Histone deacetylase

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityⁱ

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

  <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More...</a></p> Automatic assertion according to rulesⁱ

  • PIRNR:PIRNR037913

  EC:3.5.1.98

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• histone deacetylase activity Source: FlyBase <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "dSIR2 and dHDAC6: two novel, inhibitor-resistant deacetylases in Drosophila melanogaster."
    Barlow A.L., van Drunen C.M., Johnson C.A., Tweedie S., Bird A., Turner B.M.
    Exp. Cell Res. 265:90-103(2001) [PubMed] [Europe PMC] [Abstract]
  • "Individual histone deacetylases in Drosophila modulate transcription of distinct genes."
    Cho Y., Griswold A., Campbell C., Min K.T.
    Genomics 86:606-617(2005) [PubMed] [Europe PMC] [Abstract]
• metal ion binding Source: UniProtKB-KW
• NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
• protein domain specific binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "The Brm-HDAC3-Erm repressor complex suppresses dedifferentiation in Drosophila type II neuroblast lineages."
    Koe C.T., Li S., Rossi F., Wong J.J., Wang Y., Zhang Z., Chen K., Aw S.S., Richardson H.E., Robson P., Sung W.K., Yu F., Gonzalez C., Wang H.
    Elife 3:E01906-E01906(2014) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• chromatin silencing Source: FlyBase <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Drosophila histone deacetylase-3 controls imaginal disc size through suppression of apoptosis."
    Zhu C.C., Bornemann D.J., Zhitomirsky D., Miller E.L., O'Connor M.B., Simon J.A.
    PLoS Genet. 4:e1000009-e1000009(2008) [PubMed] [Europe PMC] [Abstract]
• histone deacetylation Source: FlyBaseInferred from direct assayⁱ
  • "Individual histone deacetylases in Drosophila modulate transcription of distinct genes."
    Cho Y., Griswold A., Campbell C., Min K.T.
    Genomics 86:606-617(2005) [PubMed] [Europe PMC] [Abstract]
• histone H3 deacetylation Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• histone H4 deacetylation Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• negative regulation of apoptotic process Source: FlyBaseInferred from mutant phenotypeⁱ
  • "Drosophila histone deacetylase-3 controls imaginal disc size through suppression of apoptosis."
    Zhu C.C., Bornemann D.J., Zhitomirsky D., Miller E.L., O'Connor M.B., Simon J.A.
    PLoS Genet. 4:e1000009-e1000009(2008) [PubMed] [Europe PMC] [Abstract]
• positive regulation of cell growth Source: FlyBaseInferred from mutant phenotypeⁱ
  • "Depletion of histone deacetylase 3 antagonizes PI3K-mediated overgrowth of Drosophila organs through the acetylation of histone H4 at lysine 16."
    Lv W.W., Wei H.M., Wang D.L., Ni J.Q., Sun F.L.
    J. Cell. Sci. 125:5369-5378(2012) [PubMed] [Europe PMC] [Abstract]
• positive regulation of transcription by RNA polymerase II Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• regulation of transcription, DNA-templated Source: FlyBaseInferred from direct assayⁱ
  • "Individual histone deacetylases in Drosophila modulate transcription of distinct genes."
    Cho Y., Griswold A., Campbell C., Min K.T.
    Genomics 86:606-617(2005) [PubMed] [Europe PMC] [Abstract]

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Keywords - Cellular componentⁱ

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Proteomic databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

GO - Molecular functionⁱ

• protein domain specific binding Source: UniProtKBInferred from physical interactionⁱ
  • "The Brm-HDAC3-Erm repressor complex suppresses dedifferentiation in Drosophila type II neuroblast lineages."
    Koe C.T., Li S., Rossi F., Wong J.J., Wang Y., Zhang Z., Chen K., Aw S.S., Richardson H.E., Robson P., Sung W.K., Yu F., Gonzalez C., Wang H.
    Elife 3:E01906-E01906(2014) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

        10         20         30         40         50
MTDRRVSYFY NADVGNFHYG AGHPMKPQRL AVTHSLVMNY GLHKKMKIYR 
        60         70         80         90        100
PYKASAQDML RFHSDEYIAY LQQVTPQNIQ CNSVAYTKYL AHFSVGEDCP 
       110        120        130        140        150
VFDGLFDFCA MYTGASLEGA QKLNHNHSDI CINWSGGLHH AKKFEASGFC 
       160        170        180        190        200
YVNDIVIGIL ELLKYHPRVL YIDIDVHHGD GVQEAFYLTD RVMTASFHKY 
       210        220        230        240        250
GNYFFPGTGD MYEIGAESGR YYSVNVPLKE GIDDQSYFQV FKPIISAIMD 
       260        270        280        290        300
FYRPTAIVLQ CGADSLAGDR LGCFSLSTKG HGECVKFVKE LNVPTLVVGG 
       310        320        330        340        350
GGYTLRNVAR CWTHETSLLV DQDIENDLPA TEYYDFFAPD FTLHPEINSR 
       360        370        380        390        400
QDNANSKQYL ELIVKHVYEN LKMCQHSPSV QMVQTPPDVD LEELRSNREE 
       410        420        430 
ASDPDVRISV ADEDKLVDAK NEFYDGDQDQ DKPDSAES              

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