eF-site ID 6cbi-ABCDEFHIJK PDB Code 6cbi Chain A, B, C, D, E, F, H, I, J, K click to enlarge Title PCNA in complex with inhibitor Classification CELL CYCLE Compound Proliferating cell nuclear antigen Source (6CBI) Sequence A:  MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSM DSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILK CAGNEDIITLRAEDNADTLALVFEAQEKVSDYEMKLMDLD QLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCAK DGVKFSASGELGNGNIKLSQTSEEEAVTIEMNEPVQLTFA LRYLNFFTKATPLSSTVTLSMSADVPLVVEYKIADMGHLK YYLAPKIE B:  MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSM DSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILK CAGNEDIITLRAEDNADTLALVFEAQEKVSDYEMKLMDLQ LGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCAKD GVKFSASGELGNGNIKLSQTSEEEAVTIEMNEPVQLTFAL RYLNFFTKATPLSSTVTLSMSADVPLVVEYKIADMGHLKY YLAPKI C:  MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSM DSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILK CAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMD LDVEQPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCA KDGVKFSASGELGNGNIKLSQTEEEAVTIEMNEPVQLTFA LRYLNFFTKATPLSSTVTLSMSADVPLVVEYKIADMGHLK YYLAPKI D:  MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSM DSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILK CAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMD LDVLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISC AKDGVKFSASGELGNGNIKLSQTKEEEAVTIEMNEPVQLT FALRYLNFFTKATPLSSTVTLSMSADVPLVVEYKIADMGH LKYYLAPKI E:  MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSM DSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILK CAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMD LDVEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVI SCAKDGVKFSASGELGNGNIKLSQTSNVDKEEEAVTIEMN EPVQLTFALRYLNFFTKATPLSSTVTLSMSADVPLVVEYK IADMGHLKYYLAPKI F:  MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSM DSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILK CAGNEDIITLRAEDNADTLALVFEAPEKVSDYEMKLMDLD VEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISC AKDGVKFSASGELGNGNIKLSQTSNVDKEEEAVTIEMNEP VQLTFALRYLNFFTKATPLSSTVTLSMSADVPLVVEYKIA DMGHLKYYLAPKI H:  RRQXSMTEFYH I:  QXSMTEFY J:  RRQXSMTEFYH K:  RRQXSMTEFYH Description (1)  Proliferating cell nuclear antigen, GLY-ARG-LYS-ARG-ARG-GLN-DAB-SER-MET-THR-GLU-PHE-TYR-HIS Functional site 1) chain B residue 40 type sequence M description binding site for residue SO4 B 301 source : AC1 2) chain B residue 47 type sequence L description binding site for residue SO4 B 301 source : AC1 3) chain B residue 234 type sequence P description binding site for residue SO4 B 301 source : AC1 4) chain D residue 42 type sequence S description binding site for residue SO4 D 301 source : AC2 5) chain B residue 174 type sequence E description binding site for Di-peptide GLN H 144 and DAB H 145 source : AC3 6) chain C residue 45 type sequence V description binding site for Di-peptide GLN H 144 and DAB H 145 source : AC3 7) chain C residue 252 type sequence A description binding site for Di-peptide GLN H 144 and DAB H 145 source : AC3 8) chain C residue 253 type sequence P description binding site for Di-peptide GLN H 144 and DAB H 145 source : AC3 9) chain C residue 254 type sequence K description binding site for Di-peptide GLN H 144 and DAB H 145 source : AC3 10) chain H residue 143 type sequence R description binding site for Di-peptide GLN H 144 and DAB H 145 source : AC3 11) chain H residue 146 type sequence S description binding site for Di-peptide GLN H 144 and DAB H 145 source : AC3 12) chain H residue 149 type sequence E description binding site for Di-peptide GLN H 144 and DAB H 145 source : AC3 13) chain H residue 150 type sequence F description binding site for Di-peptide GLN H 144 and DAB H 145 source : AC3 14) chain C residue 44 type sequence H description binding site for Di-peptide DAB H 145 and SER H 146 source : AC4 15) chain C residue 252 type sequence A description binding site for Di-peptide DAB H 145 and SER H 146 source : AC4 16) chain C residue 253 type sequence P description binding site for Di-peptide DAB H 145 and SER H 146 source : AC4 17) chain H residue 144 type sequence Q description binding site for Di-peptide DAB H 145 and SER H 146 source : AC4 18) chain H residue 147 type sequence M description binding site for Di-peptide DAB H 145 and SER H 146 source : AC4 19) chain H residue 148 type sequence T description binding site for Di-peptide DAB H 145 and SER H 146 source : AC4 20) chain H residue 149 type sequence E description binding site for Di-peptide DAB H 145 and SER H 146 source : AC4 21) chain H residue 150 type sequence F description binding site for Di-peptide DAB H 145 and SER H 146 source : AC4 22) chain C residue 252 type sequence A description binding site for Di-peptide DAB H 145 and GLU H 149 source : AC5 23) chain C residue 253 type sequence P description binding site for Di-peptide DAB H 145 and GLU H 149 source : AC5 24) chain H residue 144 type sequence Q description binding site for Di-peptide DAB H 145 and GLU H 149 source : AC5 25) chain H residue 146 type sequence S description binding site for Di-peptide DAB H 145 and GLU H 149 source : AC5 26) chain H residue 147 type sequence M description binding site for Di-peptide DAB H 145 and GLU H 149 source : AC5 27) chain H residue 148 type sequence T description binding site for Di-peptide DAB H 145 and GLU H 149 source : AC5 28) chain H residue 150 type sequence F description binding site for Di-peptide DAB H 145 and GLU H 149 source : AC5 29) chain H residue 152 type sequence H description binding site for Di-peptide DAB H 145 and GLU H 149 source : AC5 30) chain A residue 45 type sequence V description binding site for Di-peptide GLN I 144 and DAB I 145 source : AC6 31) chain A residue 252 type sequence A description binding site for Di-peptide GLN I 144 and DAB I 145 source : AC6 32) chain A residue 253 type sequence P description binding site for Di-peptide GLN I 144 and DAB I 145 source : AC6 33) chain A residue 254 type sequence K description binding site for Di-peptide GLN I 144 and DAB I 145 source : AC6 34) chain A residue 256 type sequence E description binding site for Di-peptide GLN I 144 and DAB I 145 source : AC6 35) chain I residue 146 type sequence S description binding site for Di-peptide GLN I 144 and DAB I 145 source : AC6 36) chain I residue 149 type sequence E description binding site for Di-peptide GLN I 144 and DAB I 145 source : AC6 37) chain I residue 150 type sequence F description binding site for Di-peptide GLN I 144 and DAB I 145 source : AC6 38) chain A residue 44 type sequence H description binding site for Di-peptide DAB I 145 and SER I 146 source : AC7 39) chain A residue 252 type sequence A description binding site for Di-peptide DAB I 145 and SER I 146 source : AC7 40) chain A residue 253 type sequence P description binding site for Di-peptide DAB I 145 and SER I 146 source : AC7 41) chain I residue 144 type sequence Q description binding site for Di-peptide DAB I 145 and SER I 146 source : AC7 42) chain I residue 147 type sequence M description binding site for Di-peptide DAB I 145 and SER I 146 source : AC7 43) chain I residue 148 type sequence T description binding site for Di-peptide DAB I 145 and SER I 146 source : AC7 44) chain I residue 149 type sequence E description binding site for Di-peptide DAB I 145 and SER I 146 source : AC7 45) chain I residue 150 type sequence F description binding site for Di-peptide DAB I 145 and SER I 146 source : AC7 46) chain A residue 252 type sequence A description binding site for Di-peptide DAB I 145 and GLU I 149 source : AC8 47) chain A residue 253 type sequence P description binding site for Di-peptide DAB I 145 and GLU I 149 source : AC8 48) chain I residue 144 type sequence Q description binding site for Di-peptide DAB I 145 and GLU I 149 source : AC8 49) chain I residue 146 type sequence S description binding site for Di-peptide DAB I 145 and GLU I 149 source : AC8 50) chain I residue 147 type sequence M description binding site for Di-peptide DAB I 145 and GLU I 149 source : AC8 51) chain I residue 148 type sequence T description binding site for Di-peptide DAB I 145 and GLU I 149 source : AC8 52) chain I residue 150 type sequence F description binding site for Di-peptide DAB I 145 and GLU I 149 source : AC8 53) chain D residue 45 type sequence V description binding site for Di-peptide GLN J 144 and DAB J 145 source : AC9 54) chain D residue 252 type sequence A description binding site for Di-peptide GLN J 144 and DAB J 145 source : AC9 55) chain D residue 253 type sequence P description binding site for Di-peptide GLN J 144 and DAB J 145 source : AC9 56) chain D residue 254 type sequence K description binding site for Di-peptide GLN J 144 and DAB J 145 source : AC9 57) chain J residue 143 type sequence R description binding site for Di-peptide GLN J 144 and DAB J 145 source : AC9 58) chain J residue 146 type sequence S description binding site for Di-peptide GLN J 144 and DAB J 145 source : AC9 59) chain J residue 149 type sequence E description binding site for Di-peptide GLN J 144 and DAB J 145 source : AC9 60) chain J residue 150 type sequence F description binding site for Di-peptide GLN J 144 and DAB J 145 source : AC9 61) chain D residue 252 type sequence A description binding site for Di-peptide DAB J 145 and GLU J 149 source : AD1 62) chain D residue 253 type sequence P description binding site for Di-peptide DAB J 145 and GLU J 149 source : AD1 63) chain J residue 144 type sequence Q description binding site for Di-peptide DAB J 145 and GLU J 149 source : AD1 64) chain J residue 146 type sequence S description binding site for Di-peptide DAB J 145 and GLU J 149 source : AD1 65) chain J residue 147 type sequence M description binding site for Di-peptide DAB J 145 and GLU J 149 source : AD1 66) chain J residue 148 type sequence T description binding site for Di-peptide DAB J 145 and GLU J 149 source : AD1 67) chain J residue 150 type sequence F description binding site for Di-peptide DAB J 145 and GLU J 149 source : AD1 68) chain D residue 44 type sequence H description binding site for Di-peptide DAB J 145 and SER J 146 source : AD2 69) chain D residue 252 type sequence A description binding site for Di-peptide DAB J 145 and SER J 146 source : AD2 70) chain D residue 253 type sequence P description binding site for Di-peptide DAB J 145 and SER J 146 source : AD2 71) chain J residue 144 type sequence Q description binding site for Di-peptide DAB J 145 and SER J 146 source : AD2 72) chain J residue 147 type sequence M description binding site for Di-peptide DAB J 145 and SER J 146 source : AD2 73) chain J residue 148 type sequence T description binding site for Di-peptide DAB J 145 and SER J 146 source : AD2 74) chain J residue 149 type sequence E description binding site for Di-peptide DAB J 145 and SER J 146 source : AD2 75) chain J residue 150 type sequence F description binding site for Di-peptide DAB J 145 and SER J 146 source : AD2 76) chain E residue 45 type sequence V description binding site for Di-peptide GLN K 144 and DAB K 145 source : AD3 77) chain E residue 252 type sequence A description binding site for Di-peptide GLN K 144 and DAB K 145 source : AD3 78) chain E residue 253 type sequence P description binding site for Di-peptide GLN K 144 and DAB K 145 source : AD3 79) chain F residue 174 type sequence E description binding site for Di-peptide GLN K 144 and DAB K 145 source : AD3 80) chain K residue 143 type sequence R description binding site for Di-peptide GLN K 144 and DAB K 145 source : AD3 81) chain K residue 146 type sequence S description binding site for Di-peptide GLN K 144 and DAB K 145 source : AD3 82) chain K residue 149 type sequence E description binding site for Di-peptide GLN K 144 and DAB K 145 source : AD3 83) chain K residue 150 type sequence F description binding site for Di-peptide GLN K 144 and DAB K 145 source : AD3 84) chain E residue 252 type sequence A description binding site for Di-peptide DAB K 145 and GLU K 149 source : AD4 85) chain E residue 253 type sequence P description binding site for Di-peptide DAB K 145 and GLU K 149 source : AD4 86) chain K residue 144 type sequence Q description binding site for Di-peptide DAB K 145 and GLU K 149 source : AD4 87) chain K residue 146 type sequence S description binding site for Di-peptide DAB K 145 and GLU K 149 source : AD4 88) chain K residue 147 type sequence M description binding site for Di-peptide DAB K 145 and GLU K 149 source : AD4 89) chain K residue 148 type sequence T description binding site for Di-peptide DAB K 145 and GLU K 149 source : AD4 90) chain K residue 150 type sequence F description binding site for Di-peptide DAB K 145 and GLU K 149 source : AD4 91) chain K residue 152 type sequence H description binding site for Di-peptide DAB K 145 and GLU K 149 source : AD4 92) chain E residue 44 type sequence H description binding site for Di-peptide DAB K 145 and SER K 146 source : AD5 93) chain E residue 252 type sequence A description binding site for Di-peptide DAB K 145 and SER K 146 source : AD5 94) chain E residue 253 type sequence P description binding site for Di-peptide DAB K 145 and SER K 146 source : AD5 95) chain K residue 144 type sequence Q description binding site for Di-peptide DAB K 145 and SER K 146 source : AD5 96) chain K residue 147 type sequence M description binding site for Di-peptide DAB K 145 and SER K 146 source : AD5 97) chain K residue 148 type sequence T description binding site for Di-peptide DAB K 145 and SER K 146 source : AD5 98) chain K residue 149 type sequence E description binding site for Di-peptide DAB K 145 and SER K 146 source : AD5 99) chain K residue 150 type sequence F description binding site for Di-peptide DAB K 145 and SER K 146 source : AD5 100) chain H residue 145 type MOD_RES sequence X description Phosphothreonine; by PKA, PKB/AKT1, PIM1 and PIM2 => ECO:0000269|PubMed:10753973, ECO:0000269|PubMed:11463845, ECO:0000269|PubMed:12431783, ECO:0000269|PubMed:16982699, ECO:0000269|PubMed:20307683 source Swiss-Prot : SWS_FT_FI1 101) chain I residue 145 type MOD_RES sequence X description Phosphothreonine; by PKA, PKB/AKT1, PIM1 and PIM2 => ECO:0000269|PubMed:10753973, ECO:0000269|PubMed:11463845, ECO:0000269|PubMed:12431783, ECO:0000269|PubMed:16982699, ECO:0000269|PubMed:20307683 source Swiss-Prot : SWS_FT_FI1 102) chain J residue 145 type MOD_RES sequence X description Phosphothreonine; by PKA, PKB/AKT1, PIM1 and PIM2 => ECO:0000269|PubMed:10753973, ECO:0000269|PubMed:11463845, ECO:0000269|PubMed:12431783, ECO:0000269|PubMed:16982699, ECO:0000269|PubMed:20307683 source Swiss-Prot : SWS_FT_FI1 103) chain K residue 145 type MOD_RES sequence X description Phosphothreonine; by PKA, PKB/AKT1, PIM1 and PIM2 => ECO:0000269|PubMed:10753973, ECO:0000269|PubMed:11463845, ECO:0000269|PubMed:12431783, ECO:0000269|PubMed:16982699, ECO:0000269|PubMed:20307683 source Swiss-Prot : SWS_FT_FI1 104) chain D residue 61-80 type MOD_RES sequence RCDRNLAMGVNLTSMSKILK description Phosphothreonine; by PKA, PKB/AKT1, PIM1 and PIM2 => ECO:0000269|PubMed:10753973, ECO:0000269|PubMed:11463845, ECO:0000269|PubMed:12431783, ECO:0000269|PubMed:16982699, ECO:0000269|PubMed:20307683 source Swiss-Prot : SWS_FT_FI1 105) chain F residue 61-80 type MOD_RES sequence RCDRNLAMGVNLTSMSKILK description Phosphothreonine; by PKA, PKB/AKT1, PIM1 and PIM2 => ECO:0000269|PubMed:10753973, ECO:0000269|PubMed:11463845, ECO:0000269|PubMed:12431783, ECO:0000269|PubMed:16982699, ECO:0000269|PubMed:20307683 source Swiss-Prot : SWS_FT_FI1 106) chain H residue 146 type MOD_RES sequence S description Phosphoserine; by PKC and NUAK1 => ECO:0000269|PubMed:10753973, ECO:0000269|PubMed:25329316 source Swiss-Prot : SWS_FT_FI2 107) chain I residue 146 type MOD_RES sequence S description Phosphoserine; by PKC and NUAK1 => ECO:0000269|PubMed:10753973, ECO:0000269|PubMed:25329316 source Swiss-Prot : SWS_FT_FI2 108) chain J residue 146 type MOD_RES sequence S description Phosphoserine; by PKC and NUAK1 => ECO:0000269|PubMed:10753973, ECO:0000269|PubMed:25329316 source Swiss-Prot : SWS_FT_FI2 109) chain K residue 146 type MOD_RES sequence S description Phosphoserine; by PKC and NUAK1 => ECO:0000269|PubMed:10753973, ECO:0000269|PubMed:25329316 source Swiss-Prot : SWS_FT_FI2 110) chain D residue 14 type MOD_RES sequence K description Phosphoserine; by PKC and NUAK1 => ECO:0000269|PubMed:10753973, ECO:0000269|PubMed:25329316 source Swiss-Prot : SWS_FT_FI2 111) chain F residue 14 type MOD_RES sequence K description Phosphoserine; by PKC and NUAK1 => ECO:0000269|PubMed:10753973, ECO:0000269|PubMed:25329316 source Swiss-Prot : SWS_FT_FI2 112) chain D residue 254 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_FI6 113) chain F residue 254 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_FI6 114) chain A residue 254 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_FI6 115) chain C residue 254 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_FI6 116) chain E residue 254 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_FI6 117) chain B residue 254 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_FI6 118) chain A residue 77 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 119) chain B residue 77 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 120) chain B residue 80 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 121) chain B residue 248 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 122) chain D residue 77 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 123) chain D residue 80 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 124) chain D residue 248 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 125) chain F residue 77 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 126) chain F residue 80 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 127) chain F residue 248 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 128) chain A residue 80 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 129) chain A residue 248 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 130) chain C residue 77 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 131) chain C residue 80 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 132) chain C residue 248 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 133) chain E residue 77 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 134) chain E residue 80 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 135) chain E residue 248 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 136) chain A residue 211 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:17115032 source Swiss-Prot : SWS_FT_FI4 137) chain C residue 211 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:17115032 source Swiss-Prot : SWS_FT_FI4 138) chain E residue 211 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:17115032 source Swiss-Prot : SWS_FT_FI4 139) chain B residue 211 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:17115032 source Swiss-Prot : SWS_FT_FI4 140) chain D residue 211 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:17115032 source Swiss-Prot : SWS_FT_FI4 141) chain F residue 211 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:17115032 source Swiss-Prot : SWS_FT_FI4 142) chain A residue 164 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:17108083, ECO:0000269|PubMed:17130289 source Swiss-Prot : SWS_FT_FI5 143) chain C residue 164 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:17108083, ECO:0000269|PubMed:17130289 source Swiss-Prot : SWS_FT_FI5 144) chain E residue 164 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:17108083, ECO:0000269|PubMed:17130289 source Swiss-Prot : SWS_FT_FI5 145) chain B residue 164 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:17108083, ECO:0000269|PubMed:17130289 source Swiss-Prot : SWS_FT_FI5 146) chain D residue 164 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:17108083, ECO:0000269|PubMed:17130289 source Swiss-Prot : SWS_FT_FI5 147) chain F residue 164 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:17108083, ECO:0000269|PubMed:17130289 source Swiss-Prot : SWS_FT_FI5 148) chain A residue 61-79 type prosite sequence RCDRNLAMGVNLTSMSKIL description PCNA_2 Proliferating cell nuclear antigen signature 2. RCDRnlaMgvnLtSMsKIL source prosite : PS00293 149) chain A residue 34-57 type prosite sequence GVNLQSMDSSHVSLVQLTLRSEGF description PCNA_1 Proliferating cell nuclear antigen signature 1. GVnLqSMDsSHVsLVqLtLrsegF source prosite : PS01251

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