eF-site ID 5l6h-ABCDE PDB Code 5l6h Chain A, B, C, D, E click to enlarge Title Uba1 in complex with Ub-ABPA3 covalent adduct Classification LIGASE Compound Ubiquitin-activating enzyme E1 1 Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (RS27A_YEAST) Sequence A:  AAGEIDESLYSRQLYVLGKEAMLKMQTSNVLILGLKGLGV EIAKNVVLAGVKSMTVFDPEPVQLADLSTQFFLTEKDIGQ KRGDVTRAKLAELNAYVPVNVLDSLDDVTQLSQFQVVVAT DTVSLEDKVKINEFCHSSGIRFISSETRGLFGNTFVDLGD EFTVLDPTGEEPRTGMVSDIEPDGTVTMLDDNRHGLEDGN FVRFSEVEGLDKLNDGTLFKVEVLGPFAFRIGSVKEYGEY KKGGIFTEVKVPRKISFKSLKQQLSNPEFVFSDFAKFDRA AQLHLGFQALHQFAVRHNGELPRTMNDEDANELIKLVTDL SVQQPEVLGEGVDVNEDLIKELSYQARGDIPGVVAFFGGL VAQEVLKACSGKFTPLKQFMYFDSLESLPDPKNFPRNEKT TQPVNSRYDNQIAVFGLDFQKKIANSKVFLVGSGAIGCEM LKNWALLGLGSGSDGYIVVTDNDSIEKSNLNRQFLFRPKD VGKNKSEVAAEAVCAMNPDLKGKINAKIDKVGPETEEIFN DSFWESLDFVTNALDNVDARTYVDRRCVFYRKPLLESGTL GTKGNTQVIIPRLTESYSSSRDPPEKSIPLCTLRSFPNKI DHTIAWAKSLFQGYFTDSAENVNMYLTQPNFVEQTLKQSG DVKGVLESISDSLSSKPHNFEDCIKWARLEFEKKFNHDIK QLLFNFPKDAKTSNGEPFWSGAKRAPTPLEFDIYNNDHFH FVVAGASLRAYNYGIKSDDSNSKPNVDEYKSVIDHMIIPE FTPNANLKIQVNDDDPDDEIDQLVSSLPDPSTLAGFKLEP VDFEKDDDTNHHIEFITACSNCRAQNYFIETADRQKTKFI AGRIIPAIATTTSLVTGLVNLELYKLIDNKTDIEQYKNGF VNLALPFFGFSEPIASPKGEYNNKKYDKIWDRFDIKGDIK LSDLIEHFEKDEGLEITMLSYGVSLLYASFFPPKKLKERL NLPITQLVKLVTKKDIPAHVSTMILEIXADDKEGEDVEVP FITIHL B:  MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG C:  AGEIDESLYSRQLYVLGKEAMLKMQTSNVLILGLKGLGVE IAKNVVLAGVKSMTVFDPEPVQLADLSTQFFLTEKDIGQK RGDVTRAKLAELNAYVPVNVLDSLDDVTQLSQFQVVVATD TVSLEDKVKINEFCHSSGIRFISSETRGLFGNTFVDLGDE FTVLDPTGEEPRTGMVSDIEPDGTVTMLDDNRHGLEDGNF VRFSEVEGLDKLNDGTLFKVEVLGPFAFRIGSVKEYGEYK KGGIFTEVKVPRKISFKSLKQQLSNPEFVFSDFAKFDRAA QLHLGFQALHQFAVRHNGELPRTMNDEDANELIKLVTDLS VQQPEVLGEGVDVNEDLIKELSYQARGDIPGVVAFFGGLV AQEVLKACSGKFTPLKQFMYFDSLESLPDPKNFPRNEKTT QPVNSRYDNQIAVFGLDFQKKIANSKVFLVGSGAIGCEML KNWALLGLGSGSDGYIVVTDNDSIEKSNLNRQFLFRPKDV GKNKSEVAAEAVCAMNPDLKGKINAKIDKVGPETEEIFND SFWESLDFVTNALDNVDARTYVDRRCVFYRKPLLESGTLG TKGNTQVIIPRLTESYSSSRDPPEKSIPLCTLRSFPNKID HTIAWAKSLFQGYFTDSAENVNMYLTQPNFVEQTLKQSGD VKGVLESISDSLSSKPHNFEDCIKWARLEFEKKFNHDIKQ LLFNFPKDAKTSNGEPFWSGAKRAPTPLEFDIYNNDHFHF VVAGASLRAYNYGIKSDDSNSKPNVDEYKSVIDHMIIPEF TPNANLKIQVNDDDPDDEIDQLVSSLPDPSTLAGFKLEPV DFEKDDDTNHHIEFITACSNCRAQNYFIETADRQKTKFIA GRIIPAIATTTSLVTGLVNLELYKLIDNKTDIEQYKNGFV NLALPFFGFSEPIASPKGEYNNKKYDKIWDRFDIKGDIKL SDLIEHFEKDEGLEITMLSYGVSLLYASFFPPKKLKERLN LPITQLVKLVTKKDIPAHVSTMILEIXADDKEGEDVEVPF ITIHL D:  MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG E:  MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLR Description Functional site 1) chain A residue 21 type sequence R description binding site for residue SO4 A 1101 source : AC1 2) chain A residue 478 type sequence N description binding site for residue SO4 A 1101 source : AC1 3) chain A residue 481 type sequence R description binding site for residue SO4 A 1101 source : AC1 4) chain A residue 571 type sequence T description binding site for residue CL A 1102 source : AC2 5) chain A residue 572 type sequence K description binding site for residue CL A 1102 source : AC2 6) chain A residue 861 type sequence R description binding site for residue CL A 1103 source : AC3 7) chain B residue 74 type sequence R description binding site for residue CL A 1103 source : AC3 8) chain A residue 96 type sequence R description binding site for residue CL A 1104 source : AC4 9) chain A residue 117 type sequence V description binding site for residue CL A 1105 source : AC5 10) chain A residue 282 type sequence D description binding site for residue GOL A 1106 source : AC6 11) chain A residue 285 type sequence K description binding site for residue GOL A 1106 source : AC6 12) chain A residue 391 type sequence F description binding site for residue GOL A 1106 source : AC6 13) chain A residue 392 type sequence D description binding site for residue GOL A 1106 source : AC6 14) chain A residue 393 type sequence S description binding site for residue GOL A 1106 source : AC6 15) chain A residue 395 type sequence E description binding site for residue GOL A 1106 source : AC6 16) chain A residue 908 type sequence F description binding site for residue GOL A 1106 source : AC6 17) chain A residue 288 type sequence R description binding site for residue GOL A 1107 source : AC7 18) chain A residue 344 type sequence N description binding site for residue GOL A 1107 source : AC7 19) chain A residue 394 type sequence L description binding site for residue GOL A 1107 source : AC7 20) chain A residue 137 type sequence K description binding site for residue GOL A 1108 source : AC8 21) chain A residue 153 type sequence S description binding site for residue GOL A 1108 source : AC8 22) chain A residue 155 