ID CDYL_MOUSE Reviewed; 593 AA. AC Q9WTK2; Q3U0W2; Q6P6N3; DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 166. DE RecName: Full=Chromodomain Y-like protein {ECO:0000303|PubMed:10192397}; DE Short=CDY-like {ECO:0000303|PubMed:10192397}; DE AltName: Full=Crotonyl-CoA hydratase {ECO:0000250|UniProtKB:Q9Y232}; DE EC=4.2.1.- {ECO:0000250|UniProtKB:Q9Y232}; DE AltName: Full=Putative histone acetyltransferase Cdyl {ECO:0000305}; DE EC=2.3.1.48 {ECO:0000305|PubMed:12072557}; GN Name=Cdyl {ECO:0000303|PubMed:10192397, ECO:0000312|MGI:MGI:1339956}; 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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Testis; RX PubMed=10192397; DOI=10.1038/7771; RA Lahn B.T., Page D.C.; RT "Retroposition of autosomal mRNA yielded testis-specific gene family on RT human Y chromosome."; RL Nat. Genet. 21:429-433(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=NOD; TISSUE=Spleen; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=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 [4] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, RP AND ALTERNATIVE SPLICING. RX PubMed=12072557; DOI=10.1073/pnas.082248899; RA Lahn B.T., Tang Z.L., Zhou J., Barndt R.J., Parvinen M., Allis C.D., RA Page D.C.; RT "Previously uncharacterized histone acetyltransferases implicated in RT mammalian spermatogenesis."; RL Proc. Natl. Acad. Sci. U.S.A. 99:8707-8712(2002). RN [5] RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INTERACTION WITH HDAC1 RP AND HDAC2, AND MUTAGENESIS OF SER-516 AND 588-ARG-LYS-589. RX PubMed=12947414; DOI=10.1038/sj.embor.embor917; RA Caron C., Pivot-Pajot C., van Grunsven L.A., Col E., Lestrat C., RA Rousseaux S., Khochbin S.; RT "Cdyl: a new transcriptional co-repressor."; RL EMBO Rep. 4:877-882(2003). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-211, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Kidney, Lung, 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 (ISOFORM 2), AND SUBCELLULAR LOCATION. RX PubMed=24144980; DOI=10.1128/mcb.00866-13; RA Escamilla-Del-Arenal M., da Rocha S.T., Spruijt C.G., Masui O., Renaud O., RA Smits A.H., Margueron R., Vermeulen M., Heard E.; RT "Cdyl, a new partner of the inactive X chromosome and potential reader of RT H3K27me3 and H3K9me2."; RL Mol. Cell. Biol. 33:5005-5020(2013). RN [8] RP FUNCTION. RX PubMed=28076783; DOI=10.1016/j.celrep.2016.12.043; RA Qin R., Cao S., Lyu T., Qi C., Zhang W., Wang Y.; RT "CDYL deficiency disrupts neuronal migration and increases susceptibility RT to epilepsy."; RL Cell Rep. 18:380-390(2017). RN [9] RP INTERACTION WITH PRDM9 AND EHMT2. RX PubMed=27932493; DOI=10.1091/mbc.e16-09-0686; RA Parvanov E.D., Tian H., Billings T., Saxl R.L., Spruce C., Aithal R., RA Krejci L., Paigen K., Petkov P.M.; RT "PRDM9 interactions with other proteins provide a link between RT recombination hotspots and the chromosomal axis in meiosis."; RL Mol. Biol. Cell 28:488-499(2017). RN [10] RP FUNCTION (ISOFORM 2), SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE. RX PubMed=28803779; DOI=10.1016/j.molcel.2017.07.011; RA Liu S., Yu H., Liu Y., Liu X., Zhang Y., Bu C., Yuan S., Chen Z., Xie G., RA Li W., Xu B., Yang J., He L., Jin T., Xiong Y., Sun L., Liu X., Han C., RA Cheng Z., Liang J., Shang Y.; RT "Chromodomain protein CDYL acts as a crotonyl-CoA hydratase to regulate RT histone crotonylation and spermatogenesis."; RL Mol. Cell 67:853-866(2017). RN [11] RP FUNCTION, TISSUE SPECIFICITY, AND REPRESSION BY NEURONAL ACTIVITY. RX PubMed=28842554; DOI=10.1038/s41467-017-00368-z; RA Liu Y., Lai S., Ma W., Ke W., Zhang C., Liu S., Zhang Y., Pei F., Li S., RA Yi M., Shu Y., Shang Y., Liang J., Huang Z.; RT "CDYL suppresses epileptogenesis in mice through repression of axonal RT Nav1.6 sodium channel expression."; RL Nat. Commun. 8:355-355(2017). RN [12] RP SUBCELLULAR LOCATION. RX PubMed=29177481; DOI=10.1093/jmcb/mjx050; RA Abu-Zhayia E.R., Awwad S.W., Ben-Oz B.M., Khoury-Haddad H., Ayoub N.; RT "CDYL1 fosters double-strand break-induced transcription silencing and RT promotes homology-directed repair."; RL J. Mol. Cell Biol. 10:341-357(2018). RN [13] RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY SOCIAL DEFEAT STRESS. RX PubMed=30665597; DOI=10.1016/j.biopsych.2018.11.025; RA Liu Y., Li M., Fan M., Song Y., Yu H., Zhi X., Xiao K., Lai S., Zhang J., RA Jin X., Shang Y., Liang J., Huang Z.; RT "Chromodomain Y-like Protein-Mediated Histone Crotonylation Regulates RT Stress-Induced Depressive Behaviors."; RL Biol. Psychiatry 85:635-649(2019). CC -!- FUNCTION: [Isoform 2]: Chromatin reader protein that recognizes and CC binds histone H3 trimethylated at 'Lys-9', dimethylated at 'Lys-27' and CC trimethylated at 'Lys-27' (H3K9me3, H3K27me2 and H3K27me3, CC respectively) (PubMed:12947414). Part of multimeric repressive CC chromatin complexes, where it is required for transmission and CC restoration of repressive histone marks, thereby preserving the CC epigenetic landscape (PubMed:12947414). Required for chromatin CC targeting and maximal enzymatic activity of Polycomb repressive complex CC 2 (PRC2); acts as a positive regulator of PRC2 activity by bridging the CC pre-existing histone H3K27me3 and newly recruited PRC2 on neighboring CC nucleosomes (By similarity). Acts as a corepressor for REST by CC facilitating histone-lysine N-methyltransferase EHMT2 recruitment and CC H3K9 dimethylation at REST target genes for repression (By similarity). CC Involved in X chromosome inactivation in females: recruited to Xist CC RNA-coated X chromosome and facilitates propagation of H3K9me2 by CC anchoring EHMT2 (PubMed:24144980). Promotes EZH2 accumulation and CC H3K27me3 methylation at DNA double strand breaks (DSBs), thereby CC facilitating transcriptional repression at sites of DNA damage and CC homology-directed repair of DSBs (By similarity). Required for neuronal CC migration during brain development by repressing expression of RHOA CC (PubMed:28076783). By repressing the expression of SCN8A, contributes CC to the inhibition of intrinsic neuronal excitability and CC epileptogenesis (PubMed:28842554). In addition to acting as a chromatin CC reader, acts as a hydro-lyase (By similarity). Shows crotonyl-coA CC hydratase activity by mediating the conversion of crotonyl-CoA ((2E)- CC butenoyl-CoA) to beta-hydroxybutyryl-CoA (3-hydroxybutanoyl-CoA), CC thereby acting as a negative regulator of histone crotonylation (By CC similarity). Histone crotonylation is required during spermatogenesis; CC down-regulation of histone crotonylation by CDYL regulates the CC reactivation of sex chromosome-linked genes in round spermatids and CC histone replacement in elongating spermatids (PubMed:28803779). By CC regulating histone crotonylation and trimethylation of H3K27, may be CC involved in stress-induced depression-like behaviors, possibly by CC regulating VGF expression (PubMed:30665597). May have histone CC acetyltransferase activity; such activity is however unsure in vivo CC (PubMed:12072557). {ECO:0000250|UniProtKB:Q9Y232, CC ECO:0000269|PubMed:12072557, ECO:0000269|PubMed:12947414, CC ECO:0000269|PubMed:24144980, ECO:0000269|PubMed:28076783, CC ECO:0000269|PubMed:28803779, ECO:0000269|PubMed:28842554, CC ECO:0000269|PubMed:30665597}. CC -!- FUNCTION: [Isoform 1]: Not able to recognize and bind histone H3K9me3, CC histone H3K27me2 and histone H3K27me3, due to the presence of a N- CC terminal extension that inactivates the chromo domain. CC {ECO:0000250|UniProtKB:Q9Y232}. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L- CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; CC Evidence={ECO:0000305|PubMed:12072557}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-hydroxybutanoyl-CoA = (2E)-butenoyl-CoA + H2O; CC Xref=Rhea:RHEA:45584, ChEBI:CHEBI:15377, ChEBI:CHEBI:57332, CC ChEBI:CHEBI:78611; Evidence={ECO:0000250|UniProtKB:Q9Y232}; CC -!- SUBUNIT: Forms multimers and multimerization is required for stable CC binding to chromatin (By similarity). Interacts with HDAC1 and HDAC2 CC via its C-terminal acetyl-CoA-binding domain (PubMed:12947414). CC Interacts with EZH2, EED, SUZ12, REST, EHMT1 and EHMT2 (By similarity). CC Part of a complex containing at least CDYL, REST, WIZ, SETB1, EHMT1 and CC EHMT2 (By similarity). Part of a complex containing at least CDYL, CC MIER1, MIER2, HDAC1 and HDAC2 (By similarity). Interacts with CHAF1A CC and CHAF1B; bridging the CAF-1 complex to the MCM2-7 (MCM) complex (By CC similarity). Interacts with MCM3 and MCM5; bridging the CAF-1 complex CC to the MCM2-7 (MCM) complex (By similarity). Interacts with EHMT2 and CC PRDM9; interaction only takes place when PRDM9 is bound to hotspot DNA CC (PubMed:27932493). {ECO:0000250|UniProtKB:Q9Y232, CC ECO:0000269|PubMed:12947414, ECO:0000269|PubMed:27932493}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus CC {ECO:0000269|PubMed:12072557, ECO:0000269|PubMed:12947414, CC ECO:0000269|PubMed:24144980, ECO:0000269|PubMed:29177481}. Chromosome CC {ECO:0000269|PubMed:12947414, ECO:0000269|PubMed:24144980, CC ECO:0000269|PubMed:29177481}. Note=Recognizes and binds histone H3 CC trimethylated at 'Lys-9', dimethylated at 'Lys-27' and trimethylated at CC 'Lys-27' (H3K9me3, H3K27me2 and H3K27me3, respectively) on chromatin CC (PubMed:24144980). Multimerization is required for chromatin-binding CC (By similarity). Recruited to Xist RNA-coated X chromosome CC (PubMed:24144980). Recruited to sites of DNA double strand breaks in a CC PARP1-dependent fashion (PubMed:29177481). CC {ECO:0000250|UniProtKB:Q9Y232, ECO:0000269|PubMed:24144980, CC ECO:0000269|PubMed:29177481}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=a {ECO:0000250|UniProtKB:Q9Y232}, CDYL1a CC {ECO:0000250|UniProtKB:Q9Y232}; CC IsoId=Q9WTK2-1; Sequence=Displayed; CC Name=2; Synonyms=b {ECO:0000250|UniProtKB:Q9Y232}, CDYL1b CC {ECO:0000250|UniProtKB:Q9Y232}; CC IsoId=Q9WTK2-2; Sequence=VSP_026385, VSP_026386; CC -!- TISSUE SPECIFICITY: Highly expressed in testis (at protein level) CC (PubMed:10192397). Expressed in the hippocampus (at protein level) CC (PubMed:28842554). Expressed in the medial prefrontal cortex, prelimbic CC cortex, intralimbic cortex and cingulate cortex area (at protein level) CC (PubMed:30665597). Isoform 1: Expressed as 2 transcripts encoding the CC same protein, a ubiquitous transcript and a highly expressed testis- CC specific transcript (PubMed:10192397). {ECO:0000269|PubMed:10192397, CC ECO:0000269|PubMed:28842554, ECO:0000269|PubMed:30665597}. CC -!- DEVELOPMENTAL STAGE: Highly expressed in elongating spermatids during CC histone hyperacetylation. {ECO:0000269|PubMed:12072557, CC ECO:0000269|PubMed:12947414}. CC -!- INDUCTION: Down-regulated upon neuronal activity in the hippocampus CC (PubMed:28842554). Up-regulated after social defeat stress CC (PubMed:30665597). {ECO:0000269|PubMed:28842554, CC ECO:0000269|PubMed:30665597}. CC -!- DOMAIN: The chromo domain recognizes and binds histone H3K9me3, histone CC H3K27me2 and histone H3K27me3. {ECO:0000250|UniProtKB:Q9Y232}. CC -!