GCN5_YEAST
ID GCN5_YEAST Reviewed; 439 AA.
AC Q03330; D6VV32; Q6B165;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Histone acetyltransferase GCN5 {ECO:0000305};
DE EC=2.3.1.48 {ECO:0000269|PubMed:10026213};
DE AltName: Full=Histone crotonyltransferase GCN5 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:31699900};
GN Name=GCN5 {ECO:0000303|PubMed:1396595, ECO:0000312|SGD:S000003484};
GN Synonyms=ADA4 {ECO:0000303|PubMed:7957049},
GN SWI9 {ECO:0000312|SGD:S000003484}; OrderedLocusNames=YGR252W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1396595; DOI=10.1002/j.1460-2075.1992.tb05507.x;
RA Georgakopoulos T., Thireos G.;
RT "Two distinct yeast transcriptional activators require the function of the
RT GCN5 protein to promote normal levels of transcription.";
RL EMBO J. 11:4145-4152(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-170.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9133742;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<373::aid-yea82>3.0.co;2-v;
RA Feroli F., Carignani G., Pavanello A., Guerreiro P., Azevedo D.,
RA Rodrigues-Pousada C., Melchioretto P., Panzeri L., Agostoni Carbone M.L.;
RT "Analysis of a 17.9 kb region from Saccharomyces cerevisiae chromosome VII
RT reveals the presence of eight open reading frames, including BRF1
RT (TFIIIB70) and GCN5 genes.";
RL Yeast 13:373-377(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 170-439.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9133741;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<369::aid-yea81>3.0.co;2-v;
RA Mazzoni C., Ruzzi M., Rinaldi T., Solinas F., Montebove F., Frontali L.;
RT "Sequence analysis of a 10.5 kb DNA fragment from the yeast chromosome VII
RT reveals the presence of three new open reading frames and of a tRNAThr
RT gene.";
RL Yeast 13:369-372(1997).
RN [7]
RP INTERACTION WITH ADA2.
RX PubMed=7957049; DOI=10.1002/j.1460-2075.1994.tb06806.x;
RA Marcus G.A., Silverman N., Berger S.L., Horiuchi J., Guarente L.;
RT "Functional similarity and physical association between GCN5 and ADA2:
RT putative transcriptional adaptors.";
RL EMBO J. 13:4807-4815(1994).
RN [8]
RP IDENTIFICATION IN THE ADA/GCN5 COMPLEX.
RC STRAIN=ATCC MYA-3516 / BWG1-7A;
RX PubMed=9154821; DOI=10.1128/mcb.17.6.3220;
RA Horiuchi J., Silverman N., Pina B., Marcus G.A., Guarente L.;
RT "ADA1, a novel component of the ADA/GCN5 complex, has broader effects than
RT GCN5, ADA2, or ADA3.";
RL Mol. Cell. Biol. 17:3220-3228(1997).
RN [9]
RP IDENTIFICATION IN A SAGA COMPLEX WITH SPT2; SPT7; SPT8; SPT20; HFI1 ADA2;
RP ADA3 AND TRA1.
RX PubMed=9885573; DOI=10.1016/s1097-2765(00)80300-7;
RA Grant P.A., Schieltz D., Pray-Grant M.G., Yates J.R. III, Workman J.L.;
RT "The ATM-related cofactor Tra1 is a component of the purified SAGA
RT complex.";
RL Mol. Cell 2:863-867(1998).
RN [10]
RP FUNCTION IN HISTONE ACETYLATION AT THE SAGA COMPLEX, FUNCTION IN HISTONE
RP ACETYLATION AT THE ADA COMPLEX, AND CATALYTIC ACTIVITY.
RX PubMed=10026213; DOI=10.1074/jbc.274.9.5895;
RA Grant P.A., Eberharter A., John S., Cook R.G., Turner B.M., Workman J.L.;
RT "Expanded lysine acetylation specificity of Gcn5 in native complexes.";
RL J. Biol. Chem. 274:5895-5900(1999).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=10549298; DOI=10.1016/s1097-2765(00)80217-8;
RA Natarajan K., Jackson B.M., Zhou H., Winston F., Hinnebusch A.G.;
RT "Transcriptional activation by Gcn4p involves independent interactions with
RT the SWI/SNF complex and the SRB/mediator.";
RL Mol. Cell 4:657-664(1999).
RN [12]
RP FUNCTION, IDENTIFICATION IN THE ADA COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=10490601; DOI=10.1128/mcb.19.10.6621;
RA Eberharter A., Sterner D.E., Schieltz D., Hassan A., Yates J.R. III,
RA Berger S.L., Workman J.L.;
RT "The ADA complex is a distinct histone acetyltransferase complex in
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 19:6621-6631(1999).
RN [13]
RP REVIEW.
RX PubMed=10940244; DOI=10.1146/annurev.biophys.29.1.81;
RA Dyda F., Klein D.C., Hickman A.B.;
RT "GCN5-related N-acetyltransferases: a structural overview.";
RL Annu. Rev. Biophys. Biomol. Struct. 29:81-103(2000).
RN [14]
RP FUNCTION IN ACETYLATION OF HISTONES H2B AND H3.
RX PubMed=11545749; DOI=10.1016/s1097-2765(01)00301-x;
RA Suka N., Suka Y., Carmen A.A., Wu J., Grunstein M.;
RT "Highly specific antibodies determine histone acetylation site usage in
RT yeast heterochromatin and euchromatin.";
RL Mol. Cell 8:473-479(2001).
RN [15]
RP FUNCTION, AND IDENTIFICATION IN THE SLIK COMPLEX.
RX PubMed=12446794; DOI=10.1128/mcb.22.24.8774-8786.2002;
RA Pray-Grant M.G., Schieltz D., McMahon S.J., Wood J.M., Kennedy E.L.,
RA Cook R.G., Workman J.L., Yates J.R. III, Grant P.A.;
RT "The novel SLIK histone acetyltransferase complex functions in the yeast
RT retrograde response pathway.";
RL Mol. Cell. Biol. 22:8774-8786(2002).
RN [16]
RP FUNCTION, AND IDENTIFICATION IN THE SALSA COMPLEX.
RX PubMed=12186975; DOI=10.1073/pnas.182021199;
RA Sterner D.E., Belotserkovskaya R., Berger S.L.;
RT "SALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates
RT with activated transcription.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11622-11627(2002).
RN [17]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [18]
RP FUNCTION, AND IDENTIFICATION IN THE SLIK COMPLEX.
RX PubMed=15647753; DOI=10.1038/nature03242;
RA Pray-Grant M.G., Daniel J.A., Schieltz D., Yates J.R. III, Grant P.A.;
RT "Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-
RT dependent acetylation.";
RL Nature 433:434-438(2005).
RN [19]
RP FUNCTION IN HTZ1 ACETYLATION.
RX PubMed=16543222; DOI=10.1101/gad.1386306;
RA Babiarz J.E., Halley J.E., Rine J.;
RT "Telomeric heterochromatin boundaries require NuA4-dependent acetylation of
RT histone variant H2A.Z in Saccharomyces cerevisiae.";
RL Genes Dev. 20:700-710(2006).
RN [20]
RP FUNCTION IN HTZ1 ACETYLATION.
RX PubMed=16543223; DOI=10.1101/gad.1395506;
RA Millar C.B., Xu F., Zhang K., Grunstein M.;
RT "Acetylation of H2AZ Lys 14 is associated with genome-wide gene activity in
RT yeast.";
RL Genes Dev. 20:711-722(2006).
RN [21]
RP FUNCTION IN ACETYLATION OF HISTONE H3.
RX PubMed=17189264; DOI=10.1074/jbc.m607909200;
RA Morris S.A., Rao B., Garcia B.A., Hake S.B., Diaz R.L., Shabanowitz J.,
RA Hunt D.F., Allis C.D., Lieb J.D., Strahl B.D.;
RT "Identification of histone H3 lysine 36 acetylation as a highly conserved
RT histone modification.";
RL J. Biol. Chem. 282:7632-7640(2007).
RN [22]
RP FUNCTION.
RX PubMed=19822662; DOI=10.1128/mcb.01033-09;
RA Ginsburg D.S., Govind C.K., Hinnebusch A.G.;
RT "NuA4 lysine acetyltransferase Esa1 is targeted to coding regions and
RT stimulates transcription elongation with Gcn5.";
RL Mol. Cell. Biol. 29:6473-6487(2009).
RN [23]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31699900; DOI=10.1074/jbc.ra119.010302;
RA Kollenstart L., de Groot A.J.L., Janssen G.M.C., Cheng X., Vreeken K.,
RA Martino F., Cote J., van Veelen P.A., van Attikum H.;
RT "Gcn5 and Esa1 function as histone crotonyltransferases to regulate
RT crotonylation-dependent transcription.";
RL J. Biol. Chem. 294:20122-20134(2019).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 99-262.
RX PubMed=10430873; DOI=10.1073/pnas.96.16.8931;
RA Trievel R.C., Rojas J.R., Sterner D.E., Venkataramani R.N., Wang L.,
RA Zhou J., Allis C.D., Berger S.L., Marmorstein R.;
RT "Crystal structure and mechanism of histone acetylation of the yeast GCN5
RT transcriptional coactivator.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:8931-8936(1999).
RN [25]
RP 3D-STRUCTURE MODELING OF THE SAGA COMPLEX.
RX PubMed=15260971; DOI=10.1016/j.molcel.2004.06.005;
RA Wu P.Y., Ruhlmann C., Winston F., Schultz P.;
RT "Molecular architecture of the S. cerevisiae SAGA complex.";
RL Mol. Cell 15:199-208(2004).
CC -!- FUNCTION: Histone acetyltransferase that acetylates histone H2B to form
CC H2BK11ac and H2BK16ac, histone H3 to form H3K9ac, H3K14ac, H3K18ac,
CC H3K23ac, H3K27ac and H3K36ac, with a lower preference histone H4 to
CC form H4K8ac and H4K16ac, and contributes to H2A.Z acetylation
CC (PubMed:10026213, PubMed:11545749, PubMed:16543222, PubMed:16543223,
CC PubMed:17189264). Acetylation of histones gives a specific tag for
CC epigenetic transcription activation and elongation (PubMed:10026213,
CC PubMed:11545749, PubMed:16543222, PubMed:16543223, PubMed:17189264,
CC PubMed:19822662). Operates in concert with certain DNA-binding
CC transcriptional activators such as GCN4 or HAP2/3/4 (PubMed:10026213,
CC PubMed:11545749, PubMed:16543222, PubMed:16543223, PubMed:17189264).
CC Its acetyltransferase activity seems to be dependent on the association
CC in different multisubunit complexes (PubMed:10026213, PubMed:11545749,
CC PubMed:16543222, PubMed:16543223, PubMed:17189264). Functions as
CC histone acetyltransferase component of the transcription regulatory
CC histone acetylation (HAT) complexes SAGA, SALSA and ADA
CC (PubMed:10026213, PubMed:12186975, PubMed:9154821). SAGA is involved in
CC RNA polymerase II-dependent transcriptional regulation of approximately
CC 10% of yeast genes (PubMed:10026213). At the promoters, SAGA is
CC required for recruitment of the basal transcription machinery
CC (PubMed:10026213). It influences RNA polymerase II transcriptional
CC activity through different activities such as TBP interaction (SPT3,
CC SPT8 and SPT20) and promoter selectivity, interaction with
CC transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin
CC modification through histone acetylation (GCN5) and deubiquitination
CC (UBP8) (PubMed:10026213). SAGA acetylates nucleosomal histone H3 to
CC some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac)
CC (PubMed:10026213). SAGA interacts with DNA via upstream activating
CC sequences (UASs) (PubMed:10026213). SALSA, an altered form of SAGA, may
CC be involved in positive transcriptional regulation (PubMed:12186975).
CC The ADA histone acetyltransferase complex preferentially acetylates
CC nucleosomal histones H3 (to form H3K14ac and H3K18ac) and H2B, leading
CC to transcription regulation (PubMed:9154821). SLIK is proposed to have
CC partly overlapping functions with SAGA (PubMed:12446794,
CC PubMed:15647753). It preferentially acetylates methylated histone H3,
CC at least after activation at the GAL1-10 locus (PubMed:15647753). In
CC addition to histone acetyltransferase, can use different acyl-CoA
CC substrates, such as (2E)-butenoyl-CoA (crotonyl-CoA) and is able to
CC mediate histone crotonylation (PubMed:31699900).
CC {ECO:0000269|PubMed:10026213, ECO:0000269|PubMed:11545749,
CC ECO:0000269|PubMed:12186975, ECO:0000269|PubMed:12446794,
CC ECO:0000269|PubMed:15647753, ECO:0000269|PubMed:16543222,
CC ECO:0000269|PubMed:16543223, ECO:0000269|PubMed:17189264,
CC ECO:0000269|PubMed:19822662, ECO:0000269|PubMed:31699900,
CC ECO:0000269|PubMed:9154821}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000269|PubMed:10026213};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-butenoyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-
CC (2E)-butenoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:53908, Rhea:RHEA-
CC COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57332,
CC ChEBI:CHEBI:137954; Evidence={ECO:0000269|PubMed:31699900};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53909;
CC Evidence={ECO:0000269|PubMed:31699900};
CC -!- SUBUNIT: Component of the 1.8 MDa SAGA complex, which consists of at
CC least of TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12,
CC TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and
CC SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2
CC copies. SAGA is built of 5 distinct domains with specialized functions.
