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Reviewed, UniProtKB/Swiss-Prot Q96DB2 (HDA11_HUMAN)

Last modified June 16, 2009. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Histone deacetylase 11
      Short name=HD11
    EC=3.5.1.98
Gene names
Name: HDAC11
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length347 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HDAC6Q9UBN71EBI-301713,EBI-301697

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 347347Histone deacetylase 11
PRO_0000114715

Regions

Region14 – 326313Histone deacetylase

Sites

Active site1431 By similarity

Experimental info

Sequence conflict151R → P in BAB15272. Ref.1
Sequence conflict1131P → A Ref.3
Sequence conflict2121D → Y in CAB70712. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q96DB2-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 0D976CAF6EAC7A15

FASTA34739,183
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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

AK025426 mRNA. Translation: BAB15127.1. Sequence problems.
AK025890 mRNA. Translation: BAB15272.1.
BC009676 mRNA. Translation: AAH09676.1.
AL137362 mRNA. Translation: CAB70712.1. Frameshift.
IPIIPI00304324.
RefSeqNP_079103.2.
UniGeneHs.661908

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ96DB2. 4 interactions.

Proteomic databases

PRIDEQ96DB2.

Genome annotation databases

EnsemblENSG00000163517. Homo sapiens. [Contig view]
GeneID79885.

Organism-specific databases

GeneCardsGC03P013496.
H-InvDBHIX0003075.
HGNCHGNC:19086. HDAC11.
MIM607226. gene.
PharmGKBPA38793.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ96DB2.
HOVERGENQ96DB2.
OMAQ96DB2. HTTQLYQ.

Enzyme and pathway databases

Pathway_Interaction_DBhdac_classi_pathway. Signaling events mediated by HDAC Class I.
hdac_classii_pathway. Signaling events mediated by HDAC Class II.
ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ96DB2.
BgeeQ96DB2.
CleanExHS_HDAC11.
GermOnlineENSG00000163517. Homo sapiens.

Family and domain databases

InterProIPR000286. His_deacetylse.
[Graphical view]
Gene3DG3DSA:3.40.800.20. His_deacetylse. 1 hit.
PANTHERPTHR10625. His_deacetylse. 1 hit.
PfamPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PRINTSPR01270. HDASUPER.
ProtoNetSearch...

Other Resources

BindingDBQ96DB2.
NextBio69691.
SOURCESearch...

Entry information

Entry nameHDA11_HUMAN
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents