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Entry version 168 (18 Sep 2019)
Sequence version 2 (26 Jun 2007)
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Protein

Chromodomain Y-like protein

Gene

CDYL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Isoform 2: Chromatin reader protein that recognizes and binds histone H3 trimethylated at 'Lys-9', dimethylated at 'Lys-27' and trimethylated at 'Lys-27' (H3K9me3, H3K27me2 and H3K27me3, respectively) (PubMed:19808672, PubMed:28402439). Part of multimeric repressive chromatin complexes, where it is required for transmission and restoration of repressive histone marks, thereby preserving the epigenetic landscape (PubMed:28402439). 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 (PubMed:22009739). Acts as a corepressor for REST by facilitating histone-lysine N-methyltransferase EHMT2 recruitment and H3K9 dimethylation at REST target genes for repression (PubMed:19061646). Involved in X chromosome inactivation in females: recruited to Xist RNA-coated X chromosome and facilitates propagation of H3K9me2 by anchoring EHMT2 (By similarity). Promotes EZH2 accumulation and H3K27me3 methylation at DNA double strand breaks (DSBs), thereby facilitating transcriptional repression at sites of DNA damage and homology-directed repair of DSBs (PubMed:29177481). Required for neuronal migration during brain development by repressing expression of RHOA (By similarity). By repressing the expression of SCN8A, contributes to the inhibition of intrinsic neuronal excitability and epileptogenesis (By similarity). In addition to acting as a chromatin reader, acts as a hydro-lyase (PubMed:28803779). Shows crotonyl-coA hydratase activity by mediating the conversion of crotonyl-CoA ((2E)-butenoyl-CoA) to beta-hydroxybutyryl-CoA (3-hydroxybutanoyl-CoA), thereby acting as a negative regulator of histone crotonylation (PubMed:28803779). Histone crotonylation is required during spermatogenesis; down-regulation of histone crotonylation by CDYL regulates the reactivation of sex chromosome-linked genes in round spermatids and histone replacement in elongating spermatids (By similarity). By regulating histone crotonylation and trimethylation of H3K27, may be involved in stress-induced depression-like behaviors, possibly by regulating VGF expression (By similarity).By similarity6 Publications
Isoform 1: Not able to recognize and bind histone H3K9me3, histone H3K27me2 and histone H3K27me3, due to the presence of a N-terminal extension that inactivates the chromo domain (PubMed:19808672).1 Publication
Isoform 3: Not able to recognize and bind histone H3K9me3, histone H3K27me2 and histone H3K27me3, due to the absence of the chromo domain (PubMed:19808672). Acts as a negative regulator of isoform 2 by displacing isoform 2 from chromatin.1 Publication

Caution

Was initially reported to display histone acetyltransferase activity, with a preference for histone H4 (PubMed:12072557). Such activity is however unsure in vivo. Histone acetyltransferase activity would be in contradiction with the function of the protein in corepressor complexes (PubMed:19061646, PubMed:22009739). Moreover, crystallographic studies demonstrated that it does not share any similarity with other acetyltransferases and instead forms a crotonase-like fold (PubMed:19507244).4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=73.75 µM for (2E)-butenoyl-CoA1 Publication

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionLyase, Repressor
    Biological processDifferentiation, Spermatogenesis, Transcription, Transcription regulation

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Chromodomain Y-like protein1 Publication
    Short name:
    CDY-like1 Publication
    Alternative name(s):
    Crotonyl-CoA hydratase1 Publication (EC:4.2.1.-1 Publication)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:CDYL1 PublicationImported
    Synonyms:CDYL11 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 6

    Organism-specific databases

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:1811 CDYL

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    603778 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_Q9Y232

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Chromosome, Nucleus

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi205S → A: No impact on recruitment to DNA double strand breaks. 1 Publication1
    Mutagenesisi521S → A: Abolishes CoA-binding and ability to inhibit histone crotonylation. 1 Publication1

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    9425

    Open Targets

    More...
    OpenTargetsi
    ENSG00000153046

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA26356

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL3879827

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    CDYL

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    150421527

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000802211 – 598Chromodomain Y-like proteinAdd BLAST598

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei88PhosphoserineCombined sources1
    Modified residuei135N6,N6,N6-trimethyllysine; by EHMT2; alternate1 Publication1
    Modified residuei135N6,N6-dimethyllysine; by EHMT2; alternate1 Publication1
    Modified residuei135N6-methyllysine; by EHMT2; alternate1 Publication1
    Modified residuei170PhosphoserineCombined sources1
    Modified residuei201PhosphoserineCombined sources1
    Modified residuei216PhosphoserineCombined sources1

    Keywords - PTMi

    Methylation, Phosphoprotein

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    Q9Y232

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    Q9Y232

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...
    MassIVEi
    Q9Y232

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    Q9Y232

    PeptideAtlas

    More...
    PeptideAtlasi
    Q9Y232

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q9Y232

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    85621 [Q9Y232-1]
    85622 [Q9Y232-2]
    85623 [Q9Y232-3]
    85624 [Q9Y232-4]

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q9Y232

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...
    PhosphoSitePlusi
    Q9Y232

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Expressed in the hippocampus with reduced expression in epileptic tissue compared to normal adjacent tissue (at protein level) (PubMed:28842554). Ubiquitous (PubMed:19808672). Expressed at moderate levels in all tissues examined (PubMed:19808672). Isoform 2: Most abundantly expressed isoform (PubMed:19808672).2 Publications

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000153046 Expressed in 226 organ(s), highest expression level in placenta

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    Q9Y232 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q9Y232 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    CAB012249
    HPA035578

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Forms multimers and multimerization is required for stable binding to chromatin (PubMed:19808672).

    Interacts with HDAC1 and HDAC2 via its C-terminal acetyl-CoA-binding domain (By similarity).

    Interacts with EZH2, EED, SUZ12, REST, EHMT1 and EHMT2 (PubMed:19061646).

    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 (PubMed:22009739).

    Interacts with CHAF1A and CHAF1B; bridging the CAF-1 complex to the MCM2-7 (MCM) complex (PubMed:28402439).

    Interacts with MCM3 and MCM5; bridging the CAF-1 complex to the MCM2-7 (MCM) complex (PubMed:28402439). Recruited to Xist RNA-coated X chromosome (By similarity).

    By similarity4 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

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

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    114818, 50 interactors

    CORUM comprehensive resource of mammalian protein complexes

    More...
    CORUMi
    Q9Y232

    Protein interaction database and analysis system

    More...
    IntActi
    Q9Y232, 33 interactors

    Molecular INTeraction database

    More...
    MINTi
    Q9Y232

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000380718

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    Q9Y232

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1598
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    Q9Y232

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    Q9Y232

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini61 – 121ChromoPROSITE-ProRule annotationAdd BLAST61

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni61 – 309Interaction with EZH21 PublicationAdd BLAST249
    Regioni362 – 594Acetyl-CoA-binding domainSequence analysisAdd BLAST233

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The chromo domain recognizes and binds histone H3K9me3, histone H3K27me2 and histone H3K27me3.1 Publication
    The acetyl-CoA-binding domain mediates crotonyl-coA hydratase activity (PubMed:28803779). The acetyl-CoA-binding domain is required for recruitment to sites of DNA double strand breaks and for binding to poly (ADP ribose) moieties (PubMed:29177481).2 Publications

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG0016 Eukaryota
    KOG1911 Eukaryota
    COG1024 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000155106

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q9Y232

    KEGG Orthology (KO)

    More...
    KOi
    K00653

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    FQNESPE

    Database of Orthologous Groups

    More...
    OrthoDBi
    1471901at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q9Y232

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF313375

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.10.12.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR016197 Chromo-like_dom_sf
    IPR000953 Chromo/chromo_shadow_dom
    IPR023780 Chromo_domain
    IPR023779 Chromodomain_CS
    IPR029045 ClpP/crotonase-like_dom_sf
    IPR001753 Enoyl-CoA_hydra/iso
    IPR014748 Enoyl-CoA_hydra_C

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00385 Chromo, 1 hit
    PF00378 ECH_1, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00298 CHROMO, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52096 SSF52096, 1 hit
    SSF54160 SSF54160, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00598 CHROMO_1, 1 hit
    PS50013 CHROMO_2, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    This entry describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

    This entry has 4 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

    Isoform 1 (identifier: Q9Y232-1) [UniParc]FASTAAdd to basket
    Also known as: a1 Publication, CDYL1a1 Publication

    This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
            10         20         30         40         50
    MTFQASHRSA WGKSRKKNWQ YEGPTQKLFL KRNNVSAPDG PSDPSISVSS
    60 70 80 90 100
    EQSGAQQPPA LQVERIVDKR KNKKGKTEYL VRWKGYDSED DTWEPEQHLV
    110 120 130 140 150
    NCEEYIHDFN RRHTEKQKES TLTRTNRTSP NNARKQISRS TNSNFSKTSP
    160 170 180 190 200
    KALVIGKDHE SKNSQLFAAS QKFRKNTAPS LSSRKNMDLA KSGIKILVPK
    210 220 230 240 250
    SPVKSRTAVD GFQSESPEKL DPVEQGQEDT VAPEVAAEKP VGALLGPGAE
    260 270 280 290 300
    RARMGSRPRI HPLVPQVPGP VTAAMATGLA VNGKGTSPFM DALTANGTTN
    310 320 330 340 350
    IQTSVTGVTA SKRKFIDDRR DQPFDKRLRF SVRQTESAYR YRDIVVRKQD
    360 370 380 390 400
    GFTHILLSTK SSENNSLNPE VMREVQSALS TAAADDSKLV LLSAVGSVFC
    410 420 430 440 450
    CGLDFIYFIR RLTDDRKRES TKMAEAIRNF VNTFIQFKKP IIVAVNGPAI
    460 470 480 490 500
    GLGASILPLC DVVWANEKAW FQTPYTTFGQ SPDGCSTVMF PKIMGGASAN
    510 520 530 540 550
    EMLLSGRKLT AQEACGKGLV SQVFWPGTFT QEVMVRIKEL ASCNPVVLEE
    560 570 580 590
    SKALVRCNMK MELEQANERE CEVLKKIWGS AQGMDSMLKY LQRKIDEF
    Length:598
    Mass (Da):66,482
    Last modified:June 26, 2007 - v2
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA34E7221130626EC
    GO
    Isoform 2 (identifier: Q9Y232-2) [UniParc]FASTAAdd to basket
    Also known as: b1 Publication, CDYL1b1 Publication

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

    Note: Major isoform.1 Publication
    Show »
    Length:544
    Mass (Da):60,609
    Checksum:iD30E1CE197B67FC7
    GO
    Isoform 3 (identifier: Q9Y232-3) [UniParc]FASTAAdd to basket
    Also known as: c1 Publication, CDYL1c1 Publication

    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

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    C9JQG7C9JQG7_HUMAN
    Chromodomain Y-like protein
    CDYL
    171Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

    <p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence CAB43304 differs from that shown.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti205S → N in BAF84290 (PubMed:14702039).Curated1
    Sequence conflicti291D → N in BAG59526 (PubMed:14702039).Curated1
    Sequence conflicti443V → L in BAF84290 (PubMed:14702039).Curated1
    Sequence conflicti558N → S in BAG59526 (PubMed:14702039).Curated1
    Sequence conflicti584M → T in AAI19683 (PubMed:15489334).Curated1
    Sequence conflicti591L → M in AAI19683 (PubMed:15489334).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_0329362T → A1 PublicationCorresponds to variant dbSNP:rs3812179Ensembl.1
    Natural variantiVAR_0329379S → P1 PublicationCorresponds to variant dbSNP:rs3812178Ensembl.1
    Natural variantiVAR_03293848V → A1 PublicationCorresponds to variant dbSNP:rs13196069Ensembl.1
    Natural variantiVAR_03293960A → G1 PublicationCorresponds to variant dbSNP:rs28360500Ensembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0263821 – 289Missing in isoform 3. 1 PublicationAdd BLAST289
    Alternative sequenceiVSP_0410251 – 186Missing in isoform 4. 1 PublicationAdd BLAST186
    Alternative sequenceiVSP_0263831 – 54Missing in isoform 2. 2 PublicationsAdd BLAST54
    Alternative sequenceiVSP_02638455 – 62AQQPPALQ → MASEELYE in isoform 2. 2 Publications8

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    AF081258 mRNA Translation: AAD22734.1
    AF081259 mRNA Translation: AAD22735.1
    AK291601 mRNA Translation: BAF84290.1
    AK296985 mRNA Translation: BAG59526.1
    AL022725 Genomic DNA No translation available.
    AL356747 Genomic DNA No translation available.
    AL359643 Genomic DNA No translation available.
    BC061516 mRNA Translation: AAH61516.1
    BC108725 mRNA Translation: AAI08726.1
    BC119682 mRNA Translation: AAI19683.1
    AL050164 mRNA Translation: CAB43304.1 Sequence problems.

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS4491.2 [Q9Y232-2]
    CCDS47364.1 [Q9Y232-4]

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    T08789

    NCBI Reference Sequences

    More...
    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]

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000328908; ENSP00000330512; ENSG00000153046 [Q9Y232-1]
    ENST00000343762; ENSP00000340908; ENSG00000153046 [Q9Y232-4]
    ENST00000397588; ENSP00000380718; ENSG00000153046 [Q9Y232-2]
    ENST00000449732; ENSP00000394076; ENSG00000153046 [Q9Y232-4]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    9425

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:9425

    UCSC genome browser

    More...
    UCSCi
    uc003mwi.4 human [Q9Y232-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF081258 mRNA Translation: AAD22734.1
    AF081259 mRNA Translation: AAD22735.1
    AK291601 mRNA Translation: BAF84290.1
    AK296985 mRNA Translation: BAG59526.1
    AL022725 Genomic DNA No translation available.
    AL356747 Genomic DNA No translation available.
    AL359643 Genomic DNA No translation available.
    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]

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2DNTNMR-A63-119[»]
    2GTRX-ray1.90A/B/C338-598[»]
    SMRiQ9Y232
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi114818, 50 interactors
    CORUMiQ9Y232
    IntActiQ9Y232, 33 interactors
    MINTiQ9Y232
    STRINGi9606.ENSP00000380718

    Chemistry databases

    BindingDBiQ9Y232
    ChEMBLiCHEMBL3879827

    PTM databases

    iPTMnetiQ9Y232
    PhosphoSitePlusiQ9Y232

    Polymorphism and mutation databases

    BioMutaiCDYL
    DMDMi150421527

    Proteomic databases

    EPDiQ9Y232
    jPOSTiQ9Y232
    MassIVEiQ9Y232
    PaxDbiQ9Y232
    PeptideAtlasiQ9Y232
    PRIDEiQ9Y232
    ProteomicsDBi85621 [Q9Y232-1]
    85622 [Q9Y232-2]
    85623 [Q9Y232-3]
    85624 [Q9Y232-4]

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    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.4 human [Q9Y232-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    9425
    DisGeNETi9425

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    CDYL
    HGNCiHGNC:1811 CDYL
    HPAiCAB012249
    HPA035578
    MIMi603778 gene
    neXtProtiNX_Q9Y232
    OpenTargetsiENSG00000153046
    PharmGKBiPA26356

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG0016 Eukaryota
    KOG1911 Eukaryota
    COG1024 LUCA
    GeneTreeiENSGT00940000155106
    InParanoidiQ9Y232
    KOiK00653
    OMAiFQNESPE
    OrthoDBi1471901at2759
    PhylomeDBiQ9Y232
    TreeFamiTF313375

    Miscellaneous databases

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...
    ChiTaRSi
    CDYL human
    EvolutionaryTraceiQ9Y232

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

    More...
    GenomeRNAii
    9425

    Pharos

    More...
    Pharosi
    Q9Y232

    Protein Ontology

    More...
    PROi
    PR:Q9Y232

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000153046 Expressed in 226 organ(s), highest expression level in placenta
    ExpressionAtlasiQ9Y232 baseline and differential
    GenevisibleiQ9Y232 HS

    Family and domain databases

    Gene3Di1.10.12.10, 1 hit
    InterProiView protein in InterPro
    IPR016197 Chromo-like_dom_sf
    IPR000953 Chromo/chromo_shadow_dom
    IPR023780 Chromo_domain
    IPR023779 Chromodomain_CS
    IPR029045 ClpP/crotonase-like_dom_sf
    IPR001753 Enoyl-CoA_hydra/iso
    IPR014748 Enoyl-CoA_hydra_C
    PfamiView protein in Pfam
    PF00385 Chromo, 1 hit
    PF00378 ECH_1, 1 hit
    SMARTiView protein in SMART
    SM00298 CHROMO, 1 hit
    SUPFAMiSSF52096 SSF52096, 1 hit
    SSF54160 SSF54160, 1 hit
    PROSITEiView protein in PROSITE
    PS00598 CHROMO_1, 1 hit
    PS50013 CHROMO_2, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCDYL_HUMAN
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9Y232
    Secondary accession number(s): A8K6D6
    , B4DLG4, Q0VDG7, Q32NC5, Q5VX99, Q6P7T5, Q9BWZ2, Q9Y424
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 19, 2003
    Last sequence update: June 26, 2007
    Last modified: September 18, 2019
    This is version 168 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    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. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
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