CCNY_MOUSE
ID CCNY_MOUSE Reviewed; 341 AA.
AC Q8BGU5; Q8CI87; Q9CYN5;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Cyclin-Y;
DE AltName: Full=Cyclin fold protein 1;
GN Name=Ccny; Synonyms=Cfp1;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Skin, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Czech II, and FVB/N; TISSUE=Kidney, and Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280 AND SER-326, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, INTERACTION WITH CDK16, AND TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: Positive regulatory subunit of the cyclin-dependent kinase
CC CDK14/PFTK1. Acts as a cell-cycle regulator of Wnt signaling pathway
CC during G2/M phase by recruiting CDK14/PFTK1 to the plasma membrane and
CC promoting phosphorylation of LRP6, leading to the activation of the Wnt
CC signaling pathway (By similarity). Recruits CDK16 to the plasma
CC membrane (By similarity). Positive regulatory subunit of the cyclin-
CC dependent kinase CDK16. {ECO:0000250, 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 (By
CC similarity). Interacts with CDK14 (By similarity). Interacts with CDK16
CC (PubMed:22184064). Interacts with LRP6 (By similarity).
CC {ECO:0000250|UniProtKB:Q8ND76, ECO:0000269|PubMed:22184064}.
CC -!- INTERACTION:
CC Q8BGU5; Q04735: Cdk16; NbExp=3; IntAct=EBI-772904, EBI-11615670;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BGU5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BGU5-2; Sequence=VSP_014835;
CC -!- TISSUE SPECIFICITY: Detected in brain, heart, lung, skeletal muscle,
CC ovary, thymus and testis (at protein level).
CC {ECO:0000269|PubMed:22184064}.
CC -!- PTM: Ubiquitinated; leading to its degradation. {ECO:0000250}.
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:0000250|UniProtKB:Q8ND76}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin Y subfamily.
CC {ECO:0000305}.
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DR EMBL; AK017493; BAB30772.1; -; mRNA.
DR EMBL; AK028696; BAC26071.1; -; mRNA.
DR EMBL; AK076556; BAC36391.1; -; mRNA.
DR EMBL; BC023321; AAH23321.1; -; mRNA.
DR EMBL; BC035524; AAH35524.1; -; mRNA.
DR CCDS; CCDS29050.1; -. [Q8BGU5-1]
DR RefSeq; NP_080760.2; NM_026484.3. [Q8BGU5-1]
DR AlphaFoldDB; Q8BGU5; -.
DR SMR; Q8BGU5; -.
DR BioGRID; 212575; 5.
DR ComplexPortal; CPX-367; Cyclin Y-Cdk14 complex.
DR IntAct; Q8BGU5; 2.
DR MINT; Q8BGU5; -.
DR STRING; 10090.ENSMUSP00000050001; -.
DR iPTMnet; Q8BGU5; -.
DR PhosphoSitePlus; Q8BGU5; -.
DR SwissPalm; Q8BGU5; -.
DR EPD; Q8BGU5; -.
DR jPOST; Q8BGU5; -.
DR MaxQB; Q8BGU5; -.
DR PaxDb; Q8BGU5; -.
DR PeptideAtlas; Q8BGU5; -.
DR PRIDE; Q8BGU5; -.
DR ProteomicsDB; 279944; -. [Q8BGU5-1]
DR ProteomicsDB; 279945; -. [Q8BGU5-2]
DR Antibodypedia; 26676; 216 antibodies from 28 providers.
DR DNASU; 67974; -.
DR Ensembl; ENSMUST00000053917; ENSMUSP00000050001; ENSMUSG00000024286. [Q8BGU5-1]
DR Ensembl; ENSMUST00000234102; ENSMUSP00000157340; ENSMUSG00000024286. [Q8BGU5-2]
DR GeneID; 67974; -.
DR KEGG; mmu:67974; -.
DR UCSC; uc008eai.1; mouse. [Q8BGU5-1]
DR UCSC; uc012azd.1; mouse. [Q8BGU5-2]
DR CTD; 219771; -.
DR MGI; MGI:1915224; Ccny.
DR VEuPathDB; HostDB:ENSMUSG00000024286; -.
DR eggNOG; KOG1675; Eukaryota.
DR GeneTree; ENSGT00940000154453; -.
DR HOGENOM; CLU_055026_0_0_1; -.
DR InParanoid; Q8BGU5; -.
DR OMA; PEHKQIY; -.
DR OrthoDB; 916284at2759; -.
DR PhylomeDB; Q8BGU5; -.
DR TreeFam; TF314464; -.
DR BioGRID-ORCS; 67974; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Ccny; mouse.
DR PRO; PR:Q8BGU5; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8BGU5; protein.
DR Bgee; ENSMUSG00000024286; Expressed in aortic valve and 216 other tissues.
DR ExpressionAtlas; Q8BGU5; baseline and differential.
DR Genevisible; Q8BGU5; MM.
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; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS: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; ISS: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; ISS:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; ISO:MGI.
DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0045859; P:regulation of protein kinase activity; IBA:GO_Central.
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; Phosphoprotein; Reference proteome;
KW Ubl conjugation; Wnt signaling pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8ND76"
FT CHAIN 2..341
FT /note="Cyclin-Y"
FT /id="PRO_0000080515"
FT DOMAIN 143..265
FT /note="Cyclin N-terminal"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND76"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND76"
FT MOD_RES 30
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND76"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND76"
FT MOD_RES 37
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND76"
FT MOD_RES 67
FT /note="Phosphothreonine; by CDK14"
FT /evidence="ECO:0000250|UniProtKB:Q8ND76"
FT MOD_RES 71
FT /note="Phosphoserine; by CDK14"
FT /evidence="ECO:0000250|UniProtKB:Q8ND76"
FT MOD_RES 73
FT /note="Phosphoserine; by CDK14"
FT /evidence="ECO:0000250|UniProtKB:Q8ND76"
FT MOD_RES 75
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND76"
FT MOD_RES 83
FT /note="Phosphoserine; by CDK14"
FT /evidence="ECO:0000250|UniProtKB:Q8ND76"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND76"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND76"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND76"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 288
FT /note="Phosphoserine; by CDK14"
FT /evidence="ECO:0000250|UniProtKB:Q8ND76"
FT MOD_RES 295
FT /note="Phosphoserine; by CDK14"
FT /evidence="ECO:0000250|UniProtKB:Q8ND76"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND76"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 52..76
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014835"
FT CONFLICT 257
FT /note="L -> P (in Ref. 1; BAB30772)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 341 AA; 39395 MW; 6F16CE5B14559FCB CRC64;
MGNTTSCCVS SSPKLRRNAH SRLESYRPDT DLSREDTGCN LQHISDRENI DDLNMEFNPS
DHPRASTIFL SKSQTDVREK RKSLFINHHP PGQTSRKYSS CSTIFLDDST VSQPNLKYTI
KCVALAIYYH IKNRDPDGRM LLDIFDENLH PLSKSEVPPD YDKHNPEQKQ IYRFVRTLFS
AAQLTAECAI VTLVYLERLL TYAEIDICPA NWKRIVLGAI LLASKVWDDQ AVWNVDYCQI
LKDITVEDMN ELERQFLELL QFNINVPSSV YAKYYFDLRS LAEANNLSFP LEPLSRERAH
KLEAISRLCE DKYKDLRKPM RKRSASADNL ILPRWSPAII S
