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 03-AUG-2022, entry version 173.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH HDAC3,
RP MUTAGENESIS OF HIS-135, TISSUE SPECIFICITY, INHIBITION BY TSA, AND
RP 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 LOCATION,
RP 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 deacetylase,
RT 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., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., 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., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., 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., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA 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 project:
RT 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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA 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 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., Hartenstein B.,
RA Wiegand I., Eckert C., Roth W., Kool M., Kaden S., Groene H.J.,
RA Schulte J.H., Lindner S., Hamacher-Brady A., Brady N.R., Deubzer H.E.,
RA 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 BY
RP 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., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT 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., Fang J.,
RA Coppola D., Shibata D., Lane W.S., Zhang Y., Zhang X., Seto E.;
RT "Histone deacetylase 10 regulates DNA mismatch repair and may involve the
RT 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 polyamine
RT 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 on
CC 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 activity, if
CC any, toward N(1)-acetylspermidine (PubMed:28516954). Histone
CC deacetylase activity has been observed in vitro (PubMed:11861901,
CC PubMed:11726666, PubMed:11677242, PubMed:11739383). Has also been shown
CC to be involved in MSH2 deacetylation (PubMed:26221039). The
CC physiological relevance of protein/histone deacetylase activity is
CC unclear and could be very weak (PubMed:28516954). May play a role in
CC the promotion of late stages of autophagy, possibly autophagosome-
CC lysosome fusion and/or lysosomal exocytosis in neuroblastoma cells
CC (PubMed:23801752, PubMed:29968769). May play a role in homologous
CC recombination (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, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:61930; 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 {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 HDAC2
CC 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 -!- INTERACTION:
CC Q969S8; Q92870-2: APBB2; NbExp=3; IntAct=EBI-301762, EBI-21535880;
CC Q969S8; P54252: ATXN3; NbExp=3; IntAct=EBI-301762, EBI-946046;
CC Q969S8; P42858: HTT; NbExp=21; IntAct=EBI-301762, EBI-466029;
CC Q969S8; Q96CV9: OPTN; NbExp=3; IntAct=EBI-301762, EBI-748974;
CC Q969S8; Q7Z412: PEX26; NbExp=3; IntAct=EBI-301762, EBI-752057;
CC Q969S8; D3DTS7: PMP22; NbExp=3; IntAct=EBI-301762, EBI-25882629;
CC Q969S8; P37840: SNCA; NbExp=3; IntAct=EBI-301762, EBI-985879;
CC Q969S8; Q9BYV2: TRIM54; NbExp=2; IntAct=EBI-301762, EBI-2130429;
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 {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 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 response
CC to chemotherapy-induced DNA damage and efflux of chemotherapeutics via
CC lysosomal exocytosis, hence protecting cells from cytotoxic agents
CC (PubMed:23801752, PubMed:29968769). Expression levels may correlate
CC with survival in neuroblastoma patients, with low levels in the tumor
CC correlating with long-term patient survival and high expression with
CC poor prognosis (PubMed:23801752). Therefore has been proposed as a
CC biomarker to predict neuroblastoma chemoresistance and treatment
CC outcome (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, such
CC as HDAC4, inhibited by the antitumor drug trichostatin A (TSA).
CC {ECO:0000269|PubMed:11861901}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Protein/histone deacetylase activity in vivo is uncertain. The
CC 3D structure analysis of the zebrafish ortholog shows that a glutamate
CC gatekeeper and a sterically constricted active site confer specificity
CC for N(8)-acetylspermidine hydrolysis and disfavour acetyllysine
CC hydrolysis. Supporting this observation, has been shown to exhibit only
CC very low activity, if any, towards acetyl-lysine peptide substrates
CC (PubMed:28516954). However, histone deacetylase activity has been
CC observed in vitro (PubMed:28516954, PubMed:11861901, PubMed:11726666,
CC PubMed:11677242, PubMed:11739383). Has also been shown to be involved
CC in MSH2 deacetylation (PubMed:26221039). {ECO:0000269|PubMed:11677242,
CC ECO:0000269|PubMed:11726666, ECO:0000269|PubMed:11739383,
CC ECO:0000269|PubMed:11861901, ECO:0000269|PubMed:26221039,
CC ECO:0000269|PubMed:28516954}.
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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 AlphaFoldDB; Q969S8; -.
DR SMR; Q969S8; -.
DR BioGRID; 123818; 59.
DR CORUM; Q969S8; -.
DR IntAct; Q969S8; 30.
DR STRING; 9606.ENSP00000216271; -.
DR BindingDB; Q969S8; -.
DR ChEMBL; CHEMBL5103; -.
DR DrugBank; DB05015; Belinostat.
DR DrugBank; DB13346; Bufexamac.
DR DrugBank; DB06603; Panobinostat.
DR DrugCentral; Q969S8; -.
DR GuidetoPHARMACOLOGY; 2614; -.
DR iPTMnet; Q969S8; -.
DR PhosphoSitePlus; Q969S8; -.
DR BioMuta; HDAC10; -.
DR DMDM; 27734403; -.
DR EPD; Q969S8; -.
DR jPOST; Q969S8; -.
DR MassIVE; Q969S8; -.
DR MaxQB; Q969S8; -.
DR PaxDb; Q969S8; -.
DR PeptideAtlas; Q969S8; -.
DR PRIDE; Q969S8; -.
DR ProteomicsDB; 75833; -. [Q969S8-1]
DR ProteomicsDB; 75834; -. [Q969S8-2]
DR ProteomicsDB; 75835; -. [Q969S8-4]
DR ProteomicsDB; 75836; -. [Q969S8-5]
DR Antibodypedia; 14233; 523 antibodies from 37 providers.
DR DNASU; 83933; -.
DR Ensembl; ENST00000216271.10; ENSP00000216271.5; ENSG00000100429.18. [Q969S8-1]
DR Ensembl; ENST00000349505.4; ENSP00000343540.4; ENSG00000100429.18. [Q969S8-2]
DR Ensembl; ENST00000454936.5; ENSP00000406150.1; ENSG00000100429.18. [Q969S8-5]
DR GeneID; 83933; -.
DR KEGG; hsa:83933; -.
DR MANE-Select; ENST00000216271.10; ENSP00000216271.5; NM_032019.6; NP_114408.3.
DR UCSC; uc003bkg.4; human. [Q969S8-1]
DR CTD; 83933; -.
DR DisGeNET; 83933; -.
DR GeneCards; HDAC10; -.
DR HGNC; HGNC:18128; HDAC10.
DR HPA; ENSG00000100429; Low tissue specificity.
DR MIM; 608544; gene.
DR neXtProt; NX_Q969S8; -.
DR OpenTargets; ENSG00000100429; -.
DR PharmGKB; PA38297; -.
DR VEuPathDB; HostDB:ENSG00000100429; -.
DR eggNOG; KOG1343; Eukaryota.
DR GeneTree; ENSGT00940000160061; -.
DR HOGENOM; CLU_007727_6_0_1; -.
DR InParanoid; Q969S8; -.
DR OMA; PQVTGEM; -.
DR OrthoDB; 1484694at2759; -.
DR PhylomeDB; Q969S8; -.
DR TreeFam; TF106173; -.
DR BRENDA; 3.5.1.48; 2681.
DR BRENDA; 3.5.1.98; 2681.
DR PathwayCommons; Q969S8; -.
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 Reactome; R-HSA-350054; Notch-HLH transcription pathway.
DR SABIO-RK; Q969S8; -.
DR SignaLink; Q969S8; -.
DR SIGNOR; Q969S8; -.
DR BioGRID-ORCS; 83933; 3 hits in 1090 CRISPR screens.
DR ChiTaRS; HDAC10; human.
DR GeneWiki; HDAC10; -.
DR GenomeRNAi; 83933; -.
DR Pharos; Q969S8; Tclin.
DR PRO; PR:Q969S8; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q969S8; protein.
DR Bgee; ENSG00000100429; Expressed in granulocyte and 117 other tissues.
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 lysine 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: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; -; 1.
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 Pfam; PF00850; Hist_deacetyl; 1.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; SSF52768; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Cytoplasm; DNA damage; DNA recombination;
KW DNA repair; Hydrolase; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Zinc.
FT CHAIN 1..669
FT /note="Polyamine deacetylase HDAC10"
FT /id="PRO_0000114712"
FT REGION 1..323
FT /note="Histone deacetylase"
FT REGION 361..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 21..24
FT /note="Substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:F1QCV2"
FT ACT_SITE 135
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:F1QCV2"
FT BINDING 20
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:F1QCV2"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:F1QCV2"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:F1QCV2"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:F1QCV2"
FT BINDING 305
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:F1QCV2"
FT SITE 272
FT /note="Substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:F1QCV2"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 252..301
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_014698"
FT VAR_SEQ 252..271
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11677242"
FT /id="VSP_002089"
FT VAR_SEQ 447..669
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_014699"
FT VAR_SEQ 612..669
FT /note="NSTPQLAGILARVLNGEAPPSLGPSSVASPEDVQALMYLRGQLEPQWKMLQC
FT HPHLVA -> VSWAGWRCCGVGRGKGPVTASVFAPGPELHTPASRDPGPGAEWRGTS
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11677242,
FT ECO:0000303|PubMed:11726666"
FT /id="VSP_002090"
FT VARIANT 429
FT /note="V -> I (in dbSNP:rs34402301)"
FT /id="VAR_049356"
FT MUTAGEN 135
FT /note="H->A: Abolishes deacetylase activity. Does not
FT affect interaction with HDAC3. Loss of autophagy
FT regulation."
FT /evidence="ECO:0000269|PubMed:11726666,
FT ECO:0000269|PubMed:11861901, ECO:0000269|PubMed:23801752"
FT CONFLICT 92
FT /note="A -> T (in Ref. 6; AAS48345)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="Q -> R (in Ref. 6; AAS48345)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="Q -> QRC (in Ref. 9; CAC21653)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="Q -> QRCEG (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 594
FT /note="A -> T (in Ref. 3; AAK92205/AAK92206)"
FT /evidence="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
