HDAC9_HUMAN
ID HDAC9_HUMAN Reviewed; 1011 AA.
AC Q9UKV0; A7E2F3; B7Z4I4; B7Z917; B7Z928; B7Z940; C9JS87; E7EX34; F8W9E0;
AC O94845; O95028; Q2M2R6; Q86SL1; Q86US3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Histone deacetylase 9;
DE Short=HD9;
DE EC=3.5.1.98 {ECO:0000269|PubMed:11535832};
DE AltName: Full=Histone deacetylase 7B;
DE Short=HD7;
DE Short=HD7b;
DE AltName: Full=Histone deacetylase-related protein;
DE AltName: Full=MEF2-interacting transcription repressor MITR;
GN Name=HDAC9; Synonyms=HDAC7, HDAC7B, HDRP, KIAA0744, MITR;
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] (ISOFORMS 1 AND 4), TISSUE SPECIFICITY,
RP INTERACTION WITH MEF2, FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY
RP REGULATION.
RC TISSUE=Brain;
RX PubMed=11535832; DOI=10.1073/pnas.191375098;
RA Zhou X., Marks P.A., Rifkind R.A., Richon V.M.;
RT "Cloning and characterization of a histone deacetylase, HDAC9.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:10572-10577(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), TISSUE SPECIFICITY, AND CHROMOSOMAL
RP TRANSLOCATION WITH TGFB2.
RC TISSUE=Lens;
RX PubMed=12706107; DOI=10.1016/s0888-7543(03)00046-6;
RA David D., Cardoso J., Marques B., Marques R., Silva E.D., Santos H.,
RA Boavida M.G.;
RT "Molecular characterization of a familial translocation implicates
RT disruption of HDAC9 and possible position effect on TGFbeta2 in the
RT pathogenesis of Peters' anomaly.";
RL Genomics 81:489-503(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), TISSUE SPECIFICITY, ALTERNATIVE
RP SPLICING (ISOFORMS 3; 6 AND 7), INTERACTION WITH ETV6; NCOR1 AND BCL6,
RP FUNCTION, SUBCELLULAR LOCATION, AND SUMOYLATION.
RC TISSUE=Brain;
RX PubMed=12590135; DOI=10.1074/jbc.m212935200;
RA Petrie K., Guidez F., Howell L., Healy L., Waxman S., Greaves M.,
RA Zelent A.;
RT "The histone deacetylase 9 gene encodes multiple protein isoforms.";
RL J. Biol. Chem. 278:16059-16072(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 8; 9; 10 AND 11).
RC TISSUE=Brain, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 2-1011 (ISOFORM 6).
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 [MRNA] OF 99-650 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10523670; DOI=10.1128/mcb.19.11.7816;
RA Wang A.H., Bertos N.R., Vezmar M., Pelletier N., Crosato M., Heng H.H.,
RA Th'ng J., Han J., Yang X.-J.;
RT "HDAC4, a human histone deacetylase related to yeast HDA1, is a
RT transcriptional corepressor.";
RL Mol. Cell. Biol. 19:7816-7827(1999).
RN [10]
RP IDENTIFICATION (ISOFORM 3), INTERACTION WITH HDAC1, AND FUNCTION.
RX PubMed=10487760; DOI=10.1093/emboj/18.18.5085;
RA Sparrow D.B., Miska E.A., Langley E., Reynaud-Deonauth S., Kotecha S.,
RA Towers N., Spohr G., Kouzarides T., Mohun T.J.;
RT "MEF-2 function is modified by a novel co-repressor, MITR.";
RL EMBO J. 18:5085-5098(1999).
RN [11]
RP IDENTIFICATION (ISOFORM 3), TISSUE SPECIFICITY, INTERACTION WITH HDAC1 AND
RP HDAC3, AND FUNCTION.
RX PubMed=10655483; DOI=10.1073/pnas.97.3.1056;
RA Zhou X., Richon V.M., Rifkind R.A., Marks P.A.;
RT "Identification of a transcriptional repressor related to the noncatalytic
RT domain of histone deacetylases 4 and 5.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:1056-1061(2000).
RN [12]
RP INTERACTION WITH MEF2.
RX PubMed=10487761; DOI=10.1093/emboj/18.18.5099;
RA Miska E.A., Karlsson C., Langley E., Nielsen S.J., Pines J., Kouzarides T.;
RT "HDAC4 deacetylase associates with and represses the MEF2 transcription
RT factor.";
RL EMBO J. 18:5099-5107(1999).
