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Protein

Histone acetyltransferase type B catalytic subunit

Gene

HAT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acetylates soluble but not nucleosomal histone H4 at 'Lys-5' (H4K5ac) and 'Lys-12' (H4K12ac) and, to a lesser extent, acetylates histone H2A at 'Lys-5' (H2AK5ac). Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. May be involved in nucleosome assembly during DNA replication and repair as part of the histone H3.1 and H3.3 complexes. May play a role in DNA repair in response to free radical damage.4 Publications

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].3 Publications

Kineticsi

kcat is 4.14 (sec-1) for acetyl-CoA.1 Publication

Manual assertion based on experiment ini

  1. KM=6.68 µM for acetyl-CoA1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei276Proton donor/acceptor1 Publication1

    GO - Molecular functioni

    • H4 histone acetyltransferase activity Source: UniProtKB
    • histone acetyltransferase activity Source: ProtInc
    • histone binding Source: GO_Central

    GO - Biological processi

    • chromatin silencing at telomere Source: InterPro
    • DNA packaging Source: ProtInc
    • DNA replication-dependent nucleosome assembly Source: UniProtKB
    • DNA replication-independent nucleosome assembly Source: UniProtKB
    • histone H4 acetylation Source: UniProtKB
    • internal protein amino acid acetylation Source: ProtInc
    • response to nutrient Source: Ensembl
    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Enzyme and pathway databases

    BioCyciZFISH:HS13275-MONOMER.
    BRENDAi2.3.1.48. 2681.
    ReactomeiR-HSA-3214847. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone acetyltransferase type B catalytic subunit (EC:2.3.1.483 Publications)
    Alternative name(s):
    Histone acetyltransferase 1
    Gene namesi
    Name:HAT1
    Synonyms:KAT1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:4821. HAT1.

    Subcellular locationi

    Isoform B :
    • Cytoplasm
    • Nucleus
    • Nucleus matrix
    • Nucleusnucleoplasm

    • Note: Localization is predominantly nuclear in normal cells. Treatment with hydrogen peroxide or ionizing radiation enhances nuclear localization through redistribution of existing protein.

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB-SubCell
    • intracellular membrane-bounded organelle Source: HPA
    • nuclear chromatin Source: UniProtKB
    • nuclear chromosome, telomeric region Source: BHF-UCL
    • nuclear matrix Source: UniProtKB-SubCell
    • nucleoplasm Source: HPA
    • nucleus Source: ProtInc
    • protein complex Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi62D → A: Strongly reduces HAT activity. 1 Publication1
    Mutagenesisi64E → A: Strongly reduces HAT activity. 1 Publication1
    Mutagenesisi187E → Q: Strongly reduces HAT activity. 1 Publication1
    Mutagenesisi199W → A: Strongly reduces HAT activity. 1 Publication1
    Mutagenesisi276E → Q: Strongly reduces HAT activity. 1 Publication1
    Mutagenesisi277D → N: Strongly reduces HAT activity. 1 Publication1

    Organism-specific databases

    DisGeNETi8520.
    PharmGKBiPA29197.

    Polymorphism and mutation databases

    BioMutaiHAT1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedCombined sources
    ChainiPRO_00000839022 – 419Histone acetyltransferase type B catalytic subunitAdd BLAST418

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylalanineCombined sources1
    Modified residuei9N6-acetyllysineBy similarity1
    Modified residuei15N6-acetyllysineBy similarity1
    Modified residuei343PhosphoserineCombined sources1

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    EPDiO14929.
    MaxQBiO14929.
    PaxDbiO14929.
    PeptideAtlasiO14929.
    PRIDEiO14929.

    PTM databases

    iPTMnetiO14929.
    PhosphoSitePlusiO14929.

    Expressioni

    Developmental stagei

    Highly expressed in mitotic cells (at protein level).1 Publication

    Inductioni

    Up-regulated by estrogen.1 Publication

    Gene expression databases

    BgeeiENSG00000128708.
    CleanExiHS_HAT1.
    ExpressionAtlasiO14929. baseline and differential.
    GenevisibleiO14929. HS.

    Organism-specific databases

    HPAiCAB037191.
    HPA036788.

