GenomeNet

Database: UniProt/SWISS-PROT
Entry: HDA10_HUMAN
LinkDB: HDA10_HUMAN
Original site: HDA10_HUMAN 
ID   HDA10_HUMAN             Reviewed;         669 AA.
AC   Q969S8; Q08AP4; Q6STF9; Q96P77; Q96P78; Q9H028; Q9UGX1; Q9UGX2;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   13-FEB-2019, entry version 154.
DE   RecName: Full=Polyamine deacetylase HDAC10;
DE            EC=3.5.1.48 {ECO:0000269|PubMed:28516954};
DE            EC=3.5.1.62 {ECO:0000269|PubMed:28516954};
DE   AltName: Full=Histone deacetylase 10;
DE            Short=HD10;
GN   Name=HDAC10;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
RP   HDAC3, MUTAGENESIS OF HIS-135, TISSUE SPECIFICITY, INHIBITION BY TSA,
RP   AND SUBCELLULAR LOCATION.
RC   TISSUE=Bone marrow;
RX   PubMed=11861901; DOI=10.1093/nar/30.5.1114;
RA   Tong J.J., Liu J., Bertos N.R., Yang X.-J.;
RT   "Identification of HDAC10, a novel class II human histone deacetylase
RT   containing a leucine-rich domain.";
RL   Nucleic Acids Res. 30:1114-1123(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP   LOCATION, INHIBITION BY TSA, AND MUTAGENESIS OF HIS-135.
RC   TISSUE=Leukemia;
RX   PubMed=11726666; DOI=10.1074/jbc.M109861200;
RA   Guardiola A.R., Yao T.-P.;
RT   "Molecular cloning and characterization of a novel histone deacetylase
RT   HDAC10.";
RL   J. Biol. Chem. 277:3350-3356(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Hepatoma;
RX   PubMed=11677242; DOI=10.1074/jbc.M108931200;
RA   Kao H.-Y., Lee C.-H., Komarov A., Han C.C., Evans R.M.;
RT   "Isolation and characterization of mammalian HDAC10, a novel histone
RT   deacetylase.";
RL   J. Biol. Chem. 277:187-193(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), FUNCTION, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH HDAC2 AND NCOR2.
RX   PubMed=11739383; DOI=10.1074/jbc.M108055200;
RA   Fischer D.D., Cai R., Bhatia U., Asselbergs F.A.M., Song C., Terry R.,
RA   Trogani N., Widmer R., Atadja P., Cohen D.;
RT   "Isolation and characterization of a novel class II histone
RT   deacetylase, HDAC10.";
RL   J. Biol. Chem. 277:6656-6666(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA   Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA   Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA   Beare D.M., Dunham I.;
RT   "A genome annotation-driven approach to cloning the human ORFeome.";
RL   Genome Biol. 5:R84.1-R84.11(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RA   Lin L., Li H., Zhou G., Shen C., Xiao W., Li M., Ke R., Yang S.;
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA   Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA   Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA   Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA   Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA   Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA   Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA   Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA   Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA   Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA   Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA   Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA   Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA   Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA   Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA   Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA   Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA   Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA   Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA   Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA   Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA   Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA   Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA   Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA   Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA   Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA   Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA   Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA   Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA   Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA   Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA   Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA   O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA   Khan A.S., Lane L., Tilahun Y., Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 309-446.
RC   TISSUE=Amygdala;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [10]
RP   SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX   PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA   Hillman R.T., Green R.E., Brenner S.E.;
RT   "An unappreciated role for RNA surveillance.";
RL   Genome Biol. 5:R8.1-R8.16(2004).
RN   [11]
RP   FUNCTION.
RX   PubMed=21247901; DOI=10.1074/jbc.C110.194233;
RA   Kotian S., Liyanarachchi S., Zelent A., Parvin J.D.;
RT   "Histone deacetylases 9 and 10 are required for homologous
RT   recombination.";
RL   J. Biol. Chem. 286:7722-7726(2011).
RN   [12]
RP   FUNCTION, INTERACTION WITH HSPA8, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP   HIS-135, AND INVOLVEMENT IN RESISTANCE TO CHEMOTHERAPEUTICS.
