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Q96DB2 (HDA11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone deacetylase 11

Short name=HD11
EC=3.5.1.98
Gene names
Name:HDAC11
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length347 AA.
Sequence statusComplete.
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.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 processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   Molecular functionChromatin regulator
Hydrolase
Repressor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin modification

Traceable author statement PubMed 12711221. Source: UniProtKB

histone deacetylation

Inferred from direct assay Ref.5. Source: UniProtKB

oligodendrocyte development

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthistone deacetylase complex

Inferred from direct assay Ref.5. Source: UniProtKB

nucleus

Inferred from direct assay Ref.5. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: LIFEdb

   Molecular_functionNAD-dependent histone deacetylase activity (H3-K14 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H3-K18 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H3-K9 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H4-K16 specific)

Inferred from electronic annotation. Source: UniProtKB-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 347347Histone deacetylase 11
PRO_0000114715

Regions

Region14 – 326313Histone deacetylase

Sites

Active site1431 By similarity

Natural variations

Alternative sequence1 – 2828Missing in isoform 2.
VSP_043082
Alternative sequence85 – 10723Missing in isoform 2.
VSP_043083

Experimental info

Sequence conflict151R → P in BAB15272. Ref.1
Sequence conflict1131P → A in CAB70712. Ref.4
Sequence conflict2121D → Y in CAB70712. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 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

Isoform 2 [UniParc].

Checksum: 60C0E21BA00DF261
Show »

FASTA29633,124

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] [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. expand/collapse author list , 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.
CCDSCCDS2615.1. [Q96DB2-1]
CCDS46760.1. [Q96DB2-2]
RefSeqNP_001129513.1. NM_001136041.2. [Q96DB2-2]
NP_079103.2. NM_024827.3. [Q96DB2-1]
UniGeneHs.744132.

3D structure databases

ProteinModelPortalQ96DB2.
SMRQ96DB2. Positions 19-333.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122970. 134 interactions.
IntActQ96DB2. 129 interactions.
MINTMINT-1411829.
STRING9606.ENSP00000295757.

Chemistry

BindingDBQ96DB2.
ChEMBLCHEMBL2093865.
GuidetoPHARMACOLOGY2615.

PTM databases

PhosphoSiteQ96DB2.

Polymorphism databases

DMDM26394832.

Proteomic databases

PaxDbQ96DB2.
PRIDEQ96DB2.

Protocols and materials databases

DNASU79885.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295757; ENSP00000295757; ENSG00000163517. [Q96DB2-1]
ENST00000522202; ENSP00000429794; ENSG00000163517. [Q96DB2-2]
GeneID79885.
KEGGhsa:79885.
UCSCuc003bxy.3. human. [Q96DB2-1]
uc011auy.2. human. [Q96DB2-2]

Organism-specific databases

CTD79885.
GeneCardsGC03P013496.
HGNCHGNC:19086. HDAC11.
MIM607226. gene.
neXtProtNX_Q96DB2.
PharmGKBPA38793.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0123.
HOGENOMHOG000280018.
HOVERGENHBG051893.
InParanoidQ96DB2.
KOK11418.
OMADIIVYNA.
PhylomeDBQ96DB2.
TreeFamTF106176.

Enzyme and pathway databases

BRENDA3.5.1.98. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.

Gene expression databases

ArrayExpressQ96DB2.
BgeeQ96DB2.
CleanExHS_HDAC11.
GenevestigatorQ96DB2.

Family and domain databases

Gene3D3.40.800.20. 1 hit.
InterProIPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERPTHR10625. PTHR10625. 1 hit.
PfamPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PRINTSPR01270. HDASUPER.
ProtoNetSearch...

Other

GeneWikiHDAC11.
GenomeRNAi79885.
NextBio69691.
PROQ96DB2.
SOURCESearch...

Entry information

Entry nameHDA11_HUMAN
AccessionPrimary (citable) accession number: Q96DB2
Secondary accession number(s): B4DDK1 expand/collapse secondary AC list , Q9H6I7, Q9H6X3, Q9NTC9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human chromosome 3

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