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Q8BY71

- HAT1_MOUSE

UniProt

Q8BY71 - HAT1_MOUSE

Protein

Histone acetyltransferase type B catalytic subunit

Gene

Hat1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      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 By similarity.By similarity

    Catalytic activityi

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

    GO - Molecular functioni

    1. histone acetyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. chromatin silencing at telomere Source: InterPro
    2. response to nutrient Source: Ensembl

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Enzyme and pathway databases

    ReactomeiREACT_226917. 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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:96013. Hat1.

    Subcellular locationi

    Nucleus matrix By similarity

    GO - Cellular componenti

    1. nuclear matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 416415Histone acetyltransferase type B catalytic subunitPRO_0000227729Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei6 – 61N6-acetyllysine1 Publication
    Modified residuei12 – 121N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ8BY71.
    PaxDbiQ8BY71.
    PRIDEiQ8BY71.

    PTM databases

    PhosphoSiteiQ8BY71.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8BY71.
    BgeeiQ8BY71.
    CleanExiMM_HAT1.
    GenevestigatoriQ8BY71.

    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 By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ8BY71. 3 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BY71.
    SMRiQ8BY71. Positions 20-338.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the HAT1 family.Curated

    Phylogenomic databases

    eggNOGiNOG326277.
    GeneTreeiENSGT00390000007069.
    HOGENOMiHOG000231943.
    HOVERGENiHBG005945.
    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.

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

    Q8BY71-1 [UniParc]FASTAAdd to Basket

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    MAALEKFLVE YKSAVEKKLA EYKCNTNTAI ELKLVRFPED LENDIRTFFP    50
    EYTHQLFGDD ETAFGYKGLK ILLYYIAGSL STLFRVEYSS KVDENFDCVE 100
    ADDVEGKIRQ IIPPGFCTNT NDFLSLLEKE TNFKPFGTLL HTYTVPSQTG 150
    GETFTFQIHK ADMTCRGFRE YHERLQTFLM WFIETASFID VDDERWHYFL 200
    VFEKYNKDGA TLFATVGYMT VYNYYVYPDK TRPRVSQMLI LTPFQGQGHG 250
    AQLLETVHRY YISFPTVLDI TAEDPSRSYL KLRDFVLVKF CQFLPSFSRE 300
    RLLQGFSEDM AIQAQQMFKI NKQHARRVYE ILRLLVTDMS DAEQYRSYRL 350
    DIKRRLISPY KKKQRDLAKM KKCLRPEELT NQMNQIEISV QHEQLEERFQ 400
    ELVEDYRRVI ERLAQE 416
    Length:416
    Mass (Da):49,278
    Last modified:March 1, 2003 - v1
    Checksum:iA20D53ABF1A7C824
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK041700 mRNA. Translation: BAC31038.1.
    AK169315 mRNA. Translation: BAE41070.1.
    BC055460 mRNA. Translation: AAH55460.1.
    CCDSiCCDS16114.1.
    RefSeqiNP_080391.2. NM_026115.4.
    UniGeneiMm.272472.

    Genome annotation databases

    EnsembliENSMUST00000028408; ENSMUSP00000028408; ENSMUSG00000027018.
    GeneIDi107435.
    KEGGimmu:107435.
    UCSCiuc008kap.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK041700 mRNA. Translation: BAC31038.1 .
    AK169315 mRNA. Translation: BAE41070.1 .
    BC055460 mRNA. Translation: AAH55460.1 .
    CCDSi CCDS16114.1.
    RefSeqi NP_080391.2. NM_026115.4.
    UniGenei Mm.272472.

    3D structure databases

    ProteinModelPortali Q8BY71.
    SMRi Q8BY71. Positions 20-338.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8BY71. 3 interactions.

    PTM databases

    PhosphoSitei Q8BY71.

    Proteomic databases

    MaxQBi Q8BY71.
    PaxDbi Q8BY71.
    PRIDEi Q8BY71.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000028408 ; ENSMUSP00000028408 ; ENSMUSG00000027018 .
    GeneIDi 107435.
    KEGGi mmu:107435.
    UCSCi uc008kap.1. mouse.

    Organism-specific databases

    CTDi 8520.
    MGIi MGI:96013. Hat1.

    Phylogenomic databases

    eggNOGi NOG326277.
    GeneTreei ENSGT00390000007069.
    HOGENOMi HOG000231943.
    HOVERGENi HBG005945.
    KOi K11303.

    Enzyme and pathway databases

    Reactomei REACT_226917. HATs acetylate histones.

    Miscellaneous databases

    ChiTaRSi HAT1. mouse.
    NextBioi 358792.
    PROi Q8BY71.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8BY71.
    Bgeei Q8BY71.
    CleanExi MM_HAT1.
    Genevestigatori Q8BY71.

    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Heart and Thymus.
    2. "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].
      Strain: FVB/N.
      Tissue: Mammary tumor.
    3. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-6 AND LYS-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiHAT1_MOUSE
    AccessioniPrimary (citable) accession number: Q8BY71
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 21, 2006
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 83 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3