- DOMAIN: The acetyl-CoA-binding domain mediates crotonyl-coA hydratase CC activity (By similarity). The acetyl-CoA-binding domain is required for CC recruitment to sites of DNA double strand breaks and for binding to CC poly (ADP ribose) moieties (By similarity). CC {ECO:0000250|UniProtKB:Q9Y232}. CC -!- DISRUPTION PHENOTYPE: Mice show no overt differences in body weight, CC but males display a substantial decrease in the size and weight of the CC testis and show reduced fertility. Males show decreased epididymal CC sperm counts, sperm cell motility, and sperm velocity and a marked CC increase in cell apoptosis in the testis. CC {ECO:0000269|PubMed:28803779}. CC -!- MISCELLANEOUS: Interaction with HDAC1 or HDAC2 prevents coenzyme A CC binding. {ECO:0000269|PubMed:12947414}. CC -!- CAUTION: Was initially reported to display histone acetyltransferase CC activity, with a preference for histone H4 (PubMed:12072557). Such CC activity is however unsure in vivo. Histone acetyltransferase activity CC would be in contradiction with the function of the protein in CC corepressor complexes (PubMed:12947414). Moreover, crystallographic CC studies in human demonstrated that it does not share any similarity CC with other acetyltransferases and instead forms a crotonase-like fold. CC {ECO:0000250|UniProtKB:Q9Y232, ECO:0000269|PubMed:12072557, CC ECO:0000269|PubMed:12947414}. 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; AF081260; AAD22736.1; -; mRNA. DR EMBL; AF081261; AAD22737.1; -; mRNA. DR EMBL; AK156509; BAE33739.1; -; mRNA. DR EMBL; BC055103; AAH55103.1; -; mRNA. DR EMBL; BC062123; AAH62123.1; -; mRNA. DR CCDS; CCDS49235.1; -. [Q9WTK2-1] DR CCDS; CCDS49236.1; -. [Q9WTK2-2] DR RefSeq; NP_001116858.1; NM_001123386.1. [Q9WTK2-2] DR RefSeq; NP_034011.1; NM_009881.3. [Q9WTK2-1] DR AlphaFoldDB; Q9WTK2; -. DR SMR; Q9WTK2; -. DR BioGRID; 198666; 1. DR STRING; 10090.ENSMUSP00000074707; -. DR ChEMBL; CHEMBL4523497; -. DR GlyGen; Q9WTK2; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9WTK2; -. DR PhosphoSitePlus; Q9WTK2; -. DR SwissPalm; Q9WTK2; -. DR EPD; Q9WTK2; -. DR jPOST; Q9WTK2; -. DR MaxQB; Q9WTK2; -. DR PaxDb; 10090-ENSMUSP00000074707; -. DR PeptideAtlas; Q9WTK2; -. DR ProteomicsDB; 283874; -. [Q9WTK2-1] DR ProteomicsDB; 283875; -. [Q9WTK2-2] DR Antibodypedia; 24514; 280 antibodies from 34 providers. DR DNASU; 12593; -. DR Ensembl; ENSMUST00000075220.14; ENSMUSP00000074707.7; ENSMUSG00000059288.15. [Q9WTK2-1] DR Ensembl; ENSMUST00000163595.3; ENSMUSP00000131784.3; ENSMUSG00000059288.15. [Q9WTK2-2] DR GeneID; 12593; -. DR KEGG; mmu:12593; -. DR UCSC; uc007qce.2; mouse. [Q9WTK2-1] DR UCSC; uc007qcg.2; mouse. [Q9WTK2-2] DR AGR; MGI:1339956; -. DR CTD; 9425; -. DR MGI; MGI:1339956; Cdyl. DR VEuPathDB; HostDB:ENSMUSG00000059288; -. DR eggNOG; KOG0016; Eukaryota. DR eggNOG; KOG1911; Eukaryota. DR GeneTree; ENSGT00940000155106; -. DR HOGENOM; CLU_009834_24_0_1; -. DR InParanoid; Q9WTK2; -. DR OMA; VPRSPMN; -. DR OrthoDB; 553487at2759; -. DR PhylomeDB; Q9WTK2; -. DR TreeFam; TF313375; -. DR BRENDA; 4.2.1.150; 3474. DR BioGRID-ORCS; 12593; 6 hits in 82 CRISPR screens. DR ChiTaRS; Cdyl; mouse. DR PRO; PR:Q9WTK2; -. DR Proteomes; UP000000589; Chromosome 13. DR RNAct; Q9WTK2; Protein. DR Bgee; ENSMUSG00000059288; Expressed in seminiferous tubule of testis and 249 other cell types or tissues. DR ExpressionAtlas; Q9WTK2; baseline and differential. DR GO; GO:0005694; C:chromosome; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0016607; C:nuclear speck; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB. DR GO; GO:0120092; F:crotonyl-CoA hydratase activity; ISS:UniProtKB. DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI. DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB. DR GO; GO:0120094; P:negative regulation of peptidyl-lysine crotonylation; IDA:UniProtKB. DR GO; GO:0060816; P:random inactivation