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Protein

Histone acetyltransferase type B catalytic subunit

Gene

HAT1

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

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.6 Publications

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei255Proton donor/acceptor1 Publication1
Binding sitei258Acetyl-CoA2 Publications1
Binding sitei267Acetyl-CoA1 Publication1

GO - Molecular functioni

  • chromatin binding Source: SGD
  • H4 histone acetyltransferase activity Source: SGD
  • histone acetyltransferase activity Source: SGD

GO - Biological processi

  • chromatin silencing at telomere Source: SGD
  • DNA repair Source: UniProtKB-KW
  • histone acetylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Chromatin regulator, Transferase

Keywords - Biological processi

DNA damage, DNA repair

Enzyme and pathway databases

BioCyciYEAST:G3O-33920-MONOMER.
ReactomeiR-SCE-3214847. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase type B catalytic subunit (EC:2.3.1.481 Publication)
Gene namesi
Name:HAT1
Ordered Locus Names:YPL001W
ORF Names:LPA16W, YP8132.12
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL001W.
SGDiS000005922. HAT1.

Subcellular locationi

GO - Cellular componenti

  • chromosome, telomeric region Source: GOC
  • cytoplasm Source: SGD
  • histone acetyltransferase complex Source: SGD
  • nuclear chromatin Source: GO_Central
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi197W → E: Abolishes interaction with HAT2. 1 Publication1
Mutagenesisi199Y → E: Abolishes interaction with HAT2. 1 Publication1
Mutagenesisi202A → D: Impairs interaction with HAT2. 1 Publication1
Mutagenesisi205F → E: Abolishes interaction with HAT2. 1 Publication1
Mutagenesisi214R → A: Impairs interaction with HAT2. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000839031 – 374Histone acetyltransferase type B catalytic subunitAdd BLAST374

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei354PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12341.
PRIDEiQ12341.

PTM databases

iPTMnetiQ12341.

Interactioni

Subunit structurei

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 HIF1.5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei174Interaction with histone H4 N-terminus1 Publication1

Binary interactionsi

WithEntry#Exp.IntActNotes
HAT2P399845EBI-8176,EBI-8185

Protein-protein interaction databases

BioGridi36176. 67 interactors.
DIPiDIP-2362N.
IntActiQ12341. 13 interactors.
MINTiMINT-613871.

Structurei

Secondary structure

1374
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 11Combined sources4
Beta strandi12 – 14Combined sources3
Helixi15 – 18Combined sources4
Beta strandi19 – 31Combined sources13
Helixi37 – 40Combined sources4
Turni41 – 44Combined sources4
Beta strandi45 – 51Combined sources7
Beta strandi53 – 59Combined sources7
Turni60 – 62Combined sources3
Beta strandi65 – 70Combined sources6
Beta strandi72 – 74Combined sources3
Beta strandi78 – 80Combined sources3
Helixi83 – 88Combined sources6
Beta strandi97 – 99Combined sources3
Helixi101 – 113Combined sources13
Helixi117 – 120Combined sources4
Beta strandi121 – 128Combined sources8
Beta strandi133 – 143Combined sources11
Helixi144 – 153Combined sources10
Helixi155 – 160Combined sources6
Beta strandi175 – 181Combined sources7
Turni182 – 184Combined sources3
Beta strandi187 – 197Combined sources11
Helixi202 – 207Combined sources6
Beta strandi213 – 222Combined sources10
Helixi224 – 226Combined sources3
Beta strandi228 – 230Combined sources3
Helixi231 – 244Combined sources14
Beta strandi249 – 256Combined sources8
Helixi259 – 275Combined sources17
Helixi278 – 281Combined sources4
Helixi290 – 300Combined sources11
Helixi304 – 318Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BOBX-ray2.30A1-320[»]
4PSWX-ray2.10A4-320[»]
4PSXX-ray2.51A/D7-319[»]
ProteinModelPortaliQ12341.
SMRiQ12341.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12341.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini135 – 303N-acetyltransferasePROSITE-ProRule annotationAdd BLAST169

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni42 – 44Interaction with histone H4 N-terminus1 Publication3
Regioni194 – 196Interaction with histone H4 N-terminus1 Publication3
Regioni197 – 205Interaction with HAT22 Publications9
Regioni220 – 222Acetyl-CoA binding2 Publications3
Regioni227 – 233Acetyl-CoA binding2 Publications7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi314 – 317Poly-Leu4

Sequence similaritiesi

Belongs to the HAT1 family.Curated
Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000007069.
HOGENOMiHOG000074728.
InParanoidiQ12341.
KOiK11303.
OMAiYIERANC.
OrthoDBiEOG092C3YYH.

Family and domain databases

Gene3Di1.10.10.390. 1 hit.
3.40.630.30. 1 hit.
3.90.360.10. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
IPR019467. Hat1_N.
IPR017380. Hist_AcTrfase_B-typ_cat-su.
IPR013523. Hist_AcTrfase_HAT1_C.
[Graphical view]
PANTHERiPTHR12046. PTHR12046. 1 hit.
PfamiPF00583. Acetyltransf_1. 1 hit.
PF10394. Hat1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF038084. HAT-B_cat. 1 hit.
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12341-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSANDFKPET WTSSANEALR VSIVGENAVQ FSPLFTYPIY GDSEKIYGYK
60 70 80 90 100
DLIIHLAFDS VTFKPYVNVK YSAKLGDDNI VDVEKKLLSF LPKDDVIVRD
110 120 130 140 150
EAKWVDCFAE ERKTHNLSDV FEKVSEYSLN GEEFVVYKSS LVDDFARRMH
160 170 180 190 200
RRVQIFSLLF IEAANYIDET DPSWQIYWLL NKKTKELIGF VTTYKYWHYL
210 220 230 240 250
GAKSFDEDID KKFRAKISQF LIFPPYQNKG HGSCLYEAII QSWLEDKSIT
260 270 280 290 300
EITVEDPNEA FDDLRDRNDI QRLRKLGYDA VFQKHSDLSD EFLESSRKSL
310 320 330 340 350
KLEERQFNRL VEMLLLLNNS PSFELKVKNR LYIKNYDALD QTDPEKAREA
360 370
LQNSFILVKD DYRRIIESIN KSQG
Length:374
Mass (Da):43,873
Last modified:November 1, 1996 - v1
Checksum:i8DECA134274413E6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti87L → V in AAS56368 (PubMed:17322287).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA57583.
RefSeqiNP_015324.1. NM_001183815.1.

Genome annotation databases

EnsemblFungiiYPL001W; YPL001W; YPL001W.
GeneIDi856106.
KEGGisce:YPL001W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA57583.
RefSeqiNP_015324.1. NM_001183815.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BOBX-ray2.30A1-320[»]
4PSWX-ray2.10A4-320[»]
4PSXX-ray2.51A/D7-319[»]
ProteinModelPortaliQ12341.
SMRiQ12341.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36176. 67 interactors.
DIPiDIP-2362N.
IntActiQ12341. 13 interactors.
MINTiMINT-613871.

PTM databases

iPTMnetiQ12341.

Proteomic databases

MaxQBiQ12341.
PRIDEiQ12341.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL001W; YPL001W; YPL001W.
GeneIDi856106.
KEGGisce:YPL001W.

Organism-specific databases

EuPathDBiFungiDB:YPL001W.
SGDiS000005922. HAT1.

Phylogenomic databases

GeneTreeiENSGT00390000007069.
HOGENOMiHOG000074728.
InParanoidiQ12341.
KOiK11303.
OMAiYIERANC.
OrthoDBiEOG092C3YYH.

Enzyme and pathway databases

BioCyciYEAST:G3O-33920-MONOMER.
ReactomeiR-SCE-3214847. HATs acetylate histones.

Miscellaneous databases

EvolutionaryTraceiQ12341.
PROiQ12341.

Family and domain databases

Gene3Di1.10.10.390. 1 hit.
3.40.630.30. 1 hit.
3.90.360.10. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
IPR019467. Hat1_N.
IPR017380. Hist_AcTrfase_B-typ_cat-su.
IPR013523. Hist_AcTrfase_HAT1_C.
[Graphical view]
PANTHERiPTHR12046. PTHR12046. 1 hit.
PfamiPF00583. Acetyltransf_1. 1 hit.
PF10394. Hat1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF038084. HAT-B_cat. 1 hit.
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHAT1_YEAST
AccessioniPrimary (citable) accession number: Q12341
Secondary accession number(s): D6W411, Q6Q5I5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 153 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, Direct protein sequencing, 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

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 one 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.