Q96DB2 (HDA11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	347 AA.
Sequence status	Complete.
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.5
Catalytic activity	Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.
Subunit structure	Interacts with HDAC6. Ref.5
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
Coding sequence diversity	Alternative splicing
Molecular function	Chromatin regulator Hydrolase Repressor
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone H3 deacetylation Inferred from electronic annotation. Source: GOC histone H4 deacetylation Inferred from electronic annotation. Source: GOC oligodendrocyte development Inferred from electronic annotation. Source: Compara regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	histone deacetylase complex Inferred from direct assay Ref.5. Source: UniProtKB plasma membrane Inferred from direct assay. Source: LIFEdb
Molecular_function	NAD-dependent histone deacetylase activity (H3-K14 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H3-K18 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H3-K9 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H4-K16 specific) Inferred from electronic annotation. Source: EC histone deacetylase activity Inferred from direct assay Ref.5. Source: UniProtKB 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: Q96DB2-1)

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: Q96DB2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: Missing.
     85-107: Missing.

Note: No experimental confirmation available.

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
Natural variations
	Alternative sequence	1 – 28	28	Missing in isoform 2.		VSP_043082
	Alternative sequence	85 – 107	23	Missing in isoform 2.		VSP_043083
Experimental info
	Sequence conflict	15	1	R → P in BAB15272. Ref.1
	Sequence conflict	113	1	P → A in CAB70712. Ref.4
	Sequence conflict	212	1	D → Y in CAB70712. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 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
	Isoform 2 [UniParc]. Checksum: 60C0E21BA00DF261	FASTA	296	33,124
	10 20 30 40 50 60 MGLEKLHPFD AGKWGKVINF LKEEKLLSDS MLVEAREASE EDLLVVHTRR YLNELKRKVL 70 80 90 100 110 120 RPLRTQTGGT IMAGKLAVER GWAINVGGGF HHCSSDRGGG FCAYADITLA IKFLFERVEG 130 140 150 160 170 180 ISRATIIDLD AHQGNGHERD FMDDKRVYIM DVYNRHIYPG DRFAKQAIRR KVELEWGTED 190 200 210 220 230 240 DEYLDKVERN IKKSLQEHLP DVVVYNAGTD ILEGDRLGGL SISPAGIVKR DELVFRMVRG 250 260 270 280 290 RRVPILMVTS GGYQKRTARI IADSILNLFG LGLIGPESPS VSAQNSDTPL LPPAVP

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Colon mucosa.
[2]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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: Uterus.
[4]	"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., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 113-347 (ISOFORM 1). Tissue: Testis.
[5]	"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] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, FUNCTION, INTERACTION WITH HDAC6.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK025426 mRNA. Translation: BAB15127.1. Sequence problems. AK025890 mRNA. Translation: BAB15272.1. AK293223 mRNA. Translation: BAG56762.1. AC027124 Genomic DNA. No translation available. BC009676 mRNA. Translation: AAH09676.1. AL137362 mRNA. Translation: CAB70712.1. Frameshift.
IPI	IPI00304324. IPI01013583.
RefSeq	NP_001129513.1. NM_001136041.2. NP_079103.2. NM_024827.3.
UniGene	Hs.404802.
3D structure databases
ProteinModelPortal	Q96DB2.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96DB2. 5 interactions.
MINT	MINT-1411829.
STRING	9606.ENSP00000295757.
PTM databases
PhosphoSite	Q96DB2.
Polymorphism databases
DMDM	26394832.
Proteomic databases
PaxDb	Q96DB2.
PRIDE	Q96DB2.
Protocols and materials databases
DNASU	79885.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000295757; ENSP00000295757; ENSG00000163517. ENST00000522202; ENSP00000429794; ENSG00000163517.
GeneID	79885.
KEGG	hsa:79885.
UCSC	uc003bxy.3. human.
Organism-specific databases
CTD	79885.
GeneCards	GC03P013496.
HGNC	HGNC:19086. HDAC11.
MIM	607226. gene.
neXtProt	NX_Q96DB2.
PharmGKB	PA38793.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0123.
HOGENOM	HOG000280018.
HOVERGEN	HBG051893.
InParanoid	Q96DB2.
KO	K11418.
OMA	DRGWAIN.
PhylomeDB	Q96DB2.
Enzyme and pathway databases
BRENDA	3.5.1.98. 2681.
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_111102. Signal Transduction.
Gene expression databases
ArrayExpress	Q96DB2.
Bgee	Q96DB2.
CleanEx	HS_HDAC11.
Genevestigator	Q96DB2.
GermOnline	ENSG00000163517. Homo sapiens.
Family and domain databases
Gene3D	3.40.800.20. 1 hit.
InterPro	IPR000286. His_deacetylse. IPR023801. His_deacetylse_dom. [Graphical view]
PANTHER	PTHR10625. PTHR10625. 1 hit.
Pfam	PF00850. Hist_deacetyl. 1 hit. [Graphical view]
PRINTS	PR01270. HDASUPER.
ProtoNet	Search...
Other
BindingDB	Q96DB2.
ChEMBL	CHEMBL3310.
GenomeRNAi	79885.
NextBio	69691.
SOURCE	Search...

Entry information

Entry name

HDA11_HUMAN

Accession

Primary (citable) accession number: Q96DB2
Secondary accession number(s): B4DDK1 , Q9H6I7, Q9H6X3, Q9NTC9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2002
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.