Reviewed, UniProtKB/Swiss-Prot Q96DB2 (HDA11_HUMAN)

Names and origin

Protein names

Recommended name:
    Histone deacetylase 11
      Short name=HD11
    EC=3.5.1.98

Gene names

Name:

HDAC11

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	347 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. Ref.4
Catalytic activity	Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.
Subunit structure	Interacts with HDAC6. Ref.4
Subcellular location	Nucleus. Note: Predominantly nuclear.
Tissue specificity	Weakly expressed in most tissues. Strongly expressed in brain, heart, skeletal muscle, kidney and testis.
Miscellaneous	Its activity is inhibited by trapoxin, a known histone deacetylase inhibitor.
Sequence similarities	Belongs to the histone deacetylase family.
Sequence caution	The sequence BAB15127.1 differs from that shown. Reason: Erroneous termination at position 107. Translated as Gln. The sequence CAB70712.1 differs from that shown. Reason: Frameshift at positions 177, 198 and 200.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Molecular function	Chromatin regulator Hydrolase Repressor
Gene Ontology (GO)
Biological process	histone deacetylation Ref.4 Inferred from direct assay. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	histone deacetylase complex Ref.4 Inferred from direct assay. Source: UniProtKB plasma membrane Inferred from direct assay. Source: LIFEdb
Molecular function	histone deacetylase activity Ref.4 Inferred from direct assay. Source: UniProtKB transcription factor binding Traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HDAC6	Q9UBN7	1	EBI-301713,EBI-301697

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 347	347	Histone deacetylase 11		PRO_0000114715
Regions
	Region	14 – 326	313	Histone deacetylase
Sites
	Active site	143	1	By similarity
Experimental info
	Sequence conflict	15	1	R → P in BAB15272. Ref.1
	Sequence conflict	113	1	P → A Ref.3
	Sequence conflict	212	1	D → Y in CAB70712. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q96DB2-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 0D976CAF6EAC7A15	FASTA	347	39,183
	10 20 30 40 50 60 MLHTTQLYQH VPETRWPIVY SPRYNITFMG LEKLHPFDAG KWGKVINFLK EEKLLSDSML 70 80 90 100 110 120 VEAREASEED LLVVHTRRYL NELKWSFAVA TITEIPPVIF LPNFLVQRKV LRPLRTQTGG 130 140 150 160 170 180 TIMAGKLAVE RGWAINVGGG FHHCSSDRGG GFCAYADITL AIKFLFERVE GISRATIIDL 190 200 210 220 230 240 DAHQGNGHER DFMDDKRVYI MDVYNRHIYP GDRFAKQAIR RKVELEWGTE DDEYLDKVER 250 260 270 280 290 300 NIKKSLQEHL PDVVVYNAGT DILEGDRLGG LSISPAGIVK RDELVFRMVR GRRVPILMVT 310 320 330 340 SGGYQKRTAR IIADSILNLF GLGLIGPESP SVSAQNSDTP LLPPAVP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon mucosa.
[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]. Tissue: Uterus.
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 113-347. Tissue: Testis.
[4]	"Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family." Gao L., Cueto M.A., Asselbergs F., Atadja P. J. Biol. Chem. 277:25748-25755(2002) [PubMed: 11948178] [Abstract] Cited for: CHARACTERIZATION, FUNCTION, INTERACTION WITH HDAC6.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK025426 mRNA. Translation: BAB15127.1. Sequence problems. AK025890 mRNA. Translation: BAB15272.1. BC009676 mRNA. Translation: AAH09676.1. AL137362 mRNA. Translation: CAB70712.1. Frameshift.
IPI	IPI00304324.
RefSeq	NP_079103.2.
UniGene	Hs.661908
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96DB2. 4 interactions.
Proteomic databases
PRIDE	Q96DB2.
Genome annotation databases
Ensembl	ENSG00000163517. Homo sapiens. [Contig view]
GeneID	79885.
Organism-specific databases
GeneCards	GC03P013496.
H-InvDB	HIX0003075.
HGNC	HGNC:19086. HDAC11.
MIM	607226. gene.
PharmGKB	PA38793.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q96DB2.
HOVERGEN	Q96DB2.
OMA	Q96DB2. HTTQLYQ.
Enzyme and pathway databases
Pathway_Interaction_DB	hdac_classi_pathway. Signaling events mediated by HDAC Class I. hdac_classii_pathway. Signaling events mediated by HDAC Class II.
Reactome	REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	Q96DB2.
Bgee	Q96DB2.
CleanEx	HS_HDAC11.
GermOnline	ENSG00000163517. Homo sapiens.
Family and domain databases
InterPro	IPR000286. His_deacetylse. [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]
PRINTS	PR01270. HDASUPER.
ProtoNet	Search...
Other Resources
BindingDB	Q96DB2.
NextBio	69691.
SOURCE	Search...

Entry information

Entry name

HDA11_HUMAN

Accession

Primary (citable) accession number: Q96DB2
Secondary accession number(s): Q9H6I7, Q9H6X3, Q9NTC9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2002
Last sequence update:	December 1, 2001
Last modified:	June 16, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)