Q06592 (HPA2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone acetyltransferase HPA2
EC=2.3.1.48

Gene names

Name:	HPA2
Ordered Locus Names:	YPR193C
ORF Names:	P9677.12

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	156 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	In vitro, acetylates histone H3 'Lys-4' and 'Lys-14' and histone H4 'Lys-5' and 'Lys-12'.
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone].
Subunit structure	Forms homodimers in the absence, and homotetramers in the presence of acetyl-CoA.
Post-translational modification	Autoacetylates in an intermolecular reaction.
Sequence similarities	Belongs to the acetyltransferase family. GNAT subfamily. Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
Molecular function	Acyltransferase Chromatin regulator Transferase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein homotetramerization Inferred from direct assay Ref.4. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay PubMed 11914276. Source: SGD
Molecular_function	histone acetyltransferase activity Inferred from sequence or structural similarity Ref.4. Source: SGD protein homodimerization activity Inferred from direct assay Ref.4. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-34205,EBI-34205

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 156

156

Histone acetyltransferase HPA2

PRO_0000074633

Regions

Domain

9 – 156

148

N-acetyltransferase

Region

93 – 106

14

Acetyl-CoA binding

Sites

Site

139

1

Important for catalytic activity

Secondary structure

1

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156

Helix Strand Turn

Details...

Beta strand

9 – 13

5

Helix

16 – 18

3

Helix

19 – 32

14

Helix

39 – 50

12

Turn

52 – 54

3

Beta strand

56 – 66

11

Beta strand

69 – 78

10

Beta strand

87 – 95

9

Helix

97 – 99

3

Beta strand

101 – 103

3

Helix

104 – 118

15

Beta strand

124 – 129

6

Helix

133 – 142

10

Beta strand

143 – 145

3

Beta strand

147 – 153

7

Sequences

	Sequence		Length	Mass (Da)
	Q06592 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 707C6EA8B8ED73A7	FASTA	156	18,334
	10 20 30 40 50 60 MSNTSEDNIT VRFVTENDKE GWQRLWKSYQ DFYEVSFPDD LDDFNFGRFL DPNIKMWAAV 70 80 90 100 110 120 AVESSSEKII GMINFFNHMT TWDFKDKIYI NDLYVDENSR VKGAGGKLIQ FVYDEADKLG 130 140 150 TPSVYWCTDE SNHRAQLLYV KVGYKAPKIL YKRKGY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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(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]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] 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(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 7-156 WITH ACETYL-COA.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U25841 Genomic DNA. Translation: AAB64622.1.
AY558056 Genomic DNA. Translation: AAS56382.1.
BK006949 Genomic DNA. Translation: DAA11609.1.

PIR

S58823.

RefSeq

NP_015519.1. NM_001184290.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QSM	X-ray	2.40	A/B/C/D	5-156	[»]
1QSO	X-ray	2.90	A/B/C/D	8-156	[»]

ProteinModelPortal

Q06592.

SMR

Q06592. Positions 5-156.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2953N.

IntAct

Q06592. 4 interactions.

MINT

MINT-514906.

STRING

4932.YPR193C.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YPR193C; YPR193C; YPR193C.

GeneID

856323.

KEGG

sce:YPR193C.

Organism-specific databases

CYGD

YPR193c.

SGD

S000006397. HPA2.

Phylogenomic databases

eggNOG

COG0454.

GeneTree

ENSGT00390000015620.

HOGENOM

HOG000078521.

OMA

ETNHTAQ.

OrthoDB

EOG4W6S5F.

Gene expression databases

Genevestigator

Q06592.

GermOnline

YPR193C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.40.630.30. 1 hit.

InterPro

IPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]

Pfam

PF00583. Acetyltransf_1. 1 hit.
[Graphical view]

SUPFAM

SSF55729. Acyl_CoA_acyltransferase. 1 hit.

PROSITE

PS51186. GNAT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q06592.

NextBio

981721.

Entry information

Entry name

HPA2_YEAST

Accession

Primary (citable) accession number: Q06592
Secondary accession number(s): D6W4J3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program