CCNG1_MOUSE
ID CCNG1_MOUSE Reviewed; 294 AA.
AC P51945; O54779;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Cyclin-G1;
DE Short=Cyclin-G;
GN Name=Ccng1; Synonyms=Ccng;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Blood;
RX PubMed=8626390; DOI=10.1074/jbc.271.11.6050;
RA Horne M.C., Goolsby G.L., Donaldson K.L., Tran D., Neubauer M.G.,
RA Wahl A.F.;
RT "Cyclin G1 and cyclin G2 comprise a new family of cyclins with contrasting
RT tissue-specific and cell cycle-regulated expression.";
RL J. Biol. Chem. 271:6050-6061(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 46-294.
RX PubMed=7957050; DOI=10.1002/j.1460-2075.1994.tb06807.x;
RA Okamoto K., Beach D.;
RT "Cyclin G is a transcriptional target of the p53 tumor suppressor
RT protein.";
RL EMBO J. 13:4816-4822(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129;
RX PubMed=9441755; DOI=10.1006/geno.1997.5034;
RA Kimura S.H., Kataoka T.R., Endo Y., Nojima H.;
RT "Genomic structure and chromosomal localization of mouse cyclin G1 gene.";
RL Genomics 46:483-486(1997).
RN [4]
RP FUNCTION.
RX PubMed=8887688; DOI=10.1128/mcb.16.11.6593;
RA Okamoto K., Kamibayashi C., Serrano M., Prives C., Mumby M.C., Beach D.;
RT "p53-dependent association between cyclin G and the B' subunit of protein
RT phosphatase 2A.";
RL Mol. Cell. Biol. 16:6593-6602(1996).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9696022; DOI=10.1002/hep.510280235;
RA Jensen M.R., Factor V.M., Thorgeirsson S.S.;
RT "Regulation of cyclin G1 during murine hepatic regeneration following
RT Dipin-induced DNA damage.";
RL Hepatology 28:537-546(1998).
CC -!- FUNCTION: May play a role in growth regulation. Is associated with G2/M
CC phase arrest in response to DNA damage. May be an intermediate by which
CC p53 mediates its role as an inhibitor of cellular proliferation.
CC {ECO:0000269|PubMed:8887688, ECO:0000269|PubMed:9696022}.
CC -!- SUBUNIT: Binds to B' regulatory B subunits of protein phosphatase A
CC (PP2A) following induction by p53 (in vitro).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9696022}.
CC -!- TISSUE SPECIFICITY: Highest levels in kidney, heart and skeletal
CC muscle.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin G subfamily.
CC {ECO:0000305}.
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DR EMBL; L49507; AAC42082.1; -; mRNA.
DR EMBL; Z37110; CAA85474.1; -; mRNA.
DR EMBL; AB005559; BAA24492.1; -; Genomic_DNA.
DR CCDS; CCDS24550.1; -.
DR PIR; S51621; S51621.
DR RefSeq; NP_033961.1; NM_009831.2.
DR AlphaFoldDB; P51945; -.
DR SMR; P51945; -.
DR BioGRID; 198555; 5.
DR DIP; DIP-24179N; -.
DR STRING; 10090.ENSMUSP00000020576; -.
DR iPTMnet; P51945; -.
DR PhosphoSitePlus; P51945; -.
DR PaxDb; P51945; -.
DR PeptideAtlas; P51945; -.
DR PRIDE; P51945; -.
DR ProteomicsDB; 280016; -.
DR Antibodypedia; 28603; 309 antibodies from 30 providers.
DR DNASU; 12450; -.
DR Ensembl; ENSMUST00000020576; ENSMUSP00000020576; ENSMUSG00000020326.
DR GeneID; 12450; -.
DR KEGG; mmu:12450; -.
DR UCSC; uc007ilz.1; mouse.
DR CTD; 900; -.
DR MGI; MGI:102890; Ccng1.
DR VEuPathDB; HostDB:ENSMUSG00000020326; -.
DR eggNOG; KOG0653; Eukaryota.
DR GeneTree; ENSGT00940000154726; -.
DR HOGENOM; CLU_062642_0_0_1; -.
DR InParanoid; P51945; -.
DR OMA; CFEAQEE; -.
DR OrthoDB; 1015714at2759; -.
DR PhylomeDB; P51945; -.
DR TreeFam; TF101007; -.
DR Reactome; R-MMU-6804757; Regulation of TP53 Degradation.
DR BioGRID-ORCS; 12450; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Ccng1; mouse.
DR PRO; PR:P51945; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P51945; protein.
DR Bgee; ENSMUSG00000020326; Expressed in intercostal muscle and 253 other tissues.
DR ExpressionAtlas; P51945; baseline and differential.
DR Genevisible; P51945; MM.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0009629; P:response to gravity; IEA:Ensembl.
DR GO; GO:0010243; P:response to organonitrogen compound; IEA:Ensembl.
DR GO; GO:0006949; P:syncytium formation; ISO:MGI.
DR CDD; cd00043; CYCLIN; 1.
DR InterPro; IPR028860; CCNG1.
DR InterPro; IPR039361; Cyclin.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10177; PTHR10177; 1.
DR PANTHER; PTHR10177:SF59; PTHR10177:SF59; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SUPFAM; SSF47954; SSF47954; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cyclin; Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..294
FT /note="Cyclin-G1"
FT /id="PRO_0000080466"
FT CONFLICT 175
FT /note="D -> G (in Ref. 3; BAA24492)"
FT /evidence="ECO:0000305"
FT CONFLICT 192..198
FT /note="IIFSKAK -> SYFLRQ (in Ref. 3; BAA24492)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 294 AA; 33903 MW; 09640ADF4E739BAA CRC64;
MIEVLTTDSQ KLLHQLNTLL EQESRCQPKV CGLKLIESAH DNGLRMTARL RDFEVKDLLS
LTQFFGFDTE TFSLAVNLLD RFLSKMKVQA KHLGCVGLSC FYLAVKATEE ERNVPLATDL
IRISQYRFTV SDLMRMEKIV LEKVCWKVKA TTAFQFLQLY YSLVHDTLPF ERRNDLNFER
LEAQLKACHC RIIFSKAKPS VLALSILALE IQALKYVELT EGVECIQKHS KISGRDLTFW
QELVSKCLTE YSSNKCSKPN GQKLKWIVSG RTARQLKHSY YRITHLPTIP ETIC
