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Q941D6

- HDA14_ARATH

UniProt

Q941D6 - HDA14_ARATH

Protein

Histone deacetylase 14

Gene

HDA14

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      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 sitei202 – 2021By similarity

    GO - Molecular functioni

    1. alpha-tubulin binding Source: TAIR
    2. beta-tubulin binding Source: TAIR
    3. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
    4. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB-EC
    5. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB-EC
    6. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB-EC
    7. protein phosphatase 2A binding Source: TAIR
    8. protein self-association Source: TAIR
    9. tubulin deacetylase activity Source: TAIR

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: UniProtKB-KW
    2. transcription, DNA-templated Source: UniProtKB-KW
    3. tubulin deacetylation Source: TAIR

    Keywords - Molecular functioni

    Chromatin regulator, Hydrolase, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    BioCyciARA:AT4G33470-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone deacetylase 14 (EC:3.5.1.98)
    Gene namesi
    Name:HDA14
    Ordered Locus Names:At4g33470
    ORF Names:F17M5.230
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G33470.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. chloroplast Source: TAIR
    2. cytosol Source: TAIR
    3. nucleus Source: TAIR

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 423422Histone deacetylase 14PRO_0000280090Add
    BLAST

    Proteomic databases

    PaxDbiQ941D6.
    PRIDEiQ941D6.

    Expressioni

    Gene expression databases

    GenevestigatoriQ941D6.

    Interactioni

    Protein-protein interaction databases

    BioGridi14768. 2 interactions.
    STRINGi3702.AT4G33470.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ941D6.
    SMRiQ941D6. Positions 76-421.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni62 – 392331Histone deacetylaseAdd
    BLAST

    Sequence similaritiesi

    Belongs to the histone deacetylase family.Curated

    Phylogenomic databases

    eggNOGiCOG0123.
    HOGENOMiHOG000225183.
    InParanoidiQ941D6.
    OMAiARTAFCA.
    PhylomeDBiQ941D6.

    Family and domain databases

    Gene3Di3.40.800.20. 1 hit.
    InterProiIPR000286. His_deacetylse.
    IPR023801. His_deacetylse_dom.
    [Graphical view]
    PANTHERiPTHR10625. PTHR10625. 1 hit.
    PfamiPF00850. Hist_deacetyl. 1 hit.
    [Graphical view]
    PRINTSiPR01270. HDASUPER.

    Sequencei

    Sequence statusi: Complete.

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

    Q941D6-1 [UniParc]FASTAAdd to Basket

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    MSMALIVRPF FVPGSAGISG SRNICKKNQW RKYLLKPSGS SINCSFSTEK    50
    NPLLPSIQQL ADARLIYSVS AALGHNKESH PECSARVPAI VNALEMNELT 100
    PKFRGSQILE LANFKTATVE DIANVHDKAY VFGLEKAMDE ASDSGLIFIE 150
    GSGPTYATST TFQDSLIAAG AGMALVDSVI AASRNSVDPP IGFALIRPPG 200
    HHAVPKGPMG FCVFGNVAIA ARHAQRTHGL KRIFIIDFDV HHGNGTNDAF 250
    TEDPDIFFLS THQDGSYPGT GKISDIGKGK GEGTTLNLPL PGGSGDIAMR 300
    TVFEEIIVPC AQRFKPDIIL VSAGYDAHVL DPLANLQFTT ATYYSLAKDI 350
    KRLAKEVCGG RCVFFLEGGY NLESLSSSVA DSFRALLGED SLASEFDNPA 400
    YLYDEPMRKV RDAIQRAKSI HCL 423
    Length:423
    Mass (Da):45,577
    Last modified:December 1, 2001 - v1
    Checksum:iEA56909AFC9672E0
    GO

    Sequence cautioni

    The sequence CAB38805.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAB80064.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL035678 Genomic DNA. Translation: CAB38805.1. Sequence problems.
    AL161583 Genomic DNA. Translation: CAB80064.1. Sequence problems.
    CP002687 Genomic DNA. Translation: AEE86231.1.
    AY052234 mRNA. Translation: AAK97704.1.
    AY113069 mRNA. Translation: AAM47377.1.
    PIRiT05998.
    RefSeqiNP_567921.1. NM_119501.3.
    UniGeneiAt.26427.

    Genome annotation databases

    EnsemblPlantsiAT4G33470.1; AT4G33470.1; AT4G33470.
    GeneIDi829484.
    KEGGiath:AT4G33470.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL035678 Genomic DNA. Translation: CAB38805.1 . Sequence problems.
    AL161583 Genomic DNA. Translation: CAB80064.1 . Sequence problems.
    CP002687 Genomic DNA. Translation: AEE86231.1 .
    AY052234 mRNA. Translation: AAK97704.1 .
    AY113069 mRNA. Translation: AAM47377.1 .
    PIRi T05998.
    RefSeqi NP_567921.1. NM_119501.3.
    UniGenei At.26427.

    3D structure databases

    ProteinModelPortali Q941D6.
    SMRi Q941D6. Positions 76-421.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 14768. 2 interactions.
    STRINGi 3702.AT4G33470.1-P.

    Proteomic databases

    PaxDbi Q941D6.
    PRIDEi Q941D6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G33470.1 ; AT4G33470.1 ; AT4G33470 .
    GeneIDi 829484.
    KEGGi ath:AT4G33470.

    Organism-specific databases

    TAIRi AT4G33470.

    Phylogenomic databases

    eggNOGi COG0123.
    HOGENOMi HOG000225183.
    InParanoidi Q941D6.
    OMAi ARTAFCA.
    PhylomeDBi Q941D6.

    Enzyme and pathway databases

    BioCyci ARA:AT4G33470-MONOMER.

    Gene expression databases

    Genevestigatori Q941D6.

    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.
    Pfami PF00850. Hist_deacetyl. 1 hit.
    [Graphical view ]
    PRINTSi PR01270. HDASUPER.
    ProtoNeti Search...

    Publicationsi

    1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
      Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
      , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
      Nature 402:769-777(1999) [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.
    5. "Histone acetylation affects expression of cellular patterning genes in the Arabidopsis root epidermis."
      Xu C.-R., Liu C., Wang Y.-L., Li L.-C., Chen W.-Q., Xu Z.-H., Bai S.-N.
      Proc. Natl. Acad. Sci. U.S.A. 102:14469-14474(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiHDA14_ARATH
    AccessioniPrimary (citable) accession number: Q941D6
    Secondary accession number(s): Q9SZC4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 6, 2007
    Last sequence update: December 1, 2001
    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

    Miscellaneous

    HDA14 is not required for the cellular patterning in the root epidermis.

    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