ID CCYL1_HUMAN Reviewed; 359 AA. AC Q8N7R7; Q6NX60; DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 2. DT 27-MAR-2024, entry version 167. DE RecName: Full=Cyclin-Y-like protein 1; GN Name=CCNYL1 {ECO:0000312|HGNC:HGNC:26868}; 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 [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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [3] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, 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 [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [8] 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112 AND SER-344, AND 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; SER-112 AND SER-344, AND RP IDENTIFICATION BY 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 [12] RP SUBCELLULAR LOCATION. 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112 AND SER-344, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67 AND SER-344, 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). CC -!- FUNCTION: Key regulator of Wnt signaling implicated in various CC biological processes including male fertility, embryonic neurogenesis CC and cortex development. Activates the cyclin-dependent kinase CDK16, CC and promotes sperm maturation. {ECO:0000250|UniProtKB:D3YUJ3}. CC -!- SUBUNIT: Interacts with CDK16; this interaction mutually increases the CC stability of CDK16 and CCNYL1 and increases the kinase activity of CC CDK16. {ECO:0000250|UniProtKB:D3YUJ3}. CC -!- INTERACTION: CC Q8N7R7; Q00536: CDK16; NbExp=4; IntAct=EBI-10103094, EBI-726261; CC Q8N7R7-2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12382996, EBI-16439278; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22184064}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q8N7R7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8N7R7-2; Sequence=VSP_029134; CC Name=3; CC IsoId=Q8N7R7-3; Sequence=VSP_029133; CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin Y subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH67253.1; Type=Frameshift; Evidence={ECO:0000305}; 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; AK097751; BAC05160.1; -; mRNA. DR EMBL; AC096772; AAY24056.1; -; Genomic_DNA. DR EMBL; CH471063; EAW70420.1; -; Genomic_DNA. DR EMBL; BC067253; AAH67253.1; ALT_FRAME; mRNA. DR CCDS; CCDS2377.1; -. [Q8N7R7-3] DR CCDS; CCDS46503.1; -. [Q8N7R7-2] DR CCDS; CCDS82564.1; -. [Q8N7R7-1] DR RefSeq; NP_001135772.1; NM_001142300.1. [Q8N7R7-2] DR RefSeq; NP_001317147.1; NM_001330218.1. [Q8N7R7-1] DR RefSeq; NP_689736.1; NM_152523.2. [Q8N7R7-3] DR AlphaFoldDB; Q8N7R7; -. DR SMR; Q8N7R7; -. DR BioGRID; 127353; 65. DR IntAct; Q8N7R7; 37. DR STRING; 9606.ENSP00000295414; -. DR iPTMnet; Q8N7R7; -. DR PhosphoSitePlus; Q8N7R7; -. DR SwissPalm; Q8N7R7; -. DR BioMuta; CCNYL1; -. DR DMDM; 160380580; -. DR EPD; Q8N7R7; -. DR jPOST; Q8N7R7; -. DR MassIVE; Q8N7R7; -. DR MaxQB; Q8N7R7; -. DR PeptideAtlas; Q8N7R7; -. DR ProteomicsDB; 72321; -. [Q8N7R7-1] DR ProteomicsDB; 72322; -. [Q8N7R7-2] DR ProteomicsDB; 72323; -. [Q8N7R7-3] DR Pumba; Q8N7R7; -. DR Antibodypedia; 52166; 132 antibodies from 21 providers. DR DNASU; 151195; -. DR Ensembl; ENST00000295414.8; ENSP00000295414.3; ENSG00000163249.13. [Q8N7R7-1] DR Ensembl; ENST00000339882.9; ENSP00000342344.5; ENSG00000163249.13. [Q8N7R7-2] DR