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Q8VH37

- HDAC8_MOUSE

UniProt

Q8VH37 - HDAC8_MOUSE

Protein

Histone deacetylase 8

Gene

Hdac8

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 2 (11 Apr 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. Also involved in the deacetylation of cohesin complex protein SMC3 regulating release of cohesin complexes from chromatin. May play a role in smooth muscle cell contractility By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Binds 1 divalent metal cation per subunit.

    Enzyme regulationi

    Its activity is inhibited by trichostatin A (TSA) and butyrate, 2 well known histone deacetylase inhibitors. histone deacetylase inhibitor By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei101 – 1011SubstrateBy similarity
    Active sitei143 – 1431Proton acceptorBy similarity
    Binding sitei151 – 1511Substrate; via carbonyl oxygenBy similarity
    Metal bindingi178 – 1781Divalent metal cationBy similarity
    Metal bindingi180 – 1801Divalent metal cationBy similarity
    Metal bindingi267 – 2671Divalent metal cationBy similarity
    Binding sitei306 – 3061SubstrateBy similarity

    GO - Molecular functioni

    1. histone deacetylase activity Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    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. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. chromatin modification Source: UniProtKB
    2. regulation of cohesin localization to chromatin Source: UniProtKB
    3. regulation of transcription, DNA-templated Source: UniProtKB-KW
    4. sister chromatid cohesion Source: UniProtKB
    5. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Hydrolase, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_198961. Resolution of Sister Chromatid Cohesion.
    REACT_207679. Separation of Sister Chromatids.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone deacetylase 8 (EC:3.5.1.98)
    Short name:
    HD8
    Gene namesi
    Name:Hdac8
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:1917565. Hdac8.

    Subcellular locationi

    Nucleus By similarity. Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. histone deacetylase complex Source: UniProtKB
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 377377Histone deacetylase 8PRO_0000114709Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei39 – 391PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated by PKA on serine 39. Phosphorylation reduces deacetylase activity observed preferentially on histones H3 and H4 By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8VH37.
    PaxDbiQ8VH37.
    PRIDEiQ8VH37.

    PTM databases

    PhosphoSiteiQ8VH37.

    Expressioni

    Gene expression databases

    BgeeiQ8VH37.
    CleanExiMM_HDAC8.
    GenevestigatoriQ8VH37.

    Interactioni

    Subunit structurei

    Interacts with CBFA2T3. Interacts with phosphorylated SMG5/EST1B; this interaction protects SMG5 from ubiquitin-mediated degradation. Associates with alpha-SMA (smooth muscle alpha-actin) By similarity.By similarity

    Protein-protein interaction databases

    BioGridi213982. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8VH37.
    SMRiQ8VH37. Positions 14-377.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni14 – 324311Histone deacetylaseAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0123.
    GeneTreeiENSGT00530000062889.
    HOGENOMiHOG000225180.
    HOVERGENiHBG057112.
    InParanoidiQ8VH37.
    KOiK11405.
    OMAiCLIDGKC.
    OrthoDBiEOG722J95.
    PhylomeDBiQ8VH37.
    TreeFamiTF106175.

    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.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8VH37-1) [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

    MEMPEEPANS GHSLPPVYIY SPEYVSICDS LVKVPKRASM VHSLIEAYAL    50
    HKQMRIVKPK VASMEEMATF HTDAYLQHLQ KVSQEGDEDH PDSIEYGLGY 100
    DCPATEGIFD YAAAIGGGTI TAAQCLIDGK CKVAINWSGG WHHAKKDEAS 150
    GFCYLNDAVL GILRLRRKFD RILYVDLDLH HGDGVEDAFS FTSKVMTVSL 200
    HKFSPGFFPG TGDMSDVGLG KGRYYSVNVP IQDGIQDEKY YHICESVLKE 250
    VYQAFNPKAV VLQLGADTIA GDPMCSFNMT PVGIGKCLKY VLQWQLATLI 300
    LGGGGYNLAN TARCWTYLTG VILGKTLSSE IPDHEFFTAY GPDYVLEITP 350
    SCRPDRNEPH RIQQILNYIK GNLKHVV 377
    Length:377
    Mass (Da):41,772
    Last modified:April 11, 2003 - v2
    Checksum:iEEBD7B2517B235CD
    GO
    Isoform 2 (identifier: Q8VH37-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         246-253: SVLKEVYQ → RACFTRTP
         254-377: Missing.

    Show »
    Length:253
    Mass (Da):28,122
    Checksum:i982E94F21829B340
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti88 – 881E → D in AAL47569. 1 PublicationCurated
    Sequence conflicti118 – 1181G → A in AAL47569. 1 PublicationCurated
    Sequence conflicti130 – 1301K → M in AAL47569. 1 PublicationCurated
    Sequence conflicti170 – 1701D → E in AAL47569. 1 PublicationCurated
    Sequence conflicti187 – 1871D → V in AAL47569. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei246 – 2538SVLKEVYQ → RACFTRTP in isoform 2. 1 PublicationVSP_007178
    Alternative sequencei254 – 377124Missing in isoform 2. 1 PublicationVSP_007179Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK011332 mRNA. Translation: BAB27550.1.
    AK131998 mRNA. Translation: BAE20928.1.
    BC061257 mRNA. Translation: AAH61257.1.
    AK034511 mRNA. Translation: BAC28737.1.
    AK041965 mRNA. Translation: BAC31116.1.
    AY066003 mRNA. Translation: AAL47569.1.
    CCDSiCCDS41084.1. [Q8VH37-1]
    RefSeqiNP_081658.1. NM_027382.3. [Q8VH37-1]
    UniGeneiMm.328128.

    Genome annotation databases

    EnsembliENSMUST00000087916; ENSMUSP00000085226; ENSMUSG00000067567. [Q8VH37-1]
    GeneIDi70315.
    KEGGimmu:70315.
    UCSCiuc009typ.1. mouse. [Q8VH37-1]
    uc009tyq.1. mouse. [Q8VH37-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK011332 mRNA. Translation: BAB27550.1 .
    AK131998 mRNA. Translation: BAE20928.1 .
    BC061257 mRNA. Translation: AAH61257.1 .
    AK034511 mRNA. Translation: BAC28737.1 .
    AK041965 mRNA. Translation: BAC31116.1 .
    AY066003 mRNA. Translation: AAL47569.1 .
    CCDSi CCDS41084.1. [Q8VH37-1 ]
    RefSeqi NP_081658.1. NM_027382.3. [Q8VH37-1 ]
    UniGenei Mm.328128.

    3D structure databases

    ProteinModelPortali Q8VH37.
    SMRi Q8VH37. Positions 14-377.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 213982. 1 interaction.

    Chemistry

    BindingDBi Q8VH37.
    ChEMBLi CHEMBL2347.

    PTM databases

    PhosphoSitei Q8VH37.

    Proteomic databases

    MaxQBi Q8VH37.
    PaxDbi Q8VH37.
    PRIDEi Q8VH37.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000087916 ; ENSMUSP00000085226 ; ENSMUSG00000067567 . [Q8VH37-1 ]
    GeneIDi 70315.
    KEGGi mmu:70315.
    UCSCi uc009typ.1. mouse. [Q8VH37-1 ]
    uc009tyq.1. mouse. [Q8VH37-2 ]

    Organism-specific databases

    CTDi 55869.
    MGIi MGI:1917565. Hdac8.

    Phylogenomic databases

    eggNOGi COG0123.
    GeneTreei ENSGT00530000062889.
    HOGENOMi HOG000225180.
    HOVERGENi HBG057112.
    InParanoidi Q8VH37.
    KOi K11405.
    OMAi CLIDGKC.
    OrthoDBi EOG722J95.
    PhylomeDBi Q8VH37.
    TreeFami TF106175.

    Enzyme and pathway databases

    Reactomei REACT_198961. Resolution of Sister Chromatid Cohesion.
    REACT_207679. Separation of Sister Chromatids.

    Miscellaneous databases

    NextBioi 331374.
    PROi Q8VH37.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8VH37.
    CleanExi MM_HDAC8.
    Genevestigatori Q8VH37.

    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J.
      Tissue: Brain, Embryo and Thymus.
    2. "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: Pituitary.
    3. "Selective regulation of class I and II histone deacetylase expression in cultured neural cells."
      Ajamian F., Suuronen T., Salminen A.
      Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 58-206.
    4. Lubec G., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 195-223, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain.
    5. "ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds mSin3A through its oligomerization domain."
      Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N., Downing J.R., Meyers S., Hiebert S.W.
      Mol. Cell. Biol. 21:6470-6483(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CBFA2T3.

    Entry informationi

    Entry nameiHDAC8_MOUSE
    AccessioniPrimary (citable) accession number: Q8VH37
    Secondary accession number(s): Q3V270, Q9D0K6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 11, 2003
    Last sequence update: April 11, 2003
    Last modified: October 1, 2014
    This is version 110 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3