Full text data of CCNY
CCNY
(C10orf9, CBCP1, CFP1)
[Confidence: low (only semi-automatic identification from reviews)]
Cyclin-Y; Cyc-Y (Cyclin box protein 1; Cyclin fold protein 1; cyclin-X)
Cyclin-Y; Cyc-Y (Cyclin box protein 1; Cyclin fold protein 1; cyclin-X)
UniProt
Q8ND76
ID CCNY_HUMAN Reviewed; 341 AA.
AC Q8ND76; B7ZKX9; D3DRY9; Q2M3V4; Q2TU96; Q6NT86; Q7Z4U7; Q8TEX2;
read moreAC Q8TEX3; Q96M99; Q96P45;
DT 02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 2.
DT 22-JAN-2014, entry version 113.
DE RecName: Full=Cyclin-Y;
DE Short=Cyc-Y;
DE AltName: Full=Cyclin box protein 1;
DE AltName: Full=Cyclin fold protein 1;
DE AltName: Full=cyclin-X;
GN Name=CCNY; Synonyms=C10orf9, CBCP1, CFP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP LOCATION, INTERACTION WITH CDK14, MYRISTOYLATION AT GLY-2, AND
RP MUTAGENESIS OF GLY-2 AND ASN-3.
RX PubMed=19524571; DOI=10.1016/j.febslet.2009.06.010;
RA Jiang M., Gao Y., Yang T., Zhu X., Chen J.;
RT "Cyclin Y, a novel membrane-associated cyclin, interacts with PFTK1.";
RL FEBS Lett. 583:2171-2178(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), FUNCTION,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=18060517; DOI=10.1007/s11033-007-9156-5;
RA Li X., Wang X., Liu G., Li R., Yu L.;
RT "Identification and characterization of cyclin X which activates
RT transcriptional activities of c-Myc.";
RL Mol. Biol. Rep. 36:97-103(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Gong L., Wu K.;
RT "Identification and characterization of CBCP1, a novel gene located on
RT human chromosome 10.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA Shannon M.;
RT "Human cyclin fold protein 1.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, Cerebellum, Neuroblastoma, and Testis;
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INTERACTION WITH
RP CDK14 AND LRP6, UBIQUITINATION, MYRISTOYLATION AT GLY-2, AND
RP MUTAGENESIS OF GLY-2.
RX PubMed=20059949; DOI=10.1016/j.devcel.2009.11.006;
RA Davidson G., Shen J., Huang Y.L., Su Y., Karaulanov E.,
RA Bartscherer K., Hassler C., Stannek P., Boutros M., Niehrs C.;
RT "Cell cycle control of wnt receptor activation.";
RL Dev. Cell 17:788-799(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CDK16, AND
RP PHOSPHORYLATION AT SER-326.
RX PubMed=22184064; DOI=10.1128/MCB.06261-11;
RA Mikolcevic P., Sigl R., Rauch V., Hess M.W., Pfaller K., Barisic M.,
RA Pelliniemi L.J., Boesl M., Geley S.;
RT "Cyclin-dependent kinase 16/PCTAIRE kinase 1 is activated by cyclin Y
RT and is essential for spermatogenesis.";
RL Mol. Cell. Biol. 32:868-879(2012).
CC -!- FUNCTION: Positive regulatory subunit of the cyclin-dependent
CC kinases CDK14/PFTK1 and CDK16. Acts as a cell-cycle regulator of
CC Wnt signaling pathway during G2/M phase by recruiting CDK14/PFTK1
CC to the plasma membrane and promoting phosphorylation of LRP6,
CC leading to the activation of the Wnt signaling pathway. Recruits
CC CDK16 to the plasma membrane. Isoform 3 might play a role in the
CC activation of MYC-mediated transcription.
CC -!- SUBUNIT: Interacts with CDK14, CDK16 and LRP6.
CC -!- INTERACTION:
CC O94921:CDK14; NbExp=11; IntAct=EBI-1049189, EBI-1043945;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC side.
CC -!- SUBCELLULAR LOCATION: Isoform 3: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=b;
CC IsoId=Q8ND76-1; Sequence=Displayed;
CC Name=2; Synonyms=a;
CC IsoId=Q8ND76-2; Sequence=VSP_014834;
CC Name=3;
CC IsoId=Q8ND76-3; Sequence=VSP_014833;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DEVELOPMENTAL STAGE: Enriched at G2/M.
CC -!- PTM: Ubiquitinated; leading to its degradation.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin Y subfamily.
CC -!- SIMILARITY: Contains 1 cyclin N-terminal domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH69224.1; Type=Erroneous initiation;
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DR EMBL; AY504868; AAS79427.1; -; mRNA.
DR EMBL; AF429969; AAP97301.1; -; mRNA.
DR EMBL; AF413522; AAL07802.1; -; mRNA.
DR EMBL; AF465728; AAL78998.1; -; mRNA.
DR EMBL; AF465729; AAL78999.1; -; mRNA.
DR EMBL; AK057280; BAB71409.1; -; mRNA.
DR EMBL; AL834355; CAD39020.2; -; mRNA.
DR EMBL; AL592445; CAH70072.1; -; Genomic_DNA.
DR EMBL; AL121749; CAH70072.1; JOINED; Genomic_DNA.
DR EMBL; AL603824; CAH70072.1; JOINED; Genomic_DNA.
DR EMBL; AL592445; CAH70073.1; -; Genomic_DNA.
DR EMBL; AL121749; CAH70073.1; JOINED; Genomic_DNA.
DR EMBL; AL603824; CAH70073.1; JOINED; Genomic_DNA.
DR EMBL; AL117336; CAH70073.1; JOINED; Genomic_DNA.
DR EMBL; AL603824; CAH71567.1; -; Genomic_DNA.
DR EMBL; AL121749; CAH71567.1; JOINED; Genomic_DNA.
DR EMBL; AL592445; CAH71567.1; JOINED; Genomic_DNA.
DR EMBL; AL603824; CAH71568.1; -; Genomic_DNA.
DR EMBL; AL121749; CAH71568.1; JOINED; Genomic_DNA.
DR EMBL; AL592445; CAH71568.1; JOINED; Genomic_DNA.
DR EMBL; AL117336; CAH71568.1; JOINED; Genomic_DNA.
DR EMBL; AL117336; CAH72501.1; -; Genomic_DNA.
DR EMBL; AL121749; CAH72501.1; JOINED; Genomic_DNA.
DR EMBL; AL603824; CAH72501.1; JOINED; Genomic_DNA.
DR EMBL; AL592445; CAH72501.1; JOINED; Genomic_DNA.
DR EMBL; AL121749; CAH73707.1; -; Genomic_DNA.
DR EMBL; AL603824; CAH73707.1; JOINED; Genomic_DNA.
DR EMBL; AL592445; CAH73707.1; JOINED; Genomic_DNA.
DR EMBL; AL121749; CAH73709.1; -; Genomic_DNA.
DR EMBL; AL603824; CAH73709.1; JOINED; Genomic_DNA.
DR EMBL; AL592445; CAH73709.1; JOINED; Genomic_DNA.
DR EMBL; AL117336; CAH73709.1; JOINED; Genomic_DNA.
DR EMBL; CH471072; EAW85912.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW85913.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW85914.1; -; Genomic_DNA.
DR EMBL; BC069224; AAH69224.1; ALT_INIT; mRNA.
DR EMBL; BC094815; AAH94815.1; -; mRNA.
DR EMBL; BC104773; AAI04774.1; -; mRNA.
DR EMBL; BC104801; AAI04802.1; -; mRNA.
DR EMBL; BC143450; AAI43451.1; -; mRNA.
DR EMBL; BC143455; AAI43456.1; -; mRNA.
DR RefSeq; NP_001269781.1; NM_001282852.1.
DR RefSeq; NP_001269782.1; NM_001282853.1.
DR RefSeq; NP_001269783.1; NM_001282854.1.
DR RefSeq; NP_659449.3; NM_145012.5.
DR RefSeq; NP_859049.2; NM_181698.3.
DR RefSeq; XP_005252447.1; XM_005252390.1.
DR UniGene; Hs.14745; -.
DR UniGene; Hs.651463; -.
DR UniGene; Hs.714184; -.
DR ProteinModelPortal; Q8ND76; -.
DR IntAct; Q8ND76; 1.
DR MINT; MINT-1649053; -.
DR PhosphoSite; Q8ND76; -.
DR DMDM; 71658801; -.
DR PaxDb; Q8ND76; -.
DR PRIDE; Q8ND76; -.
DR DNASU; 219771; -.
DR Ensembl; ENST00000265375; ENSP00000265375; ENSG00000108100.
DR Ensembl; ENST00000339497; ENSP00000344275; ENSG00000108100.
DR Ensembl; ENST00000374704; ENSP00000363836; ENSG00000108100.
DR Ensembl; ENST00000374706; ENSP00000363838; ENSG00000108100.
DR GeneID; 219771; -.
DR KEGG; hsa:219771; -.
DR UCSC; uc001iyu.4; human.
DR CTD; 219771; -.
DR GeneCards; GC10P035576; -.
DR HGNC; HGNC:23354; CCNY.
DR HPA; HPA036290; -.
DR MIM; 612786; gene.
DR neXtProt; NX_Q8ND76; -.
DR PharmGKB; PA162381980; -.
DR eggNOG; NOG303674; -.
DR HOVERGEN; HBG058985; -.
DR InParanoid; Q8ND76; -.
DR OMA; YDKHDPE; -.
DR PhylomeDB; Q8ND76; -.
DR SignaLink; Q8ND76; -.
DR ChiTaRS; CCNY; human.
DR GeneWiki; CCNY_(gene); -.
DR GenomeRNAi; 219771; -.
DR NextBio; 90749; -.
DR PRO; PR:Q8ND76; -.
DR Bgee; Q8ND76; -.
DR CleanEx; HS_CCNY; -.
DR Genevestigator; Q8ND76; -.
DR GO; GO:0000308; C:cytoplasmic cyclin-dependent protein kinase holoenzyme complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein kinase activity; IDA:UniProtKB.
DR GO; GO:0060828; P:regulation of canonical Wnt receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.10.472.10; -; 1.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR012399; Cyclin_Y.
DR Pfam; PF00134; Cyclin_N; 1.
DR PIRSF; PIRSF028934; Cyclin_CG14939; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SUPFAM; SSF47954; SSF47954; 1.
DR PROSITE; PS00292; CYCLINS; FALSE_NEG.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Cell membrane;
KW Complete proteome; Cyclin; Lipoprotein; Membrane; Myristate; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation;
KW Wnt signaling pathway.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 341 Cyclin-Y.
FT /FTId=PRO_0000080514.
FT DOMAIN 143 265 Cyclin N-terminal.
FT MOD_RES 25 25 Phosphoserine.
FT MOD_RES 326 326 Phosphoserine.
FT LIPID 2 2 N-myristoyl glycine.
FT VAR_SEQ 1 54 Missing (in isoform 3).
FT /FTId=VSP_014833.
FT VAR_SEQ 52 76 Missing (in isoform 2).
FT /FTId=VSP_014834.
FT MUTAGEN 2 2 G->A: Induces a diffuse cytoplasmic
FT localization.
FT MUTAGEN 3 3 N->A: No effect on subcellular location.
FT CONFLICT 78 78 R -> G (in Ref. 4; AAL78998).
FT CONFLICT 118 118 Y -> H (in Ref. 4; AAL78999).
FT CONFLICT 155 155 S -> C (in Ref. 1; AAS79427 and 3;
FT AAL07802).
FT CONFLICT 171 171 I -> M (in Ref. 1; AAS79427 and 3;
FT AAL07802).
FT CONFLICT 190 190 I -> V (in Ref. 5; BAB71409).
FT CONFLICT 216 216 V -> A (in Ref. 1; AAS79427 and 3;
FT AAL07802).
FT CONFLICT 250 250 N -> S (in Ref. 5; BAB71409).
FT CONFLICT 268 268 S -> F (in Ref. 1; AAS79427 and 3;
FT AAL07802).
SQ SEQUENCE 341 AA; 39337 MW; 949FDE1EE45C2C6E CRC64;
MGNTTSCCVS SSPKLRRNAH SRLESYRPDT DLSREDTGCN LQHISDRENI DDLNMEFNPS
DHPRASTIFL SKSQTDVREK RKSLFINHHP PGQIARKYSS CSTIFLDDST VSQPNLKYTI
KCVALAIYYH IKNRDPDGRM LLDIFDENLH PLSKSEVPPD YDKHNPEQKQ IYRFVRTLFS
AAQLTAECAI VTLVYLERLL TYAEIDICPA NWKRIVLGAI LLASKVWDDQ AVWNVDYCQI
LKDITVEDMN ELERQFLELL QFNINVPSSV YAKYYFDLRS LAEANNLSFP LEPLSRERAH
KLEAISRLCE DKYKDLRRSA RKRSASADNL TLPRWSPAII S
//
ID CCNY_HUMAN Reviewed; 341 AA.
AC Q8ND76; B7ZKX9; D3DRY9; Q2M3V4; Q2TU96; Q6NT86; Q7Z4U7; Q8TEX2;
read moreAC Q8TEX3; Q96M99; Q96P45;
DT 02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 2.
DT 22-JAN-2014, entry version 113.
DE RecName: Full=Cyclin-Y;
DE Short=Cyc-Y;
DE AltName: Full=Cyclin box protein 1;
DE AltName: Full=Cyclin fold protein 1;
DE AltName: Full=cyclin-X;
GN Name=CCNY; Synonyms=C10orf9, CBCP1, CFP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP LOCATION, INTERACTION WITH CDK14, MYRISTOYLATION AT GLY-2, AND
RP MUTAGENESIS OF GLY-2 AND ASN-3.
RX PubMed=19524571; DOI=10.1016/j.febslet.2009.06.010;
RA Jiang M., Gao Y., Yang T., Zhu X., Chen J.;
RT "Cyclin Y, a novel membrane-associated cyclin, interacts with PFTK1.";
RL FEBS Lett. 583:2171-2178(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), FUNCTION,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=18060517; DOI=10.1007/s11033-007-9156-5;
RA Li X., Wang X., Liu G., Li R., Yu L.;
RT "Identification and characterization of cyclin X which activates
RT transcriptional activities of c-Myc.";
RL Mol. Biol. Rep. 36:97-103(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Gong L., Wu K.;
RT "Identification and characterization of CBCP1, a novel gene located on
RT human chromosome 10.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA Shannon M.;
RT "Human cyclin fold protein 1.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, Cerebellum, Neuroblastoma, and Testis;
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INTERACTION WITH
RP CDK14 AND LRP6, UBIQUITINATION, MYRISTOYLATION AT GLY-2, AND
RP MUTAGENESIS OF GLY-2.
RX PubMed=20059949; DOI=10.1016/j.devcel.2009.11.006;
RA Davidson G., Shen J., Huang Y.L., Su Y., Karaulanov E.,
RA Bartscherer K., Hassler C., Stannek P., Boutros M., Niehrs C.;
RT "Cell cycle control of wnt receptor activation.";
RL Dev. Cell 17:788-799(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CDK16, AND
RP PHOSPHORYLATION AT SER-326.
RX PubMed=22184064; DOI=10.1128/MCB.06261-11;
RA Mikolcevic P., Sigl R., Rauch V., Hess M.W., Pfaller K., Barisic M.,
RA Pelliniemi L.J., Boesl M., Geley S.;
RT "Cyclin-dependent kinase 16/PCTAIRE kinase 1 is activated by cyclin Y
RT and is essential for spermatogenesis.";
RL Mol. Cell. Biol. 32:868-879(2012).
CC -!- FUNCTION: Positive regulatory subunit of the cyclin-dependent
CC kinases CDK14/PFTK1 and CDK16. Acts as a cell-cycle regulator of
CC Wnt signaling pathway during G2/M phase by recruiting CDK14/PFTK1
CC to the plasma membrane and promoting phosphorylation of LRP6,
CC leading to the activation of the Wnt signaling pathway. Recruits
CC CDK16 to the plasma membrane. Isoform 3 might play a role in the
CC activation of MYC-mediated transcription.
CC -!- SUBUNIT: Interacts with CDK14, CDK16 and LRP6.
CC -!- INTERACTION:
CC O94921:CDK14; NbExp=11; IntAct=EBI-1049189, EBI-1043945;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC side.
CC -!- SUBCELLULAR LOCATION: Isoform 3: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=b;
CC IsoId=Q8ND76-1; Sequence=Displayed;
CC Name=2; Synonyms=a;
CC IsoId=Q8ND76-2; Sequence=VSP_014834;
CC Name=3;
CC IsoId=Q8ND76-3; Sequence=VSP_014833;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DEVELOPMENTAL STAGE: Enriched at G2/M.
CC -!- PTM: Ubiquitinated; leading to its degradation.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin Y subfamily.
CC -!- SIMILARITY: Contains 1 cyclin N-terminal domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH69224.1; Type=Erroneous initiation;
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DR EMBL; AY504868; AAS79427.1; -; mRNA.
DR EMBL; AF429969; AAP97301.1; -; mRNA.
DR EMBL; AF413522; AAL07802.1; -; mRNA.
DR EMBL; AF465728; AAL78998.1; -; mRNA.
DR EMBL; AF465729; AAL78999.1; -; mRNA.
DR EMBL; AK057280; BAB71409.1; -; mRNA.
DR EMBL; AL834355; CAD39020.2; -; mRNA.
DR EMBL; AL592445; CAH70072.1; -; Genomic_DNA.
DR EMBL; AL121749; CAH70072.1; JOINED; Genomic_DNA.
DR EMBL; AL603824; CAH70072.1; JOINED; Genomic_DNA.
DR EMBL; AL592445; CAH70073.1; -; Genomic_DNA.
DR EMBL; AL121749; CAH70073.1; JOINED; Genomic_DNA.
DR EMBL; AL603824; CAH70073.1; JOINED; Genomic_DNA.
DR EMBL; AL117336; CAH70073.1; JOINED; Genomic_DNA.
DR EMBL; AL603824; CAH71567.1; -; Genomic_DNA.
DR EMBL; AL121749; CAH71567.1; JOINED; Genomic_DNA.
DR EMBL; AL592445; CAH71567.1; JOINED; Genomic_DNA.
DR EMBL; AL603824; CAH71568.1; -; Genomic_DNA.
DR EMBL; AL121749; CAH71568.1; JOINED; Genomic_DNA.
DR EMBL; AL592445; CAH71568.1; JOINED; Genomic_DNA.
DR EMBL; AL117336; CAH71568.1; JOINED; Genomic_DNA.
DR EMBL; AL117336; CAH72501.1; -; Genomic_DNA.
DR EMBL; AL121749; CAH72501.1; JOINED; Genomic_DNA.
DR EMBL; AL603824; CAH72501.1; JOINED; Genomic_DNA.
DR EMBL; AL592445; CAH72501.1; JOINED; Genomic_DNA.
DR EMBL; AL121749; CAH73707.1; -; Genomic_DNA.
DR EMBL; AL603824; CAH73707.1; JOINED; Genomic_DNA.
DR EMBL; AL592445; CAH73707.1; JOINED; Genomic_DNA.
DR EMBL; AL121749; CAH73709.1; -; Genomic_DNA.
DR EMBL; AL603824; CAH73709.1; JOINED; Genomic_DNA.
DR EMBL; AL592445; CAH73709.1; JOINED; Genomic_DNA.
DR EMBL; AL117336; CAH73709.1; JOINED; Genomic_DNA.
DR EMBL; CH471072; EAW85912.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW85913.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW85914.1; -; Genomic_DNA.
DR EMBL; BC069224; AAH69224.1; ALT_INIT; mRNA.
DR EMBL; BC094815; AAH94815.1; -; mRNA.
DR EMBL; BC104773; AAI04774.1; -; mRNA.
DR EMBL; BC104801; AAI04802.1; -; mRNA.
DR EMBL; BC143450; AAI43451.1; -; mRNA.
DR EMBL; BC143455; AAI43456.1; -; mRNA.
DR RefSeq; NP_001269781.1; NM_001282852.1.
DR RefSeq; NP_001269782.1; NM_001282853.1.
DR RefSeq; NP_001269783.1; NM_001282854.1.
DR RefSeq; NP_659449.3; NM_145012.5.
DR RefSeq; NP_859049.2; NM_181698.3.
DR RefSeq; XP_005252447.1; XM_005252390.1.
DR UniGene; Hs.14745; -.
DR UniGene; Hs.651463; -.
DR UniGene; Hs.714184; -.
DR ProteinModelPortal; Q8ND76; -.
DR IntAct; Q8ND76; 1.
DR MINT; MINT-1649053; -.
DR PhosphoSite; Q8ND76; -.
DR DMDM; 71658801; -.
DR PaxDb; Q8ND76; -.
DR PRIDE; Q8ND76; -.
DR DNASU; 219771; -.
DR Ensembl; ENST00000265375; ENSP00000265375; ENSG00000108100.
DR Ensembl; ENST00000339497; ENSP00000344275; ENSG00000108100.
DR Ensembl; ENST00000374704; ENSP00000363836; ENSG00000108100.
DR Ensembl; ENST00000374706; ENSP00000363838; ENSG00000108100.
DR GeneID; 219771; -.
DR KEGG; hsa:219771; -.
DR UCSC; uc001iyu.4; human.
DR CTD; 219771; -.
DR GeneCards; GC10P035576; -.
DR HGNC; HGNC:23354; CCNY.
DR HPA; HPA036290; -.
DR MIM; 612786; gene.
DR neXtProt; NX_Q8ND76; -.
DR PharmGKB; PA162381980; -.
DR eggNOG; NOG303674; -.
DR HOVERGEN; HBG058985; -.
DR InParanoid; Q8ND76; -.
DR OMA; YDKHDPE; -.
DR PhylomeDB; Q8ND76; -.
DR SignaLink; Q8ND76; -.
DR ChiTaRS; CCNY; human.
DR GeneWiki; CCNY_(gene); -.
DR GenomeRNAi; 219771; -.
DR NextBio; 90749; -.
DR PRO; PR:Q8ND76; -.
DR Bgee; Q8ND76; -.
DR CleanEx; HS_CCNY; -.
DR Genevestigator; Q8ND76; -.
DR GO; GO:0000308; C:cytoplasmic cyclin-dependent protein kinase holoenzyme complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein kinase activity; IDA:UniProtKB.
DR GO; GO:0060828; P:regulation of canonical Wnt receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.10.472.10; -; 1.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR012399; Cyclin_Y.
DR Pfam; PF00134; Cyclin_N; 1.
DR PIRSF; PIRSF028934; Cyclin_CG14939; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SUPFAM; SSF47954; SSF47954; 1.
DR PROSITE; PS00292; CYCLINS; FALSE_NEG.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Cell membrane;
KW Complete proteome; Cyclin; Lipoprotein; Membrane; Myristate; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation;
KW Wnt signaling pathway.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 341 Cyclin-Y.
FT /FTId=PRO_0000080514.
FT DOMAIN 143 265 Cyclin N-terminal.
FT MOD_RES 25 25 Phosphoserine.
FT MOD_RES 326 326 Phosphoserine.
FT LIPID 2 2 N-myristoyl glycine.
FT VAR_SEQ 1 54 Missing (in isoform 3).
FT /FTId=VSP_014833.
FT VAR_SEQ 52 76 Missing (in isoform 2).
FT /FTId=VSP_014834.
FT MUTAGEN 2 2 G->A: Induces a diffuse cytoplasmic
FT localization.
FT MUTAGEN 3 3 N->A: No effect on subcellular location.
FT CONFLICT 78 78 R -> G (in Ref. 4; AAL78998).
FT CONFLICT 118 118 Y -> H (in Ref. 4; AAL78999).
FT CONFLICT 155 155 S -> C (in Ref. 1; AAS79427 and 3;
FT AAL07802).
FT CONFLICT 171 171 I -> M (in Ref. 1; AAS79427 and 3;
FT AAL07802).
FT CONFLICT 190 190 I -> V (in Ref. 5; BAB71409).
FT CONFLICT 216 216 V -> A (in Ref. 1; AAS79427 and 3;
FT AAL07802).
FT CONFLICT 250 250 N -> S (in Ref. 5; BAB71409).
FT CONFLICT 268 268 S -> F (in Ref. 1; AAS79427 and 3;
FT AAL07802).
SQ SEQUENCE 341 AA; 39337 MW; 949FDE1EE45C2C6E CRC64;
MGNTTSCCVS SSPKLRRNAH SRLESYRPDT DLSREDTGCN LQHISDRENI DDLNMEFNPS
DHPRASTIFL SKSQTDVREK RKSLFINHHP PGQIARKYSS CSTIFLDDST VSQPNLKYTI
KCVALAIYYH IKNRDPDGRM LLDIFDENLH PLSKSEVPPD YDKHNPEQKQ IYRFVRTLFS
AAQLTAECAI VTLVYLERLL TYAEIDICPA NWKRIVLGAI LLASKVWDDQ AVWNVDYCQI
LKDITVEDMN ELERQFLELL QFNINVPSSV YAKYYFDLRS LAEANNLSFP LEPLSRERAH
KLEAISRLCE DKYKDLRRSA RKRSASADNL TLPRWSPAII S
//
MIM
612786
*RECORD*
*FIELD* NO
612786
*FIELD* TI
*612786 CYCLIN Y; CCNY
;;CYCLIN-FOLD PROTEIN 1; CFP1;;
CYCLIN X; CCNX;;
CHROMOSOME 10 OPEN READING FRAME 9; C10ORF9
read more*FIELD* TX
DESCRIPTION
Cyclins, such as CCNY, control cell division cycles and regulate
cyclin-dependent kinases (e.g., CDC2; 116940) (Li et al., 2009).
CLONING
Using mass spectrometry to identify proteins upregulated in metastatic
versus nonmetastatic human colorectal adenocarcinoma cell lines,
followed by database analysis, Zhang et al. (2005) identified an isoform
of CCNY that they called CFP1 variant A. The deduced protein has a
calculated molecular mass of 36.9 kD.
By database analysis and PCR of a testis cDNA library, Li et al. (2009)
cloned CCNY, which they designated CCNX. The deduced 287-amino acid
protein has a central cyclin box and shares highest similarity with
cyclin B3 (CCNB3; 300456). RT-PCR detected highest expression in testis
and lower expression in all other tissues examined except brain and
kidney. Fluorescence-tagged CCNX was expressed predominantly in the
nucleus in a human nonsmall lung cancer cell line.
GENE STRUCTURE
Li et al. (2009) determined that the CCNY gene contains 12 exons.
MAPPING
By genomic sequence analysis, Deloukas et al. (2004) mapped the CCNY
gene to chromosome 10p11.2, where it lies between the CREM (123812) and
FZD8 (606146) genes.
GENE FUNCTION
Using the promoter regions of several cell cycle regulators and
transcription factors, Li et al. (2009) showed that CCNX specifically
activated transcription from the MYC (190080) promoter.
MOLECULAR GENETICS
For discussion of a possible association between variation in the CCNY
gene and inflammatory bowel disease, see IBD1 (266600).
*FIELD* RF
1. Deloukas, P.; Earthrowl, M. E.; Grafham, D. V.; Rubenfield, M.;
French, L.; Steward, C. A.; Sims, S. K.; Jones, M. C.; Searle, S.;
Scott, C.; Howe, K.; Hunt, S. E.; and 124 others: The DNA sequence
and comparative analysis of human chromosome 10. Nature 429: 151-157,
2004.
2. Li, X.; Wang, X.; Liu, G.; Li, R.; Yu, L.: Identification and
characterization of cyclin X which activates transcriptional activities
of c-Myc. Molec. Biol. Rep. 36: 97-103, 2009.
3. Zhang, Y.-T.; Geng, Y.-P.; Si, L.-S.; Wang, Y.-L.: Proteomic analysis
of differentially expressed proteins between metastatic and non-metastatic
human colorectal carcinoma cell lines. Europ. J. Gastroent. Hepatol. 17:
725-732, 2005.
*FIELD* CN
Marla J. F. O'Neill - updated: 12/10/2009
*FIELD* CD
Patricia A. Hartz: 5/15/2009
*FIELD* ED
terry: 12/10/2009
mgross: 5/15/2009
*RECORD*
*FIELD* NO
612786
*FIELD* TI
*612786 CYCLIN Y; CCNY
;;CYCLIN-FOLD PROTEIN 1; CFP1;;
CYCLIN X; CCNX;;
CHROMOSOME 10 OPEN READING FRAME 9; C10ORF9
read more*FIELD* TX
DESCRIPTION
Cyclins, such as CCNY, control cell division cycles and regulate
cyclin-dependent kinases (e.g., CDC2; 116940) (Li et al., 2009).
CLONING
Using mass spectrometry to identify proteins upregulated in metastatic
versus nonmetastatic human colorectal adenocarcinoma cell lines,
followed by database analysis, Zhang et al. (2005) identified an isoform
of CCNY that they called CFP1 variant A. The deduced protein has a
calculated molecular mass of 36.9 kD.
By database analysis and PCR of a testis cDNA library, Li et al. (2009)
cloned CCNY, which they designated CCNX. The deduced 287-amino acid
protein has a central cyclin box and shares highest similarity with
cyclin B3 (CCNB3; 300456). RT-PCR detected highest expression in testis
and lower expression in all other tissues examined except brain and
kidney. Fluorescence-tagged CCNX was expressed predominantly in the
nucleus in a human nonsmall lung cancer cell line.
GENE STRUCTURE
Li et al. (2009) determined that the CCNY gene contains 12 exons.
MAPPING
By genomic sequence analysis, Deloukas et al. (2004) mapped the CCNY
gene to chromosome 10p11.2, where it lies between the CREM (123812) and
FZD8 (606146) genes.
GENE FUNCTION
Using the promoter regions of several cell cycle regulators and
transcription factors, Li et al. (2009) showed that CCNX specifically
activated transcription from the MYC (190080) promoter.
MOLECULAR GENETICS
For discussion of a possible association between variation in the CCNY
gene and inflammatory bowel disease, see IBD1 (266600).
*FIELD* RF
1. Deloukas, P.; Earthrowl, M. E.; Grafham, D. V.; Rubenfield, M.;
French, L.; Steward, C. A.; Sims, S. K.; Jones, M. C.; Searle, S.;
Scott, C.; Howe, K.; Hunt, S. E.; and 124 others: The DNA sequence
and comparative analysis of human chromosome 10. Nature 429: 151-157,
2004.
2. Li, X.; Wang, X.; Liu, G.; Li, R.; Yu, L.: Identification and
characterization of cyclin X which activates transcriptional activities
of c-Myc. Molec. Biol. Rep. 36: 97-103, 2009.
3. Zhang, Y.-T.; Geng, Y.-P.; Si, L.-S.; Wang, Y.-L.: Proteomic analysis
of differentially expressed proteins between metastatic and non-metastatic
human colorectal carcinoma cell lines. Europ. J. Gastroent. Hepatol. 17:
725-732, 2005.
*FIELD* CN
Marla J. F. O'Neill - updated: 12/10/2009
*FIELD* CD
Patricia A. Hartz: 5/15/2009
*FIELD* ED
terry: 12/10/2009
mgross: 5/15/2009