CDYL
entrez
9425
canonical
uniprot
Q9Y232
canonical
ensembl
ENSG00000153046
resolver
ensp
ENSP00000330512
resolver
ensp
ENSP00000340908
resolver
ensp
ENSP00000380718
resolver
ensp
ENSP00000394076
resolver
ensp
ENSP00000561853
resolver
genesymbol
CDYL
resolver
genesymbol_syn
CDYL1
resolver
hgnc
HGNC:1811
resolver
uniprot
A8K6D6
resolver
uniprot
B4DLG4
resolver
uniprot
Q0VDG7
resolver
uniprot
Q32NC5
resolver
uniprot
Q5VX99
resolver
uniprot
Q6P7T5
resolver
uniprot
Q9BWZ2
resolver
uniprot
Q9Y424
resolver
uniprot_entry
CDYL_HUMAN
resolver
uniprot_sec
A8K6D6
resolver
uniprot_sec
B4DLG4
resolver
uniprot_sec
Q0VDG7
resolver
uniprot_sec
Q32NC5
resolver
uniprot_sec
Q5VX99
resolver
uniprot_sec
Q6P7T5
resolver
uniprot_sec
Q9BWZ2
resolver
uniprot_sec
Q9Y424
resolver
amino_acid_sequence
MTFQASHRSAWGKSRKKNWQYEGPTQKLFLKRNNVSAPDGPSDPSISVSSEQSGAQQPPALQVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHDFNRRHTEKQKESTLTRTNRTSPNNARKQISRSTNSNFSKTSPKALVIGKDHESKNSQLFAASQKFRKNTAPSLSSRKNMDLAKSGIKILVPKSPVKSRTAVDGFQSESPEKLDPVEQGQEDTVAPEVAAEKPVGALLGPGAERARMGSRPRIHPLVPQVPGPVTAAMATGLAVNGKGTSPFMDALTANGTTNIQTSVTGVTASKRKFIDDRRDQPFDKRLRFSVRQTESAYRYRDIVVRKQDGFTHILLSTKSSENNSLNPEVMREVQSALSTAAADDSKLVLLSAVGSVFCCGLDFIYFIRRLTDDRKRESTKMAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEMLLSGRKLTAQEACGKGLVSQVFWPGTFTQEVMVRIKELASCNPVVLEESKALVRCNMKMELEQANERECEVLKKIWGSAQGMDSMLKYLQRKIDEF
uniprot
proteins
ec_number
4.2.1.-
uniprot
proteins
function
FUNCTION: [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). {ECO:0000250|UniProtKB:Q9WTK2, ECO:0000269|PubMed:19061646, ECO:0000269|PubMed:19808672, ECO:0000269|PubMed:22009739, ECO:0000269|PubMed:28402439, ECO:0000269|PubMed:28803779, ECO:0000269|PubMed:29177481}.; FUNCTION: [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). {ECO:0000269|PubMed:19808672}.; FUNCTION: [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. {ECO:0000269|PubMed:19808672}.
uniprot
proteins
mass_dalton
66482
uniprot
proteins
mutagenesis
MUTAGEN 205; /note="S->A: No impact on recruitment to DNA double strand breaks."; /evidence="ECO:0000269|PubMed:29177481"; MUTAGEN 521; /note="S->A: Abolishes CoA-binding and ability to inhibit histone crotonylation."; /evidence="ECO:0000269|PubMed:28803779
uniprot
proteins
pubmed
10192397
uniprot
proteins
pubmed
12072557
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18438403
uniprot
proteins
pubmed
18450745
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19061646
uniprot
proteins
pubmed
19507244
uniprot
proteins
pubmed
19808672
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22009739
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
28402439
uniprot
proteins
pubmed
28803779
uniprot
proteins
pubmed
28842554
uniprot
proteins
pubmed
29177481
uniprot
proteins
sequence_length
598
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:18450745, ECO:0000269|PubMed:19808672, ECO:0000269|PubMed:29177481}. Chromosome {ECO:0000269|PubMed:19808672, ECO:0000269|PubMed:29177481}. Note=Recognizes and binds histone H3 trimethylated at 'Lys-9', dimethylated at 'Lys-27' and trimethylated at 'Lys-27' (H3K9me3, H3K27me2 and H3K27me3, respectively) on chromatin (PubMed:19808672). Multimerization is required for chromatin-binding (PubMed:19808672). Recruited to sites of DNA double strand breaks in a PARP1-dependent fashion (PubMed:29177481). {ECO:0000269|PubMed:19808672, ECO:0000269|PubMed:29177481}.
uniprot
proteins