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Q8VH37 (HDAC8_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone deacetylase 8

Short name=HD8
EC=3.5.1.98
Gene names
Name:Hdac8
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length377 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

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

Cofactor

Binds 1 divalent metal cation per subunit.

Enzyme regulation

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

Subunit structure

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. Ref.5

Subcellular location

Nucleus By similarity. Cytoplasm By similarity.

Post-translational modification

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

Sequence similarities

Belongs to the histone deacetylase family. HD type 1 subfamily.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandMetal-binding
   Molecular functionChromatin regulator
Hydrolase
Repressor
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin modification

Traceable author statement PubMed 12711221. Source: UniProtKB

regulation of cohesin localization to chromatin

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

sister chromatid cohesion

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Traceable author statement PubMed 12711221. Source: UniProtKB

histone deacetylase complex

Traceable author statement PubMed 12711221. Source: UniProtKB

nucleus

Traceable author statement PubMed 12711221. Source: UniProtKB

   Molecular_functionNAD-dependent histone deacetylase activity (H3-K14 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H3-K18 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H3-K9 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H4-K16 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

histone deacetylase activity

Traceable author statement PubMed 12711221. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

transcription factor binding

Traceable author statement PubMed 12711221. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8VH37-1)

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.
Isoform 2 (identifier: Q8VH37-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 377377Histone deacetylase 8
PRO_0000114709

Regions

Region14 – 324311Histone deacetylase

Sites

Active site1431Proton acceptor By similarity
Metal binding1781Divalent metal cation By similarity
Metal binding1801Divalent metal cation By similarity
Metal binding2671Divalent metal cation By similarity
Binding site1011Substrate By similarity
Binding site1511Substrate; via carbonyl oxygen By similarity
Binding site3061Substrate By similarity

Amino acid modifications

Modified residue391Phosphoserine By similarity

Natural variations

Alternative sequence246 – 2538SVLKEVYQ → RACFTRTP in isoform 2.
VSP_007178
Alternative sequence254 – 377124Missing in isoform 2.
VSP_007179

Experimental info

Sequence conflict881E → D in AAL47569. Ref.3
Sequence conflict1181G → A in AAL47569. Ref.3
Sequence conflict1301K → M in AAL47569. Ref.3
Sequence conflict1701D → E in AAL47569. Ref.3
Sequence conflict1871D → V in AAL47569. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 11, 2003. Version 2.
Checksum: EEBD7B2517B235CD

FASTA37741,772
        10         20         30         40         50         60 
MEMPEEPANS GHSLPPVYIY SPEYVSICDS LVKVPKRASM VHSLIEAYAL HKQMRIVKPK 

        70         80         90        100        110        120 
VASMEEMATF HTDAYLQHLQ KVSQEGDEDH PDSIEYGLGY DCPATEGIFD YAAAIGGGTI 

       130        140        150        160        170        180 
TAAQCLIDGK CKVAINWSGG WHHAKKDEAS GFCYLNDAVL GILRLRRKFD RILYVDLDLH 

       190        200        210        220        230        240 
HGDGVEDAFS FTSKVMTVSL HKFSPGFFPG TGDMSDVGLG KGRYYSVNVP IQDGIQDEKY 

       250        260        270        280        290        300 
YHICESVLKE VYQAFNPKAV VLQLGADTIA GDPMCSFNMT PVGIGKCLKY VLQWQLATLI 

       310        320        330        340        350        360 
LGGGGYNLAN TARCWTYLTG VILGKTLSSE IPDHEFFTAY GPDYVLEITP SCRPDRNEPH 

       370 
RIQQILNYIK GNLKHVV 

« Hide

Isoform 2 [UniParc].

Checksum: 982E94F21829B340
Show »

FASTA25328,122

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_081658.1. NM_027382.3.
UniGeneMm.328128.

3D structure databases

ProteinModelPortalQ8VH37.
SMRQ8VH37. Positions 14-377.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid213982. 1 interaction.

Chemistry

BindingDBQ8VH37.
ChEMBLCHEMBL2347.

PTM databases

PhosphoSiteQ8VH37.

Proteomic databases

PaxDbQ8VH37.
PRIDEQ8VH37.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000087916; ENSMUSP00000085226; ENSMUSG00000067567. [Q8VH37-1]
GeneID70315.
KEGGmmu:70315.
UCSCuc009typ.1. mouse. [Q8VH37-1]
uc009tyq.1. mouse. [Q8VH37-2]

Organism-specific databases

CTD55869.
MGIMGI:1917565. Hdac8.

Phylogenomic databases

eggNOGCOG0123.
GeneTreeENSGT00530000062889.
HOGENOMHOG000225180.
HOVERGENHBG057112.
InParanoidQ8VH37.
KOK11405.
OMAKCKVAIN.
OrthoDBEOG722J95.
PhylomeDBQ8VH37.
TreeFamTF106175.

Gene expression databases

BgeeQ8VH37.
CleanExMM_HDAC8.
GenevestigatorQ8VH37.

Family and domain databases

Gene3D3.40.800.20. 1 hit.
InterProIPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERPTHR10625. PTHR10625. 1 hit.
PfamPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFPIRSF037913. His_deacetylse_1. 1 hit.
PRINTSPR01270. HDASUPER.
PR01271. HISDACETLASE.
ProtoNetSearch...

Other

NextBio331374.
PROQ8VH37.
SOURCESearch...

Entry information

Entry nameHDAC8_MOUSE
AccessionPrimary (citable) accession number: Q8VH37
Secondary accession number(s): Q3V270, Q9D0K6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: April 11, 2003
Last modified: April 16, 2014
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot