CCNY_HUMAN
ID CCNY_HUMAN Reviewed; 341 AA.
AC Q8ND76; B7ZKX9; D3DRY9; Q2M3V4; Q2TU96; Q6NT86; Q7Z4U7; Q8TEX2; Q8TEX3;
AC Q96M99; Q96P45;
DT 02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 177.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP INTERACTION WITH CDK14, MYRISTOYLATION AT GLY-2, AND MUTAGENESIS OF GLY-2
RP 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, SUBCELLULAR
RP 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., 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).
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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA 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., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., 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., 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 [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 project:
RT 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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT 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 sequential
RT 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 IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 CDK14
RP AND LRP6, UBIQUITINATION, MYRISTOYLATION AT GLY-2, AND MUTAGENESIS OF
RP 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., Bartscherer K.,
RA 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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CDK16, AND PHOSPHORYLATION
RP 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 and
RT is essential for spermatogenesis.";
RL Mol. Cell. Biol. 32:868-879(2012).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-25; SER-83; SER-326
RP AND THR-331, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP PHOSPHORYLATION AT SER-25; THR-30; SER-33; THR-37; THR-67; SER-71; SER-73;
RP THR-75; SER-83; SER-99; SER-100; SER-102; SER-288; SER-295; SER-324 AND
RP SER-326, AND UBIQUITINATION.
RX PubMed=24794231; DOI=10.1016/j.febslet.2014.04.019;
RA Li S., Song W., Jiang M., Zeng L., Zhu X., Chen J.;
RT "Phosphorylation of cyclin Y by CDK14 induces its ubiquitination and
RT degradation.";
RL FEBS Lett. 588:1989-1996(2014).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-37; SER-326 AND THR-331, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
RP IDENTIFICATION IN A COMPLEX WITH CAPRIN2; LRP6 AND CDK14.
RX PubMed=27821587; DOI=10.1074/jbc.m116.744607;
RA Wang X., Jia Y., Fei C., Song X., Li L.;
RT "Caprin-2 positively regulates CDK14/Cyclin Y-mediated LRP5/6 constitutive
RT phosphorylation.";
RL J. Biol. Chem. 291:26427-26434(2016).
CC -!- FUNCTION: Positive regulatory subunit of the cyclin-dependent kinases
CC CDK14/PFTK1 and CDK16. Acts as a cell-cycle regulator of Wnt signaling
CC pathway during G2/M phase by recruiting CDK14/PFTK1 to the plasma
CC membrane and promoting phosphorylation of LRP6, leading to the
CC activation of the Wnt signaling pathway. Recruits CDK16 to the plasma
CC membrane. Isoform 3 might play a role in the activation of MYC-mediated
CC transcription. {ECO:0000269|PubMed:18060517,
CC ECO:0000269|PubMed:19524571, ECO:0000269|PubMed:20059949,
CC ECO:0000269|PubMed:22184064}.
CC -!- SUBUNIT: Found in a complex with CAPRIN2, LRP6 AND CDK14 during G2/M
CC stage; CAPRIN2 functions as a scaffold for the complex by binding to
CC CCNY via its N terminus and to CDK14 via its C terminus
CC (PubMed:27821587). Interacts with CDK14 (PubMed:19524571,
CC PubMed:20059949). Interacts with CDK16 (PubMed:22184064). Interacts
CC with LRP6 (PubMed:20059949). {ECO:0000269|PubMed:19524571,
CC ECO:0000269|PubMed:20059949, ECO:0000269|PubMed:22184064,
CC ECO:0000269|PubMed:27821587}.
CC -!- INTERACTION:
CC Q8ND76; O94921: CDK14; NbExp=7; IntAct=EBI-1049189, EBI-1043945;
CC Q8ND76; Q13616: CUL1; NbExp=3; IntAct=EBI-1049189, EBI-359390;
CC Q8ND76-1; Q00536: CDK16; NbExp=7; IntAct=EBI-11615526, EBI-726261;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18060517,
CC ECO:0000269|PubMed:19524571, ECO:0000269|PubMed:20059949,
CC ECO:0000269|PubMed:22184064}; Lipid-anchor
CC {ECO:0000269|PubMed:18060517, ECO:0000269|PubMed:19524571,
CC ECO:0000269|PubMed:20059949, ECO:0000269|PubMed:22184064}; Cytoplasmic
CC side {ECO:0000269|PubMed:18060517, ECO:0000269|PubMed:19524571,
CC ECO:0000269|PubMed:20059949, ECO:0000269|PubMed:22184064}.
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. {ECO:0000269|PubMed:18060517}.
CC -!- DEVELOPMENTAL STAGE: Enriched at G2/M. {ECO:0000269|PubMed:20059949}.
CC -!- PTM: Ubiquitinated; leading to its degradation.
CC {ECO:0000269|PubMed:20059949, ECO:0000269|PubMed:24794231}.
CC -!- PTM: Heavily phosphorylated. Phosphorylation at Ser-71 and Ser-73 by
CC CDK14 is enhanced during the G2 and M cell cycle phases, and creates a
CC phosphodegron triggering SCF-dependent ubiquitination.
CC {ECO:0000269|PubMed:24794231}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin Y subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH69224.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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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; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL603824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL117336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL121749; -; NOT_ANNOTATED_CDS; 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 CCDS; CCDS60513.1; -. [Q8ND76-2]
DR CCDS; CCDS7189.1; -. [Q8ND76-1]
DR CCDS; CCDS7190.1; -. [Q8ND76-3]
DR RefSeq; NP_001269781.1; NM_001282852.1. [Q8ND76-2]
DR RefSeq; NP_001269782.1; NM_001282853.1. [Q8ND76-3]
DR RefSeq; NP_001269783.1; NM_001282854.1.
DR RefSeq; NP_659449.3; NM_145012.5. [Q8ND76-1]
DR RefSeq; NP_859049.2; NM_181698.3. [Q8ND76-3]
DR RefSeq; XP_011517660.1; XM_011519358.1.
DR RefSeq; XP_011517662.1; XM_011519360.2.
DR RefSeq; XP_011517663.1; XM_011519361.1.
DR RefSeq; XP_011517664.1; XM_011519362.1.
DR RefSeq; XP_011517665.1; XM_011519363.1.
DR RefSeq; XP_011517666.1; XM_011519364.1.
DR RefSeq; XP_011517667.1; XM_011519365.2.
DR RefSeq; XP_011517668.1; XM_011519366.1.
DR RefSeq; XP_011517669.1; XM_011519367.1.
DR RefSeq; XP_011517670.1; XM_011519368.2.
DR RefSeq; XP_016871328.1; XM_017015839.1.
DR RefSeq; XP_016871329.1; XM_017015840.1.
DR RefSeq; XP_016871330.1; XM_017015841.1.
DR AlphaFoldDB; Q8ND76; -.
DR SMR; Q8ND76; -.
DR BioGRID; 128575; 50.
DR ComplexPortal; CPX-364; Cyclin Y-CDK14 complex.
DR ComplexPortal; CPX-379; Cyclin Y-CDK16 complex.
DR ELM; Q8ND76; -.
DR IntAct; Q8ND76; 17.
DR MINT; Q8ND76; -.
DR STRING; 9606.ENSP00000363836; -.
DR BindingDB; Q8ND76; -.
DR ChEMBL; CHEMBL3885550; -.
DR ChEMBL; CHEMBL4106161; -.
DR ChEMBL; CHEMBL4296115; -.
DR ChEMBL; CHEMBL4523634; -.
DR ChEMBL; CHEMBL4523637; -.
DR iPTMnet; Q8ND76; -.
DR PhosphoSitePlus; Q8ND76; -.
DR SwissPalm; Q8ND76; -.
DR BioMuta; CCNY; -.
DR DMDM; 71658801; -.
DR EPD; Q8ND76; -.
DR jPOST; Q8ND76; -.
DR MassIVE; Q8ND76; -.
DR MaxQB; Q8ND76; -.
DR PaxDb; Q8ND76; -.
DR PeptideAtlas; Q8ND76; -.
DR PRIDE; Q8ND76; -.
DR ProteomicsDB; 72984; -. [Q8ND76-1]
DR ProteomicsDB; 72985; -. [Q8ND76-2]
DR ProteomicsDB; 72986; -. [Q8ND76-3]
DR Antibodypedia; 26676; 216 antibodies from 28 providers.
DR DNASU; 219771; -.
DR Ensembl; ENST00000265375.13; ENSP00000265375.9; ENSG00000108100.18. [Q8ND76-3]
DR Ensembl; ENST00000339497.7; ENSP00000344275.5; ENSG00000108100.18. [Q8ND76-2]
DR Ensembl; ENST00000374704.8; ENSP00000363836.4; ENSG00000108100.18. [Q8ND76-1]
DR Ensembl; ENST00000374706.5; ENSP00000363838.1; ENSG00000108100.18. [Q8ND76-3]
DR GeneID; 219771; -.
DR KEGG; hsa:219771; -.