RX   PubMed=23801752; DOI=10.1073/pnas.1300113110;
RA   Oehme I., Linke J.P., Boeck B.C., Milde T., Lodrini M.,
RA   Hartenstein B., Wiegand I., Eckert C., Roth W., Kool M., Kaden S.,
RA   Groene H.J., Schulte J.H., Lindner S., Hamacher-Brady A., Brady N.R.,
RA   Deubzer H.E., Witt O.;
RT   "Histone deacetylase 10 promotes autophagy-mediated cell survival.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:E2592-E2601(2013).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [14]
RP   FUNCTION, AND INTERACTION WITH MSH2.
RX   PubMed=26221039; DOI=10.1074/jbc.M114.612945;
RA   Radhakrishnan R., Li Y., Xiang S., Yuan F., Yuan Z., Telles E.,
RA   Fang J., Coppola D., Shibata D., Lane W.S., Zhang Y., Zhang X.,
RA   Seto E.;
RT   "Histone deacetylase 10 regulates DNA mismatch repair and may involve
RT   the deacetylation of MutS homolog 2.";
RL   J. Biol. Chem. 290:22795-22804(2015).
RN   [15]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=28516954; DOI=10.1038/ncomms15368;
RA   Hai Y., Shinsky S.A., Porter N.J., Christianson D.W.;
RT   "Histone deacetylase 10 structure and molecular function as a
RT   polyamine deacetylase.";
RL   Nat. Commun. 8:15368-15368(2017).
RN   [16]
RP   FUNCTION, AND INVOLVEMENT IN RESISTANCE TO CHEMOTHERAPEUTICS.
RX   PubMed=29968769; DOI=10.1038/s41598-018-28265-5;
RA   Ridinger J., Koeneke E., Kolbinger F.R., Koerholz K., Mahboobi S.,
RA   Hellweg L., Gunkel N., Miller A.K., Peterziel H., Schmezer P.,
RA   Hamacher-Brady A., Witt O., Oehme I.;
RT   "Dual role of HDAC10 in lysosomal exocytosis and DNA repair promotes
RT   neuroblastoma chemoresistance.";
RL   Sci. Rep. 8:10039-10039(2018).
CC   -!- FUNCTION: Polyamine deacetylase (PDAC), which acts preferentially
CC       on N(8)-acetylspermidine, and also on acetylcadaverine and
CC       acetylputrescine (PubMed:28516954). Exhibits attenuated catalytic
CC       activity toward N(1),N(8)-diacetylspermidine and very low
CC       activity, if any, toward N(1)-acetylspermidine (PubMed:28516954).
CC       Histone deacetylase activity has been observed in vitro
CC       (PubMed:11861901, PubMed:11726666, PubMed:11677242,
CC       PubMed:11739383). Has also been shown to be involved in MSH2
CC       deacetylation (PubMed:26221039). The physiological relevance of
CC       protein/histone deacetylase activity is unclear and could be very
CC       weak (PubMed:28516954). May play a role in the promotion of late
CC       stages of autophagy, possibly autophagosome-lysosome fusion and/or
CC       lysosomal exocytosis in neuroblastoma cells (PubMed:23801752,
CC       PubMed:29968769). May play a role in homologous recombination
CC       (PubMed:21247901). May promote DNA mismatch repair
CC       (PubMed:26221039). {ECO:0000269|PubMed:11677242,
CC       ECO:0000269|PubMed:11726666, ECO:0000269|PubMed:11739383,
CC       ECO:0000269|PubMed:11861901, ECO:0000269|PubMed:21247901,
CC       ECO:0000269|PubMed:23801752, ECO:0000269|PubMed:26221039,
CC       ECO:0000269|PubMed:28516954, ECO:0000269|PubMed:29968769}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(8)-acetylspermidine = acetate + spermidine;
CC         Xref=Rhea:RHEA:23928, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:57834, ChEBI:CHEBI:58535; EC=3.5.1.48;
CC         Evidence={ECO:0000269|PubMed:28516954};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-acetylputrescine = acetate + putrescine;
CC         Xref=Rhea:RHEA:23412, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:58263, ChEBI:CHEBI:326268; EC=3.5.1.62;
CC         Evidence={ECO:0000269|PubMed:28516954};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-acetylcadaverine = acetate + cadaverine;
CC         Xref=Rhea:RHEA:51892, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:58384, ChEBI:CHEBI:134408;
CC         Evidence={ECO:0000269|PubMed:28516954};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] = acetate + L-lysyl-
CC         [protein]; Xref=Rhea:RHEA:58108, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC         COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:61930;
CC         Evidence={ECO:0000269|PubMed:11677242,
CC         ECO:0000269|PubMed:11726666, ECO:0000269|PubMed:11739383,
CC         ECO:0000269|PubMed:11861901, ECO:0000269|PubMed:26221039};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=110 uM for acetylcadaverine {ECO:0000269|PubMed:28516954};
CC         KM=170 uM for acetylputrescine {ECO:0000269|PubMed:28516954};
CC         KM=100 uM for N(8)-acetylspermidine
CC         {ECO:0000269|PubMed:28516954};
CC         KM=180 uM for N(1)-acetylspermine {ECO:0000269|PubMed:28516954};
CC         KM=150 uM for N(1),N(8)-diacetylspermidine
CC         {ECO:0000269|PubMed:28516954};
CC   -!- SUBUNIT: Interacts with HDAC3 (PubMed:11861901). Interacts with
CC       HDAC2 and NCOR2/SMRT (PubMed:11739383). Interacts with HSPA8/HSC70
CC       (PubMed:23801752). Interacts with MSH2 (PubMed:26221039).
CC       {ECO:0000269|PubMed:11739383, ECO:0000269|PubMed:11861901,
CC       ECO:0000269|PubMed:23801752, ECO:0000269|PubMed:26221039}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11677242,
CC       ECO:0000269|PubMed:11726666, ECO:0000269|PubMed:11739383,
CC       ECO:0000269|PubMed:11861901, ECO:0000269|PubMed:23801752}. Nucleus
CC       {ECO:0000269|PubMed:11677242, ECO:0000269|PubMed:11726666,
CC       ECO:0000269|PubMed:11739383, ECO:0000269|PubMed:11861901}.
CC       Note=Excluded from nucleoli. {ECO:0000269|PubMed:11726666}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=Alpha {ECO:0000303|PubMed:11677242}, HDAC10b
CC       {ECO:0000303|PubMed:11726666}, HDAC10v1
CC       {ECO:0000303|PubMed:11739383};
CC         IsoId=Q969S8-1; Sequence=Displayed;
CC       Name=2; Synonyms=Beta {ECO:0000303|PubMed:11677242};
CC         IsoId=Q969S8-2; Sequence=VSP_002089;
CC       Name=4; Synonyms=A, HDAC10v2 {ECO:0000303|PubMed:11739383};
CC         IsoId=Q969S8-4; Sequence=VSP_002090;
CC         Note=May be produced at very low levels due to a premature stop
CC         codon in the mRNA, leading to nonsense-mediated mRNA decay.;
CC       Name=5;
CC         IsoId=Q969S8-5; Sequence=VSP_014698, VSP_014699;
CC   -!- TISSUE SPECIFICITY: Widely expressed with high levels in liver and
CC       kidney. {ECO:0000269|PubMed:11677242, ECO:0000269|PubMed:11739383,
CC       ECO:0000269|PubMed:11861901}.
CC   -!- DISEASE: Note=In neuroblastoma cells, may promote autophagy in
CC       response to chemotherapy-induced DNA damage and efflux of
CC       chemotherapeutics via lysosomal exocytosis, hence protecting cells
CC       from cytotoxic agents (PubMed:23801752, PubMed:29968769).
CC       Expression levels may correlate with survival in neuroblastoma
CC       patients, with low levels in the tumor correlating with long-term
CC       patient survival and high expression with poor prognosis
CC       (PubMed:23801752). Therefore has been proposed as a biomarker to
CC       predict neuroblastoma chemoresistance and treatment outcome
CC       (PubMed:23801752). {ECO:0000269|PubMed:23801752,
CC       ECO:0000269|PubMed:29968769, ECO:0000303|PubMed:23801752}.