RN [13]
RP SUMOYLATION.
RX PubMed=12032081; DOI=10.1093/emboj/21.11.2682;
RA Kirsh O., Seeler J.-S., Pichler A., Gast A., Mueller S., Miska E.,
RA Mathieu M., Harel-Bellan A., Kouzarides T., Melchior F., Dejean A.;
RT "The SUMO E3 ligase RanBP2 promotes modification of the HDAC4
RT deacetylase.";
RL EMBO J. 21:2682-2691(2002).
RN [14]
RP FUNCTION.
RX PubMed=16611996; DOI=10.1128/mcb.26.9.3550-3564.2006;
RA Morrison B.E., Majdzadeh N., Zhang X., Lyles A., Bassel-Duby R.,
RA Olson E.N., D'Mello S.R.;
RT "Neuroprotection by histone deacetylase-related protein.";
RL Mol. Cell. Biol. 26:3550-3564(2006).
RN [15]
RP INTERACTION WITH FOXP3.
RX PubMed=17360565; DOI=10.1073/pnas.0700298104;
RA Li B., Samanta A., Song X., Iacono K.T., Bembas K., Tao R., Basu S.,
RA Riley J.L., Hancock W.W., Shen Y., Saouaf S.J., Greene M.I.;
RT "FOXP3 interactions with histone acetyltransferase and class II histone
RT deacetylases are required for repression.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:4571-4576(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [17]
RP PHOSPHORYLATION.
RX PubMed=20188095; DOI=10.1016/j.febslet.2010.02.057;
RA Harrison B.C., Huynh K., Lundgaard G.L., Helmke S.M., Perryman M.B.,
RA McKinsey T.A.;
RT "Protein kinase C-related kinase targets nuclear localization signals in a
RT subset of class IIa histone deacetylases.";
RL FEBS Lett. 584:1103-1110(2010).
RN [18]
RP VARIANT THR-921.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
CC -!- FUNCTION: Responsible for the deacetylation of lysine residues on the
CC N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone
CC deacetylation gives a tag for epigenetic repression and plays an
CC important role in transcriptional regulation, cell cycle progression
CC and developmental events. Represses MEF2-dependent transcription.
CC {ECO:0000269|PubMed:11535832}.
CC -!- FUNCTION: Isoform 3 lacks active site residues and therefore is
CC catalytically inactive. Represses MEF2-dependent transcription by
CC recruiting HDAC1 and/or HDAC3. Seems to inhibit skeletal myogenesis and
CC to be involved in heart development. Protects neurons from apoptosis,
CC both by inhibiting JUN phosphorylation by MAPK10 and by repressing JUN
CC transcription via HDAC1 recruitment to JUN promoter.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-
CC [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:61930; EC=3.5.1.98;
CC Evidence={ECO:0000269|PubMed:11535832};
CC -!- ACTIVITY REGULATION: Inhibited by Trichostatin A (TSA) and
CC suberoylanilide hydroxamic acid. {ECO:0000269|PubMed:11535832}.
CC -!- SUBUNIT: Homodimer. Interacts with CTBP1. The phosphorylated form
CC interacts with 14-3-3 (By similarity). Interacts with HDAC1 and HDAC3,
CC and probably with HDAC4 and HDAC5. Interacts with MEF2, MAPK10, ETV6,
CC NCOR1 and BCL6. Interacts with FOXP3 in the absence of T-cell
CC stimulation. {ECO:0000250|UniProtKB:Q99N13,
CC ECO:0000269|PubMed:10487760, ECO:0000269|PubMed:10487761,
CC ECO:0000269|PubMed:10655483, ECO:0000269|PubMed:11535832,
CC ECO:0000269|PubMed:12590135, ECO:0000269|PubMed:17360565}.
