eF-site ID 5yu9-ABCD PDB Code 5yu9 Chain A, B, C, D click to enlarge Title Crystal structure of EGFR 696-1022 T790M in complex with Ibrutinib Classification ONCOPROTEIN Compound Epidermal growth factor receptor Source Homo sapiens (Human) (EGFR_HUMAN) Sequence A:  NQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVK IPVAIKELREKANKEILDEAYVMASVDNPHVCRLLGICLT STVQLIMQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAK GMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLK VPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPY DGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDA DSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDS NFYRALMDEEDMDDVVDADEYL B:  PNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKV KIPVAIKELREANKEILDEAYVMASVDNPHVCRLLGICLT STVQLIMQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAK GMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLV PIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYD GIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDAD SRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSN FYRALMDEEDMDDVV C:  EAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGE KVKIPVAIKELREKANKEILDEAYVMASVDNPHVCRLLGI CLTSTVQLIMQLMPFGCLLDYVREHKDNIGSQYLLNWCVQ IAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAK LLKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGS KPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWM IDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSP TDSNFYRALMDEEDMVDADEYLIPQQ D:  NQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVK IPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLG ICLTSTVQLIMQLMPFGCLLDYVREHKDNIGSQYLLNWCV QIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLA KLLVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGS KPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWM IDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSP TDSNFYRALMDEEDMDDVVD Description Functional site 1) chain A residue 718 type sequence L description binding site for residue 1E8 A 1101 source : AC1 2) chain A residue 719 type sequence G description binding site for residue 1E8 A 1101 source : AC1 3) chain A residue 743 type sequence A description binding site for residue 1E8 A 1101 source : AC1 4) chain A residue 766 type sequence M description binding site for residue 1E8 A 1101 source : AC1 5) chain A residue 788 type sequence L description binding site for residue 1E8 A 1101 source : AC1 6) chain A residue 790 type sequence M description binding site for residue 1E8 A 1101 source : AC1 7) chain A residue 791 type sequence Q description binding site for residue 1E8 A 1101 source : AC1 8) chain A residue 793 type sequence M description binding site for residue 1E8 A 1101 source : AC1 9) chain A residue 797 type sequence C description binding site for residue 1E8 A 1101 source : AC1 10) chain A residue 841 type sequence R description binding site for residue 1E8 A 1101 source : AC1 11) chain A residue 854 type sequence T description binding site for residue 1E8 A 1101 source : AC1 12) chain A residue 855 type sequence D description binding site for residue 1E8 A 1101 source : AC1 13) chain A residue 856 type sequence F description binding site for residue 1E8 A 1101 source : AC1 14) chain C residue 953 type sequence I description binding site for residue CL C 1102 source : AC2 15) chain C residue 955 type sequence A description binding site for residue CL C 1102 source : AC2 16) chain D residue 932 type sequence R description binding site for residue CL D 1102 source : AC3 17) chain D residue 951 type sequence W description binding site for residue CL D 1102 source : AC3 18) chain B residue 743 type sequence A description binding site for Di-peptide 1E8 B 1101 and CYS B 797 source : AC4 19) chain B residue 745 type sequence K description binding site for Di-peptide 1E8 B 1101 and CYS B 797 source : AC4 20) chain B residue 766 type sequence M description binding site for Di-peptide 1E8 B 1101 and CYS B 797 source : AC4 21) chain B residue 790 type sequence M description binding site for Di-peptide 1E8 B 1101 and CYS B 797 source : AC4 22) chain B residue 791 type sequence Q description binding site for Di-peptide 1E8 B 1101 and CYS B 797 source : AC4 23) chain B residue 793 type sequence M description binding site for Di-peptide 1E8 B 1101 and CYS B 797 source : AC4 24) chain B residue 796 type sequence G description binding site for Di-peptide 1E8 B 1101 and CYS B 797 source : AC4 25) chain B residue 798 type sequence L description binding site for Di-peptide 1E8 B 1101 and CYS B 797 source : AC4 26) chain B residue 799 type sequence L description binding site for Di-peptide 1E8 B 1101 and CYS B 797 source : AC4 27) chain B residue 800 type sequence D description binding site for Di-peptide 1E8 B 1101 and CYS B 797 source : AC4 28) chain B residue 801 type sequence Y description binding site for Di-peptide 1E8 B 1101 and CYS B 797 source : AC4 29) chain B residue 841 type sequence R description binding site for Di-peptide 1E8 B 1101 and CYS B 797 source : AC4 30) chain B residue 843 type sequence V description binding site for Di-peptide 1E8 B 1101 and CYS B 797 source : AC4 31) chain B residue 854 type sequence T description binding site for Di-peptide 1E8 B 1101 and CYS B 797 source : AC4 32) chain B residue 855 type sequence D description binding site for Di-peptide 1E8 B 1101 and CYS B 797 source : AC4 33) chain C residue 726 type sequence V description binding site for Di-peptide 1E8 C 1101 and CYS C 797 source : AC5 34) chain C residue 743 type sequence A description binding site for Di-peptide 1E8 C 1101 and CYS C 797 source : AC5 35) chain C residue 766 type sequence M description binding site for Di-peptide 1E8 C 1101 and CYS C 797 source : AC5 36) chain C residue 790 type sequence M description binding site for Di-peptide 1E8 C 1101 and CYS C 797 source : AC5 37) chain C residue 791 type sequence Q description binding site for Di-peptide 1E8 C 1101 and CYS C 797 source : AC5 38) chain C residue 793 type sequence M description binding site for Di-peptide 1E8 C 1101 and CYS C 797 source : AC5 39) chain C residue 796 type sequence G description binding site for Di-peptide 1E8 C 1101 and CYS C 797 source : AC5 40) chain C residue 798 type sequence L description binding site for Di-peptide 1E8 C 1101 and CYS C 797 source : AC5 41) chain C residue 799 type sequence L description binding site for Di-peptide 1E8 C 1101 and CYS C 797 source : AC5 42) chain C residue 800 type sequence D description binding site for Di-peptide 1E8 C 1101 and CYS C 797 source : AC5 43) chain C residue 801 type sequence Y description binding site for Di-peptide 1E8 C 1101 and CYS C 797 source : AC5 44) chain C residue 841 type sequence R description binding site for Di-peptide 1E8 C 1101 and CYS C 797 source : AC5 45) chain C residue 843 type sequence V description binding site for Di-peptide 1E8 C 1101 and CYS C 797 source : AC5 46) chain C residue 854 type sequence T description binding site for Di-peptide 1E8 C 1101 and CYS C 797 source : AC5 47) chain C residue 855 type sequence D description binding site for Di-peptide 1E8 C 1101 and CYS C 797 source : AC5 48) chain C residue 856 type sequence F description binding site for Di-peptide 1E8 C 1101 and CYS C 797 source : AC5 49) chain D residue 