    Interactioni

    Subunit structurei

    Catalytic subunit of the type B histone acetyltransferase (HAT) complex, composed of RBBP7 and HAT1. Interacts with histones H4 and H2A. The interaction is dependent of the ability of RBBP7 to bind to the N-terminus of histones. Component of the histone H3.1 and H3.3 complexes.3 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei199Interaction with histone H4 N-terminus1 Publication1

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HIST2H4BP628054EBI-2339359,EBI-302023
    MEOX2A4D1275EBI-2339359,EBI-10172134
    RBBP4Q090283EBI-2339359,EBI-620823
    RELQ048643EBI-2339359,EBI-307352
    TCF4P158843EBI-2339359,EBI-533224
    TNFAIP1Q138293EBI-2339359,EBI-2505861
    vprP125203EBI-2339359,EBI-6164519From a different organism.

    GO - Molecular functioni

    Protein-protein interaction databases

    BioGridi114092. 43 interactors.
    DIPiDIP-52811N.
    IntActiO14929. 26 interactors.
    MINTiMINT-2795393.
    STRINGi9606.ENSP00000264108.

    Structurei

    Secondary structure

    1419
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi26 – 28Combined sources3
    Helixi29 – 32Combined sources4
    Beta strandi33 – 40Combined sources8
    Helixi41 – 44Combined sources4
    Helixi47 – 49Combined sources3
    Helixi57 – 60Combined sources4
    Turni61 – 64Combined sources4
    Beta strandi65 – 71Combined sources7
    Beta strandi73 – 79Combined sources7
    Turni80 – 82Combined sources3
    Beta strandi85 – 90Combined sources6
    Beta strandi92 – 94Combined sources3
    Turni97 – 99Combined sources3
    Beta strandi100 – 102Combined sources3
    Helixi107 – 112Combined sources6
    Helixi123 – 131Combined sources9
    Helixi132 – 135Combined sources4
    Beta strandi140 – 148Combined sources9
    Beta strandi157 – 164Combined sources8
    Helixi171 – 185Combined sources15
    Beta strandi199 – 210Combined sources12
    Beta strandi213 – 229Combined sources17
    Turni230 – 232Combined sources3
    Beta strandi233 – 243Combined sources11
    Helixi245 – 247Combined sources3
    Helixi252 – 265Combined sources14
    Beta strandi273 – 277Combined sources5
    Helixi280 – 294Combined sources15
    Helixi298 – 300Combined sources3
    Helixi302 – 305Combined sources4
    Helixi311 – 321Combined sources11
    Helixi325 – 339Combined sources15

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2P0WX-ray1.90A/B20-341[»]
    ProteinModelPortaliO14929.
    SMRiO14929.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO14929.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni62 – 64Interaction with histone H4 N-terminus1 Publication3
    Regioni225 – 227Interaction with histone H4 N-terminusCurated3
    Regioni241 – 243Acetyl-CoA binding1 Publication3
    Regioni248 – 254Acetyl-CoA binding1 Publication7

    Sequence similaritiesi

    Belongs to the HAT1 family.Curated

    Phylogenomic databases

    eggNOGiKOG2696. Eukaryota.
    ENOG410XPH4. LUCA.
    HOGENOMiHOG000231943.
    HOVERGENiHBG005945.
    InParanoidiO14929.
    KOiK11303.
    OrthoDBiEOG091G0A79.
    PhylomeDBiO14929.
    TreeFamiTF314995.

    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.

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform A (identifier: O14929-1) [UniParc]FASTAAdd to basket
    Also known as: a, Nuclear

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MAGFGAMEKF LVEYKSAVEK KLAEYKCNTN TAIELKLVRF PEDLENDIRT
    60 70 80 90 100
    FFPEYTHQLF GDDETAFGYK GLKILLYYIA GSLSTMFRVE YASKVDENFD
    110 120 130 140 150
    CVEADDVEGK IRQIIPPGFC TNTNDFLSLL EKEVDFKPFG TLLHTYSVLS
    160 170 180 190 200
    PTGGENFTFQ IYKADMTCRG FREYHERLQT FLMWFIETAS FIDVDDERWH
    210 220 230 240 250
    YFLVFEKYNK DGATLFATVG YMTVYNYYVY PDKTRPRVSQ MLILTPFQGQ
    260 270 280 290 300
    GHGAQLLETV HRYYTEFPTV LDITAEDPSK SYVKLRDFVL VKLCQDLPCF
    310 320 330 340 350
    SREKLMQGFN EDMAIEAQQK FKINKQHARR VYEILRLLVT DMSDAEQYRS
    360 370 380 390 400
    YRLDIKRRLI SPYKKKQRDL AKMRKCLRPE ELTNQMNQIE ISMQHEQLEE
    410
    SFQELVEDYR RVIERLAQE
    Length:419
    Mass (Da):49,513
    Last modified:January 1, 1998 - v1
    Checksum:i509DF06E0E4E2647
    GO
    Isoform B (identifier: O14929-2) [UniParc]FASTAAdd to basket
    Also known as: b

    The sequence of this isoform differs from the canonical sequence as follows:
         1-85: Missing.

    Show »
    Length:334
    Mass (Da):39,786
    Checksum:i40E4B9925CD5DF81
    GO

    Sequence cautioni

    The sequence AAH18682 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_035997317A → P in a colorectal cancer sample; somatic mutation. 1 Publication1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_0411291 – 85Missing in isoform B. 1 PublicationAdd BLAST85

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF030424 mRNA. Translation: AAC02425.1.
    AC015976 Genomic DNA. Translation: AAY14731.1.
    AC114745 Genomic DNA. Translation: AAX93247.1.
    CH471058 Genomic DNA. Translation: EAX11195.1.
    BC018682 mRNA. Translation: AAH18682.1. Different initiation.
    BC045673 mRNA. No translation available.
    BC063003 mRNA. Translation: AAH63003.1.
    CCDSiCCDS2245.1. [O14929-1]
    RefSeqiNP_003633.1. NM_003642.3. [O14929-1]
    UniGeneiHs.632532.

    Genome annotation databases

    EnsembliENST00000264108; ENSP00000264108; ENSG00000128708.
    GeneIDi8520.
    KEGGihsa:8520.
    UCSCiuc002uhi.4. human. [O14929-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Histone acetyltransferase entry

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF030424 mRNA. Translation: AAC02425.1.
    AC015976 Genomic DNA. Translation: AAY14731.1.
    AC114745 Genomic DNA. Translation: AAX93247.1.
    CH471058 Genomic DNA. Translation: EAX11195.1.
    BC018682 mRNA. Translation: AAH18682.1. Different initiation.
    BC045673 mRNA. No translation available.
    BC063003 mRNA. Translation: AAH63003.1.
    CCDSiCCDS2245.1. [O14929-1]
    RefSeqiNP_003633.1. NM_003642.3. [O14929-1]
    UniGeneiHs.632532.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2P0WX-ray1.90A/B20-341[»]
    ProteinModelPortaliO14929.
    SMRiO14929.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi114092. 43 interactors.
    DIPiDIP-52811N.
    IntActiO14929. 26 interactors.
    MINTiMINT-2795393.
    STRINGi9606.ENSP00000264108.

    PTM databases

    iPTMnetiO14929.
    PhosphoSitePlusiO14929.

    Polymorphism and mutation databases

    BioMutaiHAT1.

    Proteomic databases

    EPDiO14929.
    MaxQBiO14929.
    PaxDbiO14929.
    PeptideAtlasiO14929.
    PRIDEiO14929.

    Protocols and materials databases

    DNASUi8520.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000264108; ENSP00000264108; ENSG00000128708.
    GeneIDi8520.
    KEGGihsa:8520.
    UCSCiuc002uhi.4. human. [O14929-1]

    Organism-specific databases

    CTDi8520.
    DisGeNETi8520.
    GeneCardsiHAT1.
    HGNCiHGNC:4821. HAT1.
    HPAiCAB037191.
    HPA036788.
    MIMi603053. gene.
    neXtProtiNX_O14929.
    PharmGKBiPA29197.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG2696. Eukaryota.
    ENOG410XPH4. LUCA.
    HOGENOMiHOG000231943.
    HOVERGENiHBG005945.
    InParanoidiO14929.
    KOiK11303.
    OrthoDBiEOG091G0A79.
    PhylomeDBiO14929.
    TreeFamiTF314995.

    Enzyme and pathway databases

    BioCyciZFISH:HS13275-MONOMER.
    BRENDAi2.3.1.48. 2681.
    ReactomeiR-HSA-3214847. HATs acetylate histones.

    Miscellaneous databases

    ChiTaRSiHAT1. human.
    EvolutionaryTraceiO14929.
    GeneWikiiHAT1.
    GenomeRNAii8520.
    PROiO14929.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000128708.
    CleanExiHS_HAT1.
    ExpressionAtlasiO14929. baseline and differential.
    GenevisibleiO14929. HS.

    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...

    Entry informationi

    Entry nameiHAT1_HUMAN
    AccessioniPrimary (citable) accession number: O14929
    Secondary accession number(s): Q49A44
    , Q53QF0, Q53SU4, Q6P594, Q8WWB9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 1, 1998
    Last modified: November 30, 2016
    This is version 149 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    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.