Ensembl; ENST00000392209.7; ENSP00000376045.3; ENSG00000163249.13. [Q8N7R7-3] DR GeneID; 151195; -. DR KEGG; hsa:151195; -. DR MANE-Select; ENST00000295414.8; ENSP00000295414.3; NM_001330218.2; NP_001317147.1. DR UCSC; uc002vch.4; human. [Q8N7R7-1] DR AGR; HGNC:26868; -. DR CTD; 151195; -. DR DisGeNET; 151195; -. DR GeneCards; CCNYL1; -. DR HGNC; HGNC:26868; CCNYL1. DR HPA; ENSG00000163249; Low tissue specificity. DR MIM; 620559; gene. DR neXtProt; NX_Q8N7R7; -. DR OpenTargets; ENSG00000163249; -. DR PharmGKB; PA162382009; -. DR VEuPathDB; HostDB:ENSG00000163249; -. DR GeneTree; ENSGT00940000154453; -. DR HOGENOM; CLU_055026_0_0_1; -. DR InParanoid; Q8N7R7; -. DR OMA; RWADAYQ; -. DR OrthoDB; 5476605at2759; -. DR PhylomeDB; Q8N7R7; -. DR TreeFam; TF314464; -. DR PathwayCommons; Q8N7R7; -. DR SignaLink; Q8N7R7; -. DR BioGRID-ORCS; 151195; 70 hits in 1157 CRISPR screens. DR ChiTaRS; CCNYL1; human. DR GenomeRNAi; 151195; -. DR Pharos; Q8N7R7; Tdark. DR PRO; PR:Q8N7R7; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q8N7R7; Protein. DR Bgee; ENSG00000163249; Expressed in secondary oocyte and 147 other cell types or tissues. DR ExpressionAtlas; Q8N7R7; baseline and differential. 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:0019901; F:protein kinase binding; IEA:InterPro. DR GO; GO:0030317; P:flagellated sperm motility; ISS:UniProtKB. DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IBA:GO_Central. DR GO; GO:0001932; P:regulation of protein phosphorylation; ISS:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB. DR CDD; cd20540; CYCLIN_CCNY_like; 1. DR Gene3D; 1.10.472.10; Cyclin-like; 1. DR InterPro; IPR013763; Cyclin-like_dom. DR InterPro; IPR036915; Cyclin-like_sf. DR InterPro; IPR006671; Cyclin_N. DR InterPro; IPR012399; Cyclin_Y. DR PANTHER; PTHR14248; CYCLIN Y, ISOFORM A; 1. DR PANTHER; PTHR14248:SF32; CYCLIN-Y-LIKE PROTEIN 1; 1. DR Pfam; PF00134; Cyclin_N; 1. DR PIRSF; PIRSF028934; Cyclin_CG14939; 1. DR SMART; SM00385; CYCLIN; 1. DR SUPFAM; SSF47954; Cyclin-like; 1. DR Genevisible; Q8N7R7; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Cyclin; Differentiation; Membrane; KW Neurogenesis; Phosphoprotein; Reference proteome; Spermatogenesis. FT CHAIN 1..359 FT /note="Cyclin-Y-like protein 1" FT /id="PRO_0000309321" FT DOMAIN 145..267 FT /note="Cyclin N-terminal" FT MOD_RES 67 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 105 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 112 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 344 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..70 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_029133" FT VAR_SEQ 111..173 FT /note="VSPGQLTKKYSSCSTIFLDDSTVSQPNLRTTVKCVTLAIYYHIKNRDANRSL FT DIFDERSHPLT -> CDLSNILPHKEQ (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_029134" SQ SEQUENCE 359 AA; 40705 MW; 76381F33FE5C890C CRC64; MGNTLTCCVS PNASPKLGRR AGSAELYCAS DIYEAVSGDA VAVAPAVVEP AELDFGEGEG HHLQHISDRE MPEDLALESN PSDHPRASTI FLSKSQTDVR EKRKSNHLNH VSPGQLTKKY SSCSTIFLDD STVSQPNLRT TVKCVTLAIY YHIKNRDANR SLDIFDERSH PLTREKVPEE YFKHDPEHKF IYRFVRTLFS AAQLTAECAI VTLVYLERLL TYAEIDICPT NWKRIVLGAI LLASKVWDDQ AVWNVDYCQI LKDITVEDMN EMERHFLELL QFNINVPASV YAKYYFDLRS LADDNNLNFL FAPLSKERAQ NLEAISRLCE DKDLCRAAMR RSFSADNFIG IQRSKAILS //