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Protein

Histone acetyltransferase GCN5

Gene

GCN5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei173 – 1731Proton donor/acceptorBy similarity
Sitei173 – 1731Important for catalytic activity

GO - Molecular functioni

  1. H3 histone acetyltransferase activity Source: SGD
  2. histone acetyltransferase activity Source: SGD
  3. lysine-acetylated histone binding Source: SGD
  4. transcription coactivator activity Source: SGD

GO - Biological processi

  1. chromatin modification Source: SGD
  2. chromatin remodeling Source: SGD
  3. histone acetylation Source: SGD
  4. histone H3 acetylation Source: GOC
  5. positive regulation of transcription elongation from RNA polymerase II promoter Source: SGD
  6. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Acyltransferase, Chromatin regulator, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase GCN5 (EC:2.3.1.48)
Gene namesi
Name:GCN5
Synonyms:ADA4, SWI9
Ordered Locus Names:YGR252W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VII

Organism-specific databases

CYGDiYGR252w.
EuPathDBiFungiDB:YGR252W.
SGDiS000003484. GCN5.

Subcellular locationi

GO - Cellular componenti

  1. Ada2/Gcn5/Ada3 transcription activator complex Source: SGD
  2. chromosome, centromeric region Source: SGD
  3. cytosol Source: SGD
  4. nucleus Source: SGD
  5. SAGA complex Source: SGD
  6. SLIK (SAGA-like) complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 439439Histone acetyltransferase GCN5PRO_0000211201Add
BLAST

Proteomic databases

MaxQBiQ03330.
PaxDbiQ03330.

Expressioni

Gene expression databases

GenevestigatoriQ03330.

Interactioni

Subunit structurei

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 ADA2.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ADA2Q0233637EBI-7458,EBI-2186
HFI1Q1206020EBI-7458,EBI-8287
SLT2Q007722EBI-7458,EBI-17372

Protein-protein interaction databases

BioGridi33503. 552 interactions.
DIPiDIP-710N.
IntActiQ03330. 392 interactions.
MINTiMINT-403059.
STRINGi4932.YGR252W.

Structurei

Secondary structure

1
439
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi100 – 1056Combined sources
Helixi111 – 12717Combined sources
Helixi133 – 1419Combined sources
Beta strandi146 – 1527Combined sources
Turni153 – 1553Combined sources
Beta strandi156 – 16611Combined sources
Helixi167 – 1693Combined sources
Beta strandi171 – 1799Combined sources
Helixi188 – 20316Combined sources
Beta strandi208 – 2136Combined sources
Helixi215 – 2173Combined sources
Helixi218 – 2236Combined sources
Beta strandi227 – 2293Combined sources
Helixi234 – 2374Combined sources
Beta strandi248 – 2536Combined sources
Helixi333 – 34513Combined sources
Helixi350 – 3523Combined sources
Turni358 – 3603Combined sources
Helixi364 – 3674Combined sources
Helixi374 – 3829Combined sources
Helixi389 – 40618Combined sources
Helixi412 – 42918Combined sources
Helixi432 – 4376Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E6IX-ray1.87A324-439[»]
1YGHX-ray1.90A/B99-262[»]
ProteinModelPortaliQ03330.
SMRiQ03330. Positions 99-262, 329-438.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ03330.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini100 – 255156N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST
Domaini344 – 41471BromoPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni177 – 1793Acetyl-CoA bindingBy similarity
Regioni184 – 1907Acetyl-CoA bindingBy similarity
Regioni216 – 2194Acetyl-CoA bindingBy similarity

Sequence similaritiesi

Contains 1 bromo domain.PROSITE-ProRule annotation
Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Keywords - Domaini

Bromodomain

Phylogenomic databases

eggNOGiCOG5076.
GeneTreeiENSGT00760000119099.
HOGENOMiHOG000192257.
InParanoidiQ03330.
KOiK06062.
OMAiLLKQKEC.
OrthoDBiEOG7XM37B.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
PF00439. Bromodomain. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03330-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTKHQIEED HLDGATTDPE VKRVKLENNV EEIQPEQAET NKQEGTDKEN
60 70 80 90 100
KGKFEKETER IGGSEVVTDV EKGIVKFEFD GVEYTFKERP SVVEENEGKI
110 120 130 140 150
EFRVVNNDNT KENMMVLTGL KNIFQKQLPK MPKEYIARLV YDRSHLSMAV
160 170 180 190 200
IRKPLTVVGG ITYRPFDKRE FAEIVFCAIS STEQVRGYGA HLMNHLKDYV
210 220 230 240 250
RNTSNIKYFL TYADNYAIGY FKKQGFTKEI TLDKSIWMGY IKDYEGGTLM
260 270 280 290 300
QCSMLPRIRY LDAGKILLLQ EAALRRKIRT ISKSHIVRPG LEQFKDLNNI
310 320 330 340 350
KPIDPMTIPG LKEAGWTPEM DALAQRPKRG PHDAAIQNIL TELQNHAAAW
360 370 380 390 400
PFLQPVNKEE VPDYYDFIKE PMDLSTMEIK LESNKYQKME DFIYDARLVF
410 420 430
NNCRMYNGEN TSYYKYANRL EKFFNNKVKE IPEYSHLID
Length:439
Mass (Da):51,069
Last modified:October 1, 1993 - v1
Checksum:i3200730DDC7EF70D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti187 – 1871G → D in AAT93234 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS28051.
RefSeqiNP_011768.1. NM_001181381.1.

Genome annotation databases

EnsemblFungiiYGR252W; YGR252W; YGR252W.
GeneIDi853167.
KEGGisce:YGR252W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS28051.
RefSeqiNP_011768.1. NM_001181381.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E6IX-ray1.87A324-439[»]
1YGHX-ray1.90A/B99-262[»]
ProteinModelPortaliQ03330.
SMRiQ03330. Positions 99-262, 329-438.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33503. 552 interactions.
DIPiDIP-710N.
IntActiQ03330. 392 interactions.
MINTiMINT-403059.
STRINGi4932.YGR252W.

Chemistry

ChEMBLiCHEMBL4669.

Proteomic databases

MaxQBiQ03330.
PaxDbiQ03330.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR252W; YGR252W; YGR252W.
GeneIDi853167.
KEGGisce:YGR252W.

Organism-specific databases

CYGDiYGR252w.
EuPathDBiFungiDB:YGR252W.
SGDiS000003484. GCN5.

Phylogenomic databases

eggNOGiCOG5076.
GeneTreeiENSGT00760000119099.
HOGENOMiHOG000192257.
InParanoidiQ03330.
KOiK06062.
OMAiLLKQKEC.
OrthoDBiEOG7XM37B.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiQ03330.
NextBioi973282.
PROiQ03330.

Gene expression databases

GenevestigatoriQ03330.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
PF00439. Bromodomain. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. 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. 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.

Entry informationi

Entry nameiGCN5_YEAST
AccessioniPrimary (citable) accession number: Q03330
Secondary accession number(s): D6VV32, Q6B165
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: April 29, 2015
This is version 162 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1180 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.