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Q9Y232

- CDYL1_HUMAN

UniProt

Q9Y232 - CDYL1_HUMAN

Protein

Chromodomain Y-like protein

Gene

CDYL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (26 Jun 2007)
      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. Has histone acetyltransferase activity, with a preference for histone H4.3 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. protein binding Source: UniProtKB
    4. transcription corepressor activity Source: UniProtKB

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: UniProtKB-KW
    2. spermatogenesis Source: ProtInc
    3. 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
    Synonyms:CDYL1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:1811. CDYL.

    Subcellular locationi

    Nucleus 2 Publications

    GO - Cellular componenti

    1. nucleus Source: MGI

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26356.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 598598Chromodomain Y-like proteinPRO_0000080221Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei88 – 881Phosphoserine1 Publication
    Modified residuei135 – 1351N6,N6,N6-trimethyllysine; by EHMT2; alternate1 Publication
    Modified residuei135 – 1351N6,N6-dimethyllysine; by EHMT2; alternate1 Publication
    Modified residuei135 – 1351N6-methyllysine; by EHMT2; alternate1 Publication
    Modified residuei201 – 2011Phosphoserine1 Publication
    Modified residuei216 – 2161Phosphoserine3 Publications

    Keywords - PTMi

    Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y232.
    PaxDbiQ9Y232.
    PRIDEiQ9Y232.

    PTM databases

    PhosphoSiteiQ9Y232.

    Expressioni

    Tissue specificityi

    Ubiquitous. Expressed at moderate levels in all tissues examined. Isoform 2 is the most abundantly expressed isoform.1 Publication

    Gene expression databases

    ArrayExpressiQ9Y232.
    BgeeiQ9Y232.
    CleanExiHS_CDYL.
    GenevestigatoriQ9Y232.

    Organism-specific databases

    HPAiCAB012249.
    HPA035578.

    Interactioni

    Subunit structurei

    Forms multimers and multimerization is required for stable binding to chromatin. Interacts with HDAC1 and HDAC2 via its C-terminal acetyl-CoA-binding domain By similarity. 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 similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HIST1H3DP684315EBI-1387386,EBI-79722

    Protein-protein interaction databases

    BioGridi114818. 20 interactions.
    IntActiQ9Y232. 10 interactions.
    MINTiMINT-2829840.
    STRINGi9606.ENSP00000380718.

    Structurei

    Secondary structure

    1
    598
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi66 – 716
    Beta strandi77 – 815
    Helixi88 – 903
    Beta strandi92 – 954
    Turni96 – 983
    Helixi103 – 11311
    Beta strandi342 – 3498
    Beta strandi352 – 3576
    Beta strandi360 – 3634
    Helixi369 – 38416
    Beta strandi390 – 3978
    Helixi405 – 41410
    Helixi416 – 43621
    Beta strandi441 – 4455
    Helixi452 – 4554
    Helixi457 – 4593
    Beta strandi460 – 4667
    Beta strandi470 – 4723
    Turni475 – 4795
    Helixi486 – 4949
    Helixi496 – 50510
    Helixi511 – 5166
    Beta strandi521 – 5244
    Helixi526 – 5283
    Helixi529 – 54113
    Helixi545 – 55612
    Turni557 – 5593
    Helixi560 – 57920
    Turni581 – 5844
    Helixi585 – 59612

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DNTNMR-A63-119[»]
    2GTRX-ray1.90A/B/C338-598[»]
    ProteinModelPortaliQ9Y232.
    SMRiQ9Y232. Positions 62-120, 341-598.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y232.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini61 – 12161ChromoPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni61 – 309249Interaction with EZH2Add
    BLAST

    Sequence similaritiesi

    Contains 1 chromo domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1024.
    HOVERGENiHBG006723.
    OMAiIHDFNRR.
    OrthoDBiEOG72RN06.
    PhylomeDBiQ9Y232.
    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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y232-1) [UniParc]FASTAAdd to Basket

    Also known as: a

    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

    MTFQASHRSA WGKSRKKNWQ YEGPTQKLFL KRNNVSAPDG PSDPSISVSS    50
    EQSGAQQPPA LQVERIVDKR KNKKGKTEYL VRWKGYDSED DTWEPEQHLV 100
    NCEEYIHDFN RRHTEKQKES TLTRTNRTSP NNARKQISRS TNSNFSKTSP 150
    KALVIGKDHE SKNSQLFAAS QKFRKNTAPS LSSRKNMDLA KSGIKILVPK 200
    SPVKSRTAVD GFQSESPEKL DPVEQGQEDT VAPEVAAEKP VGALLGPGAE 250
    RARMGSRPRI HPLVPQVPGP VTAAMATGLA VNGKGTSPFM DALTANGTTN 300
    IQTSVTGVTA SKRKFIDDRR DQPFDKRLRF SVRQTESAYR YRDIVVRKQD 350
    GFTHILLSTK SSENNSLNPE VMREVQSALS TAAADDSKLV LLSAVGSVFC 400
    CGLDFIYFIR RLTDDRKRES TKMAEAIRNF VNTFIQFKKP IIVAVNGPAI 450
    GLGASILPLC DVVWANEKAW FQTPYTTFGQ SPDGCSTVMF PKIMGGASAN 500
    EMLLSGRKLT AQEACGKGLV SQVFWPGTFT QEVMVRIKEL ASCNPVVLEE 550
    SKALVRCNMK MELEQANERE CEVLKKIWGS AQGMDSMLKY LQRKIDEF 598
    Length:598
    Mass (Da):66,482
    Last modified:June 26, 2007 - v2
    Checksum:iA34E7221130626EC
    GO
    Isoform 2 (identifier: Q9Y232-2) [UniParc]FASTAAdd to Basket

    Also known as: b

    The sequence of this isoform differs from the canonical sequence as follows:
         1-54: Missing.
         55-62: AQQPPALQ → MASEELYE

    Show »
    Length:544
    Mass (Da):60,609
    Checksum:iD30E1CE197B67FC7
    GO
    Isoform 3 (identifier: Q9Y232-3) [UniParc]FASTAAdd to Basket

    Also known as: c

    The sequence of this isoform differs from the canonical sequence as follows:
         1-289: Missing.

    Show »
    Length:309
    Mass (Da):34,561
    Checksum:i6033C3171A80CB47
    GO
    Isoform 4 (identifier: Q9Y232-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-186: Missing.

    Show »
    Length:412
    Mass (Da):45,135
    Checksum:i6AFC72E69A0462A3
    GO

    Sequence cautioni

    The sequence CAB43304.1 differs from that shown. Reason:

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti205 – 2051S → N in BAF84290. (PubMed:14702039)Curated
    Sequence conflicti291 – 2911D → N in BAG59526. (PubMed:14702039)Curated
    Sequence conflicti443 – 4431V → L in BAF84290. (PubMed:14702039)Curated
    Sequence conflicti558 – 5581N → S in BAG59526. (PubMed:14702039)Curated
    Sequence conflicti584 – 5841M → T in AAI19683. (PubMed:15489334)Curated
    Sequence conflicti591 – 5911L → M in AAI19683. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2 – 21T → A.1 Publication
    Corresponds to variant rs3812179 [ dbSNP | Ensembl ].
    VAR_032936
    Natural varianti9 – 91S → P.1 Publication
    Corresponds to variant rs3812178 [ dbSNP | Ensembl ].
    VAR_032937
    Natural varianti48 – 481V → A.1 Publication
    Corresponds to variant rs13196069 [ dbSNP | Ensembl ].
    VAR_032938
    Natural varianti60 – 601A → G.1 Publication
    Corresponds to variant rs28360500 [ dbSNP | Ensembl ].
    VAR_032939

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 289289Missing in isoform 3. 1 PublicationVSP_026382Add
    BLAST
    Alternative sequencei1 – 186186Missing in isoform 4. 1 PublicationVSP_041025Add
    BLAST
    Alternative sequencei1 – 5454Missing in isoform 2. 2 PublicationsVSP_026383Add
    BLAST
    Alternative sequencei55 – 628AQQPPALQ → MASEELYE in isoform 2. 2 PublicationsVSP_026384

