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O14929

- HAT1_HUMAN

UniProt

O14929 - HAT1_HUMAN

Protein

Histone acetyltransferase type B catalytic subunit

Gene

HAT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    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.3 Publications

    Catalytic activityi

    Acetyl-CoA + [histone] = CoA + acetyl-[histone].2 Publications

    GO - Molecular functioni

    1. histone acetyltransferase activity Source: ProtInc
    2. protein binding Source: IntAct

    GO - Biological processi

    1. chromatin organization Source: Reactome
    2. chromatin silencing at telomere Source: InterPro
    3. DNA packaging Source: ProtInc
    4. DNA replication-dependent nucleosome assembly Source: UniProt
    5. DNA replication-independent nucleosome assembly Source: UniProt
    6. internal protein amino acid acetylation Source: ProtInc
    7. response to nutrient Source: Ensembl

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Enzyme and pathway databases

    ReactomeiREACT_172610. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone acetyltransferase type B catalytic subunit (EC:2.3.1.48)
    Alternative name(s):
    Histone acetyltransferase 1
    Gene namesi
    Name:HAT1
    Synonyms:KAT1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: 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

    1. cytoplasm Source: UniProtKB-SubCell
    2. intracellular membrane-bounded organelle Source: HPA
    3. nuclear chromatin Source: UniProt
    4. nuclear matrix Source: UniProtKB-SubCell
    5. nucleoplasm Source: Reactome
    6. nucleus Source: HPA
    7. protein complex Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29197.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 419418Histone acetyltransferase type B catalytic subunitPRO_0000083902Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei9 – 91N6-acetyllysineBy similarity
    Modified residuei15 – 151N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO14929.
    PaxDbiO14929.
    PeptideAtlasiO14929.
    PRIDEiO14929.

    PTM databases

    PhosphoSiteiO14929.

    Expressioni

    Developmental stagei

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

    Inductioni

    Up-regulated by estrogen.1 Publication

    Gene expression databases

    ArrayExpressiO14929.
    BgeeiO14929.
    CleanExiHS_HAT1.
    GenevestigatoriO14929.

    Organism-specific databases

    HPAiHPA036788.

    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.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HIST2H4BP628054EBI-2339359,EBI-302023
    vprP125203EBI-2339359,EBI-6164519From a different organism.

    Protein-protein interaction databases

    BioGridi114092. 26 interactions.
    DIPiDIP-52811N.
    IntActiO14929. 12 interactions.
    MINTiMINT-2795393.
    STRINGi9606.ENSP00000264108.

    Structurei

    Secondary structure

    1
    419
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi26 – 283
    Helixi29 – 324
    Beta strandi33 – 408
    Helixi41 – 444
    Helixi47 – 493
    Helixi57 – 604
    Turni61 – 644
    Beta strandi65 – 717
    Beta strandi73 – 797
    Turni80 – 823
    Beta strandi85 – 906
    Beta strandi92 – 943
    Turni97 – 993
    Beta strandi100 – 1023
    Helixi107 – 1126
    Helixi123 – 1319
    Helixi132 – 1354
    Beta strandi140 – 1489
    Beta strandi157 – 1648
    Helixi171 – 18515
    Beta strandi199 – 21012
    Beta strandi213 – 22917
    Turni230 – 2323
    Beta strandi233 – 24311
    Helixi245 – 2473
    Helixi252 – 26514
    Beta strandi273 – 2775
    Helixi280 – 29415
    Helixi298 – 3003
    Helixi302 – 3054
    Helixi311 – 32111
    Helixi325 – 33915

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2P0WX-ray1.90A/B20-341[»]
    ProteinModelPortaliO14929.
    SMRiO14929. Positions 23-341.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO14929.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the HAT1 family.Curated

    Phylogenomic databases

    eggNOGiNOG326277.
    HOGENOMiHOG000231943.
    HOVERGENiHBG005945.
    InParanoidiO14929.
    KOiK11303.
    OMAiHRYYIAS.
    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. Align

    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

    MAGFGAMEKF LVEYKSAVEK KLAEYKCNTN TAIELKLVRF PEDLENDIRT    50
    FFPEYTHQLF GDDETAFGYK GLKILLYYIA GSLSTMFRVE YASKVDENFD 100
    CVEADDVEGK IRQIIPPGFC TNTNDFLSLL EKEVDFKPFG TLLHTYSVLS 150
    PTGGENFTFQ IYKADMTCRG FREYHERLQT FLMWFIETAS FIDVDDERWH 200
    YFLVFEKYNK DGATLFATVG YMTVYNYYVY PDKTRPRVSQ MLILTPFQGQ 250
    GHGAQLLETV HRYYTEFPTV LDITAEDPSK SYVKLRDFVL VKLCQDLPCF 300
    SREKLMQGFN EDMAIEAQQK FKINKQHARR VYEILRLLVT DMSDAEQYRS 350
    YRLDIKRRLI SPYKKKQRDL AKMRKCLRPE ELTNQMNQIE ISMQHEQLEE 400
    SFQELVEDYR RVIERLAQE 419
    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 AAH18682.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti317 – 3171A → P in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035997

