CCNG1_RAT
ID CCNG1_RAT Reviewed; 294 AA.
AC P39950;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Cyclin-G1;
DE Short=Cyclin-G;
GN Name=Ccng1; Synonyms=Ccng;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fibroblast;
RX PubMed=8336937;
RA Tamura K., Kanaoka Y., Jinno S., Nagata A., Ogiso Y., Shimizu K.,
RA Hayakawa T., Nojima H., Okayama H.;
RT "Cyclin G: a new mammalian cyclin with homology to fission yeast Cig1.";
RL Oncogene 8:2113-2118(1993).
RN [2]
RP SEQUENCE REVISION TO N-TERMINUS.
RX PubMed=8954786; DOI=10.1006/geno.1996.0598;
RA Endo Y., Fujita T., Tamura K., Tsuruga H., Nojima H.;
RT "Structure and chromosomal assignment of the human cyclin G gene.";
RL Genomics 38:92-95(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Fischer; TISSUE=Embryonic fibroblast;
RX PubMed=7784084;
RA Zauberman A., Lupo A., Oren M.;
RT "Identification of p53 target genes through immune selection of genomic
RT DNA: the cyclin G gene contains two distinct p53 binding sites.";
RL Oncogene 10:2361-2366(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION.
RX PubMed=9464250; DOI=10.1006/bbrc.1997.8004;
RA Shimizu A., Nishida J., Ueoka Y., Kato K., Hachiya T., Kuriaki Y., Wake N.;
RT "CyclinG contributes to G2/M arrest of cells in response to DNA damage.";
RL Biochem. Biophys. Res. Commun. 242:529-533(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:9464250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Induced within 3 hours after growth stimulation,
CC remains elevated with no apparent cell cycle dependency.
CC -!- INDUCTION: By doxorubicin (DOX).
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin G subfamily.
CC {ECO:0000305}.
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DR EMBL; X70871; CAA50219.1; -; mRNA.
DR EMBL; BC081852; AAH81852.1; -; mRNA.
DR PIR; S37693; S37693.
DR RefSeq; NP_037055.1; NM_012923.2.
DR AlphaFoldDB; P39950; -.
DR SMR; P39950; -.
DR BioGRID; 247440; 2.
DR STRING; 10116.ENSRNOP00000063905; -.
DR PaxDb; P39950; -.
DR Ensembl; ENSRNOT00000065633; ENSRNOP00000063905; ENSRNOG00000003256.
DR GeneID; 25405; -.
DR KEGG; rno:25405; -.
DR UCSC; RGD:2295; rat.
DR CTD; 900; -.
DR RGD; 2295; Ccng1.
DR eggNOG; KOG0653; Eukaryota.
DR GeneTree; ENSGT00940000154726; -.
DR HOGENOM; CLU_062642_0_0_1; -.
DR InParanoid; P39950; -.
DR OrthoDB; 1015714at2759; -.
DR PhylomeDB; P39950; -.
DR TreeFam; TF101007; -.
DR Reactome; R-RNO-6804757; Regulation of TP53 Degradation.
DR PRO; PR:P39950; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003256; Expressed in quadriceps femoris and 20 other tissues.
DR ExpressionAtlas; P39950; baseline and differential.
DR Genevisible; P39950; RN.
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; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IEP:RGD.
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; IMP:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
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; IEP:RGD.
DR GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
DR GO; GO:0006949; P:syncytium formation; IMP:RGD.
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_0000080468"
SQ SEQUENCE 294 AA; 33934 MW; 229A5588E66F0DBC CRC64;
MIEVLTTDSQ KLLHQLNTLL EQESRCQPKV CGLKLIESAH DNGLRMTARL RDFEVKDLLS
LTQFFGFDTE TFSLAVNLLD RFLSKMKVQA KHLGCVGLSC FYLAVKSIEE ERNVPLATDL
IRISQYRFTV SDLMRMEKIV LEKVCWKVKA TTAFQFLQLY YSLIRETLPF ERRNDLNFER
LEAQLKACHC RIIFSKAKPS VLALAIIALE IQALKYVELT EGVECIQKHS KISGRDLTFW
QELVSKCLTE YSSNKCSKPN GQKLKWIVSG RTARQLKHSY YRITHLPTIP ETMG