Reviewed, UniProtKB/Swiss-Prot Q969S8 (HDA10_HUMAN)

Names and origin

Protein names

Recommended name:
    Histone deacetylase 10
      Short name=HD10
    EC=3.5.1.98

Gene names

Name:

HDAC10

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	669 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.
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. Type 2 subfamily.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Chromatin regulator Hydrolase Repressor
Gene Ontology (GO)
Biological process	histone deacetylation Ref.1 Inferred from direct assay. Source: UniProtKB regulation of transcription, DNA-dependent Ref.1 Inferred from direct assay. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Ref.1 Inferred from direct assay. Source: UniProtKB histone deacetylase complex Ref.1 Inferred from direct assay. Source: UniProtKB
Molecular function	histone deacetylase activity Ref.1 Inferred from direct assay. Source: UniProtKB histone deacetylase binding Ref.1 Inferred from direct assay. Source: UniProtKB specific transcriptional repressor activity Ref.1 Inferred from direct assay. Source: UniProtKB zinc ion binding Ref.3 Traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HDAC2	Q92769	1	EBI-301762,EBI-301821
HDAC3	O15379	1	EBI-301762,EBI-607682
NCOR2	Q9Y618	1	EBI-301762,EBI-80830

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 669	669	Histone deacetylase 10		PRO_0000114712
Regions
	Region	1 – 323	323	Histone deacetylase
Sites
	Active site	135	1	By similarity
Natural variations
	Alternative sequence	252 – 301	50	Missing in isoform 5.		VSP_014698
	Alternative sequence	252 – 271	20	Missing in isoform 2.		VSP_002089
	Alternative sequence	447 – 669	223	Missing in isoform 5.		VSP_014699
	Alternative sequence	612 – 669	58	NSTPQ…PHLVA → VSWAGWRCCGVGRGKGPVTA SVFAPGPELHTPASRDPGPG AEWRGTS in isoform 4.		VSP_002090
	Natural variant	429	1	V → I: dbSNP rs34402301.		VAR_049356
	Natural variant	584	1	G → C Ref.4		VAR_015067
Experimental info
	Mutagenesis	135	1	H → A: Abolishes deacetylase activity. Does not affect interaction with HDAC3. Ref.1 Ref.2
	Sequence conflict	92	1	A → T in AAS48345. Ref.6
	Sequence conflict	177	1	Q → R in AAS48345. Ref.6
	Sequence conflict	337	1	Q → QRC in CAC21653. Ref.9
	Sequence conflict	337	1	Q → QRCEG Ref.7
	Sequence conflict	594	1	A → T in AAK92205. Ref.3
	Sequence conflict	594	1	A → T in AAK92206. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (B) (Alpha) [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 872D9427E6893A18	FASTA	669	71,445
	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
	Isoform 2 (Beta). Checksum: 7756351E6BC838FB	FASTA	649	69,385
	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 FEGQMQATPE CFAHLTQLLQ VLAGGRVCAV LEGGYHLESL AESVCMTVQT 310 320 330 340 350 360 LLGDPAPPLS GPMAPCQSAL ESIQSARAAQ APHWKSLQQQ DVTAVPMSPS SHSPEGRPPP 370 380 390 400 410 420 LLPGGPVCKA AASAPSSLLD QPCLCPAPSV RTAVALTTPD ITLVLPPDVI QQEASALREE 430 440 450 460 470 480 TEAWARPHES LAREEALTAL GKLLYLLDGM LDGQVNSGIA ATPASAAAAT LDVAVRRGLS 490 500 510 520 530 540 HGAQRLLCVA LGQLDRPPDL AHDGRSLWLN IRGKEAAALS MFHVSTPLPV MTGGFLSCIL 550 560 570 580 590 600 GLVLPLAYGF QPDLVLVALG PGHGLQGPHA ALLAAMLRGL AGGRVLALLE ENSTPQLAGI 610 620 630 640 LARVLNGEAP PSLGPSSVAS PEDVQALMYL RGQLEPQWKM LQCHPHLVA
	Isoform 4 (A). Checksum: 0EABDDA886585928	FASTA	658	70,033
	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 AGGRVLALLE EVSWAGWRCC GVGRGKGPVT ASVFAPGPEL HTPASRDPGP GAEWRGTS
	Isoform 5. Checksum: 22DE1D205E5856A0	FASTA	396	43,016
	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 FEGGYHLESL AESVCMTVQT LLGDPAPPLS GPMAPCQSAL ESIQSARAAQ 310 320 330 340 350 360 APHWKSLQQQ DVTAVPMSPS SHSPEGRPPP LLPGGPVCKA AASAPSSLLD QPCLCPAPSV 370 380 390 RTAVALTTPD ITLVLPPDVI QQEASALREE TEAWAR

References

	« Hide 'large scale' referencesShow '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: 11861901] [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: 11726666] [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: 11677242] [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: 11739383] [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:RESEARCH84.1-RESEARCH84.11(2004) [PubMed: 15461802] [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. , 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: 10591208] [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: 15489334] [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., 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 309-446. Tissue: Amygdala.
[10]	"An unappreciated role for RNA surveillance." Hillman R.T., Green R.E., Brenner S.E. Genome Biol. 5:RESEARCH008.1-RESEARCH008.16(2004) [PubMed: 14759258] [Abstract] Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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. Translation: CAB63048.1. BC125083 mRNA. Translation: AAI25084.1. AL512711 mRNA. Translation: CAC21653.2.
IPI	IPI00012439. IPI00216339. IPI00216341. IPI00879495.
RefSeq	NP_001152758.1. NP_114408.3.
UniGene	Hs.26593
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q969S8. 3 interactions.
Proteomic databases
PRIDE	Q969S8.
Genome annotation databases
Ensembl	ENSG00000100429. Homo sapiens. [Contig view]
GeneID	83933.
KEGG	hsa:83933.
Organism-specific databases
GeneCards	GC22M049025.
H-InvDB	HIX0017331. HIX0080289.
HGNC	HGNC:18128. HDAC10.
MIM	608544. gene.
PharmGKB	PA38297.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q969S8.
OMA	Q969S8. STFHCAR.
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	Q969S8.
Bgee	Q969S8.
CleanEx	HS_HDAC10.
GermOnline	ENSG00000100429. 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
NextBio	73053.
SOURCE	Search...

Entry information

Entry name

HDA10_HUMAN

Accession

Primary (citable) accession number: Q969S8
Secondary accession number(s): Q08AP4 , Q6STF9, Q96P77, Q96P78, Q9H028, Q9UGX1, Q9UGX2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2003
Last sequence update:	December 1, 2001
Last modified:	June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)