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Q9LXN8

- HDA17_ARATH

UniProt

Q9LXN8 - HDA17_ARATH

Protein

Histone deacetylase 17

Gene

HDA17

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
  1. 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.

    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:AT3G44490-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone deacetylase 17 (EC:3.5.1.98)
    Gene namesi
    Name:HDA17
    Ordered Locus Names:At3g44490
    ORF Names:F14L2.40
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G44490.

    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 – 158158Histone deacetylase 17PRO_0000280092Add
    BLAST

    Proteomic databases

    PaxDbiQ9LXN8.

    Expressioni

    Gene expression databases

    GenevestigatoriQ9LXN8.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT3G44490.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9LXN8.
    SMRiQ9LXN8. Positions 3-105.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni3 – 5048Histone deacetylaseAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi28 – 314Poly-Gly
    Compositional biasi116 – 15641Asp-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the histone deacetylase family.Curated

    Phylogenomic databases

    eggNOGiCOG0123.
    HOGENOMiHOG000112868.
    InParanoidiQ9LXN8.
    KOiK06067.
    OMAiDNEGESH.
    PhylomeDBiQ9LXN8.

    Family and domain databases

    Gene3Di3.40.800.20. 1 hit.
    InterProiIPR000286. His_deacetylse.
    IPR023801. His_deacetylse_dom.
    [Graphical view]
    PANTHERiPTHR10625. PTHR10625. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9LXN8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAFSMLFTGH AECVKFVKKF NLPLLVTGGG GYTKENVARC WTVETGILLD    50
    TELPNEISEN DYIKYFAPDF SLKIPGGHIE NLNTKSYISS IKVQILENLR 100
    YIQHAPSVQM QEVPPDFYIP DFDEDEQNPD VRVDQRSRDK QIQRDDEYFD 150
    GDNDNDAS 158
    Length:158
    Mass (Da):18,116
    Last modified:October 1, 2000 - v1
    Checksum:iB4C29ACF84F232E0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti58 – 581S → P in BT014712. 1 PublicationCurated
    Sequence conflicti94 – 941Q → R in BT014712. 1 PublicationCurated
    Sequence conflicti133 – 1331V → A in BT014712. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL353818 Genomic DNA. Translation: CAB88531.1.
    CP002686 Genomic DNA. Translation: AEE77907.1.
    BT014712 mRNA. No translation available.
    PIRiT48929.
    RefSeqiNP_190035.1. NM_114317.2.
    UniGeneiAt.66492.

    Genome annotation databases

    EnsemblPlantsiAT3G44490.1; AT3G44490.1; AT3G44490.
    GeneIDi823574.
    KEGGiath:AT3G44490.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL353818 Genomic DNA. Translation: CAB88531.1 .
    CP002686 Genomic DNA. Translation: AEE77907.1 .
    BT014712 mRNA. No translation available.
    PIRi T48929.
    RefSeqi NP_190035.1. NM_114317.2.
    UniGenei At.66492.

    3D structure databases

    ProteinModelPortali Q9LXN8.
    SMRi Q9LXN8. Positions 3-105.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT3G44490.1-P.

    Proteomic databases

    PaxDbi Q9LXN8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G44490.1 ; AT3G44490.1 ; AT3G44490 .
    GeneIDi 823574.
    KEGGi ath:AT3G44490.

    Organism-specific databases

    TAIRi AT3G44490.

    Phylogenomic databases

    eggNOGi COG0123.
    HOGENOMi HOG000112868.
    InParanoidi Q9LXN8.
    KOi K06067.
    OMAi DNEGESH.
    PhylomeDBi Q9LXN8.

    Enzyme and pathway databases

    BioCyci ARA:AT3G44490-MONOMER.

    Gene expression databases

    Genevestigatori Q9LXN8.

    Family and domain databases

    Gene3Di 3.40.800.20. 1 hit.
    InterProi IPR000286. His_deacetylse.
    IPR023801. His_deacetylse_dom.
    [Graphical view ]
    PANTHERi PTHR10625. PTHR10625. 1 hit.
    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. Center for eukaryotic structural genomics (CESG)
      Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-158.
      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 nameiHDA17_ARATH
    AccessioniPrimary (citable) accession number: Q9LXN8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 6, 2007
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 84 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