eF-site ID 1axc-ABCDEF
PDB Code 1axc
Chain A, B, C, D, E, F

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Title HUMAN PCNA
Classification COMPLEX (DNA-BINDING PROTEIN/DNA)
Compound PCNA
Source ORGANISM_COMMON: human; ORGANISM_SCIENTIFIC: Homo sapiens;
Sequence A:  MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSM
DSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILK
CAGNEDIITLRAEDNADTLALVFEAPEKVSDYEMKLMDLD
VEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISC
AKDGVKFSASGELGNGNIKLSQTSEEEAVTIEMNEPVQLT
FALRYLNFFTKATPLSSTVTLSMSADVPLVVEYKIADMGH
LKYYLAPKI
B:  RQTSMTDFYHSKRRLIFS
C:  MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSM
DSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILK
CAGNEDIITLRAEDNADTLALVFEAPEKVSDYEMKLMDLD
VEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISC
AKDGVKFSASGELGNGNIKLSQTEEEAVTIEMNEPVQLTF
ALRYLNFFTKATPLSSTVTLSMSADVPLVVEYKIADMGHL
KYYLAPKI
D:  RQTSMTDFYHSKRRLIFS
E:  MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSM
DSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILK
CAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMD
LDVEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVI
SCAKDGVKFSASGELGNGNIKLSQTSNVEEEAVTIEMNEP
VQLTFALRYLNFFTKATPLSSTVTLSMSADVPLVVEYKIA
DMGHLKYYLAPKI
F:  RQTSMTDFYHSKRRLIFS
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 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
3) 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
4) chain D
residue 145
type MOD_RES
sequence T
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
5) chain F
residue 145
type MOD_RES
sequence T
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
6) chain B
residue 145
type MOD_RES
sequence T
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
7) chain D
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
8) chain F
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
9) chain B
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
10) chain C
residue 77
type MOD_RES
sequence K
description Phosphoserine; by PKC; in vitro => ECO:0000269|PubMed:10753973
source Swiss-Prot : SWS_FT_FI3
11) chain C
residue 80
type MOD_RES
sequence K
description Phosphoserine; by PKC; in vitro => ECO:0000269|PubMed:10753973
source Swiss-Prot : SWS_FT_FI3
12) chain C
residue 248
type MOD_RES
sequence K
description Phosphoserine; by PKC; in vitro => ECO:0000269|PubMed:10753973
source Swiss-Prot : SWS_FT_FI3
13) chain E
residue 77
type MOD_RES
sequence K
description Phosphoserine; by PKC; in vitro => ECO:0000269|PubMed:10753973
source Swiss-Prot : SWS_FT_FI3
14) chain E
residue 80
type MOD_RES
sequence K
description Phosphoserine; by PKC; in vitro => ECO:0000269|PubMed:10753973
source Swiss-Prot : SWS_FT_FI3
15) chain E
residue 248
type MOD_RES
sequence K
description Phosphoserine; by PKC; in vitro => ECO:0000269|PubMed:10753973
source Swiss-Prot : SWS_FT_FI3
16) chain D
residue 160
type MOD_RES
sequence S
description Phosphoserine; by PKC; in vitro => ECO:0000269|PubMed:10753973
source Swiss-Prot : SWS_FT_FI3
17) chain F
residue 160
type MOD_RES
sequence S
description Phosphoserine; by PKC; in vitro => ECO:0000269|PubMed:10753973
source Swiss-Prot : SWS_FT_FI3
18) chain B
residue 160
type MOD_RES
sequence S
description Phosphoserine; by PKC; in vitro => ECO:0000269|PubMed:10753973
source Swiss-Prot : SWS_FT_FI3
19) chain A
residue 211
type MOD_RES
sequence Y
description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:17115032
source Swiss-Prot : SWS_FT_FI4
20) chain C
residue 211
type MOD_RES
sequence Y
description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:17115032
source Swiss-Prot : SWS_FT_FI4
21) chain E
residue 211
type MOD_RES
sequence Y
description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:17115032
source Swiss-Prot : SWS_FT_FI4
22) 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
23) 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
24) 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
25) chain A
residue 61-79
type prosite
sequence RCDRNLAMGVNLTSMSKIL
description PCNA_2 Proliferating cell nuclear antigen signature 2. RCDRnlaMgvnLtSMsKIL
source prosite : PS00293
26) 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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