CDYL_MOUSE
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 03-AUG-2022, entry version 157.
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}.
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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 iPTMnet; Q9WTK2; -.
DR PhosphoSitePlus; Q9WTK2; -.
DR EPD; Q9WTK2; -.
DR jPOST; Q9WTK2; -.
DR MaxQB; Q9WTK2; -.
DR PaxDb; Q9WTK2; -.
DR PeptideAtlas; Q9WTK2; -.
DR PRIDE; Q9WTK2; -.
DR ProteomicsDB; 283874; -. [Q9WTK2-1]
DR ProteomicsDB; 283875; -. [Q9WTK2-2]
DR Antibodypedia; 24514; 268 antibodies from 34 providers.
DR DNASU; 12593; -.
DR Ensembl; ENSMUST00000075220; ENSMUSP00000074707; ENSMUSG00000059288. [Q9WTK2-1]
DR Ensembl; ENSMUST00000163595; ENSMUSP00000131784; ENSMUSG00000059288. [Q9WTK2-2]
DR GeneID; 12593; -.
DR KEGG; mmu:12593; -.
DR UCSC; uc007qce.2; mouse. [Q9WTK2-1]
DR UCSC; uc007qcg.2; mouse. [Q9WTK2-2]
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; 1471901at2759; -.
DR PhylomeDB; Q9WTK2; -.
DR TreeFam; TF313375; -.
DR BRENDA; 4.2.1.150; 3474.
DR BioGRID-ORCS; 12593; 6 hits in 76 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 246 other tissues.
DR ExpressionAtlas; Q9WTK2; baseline and differential.
DR Genevisible; Q9WTK2; MM.
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 Gene3D; 1.10.12.10; -; 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 Pfam; PF00385; Chromo; 1.
DR Pfam; PF00378; ECH_1; 1.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
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
