eF-site ID 4qgc-ABCD PDB Code 4qgc Chain A, B, C, D click to enlarge Title crystal structure of PKM2-K422R mutant Classification TRANSFERASE Compound Pyruvate kinase PKM Source Homo sapiens (Human) (KPYM_HUMAN) Sequence A:  DTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVETLKE MIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPI LYRPVAVALDTKGPEIRTGLIKGTAEVELKKGATLKITLD NAYMEKCDENILWLDYKNICKVVEVGSKIYVDDGLISLQV KQKGADFLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKD IQDLKFGVEQDVDMVFASFIRKASDVHEVRKVLGEKGKNI KIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEK VFLAQKMMIGRCNRAGKPVICATQMLESMIKKPRPTRAEG SDVANAVLDGADCIMLSGETAKGDYPLEAVRMQHLIAREA EAAIYHLQLFEELRRLAPDPTEATAVGAVEASFRCCSGAI IVLTKSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRG IFPVLCKDPVQEAWAEDVDLRVNFAMNVGKARGFFKKGDV VIVLTGWRPGSGFTNTMRVVPVP B:  DTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVETLKE MIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPI LYRPVAVALDTKGPEIRTGLIKGAEVELKKGATLKITLDN AYMEKCDENILWLDYKNICKVVEVGSKIYVDDGLISLQVK QKGADFLVTEVENGGSLGSKKGVNLPDLPAVSEKDIQDLK FGVEQDVDMVFASFIRKASDVHEVRKVLGEKGKNIKIISK IENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQ KMMIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVAN AVLDGADCIMLSGETAKGDYPLEAVRMQHLIAREAEAAIY HLQLFEELRRLAPSDPTEATAVGAVEASFRCCSGAIIVLT KSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGIFPV LCKDPVQEAWAEDVDLRVNFAMNVGKARGFFKKGDVVIVL TGWRPGSGFTNTMRVVPVP C:  DTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVETLKE MIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPI LYRPVAVALDTKGPEIRTGLIKGAEVELKKGATLKITLDN AYMEKCDENILWLDYKNICKVVEVGSKIYVDDGLISLQVK QKGADFLVTEVENGGSLGSKKGVNLPDLPAVSEKDIQDLK FGVEQDVDMVFASFIRKASDVHEVRKVLGEKGKNIKIISK IENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQ KMMIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVAN AVLDGADCIMLSGETAKGDYPLEAVRMQHLIAREAEAAIY HLQLFEELRRLTSDPTEATAVGAVEASFRCCSGAIIVLTK SGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGIFPVL CKDPVQEAWAEDVDLRVNFAMNVGKARGFFKKGDVVIVLT GWRPGSGFTNTMRVVPVP D:  TFLEHMCRLDIDSPPITARNTGIICTIGPASRSVETLKEM IKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPIL YRPVAVALDTKGPEIRTGLIKGAEVELKKGATLKITLDNA YMEKCDENILWLDYKNICKVVEVGSKIYVDDGLISLQVKQ KGADFLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQ DLKFGVEQDVDMVFASFIRKASDVHEVRKVLGEKGKNIKI ISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVF LAQKMMIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSD VANAVLDGADCIMLSGETAKGDYPLEAVRMQHLIAREAEA AIYHLQLFEELRRLSDPTEATAVGAVEASFRCCSGAIIVL TKSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGIFP VLCKDPVQEAWAEDVDLRVNFAMNVGKARGFFKKGDVVIV LTGWRPGSGFTNTMRVVPVP Description Functional site 1) chain A residue 75 type sequence N description BINDING SITE FOR RESIDUE K A 1001 source : AC1 2) chain A residue 77 type sequence S description BINDING SITE FOR RESIDUE K A 1001 source : AC1 3) chain A residue 113 type sequence D description BINDING SITE FOR RESIDUE K A 1001 source : AC1 4) chain A residue 114 type sequence T description BINDING SITE FOR RESIDUE K A 1001 source : AC1 5) chain A residue 433 type sequence K description BINDING SITE FOR RESIDUE SO4 A 1002 source : AC2 6) chain A residue 482 type sequence W description BINDING SITE FOR RESIDUE SO4 A 1002 source : AC2 7) chain A residue 489 type sequence R description BINDING SITE FOR RESIDUE SO4 A 1002 source : AC2 8) chain A residue 432 type sequence T description BINDING SITE FOR RESIDUE SO4 A 1003 source : AC3 9) chain A residue 433 type sequence K description BINDING SITE FOR RESIDUE SO4 A 1003 source : AC3 10) chain A residue 434 type sequence S description BINDING SITE FOR RESIDUE SO4 A 1003 source : AC3 11) chain A residue 435 type sequence G description BINDING SITE FOR RESIDUE SO4 A 1003 source : AC3 12) chain A residue 436 type sequence R description BINDING SITE FOR RESIDUE SO4 A 1003 source : AC3 13) chain A residue 437 type sequence S description BINDING SITE FOR RESIDUE SO4 A 1003 source : AC3 14) chain A residue 522 type sequence T description BINDING SITE FOR RESIDUE SO4 A 1003 source : AC3 15) chain A residue 75 type sequence N description BINDING SITE FOR RESIDUE SO4 A 1004 source : AC4 16) chain A residue 78 type sequence H description BINDING SITE FOR RESIDUE SO4 A 1004 source : AC4 17) chain A residue 120 type sequence R description BINDING SITE FOR RESIDUE SO4 A 1004 source : AC4 18) chain A residue 43 type sequence R description BINDING SITE FOR RESIDUE GOL A 1005 source : AC5 19) chain A residue 44 type sequence N description BINDING SITE FOR RESIDUE GOL A 1005 source : AC5 20) chain A residue 70 type sequence N description BINDING SITE FOR RESIDUE GOL A 1005 source : AC5 21) chain A residue 106 type sequence R description BINDING SITE FOR RESIDUE GOL A 1005 source : AC5 