enzymes 2000 J. Mol. Biol. 298 149 162 10756111 Takusagawa, F. Personal communication Part of GI: 121328 Part of SP: P13255 Glycyl-tRNA Synthetase Glycyl-tRNA Ligase 2829475 P56206 1GGM 442 AASSLDELVALCKRRGFIFQSSEIYGGLQGVYDYGPLGVELKNNLKQAWWRRNVYERDDMEGLDASVLTHRLVLHYSGHEATFADPMVDNAKARYWTPPRYFNMMFQDLRGPRGGRGLLAYLRPETAQGIFVNFKNVLDATSRKLGFGIAQIGKAFRNEITPRNFIFRVREFEQMEIEYFVRPGEDEYWHRYWVEERLKWWQEMGLSRENLVPYQQPPESSAHYAKATVDILYRFPHGSLELEGIAQRTDFDLGSHTKDQEALGITARVLRNEHSTQRLAYRDPETGKWFVPYVIEPSAGVDRGVLALLAEAFTREELPNGEERIVLKLKPQLAPIKVAVIPLVKNRPEITEYAKRLKARLLALGLGRVLYEDTGNIGKAYRRHDEVGTPFAVTVDYDTIGQSKDGTTRLKDTVTVRDRDTMEQIRLHVDELEGFLRERLRW X-ray crystallography 96 158 Disordered Relationship to function unknown Unknown Logan, D. T., Mazauric, M. H., Kern, D., and Moras, D. Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus 1995 EMBO Journal 14 4156 4167 7556056 Arnez, J. G., Dock-Bregeon, A. C., and Moras, D. Glycyl-tRNA synthetase uses a negatively charged pit for specific recognition and activation of glycine 1999 J. Mol. Biol. 286 1449 1459 10064708 121180 P10912 1A22 A33991 238 FSGSEATAAILSRAPWSLQSVNPGLKTNSSKEPKFTKCRSPERETFSCHWTDEVHHGTKNLGPIQLFYTRRNTQEWTQEWKECPDYVSAGENSCYFNSSFTSIWIPYCIKLTSNGGTVDEKCFSVDEIVQPDPPIALNWTLLNVSLTGIHADIQVRWEAPRNADIQKGWMVLEYELQYKEVNETKWKMMDPILTTSVPVYSLKVDKEYEVRVRSKQRNSGNYGEFSEVLYVTLPQMSQ X-ray crystallography 1 32 Disordered Function arises via a disorder to order transition Disordered region is not essential for protein function Protein-protein binding Clackson, T., Ultsch, M. H., Wells, J. A., and de Vos, A. M. Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity 1998 J. Mol. Biol. 277 1111 1128 9571026 Clackson, T., and Wells, J. A. A hot spot of binding energy in a hormone-receptor interface 1995 Science 267 383 386 7529940 Coat protein A [Precursor] G3P g3p (fd phage minor coat protein) 5822481 P03661 A04266 424 MKKLLFAIPLVVPFYSHSAETVESCLAKPHTENSFTNVWKDDKTLDRYANYEGCLWNATGVVVCTGDETQCYGTWVPIGLAIPENEGGGSEGGGSEGGGSEGGGTKPPEYGDTPIPGYTYINPLDGTYPPGTEQNPANPNPSLEESQPLNTFMFQNNRFRNRQGALTVYTGTVTQGTDPVKTYYQYTPVSSKAMYDAYWNGKFRDCAFHSGFNEDPFVCEYQGQSSDLPQPPVNAGGGSGGGSGGGSEGGGSEGGGSEGGGSEGGGSGGGSGSGDFDYEKMANANKGAMTENADENALQSDAKGKLDSVATDYGAAIDGFIGDVSGLANGNGATGDFAGSNSQMAQVGDGDNSPLMNNFRQYLPSLPQSVECRPYVFGAGKPYEFSIDCDKINLFRGVFAFLLYVATFMYVFSTFANILRNKES X-ray crystallography 236 274 Disordered Function arises from the disordered (extended) state Flexible linkers/spacers Holliger, P., Riechmann, L., and Williams, R. L. Crystal structure of the two N-terminal domains of g3p from filamentous phage fd at 1.9 A: evidence for conformational lability 1999 J. Mol. Biol. 288 649 657 10329170 Nilsson, N., Malmborg, A. C., and Borrebaeck, C. A. The phage infection process: a functional role for the distal linker region of bacteriophage protein 3 2000 J. Virol. 74 4229 4235 10756036 Guanine Nucleotide-Binding Protein Alpha-1 Subunit Gia1, Guanine Nucleotide-Binding Protein G(I), Alpha-1 Subunit G protein Gi Alpha 1 121020 P10824 1CIP C27423 353 GCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDAARADDARQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF X-ray crystallography 1 31 Disordered Function arises from the disordered (extended) state Function arises via a disorder to order transition Fatty acylation (myristolation and palmitoylation) Protein-lipid interaction Protein-protein binding Coleman, D. E., Berghuis, A. M., Lee, E., Linder, M. E., Gilman, A. G., and Sprang, S. R. Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis 1994 Science 265 1405 1412 8073283 Coleman, D. E., and Sprang, S. R. Structure of Gialpha1.GppNHp, autoinhibition in a galpha protein-substrate complex 1999 J. Biol. Chem. 274 16669 16672 10358003 Heat shock factor protein HSF Heat shock transcription factor HSTF 123686 P22121 1FBQ S13365 677 MGHNDSVETMDEISNPNNILLPHDGTGLDATGISGSQEPYGMVDVLNPDSLKDDSNVDEPLIEDIVNPSLDPEGVVSAEPSNEVGTPLLQQPISLDHVITRPASAGGVYSIGNSSTSSAAKLSDGDLTNATDPLLNNAHGHGQPSSESQSHSNGYHKQGQSQQPLLSLNKRKLLAKAHVDKHHSKKKLSTTRARPAFVNKLWSMVNDKSNEKFIHWSTSGESIVVPNRERFVQEVLPKYFKHSNFASFVRQLNMYGWHKVQDVKSGSMLSNNDSRWEFENENFKRGKEYLLENIVRQKSNTNILGGTTNAEVDIHILLNELETVKYNQLAIAEDLKRITKDNEMLWKENMMARERHQSQQQVLEKLLRFLSSVFGPNSAKTIGNGFQPDLIHELSDMQVNHMSNNNHNNTGNINPNAYHNETDDPMANVFGPLTPTDQGKVPLQDYKLRPRLLLKNRSMSSSSSSNLNQRQSPQNRIVGQSPPPQQQQQQQQQQGQPQGQQFSYPIQGGNQMMNQLGSPIGTQVGSPVGSQYGNQYGNQYSNQFGNQLQQQTSRPALHHGSNGEIRELTPSIVSSDSPDPAFFQDLQNNIDKQEESIQEIQDWITKLNPGPGEDGNTPIFPELNMPSYFANTGGSGQSEQPSDYGDSQIEELRNSRLHEPDRSFEEKNNGQKRRRAA Circular dichroism Nuclear magnetic resonance spectroscopy 1 196 Disordered Function arises from the disordered (extended) state Protein-protein binding 219 223 Disordered Relationship to function unknown Unknown 261 276 Disordered Relationship to function unknown Unknown 280 282 Disordered Relationship to function unknown Unknown 283 677 Undetermined Relationship to function unknown Unknown Cho, H. S., Liu, C. W., Damberger, F. F., Pelton, J. G., Nelson, H. C., and Wemmer, D. E. Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy 1996 Protein Science 5 262 269 8745404 Heparin-Binding Epidermal Growth Factor Hbegf Heparin-binding EGF-like growth factor 544477 Q99075 1XDT A38432 79 GSHMRVTLSSKPQALATPNKEEHGKRKKKGKGLGKKRDPCLRKYKDFCIHGECKYVKELRAPSCICHPGYHGERCHGLS X-ray crystallography 1 38 Disordered Relationship to function unknown Unknown Louie, G. V., Yang, W., Bowman, M. E., and Choe, S. Crystal structure of the complex of diphtheria toxin with an extracellular fragment of its receptor 1997 Mol. Cell 1 67 78 9659904 Higashiyama, S., Lau, K., Besner, G. E., Abraham, J. A., and Klagsbrun, M. Structure of heparin-binding EGF-like growth factor. Multiple forms, primary structure, and glycosylation of the mature protein 1992 J Biol Chem 267 6205 6212 1556128 high-mobility group (nonhistone chromosomal) protein 14 Nonhistone chromosomal protein HMG-14 human non-histone chromosomal protein HMG-14 [Homo sapiens] High mobility group - 14 4826758 P05114 A33310 100 MPKRKVSSAEGAAKEEPKRRSARLSAKPPAKVEAKPKKAAAKDKSSDKKVQTKGKRGAKGKQAEVANQETKEDLPAENGETKTEESPASDEAGEKEAKSD Circular dichroism Infrared Spectroscopy Nuclear magnetic resonance spectroscopy 1 100 Disordered Function arises from the disordered (extended) state Function arises via a disorder to order transition Acetylation Phosphorylation Protein-DNA binding Protein-protein binding Cary, P. D., King, D. S., Crane-Robinson, C., Bradbury, E. M., Rabbani, A., Goodwin, G. H., and Johns, E. W. Structural studies on two high-mobility-group proteins from calf thymus, HMG-14 and HMG-20 (ubiquitin), and their interaction with DNA 1980 Eur. J. Biochem. 112 577 580 6257511 Abercrombie, B. D., Kneale, G. G., Crane-Robinson, C., Bradbury, E. M., Goodwin, G. H., Walker, J. M., and Johns, E. W. Studies on the conformational properties of the high-mobility-group chromosomal protein HMG 17 and its interaction with DNA 1978 Eur. J. Biochem. 84 173 177 565710 Louie, D. F., Gloor, K. K., Galasinski, S. C., Resing, K. A., and Ahn, N. G. Phosphorylation and subcellular redistribution of high mobility group proteins 14 and 17, analyzed by mass spectrometry 2000 Protein Science 9 170 179 10739259 Bergel, M., Herrera, J. E., Thatcher, B. J., Prymakowska-Bosak, M., Vassilev, A., Nakatani, Y., Martin, B., and Bustin, M. Acetylation of novel sites in the nucleosomal binding domain of chromosomal protein HMG-14 by p300 alters its interaction with nucleosomes 2000 J. Biol. Chem. 275 11514 11520 10753971 high-mobility group nucleosomal binding domain 2 nonhistone chromosomal protein HMG-17 high mobility group protein N2 high-mobility group (nonhistone chromosomal) protein 17 [Homo sapiens] High mobility group - 17 5031749 P05204 S03700 90 MPKRKAEGDAKGDKAKVKDEPQRRSARLSAKPAPPKPEPKPKKAPAKKGEKVPKGKKGKADAGKEGNNPAENGDAKTDQAQKAEGAGDAK Circular dichroism Infrared Spectroscopy Nuclear magnetic resonance spectroscopy Small-angle X-ray Scattering 1 90 Disordered Function arises from the disordered (extended) state Function arises via a disorder to order transition Acetylation Phosphorylation Protein-DNA binding Protein-protein binding Cary, P. D., King, D. S., Crane-Robinson, C., Bradbury, E. M., Rabbani, A., Goodwin, G. H., and Johns, E. W. Structural studies on two high-mobility-group proteins from calf thymus, HMG-14 and HMG-20 (ubiquitin), and their interaction with DNA 1980 Eur. J. Biochem. 112 577 580 6257511 Abercrombie, B. D., Kneale, G. G., Crane-Robinson, C., Bradbury, E. M., Goodwin, G. H., Walker, J. M., and Johns, E. W. Studies on the conformational properties of the high-mobility-group chromosomal protein HMG 17 and its interaction with DNA 1978 Eur. J. Biochem. 84 173 177 565710 Louie, D. F., Gloor, K. K., Galasinski, S. C., Resing, K. A., and Ahn, N. G. Phosphorylation and subcellular redistribution of high mobility group proteins 14 and 17, analyzed by mass spectrometry 2000 Protein Science 9 170 179 10739259 Bergel, M., Herrera, J. E., Thatcher, B. J., Prymakowska-Bosak, M., Vassilev, A., Nakatani, Y., Martin, B., and Bustin, M. Acetylation of novel sites in the nucleosomal binding domain of chromosomal protein HMG-14 by p300 alters its interaction with nucleosomes 2000 J. Biol. Chem. 275 11514 11520 10753971 High mobility group protein HMG-I/HMG-Y HMG-I(Y) High mobility group AT-hook 1 High mobility group - I(Y) 123377 P17096 2EZD A32794 107 MSESSSKSSQPLASKQEKDGTEKRGRGRPRKQPPVSPGTALVGSQKEPSEVPTPKRPRGRPKGSKNKGAAKTRKTTTTPGRKPRGRPKKLEKEEEEGISQESSEEEQ Nuclear magnetic resonance spectroscopy 1 107 Disordered Function arises from the disordered (extended) state Function arises via a disorder to order transition Acetylation Phosphorylation Protein-DNA binding Protein-protein binding Huth, J. R., Bewley, C. A., Nissen, M. S., Evans, J. N., Reeves, R., Gronenborn, A. M., and Clore, G. M. The solution structure of an HMG-I(Y)-DNA complex defines a new architectural minor groove binding motif 1997 Nat. Struct. Biol. 4 657 665 9253416 Pierantoni, G. M., Fedele, M., Pentimalli, F., Benvenuto, G., Pero, R., Viglietto, G., Santoro, M., Chiariotti, L., and