CC Domain I (containing TRA1) probably represents the activator
CC interaction surface. Domain II (containing TAF5 and TAF6, and probably
CC TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and
CC ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing
CC HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily
CC an architectural role. Domain III also harbors the HAT activity. Domain
CC V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-
CC interacting module, which may be associated transiently with SAGA. SUS1
CC associates with the SAC3-THP1 complex. Component of the SALSA complex,
CC which consists of at least TRA1, SPT7 (C-terminal truncated form),
CC TAF5, ADA3, SPT20, TAF12, TAF6, HFI1, GCN5, ADA2 and SPT3. Component of
CC the SLIK complex, which consists of at least TRA1, CHD1, SPT7, TAF5,
CC ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, SGF29,
CC TAF10 and TAF9. Component of the ADA/GCN5 complex, that consists of
CC HFI1/ADA1, ADA2, ADA3, SPT20/ADA5 and GCN5 and is probably a subcomplex
CC of SAGA. Component of the 0.8 MDa ADA complex, which at least consists
CC of ADA2, ADA3, AHC1 and GCN5. GCN5 interacts with ADA2.
CC {ECO:0000269|PubMed:10490601, ECO:0000269|PubMed:12186975,
CC ECO:0000269|PubMed:12446794, ECO:0000269|PubMed:15647753,
CC ECO:0000269|PubMed:7957049, ECO:0000269|PubMed:9154821,
CC ECO:0000269|PubMed:9885573}.
CC -!- INTERACTION:
CC Q03330; Q02336: ADA2; NbExp=41; IntAct=EBI-7458, EBI-2186;
CC Q03330; Q12060: HFI1; NbExp=21; IntAct=EBI-7458, EBI-8287;
CC Q03330; Q00772: SLT2; NbExp=2; IntAct=EBI-7458, EBI-17372;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Sensitive to amino acid starvation.
CC {ECO:0000269|PubMed:10549298}.
CC -!- MISCELLANEOUS: Present with 1180 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GCN5 subfamily.
CC {ECO:0000305}.
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DR EMBL; X68628; CAA48602.1; -; Genomic_DNA.
DR EMBL; Z73037; CAA97281.1; -; Genomic_DNA.
DR EMBL; AY693215; AAT93234.1; -; Genomic_DNA.
DR EMBL; X99228; CAA67614.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08343.1; -; Genomic_DNA.
DR PIR; S28051; S28051.
DR RefSeq; NP_011768.1; NM_001181381.1.
DR PDB; 1E6I; X-ray; 1.87 A; A=324-439.
DR PDB; 1YGH; X-ray; 1.90 A; A/B=99-262.
DR PDB; 6CW2; X-ray; 2.67 A; D=67-317.
DR PDB; 6CW3; X-ray; 1.98 A; F/H=67-317.
DR PDBsum; 1E6I; -.
DR PDBsum; 1YGH; -.
DR PDBsum; 6CW2; -.
DR PDBsum; 6CW3; -.
DR AlphaFoldDB; Q03330; -.
DR SMR; Q03330; -.
DR BioGRID; 33503; 648.
DR ComplexPortal; CPX-608; ADA complex.
DR ComplexPortal; CPX-656; SAGA complex.
DR ComplexPortal; CPX-675; SLIK (SAGA-like) complex.
DR DIP; DIP-710N; -.
DR IntAct; Q03330; 396.
DR MINT; Q03330; -.
DR STRING; 4932.YGR252W; -.
DR BindingDB; Q03330; -.
DR ChEMBL; CHEMBL4669; -.
DR CarbonylDB; Q03330; -.
DR iPTMnet; Q03330; -.
DR MaxQB; Q03330; -.
DR PaxDb; Q03330; -.
DR PRIDE; Q03330; -.
DR ABCD; Q03330; 2 sequenced antibodies.
DR DNASU; 853167; -.
DR EnsemblFungi; YGR252W_mRNA; YGR252W; YGR252W.
DR GeneID; 853167; -.
DR KEGG; sce:YGR252W; -.
DR SGD; S000003484; GCN5.
DR VEuPathDB; FungiDB:YGR252W; -.
DR eggNOG; KOG1472; Eukaryota.
DR GeneTree; ENSGT00940000168538; -.
DR HOGENOM; CLU_015741_1_1_1; -.
DR InParanoid; Q03330; -.
DR OMA; RWMGYIK; -.
DR BioCyc; YEAST:G3O-30925-MON; -.
DR Reactome; R-SCE-5689880; Ub-specific processing proteases.
DR Reactome; R-SCE-9018519; Estrogen-dependent gene expression.
DR SABIO-RK; Q03330; -.
DR EvolutionaryTrace; Q03330; -.
DR PRO; PR:Q03330; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; Q03330; protein.
DR GO; GO:0140671; C:ADA complex; IDA:SGD.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000124; C:SAGA complex; IDA:SGD.
DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IDA:SGD.
DR GO; GO:0010484; F:H3 histone acetyltransferase activity; IDA:SGD.
DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0140068; F:histone crotonyltransferase activity; IDA:SGD.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IDA:SGD.
DR GO; GO:0003712; F:transcription coregulator activity; IDA:SGD.
DR GO; GO:0006325; P:chromatin organization; IDA:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IMP:SGD.
DR GO; GO:0016573; P:histone acetylation; IDA:SGD.
DR GO; GO:0016578; P:histone deubiquitination; IC:ComplexPortal.
DR GO; GO:0043966; P:histone H3 acetylation; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR Gene3D; 1.20.920.10; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR037800; GCN5.
DR InterPro; IPR000182; GNAT_dom.
DR PANTHER; PTHR45750; PTHR45750; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Acyltransferase; Bromodomain; Chromatin regulator;
KW Nucleus; Reference proteome; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..439
FT /note="Histone acetyltransferase GCN5"
FT /id="PRO_0000211201"
FT DOMAIN 100..255
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT DOMAIN 344..414
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 173
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 177..179
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 184..190
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 216..219
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT SITE 173
FT /note="Important for catalytic activity"
FT CONFLICT 187
FT /note="G -> D (in Ref. 4; AAT93234)"
FT /evidence="ECO:0000305"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:6CW2"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:6CW2"
FT HELIX 90..96
FT /evidence="ECO:0007829|PDB:6CW2"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:1YGH"
FT HELIX 111..127
FT /evidence="ECO:0007829|PDB:1YGH"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:6CW3"
FT HELIX 133..141
FT /evidence="ECO:0007829|PDB:1YGH"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:1YGH"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:1YGH"
FT STRAND 156..166
FT /evidence="ECO:0007829|PDB:1YGH"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:1YGH"
FT STRAND 171..179
FT /evidence="ECO:0007829|PDB:1YGH"
FT HELIX 188..203
FT /evidence="ECO:0007829|PDB:1YGH"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:1YGH"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:1YGH"
FT HELIX 218..223
FT /evidence="ECO:0007829|PDB:1YGH"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:1YGH"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:1YGH"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:6CW3"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:1YGH"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:6CW3"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:6CW3"
FT HELIX 263..279
FT /evidence="ECO:0007829|PDB:6CW3"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:6CW3"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:6CW3"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:6CW2"
FT HELIX 310..313
FT /evidence="ECO:0007829|PDB:6CW3"
FT HELIX 333..345
FT /evidence="ECO:0007829|PDB:1E6I"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:1E6I"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:1E6I"
FT HELIX 364..367
FT /evidence="ECO:0007829|PDB:1E6I"
FT HELIX 374..382
FT /evidence="ECO:0007829|PDB:1E6I"
FT HELIX 389..406
FT /evidence="ECO:0007829|PDB:1E6I"
FT HELIX 412..429
FT /evidence="ECO:0007829|PDB:1E6I"
FT HELIX 432..437
FT /evidence="ECO:0007829|PDB:1E6I"
SQ SEQUENCE 439 AA; 51069 MW; 3200730DDC7EF70D CRC64;
MVTKHQIEED HLDGATTDPE VKRVKLENNV EEIQPEQAET NKQEGTDKEN KGKFEKETER
IGGSEVVTDV EKGIVKFEFD GVEYTFKERP SVVEENEGKI EFRVVNNDNT KENMMVLTGL
KNIFQKQLPK MPKEYIARLV YDRSHLSMAV IRKPLTVVGG ITYRPFDKRE FAEIVFCAIS
STEQVRGYGA HLMNHLKDYV RNTSNIKYFL TYADNYAIGY FKKQGFTKEI TLDKSIWMGY
IKDYEGGTLM QCSMLPRIRY LDAGKILLLQ EAALRRKIRT ISKSHIVRPG LEQFKDLNNI
KPIDPMTIPG LKEAGWTPEM DALAQRPKRG PHDAAIQNIL TELQNHAAAW PFLQPVNKEE
VPDYYDFIKE PMDLSTMEIK LESNKYQKME DFIYDARLVF NNCRMYNGEN TSYYKYANRL
EKFFNNKVKE IPEYSHLID
