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Q12341

- HAT1_YEAST

UniProt

Q12341 - HAT1_YEAST

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
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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.5 Publications

    Catalytic activityi

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

    GO - Molecular functioni

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

    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

    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:2.3.1.48)
    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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    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 HIF1.4 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 – 103
    Beta strandi11 – 144
    Helixi15 – 184
    Beta strandi19 – 3113
    Helixi37 – 404
    Turni41 – 444
    Beta strandi45 – 517
    Beta strandi53 – 597
    Turni60 – 623
    Beta strandi65 – 706
    Beta strandi72 – 743
    Helixi83 – 886
    Beta strandi97 – 993
    Helixi101 – 11111
    Turni112 – 1143
    Turni117 – 1204
    Beta strandi121 – 1299
    Beta strandi132 – 1398
    Helixi144 – 15310
    Helixi155 – 1606
    Beta strandi174 – 1818
    Turni182 – 1843
    Beta strandi187 – 19610
    Beta strandi213 – 22210
    Helixi224 – 2263
    Beta strandi228 – 2303
    Helixi231 – 24515
    Beta strandi249 – 2568
    Helixi259 – 27517
    Helixi278 – 2814
    Helixi290 – 30011
    Helixi304 – 31714

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BOBX-ray2.30A1-320[»]
    ProteinModelPortaliQ12341.
    SMRiQ12341. Positions 6-320.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ12341.

    Family & Domainsi

    Domains and Repeats

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

    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.
    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

    MSANDFKPET WTSSANEALR VSIVGENAVQ FSPLFTYPIY GDSEKIYGYK    50
    DLIIHLAFDS VTFKPYVNVK YSAKLGDDNI VDVEKKLLSF LPKDDVIVRD 100
    EAKWVDCFAE ERKTHNLSDV FEKVSEYSLN GEEFVVYKSS LVDDFARRMH 150
    RRVQIFSLLF IEAANYIDET DPSWQIYWLL NKKTKELIGF VTTYKYWHYL 200
    GAKSFDEDID KKFRAKISQF LIFPPYQNKG HGSCLYEAII QSWLEDKSIT 250
    EITVEDPNEA FDDLRDRNDI QRLRKLGYDA VFQKHSDLSD EFLESSRKSL 300
    KLEERQFNRL VEMLLLLNNS PSFELKVKNR LYIKNYDALD QTDPEKAREA 350
    LQNSFILVKD DYRRIIESIN KSQG 374
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BOB X-ray 2.30 A 1-320 [» ]
    ProteinModelPortali Q12341.
    SMRi Q12341. Positions 6-320.
    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.
    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

    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 (2.3 ANGSTROMS) OF 1-320 IN COMPLEX WITH ACETYL-COENZYME A.

    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: October 1, 2014
    This is version 134 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