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Q9Y232

- CDYL1_HUMAN

UniProt

Q9Y232 - CDYL1_HUMAN

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Protein
Chromodomain Y-like protein
Gene
CDYL, CDYL1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 H4.3 Publications

Catalytic activityi

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

GO - Molecular functioni

  1. histone acetyltransferase activity Source: UniProtKB-EC
  2. methylated histone binding Source: UniProtKB
  3. protein binding Source: UniProtKB
  4. transcription corepressor activity Source: UniProtKB

GO - Biological processi

  1. regulation of transcription, DNA-templated Source: UniProtKB-KW
  2. spermatogenesis Source: ProtInc
  3. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Repressor, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Chromodomain Y-like protein (EC:2.3.1.48)
Short name:
CDY-like
Gene namesi
Name:CDYL
Synonyms:CDYL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:1811. CDYL.

Subcellular locationi

Nucleus 2 Publications

GO - Cellular componenti

  1. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26356.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 598598Chromodomain Y-like protein
PRO_0000080221Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei88 – 881Phosphoserine1 Publication
Modified residuei135 – 1351N6,N6,N6-trimethyllysine; by EHMT2; alternate1 Publication
Modified residuei135 – 1351N6,N6-dimethyllysine; by EHMT2; alternate1 Publication
Modified residuei135 – 1351N6-methyllysine; by EHMT2; alternate1 Publication
Modified residuei201 – 2011Phosphoserine1 Publication
Modified residuei216 – 2161Phosphoserine3 Publications

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Y232.
PaxDbiQ9Y232.
PRIDEiQ9Y232.

PTM databases

PhosphoSiteiQ9Y232.

Expressioni

Tissue specificityi

Ubiquitous. Expressed at moderate levels in all tissues examined. Isoform 2 is the most abundantly expressed isoform.1 Publication

Gene expression databases

ArrayExpressiQ9Y232.
BgeeiQ9Y232.
CleanExiHS_CDYL.
GenevestigatoriQ9Y232.

Organism-specific databases

HPAiCAB012249.
HPA035578.

Interactioni

Subunit structurei

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 HDAC2.3 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi114818. 20 interactions.
IntActiQ9Y232. 10 interactions.
MINTiMINT-2829840.
STRINGi9606.ENSP00000380718.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi66 – 716
Beta strandi77 – 815
Helixi88 – 903
Beta strandi92 – 954
Turni96 – 983
Helixi103 – 11311
Beta strandi342 – 3498
Beta strandi352 – 3576
Beta strandi360 – 3634
Helixi369 – 38416
Beta strandi390 – 3978
Helixi405 – 41410
Helixi416 – 43621
Beta strandi441 – 4455
Helixi452 – 4554
Helixi457 – 4593
Beta strandi460 – 4667
Beta strandi470 – 4723
Turni475 – 4795
Helixi486 – 4949
Helixi496 – 50510
Helixi511 – 5166
Beta strandi521 – 5244
Helixi526 – 5283
Helixi529 – 54113
Helixi545 – 55612
Turni557 – 5593
Helixi560 – 57920
Turni581 – 5844
Helixi585 – 59612

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DNTNMR-A63-119[»]
2GTRX-ray1.90A/B/C338-598[»]
ProteinModelPortaliQ9Y232.
SMRiQ9Y232. Positions 62-120, 341-598.

Miscellaneous databases

EvolutionaryTraceiQ9Y232.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 12161Chromo
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni61 – 309249Interaction with EZH2
Add
BLAST

Sequence similaritiesi

Contains 1 chromo domain.

Phylogenomic databases

eggNOGiCOG1024.
HOVERGENiHBG006723.
OMAiIHDFNRR.
OrthoDBiEOG72RN06.
PhylomeDBiQ9Y232.
TreeFamiTF313375.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
InterProiIPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
[Graphical view]
PfamiPF00385. Chromo. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 1 hit.
SSF54160. SSF54160. 1 hit.
PROSITEiPS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y232-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MTFQASHRSA WGKSRKKNWQ YEGPTQKLFL KRNNVSAPDG PSDPSISVSS    50
EQSGAQQPPA LQVERIVDKR KNKKGKTEYL VRWKGYDSED DTWEPEQHLV 100
NCEEYIHDFN RRHTEKQKES TLTRTNRTSP NNARKQISRS TNSNFSKTSP 150
KALVIGKDHE SKNSQLFAAS QKFRKNTAPS LSSRKNMDLA KSGIKILVPK 200
SPVKSRTAVD GFQSESPEKL DPVEQGQEDT VAPEVAAEKP VGALLGPGAE 250
RARMGSRPRI HPLVPQVPGP VTAAMATGLA VNGKGTSPFM DALTANGTTN 300
IQTSVTGVTA SKRKFIDDRR DQPFDKRLRF SVRQTESAYR YRDIVVRKQD 350
GFTHILLSTK SSENNSLNPE VMREVQSALS TAAADDSKLV LLSAVGSVFC 400
CGLDFIYFIR RLTDDRKRES TKMAEAIRNF VNTFIQFKKP IIVAVNGPAI 450
GLGASILPLC DVVWANEKAW FQTPYTTFGQ SPDGCSTVMF PKIMGGASAN 500
EMLLSGRKLT AQEACGKGLV SQVFWPGTFT QEVMVRIKEL ASCNPVVLEE 550
SKALVRCNMK MELEQANERE CEVLKKIWGS AQGMDSMLKY LQRKIDEF 598
Length:598
Mass (Da):66,482
Last modified:June 26, 2007 - v2
Checksum:iA34E7221130626EC
GO
Isoform 2 (identifier: Q9Y232-2) [UniParc]FASTAAdd to Basket

Also known as: b

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

Show »
Length:544
Mass (Da):60,609
Checksum:iD30E1CE197B67FC7
GO
Isoform 3 (identifier: Q9Y232-3) [UniParc]FASTAAdd to Basket

Also known as: c

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

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21T → A.1 Publication
Corresponds to variant rs3812179 [ dbSNP | Ensembl ].
VAR_032936
Natural varianti9 – 91S → P.1 Publication
Corresponds to variant rs3812178 [ dbSNP | Ensembl ].
VAR_032937
Natural varianti48 – 481V → A.1 Publication
Corresponds to variant rs13196069 [ dbSNP | Ensembl ].
VAR_032938
Natural varianti60 – 601A → G.1 Publication
Corresponds to variant rs28360500 [ dbSNP | Ensembl ].
VAR_032939

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 289289Missing in isoform 3.
VSP_026382Add
BLAST
Alternative sequencei1 – 186186Missing in isoform 4.
VSP_041025Add
BLAST
Alternative sequencei1 – 5454Missing in isoform 2.
VSP_026383Add
BLAST
Alternative sequencei55 – 628AQQPPALQ → MASEELYE in isoform 2.
VSP_026384

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti205 – 2051S → N in BAF84290. 1 Publication
Sequence conflicti291 – 2911D → N in BAG59526. 1 Publication
Sequence conflicti443 – 4431V → L in BAF84290. 1 Publication
Sequence conflicti558 – 5581N → S in BAG59526. 1 Publication
Sequence conflicti584 – 5841M → T in AAI19683. 1 Publication
Sequence conflicti591 – 5911L → M in AAI19683. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
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]
UniGeneiHs.269092.

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.3. human. [Q9Y232-1]
uc003mwj.3. human. [Q9Y232-2]

Polymorphism databases

DMDMi150421527.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
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 ]
UniGenei Hs.269092.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DNT NMR - A 63-119 [» ]
2GTR X-ray 1.90 A/B/C 338-598 [» ]
ProteinModelPortali Q9Y232.
SMRi Q9Y232. Positions 62-120, 341-598.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114818. 20 interactions.
IntActi Q9Y232. 10 interactions.
MINTi MINT-2829840.
STRINGi 9606.ENSP00000380718.

PTM databases

PhosphoSitei Q9Y232.

Polymorphism databases

DMDMi 150421527.

Proteomic databases

MaxQBi Q9Y232.
PaxDbi Q9Y232.
PRIDEi Q9Y232.

Protocols and materials databases

Structural Biology Knowledgebase Search...

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.3. human. [Q9Y232-1 ]
uc003mwj.3. human. [Q9Y232-2 ]

Organism-specific databases

CTDi 9425.
GeneCardsi GC06P004706.
HGNCi HGNC:1811. CDYL.
HPAi CAB012249.
HPA035578.
MIMi 603778. gene.
neXtProti NX_Q9Y232.
PharmGKBi PA26356.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1024.
HOVERGENi HBG006723.
OMAi IHDFNRR.
OrthoDBi EOG72RN06.
PhylomeDBi Q9Y232.
TreeFami TF313375.

Miscellaneous databases

ChiTaRSi CDYL. human.
EvolutionaryTracei Q9Y232.
GenomeRNAii 9425.
NextBioi 35306.
PROi Q9Y232.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y232.
Bgeei Q9Y232.
CleanExi HS_CDYL.
Genevestigatori Q9Y232.

Family and domain databases

Gene3Di 3.90.226.10. 1 hit.
InterProi IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
[Graphical view ]
Pfami PF00385. Chromo. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view ]
SMARTi SM00298. CHROMO. 1 hit.
[Graphical view ]
SUPFAMi SSF52096. SSF52096. 1 hit.
SSF54160. SSF54160. 1 hit.
PROSITEi PS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. Cited for: METHYLATION AT LYS-135, IDENTIFICATION BY MASS SPECTROMETRY.
  12. 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.

Entry informationi

Entry nameiCDYL1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y232
Secondary accession number(s): A8K6D6
, B4DLG4, Q0VDG7, Q32NC5, Q5VX99, Q6P7T5, Q9BWZ2, Q9Y424
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: June 26, 2007
Last modified: July 9, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
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.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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