Q03330 (GCN5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone acetyltransferase GCN5
EC=2.3.1.48

Gene names

Name:	GCN5
Synonyms:	ADA4, SWI9
Ordered Locus Names:	YGR252W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	439 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 H3K9ac, H3K14ac, H3K18ac, H3K23ac, H3K27ac and H3K36ac, with a lower preference histone H4 to form H4K8ac and H4K16ac, and contributes to H2A.Z acetylation. Acetylation of histones gives a specific tag for epigenetic transcription activation. Operates in concert with certain DNA-binding transcriptional activators such as GCN4 or HAP2/3/4. Its acetyltransferase activity seems to be dependent on the association in different multisubunit complexes. Functions as histone acetyltransferase component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and ADA. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. The ADA histone acetyltransferase complex preferentially acetylates nucleosomal histones H3 (to form H3K14ac and H3K18ac) and H2B, leading to transcription regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus. Ref.10 Ref.18 Ref.19
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone].
Subunit structure	Component of the 1.8 MDa SAGA complex, which consists of at least of TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5 distinct domains with specialized functions. Domain I (containing TRA1) probably represents the activator interaction surface. Domain II (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily an architectural role. Domain III also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-interacting module, which may be associated transiently with SAGA. SUS1 associates with the SAC3-THP1 complex. Component of the SALSA complex, which consists of at least TRA1, SPT7 (C-terminal truncated form), TAF5, ADA3, SPT20, TAF12, TAF6, HFI1, GCN5, ADA2 and SPT3. Component of the SLIK complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9. Component of the ADA/GCN5 complex, that consists of HFI1/ADA1, ADA2, ADA3, SPT20/ADA5 and GCN5 and is probably a subcomplex of SAGA. Component of the 0.8 MDa ADA complex, which at least consists of ADA2, ADA3, AHC1 and GCN5. GCN5 interacts with ADA2. Ref.7 Ref.8 Ref.9 Ref.11 Ref.14 Ref.15 Ref.17
Subcellular location	Nucleus.
Miscellaneous	Present with 1180 molecules/cell in log phase SD medium.
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	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of transcription elongation from RNA polymerase II promoter Inferred from mutant phenotype PubMed 19822662. Source: SGD regulation of transcription by chromatin organization Inferred from mutant phenotype PubMed 11867538. Source: SGD transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Ada2/Gcn5/Ada3 transcription activator complex Inferred from direct assay PubMed 7862114. Source: SGD SAGA complex Inferred from direct assay PubMed 9224714PubMed 9674426. Source: SGD SLIK (SAGA-like) complex Inferred from direct assay Ref.14. Source: SGD chromosome, centromeric region Inferred from direct assay PubMed 18039853. Source: SGD
Molecular_function	H3 histone acetyltransferase activity Inferred from direct assay PubMed 18458063. Source: SGD histone acetyl-lysine binding Inferred from direct assay PubMed 20126658. Source: SGD transcription coactivator activity Traceable author statement PubMed 15075257. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ADA2	Q02336	37	EBI-7458,EBI-2186
SLT2	Q00772	2	EBI-7458,EBI-17372

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 439

439

Histone acetyltransferase GCN5

PRO_0000211201

Regions

Domain

100 – 255

156

N-acetyltransferase

Domain

344 – 414

71

Bromo

Sites

Site

173

1

Important for catalytic activity

Experimental info

Sequence conflict

187

1

G → D in AAT93234. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

439

Helix Strand Turn

Details...

