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Q96DB2

- HDA11_HUMAN

UniProt

Q96DB2 - HDA11_HUMAN

Protein

Histone deacetylase 11

Gene

HDAC11

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (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.1 Publication

    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 sitei143 – 1431By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. chromatin modification Source: UniProtKB
    2. histone deacetylation Source: UniProtKB
    3. oligodendrocyte development Source: Ensembl
    4. regulation of transcription, DNA-templated Source: UniProtKB-KW
    5. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Hydrolase, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    BRENDAi3.5.1.98. 2681.
    ReactomeiREACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone deacetylase 11 (EC:3.5.1.98)
    Short name:
    HD11
    Gene namesi
    Name:HDAC11
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:19086. HDAC11.

    Subcellular locationi

    Nucleus
    Note: Predominantly nuclear.

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. histone deacetylase complex Source: UniProtKB
    3. nucleus Source: UniProtKB
    4. plasma membrane Source: LIFEdb

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA38793.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 347347Histone deacetylase 11PRO_0000114715Add
    BLAST

    Proteomic databases

    PaxDbiQ96DB2.
    PRIDEiQ96DB2.

    PTM databases

    PhosphoSiteiQ96DB2.

    Expressioni

    Tissue specificityi

    Weakly expressed in most tissues. Strongly expressed in brain, heart, skeletal muscle, kidney and testis.

    Gene expression databases

    ArrayExpressiQ96DB2.
    BgeeiQ96DB2.
    CleanExiHS_HDAC11.
    GenevestigatoriQ96DB2.

    Interactioni

    Subunit structurei

    Interacts with HDAC6.1 Publication

    Protein-protein interaction databases

    BioGridi122970. 134 interactions.
    IntActiQ96DB2. 129 interactions.
    MINTiMINT-1411829.
    STRINGi9606.ENSP00000295757.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96DB2.
    SMRiQ96DB2. Positions 19-333.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni14 – 326313Histone deacetylaseAdd
    BLAST

    Sequence similaritiesi

    Belongs to the histone deacetylase family.Curated

    Phylogenomic databases

    eggNOGiCOG0123.
    HOGENOMiHOG000280018.
    HOVERGENiHBG051893.
    InParanoidiQ96DB2.
    KOiK11418.
    OMAiDIIVYNA.
    PhylomeDBiQ96DB2.
    TreeFamiTF106176.

    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.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96DB2-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MLHTTQLYQH VPETRWPIVY SPRYNITFMG LEKLHPFDAG KWGKVINFLK    50
    EEKLLSDSML VEAREASEED LLVVHTRRYL NELKWSFAVA TITEIPPVIF 100
    LPNFLVQRKV LRPLRTQTGG TIMAGKLAVE RGWAINVGGG FHHCSSDRGG 150
    GFCAYADITL AIKFLFERVE GISRATIIDL DAHQGNGHER DFMDDKRVYI 200
    MDVYNRHIYP GDRFAKQAIR RKVELEWGTE DDEYLDKVER NIKKSLQEHL 250
    PDVVVYNAGT DILEGDRLGG LSISPAGIVK RDELVFRMVR GRRVPILMVT 300
    SGGYQKRTAR IIADSILNLF GLGLIGPESP SVSAQNSDTP LLPPAVP 347
    Length:347
    Mass (Da):39,183
    Last modified:December 1, 2001 - v1
    Checksum:i0D976CAF6EAC7A15
    GO
    Isoform 2 (identifier: Q96DB2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-28: Missing.
         85-107: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:296
    Mass (Da):33,124
    Checksum:i60C0E21BA00DF261
    GO

    Sequence cautioni

    The sequence CAB70712.1 differs from that shown. Reason: Frameshift at positions 177, 198 and 200.
    The sequence BAB15127.1 differs from that shown. Reason: Erroneous termination at position 107. Translated as Gln.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti15 – 151R → P in BAB15272. (PubMed:14702039)Curated
    Sequence conflicti113 – 1131P → A in CAB70712. (PubMed:17974005)Curated
    Sequence conflicti212 – 2121D → Y in CAB70712. (PubMed:17974005)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2828Missing in isoform 2. 1 PublicationVSP_043082Add
    BLAST
    Alternative sequencei85 – 10723Missing in isoform 2. 1 PublicationVSP_043083Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK025426 mRNA. Translation: BAB15127.1. Sequence problems.
    AK025890 mRNA. Translation: BAB15272.1.
    AK293223 mRNA. Translation: BAG56762.1.
    AC027124 Genomic DNA. No translation available.
    BC009676 mRNA. Translation: AAH09676.1.
    AL137362 mRNA. Translation: CAB70712.1. Frameshift.
    CCDSiCCDS2615.1. [Q96DB2-1]
    CCDS46760.1. [Q96DB2-2]
    RefSeqiNP_001129513.1. NM_001136041.2. [Q96DB2-2]
    NP_079103.2. NM_024827.3. [Q96DB2-1]
    UniGeneiHs.744132.

    Genome annotation databases

    EnsembliENST00000295757; ENSP00000295757; ENSG00000163517. [Q96DB2-1]
    ENST00000522202; ENSP00000429794; ENSG00000163517. [Q96DB2-2]
    GeneIDi79885.
    KEGGihsa:79885.
    UCSCiuc003bxy.3. human. [Q96DB2-1]
    uc011auy.2. human. [Q96DB2-2]

    Polymorphism databases

    DMDMi26394832.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK025426 mRNA. Translation: BAB15127.1 . Sequence problems.
    AK025890 mRNA. Translation: BAB15272.1 .
    AK293223 mRNA. Translation: BAG56762.1 .
    AC027124 Genomic DNA. No translation available.
    BC009676 mRNA. Translation: AAH09676.1 .
    AL137362 mRNA. Translation: CAB70712.1 . Frameshift.
    CCDSi CCDS2615.1. [Q96DB2-1 ]
    CCDS46760.1. [Q96DB2-2 ]
    RefSeqi NP_001129513.1. NM_001136041.2. [Q96DB2-2 ]
    NP_079103.2. NM_024827.3. [Q96DB2-1 ]
    UniGenei Hs.744132.

    3D structure databases

    ProteinModelPortali Q96DB2.
    SMRi Q96DB2. Positions 19-333.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122970. 134 interactions.
    IntActi Q96DB2. 129 interactions.
    MINTi MINT-1411829.
    STRINGi 9606.ENSP00000295757.

    Chemistry

    BindingDBi Q96DB2.
    ChEMBLi CHEMBL2093865.
    GuidetoPHARMACOLOGYi 2615.

    PTM databases

    PhosphoSitei Q96DB2.

    Polymorphism databases

    DMDMi 26394832.

    Proteomic databases

    PaxDbi Q96DB2.
    PRIDEi Q96DB2.

    Protocols and materials databases

    DNASUi 79885.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000295757 ; ENSP00000295757 ; ENSG00000163517 . [Q96DB2-1 ]
    ENST00000522202 ; ENSP00000429794 ; ENSG00000163517 . [Q96DB2-2 ]
    GeneIDi 79885.
    KEGGi hsa:79885.
    UCSCi uc003bxy.3. human. [Q96DB2-1 ]
    uc011auy.2. human. [Q96DB2-2 ]

    Organism-specific databases

    CTDi 79885.
    GeneCardsi GC03P013496.
    HGNCi HGNC:19086. HDAC11.
    MIMi 607226. gene.
    neXtProti NX_Q96DB2.
    PharmGKBi PA38793.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0123.
    HOGENOMi HOG000280018.
    HOVERGENi HBG051893.
    InParanoidi Q96DB2.
    KOi K11418.
    OMAi DIIVYNA.
    PhylomeDBi Q96DB2.
    TreeFami TF106176.

    Enzyme and pathway databases

    BRENDAi 3.5.1.98. 2681.
    Reactomei REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.

    Miscellaneous databases

    GeneWikii HDAC11.
    GenomeRNAii 79885.
    NextBioi 69691.
    PROi Q96DB2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96DB2.
    Bgeei Q96DB2.
    CleanExi HS_HDAC11.
    Genevestigatori Q96DB2.

    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. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Colon mucosa.
    2. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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] (ISOFORM 1).
      Tissue: Uterus.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 113-347 (ISOFORM 1).
      Tissue: Testis.
    5. "Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family."
      Gao L., Cueto M.A., Asselbergs F., Atadja P.
      J. Biol. Chem. 277:25748-25755(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, FUNCTION, INTERACTION WITH HDAC6.

    Entry informationi

    Entry nameiHDA11_HUMAN
    AccessioniPrimary (citable) accession number: Q96DB2
    Secondary accession number(s): B4DDK1
    , Q9H6I7, Q9H6X3, Q9NTC9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2002
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 125 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Its activity is inhibited by trapoxin, a known histone deacetylase inhibitor.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3