22) chain A residue 464 type sequence H description BINDING SITE FOR RESIDUE GOL A 1005 source : AC5 23) chain A residue 470 type sequence F description BINDING SITE FOR RESIDUE GOL A 1005 source : AC5 24) chain B residue 75 type sequence N description BINDING SITE FOR RESIDUE K B 1001 source : AC6 25) chain B residue 77 type sequence S description BINDING SITE FOR RESIDUE K B 1001 source : AC6 26) chain B residue 113 type sequence D description BINDING SITE FOR RESIDUE K B 1001 source : AC6 27) chain B residue 114 type sequence T description BINDING SITE FOR RESIDUE K B 1001 source : AC6 28) chain B residue 432 type sequence T description BINDING SITE FOR RESIDUE SO4 B 1002 source : AC7 29) chain B residue 433 type sequence K description BINDING SITE FOR RESIDUE SO4 B 1002 source : AC7 30) chain B residue 434 type sequence S description BINDING SITE FOR RESIDUE SO4 B 1002 source : AC7 31) chain B residue 435 type sequence G description BINDING SITE FOR RESIDUE SO4 B 1002 source : AC7 32) chain B residue 436 type sequence R description BINDING SITE FOR RESIDUE SO4 B 1002 source : AC7 33) chain B residue 437 type sequence S description BINDING SITE FOR RESIDUE SO4 B 1002 source : AC7 34) chain B residue 433 type sequence K description BINDING SITE FOR RESIDUE SO4 B 1003 source : AC8 35) chain B residue 482 type sequence W description BINDING SITE FOR RESIDUE SO4 B 1003 source : AC8 36) chain B residue 489 type sequence R description BINDING SITE FOR RESIDUE SO4 B 1003 source : AC8 37) chain B residue 43 type sequence R description BINDING SITE FOR RESIDUE GOL B 1004 source : AC9 38) chain B residue 44 type sequence N description BINDING SITE FOR RESIDUE GOL B 1004 source : AC9 39) chain B residue 70 type sequence N description BINDING SITE FOR RESIDUE GOL B 1004 source : AC9 40) chain B residue 464 type sequence H description BINDING SITE FOR RESIDUE GOL B 1004 source : AC9 41) chain B residue 466 type sequence Y description BINDING SITE FOR RESIDUE GOL B 1004 source : AC9 42) chain B residue 469 type sequence I description BINDING SITE FOR RESIDUE GOL B 1004 source : AC9 43) chain B residue 471 type sequence P description BINDING SITE FOR RESIDUE GOL B 1004 source : AC9 44) chain C residue 75 type sequence N description BINDING SITE FOR RESIDUE K C 1001 source : BC1 45) chain C residue 77 type sequence S description BINDING SITE FOR RESIDUE K C 1001 source : BC1 46) chain C residue 113 type sequence D description BINDING SITE FOR RESIDUE K C 1001 source : BC1 47) chain C residue 114 type sequence T description BINDING SITE FOR RESIDUE K C 1001 source : BC1 48) chain C residue 432 type sequence T description BINDING SITE FOR RESIDUE SO4 C 1002 source : BC2 49) chain C residue 433 type sequence K description BINDING SITE FOR RESIDUE SO4 C 1002 source : BC2 50) chain C residue 434 type sequence S description BINDING SITE FOR RESIDUE SO4 C 1002 source : BC2 51) chain C residue 436 type sequence R description BINDING SITE FOR RESIDUE SO4 C 1002 source : BC2 52) chain C residue 437 type sequence S description BINDING SITE FOR RESIDUE SO4 C 1002 source : BC2 53) chain C residue 482 type sequence W description BINDING SITE FOR RESIDUE SO4 C 1003 source : BC3 54) chain C residue 489 type sequence R description BINDING SITE FOR RESIDUE SO4 C 1003 source : BC3 55) chain C residue 518 type sequence G description BINDING SITE FOR RESIDUE SO4 C 1003 source : BC3 56) chain C residue 43 type sequence R description BINDING SITE FOR RESIDUE GOL C 1004 source : BC4 57) chain C residue 464 type sequence H description BINDING SITE FOR RESIDUE GOL C 1004 source : BC4 58) chain C residue 469 type sequence I description BINDING SITE FOR RESIDUE GOL C 1004 source : BC4 59) chain D residue 75 type sequence N description BINDING SITE FOR RESIDUE K D 1001 source : BC5 60) chain D residue 77 type sequence S description BINDING SITE FOR RESIDUE K D 1001 source : BC5 61) chain D residue 113 type sequence D description BINDING SITE FOR RESIDUE K D 1001 source : BC5 62) chain D residue 114 type sequence T description BINDING SITE FOR RESIDUE K D 1001 source : BC5 63) chain D residue 433 type sequence K description BINDING SITE FOR RESIDUE SO4 D 1002 source : BC6 64) chain D residue 482 type sequence W description BINDING SITE FOR RESIDUE SO4 D 1002 source : BC6 65) chain D residue 489 type sequence R description BINDING SITE FOR RESIDUE SO4 D 1002 source : BC6 66) chain D residue 432 type sequence T description BINDING SITE FOR RESIDUE SO4 D 1003 source : BC7 67) chain D residue 433 type sequence K description BINDING SITE FOR RESIDUE SO4 D 1003 source : BC7 68) chain D residue 434 type sequence S description BINDING SITE FOR RESIDUE SO4 D 1003 source : BC7 69) chain D residue 436 type sequence R description BINDING SITE FOR RESIDUE SO4 D 1003 