eF-site ID 1qja-ABQR PDB Code 1qja Chain A, B, Q, R click to enlarge Title 14-3-3 ZETA/PHOSPHOPEPTIDE COMPLEX (MODE 2) Classification KINASE INHIBITOR/PEPTIDE Compound 14-3-3 PROTEIN ZETA Source (1QJA) Sequence A:  MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEE RNLLSVAYKNVVGARRSSWRVVSSIEQMAREYREKIETEL RDICNDVLSLLEKFLIPNASQAESKVFYLKMKGDYYRYLA EVADKKGIVDQSQQAYQEAFEISKKEMQPTHPIRLGLALN FSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKD STLIMQLLRDNLTLWTS B:  MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEE RNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAR EYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLK MKGDYYRYLAEVAKKGIVDQSQQAYQEAFEISKKEMQPTH PIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELD TLSEESYKDSTLIMQLLRDNLTLWT Q:  RLYHXLPA R:  RLYHXLPA Description (1)  14-3-3 PROTEIN ZETA, PHOSPHOPEPTIDE Functional site 1) chain A residue 210 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P63102 source Swiss-Prot : SWS_FT_FI7 2) chain B residue 210 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P63102 source Swiss-Prot : SWS_FT_FI7 3) chain A residue 41-51 type prosite sequence RNLLSVAYKNV description 1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV source prosite : PS00796 4) chain A residue 211-230 type prosite sequence YKDSTLIMQLLRDNLTLWTS description 1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTS source prosite : PS00797 5) chain A residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0000269|Ref.8, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI2 6) chain B residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0000269|Ref.8, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI2 7) chain A residue 56 type SITE sequence R description Interaction with phosphoserine on interacting protein => ECO:0000250|UniProtKB:P63103 source Swiss-Prot : SWS_FT_FI1 8) chain A residue 127 type SITE sequence R description Interaction with phosphoserine on interacting protein => ECO:0000250|UniProtKB:P63103 source Swiss-Prot : SWS_FT_FI1 9) chain B residue 56 type SITE sequence R description Interaction with phosphoserine on interacting protein => ECO:0000250|UniProtKB:P63103 source Swiss-Prot : SWS_FT_FI1 10) chain B residue 127 type SITE sequence R description Interaction with phosphoserine on interacting protein => ECO:0000250|UniProtKB:P63103 source Swiss-Prot : SWS_FT_FI1 11) chain A residue 3 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 12) chain B residue 3 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 13) chain B residue 68 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 14) chain A residue 58 type MOD_RES sequence S description Phosphoserine; by PKA and PKB/AKT1 => ECO:0000269|PubMed:11956222, ECO:0000269|PubMed:12865427, ECO:0000269|PubMed:15883165, ECO:0000269|PubMed:16376338 source Swiss-Prot : SWS_FT_FI4 15) chain B residue 58 type MOD_RES sequence S description Phosphoserine; by PKA and PKB/AKT1 => ECO:0000269|PubMed:11956222, ECO:0000269|PubMed:12865427, ECO:0000269|PubMed:15883165, ECO:0000269|PubMed:16376338 source Swiss-Prot : SWS_FT_FI4 16) chain A residue 184 type MOD_RES sequence S description Phosphoserine; by MAPK8 => ECO:0000269|PubMed:15071501, ECO:0000269|PubMed:15696159 source Swiss-Prot : SWS_FT_FI5 17) chain B residue 184 type MOD_RES sequence S description Phosphoserine; by MAPK8 => ECO:0000269|PubMed:15071501, ECO:0000269|PubMed:15696159 source Swiss-Prot : SWS_FT_FI5 18) chain A residue 207 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI6 19) chain B residue 207 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI6

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