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Q12433 (AHC1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Protein AHC1
Alternative name(s):
ADA HAT complex component 1
Gene names
Name:AHC1
Ordered Locus Names:YOR023C
ORF Names:OR26.13
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length566 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions as component of the transcription regulatory histone acetylation (HAT) complex ADA. ADA preferentially acetylates nucleosomal histones H3 (at 'Lys-14' and 'Lys-18') and H2B. AHC1 is required for the overall structural integrity of the ADA complex. Ref.3 Ref.5 Ref.6

Subunit structure

Component of the 0.8 MDa ADA complex, which at least consists of ADA2, ADA3, AHC1 and GCN5. Ref.4

Subcellular location

Cytoplasm. Nucleus Ref.7.

Miscellaneous

Present with 339 molecules/cell in log phase SD medium.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AHC2P256496EBI-33947,EBI-21993

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 566566Protein AHC1
PRO_0000227804

Amino acid modifications

Modified residue2821Phosphoserine Ref.11
Modified residue5051Phosphoserine Ref.9 Ref.10 Ref.11

Sequences

Sequence LengthMass (Da)Tools
Q12433 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: C18AFA10E4334764

FASTA56663,869
        10         20         30         40         50         60 
MMSPAQDKLQ HQHHNPNSSS SSSSKMTNVY QVTTPKSPQD LENNMDEPFK MDTATSNPDK 

        70         80         90        100        110        120 
DSENTQRLKY ECAKGEIQNV LNLHIMLNHK HVRHLRRNVQ KVNAKLALLE TLHKDTGLLN 

       130        140        150        160        170        180 
KIERTYQLKI KQHQQHSVLG GHFHDSTATE NTNASNYNLS YPVLSDYNIN CQPLSSSSNR 

       190        200        210        220        230        240 
NLSTTRIPHH HYHTRSKSNG LLLEPSALRP ANSNIIDYRL TGSKSLSEAI TKPTPVSLPH 

       250        260        270        280        290        300 
SNSDGISSPR SSSISPLDEQ PGFQILPFKP SQMHLNHRRN YSSTCLTSNS GIIGKTENNE 

       310        320        330        340        350        360 
PIFRRYDGIL VIITCSKCDR SGFTSAQGIV NHTRLKHSKL YSSQPLAVLN NQKLLPNDKQ 

       370        380        390        400        410        420 
DPEILSKFKK LNLDPNKDYL PSDIAIPKPQ SPINHSENHT RAPKTVKNTP HLEKLYQNKE 

       430        440        450        460        470        480 
DFKKLIDMVN ETPDDLNEYL KQREIQLRYQ KEQEEESSKS DDEASYVPSP SLSATATTTT 

       490        500        510        520        530        540 
TTDPPSPPVL SSSLQRKLLR KRKLSLNSST PMEDLPLRER LRANPTDKKP RKAALLTNEL 

       550        560 
EGPDPAAKSS SYYNLRSKSR LRGSHT 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"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.
[3]"Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: characterization of an Ada complex and the SAGA (Spt/Ada) complex."
Grant P.A., Duggan L., Cote J., Roberts S.M., Brownell J.E., Candau R., Ohba R., Owen-Hughes T., Allis C.D., Winston F., Berger S.L., Workman J.L.
Genes Dev. 11:1640-1650(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE ADA COMPLEX.
[4]"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.
[5]"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 OF THE ADA COMPLEX.
[6]"A Gal4-sigma 54 hybrid protein that functions as a potent activator of RNA polymerase II transcription in yeast."
Chen B.-S., Sun Z.-W., Hampsey M.
J. Biol. Chem. 276:23881-23887(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]"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].
[9]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282 AND SER-505, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z74931 Genomic DNA. Translation: CAA99213.1.
X87331 Genomic DNA. Translation: CAA60772.1.
BK006948 Genomic DNA. Translation: DAA10806.1.
PIRS54629.
RefSeqNP_014666.1. NM_001183442.1.

3D structure databases

ProteinModelPortalQ12433.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34427. 76 interactions.
DIPDIP-896N.
IntActQ12433. 7 interactions.
MINTMINT-391720.
STRING4932.YOR023C.

Proteomic databases

MaxQBQ12433.
PaxDbQ12433.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOR023C; YOR023C; YOR023C.
GeneID854188.
KEGGsce:YOR023C.

Organism-specific databases

CYGDYOR023c.
SGDS000005549. AHC1.

Phylogenomic databases

eggNOGNOG40866.
HOGENOMHOG000033862.
KOK11370.
OMAYHTRSKS.
OrthoDBEOG7VB2QG.

Enzyme and pathway databases

BioCycYEAST:G3O-33571-MONOMER.

Gene expression databases

GenevestigatorQ12433.

Family and domain databases

InterProIPR015880. Znf_C2H2-like.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio976005.

Entry information

Entry nameAHC1_YEAST
AccessionPrimary (citable) accession number: Q12433
Secondary accession number(s): D6W290
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 107 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 XV

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

Yeast

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