eF-site ID 3p87-ABCDEFGHIJKL PDB Code 3p87 Chain A, B, C, D, E, F, G, H, I, J, K, L click to enlarge Title Structure of human PCNA bound to RNASEH2B PIP box peptide Classification HYDROLASE/DNA BINDING PROTEIN Compound Proliferating cell nuclear antigen Source null (RNH2B_HUMAN) Sequence A:  MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSM DSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILK CAGNEDIITLRAEDDTLALVFEAPNQEKVSDYEMKLMDLD VEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISC AKDGVKFSASGELGNGNIKLSQAVTIEMNEPVQLTFALRY LNFFTKATPLSSTVTLSMSADVPLVVEYKIADMGHLKYYL APKIE B:  MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSM DSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILK CAGNEDIITLRAEDDTLALVFEAPNQEKVSDYEMKLMDLD VEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISC AKDGVKFSASGELGNGNIKLSQAVTIEMNEPVQLTFALRY LNFFTKATPLSSTVTLSMSADVPLVVEYKIADMGHLKYYL APKIE C:  MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSM DSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILK CAGNEDIITLRAEDDTLALVFEAPNQEKVSDYEMKLMDLD VEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISC AKDGVKFSASGELGNGNIKLSQAVTIEMNEPVQLTFALRY LNFFTKATPLSSTVTLSMSADVPLVVEYKIADMGHLKYYL APKIE D:  MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSM DSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILK CAGNEDIITLRAEDDTLALVFEAPNQEKVSDYEMKLMDLD VEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISC AKDGVKFSASGELGNGNIKLSQAVTIEMNEPVQLTFALRY LNFFTKATPLSSTVTLSMSADVPLVVEYKIADMGHLKYYL APKIE E:  MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSM DSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILK CAGNEDIITLRAEDDTLALVFEAPNQEKVSDYEMKLMDLD VEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISC AKDGVKFSASGELGNGNIKLSQAVTIEMNEPVQLTFALRY LNFFTKATPLSSTVTLSMSADVPLVVEYKIADMGHLKYYL APKIE F:  MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSM DSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILK CAGNEDIITLRAEDDTLALVFEAPNQEKVSDYEMKLMDLD VEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISC AKDGVKFSASGELGNGNIKLSQAVTIEMNEPVQLTFALRY LNFFTKATPLSSTVTLSMSADVPLVVEYKIADMGHLKYYL APKIE G:  KSGMKSIDTFF H:  DKSGMKSIDTFF I:  DKSGMKSIDTFF J:  KSGMKSIDTFF K:  DKSGMKSIDTFF L:  KSGMKSIDTFF Description Functional site 1) 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 2) 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 3) 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 4) 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 5) 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 6) 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 7) chain H residue 295 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI1 8) chain I residue 295 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI1 9) chain J residue 295 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI1 10) chain K residue 295 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI1 11) chain L residue 295 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI1 12) chain G residue 295 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI1 13) chain H residue 296 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 14) chain I residue 296 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 15) chain J residue 296 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 16) chain K residue 296 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 17) chain L residue 296 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 18) chain G residue 296 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 19) chain C residue 77 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 20) chain C residue 80 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 21) chain C residue 248 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 22) chain D residue 77 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 23) chain D residue 80 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 24) chain D residue 248 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 25) chain E residue 77 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 26) chain E residue 80 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 27) chain E residue 248 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 28) chain F residue 77 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 29) chain F residue 80 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 30) chain F residue 248 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 31) chain A residue 77 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 32) chain A residue 80 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 33) chain A residue 248 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 34) chain B residue 77 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 35) chain B residue 80 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 36) chain B residue 248 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 37) chain A residue 211 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:17115032 source Swiss-Prot : SWS_FT_FI4 38) chain B residue 211 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:17115032 source Swiss-Prot : SWS_FT_FI4 39) chain C residue 211 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:17115032 source Swiss-Prot : SWS_FT_FI4 40) chain D residue 211 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:17115032 source Swiss-Prot : SWS_FT_FI4 41) chain E residue 211 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:17115032 source Swiss-Prot : SWS_FT_FI4 42) chain F residue 211 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:17115032 source Swiss-Prot : SWS_FT_FI4 43) 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 44) 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 45) 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 46) 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 47) 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 48) 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 49) chain A residue 61-79 type prosite sequence RCDRNLAMGVNLTSMSKIL description PCNA_2 Proliferating cell nuclear antigen signature 2. RCDRnlaMgvnLtSMsKIL source prosite : PS00293 50) 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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