of X chromosome; IDA:UniProtKB. DR GO; GO:0007286; P:spermatid development; IMP:UniProtKB. DR CDD; cd18634; CD_CDY; 1. DR CDD; cd06558; crotonase-like; 1. DR Gene3D; 2.40.50.40; -; 1. DR Gene3D; 1.10.12.10; Lyase 2-enoyl-coa Hydratase, Chain A, domain 2; 1. DR InterPro; IPR016197; Chromo-like_dom_sf. DR InterPro; IPR000953; Chromo/chromo_shadow_dom. DR InterPro; IPR023780; Chromo_domain. DR InterPro; IPR023779; Chromodomain_CS. DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf. DR InterPro; IPR001753; Enoyl-CoA_hydra/iso. DR InterPro; IPR014748; Enoyl-CoA_hydra_C. DR PANTHER; PTHR43684; -; 1. DR PANTHER; PTHR43684:SF5; CHROMODOMAIN Y-LIKE PROTEIN; 1. DR Pfam; PF00385; Chromo; 1. DR Pfam; PF00378; ECH_1; 1. DR SMART; SM00298; CHROMO; 1. DR SUPFAM; SSF54160; Chromo domain-like; 1. DR SUPFAM; SSF52096; ClpP/crotonase; 1. DR PROSITE; PS00598; CHROMO_1; 1. DR PROSITE; PS50013; CHROMO_2; 1. DR Genevisible; Q9WTK2; MM. PE 1: Evidence at protein level; KW Acyltransferase; Alternative splicing; Chromosome; Differentiation; Lyase; KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Repressor; KW Spermatogenesis; Transcription; Transcription regulation; Transferase. FT CHAIN 1..593 FT /note="Chromodomain Y-like protein" FT /id="PRO_0000080222" FT DOMAIN 56..116 FT /note="Chromo" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053" FT REGION 1..30 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 56..304 FT /note="Interaction with EZH2" FT /evidence="ECO:0000250|UniProtKB:Q9Y232" FT REGION 110..158 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 200..223 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 357..589 FT /note="Acetyl-CoA-binding domain" FT /evidence="ECO:0000255" FT COMPBIAS 119..146 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 83 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 130 FT /note="N6,N6,N6-trimethyllysine; by EHMT2; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9Y232" FT MOD_RES 130 FT /note="N6,N6-dimethyllysine; by EHMT2; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9Y232" FT MOD_RES 130 FT /note="N6-methyllysine; by EHMT2; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9Y232" FT MOD_RES 165 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Y232" FT MOD_RES 196 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Y232" FT MOD_RES 211 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT VAR_SEQ 1..49 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16141072" FT /id="VSP_026385" FT VAR_SEQ 50..57 FT /note="AIQDAETQ -> MASEELYE (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16141072" FT /id="VSP_026386" FT MUTAGEN 516 FT /note="S->A: Abolishes CoA-binding. No effect on FT transcriptional repressor activity." FT /evidence="ECO:0000269|PubMed:12947414" FT MUTAGEN 588..589 FT /note="RK->AA: Abolishes CoA-binding. No effect on FT transcriptional repressor activity." FT /evidence="ECO:0000269|PubMed:12947414" FT CONFLICT 489 FT /note="M -> I (in Ref. 2; BAE33739)" FT /evidence="ECO:0000305" SQ SEQUENCE 593 AA; 65211 MW; 470D5B97D7E52CCA CRC64; MGIGNSQPNS QEAQLCTLPE KAEQPTDDNT CQQNNVVPAT VSEPDQASPA IQDAETQVES IVDKRKNKKG KTEYLVRWKG YDSEDDTWEP EQHLVNCEEY IHDFNRRHNE RQKEGSLARA SRASPSNARK QISRSTHSTL SKTNSKALVV GKDHESKSSQ LLAASQKFRK NPAPSLANRK NMDLAKSGIK ILVPKSPVKG RTSVDGFQGE SPEKLDPVDQ GAEDTVAPEV TAEKPTGALL GPGAERARMG SRPRIHPLVP QVSGPVTAAM ATGLAVNGKG TSPFMDALAA NGTVTIQTSV TGVTAGKRKF IDDRRDQPFD KRLRFSVRQT ESAYRYRDIV VRKQDGFTHI LLSTKSSENN SLNPEVMKEV QSALSTAAAD DSKLVLLSAV GSVFCCGLDF IYFIRRLTDD RKRESTKMAD AIRNFVNTFI QFKKPIIVAV NGPAIGLGAS ILPLCDVVWA NEKAWFQTPY TTFGQSPDGC STVMFPKIMG GASANEMLFS GRKLTAQEAC GKGLVSQVFW PGTFTQEVMV RIKELASCNP VVLEESKALV RCNMKMELEQ ANERECEVLK KIWGSAQGMD SMLKYLQRKI DEF //