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Q9UUK2 (GCN5_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone acetyltransferase gcn5

EC=2.3.1.48
Gene names
Name:gcn5
ORF Names:SPAC1952.05
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length454 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acetylates histone H2B to form H2BK11ac and H2BK16ac, histone H3 to form H3K14ac, and with a lower preference histone H4 to form H4K8ac and H4K16ac. Acetylation of histones gives a specific tag for epigenetic transcription activation By similarity. Ref.1

Catalytic activity

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

Subunit structure

Interacts with taf72. Ref.3

Subcellular location

Nucleus By similarity.

Sequence similarities

Belongs to the acetyltransferase family. GCN5 subfamily.

Contains 1 bromo domain.

Contains 1 N-acetyltransferase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 454454Histone acetyltransferase gcn5
PRO_0000211199

Regions

Domain118 – 273156N-acetyltransferase
Domain360 – 43071Bromo

Sites

Site1911Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9UUK2 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: FF99039B00E8ECB3

FASTA45451,976
        10         20         30         40         50         60 
MSNSLNDQTR PPDSSVVDST SSNFPNASND SVHDKPVKQD EQSNPNVREA IANSDGQESL 

        70         80         90        100        110        120 
AVKENKDTES SSSHFVPNGV SNSKKRKLVA TDLDVDFDIS SVRVTEKPSV LEEKSGVIQF 

       130        140        150        160        170        180 
RVVSNDDTAD SMIMLTGLKN IFMKQLPKMP KEYITRLIYD RNHLSMTIVK DNLHVVGGIT 

       190        200        210        220        230        240 
YRPFEQRGFA EIVFCAIASN EQVRGYGSHL MNHLKDYVRG TTTIQHFLTY ADNYAIGYFK 

       250        260        270        280        290        300 
KQGFTKEITL DKSIWVGYIK DYEGGTLMQC TMIPKIKYLE ANLILAIQKA AVVSKINRIT 

       310        320        330        340        350        360 
RSNVVYPGLD VFKDGPAHIE PSQVPGLMEV GWCKEMEELS KKPRPKPFFA VLEMLFTEMQ 

       370        380        390        400        410        420 
NHPSSWPFMQ PVSKEDVPDY YEVIEHPMDL STMEFRLRNN QYESVEEFIR DAKYIFDNCR 

       430        440        450 
SYNDSNTTYY KNADRLEKFF QKKLRETEYS HLAD 

« Hide

References

« Hide 'large scale' references
[1]"Roles of histone acetylation and chromatin remodeling factor in a meiotic recombination hotspot."
Yamada T., Mizuno K., Hirota K., Kon N., Wahls W.P., Hartsuiker E., Murofushi H., Shibata T., Ohta K.
EMBO J. 23:1792-1803(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[3]"Two WD repeat-containing TATA-binding protein-associated factors in fission yeast that suppress defects in the anaphase-promoting complex."
Mitsuzawa H., Seino H., Yamao F., Ishihama A.
J. Biol. Chem. 276:17117-17124(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TAF72.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB162439 Genomic DNA. Translation: BAD11106.1.
CU329670 Genomic DNA. Translation: CAB52569.1.
PIRT37933.
RefSeqNP_594807.1. NM_001020236.2.

3D structure databases

ProteinModelPortalQ9UUK2.
SMRQ9UUK2. Positions 118-280.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid278971. 265 interactions.
IntActQ9UUK2. 3 interactions.
MINTMINT-8210502.
STRING4896.SPAC1952.05-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC1952.05.1; SPAC1952.05.1:pep; SPAC1952.05.
GeneID2542513.
KEGGspo:SPAC1952.05.

Organism-specific databases

PomBaseSPAC1952.05.

Phylogenomic databases

eggNOGCOG5076.
HOGENOMHOG000192257.
KOK06062.
OMADNCRKYN.
OrthoDBEOG7XM37B.
PhylomeDBQ9UUK2.

Family and domain databases

Gene3D1.20.920.10. 1 hit.
3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR000182. GNAT_dom.
[Graphical view]
PfamPF13508. Acetyltransf_7. 1 hit.
PF00439. Bromodomain. 1 hit.
[Graphical view]
PRINTSPR00503. BROMODOMAIN.
SMARTSM00297. BROMO. 1 hit.
[Graphical view]
SUPFAMSSF47370. SSF47370. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20803566.

Entry information

Entry nameGCN5_SCHPO
AccessionPrimary (citable) accession number: Q9UUK2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names