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Protein

Proliferating cell nuclear antigen

Gene

PCNA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Plays a key role in DNA damage response (DDR) by being conveniently positioned at the replication fork to coordinate DNA replication with DNA repair and DNA damage tolerance pathways (PubMed:24939902). Acts as a loading platform to recruit DDR proteins that allow completion of DNA replication after DNA damage and promote postreplication repair: Monoubiquitinated PCNA leads to recruitment of translesion (TLS) polymerases, while 'Lys-63'-linked polyubiquitination of PCNA is involved in error-free pathway and employs recombination mechanisms to synthesize across the lesion.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi61 – 8020Sequence AnalysisAdd
BLAST

GO - Molecular functioni

  • chromatin binding Source: UniProtKB
  • damaged DNA binding Source: UniProtKB
  • dinucleotide insertion or deletion binding Source: BHF-UCL
  • DNA polymerase binding Source: UniProtKB
  • DNA polymerase processivity factor activity Source: GO_Central
  • histone acetyltransferase binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • MutLalpha complex binding Source: HGNC
  • purine-specific mismatch base pair DNA N-glycosylase activity Source: BHF-UCL
  • receptor tyrosine kinase binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair, DNA replication

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_111214. G0 and Early G1.
REACT_1287. Translesion Synthesis by POLH.
REACT_1385. Processive synthesis on the lagging strand.
REACT_1792. Polymerase switching.
REACT_1838. Leading Strand Synthesis.
REACT_1993. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
REACT_264347. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
REACT_264501. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
REACT_355158. Translesion synthesis by POLK.
REACT_355250. Termination of translesion DNA synthesis.
REACT_355324. Translesion synthesis by POLI.
REACT_355480. Recognition of DNA damage by PCNA-containing replication complex.
REACT_355510. PCNA-Dependent Long Patch Base Excision Repair.
REACT_378. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
REACT_471. E2F mediated regulation of DNA replication.
REACT_683. G1/S-Specific Transcription.
REACT_70. Removal of the Flap Intermediate.
REACT_7961. Telomere C-strand (Lagging Strand) Synthesis.
REACT_7987. Polymerase switching on the C-strand of the telomere.
REACT_7999. Removal of the Flap Intermediate from the C-strand.
REACT_8. Translesion synthesis by REV1.
REACT_8027. Processive synthesis on the C-strand of the telomere.
SignaLinkiP12004.

Names & Taxonomyi

Protein namesi
Recommended name:
Proliferating cell nuclear antigen
Short name:
PCNA
Alternative name(s):
Cyclin
Gene namesi
Name:PCNA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:8729. PCNA.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: MGI
  • cytoplasm Source: HPA
  • DNA replication factor C complex Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • nuclear replication fork Source: BHF-UCL
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • PCNA complex Source: UniProtKB
  • PCNA-p21 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Ataxia-telangiectasia-like disorder 2 (ATLD2)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA neurodegenerative disorder due to defects in DNA excision repair. ATLD2 is characterized by developmental delay, ataxia, sensorineural hearing loss, short stature, cutaneous and ocular telangiectasia, and photosensitivity.

See also OMIM:615919
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti228 – 2281S → I in ATLD2; a hypomorphic mutation affecting DNA repair in response to UV; results in significantly decreased interaction with FEN1, LIG1 and ERCC5. 1 Publication
VAR_071871

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi13 – 131K → R: Inhibits acetylation, recruitement to DNA damage sites, inducible ubiquitination and protein degradation, DNA replication and repair synthesis efficiencies, but homotrimer formation, nuclear recruitement to DNA damage sites, interactions with CREBBP, EP300 and POLD1 are similar as the wild-type; in association with R-14; R-20; R-77 and R-80. 1 Publication
Mutagenesisi14 – 141K → R: Inhibits acetylation, recruitement to DNA damage sites, inducible ubiquitination and protein degradation, DNA replication and repair synthesis efficiencies, but homotrimer formation, nuclear recruitement to DNA damage sites, interactions with CREBBP, EP300 and POLD1 are similar as the wild-type; in association with R-13; R-20; R-77 and R-80. 1 Publication
Mutagenesisi20 – 201K → R: Inhibits acetylation, recruitement to DNA damage sites, inducible ubiquitination and protein degradation, DNA replication and repair synthesis efficiencies, but homotrimer formation, nuclear recruitement to DNA damage sites, interactions with CREBBP, EP300 and POLD1 are similar as the wild-type; in association with R-13; R-14; R-77 and R-80. 1 Publication
Mutagenesisi77 – 771K → A: Inhibits recruitement to DNA damage sites, but nuclear localization is similar as the wild-type; in association with A-80. 1 Publication
Mutagenesisi77 – 771K → R: Inhibits acetylation, recruitement to DNA damage sites, inducible ubiquitination and protein degradation, DNA replication and repair synthesis efficiencies, but homotrimer formation, nuclear recruitement to DNA damage sites, interactions with CREBBP, EP300 and POLD1 are similar as the wild-type; in association with R-13; R-14; R-20 and R-80. 1 Publication
Mutagenesisi80 – 801K → A: Inhibits recruitement to DNA damage sites, but nuclear localization is similar as the wild-type; in association with A-77. 1 Publication
Mutagenesisi80 – 801K → R: Inhibits acetylation, recruitement to DNA damage sites, inducible ubiquitination and protein degradation, DNA replication and repair synthesis efficiencies, but homotrimer formation, nuclear recruitement to DNA damage sites, interactions with CREBBP, EP300 and POLD1 are similar as the wild-type; in association with R-13; R-14; R-20 and R-77. 1 Publication
Mutagenesisi164 – 1641K → R: Abolishes ubiquitination. No effect on interaction with SHPRH. 4 Publications
Mutagenesisi211 – 2111Y → F: Alters chromatin-associated PCNA stability and its function in DNA replication and repair. 1 Publication

Keywords - Diseasei

Deafness, Disease mutation, Dwarfism, Neurodegeneration

Organism-specific databases

MIMi615919. phenotype.
PharmGKBiPA263.

Polymorphism and mutation databases

BioMutaiPCNA.
DMDMi129694.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 261261Proliferating cell nuclear antigenPRO_0000149158Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141N6-acetyllysine1 Publication
Modified residuei77 – 771N6-acetyllysine1 Publication
Modified residuei80 – 801N6-acetyllysine1 Publication
Cross-linki164 – 164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
Modified residuei211 – 2111Phosphotyrosine; by EGFR1 Publication
Modified residuei248 – 2481N6-acetyllysine1 Publication

Post-translational modificationi

Phosphorylated. Phosphorylation at Tyr-211 by EGFR stabilizes chromatin-associated PCNA.1 Publication
Acetylated by CREBBP and p300/EP300; preferentially acetylated by CREBBP on Lys-80, Lys-13 and Lys-14 and on Lys-77 by p300/EP300 upon loading on chromatin in response to UV irradiation (PubMed:24939902, PubMed:19419956). Lysine acetylation disrupts association with chromatin, hence promoting PCNA ubiquitination and proteasomal degradation in response to UV damage in a CREBBP- and EP300-dependent manner (PubMed:24939902). Acetylation disrupts interaction with NUDT15 and promotes degradation (PubMed:19419956).1 Publication
Ubiquitinated (PubMed:24939902). Following DNA damage, can be either monoubiquitinated to stimulate direct bypass of DNA lesions by specialized DNA polymerases or polyubiquitinated to promote recombination-dependent DNA synthesis across DNA lesions by template switching mechanisms. Following induction of replication stress, monoubiquitinated by the UBE2B-RAD18 complex on Lys-164, leading to recruit translesion (TLS) polymerases, which are able to synthesize across DNA lesions in a potentially error-prone manner. An error-free pathway also exists and requires non-canonical polyubiquitination on Lys-164 through 'Lys-63' linkage of ubiquitin moieties by the E2 complex UBE2N-UBE2V2 and the E3 ligases, HLTF, RNF8 and SHPRH. This error-free pathway, also known as template switching, employs recombination mechanisms to synthesize across the lesion, using as a template the undamaged, newly synthesized strand of the sister chromatid. Monoubiquitination at Lys-164 also takes place in undamaged proliferating cells, and is mediated by the DCX(DTL) complex, leading to enhance PCNA-dependent translesion DNA synthesis. Sumoylated during S phase.9 Publications
Methylated on glutamate residues by ARMT1/C6orf211.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP12004.
PaxDbiP12004.
PeptideAtlasiP12004.
PRIDEiP12004.

2D gel databases

SWISS-2DPAGEP12004.

PTM databases

PhosphoSiteiP12004.

Expressioni

Gene expression databases

BgeeiP12004.
CleanExiHS_PCNA.
GenevestigatoriP12004.

Organism-specific databases

HPAiCAB000148.
HPA030521.
HPA030522.
HPA030523.

Interactioni

Subunit structurei

Homotrimer (PubMed:24939902). Interacts with p300/EP300; the interaction occurs on chromatin in UV-irradiated damaged cells (PubMed:24939902). Interacts with CREBBP (via transactivation domain and C-terminus); the interaction occurs on chromatin in UV-irradiated damaged cells (PubMed:24939902). Interacts with POLD1 (PubMed:24939902). Forms a complex with activator 1 heteropentamer in the presence of ATP. Interacts with EXO1, POLH, POLK, DNMT1, ERCC5, FEN1, CDC6 and POLDIP2. Interacts with APEX2; this interaction is triggered by reactive oxygen species and increased by misincorporation of uracil in nuclear DNA. Forms a ternary complex with DNTTIP2 and core histone. Interacts with KCTD10 and PPP1R15A. Interacts with POLD3 and POLD4. Interacts with BAZ1B; the interaction is direct. Interacts with HLTF and SHPRH. Interacts with NUDT15. Interaction is disrupted in response to UV irradiation and acetylation. Interacts with CDKN1A/p21(CIP1) and CDT1; interacts via their PIP-box which also recruits the DCX(DTL) complex. Interacts with DDX11. Interacts with EGFR; positively regulates PCNA. Interacts with PARPBP. Interacts (when ubiquitinated) with SPRTN; leading to enhance RAD18-mediated PCNA ubiquitination. Interacts (when polyubiquitinated) with ZRANB3. Interacts with SMARCAD1. Interacts with CDKN1C. Interacts with KIAA0101/PAF15 (via PIP-box). Interacts with RTEL1 (via PIP-box); the interaction is direct and essential for the suppression of telomere fragility. Interacts with FAM111A (via PIP-box); the interaction is direct and required for PCNA loading on chromatin binding. Interacts with LIG1. Interacts with SETMAR. Interacts with ANKRD17.By similarity37 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-358311,EBI-358311
Q8TE306EBI-358311,EBI-8874509
ALDOAP040753EBI-358311,EBI-709613
CDKN1AP3893615EBI-358311,EBI-375077
CDKN2AP427718EBI-358311,EBI-375053
CDT1Q9H2112EBI-358311,EBI-456953
CHAF1AQ131113EBI-358311,EBI-1020839
ENO1P067333EBI-358311,EBI-353877
FEN1P397484EBI-358311,EBI-707816
Gadd45gQ9Z1119EBI-358311,EBI-1173616From a different organism.
GAPDHP044063EBI-358311,EBI-354056
ING2Q9H1603EBI-358311,EBI-389787
MSH3P205853EBI-358311,EBI-1164205
PGAM1P186692EBI-358311,EBI-717905
POLD1P283402EBI-358311,EBI-716569
POLD3Q150544EBI-358311,EBI-864956
POLD4Q9HCU84EBI-358311,EBI-864968
TMEM218A2RU143EBI-358311,EBI-10173151
TPI1P601742EBI-358311,EBI-717475

Protein-protein interaction databases

BioGridi111142. 238 interactions.
DIPiDIP-1098N.
IntActiP12004. 54 interactions.
MINTiMINT-5000943.
STRINGi9606.ENSP00000368438.

Structurei

Secondary structure

1
261
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Helixi10 – 2011Combined sources
Beta strandi24 – 318Combined sources
Beta strandi34 – 407Combined sources
Beta strandi44 – 5310Combined sources
Helixi54 – 563Combined sources
Beta strandi57 – 648Combined sources
Beta strandi66 – 716Combined sources
Helixi72 – 798Combined sources
Beta strandi87 – 926Combined sources
Beta strandi94 – 963Combined sources
Beta strandi97 – 1048Combined sources
Beta strandi106 – 1083Combined sources
Beta strandi111 – 1177Combined sources
Beta strandi121 – 1277Combined sources
Beta strandi134 – 1407Combined sources
Helixi141 – 15212Combined sources
Beta strandi156 – 1638Combined sources
Beta strandi166 – 1738Combined sources
Beta strandi176 – 1827Combined sources
Beta strandi196 – 2016Combined sources
Beta strandi203 – 2086Combined sources
Helixi209 – 2157Combined sources
Helixi216 – 2216Combined sources
Beta strandi223 – 2297Combined sources
Beta strandi231 – 2333Combined sources
Beta strandi235 – 2417Combined sources
Turni242 – 2443Combined sources
Beta strandi245 – 2517Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AXCX-ray2.60A/C/E1-261[»]
1U76X-ray2.60A/C/E1-261[»]
1U7BX-ray1.88A1-261[»]
1UL1X-ray2.90A/B/C1-261[»]
1VYJX-ray2.80A/C/E/G/I/K1-261[»]
1VYMX-ray2.30A/B/C1-261[»]
1W60X-ray3.15A/B1-261[»]
2ZVKX-ray2.70A/B/C1-261[»]
2ZVLX-ray2.50A/B/C/D/E/F1-261[»]
2ZVMX-ray2.30A/B/C1-261[»]
3P87X-ray2.99A/B/C/D/E/F1-261[»]
3TBLX-ray2.90A/B/C1-261[»]
3VKXX-ray2.10A1-261[»]
3WGWX-ray2.80A/B1-261[»]
4D2GX-ray2.65A/B/C1-261[»]
ProteinModelPortaliP12004.
SMRiP12004. Positions 1-255.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12004.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni7 – 10094Interaction with NUDT15Add
BLAST

Sequence similaritiesi

Belongs to the PCNA family.Curated

Phylogenomic databases

eggNOGiCOG0592.
GeneTreeiENSGT00390000004965.
HOGENOMiHOG000211098.
HOVERGENiHBG000947.
InParanoidiP12004.
KOiK04802.
OMAiVTFVFES.
OrthoDBiEOG7JX34W.
PhylomeDBiP12004.
TreeFamiTF313441.

Family and domain databases

HAMAPiMF_00317. DNApol_clamp_arch.
InterProiIPR000730. Pr_cel_nuc_antig.
IPR022649. Pr_cel_nuc_antig_C.
IPR022659. Pr_cel_nuc_antig_CS.
IPR022648. Pr_cel_nuc_antig_N.
[Graphical view]
PANTHERiPTHR11352. PTHR11352. 1 hit.
PfamiPF02747. PCNA_C. 1 hit.
PF00705. PCNA_N. 1 hit.
[Graphical view]
PRINTSiPR00339. PCNACYCLIN.
TIGRFAMsiTIGR00590. pcna. 1 hit.
PROSITEiPS01251. PCNA_1. 1 hit.
PS00293. PCNA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P12004-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFEARLVQGS ILKKVLEALK DLINEACWDI SSSGVNLQSM DSSHVSLVQL
60 70 80 90 100
TLRSEGFDTY RCDRNLAMGV NLTSMSKILK CAGNEDIITL RAEDNADTLA
110 120 130 140 150
LVFEAPNQEK VSDYEMKLMD LDVEQLGIPE QEYSCVVKMP SGEFARICRD
160 170 180 190 200
LSHIGDAVVI SCAKDGVKFS ASGELGNGNI KLSQTSNVDK EEEAVTIEMN
210 220 230 240 250
EPVQLTFALR YLNFFTKATP LSSTVTLSMS ADVPLVVEYK IADMGHLKYY
260
LAPKIEDEEG S
Length:261
Mass (Da):28,769
Last modified:October 1, 1989 - v1
Checksum:iE6F08E7EDBC48B00
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti228 – 2281S → I in ATLD2; a hypomorphic mutation affecting DNA repair in response to UV; results in significantly decreased interaction with FEN1, LIG1 and ERCC5. 1 Publication
VAR_071871

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15796 mRNA. Translation: AAA35736.1.
J04718 Genomic DNA. Translation: AAA60040.1.
AF527838 Genomic DNA. Translation: AAM78556.1.
AK313286 mRNA. Translation: BAG36094.1.
AL121924 Genomic DNA. Translation: CAC27344.1.
CH471133 Genomic DNA. Translation: EAX10428.1.
CH471133 Genomic DNA. Translation: EAX10429.1.
CH471133 Genomic DNA. Translation: EAX10430.1.
BC000491 mRNA. Translation: AAH00491.1.
BC062439 mRNA. Translation: AAH62439.1.
CCDSiCCDS13087.1.
PIRiA27445. WMHUET.
RefSeqiNP_002583.1. NM_002592.2.
NP_872590.1. NM_182649.1.
UniGeneiHs.147433.
Hs.744934.

Genome annotation databases

EnsembliENST00000379143; ENSP00000368438; ENSG00000132646.
ENST00000379160; ENSP00000368458; ENSG00000132646.
GeneIDi5111.
KEGGihsa:5111.
UCSCiuc002wlp.3. human.