type sequence E description binding site for residue GOL A 1108 source : AC8 23) chain A residue 162 type sequence N description binding site for residue GOL A 1108 source : AC8 24) chain A residue 811 type sequence L description binding site for residue GOL A 1109 source : AC9 25) chain A residue 813 type sequence G description binding site for residue GOL A 1109 source : AC9 26) chain A residue 814 type sequence F description binding site for residue GOL A 1109 source : AC9 27) chain A residue 819 type sequence V description binding site for residue GOL A 1110 source : AD1 28) chain A residue 828 type sequence N description binding site for residue GOL A 1110 source : AD1 29) chain A residue 830 type sequence H description binding site for residue GOL A 1110 source : AD1 30) chain A residue 713 type sequence R description binding site for residue GOL A 1111 source : AD2 31) chain A residue 24 type sequence Y description binding site for residue GOL A 1112 source : AD3 32) chain A residue 854 type sequence K description binding site for residue GOL A 1112 source : AD3 33) chain A residue 443 type sequence G description binding site for residue 6O2 B 101 source : AD4 34) chain A residue 444 type sequence A description binding site for residue 6O2 B 101 source : AD4 35) chain A residue 470 type sequence D description binding site for residue 6O2 B 101 source : AD4 36) chain A residue 472 type sequence D description binding site for residue 6O2 B 101 source : AD4 37) chain A residue 481 type sequence R description binding site for residue 6O2 B 101 source : AD4 38) chain A residue 482 type sequence Q description binding site for residue 6O2 B 101 source : AD4 39) chain A residue 494 type sequence K description binding site for residue 6O2 B 101 source : AD4 40) chain A residue 520 type sequence V description binding site for residue 6O2 B 101 source : AD4 41) chain A residue 542 type sequence A description binding site for residue 6O2 B 101 source : AD4 42) chain A residue 543 type sequence L description binding site for residue 6O2 B 101 source : AD4 43) chain A residue 544 type sequence D description binding site for residue 6O2 B 101 source : AD4 44) chain A residue 545 type sequence N description binding site for residue 6O2 B 101 source : AD4 45) chain A residue 548 type sequence A description binding site for residue 6O2 B 101 source : AD4 46) chain B residue 76 type sequence G description binding site for residue 6O2 B 101 source : AD4 47) chain C residue 21 type sequence R description binding site for residue SO4 C 1101 source : AD5 48) chain C residue 478 type sequence N description binding site for residue SO4 C 1101 source : AD5 49) chain C residue 481 type sequence R description binding site for residue SO4 C 1101 source : AD5 50) chain C residue 571 type sequence T description binding site for residue CL C 1102 source : AD6 51) chain C residue 514 type sequence N description binding site for residue CL C 1103 source : AD7 52) chain C residue 861 type sequence R description binding site for residue CL C 1104 source : AD8 53) chain D residue 74 type sequence R description binding site for residue CL C 1104 source : AD8 54) chain A residue 944 type sequence E description binding site for residue MG C 1106 source : AD9 55) chain C residue 1008 type sequence D description binding site for residue MG C 1106 source : AD9 56) chain C residue 713 type sequence R description binding site for residue GOL C 1107 source : AE1 57) chain C residue 714 type sequence A description binding site for residue GOL C 1107 source : AE1 58) chain C residue 846 type sequence F description binding site for residue GOL C 1107 source : AE1 59) chain C residue 267 type sequence K description binding site for residue GOL C 1108 source : AE2 60) chain C residue 271 type sequence Q description binding site for residue GOL C 1108 source : AE2 61) chain C residue 274 type sequence S description binding site for residue GOL C 1108 source : AE2 62) chain C residue 275 type sequence N description binding site for residue GOL C 1108 source : AE2 63) chain C residue 282 type sequence D description binding site for residue GOL C 1109 source : AE3 64) chain C residue 285 type sequence K description binding site for residue GOL C 1109 source : AE3 65) chain C residue 391 type sequence F description binding site for residue GOL C 1109 source : AE3 66) chain C residue 392 type sequence D description binding site for residue GOL C 1109 source : AE3 67) chain C residue 393 type sequence S description binding site for residue GOL C 1109 source : AE3 68) chain C residue 395 type sequence E description binding site for residue GOL C 1109 source : AE3 69) chain C residue 895 type sequence K description binding site for residue GOL C 1109 source : AE3 70) chain C residue 908 type sequence F description binding site for residue GOL C 1109 source : AE3 71) chain C residue 288 type sequence R description binding site for residue GOL C 1110 source : AE4 72) chain C residue 344 type sequence N description binding site for residue GOL C 1110 source : AE4 73) chain C residue 114 type sequence L description binding site for residue ACT C 1111 source : AE5 74) chain C residue 117 type sequence V description binding site for residue ACT C 1111 source : AE5 75) chain C residue 136 type sequence D description binding site for residue ACT C 1111 source : AE5 76) chain C residue 443 type sequence G description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 77) chain C residue 444 type sequence A description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 78) chain C residue 445 type sequence I description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 79) chain C residue 470 type sequence D description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 80) chain C residue 471 type sequence N description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 81) chain C residue 472 type sequence D description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 82) chain C residue 481 type sequence R description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 83) chain C residue 482 type sequence Q description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 84) chain C residue 494 type sequence K description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 85) chain C residue 520 type sequence V description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 86) chain C residue 542 type sequence A description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 87) chain C residue 543 type sequence L description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 88) chain C residue 544 type sequence D description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 89) chain C residue 545 type sequence N description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 90) chain C residue 548 type sequence A description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 91) chain D residue 75 type sequence G description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 92) chain A residue 21 type catalytic sequence R description 307 source MCSA : MCSA1 93) chain A residue 481 type catalytic sequence R description 307 source MCSA : MCSA1 94) chain A residue 544 type catalytic sequence D description 307 source MCSA : MCSA1 95) chain A residue 600 type catalytic sequence C description 307 source MCSA : MCSA1 96) chain A residue 601 type catalytic sequence T description 307 source MCSA : MCSA1 97) chain A residue 603 type catalytic sequence R description 307 source MCSA : MCSA1 98) chain A residue 781 type catalytic sequence N description 307 source MCSA : MCSA1 99) chain A residue 782 type catalytic sequence D description 307 source MCSA : MCSA1 100) chain A residue 600 type catalytic sequence C description 939 source MCSA : MCSA2 101) chain A residue 601 type catalytic sequence T description 939 source MCSA : MCSA2 102) chain A residue 603 type catalytic sequence R description 939 source MCSA : MCSA2 103) chain A residue 781 type catalytic sequence N description 939 source MCSA : MCSA2 104) chain A residue 782 type catalytic sequence D description 939 source MCSA : MCSA2 105) chain C residue 21 type catalytic sequence R description 307 source MCSA : MCSA3 106) chain C residue 481 type catalytic sequence R description 307 source MCSA : MCSA3 107) chain C residue 544 type catalytic sequence D description 307 source MCSA : MCSA3 108) chain C residue 600 type catalytic sequence C description 307 source MCSA : MCSA3 109) chain C residue 601 type catalytic sequence T description 307 source MCSA : MCSA3 110) chain C residue 603 type catalytic sequence R description 307 source MCSA : MCSA3 111) chain C residue 781 type catalytic sequence N description 307 source MCSA : MCSA3 112) chain C residue 782 type catalytic sequence D description 307 source MCSA : MCSA3 113) chain C residue 600 type catalytic sequence C description 939 source MCSA : MCSA4 114) chain C residue 601 type catalytic sequence T description 939 source MCSA : MCSA4 115) chain C residue 603 type catalytic sequence R description 939 source MCSA : MCSA4 116) chain C residue 781 type catalytic sequence N description 939 source MCSA : MCSA4 117) chain C residue 782 type catalytic sequence D description 939 source MCSA : MCSA4 118) chain A residue 595 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI6 119) chain A residue 608 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI6 120) chain C residue 595 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI6 121) chain C residue 608 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI6 122) chain A residue 376-384 type prosite sequence KACSGKFTP description UBIQUITIN_ACTIVAT_1 Ubiquitin-activating enzyme signature 1. KACSGKFtP source prosite : PS00536 123) chain A residue 598-606 type prosite sequence PLCTLRSFP description UBIQUITIN_ACTIVAT_2 Ubiquitin-activating enzyme active site. PLCTLRsFP source prosite : PS00865 124) chain B residue 27-52 type prosite sequence KSKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KskIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299 125) chain B residue 6 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI1 126) chain D residue 27 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI1 127) chain D residue 29 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI1 128) chain D residue 33 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI1 129) chain D residue 48 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI1 130) chain D residue 63 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI1 131) chain E residue 6 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI1 132) chain E residue 11 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI1 133) chain E residue 27 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI1 134) chain E residue 29 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI1 135) chain E residue 33 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI1 136) chain B residue 11 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI1 137) chain E residue 48 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI1 138) chain E residue 63 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI1 139) chain B residue 27 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI1 140) chain B residue 29 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI1 141) chain B residue 33 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI1 142) chain B residue 48 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI1 143) chain B residue 63 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI1 144) chain D residue 6 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI1 145) chain D residue 11 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62979 source Swiss-Prot : SWS_FT_FI1 146) chain A residue 444 type CROSSLNK sequence A description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) => ECO:0000255|PROSITE-ProRule:PRU00214 source Swiss-Prot : SWS_FT_FI2 147) chain C residue 544 type CROSSLNK sequence D description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) => ECO:0000255|PROSITE-ProRule:PRU00214 source Swiss-Prot : SWS_FT_FI2 148) chain B residue 76 type CROSSLNK sequence G description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) => ECO:0000255|PROSITE-ProRule:PRU00214 source Swiss-Prot : SWS_FT_FI2 149) chain A residue 481 type CROSSLNK sequence R description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) => ECO:0000255|PROSITE-ProRule:PRU00214 source Swiss-Prot : SWS_FT_FI2 150) chain D residue 76 type CROSSLNK sequence G description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) => ECO:0000255|PROSITE-ProRule:PRU00214 source Swiss-Prot : SWS_FT_FI2 151) chain A residue 544 type CROSSLNK sequence D description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) => ECO:0000255|PROSITE-ProRule:PRU00214 source Swiss-Prot : SWS_FT_FI2 152) chain C residue 470 type CROSSLNK sequence D description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) => ECO:0000255|PROSITE-ProRule:PRU00214 source Swiss-Prot : SWS_FT_FI2 153) chain C residue 481 type CROSSLNK sequence R description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) => ECO:0000255|PROSITE-ProRule:PRU00214 source Swiss-Prot : SWS_FT_FI2 154) chain C residue 494 type CROSSLNK sequence K description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) => ECO:0000255|PROSITE-ProRule:PRU00214 source Swiss-Prot : SWS_FT_FI2 155) chain A residue 265 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17287358 source Swiss-Prot : SWS_FT_FI4 156) chain C residue 265 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17287358 source Swiss-Prot : SWS_FT_FI4 157) chain A residue 914 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI5 158) chain C residue 914 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI5

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