726 type sequence V description binding site for Di-peptide 1E8 D 1101 and CYS D 797 source : AC6 50) chain D residue 743 type sequence A description binding site for Di-peptide 1E8 D 1101 and CYS D 797 source : AC6 51) chain D residue 745 type sequence K description binding site for Di-peptide 1E8 D 1101 and CYS D 797 source : AC6 52) chain D residue 766 type sequence M description binding site for Di-peptide 1E8 D 1101 and CYS D 797 source : AC6 53) chain D residue 790 type sequence M description binding site for Di-peptide 1E8 D 1101 and CYS D 797 source : AC6 54) chain D residue 791 type sequence Q description binding site for Di-peptide 1E8 D 1101 and CYS D 797 source : AC6 55) chain D residue 793 type sequence M description binding site for Di-peptide 1E8 D 1101 and CYS D 797 source : AC6 56) chain D residue 796 type sequence G description binding site for Di-peptide 1E8 D 1101 and CYS D 797 source : AC6 57) chain D residue 798 type sequence L description binding site for Di-peptide 1E8 D 1101 and CYS D 797 source : AC6 58) chain D residue 799 type sequence L description binding site for Di-peptide 1E8 D 1101 and CYS D 797 source : AC6 59) chain D residue 800 type sequence D description binding site for Di-peptide 1E8 D 1101 and CYS D 797 source : AC6 60) chain D residue 801 type sequence Y description binding site for Di-peptide 1E8 D 1101 and CYS D 797 source : AC6 61) chain D residue 841 type sequence R description binding site for Di-peptide 1E8 D 1101 and CYS D 797 source : AC6 62) chain D residue 843 type sequence V description binding site for Di-peptide 1E8 D 1101 and CYS D 797 source : AC6 63) chain D residue 854 type sequence T description binding site for Di-peptide 1E8 D 1101 and CYS D 797 source : AC6 64) chain D residue 855 type sequence D description binding site for Di-peptide 1E8 D 1101 and CYS D 797 source : AC6 65) chain B residue 837 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028 source Swiss-Prot : SWS_FT_FI1 66) chain A residue 837 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028 source Swiss-Prot : SWS_FT_FI1 67) chain C residue 837 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028 source Swiss-Prot : SWS_FT_FI1 68) chain D residue 837 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028 source Swiss-Prot : SWS_FT_FI1 69) chain A residue 1016 type SITE sequence Y description Important for interaction with PIK3C2B source Swiss-Prot : SWS_FT_FI6 70) chain C residue 1016 type SITE sequence Y description Important for interaction with PIK3C2B source Swiss-Prot : SWS_FT_FI6 71) chain B residue 718 type BINDING sequence L description BINDING => ECO:0000269|PubMed:19563760, ECO:0007744|PDB:2GS7, ECO:0007744|PDB:3GT8, ECO:0007744|PDB:4ZSE, ECO:0007744|PDB:5CNN, ECO:0007744|PDB:5CNO, ECO:0007744|PDB:5D41 source Swiss-Prot : SWS_FT_FI2 72) chain A residue 718 type BINDING sequence L description BINDING => ECO:0000269|PubMed:19563760, ECO:0007744|PDB:2GS7, ECO:0007744|PDB:3GT8, ECO:0007744|PDB:4ZSE, ECO:0007744|PDB:5CNN, ECO:0007744|PDB:5CNO, ECO:0007744|PDB:5D41 source Swiss-Prot : SWS_FT_FI2 73) chain C residue 718 type BINDING sequence L description BINDING => ECO:0000269|PubMed:19563760, ECO:0007744|PDB:2GS7, ECO:0007744|PDB:3GT8, ECO:0007744|PDB:4ZSE, ECO:0007744|PDB:5CNN, ECO:0007744|PDB:5CNO, ECO:0007744|PDB:5D41 source Swiss-Prot : SWS_FT_FI2 74) chain D residue 718 type BINDING sequence L description BINDING => ECO:0000269|PubMed:19563760, ECO:0007744|PDB:2GS7, ECO:0007744|PDB:3GT8, ECO:0007744|PDB:4ZSE, ECO:0007744|PDB:5CNN, ECO:0007744|PDB:5CNO, ECO:0007744|PDB:5D41 source Swiss-Prot : SWS_FT_FI2 75) chain B residue 745 