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Q06592

- HPA2_YEAST

UniProt

Q06592 - HPA2_YEAST

Protein

Histone acetyltransferase HPA2

Gene

HPA2

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 111 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    In vitro, acetylates histone H3 'Lys-4' and 'Lys-14' and histone H4 'Lys-5' and 'Lys-12'.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei139 – 1391Important for catalytic activity

    GO - Molecular functioni

    1. histone acetyltransferase activity Source: SGD
    2. identical protein binding Source: IntAct
    3. protein homodimerization activity Source: SGD

    GO - Biological processi

    1. histone acetylation Source: SGD
    2. protein homotetramerization Source: SGD

    Keywords - Molecular functioni

    Acyltransferase, Chromatin regulator, Transferase

    Enzyme and pathway databases

    BioCyciYEAST:G3O-34315-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone acetyltransferase HPA2 (EC:2.3.1.48)
    Gene namesi
    Name:HPA2
    Ordered Locus Names:YPR193C
    ORF Names:P9677.12
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XVI

    Organism-specific databases

    CYGDiYPR193c.
    SGDiS000006397. HPA2.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 156156Histone acetyltransferase HPA2PRO_0000074633Add
    BLAST

    Post-translational modificationi

    Autoacetylates in an intermolecular reaction.

    Expressioni

    Gene expression databases

    GenevestigatoriQ06592.

    Interactioni

    Subunit structurei

    Forms homodimers in the absence, and homotetramers in the presence of acetyl-CoA.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-34205,EBI-34205

    Protein-protein interaction databases

    BioGridi36365. 49 interactions.
    DIPiDIP-2953N.
    IntActiQ06592. 4 interactions.
    MINTiMINT-514906.
    STRINGi4932.YPR193C.

    Structurei

    Secondary structure

    1
    156
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 135
    Helixi16 – 183
    Helixi19 – 3214
    Helixi39 – 5012
    Turni52 – 543
    Beta strandi56 – 6611
    Beta strandi69 – 7810
    Beta strandi87 – 959
    Helixi97 – 993
    Beta strandi101 – 1033
    Helixi104 – 11815
    Beta strandi124 – 1296
    Helixi133 – 14210
    Beta strandi143 – 1453
    Beta strandi147 – 1537

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QSMX-ray2.40A/B/C/D5-156[»]
    1QSOX-ray2.90A/B/C/D8-156[»]
    ProteinModelPortaliQ06592.
    SMRiQ06592. Positions 5-156.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ06592.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini9 – 156148N-acetyltransferasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni93 – 10614Acetyl-CoA bindingAdd
    BLAST

    Sequence similaritiesi

    Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0454.
    GeneTreeiENSGT00390000015620.
    HOGENOMiHOG000078521.
    OMAiTHESTWI.
    OrthoDBiEOG7X3R3Q.

    Family and domain databases

    Gene3Di3.40.630.30. 1 hit.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR000182. GNAT_dom.
    [Graphical view]
    PfamiPF00583. Acetyltransf_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF55729. SSF55729. 1 hit.
    PROSITEiPS51186. GNAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q06592-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNTSEDNIT VRFVTENDKE GWQRLWKSYQ DFYEVSFPDD LDDFNFGRFL    50
    DPNIKMWAAV AVESSSEKII GMINFFNHMT TWDFKDKIYI NDLYVDENSR 100
    VKGAGGKLIQ FVYDEADKLG TPSVYWCTDE SNHRAQLLYV KVGYKAPKIL 150
    YKRKGY 156
    Length:156
    Mass (Da):18,334
    Last modified:November 1, 1996 - v1
    Checksum:i707C6EA8B8ED73A7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U25841 Genomic DNA. Translation: AAB64622.1.
    AY558056 Genomic DNA. Translation: AAS56382.1.
    BK006949 Genomic DNA. Translation: DAA11609.1.
    PIRiS58823.
    RefSeqiNP_015519.1. NM_001184290.1.

    Genome annotation databases

    EnsemblFungiiYPR193C; YPR193C; YPR193C.
    GeneIDi856323.
    KEGGisce:YPR193C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U25841 Genomic DNA. Translation: AAB64622.1 .
    AY558056 Genomic DNA. Translation: AAS56382.1 .
    BK006949 Genomic DNA. Translation: DAA11609.1 .
    PIRi S58823.
    RefSeqi NP_015519.1. NM_001184290.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QSM X-ray 2.40 A/B/C/D 5-156 [» ]
    1QSO X-ray 2.90 A/B/C/D 8-156 [» ]
    ProteinModelPortali Q06592.
    SMRi Q06592. Positions 5-156.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36365. 49 interactions.
    DIPi DIP-2953N.
    IntActi Q06592. 4 interactions.
    MINTi MINT-514906.
    STRINGi 4932.YPR193C.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YPR193C ; YPR193C ; YPR193C .
    GeneIDi 856323.
    KEGGi sce:YPR193C.

    Organism-specific databases

    CYGDi YPR193c.
    SGDi S000006397. HPA2.

    Phylogenomic databases

    eggNOGi COG0454.
    GeneTreei ENSGT00390000015620.
    HOGENOMi HOG000078521.
    OMAi THESTWI.
    OrthoDBi EOG7X3R3Q.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-34315-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q06592.
    NextBioi 981721.

    Gene expression databases

    Genevestigatori Q06592.

    Family and domain databases

    Gene3Di 3.40.630.30. 1 hit.
    InterProi IPR016181. Acyl_CoA_acyltransferase.
    IPR000182. GNAT_dom.
    [Graphical view ]
    Pfami PF00583. Acetyltransf_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55729. SSF55729. 1 hit.
    PROSITEi PS51186. GNAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. "Crystal structure of the histone acetyltransferase Hpa2: a tetrameric member of the Gcn5-related N-acetyltransferase superfamily."
      Angus-Hill M.L., Dutnall R.N., Tafrov S.T., Sternglanz R., Ramakrishnan V.
      J. Mol. Biol. 294:1311-1325(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 7-156 WITH ACETYL-COA.

    Entry informationi

    Entry nameiHPA2_YEAST
    AccessioniPrimary (citable) accession number: Q06592
    Secondary accession number(s): D6W4J3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2004
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 111 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, 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