eF-site ID 6nra-ABCDEFGHIJKLMNOP PDB Code 6nra Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P Title hTRiC-hPFD Class1 (No PFD) Classification CHAPERONE Compound T-complex protein 1 subunit alpha Source (TCPQ_HUMAN) Sequence A:  TGETIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDV TITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTS VVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYI NENLIVNTDELGRDCLINAAKTSMSSKIIGINGDFFANMV VDAVLAIKYTDIRGQPRYPVNSVNILKAHGRSQMESMLIS GYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQV VITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGI DDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGATILSTLA NLEGEETFEAAMLGQAEEVVQERICDDELILIKNTKARTS ASIILRGANDFMCDEMERSLHDALCVVKRVLESKSVVPGG GAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTL AVNAAQDSTDLVAKLRAFHNEAQVNPERKNLKWIGLDLSN GKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIK L B:  ADEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSS GRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEV GDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATK AAREALLSSAVDHGSDEVKFRQDLMNIAGTTLSSKLLTHH KDHFTKLAVEAVLRLKGSGNLEAIHIIKKLGGSLADSYLD EGFLLDKKIGVNQPKRIENAKILIANTGMDTDKIKIFGSR VRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQL IYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTF DHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVL RGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEM LMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAG YDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITE SFQVKRQVLLSAAEAAEVILRVDNIIKAA C:  RESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMG GIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDGT TSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMIS TLKKISIPVDISDSDMMLNIINSSITTKAISRWSSLACNI ALDAVKMVQFEENGRKEIDIKKYARVEKIPGGIIEDSCVL RGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYKKGESQTD IEITREEDFTRILQMEEEYIQQLCEDIIQLKPDVVITEKG ISDLAQHYLMRANITAIRRVRKTDNNRIARACGARIVSRP EELREDDVGTGAGLLEIKKIGDEYFTFITDCKDPKACTIL LRGASKEILSEVERNLQDAMQVCRNVLLDPQLVPGGGASE MAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNC GASTIRLLTSLRAKHTQENCETWGVNGETGTLVDMKELGI WEPLAVKLQTYKTAVETAVLLLRIDDIVS D:  DRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGK GDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDG TTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGI EILTDMSRPVELSDRETLLNSATTSLNSKVVSQYSSLLSP MSVNAVMKVIDPATATSVDLRDIKIVKKLGGTIDDCELVE GLVLTQKVSNSGITRVEKAKIGLIQFCLSAPKTDMDNQIV VSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSIL RDALSDLALHFLNKMKIMVIKDIEREDIEFICKTIGTKPV AHIDQFTADMLGSAELAEEVNLNGSGKLLKITGCASPGKT VTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGG GAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTL AENAGLNPISTVTELRNRHAQGEKTAGINVRKGGISNILE ELVVQPLLVSVSALTLATETVRSILKID E:  KSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDK DGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGD GTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVA IEHLDKISDSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQ MAEIAVNAVLTVADMERRDVDFELIKVEGKVGGRLEDTKL IKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPKPKTKH KLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQW GFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPR FSELTAEKLGFAGLVQEISFGTTKDKMLVIEQCKNSRAVT IFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGA AEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSE NSGMNPIQTMTEVRARQVKEMNPALGIDCLHKGTNDMKQQ HVIETLIGKKQQISLATQMVRMILKIDDIRKPGESEE F:  EVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGA GDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDG TTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKAL QFLEEVKVSREMDRETLIDVARTSLRTKVHAELADVLTEA VVDSILAIKKQDEPIDLFMIEIMEMKHKSETDTSLIRGLV LDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYK SAEEREKLVKAERKFIEDRVKKIIELKRKVCGDSDKGFVV INQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGV ALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRS VTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGA GAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVL AQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAE VGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAG G:  TDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDG RGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGD GTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLA VNKIKEIAVTVKKADKVEQRKLLEKCAMTALSSKLISQQK AFFAKMVVDAVMMLDDLLQLKMIGIKKVQGGALEDSQLVA GVAFKKTFSYAGFEMQPKKYHNPKIALLNVELELKAEKDN AEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSK LPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGGSIQT SVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTF ILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAGGGAI EMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDN AGFDATNILNKLRARHAQGGTWYGVDINNEDIADNFEAFV WEPAMVRINALTAASEAACLIVSVDETIKNPR H:  MLKEGAKHFSGLEEAVYRNIQACKELAQTTRTAYGPNGMN KMVINHLEKLFVTNDAATILRELEVQHPAAKMIVMASHMQ EQEVGDGTNFVLVFAGALLELAEELLRIGLSVSEVIEGYE IACRKAHEILPNLVCCSAKNLRDIDEVSSLLRTSIMSKQY GNEVFLAKLIAQACVSIFPDSGHFNVDNIRVCKILGSGIS SSSVLHGMVFKKETEGDVTSVKDAKIAVYSCPFDGMITET KGTVLIKTAEELMNFSKGEENLMDAQVKAIADTGANVVVT GGKVADMALHYANKYNIMLVRLNSKWDLRRLCKTVGATAL PRLTPPVLEEMGHCDSVYLSEVGDTQVVVFKHEKEDGAIS TIVLRGSTDNLMDDIERAVDDGVNTFKVLTRDKRLVPGGG ATEIELAKQITSYGETCPGLEQYAIKKFAEAFEAIPRALA ENSGVKANEVISKLYAVHQEGNKNVGLDIEAEVPAVKDML EAGILDTYLGKYWAIKLATNAAVTVLRVDQ I:  MEGPLSVFGDRSTGETIRSQNVMAAASIANIVKSSLGPVG LDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELAD LQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISG YRLACKEAVRYINENLIVNTDELGRDCLINAAKTSMSSKI IGINGDFFANMVVDAVLAIKYTDIRGQPRYPVNSVNILKA HGRSQMESMLISGYALNCVVGSQGMPKRIVNAKIACLDFS LQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILA TGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIA KASGATILSTLANLEGEETFEAAMLGQAEEVVQERICDDE LILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVK RVLESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAE FARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVNPER KNLKWIGLDLSNGKPRDNKQAGVFEPTIVKVKSLKFATEA AITILRIDDLIKLH J:  ADEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSS GRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEV GDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATK AAREALLSSAVDHGSDEVKFRQDLMNIAGTTLSSKLLTHH KDHFTKLAVEAVLRLKGSGNLEAIHIIKKLGGSLADSYLD EGFLLDKKIGVNQPKRIENAKILIANTGMDTDKIKIFGSR VRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQL IYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTF DHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVL RGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEM LMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAG YDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITE SFQVKRQVLLSAAEAAEVILRVDNIIKA K:  NTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLD PMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVG DGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDD MISTLKKISIPVDISDSDMMLNIINSSITTKAISRWSSLA CNIALDAVKMVQFEENGRKEIDIKKYARVEKIPGGIIEDS CVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYKKGES QTDIEITREEDFTRILQMEEEYIQQLCEDIIQLKPDVVIT EKGISDLAQHYLMRANITAIRRVRKTDNNRIARACGARIV SRPEELREDDVGTGAGLLEIKKIGDEYFTFITDCKDPKAC TILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLVPGGG ASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLI QNCGASTIRLLTSLRAKHTQENCETWGVNGETGTLVDMKE LGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSG L:  RDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKG DVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGT TSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGIE ILTDMSRPVELSDRETLLNSATTSLNSKVVSQYSSLLSPM SVNAVMKVIDPATATSVDLRDIKIVKKLGGTIDDCELVEG LVLTQKVSNSGITRVEKAKIGLIQFCLSAPKTDMDNQIVV SDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSILR DALSDLALHFLNKMKIMVIKDIEREDIEFICKTIGTKPVA HIDQFTADMLGSAELAEEVNLNGSGKLLKITGCASPGKTV TIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGG APEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLA ENAGLNPISTVTELRNRHAQGEKTAGINVRKGGISNILEE LVVQPLLVSVSALTLATETVRSILKIDDVVNTR M:  KSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDK DGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGD GTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVA IEHLDKISDSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQ MAEIAVNAVLTVADMERRDVDFELIKVEGKVGGRLEDTKL IKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPKPKTKH KLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQW GFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPR FSELTAEKLGFAGLVQEISFGTTKDKMLVIEQCKNSRAVT IFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGA AEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSE NSGMNPIQTMTEVRARQVKEMNPALGIDCLHKGTNDMKQQ HVIETLIGKKQQISLATQMVRMILKIDDIRKPGESEE N:  AEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSG AGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGD GTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKA LQFLEEVKVSREMDRETLIDVARTSLRTKVHAELADVLTE AVVDSILAIKKQDEPIDLFMIEIMEMKHKSETDTSLIRGL VLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFY KSAEEREKLVKAERKFIEDRVKKIIELKRKVCGDSDKGFV VINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGG VALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPR SVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPG AGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKV LAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAA EVGVWDNYCVKKQLLHSCTVIATNILLVDEIMR O:  GTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVD GRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVG DGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQL AVNKIKEIAVTVKKADKVEQRKLLEKCAMTALSSKLISQQ KAFFAKMVVDAVMMLDDLLQLKMIGIKKVQGGALEDSQLV AGVAFKKTFSYAGFEMQPKKYHNPKIALLNVELELKAEKD NAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLS KLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGGSIQ TSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCT FILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAGGGA IEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCD NAGFDATNILNKLRARHAQGGTWYGVDINNEDIADNFEAF VWEPAMVRINALTAASEAACLIVSVDETIKNPRS P:  AKHFSGLEEAVYRNIQACKELAQTTRTAYGPNGMNKMVIN HLEKLFVTNDAATILRELEVQHPAAKMIVMASHMQEQEVG DGTNFVLVFAGALLELAEELLRIGLSVSEVIEGYEIACRK AHEILPNLVCCSAKNLRDIDEVSSLLRTSIMSKQYGNEVF LAKLIAQACVSIFPDSGHFNVDNIRVCKILGSGISSSSVL HGMVFKKETEGDVTSVKDAKIAVYSCPFDGMITETKGTVL IKTAEELMNFSKGEENLMDAQVKAIADTGANVVVTGGKVA DMALHYANKYNIMLVRLNSKWDLRRLCKTVGATALPRLTP PVLEEMGHCDSVYLSEVGDTQVVVFKHEKEDGAISTIVLR GSTDNLMDDIERAVDDGVNTFKVLTRDKRLVPGGGATEIE LAKQITSYGETCPGLEQYAIKKFAEAFEAIPRALAENSGV KANEVISKLYAVHQEGNKNVGLDIEAEVPAVKDMLEAGIL DTYLGKYWAIKLATNAAVTVLRVDQIIMA Description Functional site 1) chain H residue 282-293 type prosite sequence AIADTGANVVVT description ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. AIADTGANVVVT source prosite : PS00141 2) chain B residue 95-120 type prosite sequence VGDGTTSVTVLAAELLREAESLIAKK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGDGTTSVTVlAaellreaesl........IAKK source prosite : PS00107 3) chain H residue 224 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI6 4) chain H residue 254 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI6 5) chain H residue 260 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI6 6) chain P residue 224 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI6 7) chain P residue 254 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI6 8) chain P residue 260 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI6 9) chain C residue 430 type CROSSLNK sequence T description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0007744|PubMed:25114211 source Swiss-Prot : SWS_FT_FI7 10) chain H residue 459 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0007744|PubMed:25114211 source Swiss-Prot : SWS_FT_FI7 11) chain K residue 430 type CROSSLNK sequence T description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0007744|PubMed:25114211 source Swiss-Prot : SWS_FT_FI7 12) chain P residue 459 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0007744|PubMed:25114211 source Swiss-Prot : SWS_FT_FI7 13) chain C residue 248 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI8 14) chain C residue 249 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI8 15) chain K residue 15 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI8 16) chain K residue 248 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI8 17) chain K residue 249 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI8 18) chain C residue 381 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25114211 source Swiss-Prot : SWS_FT_FI9 19) chain K residue 381 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25114211 source Swiss-Prot : SWS_FT_FI9 20) chain H residue 23 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 21) chain P residue 23 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 22) chain O residue 67 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 23) chain O residue 320 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 24) chain N residue 199 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 25) chain N residue 365 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 26) chain N residue 377 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 27) chain N residue 388 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 28) chain H residue 30 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 29) chain P residue 30 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 30) chain M residue 346 type MOD_RES sequence S description Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 31) chain M residue 539 type MOD_RES sequence S description Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 32) chain L residue 288 type MOD_RES sequence K description Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 33) chain L residue 302 type MOD_RES sequence K description Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 34) chain L residue 319 type MOD_RES sequence K description Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 35) chain L residue 326 type MOD_RES sequence K description Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 36) chain H residue 162 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 37) chain M residue 214 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 38) chain M residue 265 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 39) chain M residue 275 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 40) chain M residue 279 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 41) chain M residue 392 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 42) chain H residue 213 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 43) chain H residue 269 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 44) chain H residue 317 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 45) chain P residue 162 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 46) chain P residue 213 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 47) chain P residue 269 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 48) chain P residue 317 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 49) chain H residue 318 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 50) chain H residue 400 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 51) chain H residue 466 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 52) chain P residue 318 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 53) chain P residue 400 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 54) chain P residue 466 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 55) chain H residue 505 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI5 56) chain P residue 505 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI5 57) chain J residue 248 type MOD_RES sequence K description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI5 58) chain D residue 98-106 type prosite sequence QDIEAGDGT description TCP1_3 Chaperonins TCP-1 signature 3. QDieAGDGT source prosite : PS00995 59) chain C residue 87-95 type prosite sequence QDEEVGDGT description TCP1_3 Chaperonins TCP-1 signature 3. QDieAGDGT source prosite : PS00995 60) chain H residue 93-101 type prosite sequence QEQEVGDGT description TCP1_3 Chaperonins TCP-1 signature 3. QDieAGDGT source prosite : PS00995 61) chain B residue 91-99 type prosite sequence QDDEVGDGT description TCP1_3 Chaperonins TCP-1 signature 3. QDieAGDGT source prosite : PS00995 62) chain A residue 82-90 type prosite sequence QDKEVGDGT description TCP1_3 Chaperonins TCP-1 signature 3. QDieAGDGT source prosite : PS00995 63) chain E residue 98-106 type prosite sequence QDDEIGDGT description TCP1_3 Chaperonins TCP-1 signature 3. QDieAGDGT source prosite : PS00995 64) chain F residue 84-92 type prosite sequence QDDITGDGT description TCP1_3 Chaperonins TCP-1 signature 3. QDieAGDGT source prosite : PS00995 65) chain G residue 86-94 type prosite sequence QDAEVGDGT description TCP1_3 Chaperonins TCP-1 signature 3. QDieAGDGT source prosite : PS00995 66) chain D residue 49-61 type prosite sequence RTSLGPKGMDKMI description TCP1_1 Chaperonins TCP-1 signature 1. RTsLGPkGmdKMI source prosite : PS00750 67) chain C residue 38-50 type prosite sequence RTCLGPKSMMKML description TCP1_1 Chaperonins TCP-1 signature 1. RTsLGPkGmdKMI source prosite : PS00750 68) chain H residue 44-56 type prosite sequence RTAYGPNGMNKMV description TCP1_1 Chaperonins TCP-1 signature 1. RTsLGPkGmdKMI source prosite : PS00750 69) chain B residue 40-52 type prosite sequence KSTLGPKGMDKIL description TCP1_1 Chaperonins TCP-1 signature 1. RTsLGPkGmdKMI source prosite : PS00750 70) chain A residue 33-45 type prosite sequence KSSLGPVGLDKML description TCP1_1 Chaperonins TCP-1 signature 1. RTsLGPkGmdKMI source prosite : PS00750 71) chain E residue 49-61 type prosite sequence RTSLGPNGLDKMM description TCP1_1 Chaperonins TCP-1 signature 1. RTsLGPkGmdKMI source prosite : PS00750 72) chain F residue 35-47 type prosite sequence RTNLGPKGTMKML description TCP1_1 Chaperonins TCP-1 signature 1. RTsLGPkGmdKMI source prosite : PS00750 73) chain G residue 37-49 type prosite sequence RTTLGPRGMDKLI description TCP1_1 Chaperonins TCP-1 signature 1. RTsLGPkGmdKMI source prosite : PS00750 74) chain D residue 70-86 type prosite sequence ITNDGATILKQMQVLHP description TCP1_2 Chaperonins TCP-1 signature 2. ITNDGATILkqMqVlHP source prosite : PS00751 75) chain C residue 59-75 type prosite sequence MTNDGNAILREIQVQHP description TCP1_2 Chaperonins TCP-1 signature 2. ITNDGATILkqMqVlHP source prosite : PS00751 76) chain H residue 65-81 type prosite sequence VTNDAATILRELEVQHP description TCP1_2 Chaperonins TCP-1 signature 2. ITNDGATILkqMqVlHP source prosite : PS00751 77) chain B residue 63-79 type prosite sequence VTNDGATILKNIGVDNP description TCP1_2 Chaperonins TCP-1 signature 2. ITNDGATILkqMqVlHP source prosite : PS00751 78) chain A residue 54-70 type prosite sequence ITNDGATILKLLEVEHP description TCP1_2 Chaperonins TCP-1 signature 2. ITNDGATILkqMqVlHP source prosite : PS00751 79) chain E residue 70-86 type prosite sequence VTNDGATILSMMDVDHQ description TCP1_2 Chaperonins TCP-1 signature 2. ITNDGATILkqMqVlHP source prosite : PS00751 80) chain F residue 56-72 type prosite sequence LTKDGNVLLHEMQIQHP description TCP1_2 Chaperonins TCP-1 signature 2. ITNDGATILkqMqVlHP source prosite : PS00751 81) chain G residue 58-74 type prosite sequence ISNDGATILKLLDVVHP description TCP1_2 Chaperonins TCP-1 signature 2. ITNDGATILkqMqVlHP source prosite : PS00751

Display surface Download Links