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Q9WTK2

- CDYL_MOUSE

UniProt

Q9WTK2 - CDYL_MOUSE

Protein

Chromodomain Y-like protein

Gene

Cdyl

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Acts as a RE1-silencing transcription factor (REST) corepressor that facilitates histone-lysine N-methyltransferase EHMT2 recruitment and H3K9 dimethylation at REST target genes for repression. Required for chromatin targeting and maximal enzymatic activity of polycomb repressive complex 2 (PRC2); acts as a positive regulator of PRC2 activity by bridging the pre-existing histone H3K27me3 and newly recruited PRC2 on neighboring nucleosomes By similarity. Has histone acetyltransferase activity. May play a role in histone hyperacetylation during spermatid maturation.By similarity2 Publications

    Catalytic activityi

    Acetyl-CoA + [histone] = CoA + acetyl-[histone].

    GO - Molecular functioni

    1. histone acetyltransferase activity Source: UniProtKB-EC
    2. methylated histone binding Source: UniProtKB
    3. transcription corepressor activity Source: UniProtKB

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: UniProtKB-KW
    2. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Acyltransferase, Repressor, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chromodomain Y-like protein (EC:2.3.1.48)
    Short name:
    CDY-like
    Gene namesi
    Name:Cdyl
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:1339956. Cdyl.

    Subcellular locationi

    Nucleus 2 Publications

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi516 – 5161S → A: Abolishes CoA-binding. No effect on transcriptional repressor activity. 1 Publication
    Mutagenesisi588 – 5892RK → AA: Abolishes CoA-binding. No effect on transcriptional repressor activity.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 593593Chromodomain Y-like proteinPRO_0000080222Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei130 – 1301N6,N6,N6-trimethyllysine; by EHMT2; alternateBy similarity
    Modified residuei130 – 1301N6,N6-dimethyllysine; by EHMT2; alternateBy similarity
    Modified residuei130 – 1301N6-methyllysine; by EHMT2; alternateBy similarity

    Keywords - PTMi

    Methylation

    Proteomic databases

    PaxDbiQ9WTK2.
    PRIDEiQ9WTK2.

    PTM databases

    PhosphoSiteiQ9WTK2.

    Expressioni

    Tissue specificityi

    Highly expressed in testis (at protein level). Expressed as 2 transcripts: a ubiquitous transcript and a highly expressed testis-specific transcript.

    Developmental stagei

    Highly expressed in elongating spermatids during histone hyperacetylation.2 Publications

    Gene expression databases

    ArrayExpressiQ9WTK2.
    BgeeiQ9WTK2.
    CleanExiMM_CDYL.
    GenevestigatoriQ9WTK2.

    Interactioni

    Subunit structurei

    Forms multimers and multimerization is required for stable binding to chromatin. Interacts with histone H3K9me3, histone H3K27me2 and histone H3K27me3. Interacts with EZH2, EED, SUZ12, REST, EHMT1 and EHMT2. Part of a complex containing at least CDYL, REST, WIZ, SETB1, EHMT1 and EHMT2. Part of a complex containing at least CDYL, MIER1, MIER2, HDAC1 and HDAC2 By similarity. Interacts with HDAC1 and HDAC2 via its C-terminal acetyl-CoA-binding domain.By similarity1 Publication

    Protein-protein interaction databases

    IntActiQ9WTK2. 1 interaction.
    MINTiMINT-4090565.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9WTK2.
    SMRiQ9WTK2. Positions 57-114, 336-593.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini56 – 11661ChromoPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni56 – 304249Interaction with EZH2By similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 1 chromo domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1024.
    GeneTreeiENSGT00670000097595.
    HOGENOMiHOG000111507.
    HOVERGENiHBG006723.
    InParanoidiQ9WTK2.
    OMAiIHDFNRR.
    OrthoDBiEOG72RN06.
    PhylomeDBiQ9WTK2.
    TreeFamiTF313375.

    Family and domain databases

    Gene3Di3.90.226.10. 1 hit.
    InterProiIPR023780. Chromo_domain.
    IPR000953. Chromo_domain/shadow.
    IPR016197. Chromodomain-like.
    IPR023779. Chromodomain_CS.
    IPR029045. ClpP/crotonase-like_dom.
    IPR001753. Crotonase_core_superfam.
    [Graphical view]
    PfamiPF00385. Chromo. 1 hit.
    PF00378. ECH. 1 hit.
    [Graphical view]
    SMARTiSM00298. CHROMO. 1 hit.
    [Graphical view]
    SUPFAMiSSF52096. SSF52096. 1 hit.
    SSF54160. SSF54160. 1 hit.
    PROSITEiPS00598. CHROMO_1. 1 hit.
    PS50013. CHROMO_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9WTK2-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGIGNSQPNS QEAQLCTLPE KAEQPTDDNT CQQNNVVPAT VSEPDQASPA    50
    IQDAETQVES IVDKRKNKKG KTEYLVRWKG YDSEDDTWEP EQHLVNCEEY 100
    IHDFNRRHNE RQKEGSLARA SRASPSNARK QISRSTHSTL SKTNSKALVV 150
    GKDHESKSSQ LLAASQKFRK NPAPSLANRK NMDLAKSGIK ILVPKSPVKG 200
    RTSVDGFQGE SPEKLDPVDQ GAEDTVAPEV TAEKPTGALL GPGAERARMG 250
    SRPRIHPLVP QVSGPVTAAM ATGLAVNGKG TSPFMDALAA NGTVTIQTSV 300
    TGVTAGKRKF IDDRRDQPFD KRLRFSVRQT ESAYRYRDIV VRKQDGFTHI 350
    LLSTKSSENN SLNPEVMKEV QSALSTAAAD DSKLVLLSAV GSVFCCGLDF 400
    IYFIRRLTDD RKRESTKMAD AIRNFVNTFI QFKKPIIVAV NGPAIGLGAS 450
    ILPLCDVVWA NEKAWFQTPY TTFGQSPDGC STVMFPKIMG GASANEMLFS 500
    GRKLTAQEAC GKGLVSQVFW PGTFTQEVMV RIKELASCNP VVLEESKALV 550
    RCNMKMELEQ ANERECEVLK KIWGSAQGMD SMLKYLQRKI DEF 593
    Length:593
    Mass (Da):65,211
    Last modified:November 1, 1999 - v1
    Checksum:i470D5B97D7E52CCA
    GO
    Isoform 2 (identifier: Q9WTK2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-49: Missing.
         50-57: AIQDAETQ → MASEELYE

    Show »
    Length:544
    Mass (Da):60,142
    Checksum:iB8E3B85969ED9103
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti489 – 4891M → I in BAE33739. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4949Missing in isoform 2. 2 PublicationsVSP_026385Add
    BLAST
    Alternative sequencei50 – 578AIQDAETQ → MASEELYE in isoform 2. 2 PublicationsVSP_026386

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF081260 mRNA. Translation: AAD22736.1.
    AF081261 mRNA. Translation: AAD22737.1.
    AK156509 mRNA. Translation: BAE33739.1.
    BC055103 mRNA. Translation: AAH55103.1.
    BC062123 mRNA. Translation: AAH62123.1.
    CCDSiCCDS49235.1. [Q9WTK2-1]
    CCDS49236.1. [Q9WTK2-2]
    RefSeqiNP_001116858.1. NM_001123386.1. [Q9WTK2-2]
    NP_034011.1. NM_009881.3. [Q9WTK2-1]
    UniGeneiMm.29002.

    Genome annotation databases

    EnsembliENSMUST00000075220; ENSMUSP00000074707; ENSMUSG00000059288. [Q9WTK2-1]
    ENSMUST00000163595; ENSMUSP00000131784; ENSMUSG00000059288. [Q9WTK2-2]
    GeneIDi12593.
    KEGGimmu:12593.
    UCSCiuc007qce.2. mouse. [Q9WTK2-1]
    uc007qcg.2. mouse. [Q9WTK2-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF081260 mRNA. Translation: AAD22736.1 .
    AF081261 mRNA. Translation: AAD22737.1 .
    AK156509 mRNA. Translation: BAE33739.1 .
    BC055103 mRNA. Translation: AAH55103.1 .
    BC062123 mRNA. Translation: AAH62123.1 .
    CCDSi CCDS49235.1. [Q9WTK2-1 ]
    CCDS49236.1. [Q9WTK2-2 ]
    RefSeqi NP_001116858.1. NM_001123386.1. [Q9WTK2-2 ]
    NP_034011.1. NM_009881.3. [Q9WTK2-1 ]
    UniGenei Mm.29002.

    3D structure databases

    ProteinModelPortali Q9WTK2.
    SMRi Q9WTK2. Positions 57-114, 336-593.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9WTK2. 1 interaction.
    MINTi MINT-4090565.

    PTM databases

    PhosphoSitei Q9WTK2.

    Proteomic databases

    PaxDbi Q9WTK2.
    PRIDEi Q9WTK2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000075220 ; ENSMUSP00000074707 ; ENSMUSG00000059288 . [Q9WTK2-1 ]
    ENSMUST00000163595 ; ENSMUSP00000131784 ; ENSMUSG00000059288 . [Q9WTK2-2 ]
    GeneIDi 12593.
    KEGGi mmu:12593.
    UCSCi uc007qce.2. mouse. [Q9WTK2-1 ]
    uc007qcg.2. mouse. [Q9WTK2-2 ]

    Organism-specific databases

    CTDi 9425.
    MGIi MGI:1339956. Cdyl.

    Phylogenomic databases

    eggNOGi COG1024.
    GeneTreei ENSGT00670000097595.
    HOGENOMi HOG000111507.
    HOVERGENi HBG006723.
    InParanoidi Q9WTK2.
    OMAi IHDFNRR.
    OrthoDBi EOG72RN06.
    PhylomeDBi Q9WTK2.
    TreeFami TF313375.

    Miscellaneous databases

    NextBioi 281746.
    PROi Q9WTK2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9WTK2.
    Bgeei Q9WTK2.
    CleanExi MM_CDYL.
    Genevestigatori Q9WTK2.

    Family and domain databases

    Gene3Di 3.90.226.10. 1 hit.
    InterProi IPR023780. Chromo_domain.
    IPR000953. Chromo_domain/shadow.
    IPR016197. Chromodomain-like.
    IPR023779. Chromodomain_CS.
    IPR029045. ClpP/crotonase-like_dom.
    IPR001753. Crotonase_core_superfam.
    [Graphical view ]
    Pfami PF00385. Chromo. 1 hit.
    PF00378. ECH. 1 hit.
    [Graphical view ]
    SMARTi SM00298. CHROMO. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52096. SSF52096. 1 hit.
    SSF54160. SSF54160. 1 hit.
    PROSITEi PS00598. CHROMO_1. 1 hit.
    PS50013. CHROMO_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Retroposition of autosomal mRNA yielded testis-specific gene family on human Y chromosome."
      Lahn B.T., Page D.C.
      Nat. Genet. 21:429-433(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Testis.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: NOD.
      Tissue: Spleen.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Testis.
    4. "Previously uncharacterized histone acetyltransferases implicated in mammalian spermatogenesis."
      Lahn B.T., Tang Z.L., Zhou J., Barndt R.J., Parvinen M., Allis C.D., Page D.C.
      Proc. Natl. Acad. Sci. U.S.A. 99:8707-8712(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, ALTERNATIVE SPLICING.
    5. Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INTERACTION WITH HDAC1 AND HDAC2, MUTAGENESIS OF SER-516 AND 588-ARG-LYS-589.

    Entry informationi

    Entry nameiCDYL_MOUSE
    AccessioniPrimary (citable) accession number: Q9WTK2
    Secondary accession number(s): Q3U0W2, Q6P6N3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2003
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 104 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Interaction with HDAC1 or HDAC2 prevents coenzyme A binding.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3