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8585Missing in isoform B. 1 PublicationVSP_041129Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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. [O14929-1]
    GeneIDi8520.
    KEGGihsa:8520.
    UCSCiuc002uhi.3. human. [O14929-1]
    uc010fqi.2. human. [O14929-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Histone acetyltransferase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS2245.1. [O14929-1 ]
    RefSeqi NP_003633.1. NM_003642.3. [O14929-1 ]
    UniGenei Hs.632532.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2P0W X-ray 1.90 A/B 20-341 [» ]
    ProteinModelPortali O14929.
    SMRi O14929. Positions 23-341.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114092. 26 interactions.
    DIPi DIP-52811N.
    IntActi O14929. 12 interactions.
    MINTi MINT-2795393.
    STRINGi 9606.ENSP00000264108.

    PTM databases

    PhosphoSitei O14929.

    Proteomic databases

    MaxQBi O14929.
    PaxDbi O14929.
    PeptideAtlasi O14929.
    PRIDEi O14929.

    Protocols and materials databases

    DNASUi 8520.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264108 ; ENSP00000264108 ; ENSG00000128708 . [O14929-1 ]
    GeneIDi 8520.
    KEGGi hsa:8520.
    UCSCi uc002uhi.3. human. [O14929-1 ]
    uc010fqi.2. human. [O14929-2 ]

    Organism-specific databases

    CTDi 8520.
    GeneCardsi GC02P172742.
    HGNCi HGNC:4821. HAT1.
    HPAi HPA036788.
    MIMi 603053. gene.
    neXtProti NX_O14929.
    PharmGKBi PA29197.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG326277.
    HOGENOMi HOG000231943.
    HOVERGENi HBG005945.
    InParanoidi O14929.
    KOi K11303.
    OMAi HRYYIAS.
    PhylomeDBi O14929.
    TreeFami TF314995.

    Enzyme and pathway databases

    Reactomei REACT_172610. HATs acetylate histones.

    Miscellaneous databases

    EvolutionaryTracei O14929.
    GeneWikii HAT1.
    GenomeRNAii 8520.
    NextBioi 31898.
    PROi O14929.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O14929.
    Bgeei O14929.
    CleanExi HS_HAT1.
    Genevestigatori O14929.

    Family and domain databases

    Gene3Di 3.40.630.30. 1 hit.
    3.90.360.10. 1 hit.
    InterProi IPR016181. Acyl_CoA_acyltransferase.
    IPR019467. Hat1_N.
    IPR017380. Hist_AcTrfase_B-typ_cat-su.
    [Graphical view ]
    PANTHERi PTHR12046. PTHR12046. 1 hit.
    Pfami PF10394. Hat1_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038084. HAT-B_cat. 1 hit.
    SUPFAMi SSF55729. SSF55729. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase."
      Verreault A., Kaufman P.D., Kobayashi R., Stillman B.
      Curr. Biol. 8:96-108(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, ENZYME ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION.
      Tissue: Teratocarcinoma.
    2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-419 (ISOFORM A).
      Tissue: Brain, Lung and Testis.
    5. "Effects of acetylation of histone H4 at lysines 8 and 16 on activity of the Hat1 histone acetyltransferase."
      Makowski A.M., Dutnall R.N., Annunziato A.T.
      J. Biol. Chem. 276:43499-43502(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    6. "Quantitative real-time RT-PCR analysis of eight novel estrogen-regulated genes in breast cancer."
      Sorbello V., Fuso L., Sfiligoi C., Scafoglio C., Ponzone R., Biglia N., Weisz A., Sismondi P., De Bortoli M.
      Int. J. Biol. Markers 18:123-129(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY ESTROGEN.
    7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    8. "Irradiation with heavy-ion particles changes the cellular distribution of human histone acetyltransferase HAT1."
      Lebel E.A., Boukamp P., Tafrov S.T.
      Mol. Cell. Biochem. 339:271-284(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
    9. Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: VARIANT [LARGE SCALE ANALYSIS] PRO-317.

    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: October 1, 2014
    This is version 125 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

    External Data

    Dasty 3