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17349580, ECO:0000269|PubMed:19563760, ECO:0007744|PDB:2EB3, ECO:0007744|PDB:2GS7, ECO:0007744|PDB:2ITN, ECO:0007744|PDB:3GT8, ECO:0007744|PDB:3VJN, ECO:0007744|PDB:3VJO, ECO:0007744|PDB:4RIW, ECO:0007744|PDB:4RIY, ECO:0007744|PDB:4ZSE, ECO:0007744|PDB:5CNN, ECO:0007744|PDB:5CNO, ECO:0007744|PDB:5D41 source Swiss-Prot : SWS_FT_FI3 76) chain A residue 745 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17349580, ECO:0000269|PubMed:19563760, ECO:0007744|PDB:2EB3, ECO:0007744|PDB:2GS7, ECO:0007744|PDB:2ITN, ECO:0007744|PDB:3GT8, ECO:0007744|PDB:3VJN, ECO:0007744|PDB:3VJO, ECO:0007744|PDB:4RIW, ECO:0007744|PDB:4RIY, ECO:0007744|PDB:4ZSE, ECO:0007744|PDB:5CNN, ECO:0007744|PDB:5CNO, ECO:0007744|PDB:5D41 source Swiss-Prot : SWS_FT_FI3 77) chain C residue 745 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17349580, ECO:0000269|PubMed:19563760, ECO:0007744|PDB:2EB3, ECO:0007744|PDB:2GS7, ECO:0007744|PDB:2ITN, ECO:0007744|PDB:3GT8, ECO:0007744|PDB:3VJN, ECO:0007744|PDB:3VJO, ECO:0007744|PDB:4RIW, ECO:0007744|PDB:4RIY, ECO:0007744|PDB:4ZSE, ECO:0007744|PDB:5CNN, ECO:0007744|PDB:5CNO, ECO:0007744|PDB:5D41 source Swiss-Prot : SWS_FT_FI3 78) chain D residue 745 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17349580, ECO:0000269|PubMed:19563760, ECO:0007744|PDB:2EB3, ECO:0007744|PDB:2GS7, ECO:0007744|PDB:2ITN, ECO:0007744|PDB:3GT8, ECO:0007744|PDB:3VJN, ECO:0007744|PDB:3VJO, ECO:0007744|PDB:4RIW, ECO:0007744|PDB:4RIY, ECO:0007744|PDB:4ZSE, ECO:0007744|PDB:5CNN, ECO:0007744|PDB:5CNO, ECO:0007744|PDB:5D41 source Swiss-Prot : SWS_FT_FI3 79) chain B residue 790 type BINDING sequence M description BINDING => ECO:0000269|PubMed:17349580, ECO:0000269|PubMed:19563760, ECO:0007744|PDB:2EB3, ECO:0007744|PDB:2GS7, ECO:0007744|PDB:2ITN, ECO:0007744|PDB:2ITV, ECO:0007744|PDB:2ITX, ECO:0007744|PDB:3GT8, ECO:0007744|PDB:3VJN, ECO:0007744|PDB:3VJO, ECO:0007744|PDB:4RIW, ECO:0007744|PDB:4RIX, ECO:0007744|PDB:4RIY, ECO:0007744|PDB:4ZSE, ECO:0007744|PDB:5CNN, ECO:0007744|PDB:5CNO, ECO:0007744|PDB:5D41 source Swiss-Prot : SWS_FT_FI4 80) chain A residue 790 type BINDING sequence M description BINDING => ECO:0000269|PubMed:17349580, ECO:0000269|PubMed:19563760, ECO:0007744|PDB:2EB3, ECO:0007744|PDB:2GS7, ECO:0007744|PDB:2ITN, ECO:0007744|PDB:2ITV, ECO:0007744|PDB:2ITX, ECO:0007744|PDB:3GT8, ECO:0007744|PDB:3VJN, ECO:0007744|PDB:3VJO, ECO:0007744|PDB:4RIW, ECO:0007744|PDB:4RIX, ECO:0007744|PDB:4RIY, ECO:0007744|PDB:4ZSE, ECO:0007744|PDB:5CNN, ECO:0007744|PDB:5CNO, ECO:0007744|PDB:5D41 source Swiss-Prot : SWS_FT_FI4 81) chain C residue 790 type BINDING sequence M description BINDING => ECO:0000269|PubMed:17349580, ECO:0000269|PubMed:19563760, ECO:0007744|PDB:2EB3, ECO:0007744|PDB:2GS7, ECO:0007744|PDB:2ITN, ECO:0007744|PDB:2ITV, ECO:0007744|PDB:2ITX, ECO:0007744|PDB:3GT8, ECO:0007744|PDB:3VJN, ECO:0007744|PDB:3VJO, ECO:0007744|PDB:4RIW, ECO:0007744|PDB:4RIX, ECO:0007744|PDB:4RIY, ECO:0007744|PDB:4ZSE, ECO:0007744|PDB:5CNN, ECO:0007744|PDB:5CNO, ECO:0007744|PDB:5D41 source Swiss-Prot : SWS_FT_FI4 82) chain D residue 790 type BINDING sequence M description BINDING => ECO:0000269|PubMed:17349580, ECO:0000269|PubMed:19563760, ECO:0007744|PDB:2EB3, ECO:0007744|PDB:2GS7, ECO:0007744|PDB:2ITN, ECO:0007744|PDB:2ITV, ECO:0007744|PDB:2ITX, ECO:0007744|PDB:3GT8, ECO:0007744|PDB:3VJN, ECO:0007744|PDB:3VJO, ECO:0007744|PDB:4RIW, ECO:0007744|PDB:4RIX, ECO:0007744|PDB:4RIY, ECO:0007744|PDB:4ZSE, ECO:0007744|PDB:5CNN, ECO:0007744|PDB:5CNO, ECO:0007744|PDB:5D41 source Swiss-Prot : SWS_FT_FI4 83) chain A residue 855 type BINDING sequence D description BINDING => ECO:0000269|PubMed:17349580, ECO:0000269|PubMed:19563760, ECO:0007744|PDB:2EB3, ECO:0007744|PDB:2GS7, ECO:0007744|PDB:2ITN, ECO:0007744|PDB:2ITV, ECO:0007744|PDB:2ITX, ECO:0007744|PDB:3GT8, ECO:0007744|PDB:3VJN, ECO:0007744|PDB:4RIW, ECO:0007744|PDB:4RIX, ECO:0007744|PDB:4RIY, ECO:0007744|PDB:4ZSE, ECO:0007744|PDB:5CNN, ECO:0007744|PDB:5CNO, ECO:0007744|PDB:5D41 source Swiss-Prot : SWS_FT_FI5 84) chain B residue 855 type BINDING sequence D description BINDING => ECO:0000269|PubMed:17349580, ECO:0000269|PubMed:19563760, ECO:0007744|PDB:2EB3, ECO:0007744|PDB:2GS7, ECO:0007744|PDB:2ITN, ECO:0007744|PDB:2ITV, ECO:0007744|PDB:2ITX, ECO:0007744|PDB:3GT8, ECO:0007744|PDB:3VJN, ECO:0007744|PDB:4RIW, ECO:0007744|PDB:4RIX, ECO:0007744|PDB:4RIY, ECO:0007744|PDB:4ZSE, ECO:0007744|PDB:5CNN, ECO:0007744|PDB:5CNO, ECO:0007744|PDB:5D41 source Swiss-Prot : SWS_FT_FI5 85) chain C residue 855 type BINDING sequence D description BINDING => ECO:0000269|PubMed:17349580, ECO:0000269|PubMed:19563760, ECO:0007744|PDB:2EB3, ECO:0007744|PDB:2GS7, ECO:0007744|PDB:2ITN, ECO:0007744|PDB:2ITV, ECO:0007744|PDB:2ITX, ECO:0007744|PDB:3GT8, ECO:0007744|PDB:3VJN, ECO:0007744|PDB:4RIW, ECO:0007744|PDB:4RIX, ECO:0007744|PDB:4RIY, ECO:0007744|PDB:4ZSE, ECO:0007744|PDB:5CNN, ECO:0007744|PDB:5CNO, ECO:0007744|PDB:5D41 source Swiss-Prot : SWS_FT_FI5 86) chain D residue 855 type BINDING sequence D description BINDING => ECO:0000269|PubMed:17349580, ECO:0000269|PubMed:19563760, ECO:0007744|PDB:2EB3, ECO:0007744|PDB:2GS7, ECO:0007744|PDB:2ITN, ECO:0007744|PDB:2ITV, ECO:0007744|PDB:2ITX, ECO:0007744|PDB:3GT8, ECO:0007744|PDB:3VJN, ECO:0007744|PDB:4RIW, ECO:0007744|PDB:4RIX, ECO:0007744|PDB:4RIY, ECO:0007744|PDB:4ZSE, ECO:0007744|PDB:5CNN, ECO:0007744|PDB:5CNO, ECO:0007744|PDB:5D41 source Swiss-Prot : SWS_FT_FI5 87) chain A residue 929 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI14 88) chain A residue 970 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI14 89) chain B residue 929 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI14 90) chain B residue 970 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI14 91) chain C residue 929 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI14 92) chain C residue 970 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI14 93) chain D residue 929 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI14 94) chain D residue 970 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI14 95) chain A residue 757 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:33996800 source Swiss-Prot : SWS_FT_FI15 96) chain A residue 960 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:33996800 source Swiss-Prot : SWS_FT_FI15 97) chain B residue 757 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:33996800 source Swiss-Prot : SWS_FT_FI15 98) chain B residue 960 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:33996800 source Swiss-Prot : SWS_FT_FI15 99) chain C residue 757 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:33996800 source Swiss-Prot : SWS_FT_FI15 100) chain C residue 960 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:33996800 source Swiss-Prot : SWS_FT_FI15 101) chain D residue 757 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:33996800 source Swiss-Prot : SWS_FT_FI15 102) chain D residue 960 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:33996800 source Swiss-Prot : SWS_FT_FI15 103) chain A residue 716 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:33996800 source Swiss-Prot : SWS_FT_FI13 104) chain A residue 737 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:33996800 source Swiss-Prot : SWS_FT_FI13 105) chain C residue 716 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:33996800 source Swiss-Prot : SWS_FT_FI13 106) chain A residue 754 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:33996800 source Swiss-Prot : SWS_FT_FI13 107) chain B residue 716 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:33996800 source Swiss-Prot : SWS_FT_FI13 108) chain B residue 737 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:33996800 source Swiss-Prot : SWS_FT_FI13 109) chain C residue 737 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:33996800 source Swiss-Prot : SWS_FT_FI13 110) chain C residue 754 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:33996800 source Swiss-Prot : SWS_FT_FI13 111) chain D residue 716 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:33996800 source Swiss-Prot : SWS_FT_FI13 112) chain D residue 737 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:33996800 source Swiss-Prot : SWS_FT_FI13 113) chain D residue 754 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:33996800 source Swiss-Prot : SWS_FT_FI13 114) chain A residue 718-745 type prosite sequence LGSGAFGTVYKGLWIPEGEKVKIPVAIK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGAFGTVYkGlwipegekvkip......VAIK source prosite : PS00107 115) chain A residue 833-845 type prosite sequence LVHRDLAARNVLV description PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. LVHrDLAARNVLV source prosite : PS00109 116) chain A residue 1016 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19563760, ECO:0000269|PubMed:23774213 source Swiss-Prot : SWS_FT_FI12 117) chain C residue 1016 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19563760, ECO:0000269|PubMed:23774213 source Swiss-Prot : SWS_FT_FI12 118) chain A residue 995 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI10 119) chain B residue 995 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI10 120) chain C residue 995 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI10 121) chain D residue 995 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI10 122) chain B residue 998 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19563760, ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI11 123) chain A residue 998 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19563760, ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI11 124) chain C residue 998 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19563760, ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI11 125) chain D residue 998 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19563760, ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI11 126) chain A residue 745 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674 source Swiss-Prot : SWS_FT_FI7 127) chain B residue 745 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674 source Swiss-Prot : SWS_FT_FI7 128) chain C residue 745 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674 source Swiss-Prot : SWS_FT_FI7 129) chain D residue 745 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674 source Swiss-Prot : SWS_FT_FI7 130) chain A residue 991 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:16083266, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 131) chain B residue 991 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:16083266, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 132) chain C residue 991 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:16083266, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 133) chain D residue 991 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:16083266, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9

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