CCNG1_HUMAN
ID CCNG1_HUMAN Reviewed; 295 AA.
AC P51959; B2R7B2; B4DLW7; D3DQK7; Q15757; Q96L32;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Cyclin-G1;
DE Short=Cyclin-G;
GN Name=CCNG1; Synonyms=CCNG, CYCG1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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] (ISOFORM 1).
RC TISSUE=Fetal spleen;
RX PubMed=8806701;
RA Bates S.A., Rowan S., Vousden K.H.;
RT "Characterisation of human cyclin G1 and G2: DNA damage inducible genes.";
RL Oncogene 13:1103-1109(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RC TISSUE=Mammary gland;
RX PubMed=10196184; DOI=10.1074/jbc.274.16.11022;
RA Reimer C.L., Borras A.M., Kurdistani S.K., Garreau J.R., Chung M.,
RA Aaronson S.A., Lee S.W.;
RT "Altered regulation of cyclin G in human breast cancer and its specific
RT localization at replication foci in response to DNA damage in p53+/+
RT cells.";
RL J. Biol. Chem. 274:11022-11029(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-178 AND LEU-179.
RG NIEHS SNPs program;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, and Prostate;
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 [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-295 (ISOFORM 1).
RC TISSUE=Fibroblast;
RA Wu L., Hall F.L.;
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P51959; Q8NA61: CBY2; NbExp=3; IntAct=EBI-3905829, EBI-741724;
CC P51959; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-3905829, EBI-11977221;
CC P51959; O95995: GAS8; NbExp=3; IntAct=EBI-3905829, EBI-1052570;
CC P51959; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-3905829, EBI-2549423;
CC P51959; P42858: HTT; NbExp=3; IntAct=EBI-3905829, EBI-466029;
CC P51959; Q6A162: KRT40; NbExp=3; IntAct=EBI-3905829, EBI-10171697;
CC P51959; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-3905829, EBI-10172290;
CC P51959; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-3905829, EBI-741037;
CC P51959; Q9P286: PAK5; NbExp=4; IntAct=EBI-3905829, EBI-741896;
CC P51959; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-3905829, EBI-302345;
CC P51959; P30153: PPP2R1A; NbExp=2; IntAct=EBI-3905829, EBI-302388;
CC P51959; Q93062: RBPMS; NbExp=3; IntAct=EBI-3905829, EBI-740322;
CC P51959; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-3905829, EBI-1105213;
CC P51959; Q15025: TNIP1; NbExp=8; IntAct=EBI-3905829, EBI-357849;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10196184}. Note=DNA
CC replication foci after DNA damage.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P51959-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P51959-2; Sequence=VSP_056943;
CC -!- TISSUE SPECIFICITY: High levels in skeletal muscle, ovary, kidney and
CC colon.
CC -!- DEVELOPMENTAL STAGE: Very low levels in normal cells during G1 phase,
CC which increase as cells enter the S phase and stay high throughout the
CC S and G2/M phases. In breast cancer cells consistent high levels are
CC found throughout the cell cycle.
CC -!- INDUCTION: Activated in breast and prostate cancer cells. Activated by
CC actinomycin-D induced DNA damage.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin G subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB03903.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA54821.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/ccng1/";
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; L49504; AAC41977.1; -; mRNA.
DR EMBL; U47413; AAC50688.1; -; mRNA.
DR EMBL; D86077; BAA13007.1; -; Genomic_DNA.
DR EMBL; D78341; BAA11353.1; -; mRNA.
DR EMBL; U53328; AAB03903.1; ALT_INIT; mRNA.
DR EMBL; AK297190; BAG59679.1; -; mRNA.
DR EMBL; AK312913; BAG35759.1; -; mRNA.
DR EMBL; AK316234; BAH14605.1; -; mRNA.
DR EMBL; BT007134; AAP35798.1; -; mRNA.
DR EMBL; AY791292; AAV40836.1; -; Genomic_DNA.
DR EMBL; AC112205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW61528.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61529.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61530.1; -; Genomic_DNA.
DR EMBL; BC000196; AAH00196.1; -; mRNA.
DR EMBL; BC007093; AAH07093.1; -; mRNA.
DR EMBL; X77794; CAA54821.1; ALT_INIT; mRNA.
DR CCDS; CCDS4360.1; -. [P51959-1]
DR PIR; G02401; G02401.
DR RefSeq; NP_004051.1; NM_004060.3. [P51959-1]
DR RefSeq; NP_954854.1; NM_199246.1. [P51959-1]
DR AlphaFoldDB; P51959; -.
DR SMR; P51959; -.
DR BioGRID; 107340; 47.
DR ELM; P51959; -.
DR IntAct; P51959; 30.
DR MINT; P51959; -.
DR STRING; 9606.ENSP00000344635; -.
DR iPTMnet; P51959; -.
DR PhosphoSitePlus; P51959; -.
DR BioMuta; CCNG1; -.
DR DMDM; 2506334; -.
DR MassIVE; P51959; -.
DR PaxDb; P51959; -.
DR PeptideAtlas; P51959; -.
DR PRIDE; P51959; -.
DR ProteomicsDB; 4569; -.
DR ProteomicsDB; 56462; -. [P51959-1]
DR Antibodypedia; 28603; 309 antibodies from 30 providers.
DR DNASU; 900; -.
DR Ensembl; ENST00000340828.7; ENSP00000344635.2; ENSG00000113328.19. [P51959-1]
DR Ensembl; ENST00000393929.5; ENSP00000377506.1; ENSG00000113328.19. [P51959-1]
DR Ensembl; ENST00000512163.5; ENSP00000424315.1; ENSG00000113328.19. [P51959-2]
DR GeneID; 900; -.
DR KEGG; hsa:900; -.
DR MANE-Select; ENST00000340828.7; ENSP00000344635.2; NM_004060.4; NP_004051.1.
DR UCSC; uc003lzb.4; human. [P51959-1]
DR CTD; 900; -.
DR DisGeNET; 900; -.
DR GeneCards; CCNG1; -.
DR HGNC; HGNC:1592; CCNG1.
DR HPA; ENSG00000113328; Low tissue specificity.
DR MIM; 601578; gene.
DR neXtProt; NX_P51959; -.
DR OpenTargets; ENSG00000113328; -.
DR PharmGKB; PA26157; -.
DR VEuPathDB; HostDB:ENSG00000113328; -.
DR eggNOG; KOG0653; Eukaryota.
DR GeneTree; ENSGT00940000154726; -.
DR HOGENOM; CLU_062642_0_2_1; -.
DR InParanoid; P51959; -.
DR OMA; CFEAQEE; -.
DR OrthoDB; 1015714at2759; -.
DR PhylomeDB; P51959; -.
DR TreeFam; TF101007; -.
DR PathwayCommons; P51959; -.
DR Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
DR SignaLink; P51959; -.
DR BioGRID-ORCS; 900; 14 hits in 1080 CRISPR screens.
DR ChiTaRS; CCNG1; human.
DR GeneWiki; CCNG1; -.
DR GenomeRNAi; 900; -.
DR Pharos; P51959; Tbio.
DR PRO; PR:P51959; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P51959; protein.
DR Bgee; ENSG00000113328; Expressed in jejunal mucosa and 215 other tissues.
DR ExpressionAtlas; P51959; baseline and differential.
DR Genevisible; P51959; HS.
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; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
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; IEA:Ensembl.
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 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Cyclin; Mitosis; Nucleus;
KW Reference proteome.
FT CHAIN 1..295
FT /note="Cyclin-G1"
FT /id="PRO_0000080465"
FT VAR_SEQ 1..134
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056943"
FT VARIANT 178
FT /note="N -> H (in dbSNP:rs2069352)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_021079"
FT VARIANT 179
FT /note="F -> L (in dbSNP:rs11541970)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_021080"
FT CONFLICT 128
FT /note="R -> M (in Ref. 4; AAB03903)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="K -> E (in Ref. 10; AAH07093)"
FT /evidence="ECO:0000305"
FT CONFLICT 275..295
FT /note="RQLKHSYYRITHLPTIPEMVP -> LKWSLNWIITAPKNFSEAFLHNLVLWI
FT P (in Ref. 4; AAB03903)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 295 AA; 34074 MW; EA0B02C83F3B6BF3 CRC64;
MIEVLTTTDS QKLLHQLNAL LEQESRCQPK VCGLRLIESA HDNGLRMTAR LRDFEVKDLL
SLTQFFGFDT ETFSLAVNLL DRFLSKMKVQ PKHLGCVGLS CFYLAVKSIE EERNVPLATD
LIRISQYRFT VSDLMRMEKI VLEKVCWKVK ATTAFQFLQL YYSLLQENLP LERRNSINFE
RLEAQLKACH CRIIFSKAKP SVLALSIIAL EIQAQKCVEL TEGIECLQKH SKINGRDLTF
WQELVSKCLT EYSSNKCSKP NVQKLKWIVS GRTARQLKHS YYRITHLPTI PEMVP