Beta strand

100 – 105

6

Helix

111 – 127

17

Helix

133 – 141

9

Beta strand

146 – 152

7

Turn

153 – 155

3

Beta strand

156 – 166

11

Helix

167 – 169

3

Beta strand

171 – 179

9

Helix

188 – 203

16

Beta strand

208 – 213

6

Helix

215 – 217

3

Helix

218 – 223

6

Beta strand

227 – 229

3

Helix

234 – 237

4

Beta strand

248 – 253

6

Helix

333 – 345

13

Helix

350 – 352

3

Turn

358 – 360

3

Helix

364 – 367

4

Helix

374 – 382

9

Helix

389 – 406

18

Helix

412 – 429

18

Helix

432 – 437

6

Sequences

	Sequence		Length	Mass (Da)
	Q03330 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 3200730DDC7EF70D	FASTA	439	51,069
	10 20 30 40 50 60 MVTKHQIEED HLDGATTDPE VKRVKLENNV EEIQPEQAET NKQEGTDKEN KGKFEKETER 70 80 90 100 110 120 IGGSEVVTDV EKGIVKFEFD GVEYTFKERP SVVEENEGKI EFRVVNNDNT KENMMVLTGL 130 140 150 160 170 180 KNIFQKQLPK MPKEYIARLV YDRSHLSMAV IRKPLTVVGG ITYRPFDKRE FAEIVFCAIS 190 200 210 220 230 240 STEQVRGYGA HLMNHLKDYV RNTSNIKYFL TYADNYAIGY FKKQGFTKEI TLDKSIWMGY 250 260 270 280 290 300 IKDYEGGTLM QCSMLPRIRY LDAGKILLLQ EAALRRKIRT ISKSHIVRPG LEQFKDLNNI 310 320 330 340 350 360 KPIDPMTIPG LKEAGWTPEM DALAQRPKRG PHDAAIQNIL TELQNHAAAW PFLQPVNKEE 370 380 390 400 410 420 VPDYYDFIKE PMDLSTMEIK LESNKYQKME DFIYDARLVF NNCRMYNGEN TSYYKYANRL 430 EKFFNNKVKE IPEYSHLID

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Two distinct yeast transcriptional activators require the function of the GCN5 protein to promote normal levels of transcription." Georgakopoulos T., Thireos G. EMBO J. 11:4145-4152(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"Analysis of a 17.9 kb region from Saccharomyces cerevisiae chromosome VII reveals the presence of eight open reading frames, including BRF1 (TFIIIB70) and GCN5 genes." Feroli F., Carignani G., Pavanello A., Guerreiro P., Azevedo D., Rodrigues-Pousada C., Melchioretto P., Panzeri L., Agostoni Carbone M.L. Yeast 13:373-377(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-170. Strain: ATCC 96604 / S288c / FY1679.
[6]	"Sequence analysis of a 10.5 kb DNA fragment from the yeast chromosome VII reveals the presence of three new open reading frames and of a tRNAThr gene." Mazzoni C., Ruzzi M., Rinaldi T., Solinas F., Montebove F., Frontali L. Yeast 13:369-372(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 170-439. Strain: ATCC 204508 / S288c.
[7]	"Functional similarity and physical association between GCN5 and ADA2: putative transcriptional adaptors." Marcus G.A., Silverman N., Berger S.L., Horiuchi J., Guarente L. EMBO J. 13:4807-4815(1994) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ADA2.
[8]	"ADA1, a novel component of the ADA/GCN5 complex, has broader effects than GCN5, ADA2, or ADA3." Horiuchi J., Silverman N., Pina B., Marcus G.A., Guarente L. Mol. Cell. Biol. 17:3220-3228(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE ADA/GCN5 COMPLEX. Strain: ATCC MYA-3516 / BWG1-7A.
[9]	"The ATM-related cofactor Tra1 is a component of the purified SAGA complex." Grant P.A., Schieltz D., Pray-Grant M.G., Yates J.R. III, Workman J.L. Mol. Cell 2:863-867(1998) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A SAGA COMPLEX WITH SPT2; SPT7; SPT8; SPT20; HFI1 ADA2; ADA3 AND TRA1.
[10]	"Expanded lysine acetylation specificity of Gcn5 in native complexes." Grant P.A., Eberharter A., John S., Cook R.G., Turner B.M., Workman J.L. J. Biol. Chem. 274:5895-5900(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN HISTONE ACETYLATION AT THE SAGA COMPLEX, FUNCTION IN HISTONE ACETYLATION AT THE ADA COMPLEX.
[11]	"The ADA complex is a distinct histone acetyltransferase complex in Saccharomyces cerevisiae." Eberharter A., Sterner D.E., Schieltz D., Hassan A., Yates J.R. III, Berger S.L., Workman J.L. Mol. Cell. Biol. 19:6621-6631(1999) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE ADA COMPLEX, MASS SPECTROMETRY.
[12]	"GCN5-related N-acetyltransferases: a structural overview." Dyda F., Klein D.C., Hickman A.B. Annu. Rev. Biophys. Biomol. Struct. 29:81-103(2000) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[13]	"Highly specific antibodies determine histone acetylation site usage in yeast heterochromatin and euchromatin." Suka N., Suka Y., Carmen A.A., Wu J., Grunstein M. Mol. Cell 8:473-479(2001) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION OF HISTONES H2B AND H3.
[14]	"The novel SLIK histone acetyltransferase complex functions in the yeast retrograde response pathway." Pray-Grant M.G., Schieltz D., McMahon S.J., Wood J.M., Kennedy E.L., Cook R.G., Workman J.L., Yates J.R. III, Grant P.A. Mol. Cell. Biol. 22:8774-8786(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE SLIK COMPLEX.
[15]	"SALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates with activated transcription." Sterner D.E., Belotserkovskaya R., Berger S.L. Proc. Natl. Acad. Sci. U.S.A. 99:11622-11627(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE SALSA COMPLEX.
[16]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[17]	"Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation." Pray-Grant M.G., Daniel J.A., Schieltz D., Yates J.R. III, Grant P.A. Nature 433:434-438(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE SLIK COMPLEX.
[18]	"Telomeric heterochromatin boundaries require NuA4-dependent acetylation of histone variant H2A.Z in Saccharomyces cerevisiae." Babiarz J.E., Halley J.E., Rine J. Genes Dev. 20:700-710(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN HTZ1 ACETYLATION.
[19]	"Acetylation of H2AZ Lys 14 is associated with genome-wide gene activity in yeast." Millar C.B., Xu F., Zhang K., Grunstein M. Genes Dev. 20:711-722(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN HTZ1 ACETYLATION.
[20]	"Identification of histone H3 lysine 36 acetylation as a highly conserved histone modification." Morris S.A., Rao B., Garcia B.A., Hake S.B., Diaz R.L., Shabanowitz J., Hunt D.F., Allis C.D., Lieb J.D., Strahl B.D. J. Biol. Chem. 282:7632-7640(2007) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION OF HISTONE H3.
[21]	"Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator." Trievel R.C., Rojas J.R., Sterner D.E., Venkataramani R.N., Wang L., Zhou J., Allis C.D., Berger S.L., Marmorstein R. Proc. Natl. Acad. Sci. U.S.A. 96:8931-8936(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 99-262.
[22]	"Molecular architecture of the S. cerevisiae SAGA complex." Wu P.Y., Ruhlmann C., Winston F., Schultz P. Mol. Cell 15:199-208(2004) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING OF THE SAGA COMPLEX.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X68628 Genomic DNA. Translation: CAA48602.1.
Z73037 Genomic DNA. Translation: CAA97281.1.
AY693215 Genomic DNA. Translation: AAT93234.1.
X99228 Genomic DNA. Translation: CAA67614.1.
BK006941 Genomic DNA. Translation: DAA08343.1.

PIR

S28051.

RefSeq

NP_011768.1. NM_001181381.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E6I	X-ray	1.87	A	324-439	[»]
1YGH	X-ray	1.90	A/B	99-262	[»]

ProteinModelPortal

Q03330.

SMR

Q03330. Positions 99-262, 329-438.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-710N.

IntAct

Q03330. 393 interactions.

MINT

MINT-403059.

STRING

4932.YGR252W.

Proteomic databases

PaxDb

Q03330.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YGR252W; YGR252W; YGR252W.

GeneID

853167.

KEGG

sce:YGR252W.

Organism-specific databases

CYGD

YGR252w.

SGD

S000003484. GCN5.

Phylogenomic databases

eggNOG

COG5076.

GeneTree

ENSGT00660000095339.

HOGENOM

HOG000192257.

KO

K06062.

OMA

SVWMGYI.

OrthoDB

EOG412QF2.

Enzyme and pathway databases

SABIO-RK

Q03330.

Gene expression databases

Genevestigator

Q03330.

GermOnline

YGR252W. Saccharomyces cerevisiae.

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

PF00583. Acetyltransf_1. 1 hit.
PF00439. Bromodomain. 1 hit.
[Graphical view]

PRINTS

PR00503. BROMODOMAIN.

SMART

SM00297. BROMO. 1 hit.
[Graphical view]

SUPFAM

SSF55729. Acyl_CoA_acyltransferase. 1 hit.
SSF47370. Bromodomain. 1 hit.

PROSITE

PS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51186. GNAT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL4669.

EvolutionaryTrace

Q03330.

NextBio

973282.

Entry information

Entry name

GCN5_YEAST

Accession

Primary (citable) accession number: Q03330
Secondary accession number(s): D6VV32, Q6B165

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	May 1, 2013
This is version 142 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program