source : BC7 70) chain D residue 437 type sequence S description BINDING SITE FOR RESIDUE SO4 D 1003 source : BC7 71) chain D residue 43 type sequence R description BINDING SITE FOR RESIDUE GOL D 1004 source : BC8 72) chain D residue 44 type sequence N description BINDING SITE FOR RESIDUE GOL D 1004 source : BC8 73) chain D residue 70 type sequence N description BINDING SITE FOR RESIDUE GOL D 1004 source : BC8 74) chain D residue 106 type sequence R description BINDING SITE FOR RESIDUE GOL D 1004 source : BC8 75) chain D residue 464 type sequence H description BINDING SITE FOR RESIDUE GOL D 1004 source : BC8 76) chain D residue 469 type sequence I description BINDING SITE FOR RESIDUE GOL D 1004 source : BC8 77) chain D residue 470 type sequence F description BINDING SITE FOR RESIDUE GOL D 1004 source : BC8 78) chain A residue 70 type BINDING sequence N description BINDING => ECO:0000269|PubMed:23064226 source Swiss-Prot : SWS_FT_FI1 79) chain D residue 70 type BINDING sequence N description BINDING => ECO:0000269|PubMed:23064226 source Swiss-Prot : SWS_FT_FI1 80) chain D residue 106 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23064226 source Swiss-Prot : SWS_FT_FI1 81) chain D residue 464 type BINDING sequence H description BINDING => ECO:0000269|PubMed:23064226 source Swiss-Prot : SWS_FT_FI1 82) chain A residue 106 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23064226 source Swiss-Prot : SWS_FT_FI1 83) chain A residue 464 type BINDING sequence H description BINDING => ECO:0000269|PubMed:23064226 source Swiss-Prot : SWS_FT_FI1 84) chain B residue 70 type BINDING sequence N description BINDING => ECO:0000269|PubMed:23064226 source Swiss-Prot : SWS_FT_FI1 85) chain B residue 106 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23064226 source Swiss-Prot : SWS_FT_FI1 86) chain B residue 464 type BINDING sequence H description BINDING => ECO:0000269|PubMed:23064226 source Swiss-Prot : SWS_FT_FI1 87) chain C residue 70 type BINDING sequence N description BINDING => ECO:0000269|PubMed:23064226 source Swiss-Prot : SWS_FT_FI1 88) chain C residue 106 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23064226 source Swiss-Prot : SWS_FT_FI1 89) chain C residue 464 type BINDING sequence H description BINDING => ECO:0000269|PubMed:23064226 source Swiss-Prot : SWS_FT_FI1 90) chain A residue 41 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI10 91) chain B residue 41 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI10 92) chain C residue 41 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI10 93) chain D residue 41 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI10 94) chain A residue 62 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI11 95) chain A residue 89 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI11 96) chain B residue 62 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI11 97) chain B residue 89 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI11 98) chain C residue 62 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI11 99) chain C residue 89 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI11 100) chain D residue 62 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI11 101) chain D residue 89 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI11 102) chain A residue 305 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:21700219 source Swiss-Prot : SWS_FT_FI22 103) chain B residue 305 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:21700219 source Swiss-Prot : SWS_FT_FI22 104) chain C residue 305 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:21700219 source Swiss-Prot : SWS_FT_FI22 105) chain D residue 305 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:21700219 source Swiss-Prot : SWS_FT_FI22 106) chain A residue 403 type MOD_RES sequence P description 4-hydroxyproline => ECO:0000269|PubMed:21620138 source Swiss-Prot : SWS_FT_FI23 107) chain A residue 408 type MOD_RES sequence P description 4-hydroxyproline => ECO:0000269|PubMed:21620138 source Swiss-Prot : SWS_FT_FI23 108) chain B residue 403 type MOD_RES sequence P description 4-hydroxyproline => ECO:0000269|PubMed:21620138 source Swiss-Prot : SWS_FT_FI23 109) chain B residue 408 type MOD_RES sequence P description 4-hydroxyproline => ECO:0000269|PubMed:21620138 source Swiss-Prot : SWS_FT_FI23 110) chain C residue 408 type MOD_RES sequence P description 4-hydroxyproline => ECO:0000269|PubMed:21620138 source Swiss-Prot : SWS_FT_FI23 111) chain D residue 408 type MOD_RES sequence P description 4-hydroxyproline => ECO:0000269|PubMed:21620138 source Swiss-Prot : SWS_FT_FI23 112) chain A residue 433 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:24120661, ECO:0000269|PubMed:26787900, ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI24 113) chain B residue 433 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:24120661, ECO:0000269|PubMed:26787900, ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI24 114) chain C residue 433 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:24120661, ECO:0000269|PubMed:26787900, ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI24 115) chain D residue 433 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:24120661, ECO:0000269|PubMed:26787900, ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI24 116) chain A residue 265-277 type prosite sequence IKIISKIENHEGV description PYRUVATE_KINASE Pyruvate kinase active site signature. IkIISKIENhEGV source prosite : PS00110 117) chain D residue 266 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI27 118) chain D residue 270 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI27 119) chain A residue 266 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI27 120) chain A residue 270 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI27 121) chain B residue 266 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI27 122) chain B residue 270 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI27 123) chain C residue 266 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI27 124) chain C residue 270 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI27 125) chain A residue 475 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI25 126) chain B residue 475 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI25 127) chain C residue 475 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI25 128) chain D residue 475 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI25 129) chain A residue 115 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI26 130) chain B residue 115 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI26 131) chain C residue 115 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI26 132) chain D residue 115 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI26 133) chain A residue 166 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0007744|PubMed:25114211 source Swiss-Prot : SWS_FT_FI28 134) chain B residue 166 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0007744|PubMed:25114211 source Swiss-Prot : SWS_FT_FI28 135) chain C residue 166 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0007744|PubMed:25114211 source Swiss-Prot : SWS_FT_FI28 136) chain D residue 166 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0007744|PubMed:25114211 source Swiss-Prot : SWS_FT_FI28 137) chain A residue 66 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI12 138) chain A residue 498 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI12 139) chain B residue 66 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI12 140) chain B residue 498 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI12 141) chain C residue 66 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI12 142) chain C residue 498 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI12 143) chain D residue 66 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI12 144) chain D residue 498 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI12 145) chain A residue 97 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P11980 source Swiss-Prot : SWS_FT_FI13 146) chain A residue 100 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P11980 source Swiss-Prot : SWS_FT_FI13 147) chain B residue 97 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P11980 source Swiss-Prot : SWS_FT_FI13 148) chain B residue 100 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P11980 source Swiss-Prot : SWS_FT_FI13 149) chain C residue 97 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P11980 source Swiss-Prot : SWS_FT_FI13 150) chain C residue 100 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P11980 source Swiss-Prot : SWS_FT_FI13 151) chain D residue 97 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P11980 source Swiss-Prot : SWS_FT_FI13 152) chain D residue 100 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P11980 source Swiss-Prot : SWS_FT_FI13 153) chain A residue 105 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI14 154) chain B residue 105 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI14 155) chain C residue 105 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI14 156) chain D residue 105 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI14 157) chain A residue 148 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI16 158) chain B residue 148 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI16 159) chain C residue 148 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI16 160) chain D residue 148 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI16 161) chain A residue 166 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI17 162) chain A residue 322 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI17 163) chain B residue 166 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI17 164) chain B residue 322 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI17 165) chain C residue 166 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI17 166) chain C residue 322 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI17 167) chain D residue 166 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI17 168) chain D residue 322 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI17 169) chain A residue 175 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI18 170) chain B residue 175 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI18 171) chain C residue 175 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI18 172) chain D residue 175 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI18 173) chain A residue 432 type BINDING sequence T description BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI4 174) chain C residue 482 type BINDING sequence W description BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI4 175) chain C residue 489 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI4 176) chain C residue 516 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI4 177) chain D residue 432 type BINDING sequence T description BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI4 178) chain D residue 482 type BINDING sequence W description BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI4 179) chain D residue 489 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI4 180) chain D residue 516 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI4 181) chain A residue 482 type BINDING sequence W description BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI4 182) chain A residue 489 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI4 183) chain A residue 516 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI4 184) chain B residue 432 type BINDING sequence T description BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI4 185) chain B residue 482 type BINDING sequence W description BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI4 186) chain B residue 489 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI4 187) chain B residue 516 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI4 188) chain C residue 432 type BINDING sequence T description BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI4 189) chain A residue 270 type SITE sequence K description Transition state stabilizer => ECO:0000250|UniProtKB:P00549 source Swiss-Prot : SWS_FT_FI5 190) chain B residue 270 type SITE sequence K description Transition state stabilizer => ECO:0000250|UniProtKB:P00549 source Swiss-Prot : SWS_FT_FI5 191) chain C residue 270 type SITE sequence K description Transition state stabilizer => ECO:0000250|UniProtKB:P00549 source Swiss-Prot : SWS_FT_FI5 192) chain D residue 270 type SITE sequence K description Transition state stabilizer => ECO:0000250|UniProtKB:P00549 source Swiss-Prot : SWS_FT_FI5 193) chain A residue 195 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI19 194) chain B residue 195 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI19 195) chain C residue 195 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI19 196) chain D residue 195 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI19 197) chain A residue 73 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 198) chain B residue 328 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 199) chain C residue 73 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 200) chain C residue 270 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 201) chain C residue 295 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 202) chain C residue 296 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 203) chain C residue 328 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 204) chain D residue 73 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 205) chain D residue 270 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 206) chain D residue 295 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 207) chain D residue 296 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 208) chain A residue 270 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 209) chain D residue 328 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 210) chain A residue 295 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 211) chain A residue 296 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 212) chain A residue 328 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 213) chain B residue 73 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 