GenomeNet

Database: UniProt/SWISS-PROT
Entry: HDAC4_MOUSE
LinkDB: HDAC4_MOUSE
Original site: HDAC4_MOUSE 
ID   HDAC4_MOUSE             Reviewed;        1076 AA.
AC   Q6NZM9; Q3TRZ9; Q3U2J3; Q3V3Y4;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   16-JAN-2019, entry version 132.
DE   RecName: Full=Histone deacetylase 4;
DE            Short=HD4;
DE            EC=3.5.1.98;
GN   Name=Hdac4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Dendritic cell, Epididymis, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   [3]
RP   INTERACTION WITH HDAC7.
RX   PubMed=10984530; DOI=10.1073/pnas.97.19.10330;
RA   Downes M., Ordentlich P., Kao H.-Y., Alvarez J.G.A., Evans R.M.;
RT   "Identification of a nuclear domain with deacetylase activity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:10330-10335(2000).
RN   [4]
RP   INTERACTION WITH MYOCD.
RX   PubMed=15601857; DOI=10.1128/MCB.25.1.364-376.2005;
RA   Cao D., Wang Z., Zhang C.L., Oh J., Xing W., Li S., Richardson J.A.,
RA   Wang D.Z., Olson E.N.;
RT   "Modulation of smooth muscle gene expression by association of histone
RT   acetyltransferases and deacetylases with myocardin.";
RL   Mol. Cell. Biol. 25:364-376(2005).
RN   [5]
RP   INTERACTION WITH AHRR.
RX   PubMed=17949687; DOI=10.1016/j.bbrc.2007.09.131;
RA   Oshima M., Mimura J., Yamamoto M., Fujii-Kuriyama Y.;
RT   "Molecular mechanism of transcriptional repression of AhR repressor
RT   involving ANKRA2, HDAC4, and HDAC5.";
RL   Biochem. Biophys. Res. Commun. 364:276-282(2007).
RN   [6]
RP   PHOSPHORYLATION BY CAMK2D.
RX   PubMed=17923476; DOI=10.1074/jbc.M707083200;
RA   Zhang T., Kohlhaas M., Backs J., Mishra S., Phillips W., Dybkova N.,
RA   Chang S., Ling H., Bers D.M., Maier L.S., Olson E.N., Brown J.H.;
RT   "CaMKIIdelta isoforms differentially affect calcium handling but
RT   similarly regulate HDAC/MEF2 transcriptional responses.";
RL   J. Biol. Chem. 282:35078-35087(2007).
RN   [7]
RP   PHOSPHORYLATION AT SER-245 AND SER-465.
RX   PubMed=17468767; DOI=10.1038/nm1573;
RA   Berdeaux R., Goebel N., Banaszynski L., Takemori H., Wandless T.,
RA   Shelton G.D., Montminy M.;
RT   "SIK1 is a class II HDAC kinase that promotes survival of skeletal
RT   myocytes.";
RL   Nat. Med. 13:597-603(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209 AND SER-562, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [10]
RP   INTERACTION WITH DHX36.
RX   PubMed=21590736; DOI=10.1002/jbmr.426;
RA   Kim H.N., Lee J.H., Bae S.C., Ryoo H.M., Kim H.H., Ha H., Lee Z.H.;
RT   "Histone deacetylase inhibitor MS-275 stimulates bone formation in
RT   part by enhancing Dhx36-mediated TNAP transcription.";
RL   J. Bone Miner. Res. 26:2161-2173(2011).
RN   [11]
RP   INTERACTION WITH ZBTB7B.
RX   PubMed=22730529; DOI=10.4049/jimmunol.1201077;
RA   Rui J., Liu H., Zhu X., Cui Y., Liu X.;
RT   "Epigenetic silencing of CD8 genes by ThPOK-mediated deacetylation
RT   during CD4 T cell differentiation.";
RL   J. Immunol. 189:1380-1390(2012).
CC   -!- FUNCTION: Responsible for the deacetylation of lysine residues on
CC       the N-terminal part of the core histones (H2A, H2B, H3 and H4).
CC       Histone deacetylation gives a tag for epigenetic repression and
CC       plays an important role in transcriptional regulation, cell cycle
CC       progression and developmental events. Histone deacetylases act via
CC       the formation of large multiprotein complexes. Involved in muscle
CC       maturation via its interaction with the myocyte enhancer factors
CC       such as MEF2A, MEF2C and MEF2D. Deacetylates HSPA1A and HSPA1A at
CC       'Lys-77' leading to their preferential binding to co-chaperone
CC       STUB1. {ECO:0000250|UniProtKB:P56524}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of an N(6)-acetyl-lysine residue of a histone
CC         to yield a deacetylated histone.; EC=3.5.1.98;
CC   -!- SUBUNIT: Homodimer. Homodimerization via its N-terminal domain (By
CC       similarity). Interacts with HDAC7 (PubMed:10984530). Interacts
CC       with MEF2A, MEF2C, MEF2D, MORC2 and NR2C1. Interacts with a 14-3-3
CC       chaperone protein in a phosphorylation dependent manner. Interacts
CC       with BTBD14B. Interacts with KDM5B. Interacts (via PxLPxI/L motif)
CC       with ANKRA2 (via ankyrin repeats). Interacts with CUL7 (as part of
CC       the 3M complex); negatively regulated by ANKRA2. Interacts with
CC       EP300 in the presence of TFAP2C (By similarity). Interacts with
CC       AHRR (PubMed:17949687). Interacts with MYOCD (PubMed:15601857).
CC       Interacts with HSPA1A and HSPA1B leading to their deacetylation at
CC       'Lys-77' (By similarity). Interacts with ZBTB7B; the interaction
CC       allows the recruitment of HDAC4 on CD8 loci for deacetylation and
CC       possible inhibition of CD8 genes expression (PubMed:22730529).
CC       Interacts with DHX36 (PubMed:21590736).
CC       {ECO:0000250|UniProtKB:P56524, ECO:0000250|UniProtKB:Q99P99,
CC       ECO:0000269|PubMed:10984530, ECO:0000269|PubMed:15601857,
CC       ECO:0000269|PubMed:17949687, ECO:0000269|PubMed:21590736,
CC       ECO:0000269|PubMed:22730529}.
CC   -!- INTERACTION:
CC       P23242:Gja1; NbExp=2; IntAct=EBI-646397, EBI-298630;
CC       Q08775:Runx2; NbExp=3; IntAct=EBI-646397, EBI-903354;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between
CC       the nucleus and the cytoplasm. Upon muscle cells differentiation,
CC       it accumulates in the nuclei of myotubes, suggesting a positive
CC       role of nuclear HDAC4 in muscle differentiation. The export to
CC       cytoplasm depends on the interaction with a 14-3-3 chaperone
CC       protein and is due to its phosphorylation at Ser-245, Ser-465 and
CC       Ser-629 by CaMK4 and SIK1. The nuclear localization probably
CC       depends on sumoylation (By similarity). {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6NZM9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6NZM9-2; Sequence=VSP_023952, VSP_023953;
CC         Note=No experimental confirmation available.;
CC   -!- DOMAIN: The nuclear export sequence mediates the shuttling between
CC       the nucleus and the cytoplasm. {ECO:0000250}.
CC   -!- DOMAIN: The PxLPxI/L motif mediates interaction with ankyrin
CC       repeats of ANKRA2. {ECO:0000250|UniProtKB:P56524}.
CC   -!- PTM: Phosphorylated by CaMK4 at Ser-245, Ser-465 and Ser-629.
CC       Phosphorylation at other residues by CaMK2D is required for the
CC       interaction with 14-3-3. Phosphorylation at Ser-349, within the
CC       PxLPxI/L motif, impairs the binding of ANKRA2 but generates a
CC       high-affinity docking site for 14-3-3 (By similarity).
CC       {ECO:0000250|UniProtKB:P56524}.
CC   -!- PTM: Sumoylation on Lys-556 is promoted by the E3 SUMO-protein
CC       ligase RANBP2, and prevented by phosphorylation by CaMK4.
CC       {ECO:0000269|PubMed:17468767, ECO:0000269|PubMed:17923476}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC       subfamily. {ECO:0000305}.
DR   EMBL; AK029933; BAE43272.1; -; mRNA.
DR   EMBL; AK155250; BAE33147.1; -; mRNA.
DR   EMBL; AK162369; BAE36877.1; -; mRNA.
DR   EMBL; BC066052; AAH66052.1; -; mRNA.
DR   CCDS; CCDS48324.1; -. [Q6NZM9-1]
DR   RefSeq; NP_997108.1; NM_207225.2. [Q6NZM9-1]
DR   RefSeq; XP_017174977.1; XM_017319488.1. [Q6NZM9-1]
DR   UniGene; Mm.318567; -.
DR   ProteinModelPortal; Q6NZM9; -.
DR   SMR; Q6NZM9; -.
DR   BioGrid; 229009; 15.
DR   CORUM; Q6NZM9; -.
DR   DIP; DIP-36317N; -.
DR   IntAct; Q6NZM9; 10.
DR   MINT; Q6NZM9; -.
DR   STRING; 10090.ENSMUSP00000008995; -.
DR   ChEMBL; CHEMBL3832944; -.
DR   iPTMnet; Q6NZM9; -.
DR   PhosphoSitePlus; Q6NZM9; -.
DR   EPD; Q6NZM9; -.
DR   jPOST; Q6NZM9; -.
DR   PaxDb; Q6NZM9; -.
DR   PeptideAtlas; Q6NZM9; -.
DR   PRIDE; Q6NZM9; -.
DR   Ensembl; ENSMUST00000008995; ENSMUSP00000008995; ENSMUSG00000026313. [Q6NZM9-1]
DR   Ensembl; ENSMUST00000097644; ENSMUSP00000095249; ENSMUSG00000026313. [Q6NZM9-1]
DR   GeneID; 208727; -.
DR   KEGG; mmu:208727; -.
DR   UCSC; uc007cbe.2; mouse. [Q6NZM9-2]
DR   UCSC; uc007cbf.2; mouse. [Q6NZM9-1]
DR   CTD; 9759; -.
DR   MGI; MGI:3036234; Hdac4.
DR   eggNOG; KOG1343; Eukaryota.
DR   eggNOG; COG0123; LUCA.
DR   GeneTree; ENSGT00940000157440; -.
DR   HOGENOM; HOG000232065; -.
DR   HOVERGEN; HBG057100; -.
DR   InParanoid; Q6NZM9; -.
DR   KO; K11406; -.
DR   OMA; VEAQKCE; -.
DR   OrthoDB; 1484694at2759; -.
DR   PhylomeDB; Q6NZM9; -.
DR   TreeFam; TF106174; -.
DR   Reactome; R-MMU-4090294; SUMOylation of intracellular receptors.
DR   Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR   Reactome; R-MMU-8951936; RUNX3 regulates p14-ARF.
DR   ChiTaRS; Hdac4; mouse.
DR   PRO; PR:Q6NZM9; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   Bgee; ENSMUSG00000026313; Expressed in 240 organ(s), highest expression level in ear vesicle.
DR   CleanEx; MM_HDAC4; -.
DR   ExpressionAtlas; Q6NZM9; baseline and differential.
DR   Genevisible; Q6NZM9; MM.
DR   GO; GO:0031672; C:A band; ISO:MGI.
DR   GO; GO:0042641; C:actomyosin; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0000118; C:histone deacetylase complex; ISO:MGI.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0030017; C:sarcomere; ISO:MGI.
DR   GO; GO:0017053; C:transcriptional repressor complex; ISO:MGI.
DR   GO; GO:0030018; C:Z disc; ISO:MGI.
DR   GO; GO:0033613; F:activating transcription factor binding; ISO:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0004407; F:histone deacetylase activity; ISO:MGI.
DR   GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
DR   GO; GO:0030955; F:potassium ion binding; ISO:MGI.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; ISO:MGI.
DR   GO; GO:0033558; F:protein deacetylase activity; IDA:MGI.
DR   GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR   GO; GO:0070491; F:repressing transcription factor binding; ISO:MGI.
DR   GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0001085; F:RNA polymerase II transcription factor binding; ISO:MGI.
DR   GO; GO:0019789; F:SUMO transferase activity; ISO:MGI.
DR   GO; GO:0003714; F:transcription corepressor activity; IGI:MGI.
DR   GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR   GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR   GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IEA:Ensembl.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR   GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
DR   GO; GO:0016575; P:histone deacetylation; ISO:MGI.
DR   GO; GO:0070932; P:histone H3 deacetylation; ISO:MGI.
DR   GO; GO:0070933; P:histone H4 deacetylation; ISO:MGI.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IDA:MGI.
DR   GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO:MGI.
DR   GO; GO:0045820; P:negative regulation of glycolytic process; IMP:BHF-UCL.
DR   GO; GO:0010832; P:negative regulation of myotube differentiation; ISO:MGI.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:MGI.
DR   GO; GO:1902894; P:negative regulation of pri-miRNA transcription by RNA polymerase II; IMP:BHF-UCL.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR   GO; GO:0002076; P:osteoblast development; IMP:MGI.
DR   GO; GO:0034983; P:peptidyl-lysine deacetylation; ISO:MGI.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; ISO:MGI.
DR   GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR   GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISO:MGI.
DR   GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
DR   GO; GO:0033235; P:positive regulation of protein sumoylation; ISS:UniProtKB.
DR   GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; ISO:MGI.
DR   GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:MGI.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:BHF-UCL.
DR   GO; GO:0006476; P:protein deacetylation; ISO:MGI.
DR   GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; IMP:MGI.
DR   GO; GO:0040029; P:regulation of gene expression, epigenetic; ISO:MGI.
DR   GO; GO:0043393; P:regulation of protein binding; ISO:MGI.
DR   GO; GO:0048742; P:regulation of skeletal muscle fiber development; IGI:MGI.
DR   GO; GO:0051153; P:regulation of striated muscle cell differentiation; IGI:MGI.
DR   GO; GO:0014894; P:response to denervation involved in regulation of muscle adaptation; IMP:BHF-UCL.
DR   GO; GO:0042493; P:response to drug; ISO:MGI.
DR   GO; GO:0070555; P:response to interleukin-1; ISO:MGI.
DR   GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR   Gene3D; 3.40.800.20; -; 1.
DR   InterPro; IPR033660; HDAC4.
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   PANTHER; PTHR10625; PTHR10625; 1.
DR   PANTHER; PTHR10625:SF100; PTHR10625:SF100; 1.
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; Coiled coil;
KW   Complete proteome; Cytoplasm; Hydrolase; Isopeptide bond;
KW   Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW   Transcription; Transcription regulation; Ubl conjugation; Zinc.
FT   CHAIN         1   1076       Histone deacetylase 4.
FT                                /FTId=PRO_0000281033.
FT   REGION      117    312       Interaction with MEF2A. {ECO:0000250}.
FT   REGION      652   1076       Histone deacetylase. {ECO:0000250}.
FT   COILED       66    169       {ECO:0000255}.
FT   MOTIF       348    353       PxLPxI/L motif; mediates interaction with
FT                                ANKRA2 and 14-3-3 proteins.
FT                                {ECO:0000250|UniProtKB:P56524}.
FT   MOTIF      1043   1076       Nuclear export signal. {ECO:0000250}.
FT   COMPBIAS    464    499       Gln-rich.
FT   COMPBIAS    561    568       Poly-Glu.
FT   ACT_SITE    795    795       {ECO:0000250}.
FT   METAL       664    664       Zinc. {ECO:0000250}.
