Reviewed, UniProtKB/Swiss-Prot Q8VH37 (HDAC8_MOUSE)

Names and origin

Protein names

Recommended name:
    Histone deacetylase 8
      Short name=HD8
    EC=3.5.1.98

Gene names

Name:

Hdac8

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 transcription Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Traceable author statement. Source: UniProtKB histone deacetylase complex Traceable author statement. Source: UniProtKB
Molecular function	histone deacetylase activity Traceable author statement. Source: UniProtKB transcription factor binding Traceable 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

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 11, 2003. Version 2. Checksum: EEBD7B2517B235CD	FASTA	377	41,772
	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
	Isoform 2. Checksum: 982E94F21829B340	FASTA	253	28,122
	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 YHICERACFT RTP

References

	« Hide 'large scale' referencesShow '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. , 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: 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
EMBLGenBankDDBJ	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

Integrated into UniProtKB/Swiss-Prot:	April 11, 2003
Last sequence update:	April 11, 2003
Last modified:	November 3, 2009
This is version 65 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)