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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
  • enzyme binding Source: BHF-UCL
  • 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

ReactomeiR-HSA-110312. Translesion synthesis by REV1.
R-HSA-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-HSA-110320. Translesion Synthesis by POLH.
R-HSA-113510. E2F mediated regulation of DNA replication.
R-HSA-1538133. G0 and Early G1.
R-HSA-174411. Polymerase switching on the C-strand of the telomere.
R-HSA-174414. Processive synthesis on the C-strand of the telomere.
R-HSA-174417. Telomere C-strand (Lagging Strand) Synthesis.
R-HSA-174437. Removal of the Flap Intermediate from the C-strand.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-5358565. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
R-HSA-5358606. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
R-HSA-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-HSA-5655862. Translesion synthesis by POLK.
R-HSA-5656121. Translesion synthesis by POLI.
R-HSA-5656169. Termination of translesion DNA synthesis.
R-HSA-5685942. HDR through Homologous Recombination (HRR).
R-HSA-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-HSA-5696400. Dual Incision in GG-NER.
R-HSA-6782135. Dual incision in TC-NER.
R-HSA-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-HSA-6804114. TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
R-HSA-69091. Polymerase switching.
R-HSA-69109. Leading Strand Synthesis.
R-HSA-69166. Removal of the Flap Intermediate.
R-HSA-69183. Processive synthesis on the lagging strand.
R-HSA-69205. G1/S-Specific Transcription.
SignaLinkiP12004.
SIGNORiP12004.

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
Proteomesi
  • UP000005640 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 chromosome, telomeric region Source: BHF-UCL
  • nuclear replication fork Source: BHF-UCL
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • PCNA complex Source: UniProtKB
  • PCNA-p21 complex Source: UniProtKB
  • replisome Source: BHF-UCL
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
Corresponds to variant rs369958038 [ dbSNP | Ensembl ].
VAR_071871

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi13 – 131K → R: Inhibits acetylation, recruitment to DNA damage sites, inducible ubiquitination and protein degradation, DNA replication and repair synthesis efficiencies, but homotrimer formation, nuclear recruitment 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, recruitment to DNA damage sites, inducible ubiquitination and protein degradation, DNA replication and repair synthesis efficiencies, but homotrimer formation, nuclear recruitment 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, recruitment to DNA damage sites, inducible ubiquitination and protein degradation, DNA replication and repair synthesis efficiencies, but homotrimer formation, nuclear recruitment 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 recruitment 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, recruitment to DNA damage sites, inducible ubiquitination and protein degradation, DNA replication and repair synthesis efficiencies, but homotrimer formation, nuclear recruitment 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 recruitment 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, recruitment to DNA damage sites, inducible ubiquitination and protein degradation, DNA replication and repair synthesis efficiencies, but homotrimer formation, nuclear recruitment 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

MalaCardsiPCNA.
MIMi615919. phenotype.
PharmGKBiPA263.

Chemistry

ChEMBLiCHEMBL2346488.

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-acetyllysineCombined sources
Modified residuei80 – 801N6-acetyllysineCombined sources
Cross-linki164 – 164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki164 – 164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate2 Publications
Modified residuei211 – 2111Phosphotyrosine; by EGFR1 Publication
Modified residuei248 – 2481N6-acetyllysineCombined sources

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

EPDiP12004.
MaxQBiP12004.
PaxDbiP12004.
PeptideAtlasiP12004.
PRIDEiP12004.
TopDownProteomicsiP12004.

2D gel databases

SWISS-2DPAGEP12004.

PTM databases

iPTMnetiP12004.
PhosphoSiteiP12004.
SwissPalmiP12004.

Expressioni

Gene expression databases

BgeeiENSG00000132646.
CleanExiHS_PCNA.
GenevisibleiP12004. HS.

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 (Ref. 6, PubMed:9305916, PubMed:9302295, PubMed:11784855, PubMed:12522211, PubMed:15225546, PubMed:24911150). Interacts with APEX2; this interaction is triggered by reactive oxygen species and increased by misincorporation of uracil in nuclear DNA (PubMed:11376153, PubMed:19443450). Forms a ternary complex with DNTTIP2 and core histone (PubMed:12786946). Interacts with KCTD10 and PPP1R15A (By similarity). Interacts with POLD3 and POLD4 (PubMed:16510448). Interacts with BAZ1B; the interaction is direct (PubMed:15543136). Interacts with HLTF and SHPRH (PubMed:17130289, PubMed:18719106). Interacts with NUDT15 (PubMed:19419956). Interaction is disrupted in response to UV irradiation and acetylation (PubMed:19419956). Interacts with CDKN1A/p21(CIP1) and CDT1; interacts via their PIP-box which also recruits the DCX(DTL) complex (PubMed:16949367). Interacts with DDX11 (PubMed:18499658). Interacts with EGFR; positively regulates PCNA (PubMed:17115032). Interacts with PARPBP (PubMed:22153967). Interacts (when ubiquitinated) with SPRTN; leading to enhance RAD18-mediated PCNA ubiquitination (PubMed:22681887). Interacts (when polyubiquitinated) with ZRANB3 (PubMed:22704558, PubMed:22705370, PubMed:22759634). Interacts with SMARCAD1 (PubMed:21549307). Interacts with CDKN1C (PubMed:22634751). Interacts with KIAA0101/PAF15 (via PIP-box) (PubMed:21628590, PubMed:23000965). Interacts with RTEL1 (via PIP-box); the interaction is direct and essential for the suppression of telomere fragility (PubMed:24115439). Interacts with FAM111A (via PIP-box); the interaction is direct and required for PCNA loading on chromatin binding (PubMed:24561620). Interacts with LIG1 (PubMed:24911150). Interacts with SETMAR (PubMed:20457750). Interacts with ANKRD17 (PubMed:23711367). Interacts with FBXO18/FBH1 (via PIP-box); the interaction recruits the DCX(DTL) complex and promotes ubiquitination and degradation of FBXO18/FBH1 (PubMed:23677613).By similarity38 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-358311,EBI-358311
Q8TE306EBI-358311,EBI-8874509
ALDOAP040753EBI-358311,EBI-709613
CDKN1AP3893624EBI-358311,EBI-375077
CDKN2AP427718EBI-358311,EBI-375053
CDT1Q9H2112EBI-358311,EBI-456953
CHAF1AQ131114EBI-358311,EBI-1020839
ENO1P067333EBI-358311,EBI-353877
FEN1P397486EBI-358311,EBI-707816
Gadd45gQ9Z1119EBI-358311,EBI-1173616From a different organism.
GAPDHP044063EBI-358311,EBI-354056
ING2Q9H1603EBI-358311,EBI-389787
MSH3P205853EBI-358311,EBI-1164205
PB1B4URF52EBI-358311,EBI-6050669From a different organism.
PB2B4URF72EBI-358311,EBI-6050648From a different organism.
PGAM1P186692EBI-358311,EBI-717905
POLD1P283403EBI-358311,EBI-716569
POLD2P490052EBI-358311,EBI-372354
POLD3Q150545EBI-358311,EBI-864956
POLD4Q9HCU84EBI-358311,EBI-864968
TMEM218A2RU143EBI-358311,EBI-10173151
TPI1P601742EBI-358311,EBI-717475

GO - Molecular functioni

  • DNA polymerase binding Source: UniProtKB
  • enzyme binding Source: BHF-UCL
  • histone acetyltransferase binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • MutLalpha complex binding Source: HGNC
  • receptor tyrosine kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111142. 284 interactions.
DIPiDIP-1098N.
IntActiP12004. 103 interactions.
MINTiMINT-5000943.
STRINGi9606.ENSP00000368438.

Chemistry

BindingDBiP12004.

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 – 1094Combined sources
Beta strandi111 – 1177Combined sources
Beta strandi121 – 1266Combined sources
Beta strandi134 – 1407Combined sources
Helixi141 – 15212Combined sources
Beta strandi156 – 1638Combined sources
Beta strandi166 – 1738Combined sources
Beta strandi176 – 1827Combined sources
Helixi191 – 1933Combined 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[»]
3JA9electron microscopy22.00A/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[»]
4RJFX-ray2.01A/C/E1-261[»]
4ZTDX-ray2.20A/B/C2-254[»]
5E0TX-ray2.67A/B/C1-261[»]
5E0UX-ray1.93A/B/C1-261[»]
5E0VX-ray2.07A/B1-261[»]
5IY4X-ray2.94A/C/E1-261[»]
ProteinModelPortaliP12004.
SMRiP12004. Positions 1-255.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12004.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni7 – 10094Interaction with NUDT151 PublicationAdd
BLAST

Sequence similaritiesi

Belongs to the PCNA family.Curated

Phylogenomic databases

eggNOGiKOG1636. Eukaryota.
COG0592. LUCA.
GeneTreeiENSGT00390000004965.
HOGENOMiHOG000211098.
HOVERGENiHBG000947.
InParanoidiP12004.
KOiK04802.
OMAiSDGFDKY.
OrthoDBiEOG091G0GQ7.
PhylomeDBiP12004.
TreeFamiTF313441.

Family and domain databases

HAMAPiMF_00317. DNApol_clamp_arch. 1 hit.
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
Corresponds to variant rs369958038 [ dbSNP | Ensembl ].
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.4. 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[»]
3JA9electron microscopy22.00A/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[»]
4RJFX-ray2.01A/C/E1-261[»]
4ZTDX-ray2.20A/B/C2-254[»]
5E0TX-ray2.67A/B/C1-261[»]
5E0UX-ray1.93A/B/C1-261[»]
5E0VX-ray2.07A/B1-261[»]
5IY4X-ray2.94A/C/E1-261[»]
ProteinModelPortaliP12004.
SMRiP12004. Positions 1-255.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111142. 284 interactions.
DIPiDIP-1098N.
IntActiP12004. 103 interactions.
MINTiMINT-5000943.
STRINGi9606.ENSP00000368438.

Chemistry

BindingDBiP12004.
ChEMBLiCHEMBL2346488.

PTM databases

iPTMnetiP12004.
PhosphoSiteiP12004.
SwissPalmiP12004.

Polymorphism and mutation databases

BioMutaiPCNA.
DMDMi129694.

2D gel databases

SWISS-2DPAGEP12004.

Proteomic databases

EPDiP12004.
MaxQBiP12004.
PaxDbiP12004.
PeptideAtlasiP12004.
PRIDEiP12004.
TopDownProteomicsiP12004.

Protocols and materials databases

DNASUi5111.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379143; ENSP00000368438; ENSG00000132646.
ENST00000379160; ENSP00000368458; ENSG00000132646.
GeneIDi5111.
KEGGihsa:5111.
UCSCiuc002wlp.4. human.

Organism-specific databases

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

Phylogenomic databases

eggNOGiKOG1636. Eukaryota.
COG0592. LUCA.
GeneTreeiENSGT00390000004965.
HOGENOMiHOG000211098.
HOVERGENiHBG000947.
InParanoidiP12004.
KOiK04802.
OMAiSDGFDKY.
OrthoDBiEOG091G0GQ7.
PhylomeDBiP12004.
TreeFamiTF313441.

Enzyme and pathway databases

ReactomeiR-HSA-110312. Translesion synthesis by REV1.
R-HSA-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-HSA-110320. Translesion Synthesis by POLH.
R-HSA-113510. E2F mediated regulation of DNA replication.
R-HSA-1538133. G0 and Early G1.
R-HSA-174411. Polymerase switching on the C-strand of the telomere.
R-HSA-174414. Processive synthesis on the C-strand of the telomere.
R-HSA-174417. Telomere C-strand (Lagging Strand) Synthesis.
R-HSA-174437. Removal of the Flap Intermediate from the C-strand.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-5358565. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
R-HSA-5358606. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
R-HSA-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-HSA-5655862. Translesion synthesis by POLK.
R-HSA-5656121. Translesion synthesis by POLI.
R-HSA-5656169. Termination of translesion DNA synthesis.
R-HSA-5685942. HDR through Homologous Recombination (HRR).
R-HSA-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-HSA-5696400. Dual Incision in GG-NER.
R-HSA-6782135. Dual incision in TC-NER.
R-HSA-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-HSA-6804114. TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
R-HSA-69091. Polymerase switching.
R-HSA-69109. Leading Strand Synthesis.
R-HSA-69166. Removal of the Flap Intermediate.
R-HSA-69183. Processive synthesis on the lagging strand.
R-HSA-69205. G1/S-Specific Transcription.
SignaLinkiP12004.
SIGNORiP12004.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000132646.
CleanExiHS_PCNA.
GenevisibleiP12004. HS.

Family and domain databases

HAMAPiMF_00317. DNApol_clamp_arch. 1 hit.
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]
ProtoNetiSearch...

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: September 7, 2016
This is version 193 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

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 one 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.