Histone acetyltransferase type B catalytic subunit - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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Q12341 (HAT1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 112. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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 (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	374 AA.
Sequence status	Complete.
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.7 Ref.8 Ref.9 Ref.10
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone].
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.9 Ref.10.
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 Reference proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW chromatin silencing at telomere Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from direct assay Ref.1 Ref.6. Source: SGD histone acetyltransferase complex Inferred from direct assay Ref.1 Ref.6. Source: SGD
Molecular function	histone acetyltransferase activity Inferred from direct assay Ref.2 Ref.1. Source: SGD histone binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HAT2	P39984	9	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

Poly-Leu

Amino acid modifications

Modified residue

354

Phosphoserine Ref.11

Experimental info

Sequence conflict

L → V in AAS56368. Ref.5

Secondary structure

374

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q12341 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 8DECA134274413E6
Show »

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

« Hide

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. Hani J. Nature 387:103-105(1997) [PubMed: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"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. LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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

EMBL
GenBank
DDBJ

Z48483 Genomic DNA. Translation: CAA88385.1.
Z71255 Genomic DNA. Translation: CAA95040.1.
U33335 Genomic DNA. Translation: AAB68104.1.
AY558042 Genomic DNA. Translation: AAS56368.1.
BK006949 Genomic DNA. Translation: DAA11427.1.

PIR

A57583.

RefSeq

NP_015324.1. NM_001183815.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

Q12341.

SMR

Q12341. Positions 6-320.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2362N.

IntAct

Q12341. 16 interactions.

MINT

MINT-613871.

STRING

Q12341.

Proteomic databases

PeptideAtlas

Q12341.

PRIDE

Q12341.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YPL001W; YPL001W; YPL001W.

GeneID

856106.

KEGG

sce:YPL001W.

NMPDR

fig|4932.3.peg.6458.

Organism-specific databases

CYGD

YPL001w.

SGD

S000005922. HAT1.

Phylogenomic databases

eggNOG

fuNOG05412.

GeneTree

EFGT00050000006020.

HOGENOM

HBG738699.

OMA

TAGPLHI.

OrthoDB

EOG4G7G7K.

Gene expression databases

ArrayExpress

Q12341.

Genevestigator

Q12341.

GermOnline

YPL001W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR000182. AcTrfase_GCN5-related_dom.
IPR016181. Acyl_CoA_acyltransferase.
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:3.90.360.10. G3DSA:3.90.360.10. 1 hit.
G3DSA:1.10.10.390. Histone_AcTrfase_HAT1_C. 1 hit.

K11303.

Pfam

PF10394. Hat1_N. 1 hit.
[Graphical view]

PIRSF

PIRSF038084. HAT-B_cat. 1 hit.

SUPFAM

SSF55729. Acyl_CoA_acyltransferase. 1 hit.

PROSITE

PS51186. GNAT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

981164.

Entry information

Entry name

HAT1_YEAST

Accession

Primary (citable) accession number: Q12341
Secondary accession number(s): D6W411, Q6Q5I5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	December 14, 2011
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents