Reviewed, UniProtKB/Swiss-Prot Q12341 (HAT1_YEAST)

Names and origin

Protein names

Recommended name:
    Histone acetyltransferase type B catalytic subunit
    EC=2.3.1.48

Gene names

Name:	HAT1
Ordered Locus Names:	YPL001W
ORF Names:	LPA16W, YP8132.12

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	374 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of free histone H4 in the cytoplasm. The complex is also found in the nucleus, however it is not certain that it modifies histone H4 when packaged in chromatin. Histone H4 'Lys-12' acetylation is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair. Ref.2 Ref.6 Ref.7 Ref.8 Ref.9
Catalytic activity	Acetyl-CoA + histone = CoA + acetylhistone.
Subunit structure	Component of the HAT-B complex composed of at least HAT1 and HAT2. In the cytoplasm, this complex binds to the histone H4 tail. In the nucleus, the HAT-B complex has an additional component, the histone H3/H4 chaperone HIF1.
Subcellular location	Cytoplasm. Nucleus. Ref.8 Ref.9
Sequence similarities	Belongs to the HAT1 family. Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Cytoplasm Nucleus
Molecular function	Acyltransferase Chromatin regulator Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW chromatin silencing at telomere Ref.6 Ref.9 Inferred from genetic interaction. Source: SGD histone acetylation Ref.1 Ref.2 Ref.5 Inferred from direct assay. Source: SGD
Cellular component	cytoplasm Ref.1 Ref.5 Inferred from direct assay. Source: SGD histone acetyltransferase complex Ref.1 Ref.5 Ref.8 Inferred from direct assay. Source: SGD
Molecular function	H3/H4 histone acetyltransferase activity Ref.1 Ref.2 Ref.5 Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ELA1	P53861	1	EBI-8176,EBI-29191
HAT2	P39984	1	EBI-8176,EBI-8185

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 374

374

Histone acetyltransferase type B catalytic subunit

PRO_0000083903

Regions

Domain

135 – 303

169

N-acetyltransferase

Compositional bias

314 – 317

4

Poly-Leu

Amino acid modifications

Modified residue

354

1

Phosphoserine Ref.10

Experimental info

Sequence conflict

87

1

L → V in AAS56368. Ref.4

Secondary structure

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374

Helix Strand Turn

Details...

Helix

8 – 10

3

Beta strand

11 – 14

4

Helix

15 – 18

4

Beta strand

19 – 31

13

Helix

37 – 40

4

Turn

41 – 44

4

Beta strand

45 – 51

7

Beta strand

53 – 59

7

Turn

60 – 62

3

Beta strand

65 – 70

6

Beta strand

72 – 74

3

Helix

83 – 88

6

Beta strand

97 – 99

3

Helix

101 – 111

11

Turn

112 – 114

3

Turn

117 – 120

4

Beta strand

121 – 129

9

Beta strand

132 – 139

8

Helix

144 – 153

10

Helix

155 – 160

6

Beta strand

174 – 181

8

Turn

182 – 184

3

Beta strand

187 – 196

10

Beta strand

213 – 222

10

Helix

224 – 226

3

Beta strand

228 – 230

3

Helix

231 – 245

15

Beta strand

249 – 256

8

Helix

259 – 275

17

Helix

278 – 281

4

Helix

290 – 300

11

Helix

304 – 317

14

Sequences

	Sequence		Length	Mass (Da)
	Q12341-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 8DECA134274413E6	FASTA	374	43,873
	10 20 30 40 50 60 MSANDFKPET WTSSANEALR VSIVGENAVQ FSPLFTYPIY GDSEKIYGYK DLIIHLAFDS 70 80 90 100 110 120 VTFKPYVNVK YSAKLGDDNI VDVEKKLLSF LPKDDVIVRD EAKWVDCFAE ERKTHNLSDV 130 140 150 160 170 180 FEKVSEYSLN GEEFVVYKSS LVDDFARRMH RRVQIFSLLF IEAANYIDET DPSWQIYWLL 190 200 210 220 230 240 NKKTKELIGF VTTYKYWHYL GAKSFDEDID KKFRAKISQF LIFPPYQNKG HGSCLYEAII 250 260 270 280 290 300 QSWLEDKSIT EITVEDPNEA FDDLRDRNDI QRLRKLGYDA VFQKHSDLSD EFLESSRKSL 310 320 330 340 350 360 KLEERQFNRL VEMLLLLNNS PSFELKVKNR LYIKNYDALD QTDPEKAREA LQNSFILVKD 370 DYRRIIESIN KSQG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The major cytoplasmic histone acetyltransferase in yeast: links to chromatin replication and histone metabolism." Parthun M.R., Widom J., Gottschling D.E. Cell 87:85-94(1996) [PubMed: 8858151] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, ACETYLATION OF HISTONE H4, INTERACTION WITH HAT2 AND HISTONE H4.
[2]	"Identification of a gene encoding a yeast histone H4 acetyltransferase." Kleff S., Andrulis E.D., Anderson C.W., Sternglanz R. J. Biol. Chem. 270:24674-24677(1995) [PubMed: 7559580] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[3]	"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: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	"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: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"HAT1 and HAT2 proteins are components of a yeast nuclear histone acetyltransferase enzyme specific for free histone H4." Ruiz-Garcia A.B., Sendra R., Galiana M., Pamblanco M., Perez-Ortin J.E., Tordera V. J. Biol. Chem. 273:12599-12605(1998) [PubMed: 9575221] [Abstract] Cited for: ACETYLATION OF HISTONE H4 BY THE HAT-B COMPLEX.
[6]	"Type B histone acetyltransferase Hat1p participates in telomeric silencing." Kelly T.J., Qin S., Gottschling D.E., Parthun M.R. Mol. Cell. Biol. 20:7051-7058(2000) [PubMed: 10982821] [Abstract] Cited for: FUNCTION, ACETYLATION OF HISTONE H4.
[7]	"Histone H3 and the histone acetyltransferase Hat1p contribute to DNA double-strand break repair." Qin S., Parthun M.R. Mol. Cell. Biol. 22:8353-8365(2002) [PubMed: 12417736] [Abstract] Cited for: FUNCTION.
[8]	"Hif1 is a component of yeast histone acetyltransferase B, a complex mainly localized in the nucleus." Poveda A., Pamblanco M., Tafrov S., Tordera V., Sternglanz R., Sendra R. J. Biol. Chem. 279:16033-16043(2004) [PubMed: 14761951] [Abstract] Cited for: INTERACTION WITH HIF1 AND HISTONE H4, FUNCTION OF THE HAT-B COMPLEX, SUBCELLULAR LOCATION.
[9]	"The nuclear Hat1p/Hat2p complex: a molecular link between type B histone acetyltransferases and chromatin assembly." Ai X., Parthun M.R. Mol. Cell 14:195-205(2004) [PubMed: 15099519] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE HAT-B COMPLEX, MASS SPECTROMETRY, INTERACTION WITH HISTONES H3 AND H4, SUBCELLULAR LOCATION.
[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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, MASS SPECTROMETRY.
[11]	"Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily." Dutnall R.N., Tafrov S.T., Sternglanz R., Ramakrishnan V. Cell 94:427-438(1998) [PubMed: 9727486] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-320 IN COMPLEX WITH ACETYL-COENZYME A.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Z48483 Genomic DNA. Translation: CAA88385.1.
Z71255 Genomic DNA. Translation: CAA95040.1.
U33335 Genomic DNA. Translation: AAB68104.1.
AY558042 Genomic DNA. Translation: AAS56368.1.

PIR

A57583.

RefSeq

NP_015324.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BOB	X-ray	2.30	A	1-320	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:2362N.

IntAct

Q12341. 13 interactions.

Proteomic databases

PeptideAtlas

Q12341.

PRIDE

Q12341.

Genome annotation databases

Ensembl

YPL001W. Saccharomyces cerevisiae. [Contig view]

GeneID

856106.

GenomeReviews

Gene locus YPL001W in contig U00094_GR.

KEGG

sce:YPL001W.

NMPDR

fig|4932.3.peg.6458.

Organism-specific databases

CYGD

YPL001w.

SGD

S000005922. HAT1.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

Q12341.

OMA

Q12341. AETIYGY.

Enzyme and pathway databases

BRENDA

2.3.1.48. 250.

Gene expression databases

ArrayExpress

Q12341.

GermOnline

YPL001W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR016181. Acyl_CoA_acyltransferase.
IPR000182. GCN5-rel_AcTrfase.
IPR019467. Hat1_N.
IPR017380. Hist_AcTrfase_B-typ_cat-su.
IPR013523. Hist_AcTrfase_HAT1_C.
[Graphical view]

Gene3D

G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
G3DSA:1.10.10.390. Histone_AcTrfase_HAT1_C. 1 hit.

Pfam

PF10394. Hat1_N. 1 hit.
[Graphical view]

PIRSF

PIRSF038084. HAT-B_cat. 1 hit.

PROSITE

PS51186. GNAT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

981164.

Entry information

Entry name

HAT1_YEAST

Accession

Primary (citable) accession number: Q12341
Secondary accession number(s): Q6Q5I5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)