eF-site ID 4jpz-ABCEHI PDB Code 4jpz Chain A, B, C, E, H, I click to enlarge Title Voltage-gated sodium channel 1.2 C-terminal domain in complex with FGF13U and Ca2+/calmodulin Classification TRANSPORT PROTEIN Compound Fibroblast growth factor 13 Source Homo sapiens (Human) (CALM_HUMAN) Sequence A:  PQLKGIVTKLYSRQGYHLQLQADGTIDGTKDEDSTYTLFN LIPVGLRVVAIQGVQTKLYLAMNSEGYLYTSELFTPECKF KESVFENYYVTYSSMIYRQQQSGRGWYLGLNKEGEIMKGN HVKKNKPAAHFLPKPLKVAMYKEPSLHD B:  EPLSEDDFEMFYEVWEKFDPDATQFIEFAKLSDFADALDP PLLIAKPNKVQLIAMDLPMVSGDRIHCLDILFAFTKRVLG ESGEMDALRIQMEERFMASNPSKVSYEPITTTLKRKQEEV SAIIIQRAYRRYLLKQKVKKVS C:  EEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTE AELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEI REAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMI READIDGDGQVNYEEFVQMMTAK E:  PQLKGIVTKLYSRQGYHLQLQADGTIDGTKDEDSTYTLFN LIPVGLRVVAIQGVQTKLYLAMNSEGYLYTSELFTPECKF KESVFENYYVTYSSMIYRQQQSGRGWYLGLNKEGEIMKGN HVKKNKPAAHFLPKPLKVAMYKEPSLHD H:  EPLSEDDFEMFYEVWEKFDPDATQFIEFAKLSDFADALDP PLLIAKPNKVQLIAMDLPMVSGDRIHCLDILFAFTKRVLG ESGEMDALRIQMEERFMASNPSKVSYEPITTTLKRKQEEV SAIIIQRAYRRYLLKQKVKKVS I:  EEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTE AELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEI REAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMI READIDGDGQVNYEEFVQMMTAK Description Functional site 1) chain C residue 21 type sequence D description BINDING SITE FOR RESIDUE CA C 201 source : AC1 2) chain C residue 23 type sequence D description BINDING SITE FOR RESIDUE CA C 201 source : AC1 3) chain C residue 25 type sequence D description BINDING SITE FOR RESIDUE CA C 201 source : AC1 4) chain C residue 27 type sequence T description BINDING SITE FOR RESIDUE CA C 201 source : AC1 5) chain C residue 32 type sequence E description BINDING SITE FOR RESIDUE CA C 201 source : AC1 6) chain C residue 57 type sequence D description BINDING SITE FOR RESIDUE CA C 202 source : AC2 7) chain C residue 59 type sequence D description BINDING SITE FOR RESIDUE CA C 202 source : AC2 8) chain C residue 61 type sequence N description BINDING SITE FOR RESIDUE CA C 202 source : AC2 9) chain C residue 63 type sequence T description BINDING SITE FOR RESIDUE CA C 202 source : AC2 10) chain C residue 68 type sequence E description BINDING SITE FOR RESIDUE CA C 202 source : AC2 11) chain C residue 94 type sequence D description BINDING SITE FOR RESIDUE CA C 203 source : AC3 12) chain C residue 96 type sequence D description BINDING SITE FOR RESIDUE CA C 203 source : AC3 13) chain C residue 98 type sequence N description BINDING SITE FOR RESIDUE CA C 203 source : AC3 14) chain C residue 100 type sequence Y description BINDING SITE FOR RESIDUE CA C 203 source : AC3 15) chain C residue 130 type sequence D description BINDING SITE FOR RESIDUE CA C 204 source : AC4 16) chain C residue 132 type sequence D description BINDING SITE FOR RESIDUE CA C 204 source : AC4 17) chain C residue 134 type sequence D description BINDING SITE FOR RESIDUE CA C 204 source : AC4 18) chain C residue 136 type sequence Q description BINDING SITE FOR RESIDUE CA C 204 source : AC4 19) chain I residue 21 type sequence D description BINDING SITE FOR RESIDUE CA I 201 source : AC5 20) chain I residue 23 type sequence D description BINDING SITE FOR RESIDUE CA I 201 source : AC5 21) chain I residue 25 type sequence D description BINDING SITE FOR RESIDUE CA I 201 source : AC5 22) chain I residue 27 type sequence T description BINDING SITE FOR RESIDUE CA I 201 source : AC5 23) chain I residue 32 type sequence E description BINDING SITE FOR RESIDUE CA I 201 source : AC5 24) chain I residue 57 type sequence D description BINDING SITE FOR RESIDUE CA I 202 source : AC6 25) chain I residue 59 type sequence D description BINDING SITE FOR RESIDUE CA I 202 source : AC6 26) chain I residue 61 type sequence N description BINDING SITE FOR RESIDUE CA I 202 source : AC6 27) chain I residue 63 type sequence T description BINDING SITE FOR RESIDUE CA I 202 source : AC6 28) chain I residue 68 type sequence E description BINDING SITE FOR RESIDUE CA I 202 source : AC6 29) chain I residue 94 type sequence D description BINDING SITE FOR RESIDUE CA I 203 source : AC7 30) chain I residue 96 type sequence D description BINDING SITE FOR RESIDUE CA I 203 source : AC7 31) chain I residue 98 type sequence N description BINDING SITE FOR RESIDUE CA I 203 source : AC7 32) chain I residue 100 type sequence Y description BINDING SITE FOR RESIDUE CA I 203 source : AC7 33) chain I residue 130 type sequence D description BINDING SITE FOR RESIDUE CA I 204 source : AC8 34) chain I residue 132 type sequence D description BINDING SITE FOR RESIDUE CA I 204 source : AC8 35) chain I residue 134 type sequence D description BINDING SITE FOR RESIDUE CA I 204 source : AC8 36) chain I residue 136 type sequence Q description BINDING SITE FOR RESIDUE CA I 204 source : AC8 37) chain C residue 21-33 type prosite sequence DKDGDGTITTKEL description EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL source prosite : PS00018 38) chain C residue 57-69 type prosite sequence DADGNGTIDFPEF description EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL source prosite : PS00018 39) chain C residue 94-106 type prosite sequence DKDGNGYISAAEL description EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL source prosite : PS00018 40) chain C residue 130-142 type prosite sequence DIDGDGQVNYEEF description EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL source prosite : PS00018 41) chain C residue 45 type MOD_RES sequence T description Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29 source Swiss-Prot : SWS_FT_FI5 42) chain I residue 45 type MOD_RES sequence T description Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29 source Swiss-Prot : SWS_FT_FI5 43) chain C residue 95 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 44) chain I residue 95 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 45) chain C residue 100 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI8 46) chain I residue 100 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI8 47) chain A residue 76-99 type prosite sequence GYLYTSELFTPECKFKESVFENYY description HBGF_FGF HBGF/FGF family signature. GyLyTselftp.ECkFkEsvfenyY source prosite : PS00247 48) chain C residue 21 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 49) chain C residue 68 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 50) chain I residue 21 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 51) chain I residue 23 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 52) chain I residue 25 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 53) chain I residue 27 type BINDING sequence T description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 54) chain I residue 32 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 55) chain I residue 57 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 56) chain I residue 59 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 57) chain I residue 61 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 58) chain I residue 63 type BINDING sequence T description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 59) chain C residue 23 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 60) chain I residue 68 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 61) chain C residue 25 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 62) chain C residue 27 type BINDING sequence T description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 63) chain C residue 32 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 64) chain C residue 57 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 65) chain C residue 59 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 66) chain C residue 61 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 67) chain C residue 63 type BINDING sequence T description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 68) chain C residue 111 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI10 69) chain I residue 111 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI10 70) chain C residue 116 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0007744|PubMed:24129315 source Swiss-Prot : SWS_FT_FI11 71) chain I residue 116 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0007744|PubMed:24129315 source Swiss-Prot : SWS_FT_FI11 72) chain C residue 139 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI12 73) chain I residue 139 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI12 74) chain C residue 22 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157 source Swiss-Prot : SWS_FT_FI13 75) chain I residue 22 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157 source Swiss-Prot : SWS_FT_FI13 76) chain C residue 94 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 77) chain C residue 141 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 78) chain I residue 94 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 79) chain I residue 96 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 80) chain I residue 98 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 81) chain I residue 100 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 82) chain I residue 105 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 83) chain I residue 130 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 84) chain I residue 132 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 85) chain I residue 134 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 86) chain I residue 136 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 87) chain C residue 96 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 88) chain I residue 141 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 89) chain C residue 98 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 90) chain C residue 100 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 91) chain C residue 105 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 92) chain C residue 130 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 93) chain C residue 132 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 94) chain C residue 134 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 95) chain C residue 136 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 96) chain C residue 22 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 97) chain I residue 22 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 98) chain C residue 82 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 99) chain I residue 82 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 100) chain C residue 102 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 101) chain I residue 102 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9

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