ID   PCNA_MOUSE              Reviewed;         261 AA.
AC   P17918;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 2.
DT   15-DEC-2009, entry version 103.
DE   RecName: Full=Proliferating cell nuclear antigen;
DE            Short=PCNA;
DE   AltName: Full=Cyclin;
GN   Name=Pcna;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Lymphoid tissue;
RX   MEDLINE=92297962; PubMed=1726365;
RA   Shipman-Appasamy P.M., Cohen K.S., Prystowsky M.B.;
RT   "Nucleotide sequence of murine PCNA: interspecies comparison of the
RT   cDNA and the 5' flanking region of the gene.";
RL   DNA Seq. 2:181-191(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C57BL/6; TISSUE=Spleen;
RX   MEDLINE=91252282; PubMed=1674997; DOI=10.1093/nar/19.9.2403;
RA   Yamaguchi M., Hayashi Y., Hirose F., Matsuoka S., Moriuchi T.,
RA   Shiroishi T., Moriwaki K., Matsukage A.;
RT   "Molecular cloning and structural analysis of mouse gene and
RT   pseudogenes for proliferating cell nuclear antigen.";
RL   Nucleic Acids Res. 19:2403-2410(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-42.
RC   TISSUE=T-cell;
RX   MEDLINE=89155592; PubMed=2906640; DOI=10.1002/jcb.240380306;
RA   Shipman P.M., Sabath D.E., Fischer A.H., Comber P.G., Sullivan K.,
RA   Tan E.M., Prystowsky M.B.;
RT   "Cyclin mRNA and protein expression in recombinant interleukin 2-
RT   stimulated cloned murine T lymphocytes.";
RL   J. Cell. Biochem. 38:189-198(1988).
RN   [5]
RP   INTERACTION WITH PPP1R15A AND HHV-1 ICP34.5.
RX   PubMed=9371605;
RA   Brown S.M., MacLean A.R., McKie E.A., Harland J.;
RT   "The herpes simplex virus virulence factor ICP34.5 and the cellular
RT   protein MyD116 complex with proliferating cell nuclear antigen through
RT   the 63-amino-acid domain conserved in ICP34.5, MyD116, and GADD34.";
RL   J. Virol. 71:9442-9449(1997).
RN   [6]
RP   INTERACTION WITH APEX2.
RX   MEDLINE=22461585; PubMed=12573260; DOI=10.1016/S0888-7543(02)00009-5;
RA   Ide Y., Tsuchimoto D., Tominaga Y., Iwamoto Y., Nakabeppu Y.;
RT   "Characterization of the genomic structure and expression of the mouse
RT   Apex2 gene.";
RL   Genomics 81:47-57(2003).
CC   -!- FUNCTION: This protein is an auxiliary protein of DNA polymerase
CC       delta and is involved in the control of eukaryotic DNA replication
CC       by increasing the polymerase's processibility during elongation of
CC       the leading strand.
CC   -!- SUBUNIT: Homotrimer (By similarity). Forms a complex with
CC       activator 1 heteropentamer in the presence of ATP. Interacts with
CC       POLH, POLK, DNMT1, ERCC5, FEN1, CDC6, POLD1, POLD3, POLD4 and
CC       POLDIP2. Interacts with EXO1, KCTD10 and SHPRH. Forms a ternary
CC       complex with DNTTIP2 and core histone. Interacts with BAZ1B; the
CC       interaction is direct. Interacts with HLTF and SHPRH (By
CC       similarity). Interacts with APEX2 and PPP1R15A. Interacts with
CC       HHV-1 ICP34.5. Interacts with NUDT15 (By similarity). Interaction
CC       is disrupted in response to UV irradiation and acetylation (By
CC       similarity).
CC   -!- INTERACTION:
CC       Q9Z111:Gadd45g; NbExp=1; IntAct=EBI-1173716, EBI-1173616;
CC       P62137:Ppp1ca; NbExp=2; IntAct=EBI-1173716, EBI-357187;
CC       P63087-1:Ppp1cc; NbExp=1; IntAct=EBI-1173716, EBI-450267;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- INDUCTION: Induced in IL2-stimulated proliferating T-lymphocytes.