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

PCNA entry

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15796 mRNA. Translation: AAA35736.1.
J04718 Genomic DNA. Translation: AAA60040.1.
AF527838 Genomic DNA. Translation: AAM78556.1.
AK313286 mRNA. Translation: BAG36094.1.
AL121924 Genomic DNA. Translation: CAC27344.1.
CH471133 Genomic DNA. Translation: EAX10428.1.
CH471133 Genomic DNA. Translation: EAX10429.1.
CH471133 Genomic DNA. Translation: EAX10430.1.
BC000491 mRNA. Translation: AAH00491.1.
BC062439 mRNA. Translation: AAH62439.1.
CCDSiCCDS13087.1.
PIRiA27445. WMHUET.
RefSeqiNP_002583.1. NM_002592.2.
NP_872590.1. NM_182649.1.
UniGeneiHs.147433.
Hs.744934.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AXCX-ray2.60A/C/E1-261[»]
1U76X-ray2.60A/C/E1-261[»]
1U7BX-ray1.88A1-261[»]
1UL1X-ray2.90A/B/C1-261[»]
1VYJX-ray2.80A/C/E/G/I/K1-261[»]
1VYMX-ray2.30A/B/C1-261[»]
1W60X-ray3.15A/B1-261[»]
2ZVKX-ray2.70A/B/C1-261[»]
2ZVLX-ray2.50A/B/C/D/E/F1-261[»]
2ZVMX-ray2.30A/B/C1-261[»]
3P87X-ray2.99A/B/C/D/E/F1-261[»]
3TBLX-ray2.90A/B/C1-261[»]
3VKXX-ray2.10A1-261[»]
3WGWX-ray2.80A/B1-261[»]
4D2GX-ray2.65A/B/C1-261[»]
ProteinModelPortaliP12004.
SMRiP12004. Positions 1-255.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111142. 238 interactions.
DIPiDIP-1098N.
IntActiP12004. 54 interactions.
MINTiMINT-5000943.
STRINGi9606.ENSP00000368438.

Chemistry

BindingDBiP12004.
ChEMBLiCHEMBL2346488.

PTM databases

PhosphoSiteiP12004.

Polymorphism and mutation databases

BioMutaiPCNA.
DMDMi129694.

2D gel databases

SWISS-2DPAGEP12004.

Proteomic databases

MaxQBiP12004.
PaxDbiP12004.
PeptideAtlasiP12004.
PRIDEiP12004.

Protocols and materials databases

DNASUi5111.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379143; ENSP00000368438; ENSG00000132646.
ENST00000379160; ENSP00000368458; ENSG00000132646.
GeneIDi5111.
KEGGihsa:5111.
UCSCiuc002wlp.3. human.

Organism-specific databases

CTDi5111.
GeneCardsiGC20M005095.
HGNCiHGNC:8729. PCNA.
HPAiCAB000148.
HPA030521.
HPA030522.
HPA030523.
MIMi176740. gene.
615919. phenotype.
neXtProtiNX_P12004.
PharmGKBiPA263.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0592.
GeneTreeiENSGT00390000004965.
HOGENOMiHOG000211098.
HOVERGENiHBG000947.
InParanoidiP12004.
KOiK04802.
OMAiVTFVFES.
OrthoDBiEOG7JX34W.
PhylomeDBiP12004.
TreeFamiTF313441.

Enzyme and pathway databases

ReactomeiREACT_111214. G0 and Early G1.
REACT_1287. Translesion Synthesis by POLH.
REACT_1385. Processive synthesis on the lagging strand.
REACT_1792. Polymerase switching.
REACT_1838. Leading Strand Synthesis.
REACT_1993. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
REACT_264347. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
REACT_264501. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
REACT_355158. Translesion synthesis by POLK.
REACT_355250. Termination of translesion DNA synthesis.
REACT_355324. Translesion synthesis by POLI.
REACT_355480. Recognition of DNA damage by PCNA-containing replication complex.
REACT_355510. PCNA-Dependent Long Patch Base Excision Repair.
REACT_378. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
REACT_471. E2F mediated regulation of DNA replication.
REACT_683. G1/S-Specific Transcription.
REACT_70. Removal of the Flap Intermediate.
REACT_7961. Telomere C-strand (Lagging Strand) Synthesis.
REACT_7987. Polymerase switching on the C-strand of the telomere.
REACT_7999. Removal of the Flap Intermediate from the C-strand.
REACT_8. Translesion synthesis by REV1.
REACT_8027. Processive synthesis on the C-strand of the telomere.
SignaLinkiP12004.

Miscellaneous databases

ChiTaRSiPCNA. human.
EvolutionaryTraceiP12004.
GeneWikiiProliferating_cell_nuclear_antigen.
GenomeRNAii5111.
NextBioi19722.
PROiP12004.
SOURCEiSearch...

Gene expression databases

BgeeiP12004.
CleanExiHS_PCNA.
GenevestigatoriP12004.

Family and domain databases

HAMAPiMF_00317. DNApol_clamp_arch.
InterProiIPR000730. Pr_cel_nuc_antig.
IPR022649. Pr_cel_nuc_antig_C.
IPR022659. Pr_cel_nuc_antig_CS.
IPR022648. Pr_cel_nuc_antig_N.
[Graphical view]
PANTHERiPTHR11352. PTHR11352. 1 hit.
PfamiPF02747. PCNA_C. 1 hit.
PF00705. PCNA_N. 1 hit.
[Graphical view]
PRINTSiPR00339. PCNACYCLIN.
TIGRFAMsiTIGR00590. pcna. 1 hit.
PROSITEiPS01251. PCNA_1. 1 hit.
PS00293. PCNA_2. 1 hit.
[Graphical view]
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Publicationsi

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  1. "Cloning and sequence of the human nuclear protein cyclin: homology with DNA-binding proteins."
    Almendral J.M., Huebsch D., Blundell P.A., Macdonald-Bravo H., Bravo R.
    Proc. Natl. Acad. Sci. U.S.A. 84:1575-1579(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Structure of the human gene for the proliferating cell nuclear antigen."
    Travali S., Ku D.H., Rizzo M.G., Ottavio L., Baserga R., Calabretta B.
    J. Biol. Chem. 264:7466-7472(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. NIEHS SNPs program
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Skeletal muscle.
  5. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Bone marrow and Lung.
  8. "The cell-cycle regulated proliferating cell nuclear antigen is required for SV40 DNA replication in vitro."
    Prelich G., Kostura M., Marshak D.R., Mathews M.B., Stillman B.
    Nature 326:471-475(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-26.
  9. Lubec G., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 169-181, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  10. "The DNA repair endonuclease XPG binds to proliferating cell nuclear antigen (PCNA) and shares sequence elements with the PCNA-binding regions of FEN-1 and cyclin-dependent kinase inhibitor p21."
    Gary R., Ludwig D.L., Cornelius H.L., MacInnes M.A., Park M.S.
    J. Biol. Chem. 272:24522-24529(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ERCC5/XPG.
  11. "Human DNA-(cytosine-5) methyltransferase-PCNA complex as a target for p21WAF1."
    Chuang L.S.-H., Ian H.-I., Koh T.-W., Ng H.-H., Xu G., Li B.F.L.
    Science 277:1996-2000(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DNMT1.
  12. "Human CDC6/Cdc18 associates with Orc1 and cyclin-cdk and is selectively eliminated from the nucleus at the onset of S phase."
    Saha P., Chen J., Thome K.C., Lawlis S.J., Hou Z.H., Hendricks M., Parvin J.D., Dutta A.
    Mol. Cell. Biol. 18:2758-2767(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDC6.
  13. "Human APE2 protein is mostly localized in the nuclei and to some extent in the mitochondria, while nuclear APE2 is partly associated with proliferating cell nuclear antigen."
    Tsuchimoto D., Sakai Y., Sakumi K., Nishioka K., Sasaki M., Fujiwara T., Nakabeppu Y.
    Nucleic Acids Res. 29:2349-2360(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH APEX2.
  14. "Stimulation of DNA synthesis activity of human DNA polymerase kappa by PCNA."
    Haracska L., Unk I., Johnson R.E., Phillips B.B., Hurwitz J., Prakash L., Prakash S.
    Mol. Cell. Biol. 22:784-791(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH POLK.
  15. "Terminal deoxynucleotidyltransferase forms a ternary complex with a novel chromatin remodeling protein with 82 kDa and core histone."
    Fujita K., Shimazaki N., Ohta Y., Kubota T., Ibe S., Toji S., Tamai K., Fujisaki S., Hayano T., Koiwai O.
    Genes Cells 8:559-571(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DNTTIP2.
  16. "Identification of a novel protein, PDIP38, that interacts with the p50 subunit of DNA polymerase delta and proliferating cell nuclear antigen."
    Liu L., Rodriguez-Belmonte E.M., Mazloum N., Xie B., Lee M.Y.W.T.
    J. Biol. Chem. 278:10041-10047(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH POLDIP2.
    Tissue: Placenta.
  17. "A defined human system that supports bidirectional mismatch-provoked excision."
    Dzantiev L., Constantin N., Genschel J., Iyer R.R., Burgers P.M., Modrich P.
    Mol. Cell 15:31-41(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EXO1.
  18. "Interaction of human DNA polymerase eta with monoubiquitinated PCNA: a possible mechanism for the polymerase switch in response to DNA damage."
    Kannouche P.L., Wing J., Lehmann A.R.
    Mol. Cell 14:491-500(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, INTERACTION WITH POLH.
  19. "The Williams syndrome transcription factor interacts with PCNA to target chromatin remodelling by ISWI to replication foci."
    Poot R.A., Bozhenok L., van den Berg D.L.C., Steffensen S., Ferreira F., Grimaldi M., Gilbert N., Ferreira J., Varga-Weisz P.D.
    Nat. Cell Biol. 6:1236-1244(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BAZ1B.
  20. "Functional roles of p12, the fourth subunit of human DNA polymerase delta."
    Li H., Xie B., Zhou Y., Rahmeh A., Trusa S., Zhang S., Gao Y., Lee E.Y., Lee M.Y.
    J. Biol. Chem. 281:14748-14755(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH POLD1; POLD3 AND POLD4.
  21. "Human SHPRH suppresses genomic instability through proliferating cell nuclear antigen polyubiquitination."
    Motegi A., Sood R., Moinova H., Markowitz S.D., Liu P.P., Myung K.
    J. Cell Biol. 175:703-708(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SHPRH, UBIQUITINATION AT LYS-164, MUTAGENESIS OF LYS-164.
  22. "A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdt1."
    Jin J., Arias E.E., Chen J., Harper J.W., Walter J.C.
    Mol. Cell 23:709-721(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDT1.
  23. Cited for: PHOSPHORYLATION AT TYR-211 BY EGFR, MUTAGENESIS OF TYR-211, INTERACTION WITH EGFR.
  24. "Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent polyubiquitylation 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-164, MUTAGENESIS OF LYS-164.
  25. "PCNA is ubiquitinated by RNF8."
    Zhang S., Chea J., Meng X., Zhou Y., Lee E.Y.C., Lee M.Y.W.T.
    Cell Cycle 7:3399-3404(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  26. "PCNA-dependent regulation of p21 ubiquitylation and degradation via the CRL4Cdt2 ubiquitin ligase complex."
    Abbas T., Sivaprasad U., Terai K., Amador V., Pagano M., Dutta A.
    Genes Dev. 22:2496-2506(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDKN1A.
  27. "Studies with the human cohesin establishment factor, ChlR1. Association of ChlR1 with Ctf18-RFC and Fen1."
    Farina A., Shin J.H., Kim D.H., Bermudez V.P., Kelman Z., Seo Y.S., Hurwitz J.
    J. Biol. Chem. 283:20925-20936(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDX11.
  28. "CDK inhibitor p21 is degraded by a proliferating cell nuclear antigen-coupled Cul4-DDB1Cdt2 pathway during S phase and after UV irradiation."
    Nishitani H., Shiomi Y., Iida H., Michishita M., Takami T., Tsurimoto T.
    J. Biol. Chem. 283:29045-29052(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDKN1A.
  29. "Role of PCNA-dependent stimulation of 3'-phosphodiesterase and 3'-5' exonuclease activities of human Ape2 in repair of oxidative DNA damage."
    Burkovics P., Hajdu I., Szukacsov V., Unk I., Haracska L.
    Nucleic Acids Res. 37:4247-4255(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH APEX2.
  30. "Human HLTF functions as a ubiquitin ligase for proliferating cell nuclear antigen polyubiquitination."
    Unk I., Hajdu I., Fatyol K., Hurwitz J., Yoon J.-H., Prakash L., Prakash S., Haracska L.
    Proc. Natl. Acad. Sci. U.S.A. 105:3768-3773(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, INTERACTION WITH HLTF.
  31. "Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks."
    Motegi A., Liaw H.-J., Lee K.-Y., Roest H.P., Maas A., Wu X., Moinova H., Markowitz S.D., Ding H., Hoeijmakers J.H.J., Myung K.
    Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, FUNCTION, INTERACTION WITH HLTF AND SHPRH, MUTAGENESIS OF LYS-164.
  32. "Proliferating cell nuclear antigen is protected from degradation by forming a complex with MutT Homolog2."
    Yu Y., Cai J.-P., Tu B., Wu L., Zhao Y., Liu X., Li L., McNutt M.A., Feng J., He Q., Yang Y., Wang H., Sekiguchi M., Zhu W.-G.
    J. Biol. Chem. 284:19310-19320(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NUDT15, ACETYLATION AT LYS-14.
  33. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-77; LYS-80 AND LYS-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  34. "CRL4(Cdt2) E3 ubiquitin ligase monoubiquitinates PCNA to promote translesion DNA synthesis."
    Terai K., Abbas T., Jazaeri A.A., Dutta A.
    Mol. Cell 37:143-149(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, MUTAGENESIS OF LYS-164.
  35. Cited for: INTERACTION WITH SETMAR.
  36. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  37. "Maintenance of silent chromatin through replication requires SWI/SNF-like chromatin remodeler SMARCAD1."
    Rowbotham S.P., Barki L., Neves-Costa A., Santos F., Dean W., Hawkes N., Choudhary P., Will W.R., Webster J., Oxley D., Green C.M., Varga-Weisz P., Mermoud J.E.
    Mol. Cell 42:285-296(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SMARCAD1.
  38. "Proliferating cell nuclear antigen (PCNA)-associated KIAA0101/PAF15 protein is a cell cycle-regulated anaphase-promoting complex/cyclosome substrate."
    Emanuele M.J., Ciccia A., Elia A.E., Elledge S.J.
    Proc. Natl. Acad. Sci. U.S.A. 108:9845-9850(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KIAA0101.
  39. "Inhibition of homologous recombination by the PCNA-interacting protein PARI."
    Moldovan G.L., Dejsuphong D., Petalcorin M.I., Hofmann K., Takeda S., Boulton S.J., D'Andrea A.D.
    Mol. Cell 45:75-86(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PARPBP, SUMOYLATION.
  40. "Spartan/C1orf124, a reader of PCNA ubiquitylation and a regulator of UV-induced DNA damage response."
    Centore R.C., Yazinski S.A., Tse A., Zou L.
    Mol. Cell 46:625-635(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPRTN.
  41. "ZRANB3 is a structure-specific ATP-dependent endonuclease involved in replication stress response."
    Weston R., Peeters H., Ahel D.
    Genes Dev. 26:1558-1572(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZRANB3.
  42. "The HARP-like domain-containing protein AH2/ZRANB3 binds to PCNA and participates in cellular response to replication stress."
    Yuan J., Ghosal G., Chen J.
    Mol. Cell 47:410-421(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZRANB3.
  43. "Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass."
    Povlsen L.K., Beli P., Wagner S.A., Poulsen S.L., Sylvestersen K.B., Poulsen J.W., Nielsen M.L., Bekker-Jensen S., Mailand N., Choudhary C.
    Nat. Cell Biol. 14:1089-1098(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KIAA0101.
  44. "Polyubiquitinated PCNA recruits the ZRANB3 translocase to maintain genomic integrity after replication stress."
    Ciccia A., Nimonkar A.V., Hu Y., Hajdu I., Achar Y.J., Izhar L., Petit S.A., Adamson B., Yoon J.C., Kowalczykowski S.C., Livingston D.M., Haracska L., Elledge S.J.
    Mol. Cell 47:396-409(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZRANB3.
  45. Cited for: INTERACTION WITH CDKN1C.
  46. "A role for the Ankyrin repeat containing protein Ankrd17 in Nod1- and Nod2-mediated inflammatory responses."
    Menning M., Kufer T.A.
    FEBS Lett. 587:2137-2142(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ANKRD17.
  47. "RTEL1 is a replisome-associated helicase that promotes telomere and genome-wide replication."
    Vannier J.B., Sandhu S., Petalcorin M.I., Wu X., Nabi Z., Ding H., Boulton S.J.
    Science 342:239-242(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RTEL1, SUBCELLULAR LOCATION.
  48. Cited for: INVOLVEMENT IN ATLD2, INTERACTION WITH FEN1; LIG1 AND ERCC5, VARIANT ATLD2 ILE-228, CHARACTERIZATION OF VARIANT ATDL2 ILE-228.
  49. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  50. "Nascent chromatin capture proteomics determines chromatin dynamics during DNA replication and identifies unknown fork components."
    Alabert C., Bukowski-Wills J.C., Lee S.B., Kustatscher G., Nakamura K., de Lima Alves F., Menard P., Mejlvang J., Rappsilber J., Groth A.
    Nat. Cell Biol. 16:281-293(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FAM111A.
  51. "CBP and p300 acetylate PCNA to link its degradation with nucleotide excision repair synthesis."
    Cazzalini O., Sommatis S., Tillhon M., Dutto I., Bachi A., Rapp A., Nardo T., Scovassi A.I., Necchi D., Cardoso M.C., Stivala L.A., Prosperi E.
    Nucleic Acids Res. 42:8433-8448(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, INTERACTION WITH CREBBP; EP300 AND POLD1, ACETYLATION, UBIQUITINATION, ASSOCIATION WITH CHROMATIN, MUTAGENESIS OF LYS-13; LYS-14; LYS-20; LYS-77 AND LYS-80.
  52. "Human C6orf211 encodes Armt1, a protein carboxyl methyltransferase that targets PCNA and is linked to the DNA damage response."
    Perry J.J., Ballard G.D., Albert A.E., Dobrolecki L.E., Malkas L.H., Hoelz D.J.
    Cell Rep. 10:1288-1296(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION.
  53. "Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA."
    Gulbis J.M., Kelman Z., Hurwitz J., O'Donnell M., Kuriyan J.
    Cell 87:297-306(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
  54. "Structural basis for recruitment of human flap endonuclease 1 to PCNA."
    Sakurai S., Kitano K., Yamaguchi H., Hamada K., Okada K., Fukuda K., Uchida M., Ohtsuka E., Morioka H., Hakoshima T.
    EMBO J. 24:683-693(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH FEN1.

Entry informationi

Entry nameiPCNA_HUMAN
AccessioniPrimary (citable) accession number: P12004
Secondary accession number(s): B2R897, D3DW02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: May 27, 2015
This is version 179 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Antibodies against PCNA are present in sera from patients with systemic lupus erythematosus.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.