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Q03330 (GCN5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
Synonyms:ADA4, SWI9
Ordered Locus Names:YGR252W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length439 AA.
Sequence statusComplete.
Protein existenceEvidence 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 acetyltransferase family. GCN5 subfamily.

Contains 1 bromo domain.

Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainBromodomain
   Molecular functionActivator
Acyltransferase
Chromatin regulator
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin modification

Inferred from direct assay PubMed 9674426. Source: SGD

histone H3 acetylation

Inferred from direct assay PubMed 18458063. Source: GOC

histone acetylation

Inferred from direct assay PubMed 9674426. Source: SGD

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-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentAda2/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

cytosol

Inferred from direct assay PubMed 22932476. Source: SGD

nucleus

Inferred from direct assay PubMed 22932476. Source: SGD

   Molecular_functionH3 histone acetyltransferase activity

Inferred from direct assay PubMed 18458063. Source: SGD

histone acetyltransferase activity

Inferred from direct assay PubMed 8601308. Source: SGD

lysine-acetylated histone binding

Inferred from direct assay PubMed 20126658. Source: SGD

protein binding

Inferred from physical interaction Ref.11PubMed 10688190Ref.15Ref.14PubMed 14660704PubMed 15506919PubMed 16429126PubMed 16888622PubMed 20434206PubMed 21179020PubMed 21376235PubMed 21734642PubMed 9674426. Source: IntAct

transcription coactivator activity

Traceable author statement PubMed 15075257. Source: SGD

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 439439Histone acetyltransferase GCN5
PRO_0000211201

Regions

Domain100 – 255156N-acetyltransferase
Domain344 – 41471Bromo

Sites

Site1731Important for catalytic activity

Experimental info

Sequence conflict1871G → D in AAT93234. Ref.4

Secondary structure

........................................... 439
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q03330 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 3200730DDC7EF70D

FASTA43951,069
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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, IDENTIFICATION BY 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.
PIRS28051.
RefSeqNP_011768.1. NM_001181381.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E6IX-ray1.87A324-439[»]
1YGHX-ray1.90A/B99-262[»]
ProteinModelPortalQ03330.
SMRQ03330. Positions 99-262, 329-438.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33503. 549 interactions.
DIPDIP-710N.
IntActQ03330. 392 interactions.
MINTMINT-403059.
STRING4932.YGR252W.

Chemistry

ChEMBLCHEMBL4669.

Proteomic databases

MaxQBQ03330.
PaxDbQ03330.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGR252W; YGR252W; YGR252W.
GeneID853167.
KEGGsce:YGR252W.

Organism-specific databases

CYGDYGR252w.
SGDS000003484. GCN5.

Phylogenomic databases

eggNOGCOG5076.
GeneTreeENSGT00740000115051.
HOGENOMHOG000192257.
KOK06062.
OMADNCRKYN.
OrthoDBEOG7XM37B.

Enzyme and pathway databases

BioCycYEAST:G3O-30925-MONOMER.
SABIO-RKQ03330.

Gene expression databases

GenevestigatorQ03330.

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]
PfamPF00583. Acetyltransf_1. 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

EvolutionaryTraceQ03330.
NextBio973282.

Entry information

Entry nameGCN5_YEAST
AccessionPrimary (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: July 9, 2014
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references