eF-site ID 2jbp-ABCDEFGHIJKL PDB Code 2jbp Chain A, B, C, D, E, F, G, H, I, J, K, L Title Protein kinase MK2 in complex with an inhibitor (crystal form-2, co- crystallization) Classification TRANSFERASE Compound MAP KINASE-ACTIVATED PROTEIN KINASE 2 Source (MAPK2_HUMAN) Sequence A:  FHVKSGLQIKKNAIIDDYKVTSQVLGLGINGKVLQIFNKR TQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVYE NLYAGRKCLLIVMECLDGGELFSRIQDRGAFTEREASEIM KSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTD FGFAKETTAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPP FYSNSPGMKTRIRMGQYEFPNPEWSEVSEEVKMLIRNLLK TEPTQRMTITEFMNHPWIMQSTKVPQTPLHTSRVLKEDKE RWE B:  FHVKSGLQIKKNAIIDDYKVTSQVLGLGINGKVLQIFNKR TQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVYE NLYAGRKCLLIVMECLDGGELFSRIQDRGDQAFTEREASE IMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKL TDFGFAKETTPYYVAPEVLGPEKYDKSCDMWSLGVIMYIL LCGYPPFYSNISPGMKTRIRMGQYEFPNPEWSEVSEEVKM LIRNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTPLHTSR VLKEDKERWE C:  FHVKSGLQIKKNAIIDDYKVTSQVLGLGINGKVLQIFNKR TQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVYE NLYAGRKCLLIVMECLDGGELFSRIQDRGAFTEREASEIM KSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTD FGFAKETTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLC GYPPFYPGMKTRIRMGQYEFPNPEWSEVSEEVKMLIRNLL KTEPTQRMTITEFMNHPWIMQSTKVPQTPLHTSRVLKEDK ERWE D:  HVKSGLQIKKNAIIDDYKVTSQVLGLGINGKVLQIFNKRT QEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVYEN LYAGRKCLLIVMECLDGGELFSRIQDRGAFTEREASEIMK SIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDF GFAKETTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCG YPPFYSNSPGMKTRIRMGQYEFPNPEWSEVSEEVKMLIRN LLKTEPTQRMTITEFMNHPWIMQSTKVPQTPLHTSRVLKE DKERWE E:  PQFHVKSGLQIKKNAIIDDYKVTSQVLGLGINGKVLQIFN KRTQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDV YENLYAGRKCLLIVMECLDGGELFSRIQDRGAFTEREASE IMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKL TDFGFAKETTPYYVAPEVLGPEKYDKSCDMWSLGVIMYIL LCGYPPFYSNPGMKTRIRMGQYEFPNPEWSEVSEEVKMLI RNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTPLHTSRVL KED F:  QFHVKSGLQIKKNAIIDDYKVTSQVLGLGINGKVLQIFNK RTQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVY ENLYAGRKCLLIVMECLDGGELFSRIQDRGDQAFTEREAS EIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILK LTDFGFAKETTPYYVAPEVLGPEKYDKSCDMWSLGVIMYI LLCGYPPFYSPGMKTRIRMGQYEFPNPEWSEVSEEVKMLI RNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTPLHTSRVL KEDKERWE G:  QFHVKSGLQIKKNAIIDDYKVTSQVLGLGINGKVLQIFNK RTQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVY ENLYAGRKCLLIVMECLDGGELFSRIQDRAFTEREASEIM KSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTD FGFAKETTSPYYVAPEVLGPEKYDKSCDMWSLGVIMYILL CGYPPFYSNSPGMKTRIRMGQYEFPNPEWSEVSEEVKMLI RNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTPLHTSRVL KEDKERWE H:  FHVKSGLQIKKNAIIDDYKVTSQVLGLGINGKVLQIFNKR TQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVYE NLYAGRKCLLIVMECLDGGELFSRIQDRGAFTEREASEIM KSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTD FGFAKETTSHYVAPEVLGPEKYDKSCDMWSLGVIMYILLC GYPPFYISPGMKTRIRMGQYEFPNPEWSEVSEEVKMLIRN LLKTEPTQRMTITEFMNHPWIMQSTKVPQTPLHTSRVLKE DKE I:  QFHVKSGLQIKKNAIIDDYKVTSQVLGLGNGKVLQIFNKR TQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVYE NLYAGRKCLLIVMECLDGGELFSRIQDRGDQAFTEREASE IMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKL TDFGFAKETTPYYVAPEVLGPEKYDKSCDMWSLGVIMYIL LCGYPPFYSNSPGMKTRIRMGQYEFPNPEWSEVSEEVKML IRNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTPLHTSRV LKEDKERWE J:  VKSGLQIKKNAIIDDYKVTSQVLGLGINGKVLQIFNKRTQ EKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVYENL YAGRKCLLIVMECLDGGELFSRIQDRAFTEREASEIMKSI GEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGF AKETTKYDKSCDMWSLGVIMYILLCGYPPFYSEEVKMLIR NLLKTEPTQRMTITEFMNHPWIMQS K:  HVKSGLQIKKNAIIDDYKVTSQVLGLGINGKVLQIFNKRT QEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVYEN LYAGRKCLLIVMECLDGGELFSRIQDRGAFTEREASEIMK SIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDF GFAKETDKSCDMWSLGVIMYILLCGYPPFYISPGMKTRIR MGQYEFPNPEWSEVSEEVKMLIRNLLKTEPTQRMTITEFM NHPWIMQSTKVPQTPLHTSRVLKED L:  PQFHVKSGLQIKKNAIIDDYKVTSQVLGLGINGKVLQIFN KRTQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDV YENLYAGRKCLLIVMECLDGGELFSRIQDRGAFTEREASE IMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKL TDFGFAKETTYDKSCDMWSLGVIMYILLCGYPPFYSNMKT RIRMGQYEFPNPEWSEVSEEVKMLIRNLLKTEPTQRMTIT EFMNHPWIMQSTKVPQTPLHTSRVLKED Description Functional site 1) chain A residue 70 type sequence L description BINDING SITE FOR RESIDUE P4O A1351 source : AC1 2) chain A residue 72 type sequence L description BINDING SITE FOR RESIDUE P4O A1351 source : AC1 3) chain A residue 73 type sequence G description BINDING SITE FOR RESIDUE P4O A1351 source : AC1 4) chain A residue 91 type sequence A description BINDING SITE FOR RESIDUE P4O A1351 source : AC1 5) chain A residue 93 type sequence K description BINDING SITE FOR RESIDUE P4O A1351 source : AC1 6) chain A residue 139 type sequence E description BINDING SITE FOR RESIDUE P4O A1351 source : AC1 7) chain A residue 140 type sequence C description BINDING SITE FOR RESIDUE P4O A1351 source : AC1 8) chain A residue 141 type sequence L description BINDING SITE FOR RESIDUE P4O A1351 source : AC1 9) chain A residue 142 type sequence D description BINDING SITE FOR RESIDUE P4O A1351 source : AC1 10) chain A residue 191 type sequence N description BINDING SITE FOR RESIDUE P4O A1351 source : AC1 11) chain A residue 193 type sequence L description BINDING SITE FOR RESIDUE P4O A1351 source : AC1 12) chain A residue 207 type sequence D description BINDING SITE FOR RESIDUE P4O A1351 source : AC1 13) chain B residue 70 type sequence L description BINDING SITE FOR RESIDUE P4O B1351 source : AC2 14) chain B residue 72 type sequence L description BINDING SITE FOR RESIDUE P4O B1351 source : AC2 15) chain B residue 73 type sequence G description BINDING SITE FOR RESIDUE P4O B1351 source : AC2 16) chain B residue 91 type sequence A description BINDING SITE FOR RESIDUE P4O B1351 source : AC2 17) chain B residue 93 type sequence K description BINDING SITE FOR RESIDUE P4O B1351 source : AC2 18) chain B residue 139 type sequence E description BINDING SITE FOR RESIDUE P4O B1351 source : AC2 19) chain B residue 141 type sequence L description BINDING SITE FOR RESIDUE P4O B1351 source : AC2 20) chain B residue 193 type sequence L description BINDING SITE FOR RESIDUE P4O B1351 source : AC2 21) chain B residue 207 type sequence D description BINDING SITE FOR RESIDUE P4O B1351 source : AC2 22) chain C residue 70 type sequence L description BINDING SITE FOR RESIDUE P4O C1351 source : AC3 23) chain C residue 72 type sequence L description BINDING SITE FOR RESIDUE P4O C1351 source : AC3 24) chain C residue 73 type sequence G description BINDING SITE FOR RESIDUE P4O C1351 source : AC3 25) chain C residue 91 type sequence A description BINDING SITE FOR RESIDUE P4O C1351 source : AC3 26) chain C residue 93 type sequence K description BINDING SITE FOR RESIDUE P4O C1351 source : AC3 27) chain C residue 139 type sequence E description BINDING SITE FOR RESIDUE P4O C1351 source : AC3 28) chain C residue 140 type sequence C description BINDING SITE FOR RESIDUE P4O C1351 source : AC3 29) chain C residue 141 type sequence L description BINDING SITE FOR RESIDUE P4O C1351 source : AC3 30) chain C residue 142 type sequence D description BINDING SITE FOR RESIDUE P4O C1351 source : AC3 31) chain C residue 193 type sequence L description BINDING SITE FOR RESIDUE P4O C1351 source : AC3 32) chain C residue 207 type sequence D description BINDING SITE FOR RESIDUE P4O C1351 source : AC3 33) chain D residue 70 type sequence L description BINDING SITE FOR RESIDUE P4O D1351 source : AC4 34) chain D residue 72 type sequence L description BINDING SITE FOR RESIDUE P4O D1351 source : AC4 35) chain D residue 73 type sequence G description BINDING SITE FOR RESIDUE P4O D1351 source : AC4 36) chain D residue 93 type sequence K description BINDING SITE FOR RESIDUE P4O D1351 source : AC4 37) chain D residue 139 type sequence E description BINDING SITE FOR RESIDUE P4O D1351 source : AC4 38) chain D residue 140 type sequence C description BINDING SITE FOR RESIDUE P4O D1351 source : AC4 39) chain D residue 141 type sequence L description BINDING SITE FOR RESIDUE P4O D1351 source : AC4 40) chain D residue 142 type sequence D description BINDING SITE FOR RESIDUE P4O D1351 source : AC4 41) chain D residue 193 type sequence L description BINDING SITE FOR RESIDUE P4O D1351 source : AC4 42) chain D residue 207 type sequence D description BINDING SITE FOR RESIDUE P4O D1351 source : AC4 43) chain E residue 70 type sequence L description BINDING SITE FOR RESIDUE P4O E1345 source : AC5 44) chain E residue 73 type sequence G description BINDING SITE FOR RESIDUE P4O E1345 source : AC5 45) chain E residue 139 type sequence E description BINDING SITE FOR RESIDUE P4O E1345 source : AC5 46) chain E residue 141 type sequence L description BINDING SITE FOR RESIDUE P4O E1345 source : AC5 47) chain E residue 142 type sequence D description BINDING SITE FOR RESIDUE P4O E1345 source : AC5 48) chain E residue 193 type sequence L description BINDING SITE FOR RESIDUE P4O E1345 source : AC5 49) chain E residue 206 type sequence T description BINDING SITE FOR RESIDUE P4O E1345 source : AC5 50) chain E residue 207 type sequence D description BINDING SITE FOR RESIDUE P4O E1345 source : AC5 51) chain F residue 70 type sequence L description BINDING SITE FOR RESIDUE P4O F1350 source : AC6 52) chain F residue 72 type sequence L description BINDING SITE FOR RESIDUE P4O F1350 source : AC6 53) chain F residue 91 type sequence A description BINDING SITE FOR RESIDUE P4O F1350 source : AC6 54) chain F residue 93 type sequence K description BINDING SITE FOR RESIDUE P4O F1350 source : AC6 55) chain F residue 139 type sequence E description BINDING SITE FOR RESIDUE P4O F1350 source : AC6 56) chain F residue 140 type sequence C description BINDING SITE FOR RESIDUE P4O F1350 source : AC6 57) chain F residue 141 type sequence L description BINDING SITE FOR RESIDUE P4O F1350 source : AC6 58) chain F residue 191 type sequence N description BINDING SITE FOR RESIDUE P4O F1350 source : AC6 59) chain F residue 207 type sequence D description BINDING SITE FOR RESIDUE P4O F1350 source : AC6 60) chain G residue 70 type sequence L description BINDING SITE FOR RESIDUE P4O G1350 source : AC7 61) chain G residue 72 type sequence L description BINDING SITE FOR RESIDUE P4O G1350 source : AC7 62) chain G residue 73 type sequence G description BINDING SITE FOR RESIDUE P4O G1350 source : AC7 63) chain G residue 91 type sequence A description BINDING SITE FOR RESIDUE P4O G1350 source : AC7 64) chain G residue 93 type sequence K description BINDING SITE FOR RESIDUE P4O G1350 source : AC7 65) chain G residue 139 type sequence E description BINDING SITE FOR RESIDUE P4O G1350 source : AC7 66) chain G residue 140 type sequence C description BINDING SITE FOR RESIDUE P4O G1350 source : AC7 67) chain G residue 141 type sequence L description BINDING SITE FOR RESIDUE P4O G1350 source : AC7 68) chain G residue 142 type sequence D description BINDING SITE FOR RESIDUE P4O G1350 source : AC7 69) chain G residue 191 type sequence N description BINDING SITE FOR RESIDUE P4O G1350 source : AC7 70) chain G residue 193 type sequence L description BINDING SITE FOR RESIDUE P4O G1350 source : AC7 71) chain G residue 207 type sequence D description BINDING SITE FOR RESIDUE P4O G1350 source : AC7 72) chain H residue 70 type sequence L description BINDING SITE FOR RESIDUE P4O H1347 source : AC8 73) chain H residue 72 type sequence L description BINDING SITE FOR RESIDUE P4O H1347 source : AC8 74) chain H residue 78 type sequence V description BINDING SITE FOR RESIDUE P4O H1347 source : AC8 75) chain H residue 91 type sequence A description BINDING SITE FOR RESIDUE P4O H1347 source : AC8 76) chain H residue 93 type sequence K description BINDING SITE FOR RESIDUE P4O H1347 source : AC8 77) chain H residue 139 type sequence E description BINDING SITE FOR RESIDUE P4O H1347 source : AC8 78) chain H residue 141 type sequence L description BINDING SITE FOR RESIDUE P4O H1347 source : AC8 79) chain H residue 142 type sequence D description BINDING SITE FOR RESIDUE P4O H1347 source : AC8 80) chain H residue 191 type sequence N description BINDING SITE FOR RESIDUE P4O H1347 source : AC8 81) chain H residue 193 type sequence L description BINDING SITE FOR RESIDUE P4O H1347 source : AC8 82) chain H residue 207 type sequence D description BINDING SITE FOR RESIDUE P4O H1347 source : AC8 83) chain I residue 70 type sequence L description BINDING SITE FOR RESIDUE P4O I1351 source : AC9 84) chain I residue 72 type sequence L description BINDING SITE FOR RESIDUE P4O I1351 source : AC9 85) chain I residue 91 type sequence A description BINDING SITE FOR RESIDUE P4O I1351 source : AC9 86) chain I residue 93 type sequence K description BINDING SITE FOR RESIDUE P4O I1351 source : AC9 87) chain I residue 139 type sequence E description BINDING SITE FOR RESIDUE P4O I1351 source : AC9 88) chain I residue 140 type sequence C description BINDING SITE FOR RESIDUE P4O I1351 source : AC9 89) chain I residue 141 type sequence L description BINDING SITE FOR RESIDUE P4O I1351 source : AC9 90) chain I residue 193 type sequence L description BINDING SITE FOR RESIDUE P4O I1351 source : AC9 91) chain I residue 207 type sequence D description BINDING SITE FOR RESIDUE P4O I1351 source : AC9 92) chain K residue 70 type sequence L description BINDING SITE FOR RESIDUE P4O K1345 source : BC1 93) chain K residue 72 type sequence L description BINDING SITE FOR RESIDUE P4O K1345 source : BC1 94) chain K residue 73 type sequence G description BINDING SITE FOR RESIDUE P4O K1345 source : BC1 95) chain K residue 78 type sequence V description BINDING SITE FOR RESIDUE P4O K1345 source : BC1 96) chain K residue 91 type sequence A description BINDING SITE FOR RESIDUE P4O K1345 source : BC1 97) chain K residue 93 type sequence K description BINDING SITE FOR RESIDUE P4O K1345 source : BC1 98) chain K residue 139 type sequence E description BINDING SITE FOR RESIDUE P4O K1345 source : BC1 99) chain K residue 140 type sequence C description BINDING SITE FOR RESIDUE P4O K1345 source : BC1 100) chain K residue 141 type sequence L description BINDING SITE FOR RESIDUE P4O K1345 source : BC1 101) chain K residue 142 type sequence D description BINDING SITE FOR RESIDUE P4O K1345 source : BC1 102) chain K residue 191 type sequence N description BINDING SITE FOR RESIDUE P4O K1345 source : BC1 103) chain K residue 193 type sequence L description BINDING SITE FOR RESIDUE P4O K1345 source : BC1 104) chain K residue 207 type sequence D description BINDING SITE FOR RESIDUE P4O K1345 source : BC1 105) chain L residue 70 type sequence L description BINDING SITE FOR RESIDUE P4O L1345 source : BC2 106) chain L residue 72 type sequence L description BINDING SITE FOR RESIDUE P4O L1345 source : BC2 107) chain L residue 73 type sequence G description BINDING SITE FOR RESIDUE P4O L1345 source : BC2 108) chain L residue 93 type sequence K description BINDING SITE FOR RESIDUE P4O L1345 source : BC2 109) chain L residue 139 type sequence E description BINDING SITE FOR RESIDUE P4O L1345 source : BC2 110) chain L residue 140 type sequence C description BINDING SITE FOR RESIDUE P4O L1345 source : BC2 111) chain L residue 141 type sequence L description BINDING SITE FOR RESIDUE P4O L1345 source : BC2 112) chain L residue 142 type sequence D description BINDING SITE FOR RESIDUE P4O L1345 source : BC2 113) chain L residue 193 type sequence L description BINDING SITE FOR RESIDUE P4O L1345 source : BC2 114) chain L residue 206 type sequence T description BINDING SITE FOR RESIDUE P4O L1345 source : BC2 115) chain L residue 207 type sequence D description BINDING SITE FOR RESIDUE P4O L1345 source : BC2 116) chain A residue 70-93 type prosite sequence LGLGINGKVLQIFNKRTQEKFALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGLGINGKVLqIfnkrtqek..........FALK source prosite : PS00107 117) chain A residue 182-194 type prosite sequence IAHRDVKPENLLY description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHrDVKpeNLLY source prosite : PS00108 118) chain A residue 186 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 119) chain J residue 186 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 120) chain K residue 186 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 121) chain L residue 186 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 122) chain B residue 186 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 123) chain C residue 186 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 124) chain D residue 186 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 125) chain E residue 186 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 126) chain F residue 186 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 127) chain G residue 186 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 128) chain H residue 186 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 129) chain I residue 186 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 130) chain A residue 70 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 131) chain E residue 93 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 132) chain F residue 70 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 133) chain F residue 93 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 134) chain G residue 70 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 135) chain G residue 93 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 136) chain H residue 70 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 137) chain H residue 93 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 138) chain I residue 70 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 139) chain I residue 93 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 140) chain J residue 70 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 141) chain A residue 93 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 142) chain J residue 93 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 143) chain K residue 70 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 144) chain K residue 93 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 145) chain L residue 70 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 146) chain L residue 93 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 147) chain B residue 70 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 148) chain B residue 93 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 149) chain C residue 70 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 150) chain C residue 93 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 151) chain D residue 70 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 152) chain D residue 93 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 153) chain E residue 70 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 154) chain A residue 139 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 155) chain J residue 139 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 156) chain K residue 139 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 157) chain L residue 139 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 158) chain B residue 139 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 159) chain C residue 139 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 160) chain D residue 139 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 161) chain E residue 139 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 162) chain F residue 139 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 163) chain G residue 139 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 164) chain H residue 139 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 165) chain I residue 139 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 166) chain A residue 272 type MOD_RES sequence S description Phosphoserine; by MAPK14 => ECO:0000269|PubMed:8846784 source Swiss-Prot : SWS_FT_FI5 167) chain K residue 272 type MOD_RES sequence S description Phosphoserine; by MAPK14 => ECO:0000269|PubMed:8846784 source Swiss-Prot : SWS_FT_FI5 168) chain B residue 272 type MOD_RES sequence S description Phosphoserine; by MAPK14 => ECO:0000269|PubMed:8846784 source Swiss-Prot : SWS_FT_FI5 169) chain D residue 272 type MOD_RES sequence S description Phosphoserine; by MAPK14 => ECO:0000269|PubMed:8846784 source Swiss-Prot : SWS_FT_FI5 170) chain G residue 272 type MOD_RES sequence S description Phosphoserine; by MAPK14 => ECO:0000269|PubMed:8846784 source Swiss-Prot : SWS_FT_FI5 171) chain H residue 272 type MOD_RES sequence S description Phosphoserine; by MAPK14 => ECO:0000269|PubMed:8846784 source Swiss-Prot : SWS_FT_FI5 172) chain I residue 272 type MOD_RES sequence S description Phosphoserine; by MAPK14 => ECO:0000269|PubMed:8846784 source Swiss-Prot : SWS_FT_FI5 173) chain A residue 328 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 174) chain J residue 328 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 175) chain K residue 328 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 176) chain L residue 328 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 177) chain B residue 328 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 178) chain C residue 328 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 179) chain D residue 328 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 180) chain E residue 328 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 181) chain F residue 328 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 182) chain G residue 328 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 183) chain H residue 328 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 184) chain I residue 328 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 185) chain A residue 334 type MOD_RES sequence T description Phosphothreonine; by MAPK14 => ECO:0000269|PubMed:8846784, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 186) chain K residue 334 type MOD_RES sequence T description Phosphothreonine; by MAPK14 => ECO:0000269|PubMed:8846784, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 187) chain L residue 334 type MOD_RES sequence T description Phosphothreonine; by MAPK14 => ECO:0000269|PubMed:8846784, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 188) chain B residue 334 type MOD_RES sequence T description Phosphothreonine; by MAPK14 => ECO:0000269|PubMed:8846784, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 189) chain C residue 334 type MOD_RES sequence T description Phosphothreonine; by MAPK14 => ECO:0000269|PubMed:8846784, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 190) chain D residue 334 type MOD_RES sequence T description Phosphothreonine; by MAPK14 => ECO:0000269|PubMed:8846784, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 191) chain E residue 334 type MOD_RES sequence T description Phosphothreonine; by MAPK14 => ECO:0000269|PubMed:8846784, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 192) chain F residue 334 type MOD_RES sequence T description Phosphothreonine; by MAPK14 => ECO:0000269|PubMed:8846784, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 193) chain G residue 334 type MOD_RES sequence T description Phosphothreonine; by MAPK14 => ECO:0000269|PubMed:8846784, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 194) chain H residue 334 type MOD_RES sequence T description Phosphothreonine; by MAPK14 => ECO:0000269|PubMed:8846784, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 195) chain I residue 334 type MOD_RES sequence T description Phosphothreonine; by MAPK14 => ECO:0000269|PubMed:8846784, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7

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