eF-site ID 6qah-A PDB Code 6qah Chain A click to enlarge Title ERK2 mini-fragment binding Classification SIGNALING PROTEIN Compound Mitogen-activated protein kinase 1 Source (MK01_HUMAN) Sequence A:  PEMVRGQVFDVGPRYTNLSYIGEGAGMVCSAYDNVNKVRV AIKKISPFEHQTYCQRTLREIKILLRFRHENIIGINDIIR APTIEQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLY QILRGLKYIHSANVLHRDLKPSNLLLNTTXDLKICDFGLA RVADPDHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDI WSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQED LNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLD KMLTFNPHKRIEVEQALAHPYLEQYYDPSDEPIAEAPFKF LPKEKLKELIFEETARFQPG Description (1)  Mitogen-activated protein kinase 1 (E.C.2.7.11.24) Functional site 1) chain A residue 191 type sequence R description binding site for residue SO4 A 401 source : AC1 2) chain A residue 194 type sequence R description binding site for residue SO4 A 401 source : AC1 3) chain A residue 233 type sequence Y description binding site for residue SO4 A 401 source : AC1 4) chain A residue 111 type sequence D description binding site for residue HVB A 402 source : AC2 5) chain A residue 153 type sequence S description binding site for residue HVB A 402 source : AC2 6) chain A residue 154 type sequence N description binding site for residue HVB A 402 source : AC2 7) chain A residue 156 type sequence L description binding site for residue HVB A 402 source : AC2 8) chain A residue 166 type sequence C description binding site for residue HVB A 402 source : AC2 9) chain A residue 120 type sequence H description binding site for residue HVB A 403 source : AC3 10) chain A residue 121 type sequence L description binding site for residue HVB A 403 source : AC3 11) chain A residue 123 type sequence N description binding site for residue HVB A 403 source : AC3 12) chain A residue 221 type sequence M description binding site for residue HVB A 403 source : AC3 13) chain A residue 222 type sequence L description binding site for residue HVB A 403 source : AC3 14) chain A residue 281 type sequence N description binding site for residue HVB A 403 source : AC3 15) chain A residue 31-55 type prosite sequence IGEGAGMVCSAYDNVNKVRVAIKK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGAYGMVCsAydnvnkvrv.........AIKK source prosite : PS00107 16) chain A residue 145-157 type prosite sequence VLHRDLKPSNLLL description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpsNLLL source prosite : PS00108 17) chain A residue 59-161 type prosite sequence FEHQTYCQRTLREIKILLRFRHENIIGINDIIRAPTIEQM KDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLK YIHSANVLHRDLKPSNLLLNTTX description MAPK MAP kinase signature. FehqtycqrtlREikillrfrheniigindiiraptieqmkdvyivqdlmetdlykllktqhlsndhicyflyqilrglkyihsanvlh..........RDlKpsnlllnttC source prosite : PS01351 18) chain A residue 259-277 type DNA_BIND sequence KARNYLLSLPHKNKVPWNR description source Swiss-Prot : SWS_FT_FI1 19) chain A residue 284 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI10 20) chain A residue 149 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 31 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 54 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 29 type MOD_RES sequence S description Phosphoserine; by SGK1 => ECO:0000269|PubMed:19447520 source Swiss-Prot : SWS_FT_FI5 24) chain A residue 185 type MOD_RES sequence T description Phosphothreonine; by MAP2K1 and MAP2K2 => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 25) chain A residue 187 type MOD_RES sequence Y description Phosphotyrosine; by MAP2K1 and MAP2K2 => ECO:0000269|PubMed:19053285, ECO:0000269|PubMed:19494114, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI7 26) chain A residue 190 type MOD_RES sequence T description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:19060905 source Swiss-Prot : SWS_FT_FI8 27) chain A residue 246 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:18760948 source Swiss-Prot : SWS_FT_FI9 28) chain A residue 248 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:18760948 source Swiss-Prot : SWS_FT_FI9

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