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Q969S8

- HDA10_HUMAN

UniProt

Q969S8 - HDA10_HUMAN

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Protein

Histone deacetylase 10

Gene

HDAC10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei135 – 1351By similarity

GO - Molecular functioni

  1. enzyme binding Source: UniProtKB
  2. histone deacetylase activity Source: UniProtKB
  3. histone deacetylase binding Source: UniProtKB
  4. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
  5. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB-EC
  6. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB-EC
  7. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB-EC
  8. protein deacetylase activity Source: UniProtKB

GO - Biological processi

  1. chromatin modification Source: UniProtKB
  2. histone deacetylation Source: UniProtKB
  3. negative regulation of transcription, DNA-templated Source: UniProtKB
  4. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  5. Notch signaling pathway Source: Reactome
  6. oligodendrocyte development Source: Ensembl
  7. protein deacetylation Source: UniProtKB
  8. regulation of transcription, DNA-templated Source: UniProtKB
  9. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Hydrolase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BRENDAi3.5.1.98. 2681.
ReactomeiREACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
SABIO-RKQ969S8.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase 10 (EC:3.5.1.98)
Short name:
HD10
Gene namesi
Name:HDAC10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:18128. HDAC10.

Subcellular locationi

Cytoplasm. Nucleus
Note: Excluded from the nucleoli.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. histone deacetylase complex Source: UniProtKB
  3. nucleoplasm Source: UniProtKB
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi135 – 1351H → A: Abolishes deacetylase activity. Does not affect interaction with HDAC3. 2 Publications

Organism-specific databases

PharmGKBiPA38297.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 669669Histone deacetylase 10PRO_0000114712Add
BLAST

Proteomic databases

MaxQBiQ969S8.
PaxDbiQ969S8.
PRIDEiQ969S8.

PTM databases

PhosphoSiteiQ969S8.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ969S8.
CleanExiHS_HDAC10.
ExpressionAtlasiQ969S8. baseline and differential.
GenevestigatoriQ969S8.

Organism-specific databases

HPAiCAB045977.

Interactioni

Subunit structurei

Interacts with HDAC2, HDAC3 and NCOR2.2 Publications

Protein-protein interaction databases

BioGridi123818. 22 interactions.
IntActiQ969S8. 10 interactions.
STRINGi9606.ENSP00000216271.

Structurei

3D structure databases

ProteinModelPortaliQ969S8.
SMRiQ969S8. Positions 30-364.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 323323Histone deacetylaseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0123.
GeneTreeiENSGT00530000062809.
HOVERGENiHBG051892.
InParanoidiQ969S8.
KOiK11407.
OMAiGLEQRCL.
OrthoDBiEOG7992PT.
PhylomeDBiQ969S8.
TreeFamiTF106173.

Family and domain databases

Gene3Di3.40.800.20. 1 hit.
InterProiIPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERiPTHR10625. PTHR10625. 1 hit.
PfamiPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PRINTSiPR01270. HDASUPER.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q969S8-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MGTALVYHED MTATRLLWDD PECEIERPER LTAALDRLRQ RGLEQRCLRL
60 70 80 90 100
SAREASEEEL GLVHSPEYVS LVRETQVLGK EELQALSGQF DAIYFHPSTF
110 120 130 140 150
HCARLAAGAG LQLVDAVLTG AVQNGLALVR PPGHHGQRAA ANGFCVFNNV
160 170 180 190 200
AIAAAHAKQK HGLHRILVVD WDVHHGQGIQ YLFEDDPSVL YFSWHRYEHG
210 220 230 240 250
RFWPFLRESD ADAVGRGQGL GFTVNLPWNQ VGMGNADYVA AFLHLLLPLA
260 270 280 290 300
FEFDPELVLV SAGFDSAIGD PEGQMQATPE CFAHLTQLLQ VLAGGRVCAV
310 320 330 340 350
LEGGYHLESL AESVCMTVQT LLGDPAPPLS GPMAPCQSAL ESIQSARAAQ
360 370 380 390 400
APHWKSLQQQ DVTAVPMSPS SHSPEGRPPP LLPGGPVCKA AASAPSSLLD
410 420 430 440 450
QPCLCPAPSV RTAVALTTPD ITLVLPPDVI QQEASALREE TEAWARPHES
460 470 480 490 500
LAREEALTAL GKLLYLLDGM LDGQVNSGIA ATPASAAAAT LDVAVRRGLS
510 520 530 540 550
HGAQRLLCVA LGQLDRPPDL AHDGRSLWLN IRGKEAAALS MFHVSTPLPV
560 570 580 590 600
MTGGFLSCIL GLVLPLAYGF QPDLVLVALG PGHGLQGPHA ALLAAMLRGL
610 620 630 640 650
AGGRVLALLE ENSTPQLAGI LARVLNGEAP PSLGPSSVAS PEDVQALMYL
660
RGQLEPQWKM LQCHPHLVA
Length:669
Mass (Da):71,445
Last modified:December 1, 2001 - v1
Checksum:i872D9427E6893A18
GO
Isoform 2 (identifier: Q969S8-2) [UniParc]FASTAAdd to Basket

Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     252-271: Missing.

