eF-site ID 3oj3-ABCDEFGHIJKLMNOP PDB Code 3oj3 Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P click to enlarge Title Crystal structure of the A20 ZnF4 and ubiquitin complex Classification PROTEIN BINDING/HYDROLASE Compound Ubiquitin Source (TNAP3_HUMAN) Sequence A:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRL B:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLR C:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRL D:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRL E:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRL F:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRL G:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVL H:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVL I:  GTSKCRKAGCVYFGTPENKGFCTLCFIEYRENK J:  SKCRKAGCVYFGTPENKGFCTLCFIEYREN K:  SKCRKAGCVYFGTPENKGFCTLCFIEYRENK L:  SKCRKAGCVYFGTPENKGFCTLCFIEYRENK M:  SKCRKAGCVYFGTPENKGFCTLCFIEYRENK N:  SKCRKAGCVYFGTPENKGFCTLCFIEYREN O:  TSKCRKAGCVYFGTPENKGFCTLCFIEYRENK P:  SKCRKAGCVYFGTPENKGFCTLCFIEYRENK Description Functional site 1) chain I residue 607 type sequence C description BINDING SITE FOR RESIDUE ZN I 901 source : AC1 2) chain I residue 612 type sequence C description BINDING SITE FOR RESIDUE ZN I 901 source : AC1 3) chain I residue 624 type sequence C description BINDING SITE FOR RESIDUE ZN I 901 source : AC1 4) chain I residue 627 type sequence C description BINDING SITE FOR RESIDUE ZN I 901 source : AC1 5) chain J residue 607 type sequence C description BINDING SITE FOR RESIDUE ZN J 902 source : AC2 6) chain J residue 612 type sequence C description BINDING SITE FOR RESIDUE ZN J 902 source : AC2 7) chain J residue 624 type sequence C description BINDING SITE FOR RESIDUE ZN J 902 source : AC2 8) chain J residue 627 type sequence C description BINDING SITE FOR RESIDUE ZN J 902 source : AC2 9) chain K residue 607 type sequence C description BINDING SITE FOR RESIDUE ZN K 903 source : AC3 10) chain K residue 612 type sequence C description BINDING SITE FOR RESIDUE ZN K 903 source : AC3 11) chain K residue 624 type sequence C description BINDING SITE FOR RESIDUE ZN K 903 source : AC3 12) chain K residue 627 type sequence C description BINDING SITE FOR RESIDUE ZN K 903 source : AC3 13) chain L residue 607 type sequence C description BINDING SITE FOR RESIDUE ZN L 904 source : AC4 14) chain L residue 612 type sequence C description BINDING SITE FOR RESIDUE ZN L 904 source : AC4 15) chain L residue 624 type sequence C description BINDING SITE FOR RESIDUE ZN L 904 source : AC4 16) chain L residue 627 type sequence C description BINDING SITE FOR RESIDUE ZN L 904 source : AC4 17) chain M residue 607 type sequence C description BINDING SITE FOR RESIDUE ZN M 905 source : AC5 18) chain M residue 612 type sequence C description BINDING SITE FOR RESIDUE ZN M 905 source : AC5 19) chain M residue 624 type sequence C description BINDING SITE FOR RESIDUE ZN M 905 source : AC5 20) chain M residue 627 type sequence C description BINDING SITE FOR RESIDUE ZN M 905 source : AC5 21) chain N residue 607 type sequence C description BINDING SITE FOR RESIDUE ZN N 906 source : AC6 22) chain N residue 612 type sequence C description BINDING SITE FOR RESIDUE ZN N 906 source : AC6 23) chain N residue 624 type sequence C description BINDING SITE FOR RESIDUE ZN N 906 source : AC6 24) chain N residue 627 type sequence C description BINDING SITE FOR RESIDUE ZN N 906 source : AC6 25) chain O residue 607 type sequence C description BINDING SITE FOR RESIDUE ZN O 907 source : AC7 26) chain O residue 612 type sequence C description BINDING SITE FOR RESIDUE ZN O 907 source : AC7 27) chain O residue 624 type sequence C description BINDING SITE FOR RESIDUE ZN O 907 source : AC7 28) chain O residue 627 type sequence C description BINDING SITE FOR RESIDUE ZN O 907 source : AC7 29) chain P residue 607 type sequence C description BINDING SITE FOR RESIDUE ZN P 908 source : AC8 30) chain P residue 612 type sequence C description BINDING SITE FOR RESIDUE ZN P 908 source : AC8 31) chain P residue 624 type sequence C description BINDING SITE FOR RESIDUE ZN P 908 source : AC8 32) chain P residue 627 type sequence C description BINDING SITE FOR RESIDUE ZN P 908 source : AC8 33) chain A residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 34) chain B residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 35) chain C residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 36) chain D residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 37) chain E residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 38) chain F residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 39) chain G residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 40) chain H residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 41) 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 42) 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 43) 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 44) 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 45) 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 46) 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 47) 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 48) 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 49) chain A residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 50) chain B residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 51) chain C residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 52) chain D residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 53) chain E residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 54) chain F residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 55) chain G residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 56) chain H residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 57) 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 58) 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 59) 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 60) 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 61) 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 62) 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 63) 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 64) 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 65) 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 66) 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 67) 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 68) 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 69) 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 70) 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 71) 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 72) 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 73) 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 74) 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 75) 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 76) 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 77) 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 78) 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 79) 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 80) 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 81) 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 82) 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 83) 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 84) 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 85) 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 86) 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 87) 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 88) 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 89) 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 90) 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 91) 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 92) 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 93) 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 94) 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 95) 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 96) 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 97) 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 98) 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 99) 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 100) 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 101) 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 102) 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 103) 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 104) 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 105) 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 106) 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 107) 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 108) 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 109) 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 110) 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 111) 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 112) 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 113) chain A residue 27-52 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299 114) chain I residue 607 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 115) chain K residue 612 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 116) chain K residue 624 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 117) chain K residue 627 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 118) chain L residue 607 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 119) chain L residue 612 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 120) chain L residue 624 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 121) chain L residue 627 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 122) chain M residue 607 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 123) chain M residue 612 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 124) chain M residue 624 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 125) chain I residue 612 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 126) chain M residue 627 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 127) chain N residue 607 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 128) chain N residue 612 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 129) chain N residue 624 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 130) chain N residue 627 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 131) chain O residue 607 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 132) chain O residue 612 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 133) chain O residue 624 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 134) chain O residue 627 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 135) chain P residue 607 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 136) chain I residue 624 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 137) chain P residue 612 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 138) chain P residue 624 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 139) chain P residue 627 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 140) chain I residue 627 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 141) chain J residue 607 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 142) chain J residue 612 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 143) chain J residue 624 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 144) chain J residue 627 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 145) chain K residue 607 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1

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