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 106 MSDSIISFAAFILADAGLEITSDNLLTITKAAGANVDNVWADVYAKALEGKDLKEILSGFHNAGPVAGAGAASGAAAAGGDAAAEEEKEEEAAEESDDDMGFGLFD Circular dichroism Limited proteolysis Nuclear magnetic resonance spectroscopy Other techniques 1 106 106 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 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 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 Ballesta, J. P. Personal communication 60S acidic ribosomal protein P2-beta Acidic ribosomal stalk protein P2 133071 P02400 110 MKYLAAYLLLVQGGNAAPSAADIKAVVESVGAEVDEARINELLSSLEGKGSLEEIIAEGQKKFATVPTGGASSAAAGAAGAAAGGDAAEEEKEEEAKEESDDDMGFGLFD Circular dichroism Limited proteolysis Nuclear magnetic resonance spectroscopy Other techniques 1 110 110 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 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 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 Ballesta, J. P. Personal communication Early E2a Dna-Binding Protein Adenovirus ssDNA binding protein 1633461 P03265 LADT 356 SVPIVSAWEKGMEAARALMDKYHVDNDLKANFKLLPDQVEALAAVCKTWLNEEHRGLQLTFTSNKTFVTMMGRFLQAYLQSFAEVTYKHHEPTGCALWLHRCAEIEGELKCLHGSIMINKEHVIEMDVTSENGQRALKEQSSKAKIVKNRWGRNVVQISNTDARCCVHDAACPANQFSGKSCGMFFSEGAKAQVAFKQIKAFMQALYPNAQTGHGHLLMPLRCECNSKPGHAPFLGRQLPKLTPFALSNAEDLDADLISDKSVLASVHHPALIVFQCCNPVYRNSRAQGGGPNCDFKISAPDLLNALVMVRSLWSENFTELPRMVVPQFKWSTKHQYRNVSLPVAHSDARQNPFDF Other techniques X-ray crystallography 124 158 35 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 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 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 Antibacterial protein FALL-39 precursor Antibacterial protein LL-37 1706745 P49913 170 MKTQRDGHSLGRWSLVLLLLGLVMPLAIIAQVLSYKEAVLRAIDGINQRSSDANLYRLLDLDPRPTMDGDPDTPKPVSFTVKETVCPRTTQQSPEDCDFKKDGLVKRCMGTVTLNQARGSFDISCDKDNKRFALLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES Circular dichroism 134 170 37 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 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 1 107 107 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 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 Cytochrome c Apocytochrome c 117995 P00004 1CRC 104 GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWKEETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE Circular dichroism 1 104 104 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 APEX nuclease Major apurinic/apyrimidinic endonuclease Apurinic/apyrimidinic endonuclease 299037 P27695 1DEW 317 PKRGKKGAVAEDGDELRTEPEAKKSKTAAKKNDKEAAGEGPALYEDPPDHKTSPSGKPATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQELPGLSHQYWSAPSDKEGYSGVGLLSRQCPLKVSYGIGDEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQRWDEAFRKFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLPALCDSKIRSKALGSDHCPITLYLAL Limited proteolysis X-ray crystallography 1 40 40 Disordered Known to exist in disordered state, 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 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 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 GenBank AAB26054.1 B-cell-specific coactivator BOB.1/OBF.1 B cell-specific transcription co-activator 1150493 Q64693 256 MLWQKSTAPEQAPAPPRPYQGVRVKEPVKELLRRKRGHTSVGAAGPPTAGVLPHQPLATYSTVGPSCLDMEVSASTVTEEGTLCAGWLSQPAPATLHALAPWTPYTEYVSHEAVSCPYSTDMYVQPVCPSYTVVGPSSVLTYASPPLITNVTPRSTATPAVGPQLEGPEHQAPLTYFPWPQPLSTLPTSSLQYQPPAPTLSGPQFVQLPISIPEPVLQDMDDPRRAISSLTIDKLLLEEEESNTYELNHTLSVEGF Circular dichroism Limited proteolysis 1 256 256 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 Rat Bcl-Xl An Apoptosis Inhibitory Protein Bcl-xL antiapoptotic protein 2392082 P53563 1AF3 196 MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEETEPERETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIASWMATYLNDHLEPWIQENGGWDTFVDLYG Limited proteolysis X-ray crystallography 31 80 50 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 Cheng, E. H., Kirsch, D. G., Clem, R. J., Ravi, R., Kastan, M. B., Bedi, A., Ueno, K., and Hardwick, J. M. Conversion of Bcl-2 to a Bax-like death effector by caspases 1997 Science 278 1966 1968 Chang, B. S., Minn, A. J., Muchmore, S. W., Fesik, S. W., and Thompson, C. B. Identification of a novel regulatory domain in Bcl-X(L) and Bcl-2 1997 EMBO J. 16 968 977 Alpha-s1-casein precursor - bovine Alpha s-Casein 1070620 P02662 214 MKLLILTCLVAVALARPKHPIKHQGLPQEVLNENLLRFFVAPFPEVFGKEKVNELSKDIGSESTEDQAMEDIKQMEAESISSSEEIVPNSVEQKHIQKEDVPSERYLGYLEQLLRLKKYKVPQLEIVPNSAEERLHSMKEGIHAQQKEPMIGVNQELAYFYPELFRQFYQLDAYPSGAWYYVPLGTQYTDAPSFSDIPNPIGSENSEKTTMPLW Circular dichroism 1 15 15 Undetermined 16 214 199 Disordered Bhattacharyya, J., and Das, K. P. Molecular chaperone-like properties of an unfolded protein, alpha(s)-casein 1999 J. Biol. Chem. 274 15505 15509 Monoamine-sulfating phenol sulfotransferase Sulfotransferase, monoamine-preferring Catecholamine sulfotransferase 1711609 P50224 1CJM A 295 MELIQDTSRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLINTYPKSGTTWVSQILDMIYQGGDLEKCNRAPIYVRVPFLEVNDPGEPSGLETLKDTPPPRLIKSHLPLALLPQTLLDQKVKVVYVARNPKDVAVSYYHFHRMEKAHPEPGTWDSFLEKFMAGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETMDFMVQHTSFKEMKKNPMTNYTTVPQELMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL X-ray crystallography 216 261 46 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 Dajani, R., Cleasby, A., Neu, M., Wonacott, A. J., Jhoti, H., Hood, A. M., Modi, S., Hersey, A., Taskinen, J., Cooke, R. M., Manchee, G. R., and Coughtrie, M. W. X-ray crystal structure of human dopamine sulfotransferase, SULT1A3. Molecular modeling and quantitative structure-activity relationship analysis demonstrate a molecular basis for sulfotransferase substrate specificity 1999 J. Biol. Chem. 274 37862 37868 Cystic fibrosis transmembrane conductance regulator, ATP-binding cassette CFTR 14753227 P13569 1480 MQRSPLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEKLEREWDRELASKKNPKLINALRRCFFWRFMFYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGLGRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVFLSVLPYALIKGIILRKIFTTISFCIVLRMAVTRQFPWAVQTWYDSLGAINKIQDFLQKQEYKTLEYNLTTTEVVMENVTAFWEEGFGELFEKAKQNNNNRKTSNGDDSLFFSNFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPDFSSKLMGCDSFDQFSAERRNSILTETLHRFSLEGDAPVSWTETKKQSFKQTGEFGEKRKNSILNPINSIRKFSIVQKTPLQMNGIEEDSDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSVNQGQNIHRKTTASTRKVSLAPQANLTELDIYSRRLSQETGLEISEEINEEDLKECFFDDMESIPAVTTWNTYLRYITVHKSLIFVLIWCLVIFLAEVAASLVVLWLLGNTPLQDKGNSTHSRNNSYAVIITSTSSYYVFYIYVGVADTLLAMGFFRGLPLVHTLITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFISILTTGEGEGRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFIDMPTEGKPTKSTKPYKNGQLSKVMIIENSHVKKDDIWPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQAISPSDRVKLFPHRNSSKCKSKPQIAALKEETEEEVQDTRL Circular dichroism Limited proteolysis 1 707 707 Undetermined 708 831 124 Disordered Function arises from the disordered (extended) state Autoregulatory Phosphorylation 832 1480 649 Undetermined Ostedgaard, L. S., Baldursson, O., Vermeer, D. W., Welsh, M. J., and Robertson, A. D. A functional R domain from cystic fibrosis transmembrane conductance regulator is predominantly unstructured in solution 2000 Proc. Natl. Acad. Sci. USA 97 5657 5662 Human Chorionic Gonadotropin Hcg Chorionic gonadotropin 116184 P01233 1hrp B 145 SKEPLRPRCRPINATLAVEKEGCPVCITVNTTICAGYCPTMTRVLQGVLPALPQVVCNYRDVRFESIRLPGCPRGVNPVVSYAVALSCQCALCRRSTTDCGGPKDHPLTCDDPRFQDSSSSKAPPPSLPSPSRLPGPSDTPILPQ X-ray crystallography 112 145 34 Disordered Function arises from the disordered (extended) state Disordered region is not essential for protein function Glycosylation Lapthorn, A. J., Harris, D. C., Littlejohn, A., Lustbader, J. W., Canfield, R. E., Machin, K. J., Morgan, F. J., and Isaacs, N. W. Crystal structure of human chorionic gonadotropin 1994 Nature 369 455 461 Clusterin precursor Clusterin Sulfated glycoprotein 2 SGP-2 Dimeric acid glycoprotein DAG Testosterone repressed prostate message-2 TRPM-2 461756 P05371 447 MKILLLCVALLLTWDNGMVLGEQEFSDNELQELSTQGSRYVNKEIQNAVQGVKHIKTLIEKTNAERKSLLNSLEEAKKKKEGALDDTRDSEMKLKAFPEVCNETMMALWEECKPCLKHTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRIDSLLESDRQQSQVLDAMQDSFTRASGIIDTLFQDRFFTHEPQDIHHFSPMGFPHKRPHFLYPKSRLVRSLMPLSHYGPLSFHNMFQPFFDMIHQAQQAMDVQLHSPALQFPDVDFLKEGEDDPTVCKEIRHNSTGCLKMKGQCEKCQEILSVDCSTNNPAQANLRQELNDSLQVAERLTQQYNELLHSLQSKMLNTSSLLEQLNDQFTWVSQLANLTQGDDQYLRVSTVTTHSSDSEVPSRVTEVVVKLFDSDPITVVLPEEVSKDNPKFMDTVAEKALQEYRRKSRME Limited proteolysis 66 97 32 Disordered Function arises from the disordered (extended) state Function arises from the molten globule (collapsed) state Protein detergent 386 445 60 Disordered Function arises from the disordered (extended) state Function arises from the molten globule (collapsed) state Protein detergent Bailey, R. W., Yang, J., Dunker, A. K., and Griswold, M. D. 2000 Biophysical J. 78 152 cAMP-dependent protein kinase inhibitor, alpha form PKI-alpha cAMP-dependent protein kinase inhibitor, muscle/brain isoform cAMP-dependent protein kinase inhibitor 417194 P04541 1APM 76 MTDVETTYADFIASGRTGRRNAIHDILVSSASGNSNELALKLAGLDINKTEGEEDAQRSSTEQSGEAQGEAAKSES Circular dichroism X-ray crystallography 1 76 76 Disordered Function arises via a disorder to order transition Protein-protein binding Wu, H., Lustbader, J. W., Liu, Y., Canfield, R. E., and Hendrickson, W. A. Structure of human chorionic gonadotropin at 2.6 A resolution from MAD analysis of the selenomethionyl protein 1994 Structure 2 545 558 Thomas, J., Van Patten, S. M., Howard, P., Day, K. H., Mitchell, R. D., Sosnick, T., Trewhella, J., Walsh, D. A., and Maurer, R. A. Expression in Escherichia coli and characterization of the heat-stable inhibitor of the cAMP-dependent protein kinase 1991 J. Biol. Chem. 266 10906 10911 Knighton, D. R., Zheng, J. H., Ten Eyck, L. F., Xuong, N. H., Taylor, S. S., and Sowadski, J. M. Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase 1991 Science 253 414 420 Cyclin-dependent kinase inhibitor 1 p21 CDK-interacting protein 1 Melanoma differentiation associated protein 6 MDA-6 Cyclin-dependent kinase inhibitor p21 729143 P38936 164 MSEPAGDVRQNPCGSKACRRLFGPVDSEQLSRDCDALMAGCIQEARERWNFDFVTETPLEGDFAWERVRGLGLPKLYLPTGPRRGRDELGGGRRPGTSPALLQGTAEEDHVDLSLSCTLVPRSGEQAEGSPGGPGDSQGRKRRQTSMTDFYHSKRRLIFSKRKP Circular dichroism Limited proteolysis Nuclear magnetic resonance spectroscopy 1 164 164 Disordered Function arises via a disorder to order transition Known to exist in disordered state, relationship to function unknown Protein-protein binding Kriwacki, R. W., Hengst, L., Tennant, L., Reed, S. I., and Wright, P. E. Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity 1996 Proc. Natl. Acad. Sci. USA 93 11504 11509 cyclin-dependent kinase inhibitor 1C Cyclin-dependent kinase inhibitor p57 11440665 P49918 316 MSDASLRSTSTMERLVARGTFPVLVRTSACRSLFGPVDHEELSRELQARLAELNAEDQNRWDYDFQQDMPLRGPGRLQWTEVDSDSVPAFYRETVQVGRCRLLLAPRPVAVAVAVSPPLEPAAESLDGLEEAPEQLPSVPVPAPASTPPPVPVLAPAPAPAPAPVAAPVAAPVAVAVLAPAPAPAPAPAPAPAPVAARAPAPARARAPAPAPAPAPDAAPQESAEQGANQGQRGQEPLADQLHSGISGRPAAGTAAASANGAAIKKLSGPLISDFFAKRKRSAPEKSSGDVPAPCPSPSAAPGVGSVEQTPRKRLR Circular dichroism Other techniques 1 316 316 Disordered Function arises from the disordered (extended) state Protein-protein binding Adkins, J. N., and Lumb, K. J. Intrinsic structural disorder and sequence features of the cell cycle inhibitor p57Kip2 2002 Proteins 46 1 7 Cyclin-dependent kinase inhibitor 1B Cyclin-dependent kinase inhibitor p27 p27Kip1 1168871 P46527 1JSU 198 MSNVRVSNGSPSLERMDARQAEHPKPSACRNLFGPVDHEELTRDLEKHCRDMEEASQRKWNFDFQNHKPLEGKYEWQEVEKGSLPEFYYRPPRPPKGACKVPAQESQDVSGSRPAAPLIGAPANSEDTHLVDPKTDPSDSQTGLAEQCAGIRKRPATDDSSTQNKRANRTEENVSDGSPNAGSVEQTPKKPGLRRRQT Circular dichroism Other techniques X-ray crystallography 1 21 21 Undetermined 22 106 85 