AHC1_YEAST
ID AHC1_YEAST Reviewed; 566 AA.
AC Q12433; D6W290;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Protein AHC1;
DE AltName: Full=ADA HAT complex component 1;
GN Name=AHC1; OrderedLocusNames=YOR023C; ORFNames=OR26.13;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [2]
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 [3]
RP FUNCTION OF THE ADA COMPLEX.
RX PubMed=9224714; DOI=10.1101/gad.11.13.1640;
RA Grant P.A., Duggan L., Cote J., Roberts S.M., Brownell J.E., Candau R.,
RA Ohba R., Owen-Hughes T., Allis C.D., Winston F., Berger S.L., Workman J.L.;
RT "Yeast Gcn5 functions in two multisubunit complexes to acetylate
RT nucleosomal histones: characterization of an Ada complex and the SAGA
RT (Spt/Ada) complex.";
RL Genes Dev. 11:1640-1650(1997).
RN [4]
RP IDENTIFICATION IN THE ADA COMPLEX, AND IDENTIFICATION BY MASS 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 [5]
RP FUNCTION OF THE ADA COMPLEX.
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 [6]
RP FUNCTION.
RX PubMed=11313364; DOI=10.1074/jbc.m102893200;
RA Chen B.-S., Sun Z.-W., Hampsey M.;
RT "A Gal4-sigma 54 hybrid protein that functions as a potent activator of RNA
RT polymerase II transcription in yeast.";
RL J. Biol. Chem. 276:23881-23887(2001).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282 AND SER-505, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Functions as component of the transcription regulatory
CC histone acetylation (HAT) complex ADA. ADA preferentially acetylates
CC nucleosomal histones H3 (at 'Lys-14' and 'Lys-18') and H2B. AHC1 is
CC required for the overall structural integrity of the ADA complex.
CC {ECO:0000269|PubMed:10026213, ECO:0000269|PubMed:11313364,
CC ECO:0000269|PubMed:9224714}.
CC -!- SUBUNIT: Component of the 0.8 MDa ADA complex, which at least consists
CC of ADA2, ADA3, AHC1 and GCN5. {ECO:0000269|PubMed:10490601}.
CC -!- INTERACTION:
CC Q12433; P25649: AHC2; NbExp=5; IntAct=EBI-33947, EBI-21993;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 339 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z74931; CAA99213.1; -; Genomic_DNA.
DR EMBL; X87331; CAA60772.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10806.1; -; Genomic_DNA.
DR PIR; S54629; S54629.
DR RefSeq; NP_014666.1; NM_001183442.1.
DR AlphaFoldDB; Q12433; -.
DR SMR; Q12433; -.
DR BioGRID; 34427; 227.
DR ComplexPortal; CPX-608; ADA complex.
DR DIP; DIP-896N; -.
DR IntAct; Q12433; 8.
DR MINT; Q12433; -.
DR STRING; 4932.YOR023C; -.
DR iPTMnet; Q12433; -.
DR MaxQB; Q12433; -.
DR PaxDb; Q12433; -.
DR PRIDE; Q12433; -.
DR DNASU; 854188; -.
DR EnsemblFungi; YOR023C_mRNA; YOR023C; YOR023C.
DR GeneID; 854188; -.
DR KEGG; sce:YOR023C; -.
DR SGD; S000005549; AHC1.
DR VEuPathDB; FungiDB:YOR023C; -.
DR eggNOG; ENOG502QWTP; Eukaryota.
DR HOGENOM; CLU_036203_0_0_1; -.
DR InParanoid; Q12433; -.
DR OMA; QHHRRNY; -.
DR BioCyc; YEAST:G3O-33571-MON; -.
DR PRO; PR:Q12433; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12433; protein.
DR GO; GO:0140671; C:ADA complex; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0016573; P:histone acetylation; IDA:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IMP:SGD.
DR InterPro; IPR037807; AHC1.
DR PANTHER; PTHR13585:SF20; PTHR13585:SF20; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..566
FT /note="Protein AHC1"
FT /id="PRO_0000227804"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ SEQUENCE 566 AA; 63869 MW; C18AFA10E4334764 CRC64;
MMSPAQDKLQ HQHHNPNSSS SSSSKMTNVY QVTTPKSPQD LENNMDEPFK MDTATSNPDK
DSENTQRLKY ECAKGEIQNV LNLHIMLNHK HVRHLRRNVQ KVNAKLALLE TLHKDTGLLN
KIERTYQLKI KQHQQHSVLG GHFHDSTATE NTNASNYNLS YPVLSDYNIN CQPLSSSSNR
NLSTTRIPHH HYHTRSKSNG LLLEPSALRP ANSNIIDYRL TGSKSLSEAI TKPTPVSLPH
SNSDGISSPR SSSISPLDEQ PGFQILPFKP SQMHLNHRRN YSSTCLTSNS GIIGKTENNE
PIFRRYDGIL VIITCSKCDR SGFTSAQGIV NHTRLKHSKL YSSQPLAVLN NQKLLPNDKQ
DPEILSKFKK LNLDPNKDYL PSDIAIPKPQ SPINHSENHT RAPKTVKNTP HLEKLYQNKE
DFKKLIDMVN ETPDDLNEYL KQREIQLRYQ KEQEEESSKS DDEASYVPSP SLSATATTTT
TTDPPSPPVL SSSLQRKLLR KRKLSLNSST PMEDLPLRER LRANPTDKKP RKAALLTNEL
EGPDPAAKSS SYYNLRSKSR LRGSHT
