PCNA_DANRE
ID PCNA_DANRE Reviewed; 260 AA.
AC Q9PTP1; Q7ZW84;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Proliferating cell nuclear antigen;
DE Short=PCNA;
GN Name=pcna;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lee J.-S., Gye M.C.;
RT "Zebrafish Danio rerio proliferating cell nuclear antigen (PCNA): cloning
RT and characterization.";
RL Fish. Sci. 65:955-958(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259 AND SER-260, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18307296; DOI=10.1021/pr700667w;
RA Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA Slijper M., Heck A.J.R.;
RT "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT analysis down to a single embryo.";
RL J. Proteome Res. 7:1555-1564(2008).
CC -!- FUNCTION: This protein is an auxiliary protein of DNA polymerase delta
CC and is involved in the control of eukaryotic DNA replication by
CC increasing the polymerase's processibility during elongation of the
CC leading strand. {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer. Forms a complex with activator 1 heteropentamer in
CC the presence of ATP (By similarity). Component of the replisome complex
CC (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P12004}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P12004}.
CC -!- PTM: Monoubiquitinated by the ube2b-rad18 complex on Lys-164.
CC Monoubiquitination at Lys-164 also takes place in undamaged
CC proliferating cells, and is mediated by the dcx(dtl) complex, leading
CC to enhance PCNA-dependent translesion DNA synthesis (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PCNA family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF140608; AAF18324.1; -; mRNA.
DR EMBL; BC049535; AAH49535.1; -; mRNA.
DR EMBL; BC064299; AAH64299.1; -; mRNA.
DR RefSeq; NP_571479.2; NM_131404.2.
DR AlphaFoldDB; Q9PTP1; -.
DR SMR; Q9PTP1; -.
DR STRING; 7955.ENSDARP00000070780; -.
DR iPTMnet; Q9PTP1; -.
DR PaxDb; Q9PTP1; -.
DR PRIDE; Q9PTP1; -.
DR Ensembl; ENSDART00000076304; ENSDARP00000070780; ENSDARG00000054155.
DR GeneID; 30678; -.
DR KEGG; dre:30678; -.
DR CTD; 5111; -.
DR ZFIN; ZDB-GENE-000210-8; pcna.
DR eggNOG; KOG1636; Eukaryota.
DR GeneTree; ENSGT00390000004965; -.
DR HOGENOM; CLU_043978_3_0_1; -.
DR InParanoid; Q9PTP1; -.
DR OMA; EMKLINM; -.
DR OrthoDB; 1012066at2759; -.
DR PhylomeDB; Q9PTP1; -.
DR TreeFam; TF313441; -.
DR Reactome; R-DRE-110312; Translesion synthesis by REV1.
DR Reactome; R-DRE-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-DRE-110320; Translesion Synthesis by POLH.
DR Reactome; R-DRE-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-DRE-174414; Processive synthesis on the C-strand of the telomere.
DR Reactome; R-DRE-174417; Telomere C-strand (Lagging Strand) Synthesis.
DR Reactome; R-DRE-174437; Removal of the Flap Intermediate from the C-strand.
DR Reactome; R-DRE-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-DRE-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR Reactome; R-DRE-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-DRE-5655862; Translesion synthesis by POLK.
DR Reactome; R-DRE-5656121; Translesion synthesis by POLI.
DR Reactome; R-DRE-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-DRE-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-DRE-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-DRE-5696400; Dual Incision in GG-NER.
DR Reactome; R-DRE-6782135; Dual incision in TC-NER.
DR Reactome; R-DRE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-DRE-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR Reactome; R-DRE-69091; Polymerase switching.
DR Reactome; R-DRE-69166; Removal of the Flap Intermediate.
DR Reactome; R-DRE-69183; Processive synthesis on the lagging strand.
DR Reactome; R-DRE-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR PRO; PR:Q9PTP1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 10.
DR Bgee; ENSDARG00000054155; Expressed in blastula and 68 other tissues.
DR GO; GO:0005634; C:nucleus; IDA:ZFIN.
DR GO; GO:0043626; C:PCNA complex; IBA:GO_Central.
DR GO; GO:0070557; C:PCNA-p21 complex; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030337; F:DNA polymerase processivity factor activity; IBA:GO_Central.
DR GO; GO:0006272; P:leading strand elongation; IBA:GO_Central.
DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR GO; GO:0006275; P:regulation of DNA replication; IEA:InterPro.
DR GO; GO:0014823; P:response to activity; IDA:ZFIN.
DR GO; GO:0009617; P:response to bacterium; IDA:ZFIN.
DR GO; GO:0019985; P:translesion synthesis; ISS:UniProtKB.
DR HAMAP; MF_00317; DNApol_clamp_arch; 1.
DR InterPro; IPR000730; Pr_cel_nuc_antig.
DR InterPro; IPR022649; Pr_cel_nuc_antig_C.
DR InterPro; IPR022659; Pr_cel_nuc_antig_CS.
DR InterPro; IPR022648; Pr_cel_nuc_antig_N.
DR Pfam; PF02747; PCNA_C; 1.
DR Pfam; PF00705; PCNA_N; 1.
DR PRINTS; PR00339; PCNACYCLIN.
DR TIGRFAMs; TIGR00590; pcna; 1.
DR PROSITE; PS01251; PCNA_1; 1.
DR PROSITE; PS00293; PCNA_2; 1.
PE 1: Evidence at protein level;
KW DNA replication; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..260
FT /note="Proliferating cell nuclear antigen"
FT /id="PRO_0000149165"
FT DNA_BIND 61..80
FT /evidence="ECO:0000255"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT CROSSLNK 164
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
FT CONFLICT 88
FT /note="I -> Q (in Ref. 1; AAF18324)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="A -> T (in Ref. 1; AAF18324)"
FT /evidence="ECO:0000305"
FT CONFLICT 105..106
FT /note="TL -> AQ (in Ref. 1; AAF18324)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="A -> P (in Ref. 1; AAF18324)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="K -> R (in Ref. 1; AAF18324)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="S -> R (in Ref. 1; AAF18324)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="D -> H (in Ref. 1; AAF18324)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="Y -> D (in Ref. 1; AAF18324)"
FT /evidence="ECO:0000305"
FT CONFLICT 244..245
FT /note="MG -> LE (in Ref. 1; AAF18324)"
FT /evidence="ECO:0000305"
FT CONFLICT 254..255
FT /note="KI -> QIE (in Ref. 1; AAF18324)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 260 AA; 28611 MW; 59D27AC8C95B472D CRC64;
MFEARLVQGS ILKKVLEALK DLITEACWDV SSSGISLQSM DSSHVSLVQL TLRSDGFDSY
RCDRNLAMGV NLSSMSKILK CAGNEDIITL RAEDNADALA LVFETLNQEK VSDYEMKLMD
LDVEQLGIPE QEYSCVVKMP SGEFARICRD LSQIGDAVMI SCAKDGVKFS ASGELGTGNI
KLSQTSNVDK EDEAVTIEMN EPVQLIFALN YLNFFTKATP LSKTVTLSMS ADIPLVVEYK
IADMGHVKYY LAPKIDEESS