CC -!- INTERACTION:
CC Q9UKV0; P41182: BCL6; NbExp=2; IntAct=EBI-765444, EBI-765407;
CC Q9UKV0; Q06413: MEF2C; NbExp=3; IntAct=EBI-765444, EBI-2684075;
CC Q9UKV0-3; P41212: ETV6; NbExp=3; IntAct=EBI-765476, EBI-1372759;
CC Q9UKV0-3; Q60974: Ncor1; Xeno; NbExp=2; IntAct=EBI-765476, EBI-349004;
CC Q9UKV0-7; Q60974: Ncor1; Xeno; NbExp=3; IntAct=EBI-1372717, EBI-349004;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=11;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q9UKV0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UKV0-2; Sequence=VSP_002082;
CC Name=3; Synonyms=HDRP, MITR;
CC IsoId=Q9UKV0-3; Sequence=VSP_002083, VSP_002084;
CC Name=4; Synonyms=HDAC9a;
CC IsoId=Q9UKV0-4; Sequence=VSP_002085, VSP_002086;
CC Name=5; Synonyms=HDAC9b, HDAC9fl;
CC IsoId=Q9UKV0-5; Sequence=VSP_023768;
CC Name=6;
CC IsoId=Q9UKV0-6; Sequence=VSP_023766, VSP_023767, VSP_023768;
CC Name=7;
CC IsoId=Q9UKV0-7; Sequence=VSP_023766, VSP_023768;
CC Name=8;
CC IsoId=Q9UKV0-8; Sequence=VSP_043428, VSP_023767, VSP_002083,
CC VSP_002084;
CC Name=9;
CC IsoId=Q9UKV0-9; Sequence=VSP_023767, VSP_002083, VSP_002084;
CC Name=10;
CC IsoId=Q9UKV0-10; Sequence=VSP_046827, VSP_023766, VSP_002083,
CC VSP_002084;
CC Name=11;
CC IsoId=Q9UKV0-11; Sequence=VSP_046827, VSP_046828, VSP_023767,
CC VSP_002083, VSP_002084;
CC -!- TISSUE SPECIFICITY: Broadly expressed, with highest levels in brain,
CC heart, muscle and testis. Isoform 3 is present in human bladder
CC carcinoma cells (at protein level). {ECO:0000269|PubMed:10655483,
CC ECO:0000269|PubMed:11535832, ECO:0000269|PubMed:12590135,
CC ECO:0000269|PubMed:12706107}.
CC -!- PTM: Phosphorylated on Ser-220 and Ser-450; which promotes 14-3-3-
CC binding, impairs interaction with MEF2, and antagonizes antimyogenic
CC activity. Phosphorylated on Ser-240; which impairs nuclear accumulation
CC (By similarity). Isoform 7 is phosphorylated on Tyr-1010.
CC Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear
CC import. {ECO:0000250, ECO:0000269|PubMed:20188095}.
CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:12032081,
CC ECO:0000269|PubMed:12590135}.
CC -!- DISEASE: Note=A chromosomal aberration involving HDAC9 is found in a
CC family with Peters anomaly. Translocation t(1;7)(q41;p21) with TGFB2
CC resulting in lack of HDAC9 protein. {ECO:0000269|PubMed:12706107}.
CC -!- MISCELLANEOUS: [Isoform 3]: Major form in most tissues. Inactive due to
CC lack of active site residues. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 6]: Excluded from the nucleus. Does not
CC interact with ETV6. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34464.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 6]:
CC Sequence=AAI11736.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY032737; AAK66821.1; -; mRNA.
DR EMBL; AY032738; AAK66822.1; -; mRNA.
DR EMBL; AJ459808; CAD30851.1; -; mRNA.
DR EMBL; AY197371; AAO27363.1; -; mRNA.
DR EMBL; AB018287; BAA34464.2; ALT_INIT; mRNA.
DR EMBL; AK297404; BAH12570.1; -; mRNA.
DR EMBL; AK304298; BAH14153.1; -; mRNA.
DR EMBL; AK304343; BAH14164.1; -; mRNA.
DR EMBL; AK304410; BAH14176.1; -; mRNA.
DR EMBL; AC002088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC002124; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC002410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC002433; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC074193; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091697; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471073; EAW93702.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93703.1; -; Genomic_DNA.
DR EMBL; BC111735; AAI11736.1; ALT_FRAME; mRNA.
DR EMBL; BC150328; AAI50329.1; -; mRNA.
DR EMBL; BC152405; AAI52406.1; -; mRNA.
DR EMBL; AF124924; AAF04254.1; -; mRNA.
DR CCDS; CCDS47553.1; -. [Q9UKV0-7]
DR CCDS; CCDS47554.1; -. [Q9UKV0-5]
DR CCDS; CCDS47555.1; -. [Q9UKV0-1]
DR CCDS; CCDS47557.1; -. [Q9UKV0-3]
DR CCDS; CCDS56465.1; -. [Q9UKV0-8]
DR CCDS; CCDS56466.1; -. [Q9UKV0-9]
DR CCDS; CCDS56467.1; -. [Q9UKV0-10]
DR CCDS; CCDS56468.1; -. [Q9UKV0-11]
DR CCDS; CCDS83163.1; -. [Q9UKV0-6]
DR RefSeq; NP_001191073.1; NM_001204144.2. [Q9UKV0-8]
DR RefSeq; NP_001191074.1; NM_001204145.2. [Q9UKV0-9]
DR RefSeq; NP_001191075.1; NM_001204146.2.
DR RefSeq; NP_001191076.1; NM_001204147.2. [Q9UKV0-11]
DR RefSeq; NP_001191077.1; NM_001204148.2. [Q9UKV0-10]
DR RefSeq; NP_001308797.1; NM_001321868.1.
DR RefSeq; NP_001308798.1; NM_001321869.1.
DR RefSeq; NP_001308799.1; NM_001321870.1.
DR RefSeq; NP_001308800.1; NM_001321871.1.
DR RefSeq; NP_001308801.1; NM_001321872.1.
DR RefSeq; NP_001308802.1; NM_001321873.1.
DR RefSeq; NP_001308803.1; NM_001321874.1.
DR RefSeq; NP_001308804.1; NM_001321875.1.
DR RefSeq; NP_001308805.1; NM_001321876.1.
DR RefSeq; NP_001308806.1; NM_001321877.1. [Q9UKV0-6]
DR RefSeq; NP_001308807.1; NM_001321878.1.
DR RefSeq; NP_001308808.1; NM_001321879.1.
DR RefSeq; NP_001308813.1; NM_001321884.1.
DR RefSeq; NP_001308814.1; NM_001321885.1.
DR RefSeq; NP_001308815.1; NM_001321886.1.
DR RefSeq; NP_001308816.1; NM_001321887.1.
DR RefSeq; NP_001308817.1; NM_001321888.1.
DR RefSeq; NP_001308818.1; NM_001321889.1.
DR RefSeq; NP_001308819.1; NM_001321890.1.
DR RefSeq; NP_001308820.1; NM_001321891.1. [Q9UKV0-9]
DR RefSeq; NP_001308822.1; NM_001321893.1. [Q9UKV0-9]
DR RefSeq; NP_001308823.1; NM_001321894.1.
DR RefSeq; NP_001308824.1; NM_001321895.1.
DR RefSeq; NP_001308825.1; NM_001321896.1. [Q9UKV0-10]
DR RefSeq; NP_001308826.1; NM_001321897.1. [Q9UKV0-6]
DR RefSeq; NP_001308827.1; NM_001321898.1.
DR RefSeq; NP_001308828.1; NM_001321899.1.
DR RefSeq; NP_001308829.1; NM_001321900.1. [Q9UKV0-3]
DR RefSeq; NP_001308830.1; NM_001321901.1.
DR RefSeq; NP_001308831.1; NM_001321902.1.
DR RefSeq; NP_055522.1; NM_014707.3. [Q9UKV0-3]
DR RefSeq; NP_478056.1; NM_058176.2. [Q9UKV0-1]
DR RefSeq; NP_848510.1; NM_178423.2. [Q9UKV0-5]
DR RefSeq; NP_848512.1; NM_178425.3. [Q9UKV0-7]
DR RefSeq; XP_011513940.1; XM_011515638.2.
DR RefSeq; XP_011513941.1; XM_011515639.2.
DR RefSeq; XP_016868315.1; XM_017012826.1.
DR RefSeq; XP_016868317.1; XM_017012828.1.
DR AlphaFoldDB; Q9UKV0; -.
DR SMR; Q9UKV0; -.
DR BioGRID; 115083; 74.
DR DIP; DIP-39904N; -.
DR ELM; Q9UKV0; -.
DR IntAct; Q9UKV0; 33.
DR MINT; Q9UKV0; -.
DR STRING; 9606.ENSP00000408617; -.
DR BindingDB; Q9UKV0; -.
DR ChEMBL; CHEMBL4145; -.
DR DrugBank; DB05015; Belinostat.
DR DrugBank; DB06603; Panobinostat.
DR DrugBank; DB00313; Valproic acid.
DR DrugCentral; Q9UKV0; -.
DR GuidetoPHARMACOLOGY; 2620; -.
DR iPTMnet; Q9UKV0; -.
DR PhosphoSitePlus; Q9UKV0; -.
DR BioMuta; HDAC9; -.
DR DMDM; 19865267; -.
DR jPOST; Q9UKV0; -.
DR MassIVE; Q9UKV0; -.
DR MaxQB; Q9UKV0; -.
DR PaxDb; Q9UKV0; -.
DR PeptideAtlas; Q9UKV0; -.
DR PRIDE; Q9UKV0; -.
DR ProteomicsDB; 11455; -.
DR ProteomicsDB; 18971; -.
DR ProteomicsDB; 30309; -.
DR ProteomicsDB; 84881; -. [Q9UKV0-1]
DR ProteomicsDB; 84882; -. [Q9UKV0-2]
DR ProteomicsDB; 84883; -. [Q9UKV0-3]
DR ProteomicsDB; 84884; -. [Q9UKV0-4]
DR ProteomicsDB; 84885; -. [Q9UKV0-5]
DR ProteomicsDB; 84886; -. [Q9UKV0-6]
DR ProteomicsDB; 84887; -. [Q9UKV0-7]
DR ProteomicsDB; 84888; -. [Q9UKV0-8]
DR Antibodypedia; 6494; 644 antibodies from 39 providers.
DR DNASU; 9734; -.
DR Ensembl; ENST00000401921.5; ENSP00000383912.1; ENSG00000048052.24. [Q9UKV0-6]
DR Ensembl; ENST00000405010.7; ENSP00000384382.3; ENSG00000048052.24. [Q9UKV0-3]
DR Ensembl; ENST00000406451.8; ENSP00000384657.3; ENSG00000048052.24. [Q9UKV0-5]
DR Ensembl; ENST00000417496.6; ENSP00000401669.2; ENSG00000048052.24. [Q9UKV0-8]
DR Ensembl; ENST00000428307.6; ENSP00000395655.2; ENSG00000048052.24. [Q9UKV0-9]
DR Ensembl; ENST00000432645.6; ENSP00000410337.2; ENSG00000048052.24. [Q9UKV0-1]
DR Ensembl; ENST00000441542.7; ENSP00000408617.2; ENSG00000048052.24. [Q9UKV0-7]
DR Ensembl; ENST00000456174.6; ENSP00000388568.2; ENSG00000048052.24. [Q9UKV0-10]
DR Ensembl; ENST00000524023.1; ENSP00000430036.1; ENSG00000048052.24. [Q9UKV0-11]
DR Ensembl; ENST00000686413.1; ENSP00000509161.1; ENSG00000048052.24. [Q9UKV0-7]
DR GeneID; 9734; -.
DR KEGG; hsa:9734; -.
DR MANE-Select; ENST00000686413.1; ENSP00000509161.1; NM_178425.4; NP_848512.1. [Q9UKV0-7]
DR UCSC; uc003sud.2; human. [Q9UKV0-1]
DR CTD; 9734; -.
DR DisGeNET; 9734; -.
DR GeneCards; HDAC9; -.
DR HGNC; HGNC:14065; HDAC9.
DR HPA; ENSG00000048052; Tissue enhanced (choroid).
DR MIM; 606543; gene.
DR neXtProt; NX_Q9UKV0; -.
DR OpenTargets; ENSG00000048052; -.
DR PharmGKB; PA38377; -.
DR VEuPathDB; HostDB:ENSG00000048052; -.
DR eggNOG; KOG1343; Eukaryota.
DR GeneTree; ENSGT00940000160307; -.
DR HOGENOM; CLU_006530_2_0_1; -.
DR InParanoid; Q9UKV0; -.
DR OMA; FMQQPFP; -.
DR OrthoDB; 1484694at2759; -.
DR PhylomeDB; Q9UKV0; -.
DR TreeFam; TF106174; -.
DR BRENDA; 3.5.1.98; 2681.
DR PathwayCommons; Q9UKV0; -.
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-350054; Notch-HLH transcription pathway.
DR SignaLink; Q9UKV0; -.
DR SIGNOR; Q9UKV0; -.
DR BioGRID-ORCS; 9734; 20 hits in 1094 CRISPR screens.
DR ChiTaRS; HDAC9; human.
DR GeneWiki; HDAC9; -.
DR GenomeRNAi; 9734; -.
