Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Proliferating cell nuclear antigen  

UniProtKB / Swiss-Prot ID :  PCNA_HUMAN

Gene Name (Synonyms) : 
PCNA  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. Note=Forms nuclear foci representing sites of ongoing DNA replication and vary in morphology and number during S phase. Together with APEX2, is redistributed in discrete nuclear foci in presence of oxidative DNA damaging agents. 

Protein Function :  This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Induces a robust stimulatory effect on the 3'- 5' exonuclease and 3'-phosphodiesterase, but not apurinic- apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2. 

Protein Sequence MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSMDSSHVSLVQLTLRSEGFDTYRCDRNLAMGV...
Predicted Secondary Structure CEEEEEECHHHHHHHHHHHHHCCCEEEEEECCCCEEEEEECCCCEEEEEEEECHHHCCEECCCCCEEEEE...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
13Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GSILKKVLE
HHHHHHHHH
38.88Phosphositeplus
Link
14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SILKKVLEA
HHHHHHHHH
48.91Phosphositeplus
Link
77Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TSMSKILKC
HHHHHHHHC
43.34Phosphositeplus
Link
77N6-acetyllysineTSMSKILKC
HHHHHHHHC
43.34HPRD
Link
77N6-acetyllysineTSMSKILKC
HHHHHHHHC
43.34Phosphositeplus
Link
77N6-acetyllysine.TSMSKILKC
HHHHHHHHC
43.34UniProtKB
Link
80Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SKILKCAGN
HHHHHCCCC
26.05Phosphositeplus
Link
80N6-acetyllysineSKILKCAGN
HHHHHCCCC
26.05HPRD
Link
80N6-acetyllysineSKILKCAGN
HHHHHCCCC
26.05Phosphositeplus
Link
80N6-acetyllysine.SKILKCAGN
HHHHHCCCC
26.05UniProtKB
Link
81S-nitrosocysteineKILKCAGNE
HHHHCCCCC
5.41dbSNO
Link
110Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PNQEKVSDY
CCCCEEEEE
36.96Phosphositeplus
Link
162S-nitrosocysteineVVISCAKDG
EEEEEECCE
3.61dbSNO
Link
164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)ISCAKDGVK
EEEECCEEE
60.38Phosphositeplus
Link
164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ISCAKDGVK
EEEECCEEE
60.38HPRD
Link
164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ISCAKDGVK
EEEECCEEE
60.38Phosphositeplus
Link
164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ISCAKDGVK
EEEECCEEE
60.38UbiProtDB
Link
164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin).ISCAKDGVK
EEEECCEEE
60.38UniProtKB
Link
181Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NGNIKLSQT
EEEEEECCC
46.19Phosphositeplus
Link
211PhosphotyrosineFALRYLNFF
ECHHHHHHH
13.57Phosphositeplus
Link
211Phosphotyrosine; by EGFR.FALRYLNFF
ECHHHHHHH
13.57UniProtKB
Link
248Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MGHLKYYLA
CCEEEEEEC
26.61Phosphositeplus
Link
248N6-acetyllysineMGHLKYYLA
CCEEEEEEC
26.61HPRD
Link
248N6-acetyllysineMGHLKYYLA
CCEEEEEEC
26.61Phosphositeplus
Link
248N6-acetyllysine.MGHLKYYLA
CCEEEEEEC
26.61UniProtKB
Link
250PhosphotyrosineHLKYYLAPK
EEEEEECCE
8.52HPRD
Link
250PhosphotyrosineHLKYYLAPK
EEEEEECCE
8.52SysPTM
Link
254Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YLAPKIEDE
EECCEECCC
53.79Phosphositeplus
Link
261PhosphoserineDEEGS
CCCCC
40.09Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
GA45A_HUMANphysical interactionMINT-15807MINT10828065
GA45A_HUMANphysical interactionMINT-15808MINT10828065
GA45A_HUMANphysical interactionMINT-15540MINT7478510
FEN1_HUMANphysical interactionMINT-14934MINT7673186
FEN1_HUMANphysical interactionMINT-14326MINT9305916
MSH6_HUMANphysical interactionMINT-15478MINT11274057
CAF1A_HUMANdirect interactionMINT-2842204MINT16826239
CDT1_HUMANphysical interactionMINT-1955474MINT16482215
