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 24-JAN-2024, entry version 162. 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}. 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; 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; 10090-ENSMUSP00000020576; -. DR PeptideAtlas; P51945; -. DR ProteomicsDB; 280016; -. DR Antibodypedia; 28603; 368 antibodies from 30 providers. DR DNASU; 12450; -. DR Ensembl; ENSMUST00000020576.8; ENSMUSP00000020576.8; ENSMUSG00000020326.8. DR GeneID; 12450; -. DR KEGG; mmu:12450; -. DR UCSC; uc007ilz.1; mouse. DR AGR; MGI:102890; -. 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; 3032827at2759; -. DR PhylomeDB; P51945; -. DR TreeFam; TF101007; -. DR Reactome; R-MMU-6804757; Regulation of TP53 Degradation. DR BioGRID-ORCS; 12450; 3 hits in 78 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 256 other cell types or tissues. DR ExpressionAtlas; P51945; baseline and differential. 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; IBA:GO_Central. 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: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: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; cd20583; CYCLIN_CCNG1; 1. DR Gene3D; 1.10.472.10; Cyclin-like; 2. DR InterPro; IPR039361; Cyclin. DR InterPro; IPR013763; Cyclin-like_dom. DR InterPro; IPR036915; Cyclin-like_sf. DR InterPro; IPR006671; Cyclin_N. DR PANTHER; PTHR10177:SF59; CYCLIN-G1; 1. DR PANTHER; PTHR10177; CYCLINS; 1. DR Pfam; PF00134; Cyclin_N; 1. DR SMART; SM00385; CYCLIN; 1. DR SUPFAM; SSF47954; Cyclin-like; 1. DR Genevisible; P51945; MM. 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 //