DR Pharos; Q9UKV0; Tclin.
DR PRO; PR:Q9UKV0; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9UKV0; protein.
DR Bgee; ENSG00000048052; Expressed in oocyte and 201 other tissues.
DR ExpressionAtlas; Q9UKV0; baseline and differential.
DR Genevisible; Q9UKV0; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0035097; C:histone methyltransferase complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IDA:BHF-UCL.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IDA:BHF-UCL.
DR GO; GO:0004407; F:histone deacetylase activity; IDA:BHF-UCL.
DR GO; GO:0034739; F:histone deacetylase activity (H4-K16 specific); IDA:ARUK-UCL.
DR GO; GO:0042826; F:histone deacetylase binding; IDA:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005080; F:protein kinase C binding; IPI:UniProtKB.
DR GO; GO:0033558; F:protein lysine deacetylase activity; IDA:BHF-UCL.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:BHF-UCL.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:BHF-UCL.
DR GO; GO:0042113; P:B cell activation; TAS:UniProtKB.
DR GO; GO:0030183; P:B cell differentiation; TAS:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:BHF-UCL.
DR GO; GO:0042632; P:cholesterol homeostasis; IDA:ARUK-UCL.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0007507; P:heart development; ISS:BHF-UCL.
DR GO; GO:0016575; P:histone deacetylation; IDA:BHF-UCL.
DR GO; GO:0070932; P:histone H3 deacetylation; IDA:BHF-UCL.
DR GO; GO:0070933; P:histone H4 deacetylation; IDA:BHF-UCL.
DR GO; GO:1990678; P:histone H4-K16 deacetylation; IDA:ARUK-UCL.
DR GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
DR GO; GO:0001818; P:negative regulation of cytokine production; IDA:ARUK-UCL.
DR GO; GO:0051005; P:negative regulation of lipoprotein lipase activity; IDA:ARUK-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0034983; P:peptidyl-lysine deacetylation; IDA:BHF-UCL.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IMP:BHF-UCL.
DR GO; GO:0048742; P:regulation of skeletal muscle fiber development; ISS:UniProtKB.
DR GO; GO:0051153; P:regulation of striated muscle cell differentiation; ISS: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; IPR024643; Hist_deacetylase_Gln_rich_N.
DR InterPro; IPR017320; Histone_deAcase_II_euk.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR Pfam; PF12203; HDAC4_Gln; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037911; HDAC_II_euk; 1.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; SSF52768; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Chromosomal rearrangement;
KW Hydrolase; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc.
FT CHAIN 1..1011
FT /note="Histone deacetylase 9"
FT /id="PRO_0000114710"
FT REGION 23..27
FT /note="Interaction with CTBP1"
FT /evidence="ECO:0000250"
FT REGION 110..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..154
FT /note="Interaction with MEF2"
FT /evidence="ECO:0000250"
FT REGION 175..343
FT /note="Interaction with MAPK10"
FT /evidence="ECO:0000250"
FT REGION 183..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..261
FT /note="Interaction with ETV6"
FT /evidence="ECO:0000269|PubMed:12590135"
FT REGION 262..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..978
FT /note="Histone deacetylase"
FT COMPBIAS 183..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 783
FT /evidence="ECO:0000250"
FT BINDING 646
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 648
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 654
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 731
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99N13"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99N13"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99N13"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99N13"
FT VAR_SEQ 1..31