CDT1_HUMANphysical interactionMINT-1955576MINT16482215
MUTYH_HUMANphysical interactionMINT-14366MINT11092888
MUTYH_HUMANphysical interactionMINT-14367MINT11092888
CDK2_HUMANphysical interaction
physical interaction
physical interaction
DIP:40110EDIP10930425
10930425
10930425
RFC4_HUMANphysical interactionDIP:40116EDIP12400013
RAD17_HUMANphysical interactionDIP:40117EDIP12400013
PCNA_HUMANphysical interactionDIP:40118EDIP8861913
FEN1_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
DIP:40119EDIP9305916
8668533
9305916
8668533
ERCC5_HUMANphysical interaction
physical interaction
DIP:40120EDIP9305916
9305916
GA45G_HUMANphysical interaction
physical interaction
physical interaction
DIP:40122EDIP11022036
11022036
11022036
ING1_HUMANphysical interaction
physical interaction
DIP:40127EDIP11682605
11682605
CAF1A_HUMANphysical interaction
physical interaction
EBI-1202911
EBI-1202904
intact15805117
15805117
DPOD1_HUMANphysical interactionEBI-1202904
intact15805117
RFC1_HUMANin vitro
in vivo
HPRD:01456HPRD12045192
12171929
8861969
8999859
RFC4_HUMANin vitro
in vivo
HPRD:01456HPRD10051561
12171929
APEX1_HUMANin vivoHPRD:01456HPRD11601988
10559261
CDN1A_HUMANin vitroHPRD:01456HPRD12964161
12930846
8861913
CDC2_HUMANin vitroHPRD:01456HPRD7949095
CDK2_HUMANin vitroHPRD:01456HPRD10930425
MSH2_HUMANin vitroHPRD:01456HPRD12171929
8858149
CDK5_HUMANin vitroHPRD:01456HPRD7949095
CCND3_HUMANin vitroHPRD:01456HPRD7908906
CCNB1_HUMANin vivoHPRD:01456HPRD8101826
GA45A_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:01456HPRD10828065
7973727
7478510
DNMT1_HUMANin vitroHPRD:01456HPRD9302295
12354094
DNL1_HUMANin vitroHPRD:01456HPRD12171929
10559261
ERCC5_HUMANin vitro
in vivo
HPRD:01456HPRD10408173
9305916
PARP1_HUMANin vivoHPRD:01456HPRD12930846
PCNA_HUMANin vitroHPRD:01456HPRD8861913
7673244
KU70_HUMANin vitro
in vivo
HPRD:01456HPRD11239001
12171929
YBOX1_HUMANin vitro
in vivo
HPRD:01456HPRD9927044
CCND1_HUMANin vitroHPRD:01456HPRD7908906
MPIP3_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:01456HPRD11896603
RFC3_HUMANin vitro
in vivo
HPRD:01456HPRD10051561
12171929
9092549
14657243
UNG_HUMANin vitroHPRD:01456HPRD10393198
12171929
DPOD1_HUMANin vitro
in vivo
HPRD:01456HPRD12171929
12403614
15805117
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Disease Reference
Kegg disease
OMIM disease
615919Ataxia-telangiectasia-like disorder 2 (ATLD2)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-77; LYS-80 AND LYS-248, ANDMASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Tyrosine phosphorylation controls PCNA function through proteinstability.";
Wang S.C., Nakajima Y., Yu Y.L., Xia W., Chen C.T., Yang C.C.,McIntush E.W., Li L.Y., Hawke D.H., Kobayashi R., Hung M.C.;
Nat. Cell Biol. 8:1359-1368(2006).
Cited for: PHOSPHORYLATION AT TYR-211 BY EGFR, MUTAGENESIS OF TYR-211, ANDINTERACTION WITH EGFR.
Ubiquitylation
ReferencePubMed
"Human SHPRH suppresses genomic instability through proliferating cellnuclear antigen polyubiquitination.";
Motegi A., Sood R., Moinova H., Markowitz S.D., Liu P.P., Myung K.;
J. Cell Biol. 175:703-708(2006).
Cited for: INTERACTION WITH SHPRH, UBIQUITINATION AT LYS-164, AND MUTAGENESIS OFLYS-164.
"Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependentpolyubiquitylation of proliferating cell nuclear antigen.";
Unk I., Hajdu I., Fatyol K., Szakal B., Blastyak A., Bermudez V.,Hurwitz J., Prakash L., Prakash S., Haracska L.;
Proc. Natl. Acad. Sci. U.S.A. 103:18107-18112(2006).
Cited for: UBIQUITINATION AT LYS-164, AND MUTAGENESIS OF LYS-164.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures