Reviewed,
UniProtKB/Swiss-Prot Q8VH37 (HDAC8_MOUSE)
Last modified
November 3, 2009.
Version 65.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Histone deacetylase 8 Short name=HD8 EC=3.5.1.98 | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 377 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence 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 By similarity. |
| Catalytic activity | Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone. |
| Subunit structure | Interacts with CBFA2T3. Ref.5 |
| Subcellular location | Nucleus By similarity. |
| Miscellaneous | Its activity is inhibited by trichostatin A (TSA) and butyrate, two well known histone deacetylase inhibitors. histone deacetylase inhibitor By similarity. |
| Sequence similarities | Belongs to the histone deacetylase family. Type 1 subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transcription Transcription regulation |
| Cellular component | Nucleus |
| Coding sequence diversity | Alternative splicing |
| Molecular function | Chromatin regulator Hydrolase Repressor |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | histone deacetylation Inferred from electronic annotation. Source: InterPro regulation of transcriptionInferred from electronic annotation. Source: UniProtKB-KW transcriptionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Traceable author statement. Source: UniProtKB histone deacetylase complexTraceable author statement. Source: UniProtKB |
| Molecular function | histone deacetylase activity Traceable author statement. Source: UniProtKB transcription factor bindingTraceable author statement. 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 key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 377 | 377 | Histone deacetylase 8 | PRO_0000114709 | |||||
Regions | |||||||||
| Region | 14 – 324 | 311 | Histone deacetylase | ||||||
Sites | |||||||||
| Active site | 143 | 1 | By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 246 – 253 | 8 | SVLKEVYQ → RACFTRTP in isoform 2. | VSP_007178 | |||||
| Alternative sequence | 254 – 377 | 124 | Missing in isoform 2. | VSP_007179 | |||||
Experimental info | |||||||||
| Sequence conflict | 88 | 1 | E → D in AAL47569. Ref.3 | ||||||
| Sequence conflict | 118 | 1 | G → A in AAL47569. Ref.3 | ||||||
| Sequence conflict | 130 | 1 | K → M in AAL47569. Ref.3 | ||||||
| Sequence conflict | 170 | 1 | D → E in AAL47569. Ref.3 | ||||||
| Sequence conflict | 187 | 1 | D → V in AAL47569. Ref.3 | ||||||
Sequences
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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. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed: 16141072] [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: 15489334] [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, 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: 11533236] [Abstract] Cited for: INTERACTION WITH CBFA2T3. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| 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. | |
| IPI | IPI00132657. IPI00264257. |
| RefSeq | NP_081658.1. |
| UniGene | Mm.328128 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1C3P based on UniProtKB O67135. |
| SMR | Q8VH37. Positions 16-377. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q8VH37. |
PTM databases | |
| PhosphoSite | Q8VH37. |
Proteomic databases | |
| PRIDE | Q8VH37. |
Genome annotation databases | |
| Ensembl | ENSMUST00000087916; ENSMUSP00000085226; ENSMUSG00000067567; Mus musculus. [Genome view] ENSMUST00000113616; ENSMUSP00000109246; ENSMUSG00000067567; Mus musculus. [Genome view] |
| GeneID | 70315. |
| KEGG | mmu:70315. |
| UCSC | uc009typ.1. mouse. uc009tyq.1. mouse. |
Organism-specific databases | |
| CTD | 70315. |
| MGI | MGI:1917565. Hdac8. |
Phylogenomic databases | |
| HOGENOM | Q8VH37. |
| HOVERGEN | Q8VH37. |
| OMA | YHICESV. |
Gene expression databases | |
| ArrayExpress | Q8VH37. |
| Bgee | Q8VH37. |
| CleanEx | MM_HDAC8. |
| Genevestigator | Q8VH37. |
Family and domain databases | |
| InterPro | IPR000286. His_deacetylse. IPR003084. His_deacetylse_1. [Graphical view] |
| Gene3D | G3DSA:3.40.800.20. His_deacetylse. 1 hit. |
| PANTHER | PTHR10625. His_deacetylse. 1 hit. |
| Pfam | PF00850. Hist_deacetyl. 1 hit. [Graphical view] |
| PIRSF | PIRSF037913. His_deacetylse_1. 1 hit. |
| PRINTS | PR01270. HDASUPER. PR01271. HISDACETLASE. |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 331374. |
| SOURCE | Search... |
Entry information
| Entry name | HDAC8_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q8VH37 Secondary accession number(s): Q3V270, Q9D0K6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


