[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Testis; DOI=10.1038/7771; PubMed=10192397 [NCBI, ExPASy, EBI, Israel, Japan] Lahn B.T., Page D.C.; "Retroposition of autosomal mRNA yielded testis-specific gene family on human Y chromosome."; Nat. Genet. 21:429-433(1999).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[3]	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 282-541. Structural genomics consortium (SGC); "The crystal structure of catalytic domain of human testis-specific chromodomain protein Y."; Submitted (FEB-2006) to the PDB data bank.

Comments

FUNCTION: May have histone acetyltransferase activity (By similarity).
CATALYTIC ACTIVITY: Acetyl-CoA + histone = CoA + acetylhistone.
SUBCELLULAR LOCATION: Nucleus (By similarity).
TISSUE SPECIFICITY: Testis specific.
SIMILARITY: Contains 1 chromo domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF080598; AAD22733.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC069087; AAH69087.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001001722.1; -.
NP_004816.1; -.

UniGene

Hs.251375

3D structure databases

PDB

2FW2; X-ray; 2.20 A; A/B/C/D/E/F=282-541.

[ExPASy / RCSB / EBI]

2FW2; -.

Q9Y6F7; 1-64.

PTM databases

Q9Y6F7; -.

Organism-specific databases

H-InvDB

HIX0056665; -.
HIX0056697; -.

HGNC

HGNC:1810; CDY2A.
HGNC:23921; CDY2B.

GenAtlas

CDY2A.

MIM

400018; gene. [NCBI / EBI]

PharmGKB

PA26355; -.

GeneCards

Q9Y6F7.

Gene expression databases

CleanEx

HS_CDY2A; -.
HS_CDY2B; -.

GermOnline

ENSG00000129873; Homo sapiens.
ENSG00000182415; Homo sapiens.

Ontologies

GO:0000785;	Cellular component: chromatin (inferred from electronic annotation from InterPro).
GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from InterPro).
GO:0003682;	Molecular function: chromatin binding (inferred from electronic annotation from InterPro).
GO:0004402;	Molecular function: histone acetyltransferase activity (inferred from electronic annotation from EC).
GO:0006333;	Biological process: chromatin assembly or disassembly (inferred from electronic annotation from InterPro).
GO:0007283;	Biological process: spermatogenesis (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR000953; Chromodomain.
Graphical view of domain structure.

Pfam

PF00385; Chromo; 1.
Pfam graphical view of domain structure.

PRINTS

PR00504; CHROMODOMAIN.

SMART

SM00298; CHROMO; 1.
SMART graphical view of domain structure.

PROSITE

PS00598; CHROMO_1; 1.
PS50013; CHROMO_2; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q9Y6F7.

Genome annotation databases

Ensembl

ENSG00000129873; Homo sapiens. [Contig view]
ENSG00000182415; Homo sapiens. [Contig view]

GeneID

203611; -.
9426; -.

KEGG

hsa:203611; -.
hsa:9426; -.

Phylogenomic databases

HOGENOM

Q9Y6F7; -.

HOVERGEN

Q9Y6F7; -.

Other

Q9Y6F7; -.

90458; -.

CDY2A; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acyltransferase; Nucleus; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 541`	`541`	`Testis-specific chromodomain protein Y 2.`	`PRO_0000080220`
`DOMAIN`	`6 66`	`61`	`Chromo.`
`STRAND`	`286 292`	`7`
`STRAND`	`295 300`	`6`
`STRAND`	`303 306`	`4`
`HELIX`	`312 327`	`16`
`STRAND`	`331 337`	`7`
`HELIX`	`348 357`	`10`
`HELIX`	`359 379`	`21`
`STRAND`	`384 388`	`5`
`HELIX`	`395 398`	`4`
`HELIX`	`400 402`	`3`
`STRAND`	`403 409`	`7`
`STRAND`	`413 415`	`3`
`HELIX`	`418 421`	`4`
`HELIX`	`429 437`	`9`
`HELIX`	`439 446`	`8`
`STRAND`	`451 453`	`3`
`HELIX`	`454 459`	`6`
`STRAND`	`464 467`	`4`
`HELIX`	`472 483`	`12`
`HELIX`	`488 521`	`34`
`HELIX`	`524 535`	`12`

Sequence information

Length: 541 AA [This is the length of the unprocessed precursor]

Molecular weight: 60524 Da [This is the MW of the unprocessed precursor]

CRC64: 53F31A6603829E85 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASQEFEVEA IVDKRQDKNG NTQYLVRWKG YDKQDDTWEP EQHLMNCEKC VHDFNRRQTE 

        70         80         90        100        110        120 
KQKKLTWTTT SRIFSNNARR RTSRSTKANY SKNSPKTPVT DKHHRSKNCK LFAASKNVRR 

       130        140        150        160        170        180 
KAASTLSDTK NMEIINSTIE TLAPDSPFDH KKTVSGFQKL EKLDPIAADQ QDTVVFKVTE 

       190        200        210        220        230        240 
GKLLRDPLSH PGAEQTGIQN KTQMHPLMSQ MSGSVTASMA TGSATRKGIV VLIDPLAANG 

       250        260        270        280        290        300 
TTDMHTSVPR VKGGQRNITD DSRGQPFIKK MHFTIRLTES AITYRDIVVK KEDGFTQIVL 

       310        320        330        340        350        360 
STRSTEKNAL NTEVIKEMVN ALNSAAADDS KLVLFSAAGS VFCCGLDFGY FVRHLRNDRN 

       370        380        390        400        410        420 
TASLEMVDTI KNFVNTFIQF KKPIVVSVNG PAIGLGASIL PLCDLVWANE KAWFQTPYTT 

       430        440        450        460        470        480 
FGQSPDGCSS ITFPKMMGKA SANEMLIAGR KLTAREACAK GLVSQVFLTG TFTQEVMIQI 

       490        500        510        520        530        540 
KELASYNAIV LEECKALVRC NIKLELEQAN ERECEVLRKI WSSAQGIESM LKYVENKIDE 


F

Q9Y6F7 in FASTA format

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View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools