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Q9Y232 (CDYL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
Synonyms:CDYL1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length598 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. Has histone acetyltransferase activity, with a preference for histone H4. Ref.6 Ref.10 Ref.16

Catalytic activity

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

Subunit structure

Forms multimers and multimerization is required for stable binding to chromatin. Interacts with HDAC1 and HDAC2 via its C-terminal acetyl-CoA-binding domain By similarity. Interacts with histone H3K9me3, histone H3K27me2 and histone H3K27me3. Interacts with EZH2, EED, SUZ12, REST, EHMT1 and EHMT2. Part of a complex containing at least CDYL, REST, WIZ, SETB1, EHMT1 and EHMT2. Part of a complex containing at least CDYL, MIER1, MIER2, HDAC1 and HDAC2. Ref.10 Ref.13 Ref.16

Subcellular location

Nucleus Ref.8 Ref.13.

Tissue specificity

Ubiquitous. Expressed at moderate levels in all tissues examined. Isoform 2 is the most abundantly expressed isoform. Ref.13

Miscellaneous

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

Sequence similarities

Contains 1 chromo domain.

Sequence caution

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HIST1H3DP684315EBI-1387386,EBI-79722

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y232-1)

Also known as: a;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9Y232-2)

Also known as: b;

The sequence of this isoform differs from the canonical sequence as follows:
     1-54: Missing.
     55-62: AQQPPALQ → MASEELYE
Isoform 3 (identifier: Q9Y232-3)

Also known as: c;

The sequence of this isoform differs from the canonical sequence as follows:
     1-289: Missing.
Isoform 4 (identifier: Q9Y232-4)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 598598Chromodomain Y-like protein
PRO_0000080221

Regions

Domain61 – 12161Chromo
Region61 – 309249Interaction with EZH2

Amino acid modifications

Modified residue881Phosphoserine Ref.12
Modified residue1351N6,N6,N6-trimethyllysine; by EHMT2; alternate Ref.11
Modified residue1351N6,N6-dimethyllysine; by EHMT2; alternate Ref.11
Modified residue1351N6-methyllysine; by EHMT2; alternate Ref.11
Modified residue2011Phosphoserine Ref.15
Modified residue2161Phosphoserine Ref.12 Ref.15 Ref.17

Natural variations

Alternative sequence1 – 289289Missing in isoform 3.
VSP_026382
Alternative sequence1 – 186186Missing in isoform 4.
VSP_041025
Alternative sequence1 – 5454Missing in isoform 2.
VSP_026383
Alternative sequence55 – 628AQQPPALQ → MASEELYE in isoform 2.
VSP_026384
Natural variant21T → A. Ref.1
Corresponds to variant rs3812179 [ dbSNP | Ensembl ].
VAR_032936
Natural variant91S → P. Ref.1
Corresponds to variant rs3812178 [ dbSNP | Ensembl ].
VAR_032937
Natural variant481V → A. Ref.1
Corresponds to variant rs13196069 [ dbSNP | Ensembl ].
VAR_032938
Natural variant601A → G. Ref.1
Corresponds to variant rs28360500 [ dbSNP | Ensembl ].
VAR_032939

Experimental info

Sequence conflict2051S → N in BAF84290. Ref.2
Sequence conflict2911D → N in BAG59526. Ref.2
Sequence conflict4431V → L in BAF84290. Ref.2
Sequence conflict5581N → S in BAG59526. Ref.2
Sequence conflict5841M → T in AAI19683. Ref.4
Sequence conflict5911L → M in AAI19683. Ref.4

Secondary structure

....................................................... 598
Helix Strand Turn

Details...

Sequences

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

Last modified June 26, 2007. Version 2.
Checksum: A34E7221130626EC

FASTA59866,482
        10         20         30         40         50         60 
MTFQASHRSA WGKSRKKNWQ YEGPTQKLFL KRNNVSAPDG PSDPSISVSS EQSGAQQPPA 

        70         80         90        100        110        120 
LQVERIVDKR KNKKGKTEYL VRWKGYDSED DTWEPEQHLV NCEEYIHDFN RRHTEKQKES 

       130        140        150        160        170        180 
TLTRTNRTSP NNARKQISRS TNSNFSKTSP KALVIGKDHE SKNSQLFAAS QKFRKNTAPS 

       190        200        210        220        230        240 
LSSRKNMDLA KSGIKILVPK SPVKSRTAVD GFQSESPEKL DPVEQGQEDT VAPEVAAEKP 

       250        260        270        280        290        300 
VGALLGPGAE RARMGSRPRI HPLVPQVPGP VTAAMATGLA VNGKGTSPFM DALTANGTTN 

       310        320        330        340        350        360 
IQTSVTGVTA SKRKFIDDRR DQPFDKRLRF SVRQTESAYR YRDIVVRKQD GFTHILLSTK 

       370        380        390        400        410        420 
SSENNSLNPE VMREVQSALS TAAADDSKLV LLSAVGSVFC CGLDFIYFIR RLTDDRKRES 

       430        440        450        460        470        480 
TKMAEAIRNF VNTFIQFKKP IIVAVNGPAI GLGASILPLC DVVWANEKAW FQTPYTTFGQ 

       490        500        510        520        530        540 
SPDGCSTVMF PKIMGGASAN EMLLSGRKLT AQEACGKGLV SQVFWPGTFT QEVMVRIKEL 

       550        560        570        580        590 
ASCNPVVLEE SKALVRCNMK MELEQANERE CEVLKKIWGS AQGMDSMLKY LQRKIDEF 

« Hide

Isoform 2 (b) [UniParc].

Checksum: D30E1CE197B67FC7
Show »

FASTA54460,609
Isoform 3 (c) [UniParc].

Checksum: 6033C3171A80CB47
Show »

FASTA30934,561
Isoform 4 [UniParc].

Checksum: 6AFC72E69A0462A3
Show »

FASTA41245,135

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), VARIANTS ALA-2; PRO-9; ALA-48 AND GLY-60.
Tissue: Testis.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
Tissue: Placenta and Tongue.
[3]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 253-598 (ISOFORM 1).
Tissue: Eye and Uterus.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-598.
Tissue: Uterus.
[6]"Previously uncharacterized histone acetyltransferases implicated in mammalian spermatogenesis."
Lahn B.T., Tang Z.L., Zhou J., Barndt R.J., Parvinen M., Allis C.D., Page D.C.
Proc. Natl. Acad. Sci. U.S.A. 99:8707-8712(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Specificity of the chromodomain Y chromosome family of chromodomains for lysine-methylated ARK(S/T) motifs."
Fischle W., Franz H., Jacobs S.A., Allis C.D., Khorasanizadeh S.
J. Biol. Chem. 283:19626-19635(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"CDYL bridges REST and histone methyltransferases for gene repression and suppression of cellular transformation."
Mulligan P., Westbrook T.F., Ottinger M., Pavlova N., Chang B., Macia E., Shi Y.J., Barretina J., Liu J., Howley P.M., Elledge S.J., Shi Y.
Mol. Cell 32:718-726(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH REST; EHMT1 AND EHMT2, IDENTIFICATION IN A COMPLEX WITH REST; WIZ; SETB1; EHMT1 AND EHMT2, IDENTIFICATION IN A COMPLEX WITH MIER1; MIER2; HDAC1 AND HDAC2.
[11]"Protein lysine methyltransferase G9a acts on non-histone targets."
Rathert P., Dhayalan A., Murakami M., Zhang X., Tamas R., Jurkowska R., Komatsu Y., Shinkai Y., Cheng X., Jeltsch A.
Nat. Chem. Biol. 4:344-346(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-135, IDENTIFICATION BY MASS SPECTROMETRY.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88 AND SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Multimerization and H3K9me3 binding are required for CDYL1b heterochromatin association."
Franz H., Mosch K., Soeroes S., Urlaub H., Fischle W.
J. Biol. Chem. 284:35049-35059(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH H3K9ME3, TISSUE SPECIFICITY.
[14]Erratum
Franz H., Mosch K., Soeroes S., Urlaub H., Fischle W.
J. Biol. Chem. 285:11754-11754(2010)
[15]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201 AND SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Corepressor protein CDYL functions as a molecular bridge between polycomb repressor complex 2 and repressive chromatin mark trimethylated histone lysine 27."
Zhang Y., Yang X., Gui B., Xie G., Zhang D., Shang Y., Liang J.
J. Biol. Chem. 286:42414-42425(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HISTONE H3K9ME3; HISTONE H3K27ME2; HISTONE H3K27ME3; EZH2; EED AND SUZ12.
[17]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Crystal structures of human CDY proteins reveal a crotonase-like fold."
Wu H., Min J., Antoshenko T., Plotnikov A.N.
Proteins 76:1054-1061(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 338-598.
[19]"Solution structure of RSGI RUH-064, a chromo domain from human cDNA."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 55-120.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF081258 mRNA. Translation: AAD22734.1.
AF081259 mRNA. Translation: AAD22735.1.
AK291601 mRNA. Translation: BAF84290.1.
AK296985 mRNA. Translation: BAG59526.1.
AL356747, AL022725, AL359643 Genomic DNA. Translation: CAC36888.2.
AL359643, AL022725, AL356747 Genomic DNA. Translation: CAH73737.1.
AL022725, AL356747, AL359643 Genomic DNA. Translation: CAI20892.1.
BC061516 mRNA. Translation: AAH61516.1.
BC108725 mRNA. Translation: AAI08726.1.
BC119682 mRNA. Translation: AAI19683.1.
AL050164 mRNA. Translation: CAB43304.1. Sequence problems.
PIRT08789.
RefSeqNP_001137442.1. NM_001143970.1.
NP_001137443.1. NM_001143971.1.
NP_004815.3. NM_004824.3.
UniGeneHs.269092.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DNTNMR-A63-120[»]
2GTRX-ray1.90A/B/C338-598[»]
ProteinModelPortalQ9Y232.
SMRQ9Y232. Positions 62-120, 341-598.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114818. 20 interactions.
IntActQ9Y232. 10 interactions.
MINTMINT-2829840.
STRING9606.ENSP00000380718.

PTM databases

PhosphoSiteQ9Y232.

Polymorphism databases

DMDM150421527.

Proteomic databases

PaxDbQ9Y232.
PRIDEQ9Y232.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000328908; ENSP00000330512; ENSG00000153046. [Q9Y232-1]
ENST00000343762; ENSP00000340908; ENSG00000153046. [Q9Y232-4]
ENST00000397588; ENSP00000380718; ENSG00000153046. [Q9Y232-2]
ENST00000449732; ENSP00000394076; ENSG00000153046. [Q9Y232-4]
GeneID9425.
KEGGhsa:9425.
UCSCuc003mwi.3. human. [Q9Y232-1]
uc003mwj.3. human. [Q9Y232-2]

Organism-specific databases

CTD9425.
GeneCardsGC06P004706.
HGNCHGNC:1811. CDYL.
HPACAB012249.
HPA035578.
MIM603778. gene.
neXtProtNX_Q9Y232.
PharmGKBPA26356.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1024.
HOVERGENHBG006723.
OMAIHDFNRR.
OrthoDBEOG72RN06.
PhylomeDBQ9Y232.
TreeFamTF313375.

Gene expression databases

ArrayExpressQ9Y232.
BgeeQ9Y232.
CleanExHS_CDYL.
GenevestigatorQ9Y232.

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

ChiTaRSCDYL. human.
EvolutionaryTraceQ9Y232.
GenomeRNAi9425.
NextBio35306.
PROQ9Y232.
SOURCESearch...

Entry information

Entry nameCDYL1_HUMAN
AccessionPrimary (citable) accession number: Q9Y232
Secondary accession number(s): A8K6D6 expand/collapse secondary AC list , B4DLG4, Q0VDG7, Q32NC5, Q5VX99, Q6P7T5, Q9BWZ2, Q9Y424
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: June 26, 2007
Last modified: April 16, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM