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Proliferating cell nuclear antigen (PCNA) (Cyclin)

 PCNA_MOUSE              Reviewed;         261 AA.
P17918;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-MAR-1992, sequence version 2.
20-JUN-2018, entry version 184.
RecName: Full=Proliferating cell nuclear antigen;
Short=PCNA;
AltName: Full=Cyclin;
Name=Pcna;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J; TISSUE=Lymphoid tissue;
PubMed=1726365; DOI=10.3109/10425179109039688;
Shipman-Appasamy P.M., Cohen K.S., Prystowsky M.B.;
"Nucleotide sequence of murine PCNA: interspecies comparison of the
cDNA and the 5' flanking region of the gene.";
DNA Seq. 2:181-191(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=C57BL/6J; TISSUE=Spleen;
PubMed=1674997; DOI=10.1093/nar/19.9.2403;
Yamaguchi M., Hayashi Y., Hirose F., Matsuoka S., Moriuchi T.,
Shiroishi T., Moriwaki K., Matsukage A.;
"Molecular cloning and structural analysis of mouse gene and
pseudogenes for proliferating cell nuclear antigen.";
Nucleic Acids Res. 19:2403-2410(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-42.
TISSUE=T-cell;
PubMed=2906640; DOI=10.1002/jcb.240380306;
Shipman P.M., Sabath D.E., Fischer A.H., Comber P.G., Sullivan K.,
Tan E.M., Prystowsky M.B.;
"Cyclin mRNA and protein expression in recombinant interleukin 2-
stimulated cloned murine T lymphocytes.";
J. Cell. Biochem. 38:189-198(1988).
[5]
INTERACTION WITH PPP1R15A AND HHV-1 ICP34.5.
PubMed=9371605;
Brown S.M., MacLean A.R., McKie E.A., Harland J.;
"The herpes simplex virus virulence factor ICP34.5 and the cellular
protein MyD116 complex with proliferating cell nuclear antigen through
the 63-amino-acid domain conserved in ICP34.5, MyD116, and GADD34.";
J. Virol. 71:9442-9449(1997).
[6]
INTERACTION WITH APEX2.
PubMed=12573260; DOI=10.1016/S0888-7543(02)00009-5;
Ide Y., Tsuchimoto D., Tominaga Y., Iwamoto Y., Nakabeppu Y.;
"Characterization of the genomic structure and expression of the mouse
Apex2 gene.";
Genomics 81:47-57(2003).
[7]
PHOSPHORYLATION AT TYR-211.
PubMed=17115032; DOI=10.1038/ncb1501;
Wang S.C., Nakajima Y., Yu Y.L., Xia W., Chen C.T., Yang C.C.,
McIntush E.W., Li L.Y., Hawke D.H., Kobayashi R., Hung M.C.;
"Tyrosine phosphorylation controls PCNA function through protein
stability.";
Nat. Cell Biol. 8:1359-1368(2006).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Liver, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
INTERACTION WITH RTEL1, AND SUBCELLULAR LOCATION.
PubMed=24115439; DOI=10.1126/science.1241779;
Vannier J.B., Sandhu S., Petalcorin M.I., Wu X., Nabi Z., Ding H.,
Boulton S.J.;
"RTEL1 is a replisome-associated helicase that promotes telomere and
genome-wide replication.";
Science 342:239-242(2013).
-!- FUNCTION: 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 (By similarity).
{ECO:0000250|UniProtKB:P12004}.
-!- SUBUNIT: Homotrimer. Interacts with p300/EP300; the interaction
occurs on chromatin in UV-irradiated damaged cells. Interacts with
CREBBP (via transactivation domain and C-terminus); the
interaction occurs on chromatin in UV-irradiated damaged cells.
Directly interacts with POLD1, POLD3 and POLD4 subunits of the DNA
polymerase delta complex, POLD3 being the major interacting
partner; the interaction with POLD3 is inhibited by
CDKN1A/p21(CIP1). Forms a complex with activator 1 heteropentamer
in the presence of ATP. Interacts with EXO1, POLH, POLK, DNMT1,
ERCC5, FEN1, CDC6 and POLDIP2 (By similarity). Interacts with
APEX2; this interaction is triggered by reactive oxygen species
and increased by misincorporation of uracil in nuclear DNA
(PubMed:12573260). Forms a ternary complex with DNTTIP2 and core
histone (By similarity). Interacts with KCTD10 (By similarity).
Interacts with PPP1R15A (PubMed:9371605). Directly interacts with
BAZ1B. Interacts with HLTF and SHPRH. Interacts with NUDT15; this
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. The
interaction with CDKN1A inhibits POLD3 binding. 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 PCLAF (via PIP-box) (By similarity).
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. Interacts with LIG1. Interacts with SETMAR. Interacts
with ANKRD17. Interacts with FBXO18/FBH1 (via PIP-box); the
interaction recruits the DCX(DTL) complex and promotes
ubiquitination and degradation of FBXO18/FBH1. Interacts with POLN
(By similarity). Interacts with SDE2 (via PIP-box); the
interaction is direct and prevents ultraviolet light induced
monoubiquitination (By similarity). Component of the replisome
complex composed of at least DONSON, MCM2, MCM7, PCNA and TICRR;
interaction at least with PCNA occurs during DNA replication (By
similarity). Interacts with MAPK15; the interaction is chromatin
binding dependent and prevents MDM2-mediated PCNA destruction by
inhibiting the association of PCNA with MDM2 (By similarity).
{ECO:0000250|UniProtKB:P04961, ECO:0000250|UniProtKB:P12004,
ECO:0000269|PubMed:12573260, ECO:0000269|PubMed:24115439,
ECO:0000269|PubMed:9371605}.
-!- INTERACTION:
P39689:Cdkn1a; NbExp=2; IntAct=EBI-1173716, EBI-1174103;
Q9Z111:Gadd45g; NbExp=2; IntAct=EBI-1173716, EBI-1173616;
P62137:Ppp1ca; NbExp=2; IntAct=EBI-1173716, EBI-357187;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24115439}.
Note=Colocalizes with CREBBP, EP300 and POLD1 to sites of DNA
damage (By similarity). 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.
{ECO:0000250|UniProtKB:P12004}.
-!- INDUCTION: Induced in IL2-stimulated proliferating T-lymphocytes.
-!- PTM: Phosphorylated. Phosphorylation at Tyr-211 by EGFR stabilizes
chromatin-associated PCNA (By similarity).
{ECO:0000250|UniProtKB:P12004}.
-!- PTM: 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. 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. Acetylation disrupts interaction with NUDT15 and
promotes degradation (By similarity).
{ECO:0000250|UniProtKB:P12004}.
-!- PTM: Ubiquitinated. 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 (By similarity).
{ECO:0000250|UniProtKB:P12004}.
-!- PTM: Methylated on glutamate residues by ARMT1.
{ECO:0000250|UniProtKB:P12004}.
-!- SIMILARITY: Belongs to the PCNA family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; X53068; CAA37243.1; -; mRNA.
EMBL; X57800; CAA40938.1; -; Genomic_DNA.
EMBL; BC005778; AAH05778.1; -; mRNA.
EMBL; BC010343; AAH10343.1; -; mRNA.
CCDS; CCDS16771.1; -.
PIR; S15703; WMMS.
RefSeq; NP_035175.1; NM_011045.2.
UniGene; Mm.391640; -.
UniGene; Mm.7141; -.
ProteinModelPortal; P17918; -.
SMR; P17918; -.
BioGrid; 202049; 50.
ComplexPortal; CPX-541; PCNA homotrimer.
CORUM; P17918; -.
DIP; DIP-39409N; -.
IntAct; P17918; 40.
MINT; P17918; -.
STRING; 10090.ENSMUSP00000028817; -.
iPTMnet; P17918; -.
PhosphoSitePlus; P17918; -.
SwissPalm; P17918; -.
REPRODUCTION-2DPAGE; P17918; -.
EPD; P17918; -.
PaxDb; P17918; -.
PeptideAtlas; P17918; -.
PRIDE; P17918; -.
TopDownProteomics; P17918; -.
Ensembl; ENSMUST00000028817; ENSMUSP00000028817; ENSMUSG00000027342.
GeneID; 18538; -.
KEGG; mmu:18538; -.
UCSC; uc008mml.1; mouse.
CTD; 5111; -.
MGI; MGI:97503; Pcna.
eggNOG; KOG1636; Eukaryota.
eggNOG; COG0592; LUCA.
GeneTree; ENSGT00390000004965; -.
HOVERGEN; HBG000947; -.
InParanoid; P17918; -.
KO; K04802; -.
OMA; SDGFDKY; -.
OrthoDB; EOG091G0GQ7; -.
PhylomeDB; P17918; -.
TreeFam; TF313441; -.
Reactome; R-MMU-110312; Translesion synthesis by REV1.
Reactome; R-MMU-110314; Recognition of DNA damage by PCNA-containing replication complex.
Reactome; R-MMU-110320; Translesion Synthesis by POLH.
Reactome; R-MMU-174411; Polymerase switching on the C-strand of the telomere.
Reactome; R-MMU-174414; Processive synthesis on the C-strand of the telomere.
Reactome; R-MMU-174417; Telomere C-strand (Lagging Strand) Synthesis.
Reactome; R-MMU-174437; Removal of the Flap Intermediate from the C-strand.
Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
Reactome; R-MMU-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
Reactome; R-MMU-5651801; PCNA-Dependent Long Patch Base Excision Repair.
Reactome; R-MMU-5655862; Translesion synthesis by POLK.
Reactome; R-MMU-5656121; Translesion synthesis by POLI.
Reactome; R-MMU-5656169; Termination of translesion DNA synthesis.
Reactome; R-MMU-5685942; HDR through Homologous Recombination (HRR).
Reactome; R-MMU-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
Reactome; R-MMU-5696400; Dual Incision in GG-NER.
Reactome; R-MMU-6782135; Dual incision in TC-NER.
Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
Reactome; R-MMU-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
Reactome; R-MMU-69091; Polymerase switching.
Reactome; R-MMU-69166; Removal of the Flap Intermediate.
