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Protein

Histone acetyltransferase type B catalytic subunit

Gene

HAT1

Organism
Zea mays (Maize)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acetylates newly synthesized histones during DNA replication. Highly specific in vitro for the non-acetylated H4 which is acetylated sequentially at 'Lys-12' and 'Lys-5' into a di-acetylated form.

Catalytic activityi

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

Enzyme regulationi

Inhibited by 5 mM of zinc, copper and iron. Unaffected by low concentrations of detergents and irreversibly inactivated by 2% ethanol, isopropanol or dimethyl sulfoxide.

Kineticsi

  1. KM=25 µM for core histones1 Publication
  2. KM=9 µM for acetyl-CoA1 Publication

    pH dependencei

    Optimum pH is 8.2-8.5.1 Publication

    Temperature dependencei

    Optimum temperature is 37 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei200 – 2001Interaction with histone H4 N-terminusBy similarity
    Active sitei276 – 2761Proton donor/acceptorBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Enzyme and pathway databases

    BRENDAi2.3.1.48. 6752.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone acetyltransferase type B catalytic subunit (EC:2.3.1.48By similarity)
    Alternative name(s):
    Histone acetyltransferase HAT B
    Histone acetyltransferase HAT-B-p50
    Gene namesi
    Name:HAT1
    Synonyms:HAC106, HATB1
    OrganismiZea mays (Maize)
    Taxonomic identifieri4577 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea
    ProteomesiUP000007305 Componenti: Unplaced

    Organism-specific databases

    GrameneiQ8LPU4.
    MaizeGDBi273678.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 468468Histone acetyltransferase type B catalytic subunitPRO_0000232126Add
    BLAST

    Proteomic databases

    PRIDEiQ8LPU4.

    Expressioni

    Developmental stagei

    Found in the dry embryo (at protein level). Maximum level of expression 22 hours after start of seed imbibition.1 Publication

    Interactioni

    Subunit structurei

    Heteromer of HAT1/p50 and p45 subunits.1 Publication

    Protein-protein interaction databases

    STRINGi4577.GRMZM5G851405_P02.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8LPU4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni242 – 2443Acetyl-CoA bindingBy similarity
    Regioni249 – 2557Acetyl-CoA bindingBy similarity

    Sequence similaritiesi

    Belongs to the HAT1 family.Curated

    Phylogenomic databases

    HOGENOMiHOG000084749.
    KOiK11303.

    Family and domain databases

    Gene3Di3.40.630.30. 1 hit.
    3.90.360.10. 1 hit.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR019467. Hat1_N.
    IPR017380. Hist_AcTrfase_B-typ_cat-su.
    [Graphical view]
    PANTHERiPTHR12046. PTHR12046. 1 hit.
    PfamiPF10394. Hat1_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038084. HAT-B_cat. 1 hit.
    SUPFAMiSSF55729. SSF55729. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q8LPU4-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MALKQKDTDA AATATGTKKR RRVFFSDTDA GVEANECMKV FLVWNPGEVS
    60 70 80 90 100
    SVDCTAIQPF DLNHFFGEDG KIYGYKNLKI NVWISAKSFH GYADVSFDET
    110 120 130 140 150
    SDGGKGITDL KPVLQNIFGE NLVEKEEFLH TFSKECEYIR TAVTNGSAIK
    160 170 180 190 200
    HDGSYESDPA VEIVRVELQG AAAFLYSRLV PLVLLLVEGS TPIDIGEHGW
    210 220 230 240 250
    EMLLVVKKAT QEAGSKFELL GFAAVHNFYH YPESIRLRIS QILVLPPYQG
    260 270 280 290 300
    EGHGLGLLEA INYIAQSENI YDVTIESPSD YLQYVRSSID CLRLLMFDPI
    310 320 330 340 350
    KPALGAIVLS LKETNLSKRA QSLRMVPPAD LMETVRQKLK INKKQFLRCW
    360 370 380 390 400
    EILVFLSLDS QDHKSMDNFR ACIYDRMKGE ILGSASGTNR KRLLQMPTSF
    410 420 430 440 450
    NKEASFAVYW TQEIEDEDEQ TVEQQPEDLK TQEQQLNELV DIQIEEIAGV
    460
    AKNVTSRCKD KMTELVVQ
    Length:468
    Mass (Da):52,721
    Last modified:April 4, 2006 - v2
    Checksum:i049F68157ED8443C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti354 – 3541V → I in AAM28228 (Ref. 2) Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U90274 mRNA. Translation: AAC03423.2.
    AF171927 Genomic DNA. Translation: AAF06742.1.
    AY093417 mRNA. Translation: AAM28228.1.
    PIRiT02064.
    RefSeqiNP_001105187.1. NM_001111717.1.
    XP_008651846.1. XM_008653624.1.
    UniGeneiZm.94647.

    Genome annotation databases

    GeneIDi542083.
    KEGGizma:542083.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U90274 mRNA. Translation: AAC03423.2.
    AF171927 Genomic DNA. Translation: AAF06742.1.
    AY093417 mRNA. Translation: AAM28228.1.
    PIRiT02064.
    RefSeqiNP_001105187.1. NM_001111717.1.
    XP_008651846.1. XM_008653624.1.
    UniGeneiZm.94647.

    3D structure databases

    ProteinModelPortaliQ8LPU4.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi4577.GRMZM5G851405_P02.

    Proteomic databases

    PRIDEiQ8LPU4.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi542083.
    KEGGizma:542083.

    Organism-specific databases

    GrameneiQ8LPU4.
    MaizeGDBi273678.

    Phylogenomic databases

    HOGENOMiHOG000084749.
    KOiK11303.

    Enzyme and pathway databases

    BRENDAi2.3.1.48. 6752.

    Family and domain databases

    Gene3Di3.40.630.30. 1 hit.
    3.90.360.10. 1 hit.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR019467. Hat1_N.
    IPR017380. Hist_AcTrfase_B-typ_cat-su.
    [Graphical view]
    PANTHERiPTHR12046. PTHR12046. 1 hit.
    PfamiPF10394. Hat1_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038084. HAT-B_cat. 1 hit.
    SUPFAMiSSF55729. SSF55729. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    1. "Analysis of the histone acetyltransferase B complex of maize embryos."
      Lusser A., Eberharter A., Loidl A., Goralik-Schramel M., Horngacher M., Hass H., Loidl P.
      Nucleic Acids Res. 27:4427-4435(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], INTERACTION WITH P45, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION.
      Strain: cv. Cuzco 251.
    2. "Sequences from the plant chromatin consortium."
      Chandler V.L., Kaeppler S.M., Kaeppler H.F., Cone K.C.
      Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. B73.
    3. "Purification and characterization of the cytoplasmic histone acetyltransferase B of maize embryos."
      Eberharter A., Lechner T., Goralik-Schramel M., Loidl P.
      FEBS Lett. 386:75-81(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES.
    4. "Substrate and sequential site specificity of cytoplasmic histone acetyltransferases of maize and rat liver."
      Koelle D., Sarg B., Lindner H., Loidl P.
      FEBS Lett. 421:109-114(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBSTRATE SPECIFICITY.

    Entry informationi

    Entry nameiHAT1_MAIZE
    AccessioniPrimary (citable) accession number: Q8LPU4
    Secondary accession number(s): O49994
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2006
    Last sequence update: April 4, 2006
    Last modified: June 24, 2015
    This is version 67 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.