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Q9WTK2 (CDYL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chromodomain Y-like protein

Short name=CDY-like
EC=2.3.1.48
Gene names
Name:Cdyl
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length593 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a RE1-silencing transcription factor (REST) corepressor that facilitates histone-lysine N-methyltransferase EHMT2 recruitment and H3K9 dimethylation at REST target genes for repression. Required for chromatin targeting and maximal enzymatic activity of polycomb repressive complex 2 (PRC2); acts as a positive regulator of PRC2 activity by bridging the pre-existing histone H3K27me3 and newly recruited PRC2 on neighboring nucleosomes By similarity. Has histone acetyltransferase activity. May play a role in histone hyperacetylation during spermatid maturation. Ref.4 Ref.5

Catalytic activity

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

Subunit structure

Forms multimers and multimerization is required for stable binding to chromatin. Interacts with histone H3K9me3, histone H3K27me2 and histone H3K27me3. Interacts with EZH2, EED, SUZ12, REST, EHMT1 and EHMT2. Part of a complex containing at least CDYL, REST, WIZ, SETB1, EHMT1 and EHMT2. Part of a complex containing at least CDYL, MIER1, MIER2, HDAC1 and HDAC2 By similarity. Interacts with HDAC1 and HDAC2 via its C-terminal acetyl-CoA-binding domain. Ref.5

Subcellular location

Nucleus Ref.4 Ref.5.

Tissue specificity

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

Developmental stage

Highly expressed in elongating spermatids during histone hyperacetylation. Ref.4 Ref.5

Miscellaneous

Interaction with HDAC1 or HDAC2 prevents coenzyme A binding.

Sequence similarities

Contains 1 chromo domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9WTK2-1)

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.
Isoform 2 (identifier: Q9WTK2-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 593593Chromodomain Y-like protein
PRO_0000080222

Regions

Domain56 – 11661Chromo
Region56 – 304249Interaction with EZH2 By similarity

Amino acid modifications

Modified residue1301N6,N6,N6-trimethyllysine; by EHMT2; alternate By similarity
Modified residue1301N6,N6-dimethyllysine; by EHMT2; alternate By similarity
Modified residue1301N6-methyllysine; by EHMT2; alternate By similarity

Natural variations

Alternative sequence1 – 4949Missing in isoform 2.
VSP_026385
Alternative sequence50 – 578AIQDAETQ → MASEELYE in isoform 2.
VSP_026386

Experimental info

Mutagenesis5161S → A: Abolishes CoA-binding. No effect on transcriptional repressor activity. Ref.5
Mutagenesis588 – 5892RK → AA: Abolishes CoA-binding. No effect on transcriptional repressor activity.
Sequence conflict4891M → I in BAE33739. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 470D5B97D7E52CCA

FASTA59365,211
        10         20         30         40         50         60 
MGIGNSQPNS QEAQLCTLPE KAEQPTDDNT CQQNNVVPAT VSEPDQASPA IQDAETQVES 

        70         80         90        100        110        120 
IVDKRKNKKG KTEYLVRWKG YDSEDDTWEP EQHLVNCEEY IHDFNRRHNE RQKEGSLARA 

       130        140        150        160        170        180 
SRASPSNARK QISRSTHSTL SKTNSKALVV GKDHESKSSQ LLAASQKFRK NPAPSLANRK 

       190        200        210        220        230        240 
NMDLAKSGIK ILVPKSPVKG RTSVDGFQGE SPEKLDPVDQ GAEDTVAPEV TAEKPTGALL 

       250        260        270        280        290        300 
GPGAERARMG SRPRIHPLVP QVSGPVTAAM ATGLAVNGKG TSPFMDALAA NGTVTIQTSV 

       310        320        330        340        350        360 
TGVTAGKRKF IDDRRDQPFD KRLRFSVRQT ESAYRYRDIV VRKQDGFTHI LLSTKSSENN 

       370        380        390        400        410        420 
SLNPEVMKEV QSALSTAAAD DSKLVLLSAV GSVFCCGLDF IYFIRRLTDD RKRESTKMAD 

       430        440        450        460        470        480 
AIRNFVNTFI QFKKPIIVAV NGPAIGLGAS ILPLCDVVWA NEKAWFQTPY TTFGQSPDGC 

       490        500        510        520        530        540 
STVMFPKIMG GASANEMLFS GRKLTAQEAC GKGLVSQVFW PGTFTQEVMV RIKELASCNP 

       550        560        570        580        590 
VVLEESKALV RCNMKMELEQ ANERECEVLK KIWGSAQGMD SMLKYLQRKI DEF 

« Hide

Isoform 2 [UniParc].

Checksum: B8E3B85969ED9103
Show »

FASTA54460,142

References

« Hide 'large scale' references
[1]"Retroposition of autosomal mRNA yielded testis-specific gene family on human Y chromosome."
Lahn B.T., Page D.C.
Nat. Genet. 21:429-433(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Testis.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: NOD.
Tissue: Spleen.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Testis.
[4]"Previously uncharacterized histone acetyltransferases implicated in mammalian spermatogenesis."
Lahn B.T., Tang Z.L., Zhou J., Barndt R.J., Parvinen M., Allis C.D., Page D.C.
Proc. Natl. Acad. Sci. U.S.A. 99:8707-8712(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, ALTERNATIVE SPLICING.
[5]"Cdyl: a new transcriptional co-repressor."
Caron C., Pivot-Pajot C., van Grunsven L.A., Col E., Lestrat C., Rousseaux S., Khochbin S.
EMBO Rep. 4:877-882(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INTERACTION WITH HDAC1 AND HDAC2, MUTAGENESIS OF SER-516 AND 588-ARG-LYS-589.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF081260 mRNA. Translation: AAD22736.1.
AF081261 mRNA. Translation: AAD22737.1.
AK156509 mRNA. Translation: BAE33739.1.
BC055103 mRNA. Translation: AAH55103.1.
BC062123 mRNA. Translation: AAH62123.1.
RefSeqNP_001116858.1. NM_001123386.1.
NP_034011.1. NM_009881.3.
UniGeneMm.29002.

3D structure databases

ProteinModelPortalQ9WTK2.
SMRQ9WTK2. Positions 57-114, 336-593.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9WTK2. 1 interaction.
MINTMINT-4090565.

PTM databases

PhosphoSiteQ9WTK2.

Proteomic databases

PaxDbQ9WTK2.
PRIDEQ9WTK2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000075220; ENSMUSP00000074707; ENSMUSG00000059288. [Q9WTK2-1]
ENSMUST00000163595; ENSMUSP00000131784; ENSMUSG00000059288. [Q9WTK2-2]
GeneID12593.
KEGGmmu:12593.
UCSCuc007qce.2. mouse. [Q9WTK2-1]
uc007qcg.2. mouse. [Q9WTK2-2]

Organism-specific databases

CTD9425.
MGIMGI:1339956. Cdyl.

Phylogenomic databases

eggNOGCOG1024.
GeneTreeENSGT00670000097595.
HOGENOMHOG000111507.
HOVERGENHBG006723.
InParanoidQ9WTK2.
OMAIHDFNRR.
OrthoDBEOG72RN06.
PhylomeDBQ9WTK2.
TreeFamTF313375.

Gene expression databases

ArrayExpressQ9WTK2.
BgeeQ9WTK2.
CleanExMM_CDYL.
GenevestigatorQ9WTK2.

Family and domain databases

InterProIPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
IPR001753. Crotonase_core_superfam.
[Graphical view]
PfamPF00385. Chromo. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SMARTSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMSSF54160. SSF54160. 1 hit.
PROSITEPS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio281746.
PROQ9WTK2.
SOURCESearch...

Entry information

Entry nameCDYL_MOUSE
AccessionPrimary (citable) accession number: Q9WTK2
Secondary accession number(s): Q3U0W2, Q6P6N3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot