Reviewed, UniProtKB/Swiss-Prot Q9Y232 (CDYL1_HUMAN)

Names and origin

Protein names

Recommended name:
    Chromodomain Y-like protein
      Short name=CDY-like
    EC=2.3.1.48

Gene names

Name:	CDYL
Synonyms:	CDYL1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	598 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Acts as repressor of transcription By similarity. Has histone acetyltransferase activity, with a preference for histone H4.
Catalytic activity	Acetyl-CoA + histone = CoA + acetylhistone.
Subunit structure	Interacts with HDAC1 and HDAC2 via its C-terminal acetyl-CoA-binding domain By similarity.
Subcellular location	Nucleus By similarity.
Tissue specificity	Ubiquitous. Expressed at moderate levels in all tissues examined.
Miscellaneous	Interaction with HDAC1 or HDAC2 prevents Coenzyme A binding By similarity.
Sequence similarities	Contains 1 chromo domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	chromatin assembly or disassembly Inferred from electronic annotation. Source: InterPro regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW spermatogenesis Ref.1 Traceable author statement. Source: ProtInc transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chromatin Inferred from electronic annotation. Source: InterPro nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	chromatin binding Inferred from electronic annotation. Source: InterPro histone acetyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9Y232-1)

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: Q9Y232-2)

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

Isoform 3 (identifier: Q9Y232-3)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 598

598

Chromodomain Y-like protein

PRO_0000080221

Regions

Domain

61 – 121

61

Chromo

Amino acid modifications

Modified residue

88

1

Phosphoserine Ref.6 Ref.9 Ref.10

Modified residue

201

1

Phosphoserine Ref.6 Ref.10 Ref.7 Ref.8

Modified residue

216

1

Phosphoserine Ref.7

Natural variations

Alternative sequence

1 – 289

289

Missing in isoform 3.

VSP_026382

Alternative sequence

1 – 54

54

Missing in isoform 2.

VSP_026383

Alternative sequence

55 – 62

8

AQQPPALQ → MASEELYE in isoform 2.

VSP_026384

Natural variant

2

1

T → A: dbSNP rs3812179. Ref.1

VAR_032936

Natural variant

9

1

S → P: dbSNP rs3812178. Ref.1

VAR_032937

Natural variant

48

1

V → A: dbSNP rs13196069. Ref.1

VAR_032938

Natural variant

60

1

A → G: dbSNP rs28360500. Ref.1

VAR_032939

Experimental info

Sequence conflict

584

1

M → T in AAI19683. Ref.3

Sequence conflict

591

1

L → M in AAI19683. Ref.3

Secondary structure

1

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598

Helix Strand Turn

Details...

Beta strand

66 – 71

6

Beta strand

77 – 81

5

Helix

88 – 90

3

Beta strand

92 – 95

4

Turn

96 – 98

3

Helix

103 – 113

11

Beta strand

342 – 349

8

Beta strand

352 – 357

6

Beta strand

360 – 363

4

Helix

369 – 384

16

Beta strand

390 – 397

8

Helix

405 – 414

10

Helix

416 – 436

21

Beta strand

441 – 445

5

Helix

452 – 455

4

Helix

457 – 459

3

Beta strand

460 – 466

7

Beta strand

470 – 472

3

Turn

475 – 479

5

Helix

486 – 494

9

Helix

496 – 505

10

Helix

511 – 516

6

Beta strand

521 – 524

4

Helix

526 – 528

3

Helix

529 – 541

13

Helix

545 – 556

12

Turn

557 – 559

3

Helix

560 – 579

20

Turn

581 – 584

4

Helix

585 – 596

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 26, 2007. Version 2. Checksum: A34E7221130626EC	FASTA	598	66,482
	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
	Isoform 2. Checksum: D30E1CE197B67FC7	FASTA	544	60,609
	10 20 30 40 50 60 MASEELYEVE RIVDKRKNKK GKTEYLVRWK GYDSEDDTWE PEQHLVNCEE YIHDFNRRHT 70 80 90 100 110 120 EKQKESTLTR TNRTSPNNAR KQISRSTNSN FSKTSPKALV IGKDHESKNS QLFAASQKFR 130 140 150 160 170 180 KNTAPSLSSR KNMDLAKSGI KILVPKSPVK SRTAVDGFQS ESPEKLDPVE QGQEDTVAPE 190 200 210 220 230 240 VAAEKPVGAL LGPGAERARM GSRPRIHPLV PQVPGPVTAA MATGLAVNGK GTSPFMDALT 250 260 270 280 290 300 ANGTTNIQTS VTGVTASKRK FIDDRRDQPF DKRLRFSVRQ TESAYRYRDI VVRKQDGFTH 310 320 330 340 350 360 ILLSTKSSEN NSLNPEVMRE VQSALSTAAA DDSKLVLLSA VGSVFCCGLD FIYFIRRLTD 370 380 390 400 410 420 DRKRESTKMA EAIRNFVNTF IQFKKPIIVA VNGPAIGLGA SILPLCDVVW ANEKAWFQTP 430 440 450 460 470 480 YTTFGQSPDG CSTVMFPKIM GGASANEMLL SGRKLTAQEA CGKGLVSQVF WPGTFTQEVM 490 500 510 520 530 540 VRIKELASCN PVVLEESKAL VRCNMKMELE QANERECEVL KKIWGSAQGM DSMLKYLQRK IDEF
	Isoform 3. Checksum: 6033C3171A80CB47	FASTA	309	34,561
	10 20 30 40 50 60 MDALTANGTT NIQTSVTGVT ASKRKFIDDR RDQPFDKRLR FSVRQTESAY RYRDIVVRKQ 70 80 90 100 110 120 DGFTHILLST KSSENNSLNP EVMREVQSAL STAAADDSKL VLLSAVGSVF CCGLDFIYFI 130 140 150 160 170 180 RRLTDDRKRE STKMAEAIRN FVNTFIQFKK PIIVAVNGPA IGLGASILPL CDVVWANEKA 190 200 210 220 230 240 WFQTPYTTFG QSPDGCSTVM FPKIMGGASA NEMLLSGRKL TAQEACGKGL VSQVFWPGTF 250 260 270 280 290 300 TQEVMVRIKE LASCNPVVLE ESKALVRCNM KMELEQANER ECEVLKKIWG SAQGMDSMLK YLQRKIDEF

References

	« Hide 'large scale' referencesShow '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: 10192397] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ALA-2; PRO-9; ALA-48 AND GLY-60. Tissue: Testis.
[2]	"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: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: 15489334] [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.
[4]	"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: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-598. Tissue: Uterus.
[5]	"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: 12072557] [Abstract] Cited for: FUNCTION.
[6]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88 AND SER-201, MASS SPECTROMETRY. Tissue: Epithelium.
[7]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201 AND SER-216, MASS SPECTROMETRY.
[8]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, MASS SPECTROMETRY.
[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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, MASS SPECTROMETRY.
[10]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88 AND SER-201, MASS SPECTROMETRY.
[11]	"The crystal structure of human chromodomain Y-like protein." Structural genomics consortium (SGC) Submitted (MAY-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 338-598.
[12]	"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

EMBLGenBankDDBJ

AF081258 mRNA. Translation: AAD22734.1.
AF081259 mRNA. Translation: AAD22735.1.
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. Different initiation.

IPI

IPI00293963.
IPI00655922.
IPI00942198.

PIR

T08789.

RefSeq

NP_001137443.1.
NP_004815.3.

UniGene

Hs.269092

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DNT	NMR	-	A	63-120	[»]
2GTR	X-ray	1.90	A/B/C	338-598	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q9Y232.

PTM databases

PhosphoSite

Q9Y232.

Proteomic databases

PRIDE

Q9Y232.

Genome annotation databases

Ensembl

ENST00000328908; ENSP00000330512; ENSG00000153046; Homo sapiens. [Genome view]
ENST00000343762; ENSP00000340908; ENSG00000153046; Homo sapiens. [Genome view]
ENST00000397586; ENSP00000380716; ENSG00000153046; Homo sapiens. [Genome view]
ENST00000397588; ENSP00000380718; ENSG00000153046; Homo sapiens. [Genome view]
ENST00000440139; ENSP00000394740; ENSG00000153046; Homo sapiens. [Genome view]
ENST00000449732; ENSP00000394076; ENSG00000153046; Homo sapiens. [Genome view]

GeneID

9425.

UCSC

uc003mwi.1. human.
uc003mwj.1. human.

Organism-specific databases

CTD

9425.

GeneCards

GC06P004651.

H-InvDB

HIX0005550.

HGNC

HGNC:1811. CDYL.

HPA

CAB012249.

MIM

603778. gene.

PharmGKB

PA26356.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q9Y232.

HOVERGEN

Q9Y232.

OMA

ASHRSAW.

Enzyme and pathway databases

BRENDA

2.3.1.48. 247.

Gene expression databases

ArrayExpress

Q9Y232.

Bgee

Q9Y232.

CleanEx

HS_CDYL.

Genevestigator

Q9Y232.

GermOnline

ENSG00000153046. Homo sapiens.

Family and domain databases

InterPro

IPR000953. Chromodomain.
IPR001753. Crotonase_core.
[Graphical view]

Pfam

PF00385. Chromo. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]

SMART

SM00298. CHROMO. 1 hit.
[Graphical view]

PROSITE

PS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

35306.

SOURCE

Search...

Entry information

Entry name

CDYL1_HUMAN

Accession

Primary (citable) accession number: Q9Y232
Secondary accession number(s): Q0VDG7 , Q32NC5, Q5VX99, Q6P7T5, Q9BWZ2, Q9Y424

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2003
Last sequence update:	June 26, 2007
Last modified:	November 3, 2009
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.