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Q969S8 (HDA10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 10

Short name=HD10
EC=3.5.1.98
Gene names
Name:HDAC10
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length669 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.

Catalytic activity

Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.

Subunit structure

Interacts with HDAC2, HDAC3 and NCOR2. Ref.1 Ref.4

Subcellular location

Cytoplasm. Nucleus. Note: Excluded from the nucleoli.

Tissue specificity

Ubiquitous. High expression in liver, spleen, pancreas and kidney.

Sequence similarities

Belongs to the histone deacetylase family. HD type 2 subfamily.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionChromatin regulator
Hydrolase
Repressor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNotch signaling pathway

Traceable author statement. Source: Reactome

chromatin modification

Non-traceable author statement Ref.1. Source: UniProtKB

histone deacetylation

Inferred from direct assay Ref.1Ref.4. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.2. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.2Ref.1. Source: UniProtKB

oligodendrocyte development

Inferred from electronic annotation. Source: Ensembl

protein deacetylation

Inferred from direct assay PubMed 17172643. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from direct assay Ref.1. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay Ref.2Ref.1. Source: UniProtKB

histone deacetylase complex

Inferred from direct assay Ref.1. Source: UniProtKB

nucleoplasm

Inferred from direct assay Ref.2. Source: UniProtKB

nucleus

Inferred from direct assay Ref.1Ref.4. Source: UniProtKB

   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

enzyme binding

Inferred from physical interaction Ref.1. Source: UniProtKB

histone deacetylase activity

Inferred from direct assay Ref.1Ref.4. Source: UniProtKB

histone deacetylase binding

Inferred from direct assay Ref.1. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 17172643. Source: UniProtKB

protein deacetylase activity

Inferred from direct assay PubMed 17172643. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q969S8-1)

Also known as: B; Alpha;

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: Q969S8-2)

Also known as: Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     252-271: Missing.
Isoform 4 (identifier: Q969S8-4)

Also known as: A;

The sequence of this isoform differs from the canonical sequence as follows:
     612-669: NSTPQLAGIL...MLQCHPHLVA → VSWAGWRCCG...GPGAEWRGTS
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 5 (identifier: Q969S8-5)

The sequence of this isoform differs from the canonical sequence as follows:
     252-301: Missing.
     447-669: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 669669Histone deacetylase 10
PRO_0000114712

Regions

Region1 – 323323Histone deacetylase

Sites

Active site1351 By similarity

Natural variations

Alternative sequence252 – 30150Missing in isoform 5.
VSP_014698
Alternative sequence252 – 27120Missing in isoform 2.
VSP_002089
Alternative sequence447 – 669223Missing in isoform 5.
VSP_014699
Alternative sequence612 – 66958NSTPQ…PHLVA → VSWAGWRCCGVGRGKGPVTA SVFAPGPELHTPASRDPGPG AEWRGTS in isoform 4.
VSP_002090
Natural variant4291V → I.
Corresponds to variant rs34402301 [ dbSNP | Ensembl ].
VAR_049356
Natural variant5841G → C. Ref.4
VAR_015067

Experimental info

Mutagenesis1351H → A: Abolishes deacetylase activity. Does not affect interaction with HDAC3. Ref.1 Ref.2
Sequence conflict921A → T in AAS48345. Ref.6
Sequence conflict1771Q → R in AAS48345. Ref.6
Sequence conflict3371Q → QRC in CAC21653. Ref.9
Sequence conflict5941A → T in AAK92205. Ref.3
Sequence conflict5941A → T in AAK92206. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (B) (Alpha) [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 872D9427E6893A18

FASTA66971,445
        10         20         30         40         50         60 
MGTALVYHED MTATRLLWDD PECEIERPER LTAALDRLRQ RGLEQRCLRL SAREASEEEL 

        70         80         90        100        110        120 
GLVHSPEYVS LVRETQVLGK EELQALSGQF DAIYFHPSTF HCARLAAGAG LQLVDAVLTG 

       130        140        150        160        170        180 
AVQNGLALVR PPGHHGQRAA ANGFCVFNNV AIAAAHAKQK HGLHRILVVD WDVHHGQGIQ 

       190        200        210        220        230        240 
YLFEDDPSVL YFSWHRYEHG RFWPFLRESD ADAVGRGQGL GFTVNLPWNQ VGMGNADYVA 

       250        260        270        280        290        300 
AFLHLLLPLA FEFDPELVLV SAGFDSAIGD PEGQMQATPE CFAHLTQLLQ VLAGGRVCAV 

       310        320        330        340        350        360 
LEGGYHLESL AESVCMTVQT LLGDPAPPLS GPMAPCQSAL ESIQSARAAQ APHWKSLQQQ 

       370        380        390        400        410        420 
DVTAVPMSPS SHSPEGRPPP LLPGGPVCKA AASAPSSLLD QPCLCPAPSV RTAVALTTPD 

       430        440        450        460        470        480 
ITLVLPPDVI QQEASALREE TEAWARPHES LAREEALTAL GKLLYLLDGM LDGQVNSGIA 

       490        500        510        520        530        540 
ATPASAAAAT LDVAVRRGLS HGAQRLLCVA LGQLDRPPDL AHDGRSLWLN IRGKEAAALS 

       550        560        570        580        590        600 
MFHVSTPLPV MTGGFLSCIL GLVLPLAYGF QPDLVLVALG PGHGLQGPHA ALLAAMLRGL 

       610        620        630        640        650        660 
AGGRVLALLE ENSTPQLAGI LARVLNGEAP PSLGPSSVAS PEDVQALMYL RGQLEPQWKM 


LQCHPHLVA 

« Hide

Isoform 2 (Beta) [UniParc].

Checksum: 7756351E6BC838FB
Show »

FASTA64969,385
Isoform 4 (A) [UniParc].

Checksum: 0EABDDA886585928
Show »

FASTA65870,033
Isoform 5 [UniParc].

Checksum: 22DE1D205E5856A0
Show »

FASTA39643,016

References

« Hide 'large scale' references
[1]"Identification of HDAC10, a novel class II human histone deacetylase containing a leucine-rich domain."
Tong J.J., Liu J., Bertos N.R., Yang X.-J.
Nucleic Acids Res. 30:1114-1123(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH HDAC3, MUTAGENESIS OF HIS-135.
Tissue: Fetal brain.
[2]"Molecular cloning and characterization of a novel histone deacetylase HDAC10."
Guardiola A.R., Yao T.-P.
J. Biol. Chem. 277:3350-3356(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), MUTAGENESIS OF HIS-135.
Tissue: Leukemia.
[3]"Isolation and characterization of mammalian HDAC10, a novel histone deacetylase."
Kao H.-Y., Lee C.-H., Komarov A., Han C.C., Evans R.M.
J. Biol. Chem. 277:187-193(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), CHARACTERIZATION.
Tissue: Hepatoma.
[4]"Isolation and characterization of a novel class II histone deacetylase, HDAC10."
Fischer D.D., Cai R., Bhatia U., Asselbergs F.A.M., Song C., Terry R., Trogani N., Widmer R., Atadja P., Cohen D.
J. Biol. Chem. 277:6656-6666(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH HDAC2 AND NCOR2, VARIANT CYS-584.
[5]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]Lin L., Li H., Zhou G., Shen C., Xiao W., Li M., Ke R., Yang S.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
[7]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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).
[9]"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 309-446.
Tissue: Amygdala.
[10]"An unappreciated role for RNA surveillance."
Hillman R.T., Green R.E., Brenner S.E.
Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF426160 mRNA. Translation: AAL30513.1.
AF393962 mRNA. Translation: AAK84023.1.
AF407272 mRNA. Translation: AAK92205.1.
AF407273 mRNA. Translation: AAK92206.1.
CR456465 mRNA. Translation: CAG30351.1.
AY450395 mRNA. Translation: AAS48345.1.
AL022328 Genomic DNA. No translation available.
BC125083 mRNA. Translation: AAI25084.1.
AL512711 mRNA. Translation: CAC21653.2.
CCDSCCDS14088.1. [Q969S8-1]
CCDS54545.1. [Q969S8-2]
RefSeqNP_001152758.1. NM_001159286.1. [Q969S8-2]
NP_114408.3. NM_032019.5. [Q969S8-1]
UniGeneHs.26593.

3D structure databases

ProteinModelPortalQ969S8.
SMRQ969S8. Positions 30-364.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123818. 22 interactions.
IntActQ969S8. 10 interactions.
STRING9606.ENSP00000216271.

Chemistry

BindingDBQ969S8.
ChEMBLCHEMBL2093865.
GuidetoPHARMACOLOGY2614.

PTM databases

PhosphoSiteQ969S8.

Polymorphism databases

DMDM27734403.

Proteomic databases

MaxQBQ969S8.
PaxDbQ969S8.
PRIDEQ969S8.

Protocols and materials databases

DNASU83933.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216271; ENSP00000216271; ENSG00000100429. [Q969S8-1]
ENST00000349505; ENSP00000343540; ENSG00000100429. [Q969S8-2]
ENST00000454936; ENSP00000406150; ENSG00000100429. [Q969S8-5]
GeneID83933.
KEGGhsa:83933.
UCSCuc003bkg.3. human. [Q969S8-1]
uc010hav.3. human. [Q969S8-2]

Organism-specific databases

CTD83933.
GeneCardsGC22M050683.
H-InvDBHIX0080289.
HGNCHGNC:18128. HDAC10.
HPACAB045977.
MIM608544. gene.
neXtProtNX_Q969S8.
PharmGKBPA38297.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0123.
HOVERGENHBG051892.
InParanoidQ969S8.
KOK11407.
OMAGLEQRCL.
OrthoDBEOG7992PT.
PhylomeDBQ969S8.
TreeFamTF106173.

Enzyme and pathway databases

BRENDA3.5.1.98. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
SABIO-RKQ969S8.

Gene expression databases

ArrayExpressQ969S8.
BgeeQ969S8.
CleanExHS_HDAC10.
GenevestigatorQ969S8.

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

ChiTaRSHDAC10. human.
GeneWikiHDAC10.
GenomeRNAi83933.
NextBio73053.
PROQ969S8.
SOURCESearch...

Entry information

Entry nameHDA10_HUMAN
AccessionPrimary (citable) accession number: Q969S8
Secondary accession number(s): Q08AP4 expand/collapse secondary AC list , Q6STF9, Q96P77, Q96P78, Q9H028, Q9UGX1, Q9UGX2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2003
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 117 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM