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P39979 (HPA3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-acetyltransferase HPA3

EC=2.3.1.-
Gene names
Name:HPA3
Ordered Locus Names:YEL066W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length179 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

N-acetyltransferase whose physiological acetyl acceptor substrate is still unknown. In vitro, histone acetylation is very weak. Ref.3

Subcellular location

Cytoplasm. Nucleus Ref.4.

Post-translational modification

Autoacetylates.

Miscellaneous

Present with 1200 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the acetyltransferase family. GNAT subfamily.

Contains 1 N-acetyltransferase domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 179179N-acetyltransferase HPA3
PRO_0000074634

Regions

Domain32 – 179148N-acetyltransferase
Region116 – 12914Acetyl-CoA binding By similarity

Sites

Site1621Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
P39979 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 53A18264798045DD

FASTA17920,699
        10         20         30         40         50         60 
MKKTPDPSPP FASTKNVGMS NEEPEKMVND RIVVKAIEPK DEEAWNKLWK EYQGFQKTVM 

        70         80         90        100        110        120 
PPEVATTTFA RFIDPTVKLW GALAFDTETG DAIGFAHYLN HLTSWHVEEV VYMNDLYVTE 

       130        140        150        160        170 
RARVKGVGRK LIEFVYSRAD ELGTPAVYWV TDHYNHRAQL LYTKVAYKTD KVLYKRNGY 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Crystal structure of the histone acetyltransferase Hpa2: a tetrameric member of the Gcn5-related N-acetyltransferase superfamily."
Angus-Hill M.L., Dutnall R.N., Tafrov S.T., Sternglanz R., Ramakrishnan V.
J. Mol. Biol. 294:1311-1325(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ACETYLATION SUBSTRATE.
[4]"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].
[5]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U18795 Genomic DNA. Translation: AAB65021.1.
BK006939 Genomic DNA. Translation: DAA07588.1.
PIRS50523.
RefSeqNP_010848.1. NM_001178881.1.

3D structure databases

ProteinModelPortalP39979.
SMRP39979. Positions 30-179.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-2063N.
IntActP39979. 3 interactions.
MINTMINT-492186.
STRING4932.YEL066W.

Proteomic databases

PaxDbP39979.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYEL066W; YEL066W; YEL066W.
GeneID856642.
KEGGsce:YEL066W.

Organism-specific databases

CYGDYEL066w.
SGDS000000792. HPA3.

Phylogenomic databases

eggNOGCOG0454.
GeneTreeENSGT00390000015620.
HOGENOMHOG000078521.
OMAGLTHYLF.
OrthoDBEOG4W6S5F.

Enzyme and pathway databases

BioCycYEAST:G3O-30181-MONOMER.

Gene expression databases

GenevestigatorP39979.
GermOnlineYEL066W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMSSF55729. Acyl_CoA_acyltransferase. 1 hit.
PROSITEPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio982604.

Entry information

Entry nameHPA3_YEAST
AccessionPrimary (citable) accession number: P39979
Secondary accession number(s): D3DLI4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 29, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome V

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

SIMILARITY comments

Index of protein domains and families