Reviewed, UniProtKB/Swiss-Prot Q9UUK2 (GCN5_SCHPO)

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 (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

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 GCN5 family. 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
Gene Ontology (GO)
Biological process	chromatin remodeling Ref.1 Traceable author statement. Source: GeneDB_SPombe histone acetylation Ref.1 Inferred from direct assay. Source: GeneDB_SPombe reciprocal meiotic recombination Ref.1 Inferred from mutant phenotype. Source: GeneDB_SPombe regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	histone acetyltransferase activity Ref.1 Inferred from direct assay. Source: GeneDB_SPombe protein binding Ref.3 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
taf5	O13282	1	EBI-1152314,EBI-1152264

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)
	Q9UUK2-1 [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: 14988732] [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: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[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: 11279037] [Abstract] Cited for: INTERACTION WITH TAF72.

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.
3D structure databases
SMR	Q9UUK2. Positions 118-280, 352-448.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UUK2. 1 interaction.
STRING	Q9UUK2.
Genome annotation databases
GeneID	2542513.
GenomeReviews	Gene locus gcn5 in contig CU329670_GR.
KEGG	spo:SPAC1952.05.
NMPDR	fig|4896.1.peg.4777.
Organism-specific databases
GeneDB_Spombe	SPAC1952.05.
Phylogenomic databases
eggNOG	fuNOG05844.
HOGENOM	HBG749648.
OMA	GLKNIFQ.
OrthoDB	EOG9BP2TZ.
PhylomeDB	Q9UUK2.
Enzyme and pathway databases
BRENDA	2.3.1.48. 653.
Gene expression databases
ArrayExpress	Q9UUK2.
Family and domain databases
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR001487. Bromodomain. IPR018359. Bromodomain_CS. IPR000182. GCN5-rel_AcTrfase. [Graphical view]
Gene3D	G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit. G3DSA:1.20.920.10. Bromodomain. 1 hit.
Pfam	PF00583. Acetyltransf_1. 1 hit. PF00439. Bromodomain. 1 hit. [Graphical view]
PRINTS	PR00503. BROMODOMAIN.
SMART	SM00297. BROMO. 1 hit. [Graphical view]
PROSITE	PS00633. BROMODOMAIN_1. 1 hit. PS50014. BROMODOMAIN_2. 1 hit. PS51186. GNAT. 1 hit. [Graphical view]
ProtoNet	Search...

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:	February 9, 2010
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)