Reviewed, UniProtKB/Swiss-Prot Q9Z2V5 (HDAC6_MOUSE)

Names and origin

Protein names

Recommended name:
    Histone deacetylase 6
      Short name=HD6
    EC=3.5.1.98
Alternative name(s):
    Histone deacetylase mHDA2

Gene names

Name:

Hdac6

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	1149 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. Plays a central role in microtubule-dependent cell motility via deacetylation of tubulin By similarity.
Catalytic activity	Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.
Subunit structure	Interacts with HDAC11 and SIRT2. Interacts with F-actin F-actin. Interacts with BBIP10 By similarity. Interacts with CBFA2T3.
Subcellular location	Nucleus By similarity. Cytoplasm By similarity. Note: It is mainly cytoplasmic, where it is associated with microtubules By similarity.
Post-translational modification	Ubiquitinated. Its polyubiquitination however does not lead to its degradation By similarity. Sumoylated in vitro By similarity.
Sequence similarities	Belongs to the histone deacetylase family. Type 2 subfamily. Contains 1 UBP-type zinc finger.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Domain	Repeat Zinc-finger
Ligand	Actin-binding Metal-binding Zinc
Molecular function	Chromatin regulator Hydrolase Repressor
PTM	Phosphoprotein Ubl conjugation
Gene Ontology (GO)
Biological process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of microtubule depolymerization Inferred from direct assay. Source: MGI protein amino acid deacetylation Inferred from direct assay. Source: MGI protein polyubiquitination Inferred from direct assay. Source: MGI regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-dependent protein catabolic process Traceable author statement. Source: MGI
Cellular component	cytoplasm Inferred from direct assay. Source: MGI nucleus Traceable author statement. Source: MGI
Molecular function	actin binding Inferred from electronic annotation. Source: UniProtKB-KW histone deacetylase activity Ref.1 Inferred from direct assay. Source: MGI zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1149	1149	Histone deacetylase 6		PRO_0000114704
Regions
	Zinc finger	1065 – 1126	62	UBP-type
	Region	87 – 403	317	Histone deacetylase 1
	Region	481 – 799	319	Histone deacetylase 2
	Compositional bias	455 – 460	6	Poly-Glu
Sites
	Active site	215	1	1 By similarity
	Active site	610	1	2 By similarity
Amino acid modifications
	Modified residue	15	1	Phosphoserine Ref.3
	Modified residue	21	1	Phosphoserine By similarity
	Modified residue	29	1	Phosphothreonine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9Z2V5-1 [UniParc]. Last modified May 1, 2000. Version 2. Checksum: 2B98CDB228CE0D1D	FASTA	1,149	125,704
	10 20 30 40 50 60 MTSTGQDSST RQRKSRHNPQ SPLQESSATL KRGGKKCAVP HSSPNLAEVK KKGKMKKLSQ 70 80 90 100 110 120 PAEEDLVVGL QGLDLNPETR VPVGTGLVFD EQLNDFHCLW DDSFPESPER LHAIREQLIL 130 140 150 160 170 180 EGLLGRCVSF QAWFAEKEEL MLVHSLEYID LMETTQYMNE GELRVLAETY DSVYLHPNSY 190 200 210 220 230 240 SCACLATGSV LRLVDALMGA EIRNGMAVIR PPGHHAQHNL MDGYCMFNHL AVAARYAQKK 250 260 270 280 290 300 HRIQRVLIVD WDVHHGQGTQ FIFDQDPSVL YFSIHRYEHG RFWPHLKASN WSTIGFGQGQ 310 320 330 340 350 360 GYTINVPWNQ TGMRDADYIA AFLHILLPVA SEFQPQLVLV AAGFDALHGD PKGEMAATPA 370 380 390 400 410 420 GFAHLTHLLM GLAGGKLILS LEGGYNLRAL AKGISASLHT LLGDPCPMLE SCVVPCASAQ 430 440 450 460 470 480 ISIYCTLEAL EPFWEVLERS VETQEEDEVE EAVLEEEEEE GGWEATALPM DTWPLLQNRT 490 500 510 520 530 540 GLVYDEKMMS HCNLWDNHHP ETPQRILRIM CHLEEVGLAA RCLILPARPA LGSELLTCHS 550 560 570 580 590 600 AEYVEHLRTT EKMKTRDLHR EGANFDSIYI CPSTFACAKL ATGAACRLVE AVLSGEVLNG 610 620 630 640 650 660 IAVVRPPGHH AEPNAACGFC FFNSVAVAAR HAQIIAGRAL RILIVDWDVH HGNGTQHIFE 670 680 690 700 710 720 DDPSVLYVSL HRYDRGTFFP MGDEGASSQV GRDAGIGFTV NVPWNGPRMG DADYLAAWHR 730 740 750 760 770 780 LVLPIAYEFN PELVLISAGF DAAQGDPLGG CQVTPEGYAH LTHLLMGLAG GRIILILEGG 790 800 810 820 830 840 YNLASISESM AACTHSLLGD PPPQLTLLRP PQSGALVSIS EVIQVHRKYW RSLRLSKMED 850 860 870 880 890 900 KEECSSSRLV VKKLPPTASP VSAKEMTTPK GKVPEESVRK TIAALPGKES TLGQAKSKMA 910 920 930 940 950 960 KAVLAQGQSS EQAAKGTTLD LATSKETVGG ATTDLWASAA APENFPNQTT SVEALGETEP 970 980 990 1000 1010 1020 TPPASHTNKQ TTGASPLQGV TAQQSLQLGV LSTLELSREA EEAHDSEEGL LGEAAGGQDM 1030 1040 1050 1060 1070 1080 NSLMLTQGFG DFNTQDVFYA VTPLSWCPHL MAVCPIPAAG LDVSQPCKTC GTVQENWVCL 1090 1100 1110 1120 1130 1140 TCYQVYCSRY VNAHMVCHHE ASEHPLVLSC VDLSTWCYVC QAYVHQDDLQ DVKNAAHQNK FGEDMPHSH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a new family of higher eukaryotic histone deacetylases. Coordinate expression of differentiation-dependent chromatin modifiers." Verdel A., Khochbin S. J. Biol. Chem. 274:2440-2445(1999) [PubMed: 9891014] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6J. Tissue: Fetus.
[2]	"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.
[3]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 18973353] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF006603 mRNA. Translation: AAD09835.2.
IPI	IPI00323705.
PIR	T13964.
RefSeq	NP_034543.3.
UniGene	Mm.29854
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9Z2V5.
Proteomic databases
PRIDE	Q9Z2V5.
Genome annotation databases
Ensembl	ENSMUST00000033501; ENSMUSP00000033501; ENSMUSG00000031161; Mus musculus. [Genome view] ENSMUST00000115642; ENSMUSP00000111306; ENSMUSG00000031161; Mus musculus. [Genome view]
GeneID	15185.
UCSC	uc009sni.1. mouse.
Organism-specific databases
MGI	MGI:1333752. Hdac6.
Phylogenomic databases
HOVERGEN	Q9Z2V5.
Gene expression databases
ArrayExpress	Q9Z2V5.
Bgee	Q9Z2V5.
CleanEx	MM_HDAC6.
Genevestigator	Q9Z2V5.
GermOnline	ENSMUSG00000031161. Mus musculus.
Family and domain databases
InterPro	IPR000286. His_deacetylse. IPR001607. Znf_UBP. [Graphical view]
Gene3D	G3DSA:3.40.800.20. His_deacetylse. 2 hits.
PANTHER	PTHR10625. His_deacetylse. 1 hit.
Pfam	PF00850. Hist_deacetyl. 2 hits. PF02148. zf-UBP. 1 hit. [Graphical view]
PRINTS	PR01270. HDASUPER.
SMART	SM00290. ZnF_UBP. 1 hit. [Graphical view]
PROSITE	PS50271. ZF_UBP. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	287707.
SOURCE	Search...

Entry information

Entry name

HDAC6_MOUSE

Accession

Primary (citable) accession number: Q9Z2V5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 2000
Last modified:	October 13, 2009
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)