Q9UUK2 (GCN5_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone acetyltransferase gcn5
EC=2.3.1.48

Gene names

Name:	gcn5
ORF Names:	SPAC1952.05

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	454 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Bromodomain
Molecular function	Activator Acyltransferase Chromatin regulator Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chromatin remodeling Inferred from genetic interaction Ref.1. Source: PomBase negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 19056896. Source: PomBase reciprocal meiotic recombination Inferred from mutant phenotype Ref.1. Source: PomBase transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	SAGA complex Inferred from direct assay PubMed 19056896. Source: PomBase nuclear chromatin Inferred by curator. Source: PomBase
Molecular_function	H3 histone acetyltransferase activity Inferred from direct assay Ref.1. Source: PomBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 454	454	Histone acetyltransferase gcn5		PRO_0000211199
Regions
	Domain	118 – 273	156	N-acetyltransferase
	Domain	360 – 430	71	Bromo
Sites
	Site	191	1	Important for catalytic activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9UUK2 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: FF99039B00E8ECB3	FASTA	454	51,976
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
PIR	T37933.
RefSeq	NP_594807.1. NM_001020236.2.
3D structure databases
ProteinModelPortal	Q9UUK2.
SMR	Q9UUK2. Positions 118-280.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UUK2. 3 interactions.
MINT	MINT-8210502.
STRING	4896.SPAC1952.05-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC1952.05.1; SPAC1952.05.1:pep; SPAC1952.05.
GeneID	2542513.
KEGG	spo:SPAC1952.05.
Organism-specific databases
PomBase	SPAC1952.05.
Phylogenomic databases
eggNOG	COG5076.
HOGENOM	HOG000192257.
KO	K06062.
OMA	DNCRKYN.
OrthoDB	EOG7XM37B.
Family and domain databases
Gene3D	1.20.920.10. 1 hit. 3.40.630.30. 1 hit.
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR001487. Bromodomain. IPR018359. Bromodomain_CS. IPR000182. GNAT_dom. [Graphical view]
Pfam	PF13508. Acetyltransf_7. 1 hit. PF00439. Bromodomain. 1 hit. [Graphical view]
PRINTS	PR00503. BROMODOMAIN.
SMART	SM00297. BROMO. 1 hit. [Graphical view]
SUPFAM	SSF47370. SSF47370. 1 hit. SSF55729. SSF55729. 1 hit.
PROSITE	PS00633. BROMODOMAIN_1. 1 hit. PS50014. BROMODOMAIN_2. 1 hit. PS51186. GNAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20803566.

Entry information

Entry name

GCN5_SCHPO

Accession

Primary (citable) accession number: Q9UUK2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	May 1, 2000
Last modified:	December 11, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program