Reactome; R-MMU-69183; Processive synthesis on the lagging strand.
PRO; PR:P17918; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027342; -.
CleanEx; MM_PCNA; -.
ExpressionAtlas; P17918; baseline and differential.
Genevisible; P17918; MM.
GO; GO:0005813; C:centrosome; ISO:MGI.
GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IPI:MGI.
GO; GO:0005622; C:intracellular; IDA:MGI.
GO; GO:0016604; C:nuclear body; ISO:MGI.
GO; GO:0005652; C:nuclear lamina; IDA:MGI.
GO; GO:0043596; C:nuclear replication fork; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0043626; C:PCNA complex; ISS:UniProtKB.
GO; GO:0070557; C:PCNA-p21 complex; ISS:UniProtKB.
GO; GO:0005657; C:replication fork; IDA:MGI.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0003684; F:damaged DNA binding; ISS:UniProtKB.
GO; GO:0032139; F:dinucleotide insertion or deletion binding; ISO:MGI.
GO; GO:0070182; F:DNA polymerase binding; ISO:MGI.
GO; GO:0030337; F:DNA polymerase processivity factor activity; IBA:GO_Central.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0030331; F:estrogen receptor binding; ISO:MGI.
GO; GO:0035035; F:histone acetyltransferase binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0032405; F:MutLalpha complex binding; ISO:MGI.
GO; GO:0000701; F:purine-specific mismatch base pair DNA N-glycosylase activity; ISO:MGI.
GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:MGI.
GO; GO:0006287; P:base-excision repair, gap-filling; IDA:MGI.
GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:MGI.
GO; GO:0006272; P:leading strand elongation; IBA:GO_Central.
GO; GO:0006298; P:mismatch repair; ISO:MGI.
GO; GO:1902990; P:mitotic telomere maintenance via semi-conservative replication; IGI:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0032077; P:positive regulation of deoxyribonuclease activity; ISS:UniProtKB.
GO; GO:0045739; P:positive regulation of DNA repair; ISS:UniProtKB.
GO; GO:0045740; P:positive regulation of DNA replication; ISS:UniProtKB.
GO; GO:0031297; P:replication fork processing; IGI:BHF-UCL.
GO; GO:0033993; P:response to lipid; ISO:MGI.
GO; GO:0019985; P:translesion synthesis; ISS:UniProtKB.
HAMAP; MF_00317; DNApol_clamp_arch; 1.
InterPro; IPR000730; Pr_cel_nuc_antig.
InterPro; IPR022649; Pr_cel_nuc_antig_C.
InterPro; IPR022659; Pr_cel_nuc_antig_CS.
InterPro; IPR022648; Pr_cel_nuc_antig_N.
PANTHER; PTHR11352:SF0; PTHR11352:SF0; 1.
Pfam; PF02747; PCNA_C; 1.
Pfam; PF00705; PCNA_N; 1.
PRINTS; PR00339; PCNACYCLIN.
TIGRFAMs; TIGR00590; pcna; 1.
PROSITE; PS01251; PCNA_1; 1.
PROSITE; PS00293; PCNA_2; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; DNA damage; DNA repair;
DNA replication; DNA-binding; Isopeptide bond; Methylation; Nucleus;
Phosphoprotein; Reference proteome; Ubl conjugation.
CHAIN 1 261 Proliferating cell nuclear antigen.
/FTId=PRO_0000149160.
DNA_BIND 61 80 {ECO:0000255}.
MOD_RES 14 14 N6-acetyllysine.
{ECO:0000250|UniProtKB:P12004}.
MOD_RES 77 77 N6-acetyllysine.
{ECO:0000250|UniProtKB:P12004}.
MOD_RES 80 80 N6-acetyllysine.
{ECO:0000250|UniProtKB:P12004}.
MOD_RES 211 211 Phosphotyrosine; by EGFR.
{ECO:0000269|PubMed:17115032}.
MOD_RES 248 248 N6-acetyllysine.
{ECO:0000250|UniProtKB:P12004}.
CROSSLNK 164 164 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P12004}.
CROSSLNK 164 164 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P12004}.
CROSSLNK 254 254 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P12004}.
CONFLICT 3 5 EAR -> LES (in Ref. 4; no nucleotide
entry). {ECO:0000305}.
CONFLICT 67 67 A -> T (in Ref. 2; CAA37243).
{ECO:0000305}.
SEQUENCE 261 AA; 28785 MW; F705CCBDD3205986 CRC64;
MFEARLIQGS ILKKVLEALK DLINEACWDV SSGGVNLQSM DSSHVSLVQL TLRSEGFDTY
RCDRNLAMGV NLTSMSKILK CAGNEDIITL RAEDNADTLA LVFEAPNQEK VSDYEMKLMD
LDVEQLGIPE QEYSCVIKMP SGEFARICRD LSHIGDAVVI SCAKNGVKFS ASGELGNGNI
KLSQTSNVDK EEEAVTIEMN EPVHLTFALR YLNFFTKATP LSPTVTLSMS ADVPLVVEYK
IADMGHLKYY LAPKIEDEEA S


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