CC   -!- PTM: Upon methyl methanesulfonate-induced DNA damage, mono-
CC       ubiquitinated by the UBE2B-RAD18 complex on Lys-164. This induces
CC       non-canonical poly-ubiquitination on Lys-164 through 'Lys-63'
CC       linkage of ubiquitin moieties by the E2 complex UBE2N-UBE2V2 and
CC       the E3 ligases, HLTF, RNF8 and SHPRH, which is required for DNA
CC       repair. 'Lys-63' polyubiquitination prevents genomic instability
CC       on DNA damage (By similarity).
CC   -!- PTM: Acetylated in response to UV irradiation. Acetylation
CC       disrupts interaction with NUDT15 and promotes degradation (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the PCNA family.
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DR   EMBL; X53068; CAA37243.1; -; mRNA.
DR   EMBL; X57800; CAA40938.1; -; Genomic_DNA.
DR   EMBL; BC005778; AAH05778.1; -; mRNA.
DR   EMBL; BC010343; AAH10343.1; -; mRNA.
DR   IPI; IPI00113870; -.
DR   PIR; S15703; WMMS.
DR   RefSeq; NP_035175.1; -.
DR   UniGene; Mm.7141; -.
DR   SMR; P17918; 1-260.
DR   IntAct; P17918; 4.
DR   STRING; P17918; -.
DR   PhosphoSite; P17918; -.
DR   REPRODUCTION-2DPAGE; P17918; -.
DR   PRIDE; P17918; -.
DR   Ensembl; ENSMUST00000028817; ENSMUSP00000028817; ENSMUSG00000027342; Mus musculus.
DR   GeneID; 18538; -.
DR   KEGG; mmu:18538; -.
DR   UCSC; uc008mml.1; mouse.
DR   CTD; 18538; -.
DR   MGI; MGI:97503; Pcna.
DR   HOVERGEN; P17918; -.
DR   InParanoid; P17918; -.
DR   OMA; ICRDLSQ; -.
DR   OrthoDB; EOG92RGTF; -.
DR   NextBio; 294312; -.
DR   ArrayExpress; P17918; -.
DR   Bgee; P17918; -.
DR   CleanEx; MM_PCNA; -.
DR   Genevestigator; P17918; -.
DR   GermOnline; ENSMUSG00000027342; Mus musculus.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme ...; IPI:MGI.
DR   GO; GO:0005652; C:nuclear lamina; IDA:MGI.
DR   GO; GO:0043626; C:PCNA complex; IEA:InterPro.
DR   GO; GO:0005657; C:replication fork; IDA:MGI.
DR   GO; GO:0030337; F:DNA polymerase processivity factor activity; IEA:InterPro.
DR   GO; GO:0006287; P:base-excision repair, gap-filling; IDA:MGI.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; IMP:MGI.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:InterPro.
DR   InterPro; IPR000730; Pr_cel_nuc_antig.
DR   PANTHER; PTHR11352; Pr_cel_nuc_antig; 1.
DR   Pfam; PF02747; PCNA_C; 1.
DR   Pfam; PF00705; PCNA_N; 1.
DR   PRINTS; PR00339; PCNACYCLIN.
DR   PROSITE; PS01251; PCNA_1; 1.
DR   PROSITE; PS00293; PCNA_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; DNA replication; DNA-binding; Isopeptide bond; Nucleus;
KW   Ubl conjugation.
FT   CHAIN         1    261       Proliferating cell nuclear antigen.
FT                                /FTId=PRO_0000149160.
FT   DNA_BIND     61     80       Potential.
FT   MOD_RES      77     77       N6-acetyllysine (By similarity).
FT   MOD_RES      80     80       N6-acetyllysine (By similarity).
FT   MOD_RES     248    248       N6-acetyllysine (By similarity).
FT   CROSSLNK    164    164       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CONFLICT      3      5       EAR -> LES (in Ref. 4).
FT   CONFLICT     67     67       A -> T (in Ref. 2; CAA37243).
SQ   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
//