CDYL

Functionⁱ

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

Catalytic activityⁱ

3-hydroxybutanoyl-CoA
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
(2E)-butenoyl-CoA
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
H₂O
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.21
  "Chromodomain protein CDYL acts as a crotonyl-CoA hydratase to regulate histone crotonylation and spermatogenesis."
  Liu S., Yu H., Liu Y., Liu X., Zhang Y., Bu C., Yuan S., Chen Z., Xie G., Li W., Xu B., Yang J., He L., Jin T., Xiong Y., Sun L., Liu X., Han C.
  , Cheng Z., Liang J., Shang Y.
  Mol. Cell 67:853-866(2017) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION (ISOFORM 2), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF SER-521.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
3-hydroxybutanoyl-CoA
zoom
=
(2E)-butenoyl-CoA
zoom
+
H₂O

Kineticsⁱ

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Lyase, Repressor
Biological process	Differentiation, Spermatogenesis, Transcription, Transcription regulation

Enzyme and pathway databases

BRENDAⁱ	4.2.1.150, 2681
PathwayCommonsⁱ	Q9Y232

Names & Taxonomyⁱ

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)
Gene namesⁱ	Name:CDYL1 PublicationImported Synonyms:CDYL11 Publication
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 6

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:1811, CDYL
MIMⁱ	603778, gene
neXtProtⁱ	NX_Q9Y232
VEuPathDBⁱ	HostDB:ENSG00000153046

Keywords - Cellular componentⁱ

Chromosome, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	205	S → A: No impact on recruitment to DNA double strand breaks. 1 Publication		1
Mutagenesisⁱ	521	S → A: Abolishes CoA-binding and ability to inhibit histone crotonylation. 1 Publication		1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	9425
Open Targets More...OpenTargetsⁱ	ENSG00000153046
PharmGKBⁱ	PA26356

Miscellaneous databases

Pharosⁱ	Q9Y232, Tchem

Pharosⁱ

Q9Y232, Tchem

Chemistry databases

ChEMBLⁱ	CHEMBL3879827

ChEMBLⁱ

CHEMBL3879827

Genetic variation databases

BioMutaⁱ	CDYL
DMDMⁱ	150421527

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000080221	1 – 598	Chromodomain Y-like proteinAdd BLAST		598

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	88	PhosphoserineCombined sources	1
Modified residueⁱ	135	N6,N6,N6-trimethyllysine; by EHMT2; alternate1 Publication	1
Modified residueⁱ	135	N6,N6-dimethyllysine; by EHMT2; alternate1 Publication	1
Modified residueⁱ	135	N6-methyllysine; by EHMT2; alternate1 Publication	1
Modified residueⁱ	170	PhosphoserineCombined sources	1
Modified residueⁱ	201	PhosphoserineCombined sources	1
Modified residueⁱ	216	PhosphoserineCombined sources	1

Keywords - PTMⁱ

Methylation, Phosphoprotein

Proteomic databases

EPDⁱ	Q9Y232
jPOSTⁱ	Q9Y232
MassIVEⁱ	Q9Y232
PaxDbⁱ	Q9Y232
PeptideAtlas More...PeptideAtlasⁱ	Q9Y232
PRIDEⁱ	Q9Y232
ProteomicsDBⁱ	85621 [Q9Y232-1] 85622 [Q9Y232-2] 85623 [Q9Y232-3] 85624 [Q9Y232-4]

PTM databases

iPTMnetⁱ	Q9Y232
PhosphoSitePlusⁱ	Q9Y232

Expressionⁱ

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

Bgeeⁱ	ENSG00000153046, Expressed in calcaneal tendon and 239 other tissues
ExpressionAtlasⁱ	Q9Y232, baseline and differential
Genevisibleⁱ	Q9Y232, HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000153046, Low tissue specificity

HPAⁱ

ENSG00000153046, Low tissue specificity

Interactionⁱ

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).

Interacts with EHMT2 and PRDM9; interaction only takes place when PRDM9 is bound to hotspot DNA (By similarity).

By similarity4 Publications

Binary interactionsⁱ

Hide details

Q9Y232

With	#Exp.	IntAct
FXR1 [P51114]	2	EBI-1387386,EBI-713291
H3C12 [P68431]	5	EBI-1387386,EBI-79722

CDYL - isoform 2 [Q9Y232-2]

With	#Exp.	IntAct
itself	3	EBI-10986891,EBI-10986891
TTC9C [Q8N5M4]	3	EBI-10986891,EBI-2851213

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	114818, 59 interactors
CORUMⁱ	Q9Y232
IntActⁱ	Q9Y232, 36 interactors
Molecular INTeraction database More...MINTⁱ	Q9Y232
STRINGⁱ	9606.ENSP00000380718

Chemistry databases

BindingDBⁱ

Q9Y232

Miscellaneous databases

RNActⁱ	Q9Y232, protein

RNActⁱ

Q9Y232, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	66 – 71	Combined sources	6
Beta strandⁱ	77 – 81	Combined sources	5
Helixⁱ	88 – 90	Combined sources	3
Beta strandⁱ	92 – 95	Combined sources	4
Turnⁱ	96 – 98	Combined sources	3
Helixⁱ	103 – 113	Combined sources	11
Beta strandⁱ	342 – 349	Combined sources	8
Beta strandⁱ	352 – 357	Combined sources	6
Beta strandⁱ	360 – 363	Combined sources	4
Helixⁱ	369 – 384	Combined sources	16
Beta strandⁱ	390 – 397	Combined sources	8
Helixⁱ	405 – 414	Combined sources	10
Helixⁱ	416 – 436	Combined sources	21
Beta strandⁱ	441 – 445	Combined sources	5
Helixⁱ	452 – 455	Combined sources	4
Helixⁱ	457 – 459	Combined sources	3
Beta strandⁱ	460 – 466	Combined sources	7
Beta strandⁱ	470 – 472	Combined sources	3
Turnⁱ	475 – 479	Combined sources	5
Helixⁱ	486 – 494	Combined sources	9
Helixⁱ	496 – 505	Combined sources	10
Helixⁱ	511 – 516	Combined sources	6
Beta strandⁱ	521 – 524	Combined sources	4
Helixⁱ	526 – 528	Combined sources	3
Helixⁱ	529 – 541	Combined sources	13
Helixⁱ	545 – 556	Combined sources	12
Turnⁱ	557 – 559	Combined sources	3
Helixⁱ	560 – 579	Combined sources	20
Turnⁱ	581 – 584	Combined sources	4
Helixⁱ	585 – 596	Combined sources	12

Show more details

3D structure databases

SMRⁱ	Q9Y232
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q9Y232

EvolutionaryTraceⁱ

Q9Y232

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	61 – 121	ChromoPROSITE-ProRule annotationAdd BLAST		61

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	1 – 76	DisorderedSequence analysisAdd BLAST	76
Regionⁱ	61 – 309	Interaction with EZH21 PublicationAdd BLAST	249
Regionⁱ	112 – 149	DisorderedSequence analysisAdd BLAST	38
Regionⁱ	204 – 226	DisorderedSequence analysisAdd BLAST	23
Regionⁱ	362 – 594	Acetyl-CoA-binding domainSequence analysisAdd BLAST	233

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	27 – 59	Polar residuesSequence analysisAdd BLAST		33
Compositional biasⁱ	123 – 149	Polar residuesSequence analysisAdd BLAST		27

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

eggNOGⁱ	KOG0016, Eukaryota KOG1911, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000155106
HOGENOMⁱ	CLU_009834_24_0_1
InParanoidⁱ	Q9Y232
OMAⁱ	VPRSPMN
Database of Orthologous Groups More...OrthoDBⁱ	1471901at2759
PhylomeDBⁱ	Q9Y232
TreeFamⁱ	TF313375

Family and domain databases

Gene3Dⁱ	1.10.12.10, 1 hit
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
SMARTⁱ	View protein in SMART SM00298, CHROMO, 1 hit
SUPFAMⁱ	SSF52096, SSF52096, 1 hit SSF54160, SSF54160, 1 hit
PROSITEⁱ	View protein in PROSITE PS00598, CHROMO_1, 1 hit PS50013, CHROMO_2, 1 hit

Sequences (4+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 4 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 4 described isoforms and 2 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: Q9Y232-1) [UniParc]FASTA Add to basket

Also known as: a1 Publication, CDYL1a1 Publication

This isoform has been chosen as the 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

Checksum:ⁱA34E7221130626EC

GO

Isoform 2 (identifier: Q9Y232-2) [UniParc]FASTA Add 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

« Hide

        10         20         30         40         50
MASEELYEVE RIVDKRKNKK GKTEYLVRWK GYDSEDDTWE PEQHLVNCEE 
        60         70         80         90        100
YIHDFNRRHT EKQKESTLTR TNRTSPNNAR KQISRSTNSN FSKTSPKALV 
       110        120        130        140        150
IGKDHESKNS QLFAASQKFR KNTAPSLSSR KNMDLAKSGI KILVPKSPVK 
       160        170        180        190        200
SRTAVDGFQS ESPEKLDPVE QGQEDTVAPE VAAEKPVGAL LGPGAERARM 
       210        220        230        240        250
GSRPRIHPLV PQVPGPVTAA MATGLAVNGK GTSPFMDALT ANGTTNIQTS 
       260        270        280        290        300
VTGVTASKRK FIDDRRDQPF DKRLRFSVRQ TESAYRYRDI VVRKQDGFTH 
       310        320        330        340        350
ILLSTKSSEN NSLNPEVMRE VQSALSTAAA DDSKLVLLSA VGSVFCCGLD 
       360        370        380        390        400
FIYFIRRLTD DRKRESTKMA EAIRNFVNTF IQFKKPIIVA VNGPAIGLGA 
       410        420        430        440        450
SILPLCDVVW ANEKAWFQTP YTTFGQSPDG CSTVMFPKIM GGASANEMLL 
       460        470        480        490        500
SGRKLTAQEA CGKGLVSQVF WPGTFTQEVM VRIKELASCN PVVLEESKAL 
       510        520        530        540 
VRCNMKMELE QANERECEVL KKIWGSAQGM DSMLKYLQRK IDEF

Note: Major isoform.1 Publication

Show »

Length:544

Mass (Da):60,609

Checksum:ⁱD30E1CE197B67FC7

GO

Isoform 3 (identifier: Q9Y232-3) [UniParc]FASTA Add to basket

Also known as: c1 Publication, CDYL1c1 Publication

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

« Hide

        10         20         30         40         50
MDALTANGTT NIQTSVTGVT ASKRKFIDDR RDQPFDKRLR FSVRQTESAY 
        60         70         80         90        100
RYRDIVVRKQ DGFTHILLST KSSENNSLNP EVMREVQSAL STAAADDSKL 
       110        120        130        140        150
VLLSAVGSVF CCGLDFIYFI RRLTDDRKRE STKMAEAIRN FVNTFIQFKK 
       160        170        180        190        200
PIIVAVNGPA IGLGASILPL CDVVWANEKA WFQTPYTTFG QSPDGCSTVM 
       210        220        230        240        250
FPKIMGGASA NEMLLSGRKL TAQEACGKGL VSQVFWPGTF TQEVMVRIKE 
       260        270        280        290        300
LASCNPVVLE ESKALVRCNM KMELEQANER ECEVLKKIWG SAQGMDSMLK 

YLQRKIDEF

Show »

Length:309

Mass (Da):34,561

Checksum:ⁱ6033C3171A80CB47

GO

Isoform 4 (identifier: Q9Y232-4) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MDLAKSGIKI LVPKSPVKSR TAVDGFQSES PEKLDPVEQG QEDTVAPEVA 
        60         70         80         90        100
AEKPVGALLG PGAERARMGS RPRIHPLVPQ VPGPVTAAMA TGLAVNGKGT 
       110        120        130        140        150
SPFMDALTAN GTTNIQTSVT GVTASKRKFI DDRRDQPFDK RLRFSVRQTE 
       160        170        180        190        200
SAYRYRDIVV RKQDGFTHIL LSTKSSENNS LNPEVMREVQ SALSTAAADD 
       210        220        230        240        250
SKLVLLSAVG SVFCCGLDFI YFIRRLTDDR KRESTKMAEA IRNFVNTFIQ 
       260        270        280        290        300
FKKPIIVAVN GPAIGLGASI LPLCDVVWAN EKAWFQTPYT TFGQSPDGCS 
       310        320        330        340        350
TVMFPKIMGG ASANEMLLSG RKLTAQEACG KGLVSQVFWP GTFTQEVMVR 
       360        370        380        390        400
IKELASCNPV VLEESKALVR CNMKMELEQA NERECEVLKK IWGSAQGMDS 
       410 
MLKYLQRKID EF

Show »

Length:412

Mass (Da):45,135

Checksum:ⁱ6AFC72E69A0462A3

GO

Computationally mapped potential isoform sequencesⁱ

There are 2 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

C9JQG7	C9JQG7_HUMAN	Chromodomain Y-like protein Chromodomain Y-like protein	CDYL	171	Annotation score:
A0A669KAZ7	A0A669KAZ7_HUMAN	Chromodomain Y-like protein Chromodomain Y-like protein	CDYL	18	Annotation score:

Sequence cautionⁱ

The sequence CAB43304 differs from that shown.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	205	S → N in BAF84290 (PubMed:14702039).Curated	1
Sequence conflictⁱ	291	D → N in BAG59526 (PubMed:14702039).Curated	1
Sequence conflictⁱ	443	V → L in BAF84290 (PubMed:14702039).Curated	1
Sequence conflictⁱ	558	N → S in BAG59526 (PubMed:14702039).Curated	1
Sequence conflictⁱ	584	M → T in AAI19683 (PubMed:15489334).Curated	1
Sequence conflictⁱ	591	L → M in AAI19683 (PubMed:15489334).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_032936	2	T → A1 PublicationCorresponds to variant dbSNP:rs3812179Ensembl.	1
Natural variantⁱVAR_032937	9	S → P1 PublicationCorresponds to variant dbSNP:rs3812178Ensembl.	1
Natural variantⁱVAR_032938	48	V → A1 PublicationCorresponds to variant dbSNP:rs13196069Ensembl.	1
Natural variantⁱVAR_032939	60	A → G1 PublicationCorresponds to variant dbSNP:rs28360500Ensembl.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Length
Alternative sequenceⁱVSP_026382	1 – 289	Missing in isoform 3. 1 PublicationAdd BLAST	289
Alternative sequenceⁱVSP_041025	1 – 186	Missing in isoform 4. 1 PublicationAdd BLAST	186
Alternative sequenceⁱVSP_026383	1 – 54	Missing in isoform 2. 2 PublicationsAdd BLAST	54
Alternative sequenceⁱVSP_026384	55 – 62	AQQPPALQ → MASEELYE in isoform 2. 2 Publications	8

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.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS4491.2 [Q9Y232-2] CCDS47364.1 [Q9Y232-4]
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

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
UCSC genome browser More...UCSCⁱ	uc003mwi.4, human [Q9Y232-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q9Y232-3	Chromodomain Y like		PANPA		536	UniRef100_A0A2R9BE16
CDYL isoform 1		PANTR		412
Uncharacterized protein		NOMLE		412
Isoform 4 of Chromodomain Y-like protein		HUMAN		412
+2

Protein	Similar proteins		Species	Score	Length	Source
Q9Y232	(raccoon dog) hypothetical protein		NYCPR		572	UniRef90_Q9Y232
Chromodomain Y like		MANLE		570
Chromodomain Y like		HORSE		566
Chromodomain Y like		RHIRO		563
Chromo domain-containing protein		RHIBE		563
+22
Q9Y232-2	Chromodomain Y like		SURSU		553	UniRef90_Q9Y232-2
Chromodomain Y like		RHIFE		548
Chromodomain Y like		MACNE		548
Chromodomain Y like		SAIBB		547
Chromodomain Y like		CANLF		545
+134

Protein	Similar proteins		Species	Score	Length	Source
Q9Y232	Chromodomain Y-like protein		RAT		589	UniRef50_Q9Y232
Chromodomain Y-like protein		MOUSE		593
(raccoon dog) hypothetical protein		NYCPR		572
Chromodomain Y like		MANLE		570
Chromodomain Y like		HORSE		566
+796

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.
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]

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 entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	2DNT	NMR	-	A	63-119	[»]
	2GTR	X-ray	1.90	A/B/C	338-598	[»]
SMRⁱ	Q9Y232
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	114818, 59 interactors
CORUMⁱ	Q9Y232
IntActⁱ	Q9Y232, 36 interactors
MINTⁱ	Q9Y232
STRINGⁱ	9606.ENSP00000380718

Chemistry databases

BindingDBⁱ	Q9Y232
ChEMBLⁱ	CHEMBL3879827

PTM databases

iPTMnetⁱ	Q9Y232
PhosphoSitePlusⁱ	Q9Y232

Genetic variation databases

BioMutaⁱ	CDYL
DMDMⁱ	150421527

Proteomic databases

EPDⁱ	Q9Y232
jPOSTⁱ	Q9Y232
MassIVEⁱ	Q9Y232
PaxDbⁱ	Q9Y232
PeptideAtlasⁱ	Q9Y232
PRIDEⁱ	Q9Y232
ProteomicsDBⁱ	85621 [Q9Y232-1] 85622 [Q9Y232-2] 85623 [Q9Y232-3] 85624 [Q9Y232-4]

Protocols and materials databases

ABCDⁱ	Q9Y232, 2 sequenced antibodies
Antibodypediaⁱ	24514, 260 antibodies
The DNASU plasmid repository More...DNASUⁱ	9425

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.4, human [Q9Y232-1]

Organism-specific databases

CTDⁱ	9425
DisGeNETⁱ	9425
GeneCardsⁱ	CDYL
HGNCⁱ	HGNC:1811, CDYL
HPAⁱ	ENSG00000153046, Low tissue specificity
MIMⁱ	603778, gene
neXtProtⁱ	NX_Q9Y232
OpenTargetsⁱ	ENSG00000153046
PharmGKBⁱ	PA26356
VEuPathDBⁱ	HostDB:ENSG00000153046
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0016, Eukaryota KOG1911, Eukaryota
GeneTreeⁱ	ENSGT00940000155106
HOGENOMⁱ	CLU_009834_24_0_1
InParanoidⁱ	Q9Y232
OMAⁱ	VPRSPMN
OrthoDBⁱ	1471901at2759
PhylomeDBⁱ	Q9Y232
TreeFamⁱ	TF313375

Enzyme and pathway databases

BRENDAⁱ	4.2.1.150, 2681
PathwayCommonsⁱ	Q9Y232

Miscellaneous databases

BioGRID-ORCSⁱ	9425, 44 hits in 1032 CRISPR screens
ChiTaRSⁱ	CDYL, human
EvolutionaryTraceⁱ	Q9Y232
GenomeRNAiⁱ	9425
Pharosⁱ	Q9Y232, Tchem
Protein Ontology More...PROⁱ	PR:Q9Y232
RNActⁱ	Q9Y232, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000153046, Expressed in calcaneal tendon and 239 other tissues
ExpressionAtlasⁱ	Q9Y232, baseline and differential
Genevisibleⁱ	Q9Y232, HS

Family and domain databases

Gene3Dⁱ	1.10.12.10, 1 hit
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
Pfamⁱ	View protein in Pfam PF00385, Chromo, 1 hit PF00378, ECH_1, 1 hit
SMARTⁱ	View protein in SMART SM00298, CHROMO, 1 hit
SUPFAMⁱ	SSF52096, SSF52096, 1 hit SSF54160, SSF54160, 1 hit
PROSITEⁱ	View protein in PROSITE PS00598, CHROMO_1, 1 hit PS50013, CHROMO_2, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	CDYL_HUMAN
Accessionⁱ	Q9Y232Primary (citable) accession number: Q9Y232 Secondary accession number(s): A8K6D6 Q9Y424
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	September 19, 2003
	Last sequence update:	June 26, 2007
	Last modified:	September 29, 2021
	This is version 181 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

Keywords - Technical termⁱ

3D-structure, Reference proteome

Documents

Human chromosome 6
Human chromosome 6: entries, gene names and cross-references to MIM
Human entries with genetic variants
List of human entries with genetic variants
Human variants curated from literature reports
Index of human variants curated from literature reports
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q9Y232 (CDYL_HUMAN)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the 'basket' to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Chromodomain Y-like protein

Select a section on the left to see content.

<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

Caution

<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

<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

Enzyme and pathway databases

<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

Organism-specific databases

<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

Nucleus

Other locations

Nucleus

Other locations

Keywords - Cellular componenti

<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

Organism-specific databases

Miscellaneous databases

Chemistry databases

Genetic variation databases

<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

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<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

Gene expression databases

Organism-specific databases

<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

Q9Y232

CDYL - isoform 2 [Q9Y232-2]

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

Miscellaneous databases

<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

3D structure databases

Miscellaneous databases

<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

Region

Compositional bias

Phylogenomic databases

Family and domain databases

<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

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<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

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Genetic variation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Your basket is currently empty. ⁱ

Functionⁱ

Catalytic activityⁱ

Kineticsⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