Disordered Function arises via a disorder to order transition Protein-protein binding 107 198 92 Undetermined 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 Flaugh, S. L., and Lumb, K. J. Effects of macromolecular crowding on the intrinsically disordered proteins c-Fos and p27(Kip1) 2001 Biomacromolecules 2 538 540 Engineered in PDB: 1jsu Cytochrome Bc1 Complex Ubiquinol Cytochrome C Oxidoreductase, Complex III 1351360 P13272 1be3 I 274 MLSVAARSGPFAPVLSATSRGVAGALRPLVQAAVPATSESPVLDLKRSVLCRESLRGQAAGRPLVASVSLNVPASVRYSHTDIKVPDFSDYRRPEVLDSTKSSKESSEARKGFSYLVTATTTVGVAYAAKNVVSQFVSSMSASADVLAMSKIEIKLSDIPEGKNMAFKWRGKPLFVRHRTKKEIDQEAAVEVSQLRDPQHDLERVKKPEWVILIGVCTHLGCVPIANAGDFGGYYCPCHGSHYDASGRIRKGPAPLNLEVPSYEFTSDDMVIVG X-ray crystallography 1 45 45 Disordered Known to exist in disordered state, relationship to function unknown Unknown Iwata, S., Lee, J. W., Okada, K., Lee, J. K., Iwata, M., Rasmussen, B., Link, T. A., Ramaswamy, S., and Jap, B. K. Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex 1998 Science 281 64 71 DNA-binding protein RAP1 SBF-E Repressor/activator site binding protein TUF 730473 P11938 1IGN 827 MSSPDDFETAPAEYVDALDPSMVVVDSGSAAVTAPSDSAAEVKANQNEENTGATAAETSEKVDQTEVEKKDDDDTTEVGVTTTTPSIADTAATANIASTSGASVTEPTTDDTAADEKKEQVSGPPLSNMKFYLNRDADAHDSLNDIDQLARLIRANGGEVLDSKPRESKENVFIVSPYNHTNLPTVTPTYIKACCQSNSLLNMENYLVPYDNFREVVDSRLQEESHSNGVDNSNSNSDNKDSIRPKTEIISTNTNGATEDSTSEKVMVDAEQQARLQEQAQLLRQHVSSTASITSGGHNDLVQIEQPQKDTSNNNNSNVNDEDNDLLTQDNNPQTADEGNASFQAQRSMISRGALPSHNKASFTDEEDEFILDVVRKNPTRRTTHTLYDEISHYVPNHTGNSIRHRFRVYLSKRLEYVYEVDKFGKLVRDDDGNLIKTKVLPPSIKRKFSADEDYTLAIAVKKQFYRDLFQIDPDTGRSLITDEDTPTAIARRNMTMDPNHVPGSEPNFAAYRTQSRRGPIAREFFKHFAEEHAAHTENAWRDRFRKFLLAYGIDDYISYYEAEKAQNREPEPMKNLTNRPKRPGVPTPGNYNSAAKRARNYSSQRNVQPTANAASANAAAAAAAAASNSYAIPENELLDEDTMNFISSLKNDLSNISNSLPFEYPHEIAEAIRSDFSNEDIYDNIDPDTISFPPKIATTDLFLPLFFHFGSTRQFMDKLHEVISGDYEPSQAEKLVQDLCDETGIRKNFSTSILTCLSGDLMVFPRYFLNMFKDNVNPPPNVPGIWTHDDDESLKSNDQEQIRKLVKKHGTGRMEMRKRFFEKDLL Limited proteolysis X-ray crystallography 482 512 31 Disordered Known to exist in disordered state, 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 Elongation Factor G Without Nucleotide Elongation factor G 1827912 P13551 1elo 691 MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERERGITITAAVTTCFWKDHRINIIDTPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSETVWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDVLRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEEELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVEIHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHANHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKADQEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDANVGKPQVAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIPAVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYHEVDSSEMAFKIAGSMAIKEAVQKGDPVILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLRSKTQGRGSFVMFFDHYQEVPKQVQEKLIKGQ X-ray crystallography 40 67 28 Disordered 400 475 76 Disordered Known to exist in disordered state, 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 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 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 EMB-1 PROTEIN Embryonic abundant protein from carrot 119316 P17639 92 MASQQEKKELDARARQGETVVPGGTGGKSLEAQQHLAEGRSKGGQTRKEQLGGEGYHEMGRKGGLSNNDMSGGERAEQEGIDIDESKFRTKK Nuclear magnetic resonance spectroscopy 1 92 92 Disordered Known to exist in disordered state, relationship to function unknown Substrate/ligand binding Eom, J., Baker, W., Kintanar, A., and Wurtele, E. 1996 Plant Sci. 115 17 17 Estrogenic 17-Beta Hydroxysteroid Dehydrogenase Complexed 17-Beta-Estradiol 2392375 P14061 1IOL 327 ARTVVLITGCSSGIGLHLAVRLASDPSQSFKVYATLRDLKTQGRLWEAARALACPPGSLETLQLDVRDSKSVAAARERVTEGRVDVLVCNAGLGLLGPLEALGEDAVASVLEVNVVGTVRMLQAFLPDMKRRGSGRVLVTGSVGGLMGLPFNDVYCASKFALEGLCESLAVLLLPFGVHLSLIECGPVHTAFMEKVLGSPEEVLDRTDIHTFHRFYQYLAHSKQVFREAAQNPEEVAEVFLTALRAPKPTLRYFTTERFLPLLRMRLDDPSGSNYVTAMHREVFGDVPAKAEAGAEAGGGAGPGAEDEAGRSAVGDPELGDPPAAPQ X-ray crystallography 285 327 43 Disordered Known to exist in disordered state, 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 E7 protein E7 protein from HPV16 6469700 P03129 93 MHGDTPTLHEYMLDLQPETTDLYCYEQLSDSSEEEDEIDGPAGQAEPDRAHYNIVTFCCKCDSTLRLCVQSTHVDIRTLEDLLMGTLGIVCPI Circular dichroism 1 93 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 Fibronectin-binding protein precursor FNBP Fibronectin binding protein 120457 P14738 1018 MKNNLRYGIRKHKLGAASVFLGTMIVVGMGQDKEAAASEQKTTTVEENGNSATDNKTSETQTTATNVNHIEETQSYNATVTEQPSNATQVTTEEAPKAVQAPQTAQPANIETVKEEVVKEEAKPQVKETTQSQDNSGDQRQVDLTPKKATQNQVAETQVEVAQPRTASESKPRVTRSADVAEAKEASNAKVETGTDVTSKVTVEIGSIEGHNNTNKVEPHAGQRAVLKYKLKFENGLHQGDYFDFTLSNNVNTHGVSTARKVPEIKNGSVVMATGEVLEGGKIRYTFTNDIEDKVDVTAELEINLFIDPKTVQTNGNQTITSTLNEEQTSKELDVKYKDGIGNYYANLNGSIETFNKANNRFSHVAFIKPNNGKTTSVTVTGTLMKGSNQNGNQPKVRIFEYLGNNEDIAKSVYANTTDTSKFKEVTSNMSGNLNLQNNGSYSLNIENLDKTYVVHYDGEYLNGTDEVDFRTQMVGHPEQLYKYYYDRGYTLTWDNGLVLYSNKANGNEKNGPIIQNNKFEYKEDTIKETLTGQYDKNLVTTVEEEYDSSTLDIDYHTAIDGGGGYVDGYIETIEETDSSAIDIDYHTAVDSEAGHVGGYTESSEESNPIDFEESTHENSKHHADVVEYEEDTNPGGGQVTTESNLVEFDEESTKGIVTGAVSDHTTVEDTKEYTTESNLIELVDELPEEHGQAQGPVEEITKNNHHISHSGLGTENGHGNYDVIEEIEENSHVDIKSELGYEGGQNSGNQSFEEDTEEDKPKYEQGGNIVDIDFDSVPQIHGQNKGNQSFEEDTEKDKPKYEHGGNIIDIDFDSVPHIHGFNKHTEIIEEDTNKDKPSYQFGGHNSVDFEEDTLPKVSGQNEGQQTIEEDTTPPIVPPTPPTPEVPSEPETPTPPTPEVPSEPETPTPPTPEVPSEPETPTPPTPEVPAEPGKPVPPAKEEPKKPSKPVEQGKVVTPVIEINEKVKAVAPTKKPQSKKSELPETGGEESTNKGMLFGGLFSILGLALLRRNKKNHKA Nuclear magnetic resonance spectroscopy 1 744 744 Undetermined 745 873 129 Disordered Function arises via a disorder to order transition Protein-protein binding 874 1018 145 Undetermined 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 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 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 Flagellin - Salmonella typhimurium Flagellin 96744 S16121 1io1 494 AQVINTNSLSLLTQNNLNKSQSALGTAIERLSSGLRINSAKDDAAGQAIANRFTANIKGLTQASRNANDGISIAQTTEGALNEINNNLQRVRELAVQSANSTNSQSDLDSIQAEITQRLNEIDRVSGQTQFNGVKVLAQDNTLTIQVGANDGETIDIDLKQINSQTLGLDTLNVQQKYKVSDTAATVTGYADTTIALDNSTFKASATGLGGTDQKIDGDLKFDDTTGKYYAKVTVTGGTGKDGYYEVSVDKTNGEVTLAGGATSPLTGGLPATATEDVKNVQVANADLTEAKAALTAAGVTGTASVVKMSYTDNNGKTIDGGLAVKVGDDYYSATQNKDGSISINTTKYTADDGTSKTALNKLGGADGKTEVVSIGGKTYAASKAEGHNFKAQPDLAEAAATTTENPLQKIDAALAQVDTLRSDLGAVQNRFNSAITNLGNTVNNLTSARSRIEDSDYATEVSNMSRAQILQQAGTSVLAQANQVPQNVLSLLR Circular dichroism Nuclear magnetic resonance spectroscopy Other techniques X-ray crystallography 1 55 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 44 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 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 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 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 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 PIR: S16121 Negative regulator of flagellin synthesis Anti-sigma-28 factor Flagellum specific sigma factor 120306 P26477 97 MSIDRTSPLKPVSTVQTRETSDTPVQKTRQEKTSAATSASVTLSDAQAKLMQPGVSDINMERVEALKTAIRNGELKMDTGKIADSLIREAQSYLQSK Nuclear magnetic resonance spectroscopy 1 97 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 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 Eukaryotic translation initiation factor 4E binding protein 1 4E-binding protein 1 4758258 Q13541 118 MSGGSSCSQTPSRAIPATRRVVLGDGVQLPPGDYSTTPGGTLFSTTPGGTRIIYDRKFLMECRNSPVTKTPPRDLPTIPGVTSPSSDEPPMEASQSHLRNSPEDKRAGGEESQFEMDI Circular dichroism Nuclear magnetic resonance spectroscopy X-ray crystallography 1 118 118 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 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 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 Glycine N-Methyltransferase Glial cell-derived neurotrophic factor 729568 Q07731 1agq A 135 MSPDKQAAALPRRERNRQAAAASPENSRGKGRRGQRGKNRGCVLTAIHLNVTDLGLGYETKEELIFRYCSGSCEAAETMYDKILKNLSRSRRLTSDKVGQACCRPVAFDDDLSFLDDSLVYHILRKHSAKRCGCI X-ray crystallography 1 38 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 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 Ibanez, C. F. Personal communication Part of GI: 729568 Part of SP: Q07731 glucocorticoid receptor DNA binding factor 1 [Homo sapiens] Glucocorticoid receptor 4758482 Q9NRY4 834 DATSHIDNMENERIPFDLMDTVPAEALYEAHLEKLRNERKRVEMRRAFKENLETSPFITPGKPWEEARSFIMNEDFYQWLEESVYTDIYGKHQKQIIDKAKEEFQELLLEYSELFYELELDAKPSKEKMGVIQDVLGEEQRFKAIYKSSKQSVDALILKHIHFVYHPTKETCPSCPACVDAKIEHLISSRFIRPSDRNQKNSLSDPNIDRINLVILGKDALPESWPMEIRALCTNDDKYVIDGKMYELSLRPIEGNVRLPVNSFQTPTFQPHGCLCLYNSKESLSYVVESIEKSRESTLGRRDNHLVHLPLTLILVNKRGDTSGETLHSLIQQGQQIASKLQCVFLDPASAGIGYGRNINEKQISQVLKGLLDSKRNLNLVSSTASIKDLADVDLRIVMCLMCGDPFSADDILFPVLQSQTCKSSHCGSNNSVLLELPIGLHKKRIELSVLSYHSSFSIRKSRLVHGYIVFYSAKRKASLAMLRAFLCEVQDIIPIQLVALTDGAVDVLDNDLSREQLTEGEEIAQEIDGRFTSIPCSQPQHKLEIFHPFFKDVVEKKNIIEATHMYDNAAEACSTTEEVFNSPRAGSPLCNSNLQDSEEDIEPSYSLFREDTSLPSLSKDHSKLSMELEGNDGLSFIMSNFESKLNNKVPPPVKPKPPVHFEITKGDLSYLDQGHRDGQRKSVSSSPWLPQDGFDPSDYAEPMDAVVKPRNEEENIYSVPHDSTQGKIITIRNINKAQSNGSGNGSDSEMDTSSLERGRKVSIVSKPVLYRTRCTRLGGLLVTGPASAWGVMMSWGPSGRKRRIRHPRVIKGTMLSFHTKQTKTRGGGIFFAA Circular dichroism Other techniques 1 76 76 Undetermined 77 262 186 Disordered Function arises via a disorder to order transition Protein-protein binding 263 835 573 Undetermined 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 Glycine N-Methyltransferase 121328 P13255 1d2h A 292 VDSVYRTRSLGVAAEGIPDQYADGEAARVWQLYIGDTRSRTAEYKAWLLGLLRQHGCHRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYALKERWNRRKEPAFDKWVIEEANWLTLDKDVPAGDGFDAVICLGNSFAHLPDSKGDQSEHRLALKNIASMVRPGGLLVIDHKNYDYILSTGCAPPGKNIYYKSDLTKDITTSVLTVNNKAHMVTLDYTVQVPGAGRDGAPGFSKFRLSYYPHCLASFTELVQEAFGGRCQHSVLGDFKPYRPGQAYVPCYFIHVLKKTG X-ray crystallography 1 40 40 Disordered Function arises via a disorder to order transition Known to exist in disordered state, 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 Takusagawa, F. Personal communication Part of GI: 121328 Part of SP: P13255 Glycyl-tRNA Synthetase Glycyl-tRNA Ligase 2829475 P56206 1ggm A 442 AASSLDELVALCKRRGFIFQSSEIYGGLQGVYDYGPLGVELKNNLKQAWWRRNVYERDDMEGLDASVLTHRLVLHYSGHEATFADPMVDNAKARYWTPPRYFNMMFQDLRGPRGGRGLLAYLRPETAQGIFVNFKNVLDATSRKLGFGIAQIGKAFRNEITPRNFIFRVREFEQMEIEYFVRPGEDEYWHRYWVEERLKWWQEMGLSRENLVPYQQPPESSAHYAKATVDILYRFPHGSLELEGIAQRTDFDLGSHTKDQEALGITARVLRNEHSTQRLAYRDPETGKWFVPYVIEPSAGVDRGVLALLAEAFTREELPNGEERIVLKLKPQLAPIKVAVIPLVKNRPEITEYAKRLKARLLALGLGRVLYEDTGNIGKAYRRHDEVGTPFAVTVDYDTIGQSKDGTTRLKDTVTVRDRDTMEQIRLHVDELEGFLRERLRW X-ray crystallography 96 158 63 Disordered Known to exist in disordered state, 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 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 Growth Hormone Receptor 121180 P10912 1a22 B 238 FSGSEATAAILSRAPWSLQSVNPGLKTNSSKEPKFTKCRSPERETFSCHWTDEVHHGTKNLGPIQLFYTRRNTQEWTQEWKECPDYVSAGENSCYFNSSFTSIWIPYCIKLTSNGGTVDEKCFSVDEIVQPDPPIALNWTLLNVSLTGIHADIQVRWEAPRNADIQKGWMVLEYELQYKEVNETKWKMMDPILTTSVPVYSLKVDKEYEVRVRSKQRNSGNYGEFSEVLYVTLPQMSQ X-ray crystallography 1 32 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 Clackson, T., and Wells, J. A. A hot spot of binding energy in a hormone-receptor interface 1995 Science 267 383 386 Coat protein A [Precursor] G3P g3p (fd phage minor coat protein) 5822481 P03661 2G3P 424 MKKLLFAIPLVVPFYSHSAETVESCLAKPHTENSFTNVWKDDKTLDRYANYEGCLWNATGVVVCTGDETQCYGTWVPIGLAIPENEGGGSEGGGSEGGGSEGGGTKPPEYGDTPIPGYTYINPLDGTYPPGTEQNPANPNPSLEESQPLNTFMFQNNRFRNRQGALTVYTGTVTQGTDPVKTYYQYTPVSSKAMYDAYWNGKFRDCAFHSGFNEDPFVCEYQGQSSDLPQPPVNAGGGSGGGSGGGSEGGGSEGGGSEGGGSEGGGSGGGSGSGDFDYEKMANANKGAMTENADENALQSDAKGKLDSVATDYGAAIDGFIGDVSGLANGNGATGDFAGSNSQMAQVGDGDNSPLMNNFRQYLPSLPQSVECRPYVFGAGKPYEFSIDCDKINLFRGVFAFLLYVATFMYVFSTFANILRNKES 236 274 39 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 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 Mutant in PDB: 2g3p 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 A 353 GCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDAARADDARQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF X-ray crystallography 1 31 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 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 Heat shock factor protein HSF Heat shock transcription factor HSTF 123686 P22121 1FBQ 677 MGHNDSVETMDEISNPNNILLPHDGTGLDATGISGSQEPYGMVDVLNPDSLKDDSNVDEPLIEDIVNPSLDPEGVVSAEPSNEVGTPLLQQPISLDHVITRPASAGGVYSIGNSSTSSAAKLSDGDLTNATDPLLNNAHGHGQPSSESQSHSNGYHKQGQSQQPLLSLNKRKLLAKAHVDKHHSKKKLSTTRARPAFVNKLWSMVNDKSNEKFIHWSTSGESIVVPNRERFVQEVLPKYFKHSNFASFVRQLNMYGWHKVQDVKSGSMLSNNDSRWEFENENFKRGKEYLLENIVRQKSNTNILGGTTNAEVDIHILLNELETVKYNQLAIAEDLKRITKDNEMLWKENMMARERHQSQQQVLEKLLRFLSSVFGPNSAKTIGNGFQPDLIHELSDMQVNHMSNNNHNNTGNINPNAYHNETDDPMANVFGPLTPTDQGKVPLQDYKLRPRLLLKNRSMSSSSSSNLNQRQSPQNRIVGQSPPPQQQQQQQQQQGQPQGQQFSYPIQGGNQMMNQLGSPIGTQVGSPVGSQYGNQYGNQYSNQFGNQLQQQTSRPALHHGSNGEIRELTPSIVSSDSPDPAFFQDLQNNIDKQEESIQEIQDWITKLNPGPGEDGNTPIFPELNMPSYFANTGGSGQSEQPSDYGDSQIEELRNSRLHEPDRSFEEKNNGQKRRRAA Circular dichroism Nuclear magnetic resonance spectroscopy 1 196 196 Disordered Function arises from the disordered (extended) state Protein-protein binding 219 223 5 Disordered 261 276 16 Disordered 280 282 3 Disordered 283 677 395 Undetermined 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 Part in PDB: 3hsf Heparin-Binding Epidermal Growth Factor Hbegf Heparin-binding EGF-like growth factor 544477 Q99075 1xdt R 79 GSHMRVTLSSKPQALATPNKEEHGKRKKKGKGLGKKRDPCLRKYKDFCIHGECKYVKELRAPSCICHPGYHGERCHGLS X-ray crystallography 1 38 38 Disordered 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 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 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 100 MPKRKVSSAEGAAKEEPKRRSARLSAKPPAKVEAKPKKAAAKDKSSDKKVQTKGKRGAKGKQAEVANQETKEDLPAENGETKTEESPASDEAGEKEAKSD Circular dichroism Nuclear magnetic resonance spectroscopy Other techniques 1 100 100 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 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 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 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 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 90 MPKRKAEGDAKGDKAKVKDEPQRRSARLSAKPAPPKPEPKPKKAPAKKGEKVPKGKKGKADAGKEGNNPAENGDAKTDQAQKAEGAGDAK Circular dichroism Nuclear magnetic resonance spectroscopy Other techniques 1 90 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 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 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 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 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 107 MSESSSKSSQPLASKQEKDGTEKRGRGRPRKQPPVSPGTALVGSQKEPSEVPTPKRPRGRPKGSKNKGAAKTRKTTTTPGRKPRGRPKKLEKEEEEGISQESSEEEQ Nuclear magnetic resonance spectroscopy 1 107 107 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 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 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 High mobility group-T protein HMG-T HMG-T1 HMG-1 123382 P07746 204 MGKDPRKPRGKMSSYAYFVQTRREEHKKKHPEASVNFSEFSKKCSERWKTMSAKEKGKFEDLAKLDKVRYEREMRSYIPPKGEKKKRFKDPNAPKRPSSAFFIFCADFRPQVKGETPGLSIGDVAKKLGEKWNNLTAEDKVPYEKKASRLKEKYEKDITAYRNKGKVPVSMPAKAAAPAKDDDDDDDDDDDDEDDDDDDDEDDE Circular dichroism Nuclear magnetic resonance spectroscopy 1 204 204 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 NONHISTONE CHROMOSOMAL PROTEIN H6 HISTONE T High mobility group - H6 462245 P02315 70 MPKRKSATKGDEPARRSARLSARPVPKPAAKPKKAAAPKKAVKGKKAAENGDAKAEAKVQAAGDGAGNAK Circular dichroism Nuclear magnetic resonance spectroscopy 1 70 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 Histone H3 211857 Q92068 136 MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA X-ray crystallography 1 40 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 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 histone H5 - chicken 70678 P02259 1HST 189 