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF081258 mRNA. Translation: AAD22734.1.
    AF081259 mRNA. Translation: AAD22735.1.
    AK291601 mRNA. Translation: BAF84290.1.
    AK296985 mRNA. Translation: BAG59526.1.
    AL356747, AL022725, AL359643 Genomic DNA. Translation: CAC36888.2.
    AL359643, AL022725, AL356747 Genomic DNA. Translation: CAH73737.1.
    AL022725, AL356747, AL359643 Genomic DNA. Translation: CAI20892.1.
    BC061516 mRNA. Translation: AAH61516.1.
    BC108725 mRNA. Translation: AAI08726.1.
    BC119682 mRNA. Translation: AAI19683.1.
    AL050164 mRNA. Translation: CAB43304.1. Sequence problems.
    CCDSiCCDS4491.2. [Q9Y232-2]
    CCDS47364.1. [Q9Y232-4]
    PIRiT08789.
    RefSeqiNP_001137442.1. NM_001143970.1. [Q9Y232-4]
    NP_001137443.1. NM_001143971.1. [Q9Y232-4]
    NP_004815.3. NM_004824.3. [Q9Y232-2]
    UniGeneiHs.269092.

    Genome annotation databases

    EnsembliENST00000328908; ENSP00000330512; ENSG00000153046. [Q9Y232-1]
    ENST00000343762; ENSP00000340908; ENSG00000153046. [Q9Y232-4]
    ENST00000397588; ENSP00000380718; ENSG00000153046. [Q9Y232-2]
    ENST00000449732; ENSP00000394076; ENSG00000153046. [Q9Y232-4]
    GeneIDi9425.
    KEGGihsa:9425.
    UCSCiuc003mwi.3. human. [Q9Y232-1]
    uc003mwj.3. human. [Q9Y232-2]

    Polymorphism databases

    DMDMi150421527.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF081258 mRNA. Translation: AAD22734.1 .
    AF081259 mRNA. Translation: AAD22735.1 .
    AK291601 mRNA. Translation: BAF84290.1 .
    AK296985 mRNA. Translation: BAG59526.1 .
    AL356747 , AL022725 , AL359643 Genomic DNA. Translation: CAC36888.2 .
    AL359643 , AL022725 , AL356747 Genomic DNA. Translation: CAH73737.1 .
    AL022725 , AL356747 , AL359643 Genomic DNA. Translation: CAI20892.1 .
    BC061516 mRNA. Translation: AAH61516.1 .
    BC108725 mRNA. Translation: AAI08726.1 .
    BC119682 mRNA. Translation: AAI19683.1 .
    AL050164 mRNA. Translation: CAB43304.1 . Sequence problems.
    CCDSi CCDS4491.2. [Q9Y232-2 ]
    CCDS47364.1. [Q9Y232-4 ]
    PIRi T08789.
    RefSeqi NP_001137442.1. NM_001143970.1. [Q9Y232-4 ]
    NP_001137443.1. NM_001143971.1. [Q9Y232-4 ]
    NP_004815.3. NM_004824.3. [Q9Y232-2 ]
    UniGenei Hs.269092.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DNT NMR - A 63-119 [» ]
    2GTR X-ray 1.90 A/B/C 338-598 [» ]
    ProteinModelPortali Q9Y232.
    SMRi Q9Y232. Positions 62-120, 341-598.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114818. 20 interactions.
    IntActi Q9Y232. 10 interactions.
    MINTi MINT-2829840.
    STRINGi 9606.ENSP00000380718.

    PTM databases

    PhosphoSitei Q9Y232.

    Polymorphism databases

    DMDMi 150421527.

