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Q8H0W2

- HDA9_ARATH

UniProt

Q8H0W2 - HDA9_ARATH

Protein

Histone deacetylase 9

Gene

HDA9

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes By similarity.By similarity

    Catalytic activityi

    Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei137 – 1371By similarity

    GO - Molecular functioni

    1. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
    2. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB-EC
    3. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB-EC
    4. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB-EC

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: UniProtKB-KW
    2. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Hydrolase, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    BioCyciARA:AT3G44680-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone deacetylase 9 (EC:3.5.1.98)
    Gene namesi
    Name:HDA9
    Ordered Locus Names:At3g44680
    ORF Names:T18B22.80
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G44680.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 426426Histone deacetylase 9PRO_0000280088Add
    BLAST

    Proteomic databases

    PRIDEiQ8H0W2.

    Expressioni

    Gene expression databases

    GenevestigatoriQ8H0W2.

    Interactioni

    Protein-protein interaction databases

    BioGridi8914. 5 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8H0W2.
    SMRiQ8H0W2. Positions 6-370.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni6 – 318313Histone deacetylaseAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi296 – 2994Poly-Gly
    Compositional biasi384 – 42441Asp-richAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0123.
    HOGENOMiHOG000225180.
    InParanoidiQ8H0W2.
    KOiK06067.
    OMAiGDVGNVY.
    PhylomeDBiQ8H0W2.

    Family and domain databases

    Gene3Di3.40.800.20. 1 hit.
    InterProiIPR000286. His_deacetylse.
    IPR003084. His_deacetylse_1.
    IPR023801. His_deacetylse_dom.
    [Graphical view]
    PANTHERiPTHR10625. PTHR10625. 1 hit.
    PfamiPF00850. Hist_deacetyl. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037913. His_deacetylse_1. 1 hit.
    PRINTSiPR01270. HDASUPER.
    PR01271. HISDACETLASE.

    Sequencei

    Sequence statusi: Complete.

    Q8H0W2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRSKDKISYF YDGDVGSVYF GPNHPMKPHR LCMTHHLILA YGLHSKMEVY    50
    RPHKAYPIEM AQFHSPDYVE FLQRINPENQ NLFPNEMARY NLGEDCPVFE 100
    DLFEFCQLYA GGTIDAARRL NNKLCDIAIN WAGGLHHAKK CDASGFCYIN 150
    DLVLGILELL KHHPRVLYID IDVHHGDGVE EAFYFTDRVM TVSFHKFGDK 200
    FFPGTGDVKE IGEREGKFYA INVPLKDGID DSSFNRLFRT IISKVVEIYQ 250
    PGAIVLQCGA DSLARDRLGC FNLSIDGHAE CVKFVKKFNL PLLVTGGGGY 300
    TKENVARCWT VETGILLDTE LPNEIPENDY IKYFAPDFSL KIPGGHIENL 350
    NTKSYISSIK VQILENLRYI QHAPSVQMQE VPPDFYIPDF DEDEQNPDVR 400
    ADQRSRDKQI QRDDEYFDGD NDNDAS 426
    Length:426
    Mass (Da):48,688
    Last modified:March 1, 2003 - v1
    Checksum:iB7B4B9D7432C6DBD
    GO

    Sequence cautioni

    The sequence CAB72470.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL138652 Genomic DNA. Translation: CAB72470.1. Sequence problems.
    CP002686 Genomic DNA. Translation: AEE77930.1.
    BT002003 mRNA. Translation: AAN72014.1.
    BT006576 mRNA. Translation: AAP31920.1.
    PIRiT47443.
    RefSeqiNP_190054.2. NM_114336.3.
    UniGeneiAt.36124.

    Genome annotation databases

    EnsemblPlantsiAT3G44680.1; AT3G44680.1; AT3G44680.
    GeneIDi823594.
    KEGGiath:AT3G44680.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL138652 Genomic DNA. Translation: CAB72470.1 . Sequence problems.
    CP002686 Genomic DNA. Translation: AEE77930.1 .
    BT002003 mRNA. Translation: AAN72014.1 .
    BT006576 mRNA. Translation: AAP31920.1 .
    PIRi T47443.
    RefSeqi NP_190054.2. NM_114336.3.
    UniGenei At.36124.

    3D structure databases

    ProteinModelPortali Q8H0W2.
    SMRi Q8H0W2. Positions 6-370.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 8914. 5 interactions.

    Proteomic databases

    PRIDEi Q8H0W2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G44680.1 ; AT3G44680.1 ; AT3G44680 .
    GeneIDi 823594.
    KEGGi ath:AT3G44680.

    Organism-specific databases

    TAIRi AT3G44680.

    Phylogenomic databases

    eggNOGi COG0123.
    HOGENOMi HOG000225180.
    InParanoidi Q8H0W2.
    KOi K06067.
    OMAi GDVGNVY.
    PhylomeDBi Q8H0W2.

    Enzyme and pathway databases

    BioCyci ARA:AT3G44680-MONOMER.

    Gene expression databases

    Genevestigatori Q8H0W2.

    Family and domain databases

    Gene3Di 3.40.800.20. 1 hit.
    InterProi IPR000286. His_deacetylse.
    IPR003084. His_deacetylse_1.
    IPR023801. His_deacetylse_dom.
    [Graphical view ]
    PANTHERi PTHR10625. PTHR10625. 1 hit.
    Pfami PF00850. Hist_deacetyl. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037913. His_deacetylse_1. 1 hit.
    PRINTSi PR01270. HDASUPER.
    PR01271. HISDACETLASE.
    ProtoNeti Search...

    Publicationsi

    1. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
      Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
      , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
      Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    4. "Analysis of histone acetyltransferase and histone deacetylase families of Arabidopsis thaliana suggests functional diversification of chromatin modification among multicellular eukaryotes."
      Pandey R., Mueller A., Napoli C.A., Selinger D.A., Pikaard C.S., Richards E.J., Bender J., Mount D.W., Jorgensen R.A.
      Nucleic Acids Res. 30:5036-5055(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY, NOMENCLATURE.

    Entry informationi

    Entry nameiHDA9_ARATH
    AccessioniPrimary (citable) accession number: Q8H0W2
    Secondary accession number(s): Q9M1N6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 6, 2007
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 79 of the entry and version 1 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. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3