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P12004

- PCNA_HUMAN

UniProt

P12004 - PCNA_HUMAN

Protein

Proliferating cell nuclear antigen

Gene

PCNA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 171 (01 Oct 2014)
      Sequence version 1 (01 Oct 1989)
      Previous versions | rss
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    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. 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.2 Publications

    Regions

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

    GO - Molecular functioni

    1. dinucleotide insertion or deletion binding Source: BHF-UCL
    2. DNA polymerase binding Source: UniProt
    3. DNA polymerase processivity factor activity Source: InterPro
    4. identical protein binding Source: IntAct
    5. MutLalpha complex binding Source: HGNC
    6. protein binding Source: UniProtKB
    7. purine-specific mismatch base pair DNA N-glycosylase activity Source: BHF-UCL
    8. receptor tyrosine kinase binding Source: UniProtKB

    GO - Biological processi

    1. base-excision repair Source: Reactome
    2. cell proliferation Source: ProtInc
    3. DNA repair Source: UniProtKB
    4. DNA replication Source: UniProtKB
    5. DNA strand elongation involved in DNA replication Source: Reactome
    6. epithelial cell differentiation Source: UniProt
    7. G1/S transition of mitotic cell cycle Source: Reactome
    8. heart development Source: Ensembl
    9. leading strand elongation Source: RefGenome
    10. mismatch repair Source: BHF-UCL
    11. mitotic cell cycle Source: Reactome
    12. nucleotide-excision repair Source: Reactome
    13. nucleotide-excision repair, DNA gap filling Source: Reactome
    14. phosphatidylinositol-mediated signaling Source: UniProtKB
    15. positive regulation of deoxyribonuclease activity Source: UniProtKB
    16. regulation of DNA replication Source: InterPro
    17. regulation of transcription involved in G1/S transition of mitotic cell cycle Source: Reactome
    18. response to cadmium ion Source: Ensembl
    19. response to lipid Source: Ensembl
    20. telomere maintenance Source: Reactome
    21. telomere maintenance via recombination Source: Reactome
    22. telomere maintenance via semi-conservative replication Source: Reactome
    23. transcription-coupled nucleotide-excision repair Source: Reactome
    24. translesion synthesis Source: UniProtKB

    Keywords - Biological processi

    DNA damage, DNA repair, DNA replication

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_111214. G0 and Early G1.
    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_2192. Removal of DNA patch containing abasic residue.
    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_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: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:8729. PCNA.

    Subcellular locationi

    Nucleus 1 Publication
    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.

    GO - Cellular componenti

    1. centrosome Source: MGI
    2. cytoplasm Source: HPA
    3. DNA replication factor C complex Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProt
    5. nuclear replication fork Source: BHF-UCL
    6. nucleoplasm Source: Reactome
    7. nucleus Source: HPA
    8. PCNA complex Source: RefGenome
    9. PCNA-p21 complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    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

    Organism-specific databases

    PharmGKBiPA263.

    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

    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.8 Publications
    Acetylated in response to UV irradiation. Acetylation disrupts interaction with NUDT15 and promotes degradation.2 Publications
    Phosphorylated. Phosphorylation at Tyr-211 by EGFR stabilizes chromatin-associated PCNA.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, 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 By similarity. 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 POLD1, 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.By similarity33 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-358311,EBI-358311
    Q8TE306EBI-358311,EBI-8874509
    ALDOAP040753EBI-358311,EBI-709613
    CDKN1AP389366EBI-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
    PGAM1P186692EBI-358311,EBI-717905
    POLD1P283402EBI-358311,EBI-716569
    POLD3Q150544EBI-358311,EBI-864956
    POLD4Q9HCU84EBI-358311,EBI-864968
    TPI1P601742EBI-358311,EBI-717475

    Protein-protein interaction databases

    BioGridi111142. 222 interactions.
    DIPiDIP-1098N.
    IntActiP12004. 52 interactions.
    MINTiMINT-5000943.
    STRINGi9606.ENSP00000368438.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    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.
    HOGENOMiHOG000211098.
    HOVERGENiHBG000947.
    InParanoidiP12004.
    KOiK04802.
    OMAiMKLMNLD.
    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

    MFEARLVQGS ILKKVLEALK DLINEACWDI SSSGVNLQSM DSSHVSLVQL    50
    TLRSEGFDTY RCDRNLAMGV NLTSMSKILK CAGNEDIITL RAEDNADTLA 100
    LVFEAPNQEK VSDYEMKLMD LDVEQLGIPE QEYSCVVKMP SGEFARICRD 150
    LSHIGDAVVI SCAKDGVKFS ASGELGNGNI KLSQTSNVDK EEEAVTIEMN 200
    EPVQLTFALR YLNFFTKATP LSSTVTLSMS ADVPLVVEYK IADMGHLKYY 250
    LAPKIEDEEG S 261
    Length:261
    Mass (Da):28,769
    Last modified:October 1, 1989 - v1
    Checksum:iE6F08E7EDBC48B00
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi129694.

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Wikipedia

    PCNA entry

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS13087.1.
    PIRi A27445. WMHUET.
    RefSeqi NP_002583.1. NM_002592.2.
    NP_872590.1. NM_182649.1.
    UniGenei Hs.147433.
    Hs.744934.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AXC X-ray 2.60 A/C/E 1-261 [» ]
    1U76 X-ray 2.60 A/C/E 1-261 [» ]
    1U7B X-ray 1.88 A 1-261 [» ]
    1UL1 X-ray 2.90 A/B/C 1-261 [» ]
    1VYJ X-ray 2.80 A/C/E/G/I/K 1-261 [» ]
    1VYM X-ray 2.30 A/B/C 1-261 [» ]
    1W60 X-ray 3.15 A/B 1-261 [» ]
    2ZVK X-ray 2.70 A/B/C 1-261 [» ]
    2ZVL X-ray 2.50 A/B/C/D/E/F 1-261 [» ]
    2ZVM X-ray 2.30 A/B/C 1-261 [» ]
    3P87 X-ray 2.99 A/B/C/D/E/F 1-261 [» ]
    3TBL X-ray 2.90 A/B/C 1-261 [» ]
    3VKX X-ray 2.10 A 1-261 [» ]
    3WGW X-ray 2.80 A/B 1-261 [» ]
    ProteinModelPortali P12004.
    SMRi P12004. Positions 1-255.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111142. 222 interactions.
    DIPi DIP-1098N.
    IntActi P12004. 52 interactions.
    MINTi MINT-5000943.
    STRINGi 9606.ENSP00000368438.

    Chemistry

    ChEMBLi CHEMBL2346488.

    PTM databases

    PhosphoSitei P12004.

    Polymorphism databases

    DMDMi 129694.

    2D gel databases

    SWISS-2DPAGE P12004.

    Proteomic databases

    MaxQBi P12004.
    PaxDbi P12004.
    PeptideAtlasi P12004.
    PRIDEi P12004.

    Protocols and materials databases

    DNASUi 5111.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379143 ; ENSP00000368438 ; ENSG00000132646 .
    ENST00000379160 ; ENSP00000368458 ; ENSG00000132646 .
    GeneIDi 5111.
    KEGGi hsa:5111.
    UCSCi uc002wlp.3. human.

    Organism-specific databases

    CTDi 5111.
    GeneCardsi GC20M005095.
    HGNCi HGNC:8729. PCNA.
    HPAi CAB000148.
    HPA030521.
    HPA030522.
    HPA030523.
    MIMi 176740. gene.
    neXtProti NX_P12004.
    PharmGKBi PA263.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0592.
    HOGENOMi HOG000211098.
    HOVERGENi HBG000947.
    InParanoidi P12004.
    KOi K04802.
    OMAi MKLMNLD.
    OrthoDBi EOG7JX34W.
    PhylomeDBi P12004.
    TreeFami TF313441.

    Enzyme and pathway databases

    Reactomei REACT_111214. G0 and Early G1.
    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_2192. Removal of DNA patch containing abasic residue.
    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_8027. Processive synthesis on the C-strand of the telomere.
    SignaLinki P12004.

    Miscellaneous databases

    ChiTaRSi PCNA. human.
    EvolutionaryTracei P12004.
    GeneWikii Proliferating_cell_nuclear_antigen.
    GenomeRNAii 5111.
    NextBioi 19722.
    PROi P12004.
    SOURCEi Search...

    Gene expression databases

    Bgeei P12004.
    CleanExi HS_PCNA.
    Genevestigatori P12004.

    Family and domain databases

    HAMAPi MF_00317. DNApol_clamp_arch.
    InterProi IPR000730. Pr_cel_nuc_antig.
    IPR022649. Pr_cel_nuc_antig_C.
    IPR022659. Pr_cel_nuc_antig_CS.
    IPR022648. Pr_cel_nuc_antig_N.
    [Graphical view ]
    PANTHERi PTHR11352. PTHR11352. 1 hit.
    Pfami PF02747. PCNA_C. 1 hit.
    PF00705. PCNA_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00339. PCNACYCLIN.
    TIGRFAMsi TIGR00590. pcna. 1 hit.
    PROSITEi PS01251. PCNA_1. 1 hit.
    PS00293. PCNA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    36. "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.
    37. "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.
    38. "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.
    39. "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.
    40. "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.
    41. "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.
    42. "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.
    43. "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.
    44. Cited for: INTERACTION WITH CDKN1C.
    45. "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.
    46. "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.
    47. "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).
    48. "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: October 1, 2014
    This is version 171 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3