Fusco, A. High mobility group I (Y) proteins bind HIPK2, a serine-threonine kinase protein which inhibits cell growth 2001 Oncogene 20 6132 6141 11593421 Munshi, N., Agalioti, T., Lomvardas, S., Merika, M., Chen, G., and Thanos, D. Coordination of a transcriptional switch by HMGI(Y) acetylation 2001 Science 293 1133 1136 11498590 High mobility group-T protein HMG-T HMG-T1 HMG-1 123382 P07746 A24019 204 MGKDPRKPRGKMSSYAYFVQTRREEHKKKHPEASVNFSEFSKKCSERWKTMSAKEKGKFEDLAKLDKVRYEREMRSYIPPKGEKKKRFKDPNAPKRPSSAFFIFCADFRPQVKGETPGLSIGDVAKKLGEKWNNLTAEDKVPYEKKASRLKEKYEKDITAYRNKGKVPVSMPAKAAAPAKDDDDDDDDDDDDEDDDDDDDEDDE Circular dichroism Nuclear magnetic resonance spectroscopy 1 204 Disordered Function arises via a disorder to order transition Protein-DNA binding Cary, P. D., Crane-Robinson, C., Bradbury, E. M., and Dixon, G. H. Structural studies of the non-histone chromosomal proteins HMG-T and H6 from trout testis 1981 Eur. J. Biochem. 119 545 551 6273163 NONHISTONE CHROMOSOMAL PROTEIN H6 HISTONE T High mobility group - H6 462245 P02315 A02653 70 MPKRKSATKGDEPARRSARLSARPVPKPAAKPKKAAAPKKAVKGKKAAENGDAKAEAKVQAAGDGAGNAK Circular dichroism Nuclear magnetic resonance spectroscopy 1 70 Disordered Function arises via a disorder to order transition Protein-DNA binding Cary, P. D., Crane-Robinson, C., Bradbury, E. M., and Dixon, G. H. Structural studies of the non-histone chromosomal proteins HMG-T and H6 from trout testis 1981 Eur. J. Biochem. 119 545 551 6273163 211857 Q92068 I50244 136 MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA X-ray crystallography 1 40 Disordered Function arises from the disordered (extended) state Acetylation Methylation Phosphorylation Lambert, S. J., Nicholson, J. M., Chantalat, L., Reid, A. J., Donovan, M. J., and Baldwin, J. P. Purification of histone core octamers and 2.15 A X-ray analysis of crystals in KCl/phosphate 1999 Acta. Crystallogr. D. Biol. Crystallogr. 55 1048 1051 10216302 Nakayama, J., Rice, J. C., Strahl, B. D., Allis, C. D., and Grewal, S. I. Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly 2001 Science 292 110 113 11283354 70678 P02259 A93487 189 TESLVLSPAPAKPKRVKASRRSASHPTYSEMIAAAIRAEKSRGGSSRQSIQKYIKSHYKVGHNADLQIKLSIRRLLAAGVLKQTKGVGASGSFRLAKSDKAKRSPGKKKKAVRRSTSPKKAARPRKARSPAKKPKATARKARKKSRASPKKAKKPKTVKAKSRKASKAKKVKRSKPRAKSGARKSPKKK Limited proteolysis X-ray crystallography 1 21 Disordered Relationship to function unknown Unknown 101 185 Disordered Function arises via a disorder to order transition Protein-DNA binding Aviles, F. J., Chapman, G. E., Kneale, G. G., Crane-Robinson, C., and Bradbury, E. M. A nuclear-magnetic-resonance study of the globular structure of the H5 histone 1978 Eur. J. Biochem. 88 363 371 710431 Ramakrishnan, V., Finch, J. T., Graziano, V., Lee, P. L., and Sweet, R. M. Crystal structure of globular domain of histone H5 and its implications for nucleosome binding 1993 Nature 362 219 223 8384699 Graziano, V., Gerchman, S. E., Wonacott, A. J., Sweet, R. M., Wells, J. R., White, S. W., and Ramakrishnan, V. Crystallization of the globular domain of histone H5 1990 J. Mol. Biol. 212 253 257 2181148 Crane-Robinson, C. Personal communication 6435814 Q27796 1TC1 220 PREYEFAEKILFTEEEIRTRIKEVAKRIADDYKGKGLRPYVNPLVLISVLKGSFMFTADLCRALCDFNVPVRMEFICVSSYGEGLTSSGQVRMLLDTRHSIEGHHVLIVEDIVDTALTLNYLYHMYFTRRPASLKTVVLLDKREGRRVPFSADYVVANIPNAFVIGYGLDYDDTYRELRDIVVLRPEVYAEREAARQKKQRAIGSADTDRDAKREFHSKY X-ray crystallography 190 220 Disordered Relationship to function unknown Unknown Focia, P. J., Craig, S. P., 3rd, Nieves-Alicea, R., Fletterick, R. J., and Eakin, A. E. A 1.4 A crystal structure for the hypoxanthine phosphoribosyltransferase of Trypanosoma cruzi 1998 Biochemistry 37 15066 15075 9790669 6537322 Q9QXN1 2LEF 397 MPQLSGGGGGGDPELCATDEMIPFKDEGDPQKEKIFAEISHPEEEGDLADIKSSLVNESEIIPASNGHEVVGQTQSSQEPYHDKAREHPDDGKHPDGGLYNKGPSYSSYSGYIMMPNMNSDPYMSNGSLSPPIPRTSNKVPVVQPSHAVHPLTPLITYSDEHFSPGSHPSHIPSEVNPKQGMSRHPPAPEMPTFYPLSPGGVGQITPPLGWQGQPVYPITGGFRQAYPSSLSGDTSMSRFSHHMIPGPPGPHTTGIPHPAIVTPQVKQEHPHTDSDLMHVKPEHEQRKEQEPKRPHIKKPLNAFMLYMKEMRANVVAECTLKESAAINQILGRRWHALSREEQAKYYELARKERQLHMQLYPGWSARDNYGKKKKRKREKLQESTSGTGPRMTAAYI Nuclear magnetic resonance spectroscopy 1 295 Undetermined Relationship to function unknown Unknown 296 397 Disordered Function arises via a disorder to order transition DNA bending Protein-DNA binding Love, J. J., Li, X., Case, D. A., Giese, K., Grosschedl, R., and Wright, P. E. Structural basis for DNA bending by the architectural transcription factor LEF-1 1995 Nature 376 791 795 7651541 Myelin basic protein MBP Myelin A1 protein 20 kDa microtubule stabilizing protein 126796 P02687 A92089 169 AAQKRPSQRSKYLASASTMDHARHGFLPRHRDTGILDSLGRFFGSDRGAPKRGSGKDGHHAARTTHYGSLPQKAQGHRPQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQKPGFGYGGRASDYKSAHKGLKGHDAQGTLSKIFKLGGRDSRSGSPMARR Circular dichroism 1 169 Disordered Function arises via a disorder to order transition Protein-lipid interaction Polverini, E., Fasano, A., Zito, F., Riccio, P., and Cavatorta, P. Conformation of bovine myelin basic protein purified with bound lipids 1999 Eur. Biophys. J. 28 351 355 10394626 Negative factor F-protein 27 kDa protein 3'ORF Negative factor, HIV1 128023 P03406 1AVV A04008 206 MGGKWSKSSVVGWPTVRERMRRAEPAADGVGAASRDLEKHGAITSSNTAATNAACAWLEAQEEEEVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPGPGVRYPLTFGWCYKLVPVEPDKVEEANKGENTSLLHPVSLHGMDDPEREVLEWRFDSRLAFHHVARELHPEYFKNC Nuclear magnetic resonance spectroscopy X-ray crystallography 1 73 Disordered Function arises from the disordered (extended) state Function arises via a disorder to order transition Fatty acylation (myristolation and palmitoylation) Phosphorylation Protein-lipid interaction Protein-protein binding Regulation of proteolysis in vivo 149 178 Disordered Relationship to function unknown Protein-protein binding 204 206 Disordered Relationship to function unknown Unknown Lee, C. H., Saksela, K., Mirza, U. A., Chait, B. T., and Kuriyan, J. Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain 1996 Cell 85 931 942 8681387 Arold, S., Franken, P., Strub, M. P., Hoh, F., Benichou, S., Benarous, R., and Dumas, C. The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling 1997 Structure 5 1361 1372 9351809 Geyer, M., Munte, C. E., Schorr, J., Kellner, R., and Kalbitzer, H. R Structure of the anchor-domain of myristoylated and non-myristoylated HIV-1 Nef protein 1999 J. Mol. Biol. 289 123 138 10339411 Arold, S. T., and Baur, A. S. Dynamic Nef and Nef dynamics: how structure could explain the complex activities of this small HIV protein 2001 Trends Biochem. Sci. 26 356 363 11406408 1511632 P70475 T46637 1187 MDVDAEEKRHRTRSKGVRVPVEPAIQELFSCPTPGCDGTGHVSGKYARHRSVYGCPLAKKRKTQDKQPQ