CC   -!- MISCELLANEOUS: Like some other members of the HD type 2 subfamily,
CC       such as HDAC4, inhibited by the antitumor drug trichostatin A
CC       (TSA). {ECO:0000269|PubMed:11861901}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: Protein/histone deacetylase activity in vivo is
CC       uncertain. The 3D structure analysis of the zebrafish ortholog
CC       shows that a glutamate gatekeeper and a sterically constricted
CC       active site confer specificity for N(8)-acetylspermidine
CC       hydrolysis and disfavour acetyllysine hydrolysis. Supporting this
CC       observation, has been shown to exhibit only very low activity, if
CC       any, towards acetyl-lysine peptide substrates (PubMed:28516954).
CC       However, histone deacetylase activity has been observed in vitro
CC       (PubMed:28516954, PubMed:11861901, PubMed:11726666,
CC       PubMed:11677242, PubMed:11739383). Has also been shown to be
CC       involved in MSH2 deacetylation (PubMed:26221039).
CC       {ECO:0000269|PubMed:11677242, ECO:0000269|PubMed:11726666,
CC       ECO:0000269|PubMed:11739383, ECO:0000269|PubMed:11861901,
CC       ECO:0000269|PubMed:26221039, ECO:0000269|PubMed:28516954}.
DR   EMBL; AF426160; AAL30513.1; -; mRNA.
DR   EMBL; AF393962; AAK84023.1; -; mRNA.
DR   EMBL; AF407272; AAK92205.1; -; mRNA.
DR   EMBL; AF407273; AAK92206.1; -; mRNA.
DR   EMBL; CR456465; CAG30351.1; -; mRNA.
DR   EMBL; AY450395; AAS48345.1; -; mRNA.
DR   EMBL; AL022328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC125083; AAI25084.1; -; mRNA.
DR   EMBL; AL512711; CAC21653.2; -; mRNA.
DR   CCDS; CCDS14088.1; -. [Q969S8-1]
DR   CCDS; CCDS54545.1; -. [Q969S8-2]
DR   RefSeq; NP_001152758.1; NM_001159286.1. [Q969S8-2]
DR   RefSeq; NP_114408.3; NM_032019.5. [Q969S8-1]
DR   UniGene; Hs.26593; -.
DR   ProteinModelPortal; Q969S8; -.
DR   SMR; Q969S8; -.
DR   BioGrid; 123818; 39.
DR   CORUM; Q969S8; -.
DR   IntAct; Q969S8; 11.
DR   STRING; 9606.ENSP00000216271; -.
DR   BindingDB; Q969S8; -.
DR   ChEMBL; CHEMBL5103; -.
DR   DrugBank; DB05015; Belinostat.
DR   DrugBank; DB06603; Panobinostat.
DR   GuidetoPHARMACOLOGY; 2614; -.
DR   iPTMnet; Q969S8; -.
DR   PhosphoSitePlus; Q969S8; -.
DR   BioMuta; HDAC10; -.
DR   DMDM; 27734403; -.
DR   EPD; Q969S8; -.
DR   jPOST; Q969S8; -.
DR   MaxQB; Q969S8; -.
DR   PaxDb; Q969S8; -.
DR   PeptideAtlas; Q969S8; -.
DR   PRIDE; Q969S8; -.
DR   ProteomicsDB; 75833; -.
DR   ProteomicsDB; 75834; -. [Q969S8-2]
DR   ProteomicsDB; 75835; -. [Q969S8-4]
DR   ProteomicsDB; 75836; -. [Q969S8-5]
DR   DNASU; 83933; -.
DR   Ensembl; ENST00000216271; ENSP00000216271; ENSG00000100429. [Q969S8-1]
DR   Ensembl; ENST00000349505; ENSP00000343540; ENSG00000100429. [Q969S8-2]
DR   Ensembl; ENST00000454936; ENSP00000406150; ENSG00000100429. [Q969S8-5]
DR   GeneID; 83933; -.
DR   KEGG; hsa:83933; -.
DR   UCSC; uc003bkg.4; human. [Q969S8-1]
DR   CTD; 83933; -.
DR   DisGeNET; 83933; -.
DR   EuPathDB; HostDB:ENSG00000100429.17; -.
DR   GeneCards; HDAC10; -.
DR   H-InvDB; HIX0080289; -.
DR   HGNC; HGNC:18128; HDAC10.
DR   HPA; CAB045977; -.
DR   HPA; HPA056514; -.
DR   MIM; 608544; gene.
DR   neXtProt; NX_Q969S8; -.
DR   OpenTargets; ENSG00000100429; -.
DR   PharmGKB; PA38297; -.
DR   eggNOG; KOG1343; Eukaryota.
DR   eggNOG; COG0123; LUCA.
DR   GeneTree; ENSGT00940000160061; -.
DR   HOVERGEN; HBG051892; -.
DR   InParanoid; Q969S8; -.
DR   KO; K18671; -.
DR   OMA; LSQSVCM; -.
DR   OrthoDB; 1484694at2759; -.
DR   PhylomeDB; Q969S8; -.
DR   TreeFam; TF106173; -.
DR   BRENDA; 3.5.1.98; 2681.
DR   Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR   Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
DR   Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
DR   Reactome; R-HSA-3214815; HDACs deacetylate histones.
DR   SABIO-RK; Q969S8; -.
DR   SIGNOR; Q969S8; -.
DR   ChiTaRS; HDAC10; human.
DR   GeneWiki; HDAC10; -.
DR   GenomeRNAi; 83933; -.
DR   PRO; PR:Q969S8; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   Bgee; ENSG00000100429; Expressed in 157 organ(s), highest expression level in pituitary gland.
DR   ExpressionAtlas; Q969S8; baseline and differential.
DR   Genevisible; Q969S8; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0000118; C:histone deacetylase complex; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0047609; F:acetylputrescine deacetylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047611; F:acetylspermidine deacetylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019213; F:deacetylase activity; IDA:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0004407; F:histone deacetylase activity; IDA:UniProtKB.
DR   GO; GO:0042826; F:histone deacetylase binding; IDA:UniProtKB.
DR   GO; GO:0033558; F:protein deacetylase activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0006325; P:chromatin organization; NAS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0016575; P:histone deacetylation; IDA:UniProtKB.
DR   GO; GO:0035825; P:homologous recombination; IMP:UniProtKB.
DR   GO; GO:0016236; P:macroautophagy; IMP:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0014003; P:oligodendrocyte development; IEA:Ensembl.
DR   GO; GO:0034983; P:peptidyl-lysine deacetylation; IDA:UniProtKB.
DR   GO; GO:0106047; P:polyamine deacetylation; IDA:UniProtKB.
DR   GO; GO:0032425; P:positive regulation of mismatch repair; IDA:UniProtKB.
DR   GO; GO:0006476; P:protein deacetylation; IDA:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0106048; P:spermidine deacetylation; IDA:UniProtKB.
DR   Gene3D; 3.40.800.20; -; 2.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   PANTHER; PTHR10625; PTHR10625; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52768; SSF52768; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Autophagy; Complete proteome; Cytoplasm;
KW   DNA damage; DNA recombination; DNA repair; Hydrolase; Metal-binding;
KW   Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Zinc.
FT   CHAIN         1    669       Polyamine deacetylase HDAC10.
FT                                /FTId=PRO_0000114712.
FT   REGION        1    323       Histone deacetylase.
FT   MOTIF        21     24       Substrate specificity.
FT                                {ECO:0000250|UniProtKB:F1QCV2}.
FT   ACT_SITE    135    135       Proton donor/acceptor.
FT                                {ECO:0000250|UniProtKB:F1QCV2}.
FT   METAL       172    172       Zinc. {ECO:0000250|UniProtKB:F1QCV2}.
FT   METAL       174    174       Zinc; via pros nitrogen.
FT                                {ECO:0000250|UniProtKB:F1QCV2}.
FT   METAL       265    265       Zinc. {ECO:0000250|UniProtKB:F1QCV2}.
FT   BINDING      20     20       Substrate.
FT                                {ECO:0000250|UniProtKB:F1QCV2}.
FT   BINDING     305    305       Substrate.
FT                                {ECO:0000250|UniProtKB:F1QCV2}.
FT   SITE        272    272       Substrate specificity.
FT                                {ECO:0000250|UniProtKB:F1QCV2}.
FT   MOD_RES     393    393       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   VAR_SEQ     252    301       Missing (in isoform 5).
FT                                {ECO:0000303|Ref.6}.
FT                                /FTId=VSP_014698.
FT   VAR_SEQ     252    271       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:11677242}.
FT                                /FTId=VSP_002089.
FT   VAR_SEQ     447    669       Missing (in isoform 5).
FT                                {ECO:0000303|Ref.6}.
FT                                /FTId=VSP_014699.
FT   VAR_SEQ     612    669       NSTPQLAGILARVLNGEAPPSLGPSSVASPEDVQALMYLRG
FT                                QLEPQWKMLQCHPHLVA -> VSWAGWRCCGVGRGKGPVTA
FT                                SVFAPGPELHTPASRDPGPGAEWRGTS (in isoform
FT                                4). {ECO:0000303|PubMed:11677242,
FT                                ECO:0000303|PubMed:11726666}.
FT                                /FTId=VSP_002090.
FT   VARIANT     429    429       V -> I (in dbSNP:rs34402301).
FT                                /FTId=VAR_049356.
FT   MUTAGEN     135    135       H->A: Abolishes deacetylase activity.
FT                                Does not affect interaction with HDAC3.
FT                                Loss of autophagy regulation.
FT                                {ECO:0000269|PubMed:11726666,
FT                                ECO:0000269|PubMed:11861901,
FT                                ECO:0000269|PubMed:23801752}.
FT   CONFLICT     92     92       A -> T (in Ref. 6; AAS48345).
FT                                {ECO:0000305}.
FT   CONFLICT    177    177       Q -> R (in Ref. 6; AAS48345).
FT                                {ECO:0000305}.
FT   CONFLICT    337    337       Q -> QRC (in Ref. 9; CAC21653).
FT                                {ECO:0000305}.
FT   CONFLICT    337    337       Q -> QRCEG (in Ref. 4; no nucleotide
FT                                entry). {ECO:0000305}.
FT   CONFLICT    594    594       A -> T (in Ref. 3; AAK92205/AAK92206).
FT                                {ECO:0000305}.
SQ   SEQUENCE   669 AA;  71445 MW;  872D9427E6893A18 CRC64;
     MGTALVYHED MTATRLLWDD PECEIERPER LTAALDRLRQ RGLEQRCLRL SAREASEEEL
     GLVHSPEYVS LVRETQVLGK EELQALSGQF DAIYFHPSTF HCARLAAGAG LQLVDAVLTG
     AVQNGLALVR PPGHHGQRAA ANGFCVFNNV AIAAAHAKQK HGLHRILVVD WDVHHGQGIQ
     YLFEDDPSVL YFSWHRYEHG RFWPFLRESD ADAVGRGQGL GFTVNLPWNQ VGMGNADYVA
     AFLHLLLPLA FEFDPELVLV SAGFDSAIGD PEGQMQATPE CFAHLTQLLQ VLAGGRVCAV
     LEGGYHLESL AESVCMTVQT LLGDPAPPLS GPMAPCQSAL ESIQSARAAQ APHWKSLQQQ
     DVTAVPMSPS SHSPEGRPPP LLPGGPVCKA AASAPSSLLD QPCLCPAPSV RTAVALTTPD
     ITLVLPPDVI QQEASALREE TEAWARPHES LAREEALTAL GKLLYLLDGM LDGQVNSGIA
     ATPASAAAAT LDVAVRRGLS HGAQRLLCVA LGQLDRPPDL AHDGRSLWLN IRGKEAAALS
     MFHVSTPLPV MTGGFLSCIL GLVLPLAYGF QPDLVLVALG PGHGLQGPHA ALLAAMLRGL
     AGGRVLALLE ENSTPQLAGI LARVLNGEAP PSLGPSSVAS PEDVQALMYL RGQLEPQWKM
     LQCHPHLVA
//
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