214) chain B residue 270 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 215) chain B residue 295 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 216) chain B residue 296 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 217) chain A residue 266 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI20 218) chain B residue 266 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI20 219) chain C residue 266 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI20 220) chain D residue 266 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI20 221) chain A residue 270 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI21 222) chain B residue 270 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI21 223) chain C residue 270 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI21 224) chain D residue 270 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI21 225) chain A residue 75 type BINDING sequence N description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 226) chain B residue 113 type BINDING sequence D description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 227) chain B residue 114 type BINDING sequence T description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 228) chain B residue 120 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 229) chain B residue 207 type BINDING sequence K description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 230) chain B residue 272 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 231) chain C residue 75 type BINDING sequence N description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 232) chain C residue 77 type BINDING sequence S description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 233) chain C residue 113 type BINDING sequence D description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 234) chain C residue 114 type BINDING sequence T description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 235) chain C residue 120 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 236) chain A residue 77 type BINDING sequence S description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 237) chain C residue 207 type BINDING sequence K description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 238) chain C residue 272 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 239) chain D residue 75 type BINDING sequence N description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 240) chain D residue 77 type BINDING sequence S description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 241) chain D residue 113 type BINDING sequence D description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 242) chain D residue 114 type BINDING sequence T description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 243) chain D residue 120 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 244) chain D residue 207 type BINDING sequence K description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 245) chain D residue 272 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 246) chain A residue 113 type BINDING sequence D description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 247) chain A residue 114 type BINDING sequence T description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 248) chain A residue 120 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 249) chain A residue 207 type BINDING sequence K description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 250) chain A residue 272 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 251) chain B residue 75 type BINDING sequence N description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 252) chain B residue 77 type BINDING sequence S description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 253) chain A residue 433 type SITE sequence K description Crucial for phosphotyrosine binding => ECO:0000269|PubMed:27199445 source Swiss-Prot : SWS_FT_FI6 254) chain B residue 433 type SITE sequence K description Crucial for phosphotyrosine binding => ECO:0000269|PubMed:27199445 source Swiss-Prot : SWS_FT_FI6 255) chain C residue 433 type SITE sequence K description Crucial for phosphotyrosine binding => ECO:0000269|PubMed:27199445 source Swiss-Prot : SWS_FT_FI6 256) chain D residue 433 type SITE sequence K description Crucial for phosphotyrosine binding => ECO:0000269|PubMed:27199445 source Swiss-Prot : SWS_FT_FI6 257) chain A residue 37 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 258) chain B residue 37 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 259) chain C residue 37 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 260) chain D residue 37 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9

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