GENTAUR Molecular Products.

 HDAC9_MOUSE             Reviewed;         588 AA.
 Q99N13; Q4QQN7; Q8R4Y6; Q9EPT2;
 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
 20-MAR-2007, sequence version 2.
 28-MAR-2018, entry version 147.
 RecName: Full=Histone deacetylase 9;
          Short=HD9;
          EC=3.5.1.98;
 AltName: Full=Histone deacetylase 7B;
          Short=HD7b;
 AltName: Full=Histone deacetylase-related protein;
 AltName: Full=MEF2-interacting transcription repressor MITR;
 Name=Hdac9; Synonyms=Hdac7b, Hdrp, Mitr;
 Mus musculus (Mouse).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
 Muroidea; Muridae; Murinae; Mus; Mus.
 NCBI_TaxID=10090;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), HOMODIMERIZATION, INTERACTION
 WITH CTBP1; HDAC1; HDAC3; HDAC4 AND HDAC5, AND MUTAGENESIS OF
 25-ASP-LEU-26.
 STRAIN=NIH Swiss; TISSUE=Embryonic heart;
 PubMed=11022042; DOI=10.1074/jbc.M007364200;
 Zhang C.L., McKinsey T.A., Lu J.R., Olson E.N.;
 "Association of COOH-terminal-binding protein (CtBP) and MEF2-
 interacting transcription repressor (MITR) contributes to
 transcriptional repression of the MEF2 transcription factor.";
 J. Biol. Chem. 276:35-39(2001).
 [2]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
 STRAIN=Swiss Webster / NIH;
 Zhou X., Richon V.M., Rifkind R.A., Marks P.A.;
 "Cloning of the mouse HDRP cDNA.";
 Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
 STRAIN=C57BL/6J; TISSUE=Retina;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA
 project: the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [4]
 FUNCTION, PHOSPHORYLATION AT SER-220 AND SER-450, TISSUE SPECIFICITY,
 DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
 PubMed=11390982; DOI=10.1073/pnas.131198498;
 Zhang C.L., McKinsey T.A., Olson E.N.;
 "The transcriptional corepressor MITR is a signal-responsive inhibitor
 of myogenesis.";
 Proc. Natl. Acad. Sci. U.S.A. 98:7354-7359(2001).
 [5]
 PHOSPHORYLATION AT SER-220 AND SER-450, FUNCTION, AND DISRUPTION
 PHENOTYPE.
 PubMed=12202037; DOI=10.1016/S0092-8674(02)00861-9;
 Zhang C.L., McKinsey T.A., Chang S., Antos C.L., Hill J.A.,
 Olson E.N.;
 "Class II histone deacetylases act as signal-responsive repressors of
 cardiac hypertrophy.";
 Cell 110:479-488(2002).
 [6]
 PHOSPHORYLATION AT SER-240, AND SUBCELLULAR LOCATION.
 PubMed=15546868; DOI=10.1074/jbc.M411894200;
 Deng X., Ewton D.Z., Mercer S.E., Friedman E.;
 "Mirk/dyrk1B decreases the nuclear accumulation of class II histone
 deacetylases during skeletal muscle differentiation.";
 J. Biol. Chem. 280:4894-4905(2005).
 [7]
 FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DOWN-REGULATION BY
 DENERVATION, INTERACTION WITH HDAC1 AND HDAC3, AND SUBCELLULAR
 LOCATION.
 PubMed=15711539; DOI=10.1038/nn1408;
 Mejat A., Ramond F., Bassel-Duby R., Khochbin S., Olson E.N.,
 Schaeffer L.;
 "Histone deacetylase 9 couples neuronal activity to muscle chromatin
 acetylation and gene expression.";
 Nat. Neurosci. 8:313-321(2005).
 [8]
 DOWN-REGULATION BY NEURONAL APOPTOSIS, FUNCTION, AND INTERACTION WITH
 HDAC1 AND MAPK10.
 PubMed=16611996; DOI=10.1128/MCB.26.9.3550-3564.2006;
 Morrison B.E., Majdzadeh N., Zhang X., Lyles A., Bassel-Duby R.,
 Olson E.N., D'Mello S.R.;
 "Neuroprotection by histone deacetylase-related protein.";
 Mol. Cell. Biol. 26:3550-3564(2006).
 [9]
 INDUCTION BY MEF2, AND DEVELOPMENTAL STAGE.
 PubMed=17101791; DOI=10.1128/MCB.01415-06;
 Haberland M., Arnold M.A., McAnally J., Phan D., Kim Y., Olson E.N.;
 "Regulation of HDAC9 gene expression by MEF2 establishes a negative-
 feedback loop in the transcriptional circuitry of muscle
 differentiation.";
 Mol. Cell. Biol. 27:518-525(2007).
 [10]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552, AND IDENTIFICATION
 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Brain;
 PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
 Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
 Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
 "A tissue-specific atlas of mouse protein phosphorylation and
 expression.";
 Cell 143:1174-1189(2010).
 [11]
 X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 139-158 IN COMPLEX WITH MEF2
 AND DNA.
 PubMed=15567413; DOI=10.1016/j.jmb.2004.10.033;
 Han A., He J., Wu Y., Liu J.O., Chen L.;
 "Mechanism of recruitment of class II histone deacetylases by myocyte
 enhancer factor-2.";
 J. Mol. Biol. 345:91-102(2005).
 -!- FUNCTION: Devoided of intrinsic deacetylase activity, promotes the
     deacetylation of lysine residues on the N-terminal part of the
     core histones (H2A, H2B, H3 and H4) by recruiting HDAC1 and HDAC3.
     Histone deacetylation gives a tag for epigenetic repression and
     plays an important role in transcriptional regulation, cell cycle
     progression and developmental events. Represses MEF2-dependent
     transcription, inhibits skeletal myogenesis and may be involved in
     heart development. Protects neurons from apoptosis, both by
     inhibiting JUN phosphorylation by MAPK10 and by repressing JUN
     transcription via HDAC1 recruitment to JUN promoter.
     {ECO:0000269|PubMed:11390982, ECO:0000269|PubMed:12202037,
     ECO:0000269|PubMed:15711539, ECO:0000269|PubMed:16611996}.
 -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
     a histone to yield a deacetylated histone.
 -!- SUBUNIT: Homodimer. Interacts with ETV6 (By similarity). Interacts
     with MEF2, HDAC1, HDAC3, HDAC4, HDAC5, CTBP1 and MAPK10. The
     phosphorylated form interacts with 14-3-3. Interacts with FOXP3 in
     the absence of T-cell stimulation (By similarity).
     {ECO:0000250|UniProtKB:Q9UKV0, ECO:0000269|PubMed:11022042,
     ECO:0000269|PubMed:15567413, ECO:0000269|PubMed:15711539,
     ECO:0000269|PubMed:16611996}.
 -!- INTERACTION:
     P60335:Pcbp1; NbExp=6; IntAct=EBI-645361, EBI-309059;
     Q3TKT4:Smarca4; NbExp=3; IntAct=EBI-645361, EBI-1210244;
 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11390982,
     ECO:0000269|PubMed:15546868, ECO:0000269|PubMed:15711539}.
 -!- ALTERNATIVE PRODUCTS:
     Event=Alternative splicing; Named isoforms=3;
     Name=1;
       IsoId=Q99N13-1; Sequence=Displayed;
     Name=2; Synonyms=Hdrpa;
       IsoId=Q99N13-2; Sequence=VSP_023769;
       Note=No experimental confirmation available.;
     Name=3;
       IsoId=Q99N13-3; Sequence=VSP_029173;
 -!- TISSUE SPECIFICITY: Expressed at high levels in heart, brain and
     spleen. Expressed in skeletal muscle.
     {ECO:0000269|PubMed:11390982, ECO:0000269|PubMed:15711539}.
 -!- DEVELOPMENTAL STAGE: At E10.5, expressed in heart, skeletal muscle
     and neural lineages. At E11.5, expressed in heart, dorsal root
     ganglia and neural tube. At E12.5, expressed in heart, skeletal
     muscle, dorsal root ganglia, neural tube and retina. Strongly up-
     regulated in muscle between E14 and E19 as a result of motor
     innervation. {ECO:0000269|PubMed:11390982,
     ECO:0000269|PubMed:15711539, ECO:0000269|PubMed:17101791}.
 -!- INDUCTION: By MEF2 during muscle differentiation. Down-regulated
     by muscle denervation. Down-regulated by trichostatin A or sodium
     butyrate, and during neuronal apoptosis (at protein level).
     {ECO:0000269|PubMed:17101791}.
 -!- PTM: Sumoylated. {ECO:0000250}.
 -!- PTM: Phosphorylated on Ser-220 and Ser-450; which promotes 14-3-3-
     binding, impairs interaction with MEF2, and antagonizes
     antimyogenic activity. Phosphorylated on Ser-240 by DYRK1B; which
     impairs nuclear accumulation. Phosphorylated by the PKC kinases
     PKN1 and PKN2, impairing nuclear import.
     {ECO:0000269|PubMed:11390982, ECO:0000269|PubMed:12202037,
     ECO:0000269|PubMed:15546868}.
 -!- DISRUPTION PHENOTYPE: Mice do not present any abnormality at early
     age but develop cardiac hypertrophy by eight months of age.
     {ECO:0000269|PubMed:12202037}.
 -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
     subfamily. {ECO:0000305}.
 -----------------------------------------------------------------------
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 EMBL; AF324492; AAG48332.1; -; mRNA.
 EMBL; AF235053; AAK15027.1; -; mRNA.
 EMBL; AF279371; AAL86358.1; -; mRNA.
 EMBL; BC098187; AAH98187.1; -; mRNA.
 CCDS; CCDS36432.1; -. [Q99N13-1]
 RefSeq; NP_077038.2; NM_024124.3.
 UniGene; Mm.310551; -.
 UniGene; Mm.483009; -.
 PDB; 1TQE; X-ray; 2.70 A; X/Y=139-158.
 PDBsum; 1TQE; -.
 ProteinModelPortal; Q99N13; -.
 SMR; Q99N13; -.
 BioGrid; 219748; 9.
 DIP; DIP-41905N; -.
 ELM; Q99N13; -.
 IntAct; Q99N13; 7.
 STRING; 10090.ENSMUSP00000106443; -.
 ChEMBL; CHEMBL3832944; -.
 iPTMnet; Q99N13; -.
 PhosphoSitePlus; Q99N13; -.
 PaxDb; Q99N13; -.
 PeptideAtlas; Q99N13; -.
 PRIDE; Q99N13; -.
 GeneID; 79221; -.
 KEGG; mmu:79221; -.
 UCSC; uc007nja.1; mouse. [Q99N13-3]
 UCSC; uc007njb.1; mouse. [Q99N13-2]
 UCSC; uc007njc.2; mouse. [Q99N13-1]
 CTD; 9734; -.
 MGI; MGI:1931221; Hdac9.
 eggNOG; KOG1343; Eukaryota.
 eggNOG; COG0123; LUCA.
 HOGENOM; HOG000232065; -.
 HOVERGEN; HBG057100; -.
 InParanoid; Q99N13; -.
 KO; K11409; -.
 PhylomeDB; Q99N13; -.
 TreeFam; TF106174; -.
 EvolutionaryTrace; Q99N13; -.
 PRO; PR:Q99N13; -.
 Proteomes; UP000000589; Unplaced.
 CleanEx; MM_HDAC9; -.
 GO; GO:0005737; C:cytoplasm; ISO:MGI.
 GO; GO:0000118; C:histone deacetylase complex; TAS:UniProtKB.
 GO; GO:0035097; C:histone methyltransferase complex; IDA:BHF-UCL.
 GO; GO:0005634; C:nucleus; ISO:MGI.
 GO; GO:0005667; C:transcription factor complex; ISO:MGI.
 GO; GO:0004407; F:histone deacetylase activity; TAS:UniProtKB.
 GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
 GO; GO:0033558; F:protein deacetylase activity; ISO:MGI.
 GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
 GO; GO:0070491; F:repressing transcription factor binding; IPI:BHF-UCL.
 GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
 GO; GO:0008134; F:transcription factor binding; ISO:MGI.
 GO; GO:0042113; P:B cell activation; TAS:UniProtKB.
 GO; GO:0030183; P:B cell differentiation; TAS:UniProtKB.
 GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI.
 GO; GO:0006325; P:chromatin organization; TAS:UniProtKB.
 GO; GO:0007507; P:heart development; IGI:MGI.
 GO; GO:0016575; P:histone deacetylation; ISO:MGI.
 GO; GO:0070932; P:histone H3 deacetylation; ISO:MGI.
 GO; GO:0070933; P:histone H4 deacetylation; ISO:MGI.
 GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
 GO; GO:0045843; P:negative regulation of striated muscle tissue development; TAS:UniProtKB.
 GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
 GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
 GO; GO:0007399; P:nervous system development; TAS:UniProtKB.
 GO; GO:0034983; P:peptidyl-lysine deacetylation; ISO:MGI.
 GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; ISO:MGI.
 GO; GO:0048742; P:regulation of skeletal muscle fiber development; IGI:MGI.
 GO; GO:0051153; P:regulation of striated muscle cell differentiation; IGI:MGI.
 GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
 InterPro; IPR024643; Hist_deacetylase_Gln_rich_N.
 Pfam; PF12203; HDAC4_Gln; 1.
 1: Evidence at protein level;
 3D-structure; Alternative splicing; Chromatin regulator;
 Complete proteome; Hydrolase; Nucleus; Phosphoprotein;
 Reference proteome; Repressor; Transcription;
 Transcription regulation; Ubl conjugation.
 CHAIN         1    588       Histone deacetylase 9.
                              /FTId=PRO_0000114711.
 REGION       23     27       Interaction with CTBP1.
                              {ECO:0000269|PubMed:11022042}.
 REGION      136    154       Interaction with MEF2.
 REGION      175    343       Interaction with MAPK10.
                              {ECO:0000269|PubMed:16611996}.
 REGION      218    261       Interaction with ETV6. {ECO:0000250}.
 MOD_RES      22     22       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q9UKV0}.
 MOD_RES     220    220       Phosphoserine.
                              {ECO:0000269|PubMed:11390982,
                              ECO:0000269|PubMed:12202037}.
 MOD_RES     240    240       Phosphoserine; by DYRK1B.
                              {ECO:0000269|PubMed:15546868}.
 MOD_RES     450    450       Phosphoserine.
                              {ECO:0000269|PubMed:11390982,
                              ECO:0000269|PubMed:12202037}.
 MOD_RES     552    552       Phosphoserine.
                              {ECO:0000244|PubMed:21183079}.
 VAR_SEQ     177    178       Missing (in isoform 3).
                              {ECO:0000303|PubMed:11022042}.
                              /FTId=VSP_029173.
 VAR_SEQ     219    262       Missing (in isoform 2).
                              {ECO:0000303|Ref.2}.
                              /FTId=VSP_023769.
 MUTAGEN      25     26       DL->AS: Abolishes binding to CTBP1 and
                              impairs function in transcription
                              repression.
                              {ECO:0000269|PubMed:11022042}.
 CONFLICT    120    120       R -> K (in Ref. 2; AAK15027/AAL86358).
                              {ECO:0000305}.
 CONFLICT    136    136       R -> K (in Ref. 2; AAK15027/AAL86358).
                              {ECO:0000305}.
 CONFLICT    388    388       N -> T (in Ref. 3; AAH98187).
                              {ECO:0000305}.
 CONFLICT    523    523       N -> T (in Ref. 1; AAG48332).
                              {ECO:0000305}.
 HELIX       143    153       {ECO:0000244|PDB:1TQE}.
 SEQUENCE   588 AA;  65687 MW;  4ED7FA9F02BD4621 CRC64;
 MHSMISSVDV KSEVPMGLEP ISPLDLRTDL RMMMPVVDPV VREKQLQQEL LLIQQQQQIQ
 KQLLIAEFQK QHENLTRQHQ AQLQEHIKEL LAIKQQQELL EKEQKLEQQR QEQEVERHRR
 EQQLPPLRGK DRGRERAVAS TEVKQKLQEF LLSKSATKDT PTNGKNHSVG RHPKLWYTAA
 HHTSLDQSSP PLSGTSPSYK YTLPGAQDSK DDFPLRKTAS EPNLKVRSRL KQKVAERRSS
 PLLRRKDGNL VTSFKKRVFE VAESSVSSSS PGSGPSSPNN GPAGNVTENE ASALPPTPHP
 EQLVPQQRIL IHEDSMNLLS LYTSPSLPNI TLGLPAVPSP LNASNSLKDK QKCETQMLRQ
 GVPLPSQYGS SIAASSSHVH VAMEGKPNSS HQALLQHLLL KEQMRQQKLL VAGGVPLHPQ
 SPLATKERIS PGIRGTHKLP RHRPLNRTQS APLPQSTLAQ LVIQQQHQQF LEKQKQYQQQ
 IHMNKLLSKS IEQLKQPGSH LEEAEEELQG DQSMEDRAAS KDNSARSDSS ACVEDTLGQV
 GAVKVKEEPV DSDEDAQIQE MECGEQAAFM QQVIGKDLAP GFVIKVII

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