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Q8VH37

- HDAC8_MOUSE

UniProt

Q8VH37 - HDAC8_MOUSE

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Protein

Histone deacetylase 8

Gene

Hdac8

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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.
ExpressionAtlasiQ8VH37. baseline.
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

        10         20         30         40         50
MEMPEEPANS GHSLPPVYIY SPEYVSICDS LVKVPKRASM VHSLIEAYAL
60 70 80 90 100
HKQMRIVKPK VASMEEMATF HTDAYLQHLQ KVSQEGDEDH PDSIEYGLGY
110 120 130 140 150
DCPATEGIFD YAAAIGGGTI TAAQCLIDGK CKVAINWSGG WHHAKKDEAS
160 170 180 190 200
GFCYLNDAVL GILRLRRKFD RILYVDLDLH HGDGVEDAFS FTSKVMTVSL
210 220 230 240 250
HKFSPGFFPG TGDMSDVGLG KGRYYSVNVP IQDGIQDEKY YHICESVLKE
260 270 280 290 300
VYQAFNPKAV VLQLGADTIA GDPMCSFNMT PVGIGKCLKY VLQWQLATLI
310 320 330 340 350
LGGGGYNLAN TARCWTYLTG VILGKTLSSE IPDHEFFTAY GPDYVLEITP
360 370
SCRPDRNEPH RIQQILNYIK GNLKHVV
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.
ExpressionAtlasi Q8VH37. baseline.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 111 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