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Protein

Histone acetyltransferase HPA2

Gene

HPA2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

In vitro, acetylates histone H3 'Lys-4' and 'Lys-14' and histone H4 'Lys-5' and 'Lys-12'.

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei139 – 1391Important for catalytic activity

GO - Molecular functioni

  1. histone acetyltransferase activity Source: SGD
  2. identical protein binding Source: IntAct
  3. protein homodimerization activity Source: SGD

GO - Biological processi

  1. histone acetylation Source: SGD
  2. protein homotetramerization Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Chromatin regulator, Transferase

Enzyme and pathway databases

BioCyciYEAST:G3O-34315-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase HPA2 (EC:2.3.1.48)
Gene namesi
Name:HPA2
Ordered Locus Names:YPR193C
ORF Names:P9677.12
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XVI

Organism-specific databases

CYGDiYPR193c.
SGDiS000006397. HPA2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 156156Histone acetyltransferase HPA2PRO_0000074633Add
BLAST

Post-translational modificationi

Autoacetylates in an intermolecular reaction.

Expressioni

Gene expression databases

GenevestigatoriQ06592.

Interactioni

Subunit structurei

Forms homodimers in the absence, and homotetramers in the presence of acetyl-CoA.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-34205,EBI-34205

Protein-protein interaction databases

BioGridi36365. 49 interactions.
DIPiDIP-2953N.
IntActiQ06592. 4 interactions.
MINTiMINT-514906.
STRINGi4932.YPR193C.

Structurei

Secondary structure

1
156
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 135Combined sources
Helixi16 – 183Combined sources
Helixi19 – 3214Combined sources
Helixi39 – 5012Combined sources
Turni52 – 543Combined sources
Beta strandi56 – 6611Combined sources
Beta strandi69 – 7810Combined sources
Beta strandi87 – 959Combined sources
Helixi97 – 993Combined sources
Beta strandi101 – 1033Combined sources
Helixi104 – 11815Combined sources
Beta strandi124 – 1296Combined sources
Helixi133 – 14210Combined sources
Beta strandi143 – 1453Combined sources
Beta strandi147 – 1537Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QSMX-ray2.40A/B/C/D5-156[»]
1QSOX-ray2.90A/B/C/D8-156[»]
ProteinModelPortaliQ06592.
SMRiQ06592. Positions 5-156.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06592.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 156148N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni93 – 10614Acetyl-CoA bindingAdd
BLAST

Sequence similaritiesi

Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0454.
GeneTreeiENSGT00390000015620.
HOGENOMiHOG000078521.
InParanoidiQ06592.
KOiK18852.
OMAiLPLWQAY.
OrthoDBiEOG7X3R3Q.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q06592-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNTSEDNIT VRFVTENDKE GWQRLWKSYQ DFYEVSFPDD LDDFNFGRFL
60 70 80 90 100
DPNIKMWAAV AVESSSEKII GMINFFNHMT TWDFKDKIYI NDLYVDENSR
110 120 130 140 150
VKGAGGKLIQ FVYDEADKLG TPSVYWCTDE SNHRAQLLYV KVGYKAPKIL

YKRKGY
Length:156
Mass (Da):18,334
Last modified:November 1, 1996 - v1
Checksum:i707C6EA8B8ED73A7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U25841 Genomic DNA. Translation: AAB64622.1.
AY558056 Genomic DNA. Translation: AAS56382.1.
BK006949 Genomic DNA. Translation: DAA11609.1.
PIRiS58823.
RefSeqiNP_015519.1. NM_001184290.1.

Genome annotation databases

EnsemblFungiiYPR193C; YPR193C; YPR193C.
GeneIDi856323.
KEGGisce:YPR193C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U25841 Genomic DNA. Translation: AAB64622.1.
AY558056 Genomic DNA. Translation: AAS56382.1.
BK006949 Genomic DNA. Translation: DAA11609.1.
PIRiS58823.
RefSeqiNP_015519.1. NM_001184290.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QSMX-ray2.40A/B/C/D5-156[»]
1QSOX-ray2.90A/B/C/D8-156[»]
ProteinModelPortaliQ06592.
SMRiQ06592. Positions 5-156.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36365. 49 interactions.
DIPiDIP-2953N.
IntActiQ06592. 4 interactions.
MINTiMINT-514906.
STRINGi4932.YPR193C.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPR193C; YPR193C; YPR193C.
GeneIDi856323.
KEGGisce:YPR193C.

Organism-specific databases

CYGDiYPR193c.
SGDiS000006397. HPA2.

Phylogenomic databases

eggNOGiCOG0454.
GeneTreeiENSGT00390000015620.
HOGENOMiHOG000078521.
InParanoidiQ06592.
KOiK18852.
OMAiLPLWQAY.
OrthoDBiEOG7X3R3Q.

Enzyme and pathway databases

BioCyciYEAST:G3O-34315-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ06592.
NextBioi981721.

Gene expression databases

GenevestigatoriQ06592.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 7-156 WITH ACETYL-COA.

Entry informationi

Entry nameiHPA2_YEAST
AccessioniPrimary (citable) accession number: Q06592
Secondary accession number(s): D6W4J3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: November 1, 1996
Last modified: March 4, 2015
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.