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Q03330

- GCN5_YEAST

UniProt

Q03330 - GCN5_YEAST

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Protein
Histone acetyltransferase GCN5
Gene
GCN5, ADA4, SWI9, YGR252W
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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
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. protein binding Source: IntAct
  5. transcription coactivator activity Source: SGD

GO - Biological processi

  1. chromatin modification Source: SGD
  2. histone H3 acetylation Source: GOC
  3. histone acetylation Source: SGD
  4. positive regulation of transcription elongation from RNA polymerase II promoter Source: SGD
  5. regulation of transcription by chromatin organization 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: Chromosome VII

Organism-specific databases

CYGDiYGR252w.
SGDiS000003484. GCN5.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 439439Histone acetyltransferase GCN5
PRO_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
ADA2Q0233635EBI-7458,EBI-2186
HFI1Q1206018EBI-7458,EBI-8287
SLT2Q007722EBI-7458,EBI-17372

Protein-protein interaction databases

BioGridi33503. 549 interactions.
DIPiDIP-710N.
IntActiQ03330. 392 interactions.
MINTiMINT-403059.
STRINGi4932.YGR252W.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ03330.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini100 – 255156N-acetyltransferase
Add
BLAST
Domaini344 – 41471Bromo
Add
BLAST

Sequence similaritiesi

Contains 1 bromo domain.

Keywords - Domaini

Bromodomain

Phylogenomic databases

eggNOGiCOG5076.
GeneTreeiENSGT00740000115051.
HOGENOMiHOG000192257.
KOiK06062.
OMAiDNCRKYN.
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

MVTKHQIEED HLDGATTDPE VKRVKLENNV EEIQPEQAET NKQEGTDKEN    50
KGKFEKETER IGGSEVVTDV EKGIVKFEFD GVEYTFKERP SVVEENEGKI 100
EFRVVNNDNT KENMMVLTGL KNIFQKQLPK MPKEYIARLV YDRSHLSMAV 150
IRKPLTVVGG ITYRPFDKRE FAEIVFCAIS STEQVRGYGA HLMNHLKDYV 200
RNTSNIKYFL TYADNYAIGY FKKQGFTKEI TLDKSIWMGY IKDYEGGTLM 250
QCSMLPRIRY LDAGKILLLQ EAALRRKIRT ISKSHIVRPG LEQFKDLNNI 300
KPIDPMTIPG LKEAGWTPEM DALAQRPKRG PHDAAIQNIL TELQNHAAAW 350
PFLQPVNKEE VPDYYDFIKE PMDLSTMEIK LESNKYQKME DFIYDARLVF 400
NNCRMYNGEN TSYYKYANRL EKFFNNKVKE IPEYSHLID 439
Length:439
Mass (Da):51,069
Last modified:October 1, 1993 - v1
Checksum:i3200730DDC7EF70D
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti187 – 1871G → D in AAT93234. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi S28051.
RefSeqi NP_011768.1. NM_001181381.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1E6I X-ray 1.87 A 324-439 [» ]
1YGH X-ray 1.90 A/B 99-262 [» ]
ProteinModelPortali Q03330.
SMRi Q03330. Positions 99-262, 329-438.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33503. 549 interactions.
DIPi DIP-710N.
IntActi Q03330. 392 interactions.
MINTi MINT-403059.
STRINGi 4932.YGR252W.

Chemistry

ChEMBLi CHEMBL4669.

Proteomic databases

MaxQBi Q03330.
PaxDbi Q03330.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGR252W ; YGR252W ; YGR252W .
GeneIDi 853167.
KEGGi sce:YGR252W.

Organism-specific databases

CYGDi YGR252w.
SGDi S000003484. GCN5.

Phylogenomic databases

eggNOGi COG5076.
GeneTreei ENSGT00740000115051.
HOGENOMi HOG000192257.
KOi K06062.
OMAi DNCRKYN.
OrthoDBi EOG7XM37B.

Enzyme and pathway databases

BioCyci YEAST:G3O-30925-MONOMER.
SABIO-RK Q03330.

Miscellaneous databases

EvolutionaryTracei Q03330.
NextBioi 973282.

Gene expression databases

Genevestigatori Q03330.

Family and domain databases

Gene3Di 1.20.920.10. 1 hit.
3.40.630.30. 1 hit.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR000182. GNAT_dom.
[Graphical view ]
Pfami PF00583. Acetyltransf_1. 1 hit.
PF00439. Bromodomain. 1 hit.
[Graphical view ]
PRINTSi PR00503. BROMODOMAIN.
SMARTi SM00297. BROMO. 1 hit.
[Graphical view ]
SUPFAMi SSF47370. SSF47370. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEi PS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51186. GNAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 155 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.

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