Adenovirus ssDNA binding protein Early E2A DNA-binding protein P03265 P03265 118736 W7AD25 Human adenovirus type 5 529 MASREEEQRETTPERGRGAARRPPTMEDVSSPSPSPPPPRAPPKKRMRRRIESEDEEDSSQDALVPRTPSPRPSTSAADLAIAPKKKKKRPSPKPERPPSPEVIVDSEEEREDVALQMVGFSNPPVLIKHGKGGKRTVRRLNEDDPVARGMRTQEEEEEPSEAESEITVMNPLSVPIVSAWEKGMEAARALMDKYHVDNDLKANFKLLPDQVEALAAVCKTWLNEEHRGLQLTFTSNKTFVTMMGRFLQAYLQSFAEVTYKHHEPTGCALWLHRCAEIEGELKCLHGSIMINKEHVIEMDVTSENGQRALKEQSSKAKIVKNRWGRNVVQISNTDARCCVHDAACPANQFSGKSCGMFFSEGAKAQVAFKQIKAFMQALYPNAQTGHGHLLMPLRCECNSKPGHAPFLGRQLPKLTPFALSNAEDLDADLISDKSVLASVHHPALIVFQCCNPVYRNSRAQGGGPNCDFKISAPDLLNALVMVRSLWSENFTELPRMVVPEFKWSTKHQYRNVSLPVAHSDARQNPFDF Disordered - Extended Flexible Loop 297 331 IEMDVTSENGQRALKEQSSKAKIVKNRWGRNVVQI Native 1ADTA 1ADVA 1ADVB 1ANVA Function arises via a disorder to order transition Molecular recognition effectors DNA unwinding Protein-DNA binding X-ray Crystallography 7.2 ethanol 5 NaCl 1.6 phosphate buffer 100 protein 0.5 Paper 8039495 Tucker, P., Tsernoglou, D., Tucker, A., Coenjaerts, F., Leenders, H., Vliet, P. 1994 13 13 2994-3002 9545375 Dekker, J. Kanellopoulos, P. N. van Oosterhout, J. A. Stier, G. Tucker, P. A. van der Vliet, P. C. 1998 Journal of Molecular Biology 277 4 825-838 4040872 Tsernoglou, D. Tsugita, A. Tucker, A. D. van der Vliet, P. C. 1985 FEBS Lett 188 2 248-52 This region is known as the flexible loop. It goes from disordered to ordered upon binding to DNA, helps to stabilize the binding complex and plays an important role in DNA replication. Disordered - Extended 401 406 KPGHAP Native 1ADTA 1ADVA 1ADVB 1ANVA Relationship to function unknown Unknown Unknown X-ray Crystallography 7.2 ethanol 5 NaCl 1.6 phosphate buffer 100 protein 0.5 Paper 8039495 Tucker, P., Tsernoglou, D., Tucker, A., Coenjaerts, F., Leenders, H., Vliet, P. 1994 13 13 2994-3002 9545375 Dekker, J. Kanellopoulos, P. N. van Oosterhout, J. A. Stier, G. Tucker, P. A. van der Vliet, P. C. 1998 Journal of Molecular Biology 277 4 825-838 4040872 Tsernoglou, D. Tsugita, A. Tucker, A. D. van der Vliet, P. C. 1985 FEBS Lett 188 2 248-52 This region is part of the C-terminal portion of the protein which is important in chain formation and DNA replication. Disordered - Extended 453 464 PVYRNSRAQGGG Native 1ADTA 1ADVA 1ADVB 1ANVA Relationship to function unknown Unknown Unknown X-ray Crystallography 7.2 ethanol 5 NaCl 1.6 phosphate buffer 100 protein 0.5 Paper 8039495 Tucker, P., Tsernoglou, D., Tucker, A., Coenjaerts, F., Leenders, H., Vliet, P. 1994 13 13 2994-3002 9545375 Dekker, J. Kanellopoulos, P. N. van Oosterhout, J. A. Stier, G. Tucker, P. A. van der Vliet, P. C. 1998 Journal of Molecular Biology 277 4 825-838 4040872 Tsernoglou, D. Tsugita, A. Tucker, A. D. van der Vliet, P. C. 1985 FEBS Lett 188 2 248-52 This region is part of the C-terminal portion of the protein which is important for chain formation and DNA replication. Disordered - Extended 174 296 SVPIVSAWEKGMEAARALMDKYHVDNDLKANFKLLPDQVEALAAVCKTWLNEEHRGLQLTFTSNKTFVTMMGRFLQAYLQSFAEVTYKHHEPTGCALWLHRCAEIEGELKCLHGSIMINKEHV 1ADTA 1ADVA 1ADVB 1ANVA Paper Ordered 332 400 SNTDARCCVHDAACPANQFSGKSCGMFFSEGAKAQVAFKQIKAFMQALYPNAQTGHGHLLMPLRCECNS 1ADTA 1ADVA 1ADVB 1ANVA Paper Ordered 407 452 FLGRQLPKLTPFALSNAEDLDADLISDKSVLASVHHPALIVFQCCN 1ADTA 1ADVA 1ADVB 1ANVA Paper Ordered 465 529 PNCDFKISAPDLLNALVMVRSLWSENFTELPRMVVPEFKWSTKHQYRNVSLPVAHSDARQNPFDF 1ADTA 1ADVA 1ADVB 1ANVA Paper Antibacterial protein FALL-39 precursor Antibacterial protein LL-37 Antimicrobial protein CAP-18 CAP18 precursor FALL-39 peptide antibiotic hCAP-18 LL-37 P49913 P49913 1706745 I38932 Homo sapiens (Human) 170 MKTQRNGHSLGRWSLVLLLLGLVMPLAIIAQVLSYKEAVLRAIDGINQRSSDANLYRLLDLDPRPTMDGDPDTPKPVSFTVKETVCPRTTQQSPEDCDFKKDGLVKRCMGTVTLNQARGSFDISCDKDNKRFALLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES Disordered - Extended 134 170 LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES Engineered Function arises via a disorder to order transition Unknown Unknown Near-UV Circular Dichroism (CD) Spectroscopy 298 6 magnesium sulfate salt 84 sodium chloride salt 160 Paper 9452503 Johansson, J. Gudmundsson, G. H. Rottenberg, M. E. Berndt, K. D. Agerberth, B. 1998 J Biol Chem 273 6 3718-3724 The disordered region became significantly more disordered below pH 5. At pH of 2, it was completely disordered. At pH of 13, it adopted a helical structure. Antitermination protein N Antitermination protein N of bacteriophage lambda Nucleocapsid protein PN Regulatory protein N P03045 P03045 132276 P03045 Bacteriophage lambda 107 MDAQTRRRERRAEKQAQWKAANPLLVGVSAKPVNLPILSLNRKPKSRVESALNPIDLTVLAEYHKQIESNLQRIERKNQRTWYSKPGERGITCSGRQKIKGKSIPLI Disordered 1 107 MDAQTRRRERRAEKQAQWKAANPLLVGVSAKPVNLPILSLNRKPKSRVESALNPIDLTVLAEYHKQIESNLQRIERKNQRTWYSKPGERGITCSGRQKIKGKSIPLI Paper Cytochrome c Apocytochrome c P00004 117995 A00005 Equus caballus (Horse) 104 GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWKEETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE Disordered 1 104 GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWKEETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE Paper DNA-(apurinic or apyrimidinic site) lyase APE nuclease APEX nuclease Apurinic/apyrimidinic endonuclease HAP1 Major apurinic/apyrimidinic endonuclease Ref-1 P27695 Hs.73722 P27695 18375505 S23550 Homo sapiens (Human) 318 MPKRGKKGAVAEDGDELRTEPEAKKSKTAAKKNDKEAAGEGPALYEDPPDQKTSPSGKPATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQELPGLSHQYWSAPSDKEGYSGVGLLSRQCPLKVSYGIGDEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQRWDEAFRKFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLPALCDSKIRSKALGSDHCPITLYLAL Disordered - Extended 1 35 MPKRGKKGAVAEDGDELRTEPEAKKSKTAAKKNDK Complex Engineered Fragment 1BIX_ Relationship to function unknown Unknown Disordered region is not essential for protein function Unknown X-ray Crystallography 6.2 1,4- Dioxane 5 percent w/v calcium acetate 292 Kelvin 200 crystals flash cooled 110 Kelvin HEPES pH 7.4 10 MES pH 6.2 100 PEG 8000 16 to 20 percent w/v samarium acetate 7.5-30 mM well solution 3 Paper 11286553 Beernink PT, Segelke BW, Hadi MZ, Erzberger JP, Wilson DM 3rd, Rupp B 2001 J Mol Biol 307 4 1023-1034 9351835 Gorman MA, Morera S, Rothwell DG, de La Fortelle E, Mol CD, Tainer JA, Hickson ID, Freemont PS 1997 Embo J 16 21 6548-6558 The 1BIX PDB file gives the sequence as residue 44-318 but the Gorman paper says that the sturcture was modeled from residues 36-318 (Gorman 1997). The total length of the experimental sequence was 287, it did not contain the N-terminal residues 1-35. Disordered - Extended 1 43 MPKRGKKGAVAEDGDELRTEPEAKKSKTAAKKNDKEAAGEGPA Complex Engineered 1HD7A Relationship to function unknown Unknown Disordered region is not essential for protein function Unknown X-ray Crystallography 4.6 lead (II) acetate 1 polyethylene glycol 4000 25% (w/v) sodium acetate pH 4.6 0.1 Paper 11286553 Beernink PT, Segelke BW, Hadi MZ, Erzberger JP, Wilson DM 3rd, Rupp B 2001 J Mol Biol 307 4 1023-1034 Disordered - Extended 102 112 NKLPAELQELP Complex Engineered 1HD7A Relationship to function unknown Unknown Unknown X-ray Crystallography 4.6 lead (II) acetate 1 polyethylene glycol 4000 25% (w/v) sodium acetate pH 4.6 0.1 Paper 11286553 Beernink PT, Segelke BW, Hadi MZ, Erzberger JP, Wilson DM 3rd, Rupp B 2001 J Mol Biol 307 4 1023-1034 Disordered - Extended 123 127 SDKEG Complex Engineered 1HD7A Relationship to function unknown Unknown Unknown X-ray Crystallography 4.6 lead (II) acetate 1 polyethylene glycol 4000 25% (w/v) sodium acetate pH 4.6 0.1 Paper 11286553 Beernink PT, Segelke BW, Hadi MZ, Erzberger JP, Wilson DM 3rd, Rupp B 2001 J Mol Biol 307 4 1023-1034 Disordered 100 104 SENKL Complex Engineered 1BIX_ Relationship to function unknown Unknown Unknown X-ray Crystallography 6.2 1,4- Dioxane 5 percent w/v calcium acetate 292 Kelvin 200 crystals flash cooled 110 Kelvin HEPES pH 7.4 10 MES pH 6.2 100 PEG 8000 16 to 20 percent w/v samarium acetate 7.5-30 mM well solution 3 Paper 11286553 Beernink PT, Segelke BW, Hadi MZ, Erzberger JP, Wilson DM 3rd, Rupp B 2001 J Mol Biol 307 4 1023-1034 The total length of the experimental sequence was 287, it did not contain the N-terminal residues 1-35. Disordered - Extended 1 42 MPKRGKKGAVAEDGDELRTEPEAKKSKTAAKKNDKEAAGEGP Complex Engineered 1E9NA 1E9NB Relationship to function unknown Unknown Disordered region is not essential for protein function Unknown X-ray Crystallography 7.5 HECAMEG 19.5 lead (II) acetate 1 polyethylene glycol 4000 25% (w/v) sodium acetate 0.2 Tris-HCl pH 7.5 0.1 Paper 11286553 Beernink PT, Segelke BW, Hadi MZ, Erzberger JP, Wilson DM 3rd, Rupp B 2001 J Mol Biol 307 4 1023-1034 The crystal structure for this protein consists of 2 molecules of the protein, 4 platinum ions and 351 water molecules. Disordered - Extended 124 125 DK Complex Engineered 1E9NA 1E9NB Relationship to function unknown Unknown Unknown X-ray Crystallography 7.5 HECAMEG 19.5 lead (II) acetate 1 polyethylene glycol 4000 25% (w/v) sodium acetate 0.2 Tris-HCl pH 7.5 0.1 Paper 11286553 Beernink PT, Segelke BW, Hadi MZ, Erzberger JP, Wilson DM 3rd, Rupp B 2001 J Mol Biol 307 4 1023-1034 For forms I, II and III of this protein referenced in Beernick (2001) , there is relatively high thermal motion in the areas of residues 100-110, 145, 200 and 270. These areas also show large root-mean-square fluctuations. POU domain class 2, associating factor 1 B-cell-specific coactivator BOB.1/OBF.1 B cell-specific transcription co-activator BOB-1 OCA-B OCT binding factor 1 Q64693 1150493 S63588 Mus musculus (Mouse) 256 MLWQKSTAPEQAPAPPRPYQGVRVKEPVKELLRRKRGHTSVGAAGPPTAGVLPHQPLATYSTVGPSCLDMEVSASTVTEEGTLCAGWLSQPAPATLHALAPWTPYTEYVSHEAVSCPYSTDMYVQPVCPSYTVVGPSSVLTYASPPLITNVTPRSTATPAVGPQLEGPEHQAPLTYFPWPQPLSTLPTSSLQYQPPAPTLSGPQFVQLPISIPEPVLQDMDDPRRAISSLTIDKLLLEEEESNTYELNHTLSVEGF Disordered 1 256 MLWQKSTAPEQAPAPPRPYQGVRVKEPVKELLRRKRGHTSVGAAGPPTAGVLPHQPLATYSTVGPSCLDMEVSASTVTEEGTLCAGWLSQPAPATLHALAPWTPYTEYVSHEAVSCPYSTDMYVQPVCPSYTVVGPSSVLTYASPPLITNVTPRSTATPAVGPQLEGPEHQAPLTYFPWPQPLSTLPTSSLQYQPPAPTLSGPQFVQLPISIPEPVLQDMDDPRRAISSLTIDKLLLEEEESNTYELNHTLSVEGF Paper Alpha-S1 casein [Precursor] P02662 1070620 KABOSB Bos taurus (Bovine) 214 MKLLILTCLVAVALARPKHPIKHQGLPQEVLNENLLRFFVAPFPEVFGKEKVNELSKDIGSESTEDQAMEDIKQMEAESISSSEEIVPNSVEQKHIQKEDVPSERYLGYLEQLLRLKKYKVPQLEIVPNSAEERLHSMKEGIHAQQKEPMIGVNQELAYFYPELFRQFYQLDAYPSGAWYYVPLGTQYTDAPSFSDIPNPIGSENSEKTTMPLW Disordered 16 214 RPKHPIKHQGLPQEVLNENLLRFFVAPFPEVFGKEKVNELSKDIGSESTEDQAMEDIKQMEAESISSSEEIVPNSVEQKHIQKEDVPSERYLGYLEQLLRLKKYKVPQLEIVPNSAEERLHSMKEGIHAQQKEPMIGVNQELAYFYPELFRQFYQLDAYPSGAWYYVPLGTQYTDAPSFSDIPNPIGSENSEKTTMPLW Paper Monoamine-sulfating phenol sulfotransferase Catecholamine sulfotransferase EC 2.8.2.1 HAST3 M-PST Placental estrogen sulfotransferase Sulfotransferase, monoamine-preferring Thermolabile phenol sulfotransferase TL-PST P50224 Hs.458369 P50224 10835035 A55451 Homo sapiens (Human) 295 MELIQDTSRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLINTYPKSGTTWVSQILDMIYQGGDLEKCNRAPIYVRVPFLEVNDPGEPSGLETLKDTPPPRLIKSHLPLALLPQTLLDQKVKVVYVARNPKDVAVSYYHFHRMEKAHPEPGTWDSFLEKFMAGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETMDFMVQHTSFKEMKKNPMTNYTTVPQELMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL Disordered - Extended 216 261 PEETMDFMVQHTSFKEMKKNPMTNYTTVPQELMDHSISPFMRKGMA Fragment 1CJMA Function arises via a disorder to order transition Metal sponge Substrate/ligand binding X-ray Crystallography 293 lithium sulfate 0.5 PAP at 277 K pre-incubation for 1-2 hours polyethylene glycol 8000 5-7% (w/v) Paper 10543947 Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL 1999 J Mol Biol 293 3 521-530 Disordered 1 7 MELIQDT Fragment 1CJMA Function arises via a disorder to order transition Unknown Substrate/ligand binding X-ray Crystallography 293 lithium sulfate 0.5 PAP at 277 K pre-incubation for 1-2 hours polyethylene glycol 8000 5-7% (w/v) Paper 10543947 Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL 1999 J Mol Biol 293 3 521-530 Disordered 64 77 GGDLEKCNRAPIYV Fragment 1CJMA Function arises via a disorder to order transition Unknown Substrate/ligand binding X-ray Crystallography 293 lithium sulfate 0.5 PAP at 277 K pre-incubation for 1-2 hours polyethylene glycol 8000 5-7% (w/v) Paper 10543947 Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL 1999 J Mol Biol 293 3 521-530 Disordered 91 93 SGL Fragment 1CJMA Function arises via a disorder to order transition Unknown Substrate/ligand binding X-ray Crystallography 293 lithium sulfate 0.5 PAP at 277 K pre-incubation for 1-2 hours polyethylene glycol 8000 5-7% (w/v) Paper 10543947 Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL 1999 J Mol Biol 293 3 521-530 Disordered 294 295 EL Fragment 1CJMA Function arises via a disorder to order transition Unknown Substrate/ligand binding X-ray Crystallography 293 lithium sulfate 0.5 PAP at 277 K pre-incubation for 1-2 hours polyethylene glycol 8000 5-7% (w/v) Paper 10543947 Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL 1999 J Mol Biol 293 3 521-530 Disordered 216 224 PEETMDFMV Fragment 1CJMA Function arises via a disorder to order transition Unknown Substrate/ligand binding X-ray Crystallography 293 lithium sulfate 0.5 PAP at 277 K pre-incubation for 1-2 hours polyethylene glycol 8000 5-7% (w/v) Paper 10543947 Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL 1999 J Mol Biol 293 3 521-530 Ordered 8 63 SRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLINTYPKSGTTWVSQILDMIYQ 1CJMA Paper Ordered 78 90 RVPFLEVNDPGEP 1CJMA Paper Ordered 94 215 ETLKDTPPPRLIKSHLPLALLPQTLLDQKVKVVYVARNPKDVAVSYYHFHRMEKAHPEPGTWDSFLEKFMAGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSL 1CJMA Paper Ordered 262 293 GDWKTTFTVAQNERFDADYAEKMAGCSLSFRS 1CJMA Paper Cystic fibrosis transmembrane conductance regulator cAMP-dependent chloride channel CFTR Cystic fibrosis transmembrane conductance regulator, ATP-binding cassette P13569 1705762 DVHUCF Homo sapiens (Human) 1480 MQRSPLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEKLEREWDRELASKKNPKLINALRRCFFWRFMFYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGLGRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVFLSVLPYALIKGIILRKIFTTISFCIVLRMAVTRQFPWAVQTWYDSLGAINKIQDFLQKQEYKTLEYNLTTTEVVMENVTAFWEEGFGELFEKAKQNNNNRKTSNGDDSLFFSNFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPDFSSKLMGCDSFDQFSAERRNSILTETLHRFSLEGDAPVSWTETKKQSFKQTGEFGEKRKNSILNPINSIRKFSIVQKTPLQMNGIEEDSDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSVNQGQNIHRKTTASTRKVSLAPQANLTELDIYSRRLSQETGLEISEEINEEDLKECFFDDMESIPAVTTWNTYLRYITVHKSLIFVLIWCLVIFLAEVAASLVVLWLLGNTPLQDKGNSTHSRNNSYAVIITSTSSYYVFYIYVGVADTLLAMGFFRGLPLVHTLITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFISILTTGEGEGRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFIDMPTEGKPTKSTKPYKNGQLSKVMIIENSHVKKDDIWPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQAISPSDRVKLFPHRNSSKCKSKPQIAALKEETEEEVQDTRL Disordered 708 831 IRKFSIVQKTPLQMNGIEEDSDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSVNQGQNIHRKTTASTRKVSLAPQANLTELDIYSRRLSQETGLEISEEINEEDLKE Paper The sequence contains a mismatch at amino acid 470 when compared to PIR and SwissProt. Choriogonadotropin beta chain [Precursor] CG-beta Chorionic gonadotropin beta subunit Hcg Human chorionic gonadotropin P01233 116184 KTHUB Homo sapiens (Human) 145 SKEPLRPRCRPINATLAVEKEGCPVCITVNTTICAGYCPTMTRVLQGVLPALPQVVCNYRDVRFESIRLPGCPRGVNPVVSYAVALSCQCALCRRSTTDCGGPKDHPLTCDDPRFQDSSSSKAPPPSLPSPSRLPGPSDTPILPQ Disordered 112 145 DPRFQDSSSSKAPPPSLPSPSRLPGPSDTPILPQ Paper SwissProt and NCBI have a sequence of 165 amino acids. This includes a 20 amino acid signal region on the N-terminal. Clusterin [Precursor] DAG Dimeric acid glycoprotein SGP-2 Sulfated glycoprotein 2 Testosterone repressed prostate message-2 TRPM-2 P05371 461756 A27205 Rattus norvegicus (Rat) 447 MKILLLCVALLLTWDNGMVLGEQEFSDNELQELSTQGSRYVNKEIQNAVQGVKHIKTLIEKTNAERKSLLNSLEEAKKKKEGALDDTRDSEMKLKAFPEVCNETMMALWEECKPCLKHTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRIDSLLESDRQQSQVLDAMQDSFTRASGIIDTLFQDRFFTHEPQDIHHFSPMGFPHKRPHFLYPKSRLVRSLMPLSHYGPLSFHNMFQPFFDMIHQAQQAMDVQLHSPALQFPDVDFLKEGEDDPTVCKEIRHNSTGCLKMKGQCEKCQEILSVDCSTNNPAQANLRQELNDSLQVAERLTQQYNELLHSLQSKMLNTSSLLEQLNDQFTWVSQLANLTQGDDQYLRVSTVTTHSSDSEVPSRVTEVVVKLFDSDPITVVLPEEVSKDNPKFMDTVAEKALQEYRRKSRME Disordered 66 97 RKSLLNSLEEAKKKKEGALDDTRDSEMKLKAF Paper Disordered 386 445 TVTTHSSDSEVPSRVTEVVVKLFDSDPITVVLPEEVSKDNPKFMDTVAEKALQEYRRKSR Paper PIR has a mismatch at amino acid 187. cAMP-dependent protein kinase inhibitor, alpha form cAMP-dependent protein kinase inhibitor cAMP-dependent protein kinase inhibitor, muscle/brain isoform PKI-alpha P04541 48428970 A01340 Homo sapiens (Human) 75 TDVETTYADFIASGRTGRRNAIHDILVSSASGNSNELALKLAGLDINKTEGEEDAQRSSTEQSGEAQGEAAKSES Disordered 1 75 TDVETTYADFIASGRTGRRNAIHDILVSSASGNSNELALKLAGLDINKTEGEEDAQRSSTEQSGEAQGEAAKSES Paper Cyclin-dependent kinase inhibitor 1 CDK-interacting protein 1 Cyclin-dependent kinase inhibitor p21 MDA-6 Melanoma differentiation associated protein 6 p21 P38936 Hs.370771 P38936 2134956 I68674 Homo sapiens 164 MSEPAGDVRQNPCGSKACRRLFGPVDSEQLSRDCDALMAGCIQEARERWNFDFVTETPLEGDFAWERVRGLGLPKLYLPTGPRRGRDELGGGRRPGTSPALLQGTAEEDHVDLSLSCTLVPRSGEQAEGSPGGPGDSQGRKRRQTSMTDFYHSKRRLIFSKRKP Disordered - Extended p21-F (full length) 1 164 MSEPAGDVRQNPCGSKACRRLFGPVDSEQLSRDCDALMAGCIQEARERWNFDFVTETPLEGDFAWERVRGLGLPKLYLPTGPRRGRDELGGGRRPGTSPALLQGTAEEDHVDLSLSCTLVPRSGEQAEGSPGGPGDSQGRKRRQTSMTDFYHSKRRLIFSKRKP Native Function arises via a disorder to order transition Molecular assembly Protein-protein binding Aberrant mobility on SDS-PAGE gel Far-UV Circular Dichroism (CD) Gel Filtration/Size Exclusion Chromatography Insensitivity to pH Extremes Mass Spectrometry-Based High Resolution Hydrogen-Deuterium Exchange Nuclear Magnetic Resonance Sensitivity to Proteolysis Paper Cyclin-dependent kinase inhibitor 1C Cyclin-dependent kinase inhibitor p57 p57KIP2 P49918 Hs.106070 P49918 4557441 G02424 Homo sapiens 316 MSDASLRSTSTMERLVARGTFPVLVRTSACRSLFGPVDHEELSRELQARLAELNAEDQNRWDYDFQQDMPLRGPGRLQWTEVDSDSVPAFYRETVQVGRCRLLLAPRPVAVAVAVSPPLEPAAESLDGLEEAPEQLPSVPVPAPASTPPPVPVLAPAPAPAPAPVAAPVAAPVAVAVLAPAPAPAPAPAPAPAPVAAPAPAPAPAPAPAPAPAPAPDAAPQESAEQGANQGQRGQEPLADQLHSGISGRPAAGTAAASANGAAIKKLSGPLISDFFAKRKRSAPEKSSGDVPAPCPSPSAAPGVGSVEQTPRKRLR Disordered - Extended 1 316 MSDASLRSTSTMERLVARGTFPVLVRTSACRSLFGPVDHEELSRELQARLAELNAEDQNRWDYDFQQDMPLRGPGRLQWTEVDSDSVPAFYRETVQVGRCRLLLAPRPVAVAVAVSPPLEPAAESLDGLEEAPEQLPSVPVPAPASTPPPVPVLAPAPAPAPAPVAAPVAAPVAVAVLAPAPAPAPAPAPAPAPVAAPAPAPAPAPAPAPAPAPAPDAAPQESAEQGANQGQRGQEPLADQLHSGISGRPAAGTAAASANGAAIKKLSGPLISDFFAKRKRSAPEKSSGDVPAPCPSPSAAPGVGSVEQTPRKRLR Native Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Analytical Ultracentrifugation 278 Far-UV Circular Dichroism (CD) 7 DTT 0.001 NaCl salt 50 sodium phosphate salt 10 Gel Filtration/Size Exclusion Chromatography 7 DTT 1 NaCl salt 150 sodium phosphate salt 10 Intrinsic Fluorescence 7 DTT 1 NaCl salt 50 sodium phosphate salt 10 Nuclear Magnetic Resonance 303 6.6 DTT 1 NaCl salt 50 sodium phosphate salt 10 Paper 11746698 Adkins JN, Lumb KJ 2002 Proteins 46 1 1-7 9251023 Dynlacht BD, Ngwu C, Winston J, Swindell EC, Elledge SJ, Harlow E, Harper JW 1997 Methods Enzymol 283 230-44 Disordered - Extended inhibition domain 27 91 TSACRSLFGPVDHEELSRELQARLAELNAEDQNRWDYDFQQDMPLRGPGRLQWTEVDSDSVPAFY Fragment Native Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Analytical Ultracentrifugation 278 Far-UV Circular Dichroism (CD) 7 DTT 0.001 NaCl salt 50 sodium phosphate salt 10 Paper 11746698 Adkins JN, Lumb KJ 2002 Proteins 46 1 1-7 9251023 Dynlacht BD, Ngwu C, Winston J, Swindell EC, Elledge SJ, Harlow E, Harper JW 1997 Methods Enzymol 283 230-44 This fragment had 90% inhibition activity towards A-CDK2. Cyclin-dependent kinase inhibitor 1B Cyclin-dependent kinase inhibitor p27 p27Kip1 P46527 1168871 Homo sapiens (Human) 198 MSNVRVSNGSPSLERMDARQAEHPKPSACRNLFGPVDHEELTRDLEKHCRDMEEASQRKWNFDFQNHKPLEGKYEWQEVEKGSLPEFYYRPPRPPKGACKVPAQESQDVSGSRPAAPLIGAPANSEDTHLVDPKTDPSDSQTGLAEQCAGIRKRPATDDSSTQNKRANRTEENVSDGSPNAGSVEQTPKKPGLRRRQT Disordered 22 106 EHPKPSACRNLFGPVDHEELTRDLEKHCRDMEEASQRKWNFDFQNHKPLEGKYEWQEVEKGSLPEFYYRPPRPPKGACKVPAQES Paper Ubiquinol-cytochrome c reductase iron-sulfur subunit, mitochondrial [Precursor] Cytochrome Bc1 Complex Ubiquinol Cytochrome C Oxidoreductase, Complex III P13272 1351360 A34660 Bos taurus (Bovine) 274 MLSVAARSGPFAPVLSATSRGVAGALRPLVQAAVPATSESPVLDLKRSVLCRESLRGQAAGRPLVASVSLNVPASVRYSHTDIKVPDFSDYRRPEVLDSTKSSKESSEARKGFSYLVTATTTVGVAYAAKNVVSQFVSSMSASADVLAMSKIEIKLSDIPEGKNMAFKWRGKPLFVRHRTKKEIDQEAAVEVSQLRDPQHDLERVKKPEWVILIGVCTHLGCVPIANAGDFGGYYCPCHGSHYDASGRIRKGPAPLNLEVPSYEFTSDDMVIVG Disordered 1 45 MLSVAARSGPFAPVLSATSRGVAGALRPLVQAAVPATSESPVLDL Paper DNA-binding protein RAP1 Repressor/activator site binding protein SBF-E TUF P11938 730473 S50714 Saccharomyces cerevisiae (Baker's yeast) 827 MSSPDDFETAPAEYVDALDPSMVVVDSGSAAVTAPSDSAAEVKANQNEENTGATAAETSEKVDQTEVEKKDDDDTTEVGVTTTTPSIADTAATANIASTSGASVTEPTTDDTAADEKKEQVSGPPLSNMKFYLNRDADAHDSLNDIDQLARLIRANGGEVLDSKPRESKENVFIVSPYNHTNLPTVTPTYIKACCQSNSLLNMENYLVPYDNFREVVDSRLQEESHSNGVDNSNSNSDNKDSIRPKTEIISTNTNGATEDSTSEKVMVDAEQQARLQEQAQLLRQHVSSTASITSGGHNDLVQIEQPQKDTSNNNNSNVNDEDNDLLTQDNNPQTADEGNASFQAQRSMISRGALPSHNKASFTDEEDEFILDVVRKNPTRRTTHTLYDEISHYVPNHTGNSIRHRFRVYLSKRLEYVYEVDKFGKLVRDDDGNLIKTKVLPPSIKRKFSADEDYTLAIAVKKQFYRDLFQIDPDTGRSLITDEDTPTAIARRNMTMDPNHVPGSEPNFAAYRTQSRRGPIAREFFKHFAEEHAAHTENAWRDRFRKFLLAYGIDDYISYYEAEKAQNREPEPMKNLTNRPKRPGVPTPGNYNSAAKRARNYSSQRNVQPTANAASANAAAAAAAAASNSYAIPENELLDEDTMNFISSLKNDLSNISNSLPFEYPHEIAEAIRSDFSNEDIYDNIDPDTISFPPKIATTDLFLPLFFHFGSTRQFMDKLHEVISGDYEPSQAEKLVQDLCDETGIRKNFSTSILTCLSGDLMVFPRYFLNMFKDNVNPPPNVPGIWTHDDDESLKSNDQEQIRKLVKKHGTGRMEMRKRFFEKDLL Disordered 482 512 TDEDTPTAIARRNMTMDPNHVPGSEPNFAAY Paper Elongation factor G Elongation Factor G Without Nucleotide P13551 1827912 Thermus thermophilus 691 MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERERGITITAAVTTCFWKDHRINIIDTPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSETVWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDVLRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEEELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVEIHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHANHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKADQEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDANVGKPQVAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIPAVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYHEVDSSEMAFKIAGSMAIKEAVQKGDPVILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLRSKTQGRGSFVMFFDHYQEVPKQVQEKLIKGQ Disordered 40 67 HKIGEVHEGAATMDFMEQERERGITITA Paper Disordered 400 475 ESIEVPEPVIDVAIEPKTKADQEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDAN Paper EMB-1 protein Embryonic abundant protein from carrot P17639 119316 JQ2273 Daucus carota (Carrot) 92 MASQQEKKELDARARQGETVVPGGTGGKSLEAQQHLAEGRSKGGQTRKEQLGGEGYHEMGRKGGLSNNDMSGGERAEQEGIDIDESKFRTKK Disordered 1 92 MASQQEKKELDARARQGETVVPGGTGGKSLEAQQHLAEGRSKGGQTRKEQLGGEGYHEMGRKGGLSNNDMSGGERAEQEGIDIDESKFRTKK Paper E7 protein E7 protein from HPV16 P03129 6469700 Human papillomavirus type 16 93 MHGDTPTLHEYMLDLQPETTDLYCYEQLSDSSEEEDEIDGPAGQAEPDRAHYNIVTFCCKCDSTLRLCVQSTHVDIRTLEDLLMGTLGIVCPI Disordered 1 93 MHGDTPTLHEYMLDLQPETTDLYCYEQLSDSSEEEDEIDGPAGQAEPDRAHYNIVTFCCKCDSTLRLCVQSTHVDIRTLEDLLMGTLGIVCPI Paper SwissProt has a five amino acid addition at the C-terminal end of this protein. Fibronectin-binding protein [Precursor] Fibronectin binding protein FNBP P14738 120457 Staphylococcus aureus 1018 MKNNLRYGIRKHKLGAASVFLGTMIVVGMGQDKEAAASEQKTTTVEENGNSATDNKTSETQTTATNVNHIEETQSYNATVTEQPSNATQVTTEEAPKAVQAPQTAQPANIETVKEEVVKEEAKPQVKETTQSQDNSGDQRQVDLTPKKATQNQVAETQVEVAQPRTASESKPRVTRSADVAEAKEASNAKVETGTDVTSKVTVEIGSIEGHNNTNKVEPHAGQRAVLKYKLKFENGLHQGDYFDFTLSNNVNTHGVSTARKVPEIKNGSVVMATGEVLEGGKIRYTFTNDIEDKVDVTAELEINLFIDPKTVQTNGNQTITSTLNEEQTSKELDVKYKDGIGNYYANLNGSIETFNKANNRFSHVAFIKPNNGKTTSVTVTGTLMKGSNQNGNQPKVRIFEYLGNNEDIAKSVYANTTDTSKFKEVTSNMSGNLNLQNNGSYSLNIENLDKTYVVHYDGEYLNGTDEVDFRTQMVGHPEQLYKYYYDRGYTLTWDNGLVLYSNKANGNEKNGPIIQNNKFEYKEDTIKETLTGQYDKNLVTTVEEEYDSSTLDIDYHTAIDGGGGYVDGYIETIEETDSSAIDIDYHTAVDSEAGHVGGYTESSEESNPIDFEESTHENSKHHADVVEYEEDTNPGGGQVTTESNLVEFDEESTKGIVTGAVSDHTTVEDTKEYTTESNLIELVDELPEEHGQAQGPVEEITKNNHHISHSGLGTENGHGNYDVIEEIEENSHVDIKSELGYEGGQNSGNQSFEEDTEEDKPKYEQGGNIVDIDFDSVPQIHGQNKGNQSFEEDTEKDKPKYEHGGNIIDIDFDSVPHIHGFNKHTEIIEEDTNKDKPSYQFGGHNSVDFEEDTLPKVSGQNEGQQTIEEDTTPPIVPPTPPTPEVPSEPETPTPPTPEVPSEPETPTPPTPEVPSEPETPTPPTPEVPAEPGKPVPPAKEEPKKPSKPVEQGKVVTPVIEINEKVKAVAPTKKPQSKKSELPETGGEESTNKGMLFGGLFSILGLALLRRNKKNHKA Disordered 745 873 GQNSGNQSFEEDTEEDKPKYEQGGNIVDIDFDSVPQIHGQNKGNQSFEEDTEKDKPKYEHGGNIIDIDFDSVPHIHGFNKHTEIIEEDTNKDKPSYQFGGHNSVDFEEDTLPKVSGQNEGQQTIEEDTT Paper Flagellin Phase-1-I flagellin P06179 96744 S16121 Salmonella typhimurium 494 AQVINTNSLSLLTQNNLNKSQSALGTAIERLSSGLRINSAKDDAAGQAIANRFTANIKGLTQASRNANDGISIAQTTEGALNEINNNLQRVRELAVQSANSTNSQSDLDSIQAEITQRLNEIDRVSGQTQFNGVKVLAQDNTLTIQVGANDGETIDIDLKQINSQTLGLDTLNVQQKYKVSDTAATVTGYADTTIALDNSTFKASATGLGGTDQKIDGDLKFDDTTGKYYAKVTVTGGTGKDGYYEVSVDKTNGEVTLAGGATSPLTGGLPATATEDVKNVQVANADLTEAKAALTAAGVTGTASVVKMSYTDNNGKTIDGGLAVKVGDDYYSATQNKDGSISINTTKYTADDGTSKTALNKLGGADGKTEVVSIGGKTYAASKAEGHNFKAQPDLAEAAATTTENPLQKIDAALAQVDTLRSDLGAVQNRFNSAITNLGNTVNNLTSARSRIEDSDYATEVSNMSRAQILQQAGTSVLAQANQVPQNVLSLLR Disordered 1 55 AQVINTNSLSLLTQNNLNKSQSALGTAIERLSSGLRINSAKDDAAGQAIANRFTA Paper Disordered 451 494 SRIEDSDYATEVSNMSRAQILQQAGTSVLAQANQVPQNVLSLLR Paper Negative regulator of flagellin synthesis Anti-sigma-28 factor Flagellum specific sigma factor P26477 120306 A41046 Salmonella typhimurium 97 MSIDRTSPLKPVSTVQTRETSDTPVQKTRQEKTSAATSASVTLSDAQAKLMQPGVSDINMERVEALKTAIRNGELKMDTGKIADSLIREAQSYLQSK Disordered 1 97 MSIDRTSPLKPVSTVQTRETSDTPVQKTRQEKTSAATSASVTLSDAQAKLMQPGVSDINMERVEALKTAIRNGELKMDTGKIADSLIREAQSYLQSK Paper Eukaryotic translation initiation factor 4E binding protein 1 4E-binding protein 1 4E-BP1 eIF4E-binding protein 1 PHAS-I Phosphorylated heat- and acid-stable protein regulated by insulin 1 Q13541 4758258 S50866 Homo sapiens (Human) 118 MSGGSSCSQTPSRAIPATRRVVLGDGVQLPPGDYSTTPGGTLFSTTPGGTRIIYDRKFLMECRNSPVTKTPPRDLPTIPGVTSPSSDEPPMEASQSHLRNSPEDKRAGGEESQFEMDI Disordered 1 118 MSGGSSCSQTPSRAIPATRRVVLGDGVQLPPGDYSTTPGGTLFSTTPGGTRIIYDRKFLMECRNSPVTKTPPRDLPTIPGVTSPSSDEPPMEASQSHLRNSPEDKRAGGEESQFEMDI Paper Glial cell line-derived neurotrophic factor GDNF Glial cell line-derived neurotrophic factor [Precursor] Q07731 Q07731 729568 A37499 Rattus norvegicus (Rat) 211 MKLWDVVAVCLVLLHTASAFPLPAGKRLLEAPAEDHSLGHRRVPFALTSDSNMPEDYPDQFDDVMDFIQATIKRLKRSPDKQAAALPRRERNRQAAAASPENSRGKGRRGQRGKNRGCVLTAIHLNVTDLGLGYETKEELIFRYCSGSCEAAETMYDKILKNLSRSRRLTSDKVGQACCRPVAFDDDLSFLDDSLVYHILRKHSAKRCGCI Disordered - Extended 77 113 RSPDKQAAALPRRERNRQAAAASPENSRGKGRRGQRG Engineered 1AGQA 1AGQB 1AGQC 1AGQD Relationship to function unknown Molecular assembly Protein-protein binding X-ray Crystallography 273 7 Paper 9187648 Eigenbrot C, Gerber N 1997 Nat Struct Biol 4 6 435-8 10545102 Eketjall S, Fainzilber M, Murray-Rust J, Ibanez CF 1999 Embo J 18 21 5901-10 The first identifiable residue in 1AGQ was ASN 39 in chain A, LYS 38 in chain B, GLY 41 in chain C, and GLY 41 in chain D. This is supported by claims in the Eigenbrot paper as being dependent upon the monomer. The experimental protein consisted of residues 78 - 211 of SwissProt entry Q07731. Disordered - Extended 170 173 TSDK Engineered 1AGQA 1AGQB 1AGQC 1AGQD Relationship to function unknown Unknown Unknown X-ray Crystallography 273 7 Paper 10545102 Eketjall S, Fainzilber M, Murray-Rust J, Ibanez CF 1999 Embo J 18 21 5901-10 This sequence is part of a flexible loop that connects the alpha helix region to the second finger region of the protein. The experimental protein consisted of residues 78 - 211 of SwissProt entry Q07731. Ordered 114 169 KNRGCVLTAIHLNVTDLGLGYETKEELIFRYCSGSCEAAETMYDKILKNLSRSRRL 1AGQA 1AGQB 1AGQC 1AGQD Paper Ordered 174 211 VGQACCRPVAFDDDLSFLDDSLVYHILRKHSAKRCGCI 1AGQA 1AGQB 1AGQC 1AGQD Paper Glucocorticoid receptor GR P04150 Hs.126608 P04150 4758482 QRHUGA Homo sapiens (Human) 777 MDSKESLTPGREENPSSVLAQERGDVMDFYKTLRGGATVKVSASSPSLAVASQSDSKQRRLLVDFPKGSVSNAQQPDLSKAVSLSMGLYMGETETKVMGNDLGFPQQGQISLSSGETDLKLLEESIANLNRSTSVPENPKSSASTAVSAAPTEKEFPKTHSDVSSEQQHLKGQTGTNGGNVKLYTTDQSTFDILQDLEFSSGSPGKETNESPWRSDLLIDENCLLSPLAGEDDSFLLEGNSNEDCKPLILPDTKPKIKDNGDLVLSSPSNVTLPQVKTEKEDFIELCTPGVIKQEKLGTVYCQASFPGANIIGNKMSAISVHGVSTSGGQMYHYDMNTASLSQQQDQKPIFNVIPPIPVGSENWNRCQGSGDDNLTSLGTLNFPGRTVFSNGYSSPSMRPDVSSPPSSSSTATTGPPPKLCLVCSDEASGCHYGVLTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRYRKCLQAGMNLEARKTKKKIKGIQQATTGVSQETSENPGNKTIVPATLPQLTPTLVSLLEVIEPEVLYAGYDSSVPDSTWRIMTTLNMLGGRQVIAAVKWAKAIPGFRNLHLDDQMTLLQYSWMFLMAFALGWRSYRQSSANLLCFAPDLIINEQRMTLPCMYDQCKHMLYVSSELHRLQVSYEEYLCMKTLLLLSSVPKDGLKSQELFDEIRMTYIKELGKAIVKREGNSSQNWQRFYQLTKLLDSMHEVVENLLNYCFQTFLDKTMSIEFPEMLAEIITNQIPKYSNGNIKKLLFHQK Disordered - Extended 77 262 DLSKAVSLSMGLYMGETETKVMGNDLGFPQQGQISLSSGETDLKLLEESIANLNRSTSVPENPKSSASTAVSAAPTEKEFPKTHSDVSSEQQHLKGQTGTNGGNVKLYTTDQSTFDILQDLEFSSGSPGKETNESPWRSDLLIDENCLLSPLAGEDDSFLLEGNSNEDCKPLILPDTKPKIKDNGD Engineered Function arises via a disorder to order transition Molecular recognition effectors Metal binding Phosphorylation Protein-DNA binding Protein-protein binding Far-UV Circular Dichroism (CD) 295 7 dithiothreitol 1 phosphate 3 TFE Nuclear Magnetic Resonance 289 5.9 dithiothreitiol 1 phosphates 20 Paper 10196139 Baskakov IV, Kumar R, Srinivasan G, Ji YS, Bolen DW, Thompson EB 1999 J Biol Chem 274 16 10693-10696 7878043 Dahlman-Wright K, Baumann H, McEwan IJ, Almlof T, Wright AP, Gustafsson JA, Hard T 1995 Proc Natl Acad Sci U S A 92 5 1699-1703 12902338 Li, G. Wang, S. Gelehrter, T. D 2003 J Biol Chem 278 43 41779-41788 The 58 residue Tau1 core region of the disordered polypeptide from 187-244 retains 60-70% of the activity of the domain. The disordered region is devoid of structure at neutral pH in aqueous solution. The ligand-binding domain becomes notably more structured in the presence of triflouroethanol (TFE). TFE creates a more non-polar environment and favors secondary structure formation. The propensity towards alpha-helicial structure may be an important step in Tau1-mediated gene activation The sequence given in Hollenberg (1985) appears to be in error. Blasting against the Swiss-Prot sequence reveals only a 94% similarity with all the discrepancies being tyrosines replacing lysines. Glycine N-methyltransferase Folate-binding protein P13255 121328 S00112 Rattus norvegicus (Rat) 292 VDSVYRTRSLGVAAEGIPDQYADGEAARVWQLYIGDTRSRTAEYKAWLLGLLRQHGCHRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYALKERWNRRKEPAFDKWVIEEANWLTLDKDVPAGDGFDAVICLGNSFAHLPDSKGDQSEHRLALKNIASMVRPGGLLVIDHKNYDYILSTGCAPPGKNIYYKSDLTKDITTSVLTVNNKAHMVTLDYTVQVPGAGRDGAPGFSKFRLSYYPHCLASFTELVQEAFGGRCQHSVLGDFKPYRPGQAYVPCYFIHVLKKTG Disordered 1 40 VDSVYRTRSLGVAAEGIPDQYADGEAARVWQLYIGDTRSR Paper Glycyl-tRNA synthetase Glycyl-tRNA ligase 1B76_B Thermus thermophilus 442 AASSLDELVALCKRRGFIFQSSEIYGGLQGVYDYGPLGVELKNNLKQAWWRRNVYERDDMEGLDASVLTHRLVLHYSGHEATFADPMVDNAKARYWTPPRYFNMMFQDLRGPRGGRGLLAYLRPETAQGIFVNFKNVLDATSRKLGFGIAQIGKAFRNEITPRNFIFRVREFEQMEIEYFVRPGEDEYWHRYWVEERLKWWQEMGLSRENLVPYQQPPESSAHYAKATVDILYRFPHGSLELEGIAQRTDFDLGSHTKDQEALGITARVLRNEHSTQRLAYRDPETGKWFVPYVIEPSAGVDRGVLALLAEAFTREELPNGEERIVLKLKPQLAPIKVAVIPLVKNRPEITEYAKRLKARLLALGLGRVLYEDTGNIGKAYRRHDEVGTPFAVTVDYDTIGQSKDGTTRLKDTVTVRDRDTMEQIRLHVDELEGFLRERLRW Disordered 96 158 WTPPRYFNMMFQDLRGPRGGRGLLAYLRPETAQGIFVNFKNVLDATSRKLGFGIAQIGKAFRN Paper Human growth hormone binding protein hGHbp Human growth hormone receptor binding domain Human growth hormone receptor extracellular domain P10912 Hs.125180 P10912 4503993 A33991 Homo sapiens (Human) 246 FSGSEATAAILSRAPWSLQSVNPGLKTNSSKEPKFTKCRSPERETFSCHWTDEVHHGTKNLGPIQLFYTRRNTQEWTQEWKECPDYVSAGENSCYFNSSFTSIWIPYCIKLTSNGGTVDEKCFSVDEIVQPDPPIALNWTLLNVSLTGIHADIQVRWEAPRNADIQKGWMVLEYELQYKEVNETKWKMMDPILTTSVPVYSLKVDKEYEVRVRSKQRNSGNYGEFSEVLYVTLPQMSQFTCEEDFY Disordered - Extended 1 32 FSGSEATAAILSRAPWSLQSVNPGLKTNSSKE Complex 1A22B Relationship to function unknown Unknown Unknown X-ray Crystallography 1:1 complex structure determined at 2.6 Angstroms 1:2 complex structure determined at 2.6 Angstroms Paper 9571026 Clackson T, Ultsch MH, Wells JA, de Vos AM 1998 J Mol Biol 277 5 1111-1128 Disordered - Extended 52 60 DEVHHGTKN Complex 1A22B Relationship to function unknown Unknown Unknown X-ray Crystallography 1:1 complex structure determined at 2.6 Angstroms 1:2 complex structure determined at 2.6 Angstroms Paper 9571026 Clackson T, Ultsch MH, Wells JA, de Vos AM 1998 J Mol Biol 277 5 1111-1128 Disordered - Extended 144 147 VSLT Complex 1A22B Relationship to function unknown Unknown Unknown X-ray Crystallography 1:1 complex structure determined at 2.6 Angstroms 1:2 complex structure determ