eF-site ID 2wx0-ABCEFG PDB Code 2wx0 Chain A, B, C, E, F, G click to enlarge Title TAB2 NZF DOMAIN IN COMPLEX WITH Lys63-linked di-ubiquitin, P21 Classification PROTEIN BINDING Compound UBIQUITIN Source Homo sapiens (Human) (TAB2_HUMAN) Sequence A:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLR B:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRL C:  DEGAQWNCTACTFLNHPALIRCEQCEMPRHF E:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLR F:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRL G:  EGAQWNCTACTFLNHPALIRCEQCEMPRHF Description (1)  UBIQUITIN, MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 7-INTERACTING PROTEIN 2 Functional site 1) chain C residue 670 type sequence C description BINDING SITE FOR RESIDUE ZN C 1694 source : AC1 2) chain C residue 673 type sequence C description BINDING SITE FOR RESIDUE ZN C 1694 source : AC1 3) chain C residue 684 type sequence C description BINDING SITE FOR RESIDUE ZN C 1694 source : AC1 4) chain C residue 687 type sequence C description BINDING SITE FOR RESIDUE ZN C 1694 source : AC1 5) chain G residue 670 type sequence C description BINDING SITE FOR RESIDUE ZN G 1694 source : AC2 6) chain G residue 673 type sequence C description BINDING SITE FOR RESIDUE ZN G 1694 source : AC2 7) chain G residue 684 type sequence C description BINDING SITE FOR RESIDUE ZN G 1694 source : AC2 8) chain G residue 687 type sequence C description BINDING SITE FOR RESIDUE ZN G 1694 source : AC2 9) chain A residue 65 type MOD_RES sequence S description Phosphoserine; by PINK1 => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI3 10) chain B residue 65 type MOD_RES sequence S description Phosphoserine; by PINK1 => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI3 11) chain E residue 65 type MOD_RES sequence S description Phosphoserine; by PINK1 => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI3 12) chain F residue 65 type MOD_RES sequence S description Phosphoserine; by PINK1 => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI3 13) chain A residue 6 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 14) chain B residue 27 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 15) chain B residue 29 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 16) chain B residue 33 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 17) chain B residue 48 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 18) chain B residue 63 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 19) chain E residue 6 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 20) chain E residue 11 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 21) chain E residue 27 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 22) chain E residue 29 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 23) chain E residue 33 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 24) chain A residue 11 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 25) chain E residue 48 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 26) chain E residue 63 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 27) chain F residue 6 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 28) chain F residue 11 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 29) chain F residue 27 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 30) chain F residue 29 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 31) chain F residue 33 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 32) chain F residue 48 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 33) chain F residue 63 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 34) chain A residue 27 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 35) chain A residue 29 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 36) chain A residue 33 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 37) chain A residue 48 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 38) chain A residue 63 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 39) chain B residue 6 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 40) chain B residue 11 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 41) chain C residue 668-687 type prosite sequence WNCTACTFLNHPALIRCEQC description ZF_RANBP2_1 Zinc finger RanBP2-type signature. WnCta..CtflNhpalirCeqC source prosite : PS01358 42) chain A residue 27-52 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299 43) chain C residue 663-693 type ZN_FING sequence DEGAQWNCTACTFLNHPALIRCEQCEMPRHF description RanBP2-type => ECO:0000255|PROSITE-ProRule:PRU00322 source Swiss-Prot : SWS_FT_FI1 44) chain B residue 54 type ZN_FING sequence R description RanBP2-type => ECO:0000255|PROSITE-ProRule:PRU00322 source Swiss-Prot : SWS_FT_FI1 45) chain B residue 72 type ZN_FING sequence R description RanBP2-type => ECO:0000255|PROSITE-ProRule:PRU00322 source Swiss-Prot : SWS_FT_FI1 46) chain E residue 54 type ZN_FING sequence R description RanBP2-type => ECO:0000255|PROSITE-ProRule:PRU00322 source Swiss-Prot : SWS_FT_FI1 47) chain E residue 72 type ZN_FING sequence R description RanBP2-type => ECO:0000255|PROSITE-ProRule:PRU00322 source Swiss-Prot : SWS_FT_FI1 48) chain F residue 54 type ZN_FING sequence R description RanBP2-type => ECO:0000255|PROSITE-ProRule:PRU00322 source Swiss-Prot : SWS_FT_FI1 49) chain F residue 72 type ZN_FING sequence R description RanBP2-type => ECO:0000255|PROSITE-ProRule:PRU00322 source Swiss-Prot : SWS_FT_FI1 50) chain C residue 673 type MOD_RES sequence C description (Microbial infection) S-methylcysteine => ECO:0000269|PubMed:22158122, ECO:0000269|PubMed:25412445 source Swiss-Prot : SWS_FT_FI2 51) chain G residue 673 type MOD_RES sequence C description (Microbial infection) S-methylcysteine => ECO:0000269|PubMed:22158122, ECO:0000269|PubMed:25412445 source Swiss-Prot : SWS_FT_FI2 52) chain E residue 68 type MOD_RES sequence H description (Microbial infection) S-methylcysteine => ECO:0000269|PubMed:22158122, ECO:0000269|PubMed:25412445 source Swiss-Prot : SWS_FT_FI2 53) chain F residue 68 type MOD_RES sequence H description (Microbial infection) S-methylcysteine => ECO:0000269|PubMed:22158122, ECO:0000269|PubMed:25412445 source Swiss-Prot : SWS_FT_FI2

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