TESLVLSPAPAKPKRVKASRRSASHPTYSEMIAAAIRAEKSRGGSSRQSIQKYIKSHYKVGHNADLQIKLSIRRLLAAGVLKQTKGVGASGSFRLAKSDKAKRSPGKKKKAVRRSTSPKKAARPRKARSPAKKPKATARKARKKSRASPKKAKKPKTVKAKSRKASKAKKVKRSKPRAKSGARKSPKKK Limited proteolysis X-ray crystallography 1 21 21 Disordered 101 185 85 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 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 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 Crane-Robinson, C. Personal communication PIR: HSCH5 Hypoxanthine Phosphoribosyltransferase 6435814 Q27796 1tc1 B 220 PREYEFAEKILFTEEEIRTRIKEVAKRIADDYKGKGLRPYVNPLVLISVLKGSFMFTADLCRALCDFNVPVRMEFICVSSYGEGLTSSGQVRMLLDTRHSIEGHHVLIVEDIVDTALTLNYLYHMYFTRRPASLKTVVLLDKREGRRVPFSADYVVANIPNAFVIGYGLDYDDTYRELRDIVVLRPEVYAEREAARQKKQRAIGSADTDRDAKREFHSKY X-ray crystallography 190 220 31 Disordered Known to exist in disordered state, 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 lymphoid enhancer factor-1 [Rattus sp.] 6537322 Q9QXN1 2lef 397 MPQLSGGGGGGDPELCATDEMIPFKDEGDPQKEKIFAEISHPEEEGDLADIKSSLVNESEIIPASNGHEVVGQTQSSQEPYHDKAREHPDDGKHPDGGLYNKGPSYSSYSGYIMMPNMNSDPYMSNGSLSPPIPRTSNKVPVVQPSHAVHPLTPLITYSDEHFSPGSHPSHIPSEVNPKQGMSRHPPAPEMPTFYPLSPGGVGQITPPLGWQGQPVYPITGGFRQAYPSSLSGDTSMSRFSHHMIPGPPGPHTTGIPHPAIVTPQVKQEHPHTDSDLMHVKPEHEQRKEQEPKRPHIKKPLNAFMLYMKEMRANVVAECTLKESAAINQILGRRWHALSREEQAKYYELARKERQLHMQLYPGWSARDNYGKKKKRKREKLQESTSGTGPRMTAAYI 1 295 295 Undetermined 296 397 102 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 Myelin basic protein MBP Myelin A1 protein 20 kDa microtubule stabilizing protein 126796 P02687 169 AAQKRPSQRSKYLASASTMDHARHGFLPRHRDTGILDSLGRFFGSDRGAPKRGSGKDGHHAARTTHYGSLPQKAQGHRPQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQKPGFGYGGRASDYKSAHKGLKGHDAQGTLSKIFKLGGRDSRSGSPMARR Circular dichroism 1 169 169 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 Negative factor F-protein 27 kDa protein 3'ORF Negative factor, HIV1 128023 P03406 1avv 206 MGGKWSKSSVVGWPTVRERMRRAEPAADGVGAASRDLEKHGAITSSNTAATNAACAWLEAQEEEEVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPGPGVRYPLTFGWCYKLVPVEPDKVEEANKGENTSLLHPVSLHGMDDPEREVLEWRFDSRLAFHHVARELHPEYFKNC Nuclear magnetic resonance spectroscopy X-ray crystallography 1 73 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 30 Disordered Known to exist in disordered state, relationship to function unknown Protein-protein binding 204 206 3 Disordered 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 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 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 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 neural zinc finger factor-1 1511632 P70475 1187 MDVDAEEKRHRTRSKGVRVPVEPAIQELFSCPTPGCDGTGHVSGKYARHRSVYGCPLAKKRKTQDKQPQEPAPKRKPFAVKADSSSVDECYESDGTEDMDDKEEDDDEEFSEDNDEQGDDDDEDEVDREDEEEIEEEDDEDDEDDDDGDDVEEEEDDDDEEEEEEEEEEENEDHQMSCTRIMQDPEKDDNNNDEYDNYDELVAKSLLNLGKIAEDAAYRARTESEVNSNTSNSLEDHSSKNENLGRKSELSLDLDSDVVRETVDSLKLLAQGHGVVLSENISDRSYAEGMSQQDSRNMNYVMLGKPMNNGLMEKMVEESDEEVCLSSLECLRNQCFDLARKLSETNPQDRSQPPNMSVRQHVRQEDDFPGRTPDRSYSDMMNLMRLEEQLSPRSRTFSSCAKEDGCHERDDDTTTVNSDRSEEVFDMTKGNLTLLEKAIALETERAKAMREKMAMDAGRRDNLRSYEDQSPRQLAGEDRKSKSSDSHVKKPYYDPSRTEKRESKCPTPGCDGTGHVNGLYPHHRSLSGCPHKDRVPPEILAMHENVLKCPTPGCTGRGHVNSNRNSHRSLSGCPIAAAEKLAKAQEKHQSCDVSKSNQASDRVLRPMCFVKQLEIPQYGYRNNVPTTTPRSNLAKELEKYSKTSFEYNSYDNHTYGKRAIAPRCKPGTYPPKDMTMPSGTGKNASPSSSTTSSYAPSSSSNLSCGGGSSASSTCSKSSFDYTHDMEAAHMAATAILNLSTRCREMPQNLSTKPQDLCTARNPDMEVDENGTLDLSMNKQRPRDSCCPVLTPLEPMSPQQQAVMSSRCFQLSEGDCWDLPVDYTKMKPRRVDEEDPKEITPEDLDPFQEALEERRYPGEVTIPSPKPKYPQCKESKKDLITLSGCPLADKSIRSMLATSSQELKCPTPGCDGSGHITGNYASHRSLSGCPRAKKSGIRIAQSKEDKEDQEPIRCPVPGCDGQGHITGKYASHRSASGCPLAAKRQKDGYLNGSQFSWKSVKTEGMSCPTPGCDGSGHVSGSFLTHRSLSGCPRATSAMKKAKLSGEQMLTIKQRASNGIENDEEIKQLDEEIKELNESNSQMEADMIKLRTQVTITTMESNLKTIEEENKVIEQQNESLLHELANLSQSLIHSLANIQLPHMDPINEQNFDAYVTTLTEMYTNQDRYQSPENKALLENIKQAVRGIQV Nuclear magnetic resonance spectroscopy 1 486 486 Undetermined 487 606 120 Disordered 607 1187 581 Undetermined Berkovits, H. J., and B