Show »
Length:649
Mass (Da):69,385
Checksum:i7756351E6BC838FB
GO
Isoform 4 (identifier: Q969S8-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:658
Mass (Da):70,033
Checksum:i0EABDDA886585928
GO
Isoform 5 (identifier: Q969S8-5) [UniParc]FASTAAdd to Basket

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

Show »
Length:396
Mass (Da):43,016
Checksum:i22DE1D205E5856A0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti92 – 921A → T in AAS48345. 1 PublicationCurated
Sequence conflicti177 – 1771Q → R in AAS48345. 1 PublicationCurated
Sequence conflicti337 – 3371Q → QRC in CAC21653. (PubMed:17974005)Curated
Sequence conflicti594 – 5941A → T in AAK92205. (PubMed:11677242)Curated
Sequence conflicti594 – 5941A → T in AAK92206. (PubMed:11677242)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti429 – 4291V → I.
Corresponds to variant rs34402301 [ dbSNP | Ensembl ].
VAR_049356
Natural varianti584 – 5841G → C.1 Publication
VAR_015067

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei252 – 30150Missing in isoform 5. 1 PublicationVSP_014698Add
BLAST
Alternative sequencei252 – 27120Missing in isoform 2. 1 PublicationVSP_002089Add
BLAST
Alternative sequencei447 – 669223Missing in isoform 5. 1 PublicationVSP_014699Add
BLAST
Alternative sequencei612 – 66958NSTPQ…PHLVA → VSWAGWRCCGVGRGKGPVTA SVFAPGPELHTPASRDPGPG AEWRGTS in isoform 4. 2 PublicationsVSP_002090Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS14088.1. [Q969S8-1]
CCDS54545.1. [Q969S8-2]
RefSeqiNP_001152758.1. NM_001159286.1. [Q969S8-2]
NP_114408.3. NM_032019.5. [Q969S8-1]
UniGeneiHs.26593.

Genome annotation databases

EnsembliENST00000216271; ENSP00000216271; ENSG00000100429. [Q969S8-1]
ENST00000349505; ENSP00000343540; ENSG00000100429. [Q969S8-2]
ENST00000454936; ENSP00000406150; ENSG00000100429. [Q969S8-5]
GeneIDi83933.
KEGGihsa:83933.
UCSCiuc003bkg.3. human. [Q969S8-1]
uc010hav.3. human. [Q969S8-2]

Polymorphism databases

DMDMi27734403.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS14088.1. [Q969S8-1 ]
CCDS54545.1. [Q969S8-2 ]
RefSeqi NP_001152758.1. NM_001159286.1. [Q969S8-2 ]
NP_114408.3. NM_032019.5. [Q969S8-1 ]
UniGenei Hs.26593.

3D structure databases

ProteinModelPortali Q969S8.
SMRi Q969S8. Positions 30-364.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123818. 22 interactions.
IntActi Q969S8. 10 interactions.
STRINGi 9606.ENSP00000216271.

Chemistry

BindingDBi Q969S8.
ChEMBLi CHEMBL2093865.
GuidetoPHARMACOLOGYi 2614.

PTM databases

PhosphoSitei Q969S8.

Polymorphism databases

DMDMi 27734403.

Proteomic databases

MaxQBi Q969S8.
PaxDbi Q969S8.
PRIDEi Q969S8.

Protocols and materials databases

DNASUi 83933.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000216271 ; ENSP00000216271 ; ENSG00000100429 . [Q969S8-1 ]
ENST00000349505 ; ENSP00000343540 ; ENSG00000100429 . [Q969S8-2 ]
ENST00000454936 ; ENSP00000406150 ; ENSG00000100429 . [Q969S8-5 ]
GeneIDi 83933.
KEGGi hsa:83933.
UCSCi uc003bkg.3. human. [Q969S8-1 ]
uc010hav.3. human. [Q969S8-2 ]

Organism-specific databases

CTDi 83933.
GeneCardsi GC22M050683.
H-InvDB HIX0080289.
HGNCi HGNC:18128. HDAC10.
HPAi CAB045977.
MIMi 608544. gene.
neXtProti NX_Q969S8.
PharmGKBi PA38297.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0123.
GeneTreei ENSGT00530000062809.
HOVERGENi HBG051892.
InParanoidi Q969S8.
KOi K11407.
OMAi GLEQRCL.
OrthoDBi EOG7992PT.
PhylomeDBi Q969S8.
TreeFami TF106173.

Enzyme and pathway databases

BRENDAi 3.5.1.98. 2681.
Reactomei REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
SABIO-RK Q969S8.

Miscellaneous databases

ChiTaRSi HDAC10. human.
GeneWikii HDAC10.
GenomeRNAii 83933.
NextBioi 73053.
PROi Q969S8.
SOURCEi Search...

Gene expression databases

Bgeei Q969S8.
CleanExi HS_HDAC10.
ExpressionAtlasi Q969S8. baseline and differential.
Genevestigatori Q969S8.

Family and domain databases

Gene3Di 3.40.800.20. 1 hit.
InterProi IPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
[Graphical view ]
PANTHERi PTHR10625. PTHR10625. 1 hit.
Pfami PF00850. Hist_deacetyl. 1 hit.
[Graphical view ]
PRINTSi PR01270. HDASUPER.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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] [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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 309-446.
    Tissue: Amygdala.
  10. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).

Entry informationi

Entry nameiHDA10_HUMAN
AccessioniPrimary (citable) accession number: Q969S8
Secondary accession number(s): Q08AP4
, Q6STF9, Q96P77, Q96P78, Q9H028, Q9UGX1, Q9UGX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2003
Last sequence update: December 1, 2001
Last modified: October 29, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3