DR MANE-Select; ENST00000374704.8; ENSP00000363836.4; NM_145012.6; NP_659449.3.
DR UCSC; uc001iyu.6; human. [Q8ND76-1]
DR CTD; 219771; -.
DR DisGeNET; 219771; -.
DR GeneCards; CCNY; -.
DR HGNC; HGNC:23354; CCNY.
DR HPA; ENSG00000108100; Low tissue specificity.
DR MIM; 612786; gene.
DR neXtProt; NX_Q8ND76; -.
DR OpenTargets; ENSG00000108100; -.
DR PharmGKB; PA162381980; -.
DR VEuPathDB; HostDB:ENSG00000108100; -.
DR eggNOG; KOG1675; Eukaryota.
DR GeneTree; ENSGT00940000154453; -.
DR HOGENOM; CLU_055026_0_0_1; -.
DR InParanoid; Q8ND76; -.
DR OMA; PEHKQIY; -.
DR OrthoDB; 916284at2759; -.
DR PhylomeDB; Q8ND76; -.
DR TreeFam; TF314464; -.
DR PathwayCommons; Q8ND76; -.
DR SignaLink; Q8ND76; -.
DR SIGNOR; Q8ND76; -.
DR BioGRID-ORCS; 219771; 9 hits in 1083 CRISPR screens.
DR ChiTaRS; CCNY; human.
DR GeneWiki; CCNY_(gene); -.
DR GenomeRNAi; 219771; -.
DR Pharos; Q8ND76; Tbio.
DR PRO; PR:Q8ND76; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q8ND76; protein.
DR Bgee; ENSG00000108100; Expressed in sperm and 186 other tissues.
DR ExpressionAtlas; Q8ND76; baseline and differential.
DR Genevisible; Q8ND76; HS.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IPI:ComplexPortal.
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:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; IBA:GO_Central.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
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:0010508; P:positive regulation of autophagy; IDA:ComplexPortal.
DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:0045859; P:regulation of protein kinase activity; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IC:ComplexPortal.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd00043; CYCLIN; 1.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
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.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Cell membrane; Cyclin;
KW Lipoprotein; Membrane; Myristate; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation; Wnt signaling pathway.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..341
FT /note="Cyclin-Y"
FT /id="PRO_0000080514"
FT DOMAIN 143..265
FT /note="Cyclin N-terminal"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24794231,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 30
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24794231"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24794231"
FT MOD_RES 37
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24794231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 67
FT /note="Phosphothreonine; by CDK14"
FT /evidence="ECO:0000269|PubMed:24794231"
FT MOD_RES 71
FT /note="Phosphoserine; by CDK14"
FT /evidence="ECO:0000269|PubMed:24794231"
FT MOD_RES 73
FT /note="Phosphoserine; by CDK14"
FT /evidence="ECO:0000269|PubMed:24794231"
FT MOD_RES 75
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24794231"
FT MOD_RES 83
FT /note="Phosphoserine; by CDK14"
FT /evidence="ECO:0000269|PubMed:24794231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24794231"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24794231"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24794231"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGU5"
FT MOD_RES 288
FT /note="Phosphoserine; by CDK14"
FT /evidence="ECO:0000269|PubMed:24794231"
FT MOD_RES 295
FT /note="Phosphoserine; by CDK14"
FT /evidence="ECO:0000269|PubMed:24794231"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24794231"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22184064,
FT ECO:0000269|PubMed:24794231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 331
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:19524571,
FT ECO:0000269|PubMed:20059949"
FT VAR_SEQ 1..54
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:18060517"
FT /id="VSP_014833"
FT VAR_SEQ 52..76
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_014834"
FT MUTAGEN 2
FT /note="G->A: Induces a diffuse cytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:19524571,
FT ECO:0000269|PubMed:20059949"
FT MUTAGEN 3
FT /note="N->A: No effect on subcellular location."
FT /evidence="ECO:0000269|PubMed:19524571"
FT CONFLICT 78
FT /note="R -> G (in Ref. 4; AAL78998)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="Y -> H (in Ref. 4; AAL78999)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="S -> C (in Ref. 1; AAS79427 and 3; AAL07802)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="I -> M (in Ref. 1; AAS79427 and 3; AAL07802)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="I -> V (in Ref. 5; BAB71409)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="V -> A (in Ref. 1; AAS79427 and 3; AAL07802)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="N -> S (in Ref. 5; BAB71409)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="S -> F (in Ref. 1; AAS79427 and 3; AAL07802)"
FT /evidence="ECO:0000305"
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
