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Q12341 (HAT1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length374 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Ref.10

Subcellular location

Cytoplasm. Nucleus Ref.9 Ref.10.

Sequence similarities

Belongs to the HAT1 family.

Contains 1 N-acetyltransferase domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HAT2P399845EBI-8176,EBI-8185

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 374374Histone acetyltransferase type B catalytic subunit
PRO_0000083903

Regions

Domain135 – 303169N-acetyltransferase
Compositional bias314 – 3174Poly-Leu

Amino acid modifications

Modified residue3541Phosphoserine Ref.11

Experimental info

Sequence conflict871L → V in AAS56368. Ref.5

Secondary structure

....................................................... 374
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q12341 [UniParc].

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

FASTA37443,873
        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' 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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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 204508 / S288c.
[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. expand/collapse author list , 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.
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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] [Europe PMC] [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.
PIRA57583.
RefSeqNP_015324.1. NM_001183815.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BOBX-ray2.30A1-320[»]
ProteinModelPortalQ12341.
SMRQ12341. Positions 6-320.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36176. 68 interactions.
DIPDIP-2362N.
IntActQ12341. 13 interactions.
MINTMINT-613871.
STRING4932.YPL001W.

Proteomic databases

PaxDbQ12341.
PeptideAtlasQ12341.
PRIDEQ12341.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPL001W; YPL001W; YPL001W.
GeneID856106.
KEGGsce:YPL001W.

Organism-specific databases

CYGDYPL001w.
SGDS000005922. HAT1.

Phylogenomic databases

eggNOGNOG326277.
GeneTreeENSGT00390000007069.
HOGENOMHOG000074728.
KOK11303.
OMAKEANFKP.
OrthoDBEOG7HTHSD.

Enzyme and pathway databases

BioCycYEAST:G3O-33920-MONOMER.

Gene expression databases

GenevestigatorQ12341.

Family and domain databases

Gene3D1.10.10.390. 1 hit.
3.40.630.30. 1 hit.
3.90.360.10. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
IPR019467. Hat1_N.
IPR017380. Hist_AcTrfase_B-typ_cat-su.
IPR013523. Hist_AcTrfase_HAT1_C.
[Graphical view]
PANTHERPTHR12046. PTHR12046. 1 hit.
PfamPF13673. Acetyltransf_10. 1 hit.
PF10394. Hat1_N. 1 hit.
[Graphical view]
PIRSFPIRSF038084. HAT-B_cat. 1 hit.
SUPFAMSSF55729. SSF55729. 1 hit.
PROSITEPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ12341.
NextBio981164.
PROQ12341.

Entry information

Entry nameHAT1_YEAST
AccessionPrimary (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: March 19, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XVI

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references