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Q12341

- HAT1_YEAST

UniProt

Q12341 - HAT1_YEAST

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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: 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)LengthDescriptionGraphical viewFeature identifierActions
Sitei174 – 1741Interaction with histone H4 N-terminus1 Publication
Active sitei255 – 2551Proton donor/acceptor1 Publication
Binding sitei258 – 2581Acetyl-CoA2 Publications
Binding sitei267 – 2671Acetyl-CoA1 Publication

GO - Molecular functioni

  1. chromatin binding Source: SGD
  2. H4 histone acetyltransferase activity Source: SGD
  3. histone acetyltransferase activity Source: SGD

GO - Biological processi

  1. chromatin silencing at telomere Source: SGD
  2. DNA repair Source: UniProtKB-KW
  3. histone acetylation Source: SGD
  4. histone H4 acetylation Source: GOC
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.

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
ProteomesiUP000002311: Chromosome XVI

Organism-specific databases

CYGDiYPL001w.
SGDiS000005922. HAT1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. histone acetyltransferase complex Source: SGD
  3. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi197 – 1971W → E: Abolishes interaction with HAT2. 1 Publication
Mutagenesisi199 – 1991Y → E: Abolishes interaction with HAT2. 1 Publication
Mutagenesisi202 – 2021A → D: Impairs interaction with HAT2. 1 Publication
Mutagenesisi205 – 2051F → E: Abolishes interaction with HAT2. 1 Publication
Mutagenesisi214 – 2141R → A: Impairs interaction with HAT2. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 374374Histone acetyltransferase type B catalytic subunitPRO_0000083903Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei354 – 3541Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12341.
PaxDbiQ12341.
PeptideAtlasiQ12341.
PRIDEiQ12341.

Expressioni

Gene expression databases

GenevestigatoriQ12341.

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

Binary interactionsi

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

Protein-protein interaction databases

BioGridi36176. 68 interactions.
DIPiDIP-2362N.
IntActiQ12341. 13 interactions.
MINTiMINT-613871.
STRINGi4932.YPL001W.

Structurei

Secondary structure

1
374
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 114Combined sources
Beta strandi12 – 143Combined sources
Helixi15 – 184Combined sources
Beta strandi19 – 3113Combined sources
Helixi37 – 404Combined sources
Turni41 – 444Combined sources
Beta strandi45 – 517Combined sources
Beta strandi53 – 597Combined sources
Turni60 – 623Combined sources
Beta strandi65 – 706Combined sources
Beta strandi72 – 743Combined sources
Beta strandi78 – 803Combined sources
Helixi83 – 886Combined sources
Beta strandi97 – 993Combined sources
Helixi101 – 11313Combined sources
Helixi117 – 1204Combined sources
Beta strandi121 – 1288Combined sources
Beta strandi133 – 14311Combined sources
Helixi144 – 15310Combined sources
Helixi155 – 1606Combined sources
Beta strandi175 – 1817Combined sources
Turni182 – 1843Combined sources
Beta strandi187 – 19711Combined sources
Helixi202 – 2076Combined sources
Beta strandi213 – 22210Combined sources
Helixi224 – 2263Combined sources
Beta strandi228 – 2303Combined sources
Helixi231 – 24414Combined sources
Beta strandi249 – 2568Combined sources
Helixi259 – 27517Combined sources
Helixi278 – 2814Combined sources
Helixi290 – 30011Combined sources
Helixi304 – 31815Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BOBX-ray2.30A1-320[»]
4PSWX-ray2.10A4-320[»]
4PSXX-ray2.51A/D7-319[»]
ProteinModelPortaliQ12341.
SMRiQ12341. Positions 5-320.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12341.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini135 – 303169N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni42 – 443Interaction with histone H4 N-terminus1 Publication
Regioni194 – 1963Interaction with histone H4 N-terminus1 Publication
Regioni197 – 2059Interaction with HAT21 Publication
Regioni220 – 2223Acetyl-CoA binding2 Publications
Regioni227 – 2337Acetyl-CoA binding2 Publications

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi314 – 3174Poly-Leu

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG326277.
GeneTreeiENSGT00390000007069.
HOGENOMiHOG000074728.
InParanoidiQ12341.
KOiK11303.
OMAiKEANFKP.
OrthoDBiEOG7HTHSD.

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.
PfamiPF13673. Acetyltransf_10. 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti87 – 871L → V in AAS56368. (PubMed:17322287)Curated

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 .
PIRi A57583.
RefSeqi NP_015324.1. NM_001183815.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BOB X-ray 2.30 A 1-320 [» ]
4PSW X-ray 2.10 A 4-320 [» ]
4PSX X-ray 2.51 A/D 7-319 [» ]
ProteinModelPortali Q12341.
SMRi Q12341. Positions 5-320.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36176. 68 interactions.
DIPi DIP-2362N.
IntActi Q12341. 13 interactions.
MINTi MINT-613871.
STRINGi 4932.YPL001W.

Proteomic databases

MaxQBi Q12341.
PaxDbi Q12341.
PeptideAtlasi Q12341.
PRIDEi Q12341.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YPL001W ; YPL001W ; YPL001W .
GeneIDi 856106.
KEGGi sce:YPL001W.

Organism-specific databases

CYGDi YPL001w.
SGDi S000005922. HAT1.

Phylogenomic databases

eggNOGi NOG326277.
GeneTreei ENSGT00390000007069.
HOGENOMi HOG000074728.
InParanoidi Q12341.
KOi K11303.
OMAi KEANFKP.
OrthoDBi EOG7HTHSD.

Enzyme and pathway databases

BioCyci YEAST:G3O-33920-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q12341.
NextBioi 981164.
PROi Q12341.

Gene expression databases

Genevestigatori Q12341.

Family and domain databases

Gene3Di 1.10.10.390. 1 hit.
3.40.630.30. 1 hit.
3.90.360.10. 1 hit.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
IPR019467. Hat1_N.
IPR017380. Hist_AcTrfase_B-typ_cat-su.
IPR013523. Hist_AcTrfase_HAT1_C.
[Graphical view ]
PANTHERi PTHR12046. PTHR12046. 1 hit.
Pfami PF13673. Acetyltransf_10. 1 hit.
PF10394. Hat1_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF038084. HAT-B_cat. 1 hit.
SUPFAMi SSF55729. SSF55729. 1 hit.
PROSITEi PS51186. GNAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. 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, IDENTIFICATION BY 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 (2.30 ANGSTROMS) OF 1-320 IN COMPLEX WITH ACETYL-COA.
  13. "Hat2p recognizes the histone H3 tail to specify the acetylation of the newly synthesized H3/H4 heterodimer by the Hat1p/Hat2p complex."
    Li Y., Zhang L., Liu T., Chai C., Fang Q., Wu H., Agudelo Garcia P.A., Han Z., Zong S., Yu Y., Zhang X., Parthun M.R., Chai J., Xu R.M., Yang M.
    Genes Dev. 28:1217-1227(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 4-320 IN COMPLEXES WITH COENZYME A; HAT2 AND HISTONE PEPTIDES, CATALYTIC ACTIVITY, SUBUNIT, FUNCTION, ACTIVE SITE, MUTAGENESIS OF TRP-197; TYR-199; ALA-202; PHE-205 AND ARG-214.

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 26, 2014
This is version 136 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

External Data

Dasty 3