FT /note="Missing (in isoform 10 and isoform 11)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046827"
FT VAR_SEQ 1
FT /note="M -> MMSSPAQPDLMWNLVPWVLFCGCCRIFPDGVAGREQLLAQQRM (in
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043428"
FT VAR_SEQ 88
FT /note="K -> KLQQ (in isoform 6, isoform 7 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:12590135,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_023766"
FT VAR_SEQ 177..178
FT /note="Missing (in isoform 11)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046828"
FT VAR_SEQ 218..261
FT /note="Missing (in isoform 6, isoform 8, isoform 9 and
FT isoform 11)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_023767"
FT VAR_SEQ 487..574
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10523670"
FT /id="VSP_002082"
FT VAR_SEQ 575..590
FT /note="PFLEPTHTRALSVRQA -> VIGKDLAPGFVIKVII (in isoform 3,
FT isoform 8, isoform 9, isoform 10 and isoform 11)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9872452"
FT /id="VSP_002083"
FT VAR_SEQ 591..1011
FT /note="Missing (in isoform 3, isoform 8, isoform 9, isoform
FT 10 and isoform 11)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9872452"
FT /id="VSP_002084"
FT VAR_SEQ 861..879
FT /note="GTGLGEGYNINIAWTGGLD -> RFISLEPHFYLYLSGNCIA (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:11535832"
FT /id="VSP_002085"
FT VAR_SEQ 880..1011
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11535832"
FT /id="VSP_002086"
FT VAR_SEQ 1006..1011
FT /note="MSLKFS -> KYWKSVRMVAVPRGCALAGAQLQEETETVSALASLTVDVEQP
FT FAQEDSRTAGEPMEEEPAL (in isoform 5, isoform 6 and isoform
FT 7)"
FT /evidence="ECO:0000303|PubMed:12590135,
FT ECO:0000303|PubMed:12706107, ECO:0000303|PubMed:15489334"
FT /id="VSP_023768"
FT VARIANT 921
FT /note="P -> T (found in a renal cell carcinoma sample;
FT somatic mutation; dbSNP:rs1333490692)"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064719"
FT CONFLICT 16
FT /note="V -> A (in Ref. 5; BAH12570)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="L -> I (in Ref. 9; AAF04254)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="S -> I (in Ref. 5; BAH14164)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="S -> F (in Ref. 5; BAH14176)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="L -> M (in Ref. 5; BAH14164)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="V -> F (in Ref. 5; BAH14164)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="T -> P (in Ref. 9; AAF04254)"
FT /evidence="ECO:0000305"
FT CONFLICT 644..647
FT /note="HQCV -> KPNS (in Ref. 9; AAF04254)"
FT /evidence="ECO:0000305"
FT CONFLICT 746
FT /note="H -> R (in Ref. 3; AAO27363)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1011 AA; 111297 MW; 43ED2785E73CD924 CRC64;
MHSMISSVDV KSEVPVGLEP ISPLDLRTDL RMMMPVVDPV VREKQLQQEL LLIQQQQQIQ
KQLLIAEFQK QHENLTRQHQ AQLQEHIKEL LAIKQQQELL EKEQKLEQQR QEQEVERHRR
EQQLPPLRGK DRGRERAVAS TEVKQKLQEF LLSKSATKDT PTNGKNHSVS RHPKLWYTAA
HHTSLDQSSP PLSGTSPSYK YTLPGAQDAK DDFPLRKTAS EPNLKVRSRL KQKVAERRSS
PLLRRKDGNV VTSFKKRMFE VTESSVSSSS PGSGPSSPNN GPTGSVTENE TSVLPPTPHA
EQMVSQQRIL IHEDSMNLLS LYTSPSLPNI TLGLPAVPSQ LNASNSLKEK QKCETQTLRQ
GVPLPGQYGG SIPASSSHPH VTLEGKPPNS SHQALLQHLL LKEQMRQQKL LVAGGVPLHP
QSPLATKERI SPGIRGTHKL PRHRPLNRTQ SAPLPQSTLA QLVIQQQHQQ FLEKQKQYQQ
QIHMNKLLSK SIEQLKQPGS HLEEAEEELQ GDQAMQEDRA PSSGNSTRSD SSACVDDTLG
QVGAVKVKEE PVDSDEDAQI QEMESGEQAA FMQQPFLEPT HTRALSVRQA PLAAVGMDGL
EKHRLVSRTH SSPAASVLPH PAMDRPLQPG SATGIAYDPL MLKHQCVCGN STTHPEHAGR
IQSIWSRLQE TGLLNKCERI QGRKASLEEI QLVHSEHHSL LYGTNPLDGQ KLDPRILLGD
DSQKFFSSLP CGGLGVDSDT IWNELHSSGA ARMAVGCVIE LASKVASGEL KNGFAVVRPP
GHHAEESTAM GFCFFNSVAI TAKYLRDQLN ISKILIVDLD VHHGNGTQQA FYADPSILYI
SLHRYDEGNF FPGSGAPNEV GTGLGEGYNI NIAWTGGLDP PMGDVEYLEA FRTIVKPVAK
EFDPDMVLVS AGFDALEGHT PPLGGYKVTA KCFGHLTKQL MTLADGRVVL ALEGGHDLTA
ICDASEACVN ALLGNELEPL AEDILHQSPN MNAVISLQKI IEIQSMSLKF S