    Proteomic databases

    MaxQBi Q9Y232.
    PaxDbi Q9Y232.
    PRIDEi Q9Y232.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000328908 ; ENSP00000330512 ; ENSG00000153046 . [Q9Y232-1 ]
    ENST00000343762 ; ENSP00000340908 ; ENSG00000153046 . [Q9Y232-4 ]
    ENST00000397588 ; ENSP00000380718 ; ENSG00000153046 . [Q9Y232-2 ]
    ENST00000449732 ; ENSP00000394076 ; ENSG00000153046 . [Q9Y232-4 ]
    GeneIDi 9425.
    KEGGi hsa:9425.
    UCSCi uc003mwi.3. human. [Q9Y232-1 ]
    uc003mwj.3. human. [Q9Y232-2 ]

    Organism-specific databases

    CTDi 9425.
    GeneCardsi GC06P004706.
    HGNCi HGNC:1811. CDYL.
    HPAi CAB012249.
    HPA035578.
    MIMi 603778. gene.
    neXtProti NX_Q9Y232.
    PharmGKBi PA26356.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1024.
    HOVERGENi HBG006723.
    OMAi IHDFNRR.
    OrthoDBi EOG72RN06.
    PhylomeDBi Q9Y232.
    TreeFami TF313375.

    Miscellaneous databases

    ChiTaRSi CDYL. human.
    EvolutionaryTracei Q9Y232.
    GenomeRNAii 9425.
    NextBioi 35306.
    PROi Q9Y232.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y232.
    Bgeei Q9Y232.
    CleanExi HS_CDYL.
    Genevestigatori Q9Y232.

    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), VARIANTS ALA-2; PRO-9; ALA-48 AND GLY-60.
      Tissue: Testis.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
      Tissue: Placenta and Tongue.
    3. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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 2 AND 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 253-598 (ISOFORM 1).
      Tissue: Eye and Uterus.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-598.
      Tissue: Uterus.
    6. "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.
    7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Specificity of the chromodomain Y chromosome family of chromodomains for lysine-methylated ARK(S/T) motifs."
      Fischle W., Franz H., Jacobs S.A., Allis C.D., Khorasanizadeh S.
      J. Biol. Chem. 283:19626-19635(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "CDYL bridges REST and histone methyltransferases for gene repression and suppression of cellular transformation."
      Mulligan P., Westbrook T.F., Ottinger M., Pavlova N., Chang B., Macia E., Shi Y.J., Barretina J., Liu J., Howley P.M., Elledge S.J., Shi Y.
      Mol. Cell 32:718-726(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH REST; EHMT1 AND EHMT2, IDENTIFICATION IN A COMPLEX WITH REST; WIZ; SETB1; EHMT1 AND EHMT2, IDENTIFICATION IN A COMPLEX WITH MIER1; MIER2; HDAC1 AND HDAC2.
    11. Cited for: METHYLATION AT LYS-135, IDENTIFICATION BY MASS SPECTROMETRY.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88 AND SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Multimerization and H3K9me3 binding are required for CDYL1b heterochromatin association."
      Franz H., Mosch K., Soeroes S., Urlaub H., Fischle W.
      J. Biol. Chem. 284:35049-35059(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH H3K9ME3, TISSUE SPECIFICITY.
    14. Erratum
      Franz H., Mosch K., Soeroes S., Urlaub H., Fischle W.
      J. Biol. Chem. 285:11754-11754(2010)
    15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201 AND SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Corepressor protein CDYL functions as a molecular bridge between polycomb repressor complex 2 and repressive chromatin mark trimethylated histone lysine 27."
      Zhang Y., Yang X., Gui B., Xie G., Zhang D., Shang Y., Liang J.
      J. Biol. Chem. 286:42414-42425(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HISTONE H3K9ME3; HISTONE H3K27ME2; HISTONE H3K27ME3; EZH2; EED AND SUZ12.
    17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Crystal structures of human CDY proteins reveal a crotonase-like fold."
      Wu H., Min J., Antoshenko T., Plotnikov A.N.
      Proteins 76:1054-1061(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 338-598.
    19. "Solution structure of RSGI RUH-064, a chromo domain from human cDNA."
      RIKEN structural genomics initiative (RSGI)
      Submitted (OCT-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 55-120.

    Entry informationi

    Entry nameiCDYL1_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y232
    Secondary accession number(s): A8K6D6
    , B4DLG4, Q0VDG7, Q32NC5, Q5VX99, Q6P7T5, Q9BWZ2, Q9Y424
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2003
    Last sequence update: June 26, 2007
    Last modified: October 1, 2014
    This is version 123 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Interaction with HDAC1 or HDAC2 prevents Coenzyme A binding.By similarity

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3