eF-site ID 3nob-ABCDEFGH PDB Code 3nob Chain A, B, C, D, E, F, G, H click to enlarge Title Structure of K11-linked di-ubiquitin Classification PROTEIN BINDING Compound Ubiquitin Source (UBIQ_HUMAN) Sequence A:  SHMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPP DQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRG B:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLR C:  HMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPD QQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLR D:  HMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPD QQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLR E:  HMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPD QQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLR F:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG G:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRG H:  HMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPD QQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG Description Functional site 1) chain A residue 39 type sequence D description BINDING SITE FOR RESIDUE SO4 A 77 source : AC1 2) chain A residue 40 type sequence Q description BINDING SITE FOR RESIDUE SO4 A 77 source : AC1 3) chain A residue 74 type sequence R description BINDING SITE FOR RESIDUE SO4 A 77 source : AC1 4) chain B residue 35 type sequence G description BINDING SITE FOR RESIDUE SO4 A 77 source : AC1 5) chain E residue 35 type sequence G description BINDING SITE FOR RESIDUE SO4 A 77 source : AC1 6) chain F residue 39 type sequence D description BINDING SITE FOR RESIDUE SO4 A 77 source : AC1 7) chain F residue 40 type sequence Q description BINDING SITE FOR RESIDUE SO4 A 77 source : AC1 8) chain F residue 74 type sequence R description BINDING SITE FOR RESIDUE SO4 A 77 source : AC1 9) chain A residue 44 type sequence I description BINDING SITE FOR RESIDUE SO4 A 78 source : AC2 10) chain A residue 45 type sequence F description BINDING SITE FOR RESIDUE SO4 A 78 source : AC2 11) chain A residue 46 type sequence A description BINDING SITE FOR RESIDUE SO4 A 78 source : AC2 12) chain A residue 47 type sequence G description BINDING SITE FOR RESIDUE SO4 A 78 source : AC2 13) chain A residue 68 type sequence H description BINDING SITE FOR RESIDUE SO4 A 78 source : AC2 14) chain C residue 68 type sequence H description BINDING SITE FOR RESIDUE SO4 A 78 source : AC2 15) chain A residue 35 type sequence G description BINDING SITE FOR RESIDUE SO4 B 77 source : AC3 16) chain B residue 39 type sequence D description BINDING SITE FOR RESIDUE SO4 B 77 source : AC3 17) chain B residue 40 type sequence Q description BINDING SITE FOR RESIDUE SO4 B 77 source : AC3 18) chain B residue 74 type sequence R description BINDING SITE FOR RESIDUE SO4 B 77 source : AC3 19) chain E residue 39 type sequence D description BINDING SITE FOR RESIDUE SO4 B 77 source : AC3 20) chain E residue 40 type sequence Q description BINDING SITE FOR RESIDUE SO4 B 77 source : AC3 21) chain F residue 35 type sequence G description BINDING SITE FOR RESIDUE SO4 B 77 source : AC3 22) chain B residue 63 type sequence K description BINDING SITE FOR RESIDUE SO4 B 78 source : AC4 23) chain D residue 6 type sequence K description BINDING SITE FOR RESIDUE SO4 B 78 source : AC4 24) chain D residue 68 type sequence H description BINDING SITE FOR RESIDUE SO4 B 78 source : AC4 25) chain D residue 27 type sequence K description BINDING SITE FOR RESIDUE SO4 D 77 source : AC5 26) chain D residue 51 type sequence E description BINDING SITE FOR RESIDUE SO4 D 77 source : AC5 27) chain D residue 52 type sequence D description BINDING SITE FOR RESIDUE SO4 D 77 source : AC5 28) chain A residue 53 type sequence G description BINDING SITE FOR RESIDUE SO4 E 77 source : AC6 29) chain E residue 14 type sequence T description BINDING SITE FOR RESIDUE SO4 E 77 source : AC6 30) chain E residue 15 type sequence L description BINDING SITE FOR RESIDUE SO4 E 77 source : AC6 31) chain E residue 16 type sequence E description BINDING SITE FOR RESIDUE SO4 E 77 source : AC6 32) chain H residue 27 type sequence K description BINDING SITE FOR RESIDUE SO4 H 77 source : AC7 33) chain H residue 41 type sequence Q description BINDING SITE FOR RESIDUE SO4 H 77 source : AC7 34) chain H residue 42 type sequence R description BINDING SITE FOR RESIDUE SO4 H 77 source : AC7 35) chain H residue 49 type sequence Q description BINDING SITE FOR RESIDUE SO4 H 77 source : AC7 36) chain H residue 72 type sequence R description BINDING SITE FOR RESIDUE SO4 H 77 source : AC7 37) chain A residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 38) chain A residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 39) chain B residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 40) chain B residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 41) chain C residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 42) chain C residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 43) chain D residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 44) chain D residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 45) chain E residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 46) chain E residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 47) chain F residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 48) chain F residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 49) chain G residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 50) chain G residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 51) chain H residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 52) chain H residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 53) chain A residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 54) chain B residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 55) chain C residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 56) chain D residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 57) chain E residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 58) chain F residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 59) chain G residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 60) chain H residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 61) chain A residue 65 type MOD_RES sequence S description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 62) chain B residue 65 type MOD_RES sequence S description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 63) chain C residue 65 type MOD_RES sequence S description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 64) chain D residue 65 type MOD_RES sequence S description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 65) chain E residue 65 type MOD_RES sequence S description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 66) chain F residue 65 type MOD_RES sequence S description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 67) chain G residue 65 type MOD_RES sequence S description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 68) chain H residue 65 type MOD_RES sequence S description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 69) chain A residue 63 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106 source Swiss-Prot : SWS_FT_FI12 70) chain B residue 63 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106 source Swiss-Prot : SWS_FT_FI12 71) chain C residue 63 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106 source Swiss-Prot : SWS_FT_FI12 72) chain D residue 63 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106 source Swiss-Prot : SWS_FT_FI12 73) chain E residue 63 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106 source Swiss-Prot : SWS_FT_FI12 74) chain F residue 63 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106 source Swiss-Prot : SWS_FT_FI12 75) chain G residue 63 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106 source Swiss-Prot : SWS_FT_FI12 76) chain H residue 63 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106 source Swiss-Prot : SWS_FT_FI12 77) chain A residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 78) chain B residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 79) chain C residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 80) chain D residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 81) chain E residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 82) chain F residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 83) chain G residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 84) chain H residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 85) chain F residue 76 type MOD_RES sequence G description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI5 86) chain H residue 76 type MOD_RES sequence G description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI5 87) chain A residue 6 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603 source Swiss-Prot : SWS_FT_FI6 88) chain C residue 6 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603 source Swiss-Prot : SWS_FT_FI6 89) chain E residue 6 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603 source Swiss-Prot : SWS_FT_FI6 90) chain G residue 6 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603 source Swiss-Prot : SWS_FT_FI6 91) chain B residue 6 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603 source Swiss-Prot : SWS_FT_FI6 92) chain D residue 6 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603 source Swiss-Prot : SWS_FT_FI6 93) chain F residue 6 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603 source Swiss-Prot : SWS_FT_FI6 94) chain H residue 6 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603 source Swiss-Prot : SWS_FT_FI6 95) chain F residue 76 type CROSSLNK sequence G description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI7 96) chain H residue 76 type CROSSLNK sequence G description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI7 97) chain E residue 48 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI8 98) chain F residue 11 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI8 99) chain F residue 48 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI8 100) chain G residue 11 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI8 101) chain G residue 48 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI8 102) chain H residue 11 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI8 103) chain H residue 48 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI8 104) chain E residue 11 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI8 105) chain A residue 11 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI8 106) chain A residue 48 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI8 107) chain B residue 11 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI8 108) chain B residue 48 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI8 109) chain C residue 11 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI8 110) chain C residue 48 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI8 111) chain D residue 11 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI8 112) chain D residue 48 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI8 113) chain A residue 27-52 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299 114) chain B residue 33 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577 source Swiss-Prot : SWS_FT_FI11 115) chain C residue 33 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577 source Swiss-Prot : SWS_FT_FI11 116) chain D residue 33 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577 source Swiss-Prot : SWS_FT_FI11 117) chain E residue 33 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577 source Swiss-Prot : SWS_FT_FI11 118) chain F residue 33 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577 source Swiss-Prot : SWS_FT_FI11 119) chain G residue 33 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577 source Swiss-Prot : SWS_FT_FI11 120) chain H residue 33 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577 source Swiss-Prot : SWS_FT_FI11 121) chain A residue 33 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577 source Swiss-Prot : SWS_FT_FI11 122) chain B residue 29 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127 source Swiss-Prot : SWS_FT_FI10 123) chain C residue 29 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127 source Swiss-Prot : SWS_FT_FI10 124) chain D residue 29 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127 source Swiss-Prot : SWS_FT_FI10 125) chain E residue 29 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127 source Swiss-Prot : SWS_FT_FI10 126) chain F residue 29 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127 source Swiss-Prot : SWS_FT_FI10 127) chain G residue 29 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127 source Swiss-Prot : SWS_FT_FI10 128) chain H residue 29 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127 source Swiss-Prot : SWS_FT_FI10 129) chain A residue 29 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127 source Swiss-Prot : SWS_FT_FI10 130) chain A residue 27 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860 source Swiss-Prot : SWS_FT_FI9 131) chain B residue 27 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860 source Swiss-Prot : SWS_FT_FI9 132) chain C residue 27 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860 source Swiss-Prot : SWS_FT_FI9 133) chain D residue 27 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860 source Swiss-Prot : SWS_FT_FI9 134) chain E residue 27 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860 source Swiss-Prot : SWS_FT_FI9 135) chain F residue 27 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860 source Swiss-Prot : SWS_FT_FI9 136) chain G residue 27 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860 source Swiss-Prot : SWS_FT_FI9 137) chain H residue 27 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860 source Swiss-Prot : SWS_FT_FI9

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