FT   METAL       666    666       Zinc. {ECO:0000250}.
FT   METAL       672    672       Zinc. {ECO:0000250}.
FT   METAL       743    743       Zinc. {ECO:0000250}.
FT   MOD_RES     209    209       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     245    245       Phosphoserine; by CaMK4 and SIK1.
FT                                {ECO:0000269|PubMed:17468767}.
FT   MOD_RES     349    349       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P56524}.
FT   MOD_RES     465    465       Phosphoserine; by CaMK4 and SIK1.
FT                                {ECO:0000244|PubMed:19131326,
FT                                ECO:0000269|PubMed:17468767}.
FT   MOD_RES     562    562       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     629    629       Phosphoserine; by CaMK4.
FT                                {ECO:0000250|UniProtKB:P56524}.
FT   MOD_RES     630    630       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P56524}.
FT   CROSSLNK    556    556       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT                                {ECO:0000250}.
FT   VAR_SEQ       1    171       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_023952.
FT   VAR_SEQ     732    732       S -> SKKLLG (in isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_023953.
FT   CONFLICT    569    569       A -> S (in Ref. 1; BAE33147).
FT                                {ECO:0000305}.
FT   CONFLICT    904    904       R -> K (in Ref. 1; BAE33147).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1076 AA;  118562 MW;  A3CCC3CCCBB903A0 CRC64;
     MSSQSHPDGL SGRDQPVELL NPARVNHMPS TVDVATALPL QVAPTAVPMD LRLDHQFSLP
     LEPALREQQL QQELLALKQK QQIQRQILIA EFQRQHEQLS RQHEAQLHEH IKQQQEMLAM
     KHQQELLEHQ RKLERHRQEQ ELEKQHREQK LQQLKNKEKG KESAVASTEV KMKLQEFVLN
     KKKALAHRNL NHCISSDPRY WYGKTQHSSL DQSSPPQSGV SASYNHPVLG MYDAKDDFPL
     RKTASEPNLK LRSRLKQKVA ERRSSPLLRR KDGPVATALK KRPLDVTDSA CSSAPGSGPS
     SPNSSSGNVS TENGIAPTVP SAPAETSLAH RLVTREGSVA PLPLYTSPSL PNITLGLPAT
     GPAAGAAGQQ DAERLALPAL QQRILFPGTH LTPYLSTSPL ERDGAAAHNP LLQHMVLLEQ
     PPTQTPLVTG LGALPLHSQS LVGADRVSPS IHKLRQHRPL GRTQSAPLPQ NAQALQHLVI
     QQQHQQFLEK HKQQFQQQQL HLSKIISKPS EPPRQPESHP EETEEELREH QALLDEPYLD
     RLPGQKEPSL AGVQVKQEPI ESEEEEAEAT RETEPGQRPA TEQELLFRQQ ALLLEQQRIH
     QLRNYQASME AAGIPVSFGS HRPLSRAQSS PASATFPMSV QEPPTKPRFT TGLVYDTLML
     KHQCTCGNTN SHPEHAGRIQ SIWSRLQETG LRGKCECIRG RKATLEELQT VHSEAHTLLY
     GTNPLNRQKL DSSLTSVFVR LPCGGVGVDS DTIWNEVHSS GAARLAVGCV VELVFKVATG
     ELKNGFAVVR PPGHHAEEST PMGFCYFNSV AVAAKLLQQR LNVSKILIVD WDVHHGNGTQ
     QAFYNDPNVL YMSLHRYDDG NFFPGSGAPD EVGTGPGVGF NVNMAFTGGL EPPMGDAEYL
     AAFRTVVMPI ANEFAPDVVL VSSGFDAVEG HPTPLGGYNL SAKCFGYLTK QLMGLAGGRL
     VLALEGGHDL TAICDASEAC VSALLGNELE PLPEKVLHQR PNANAVHSME KVMDIHSKYW
     RCLQRLSSTV GHSLIEAQKC EKEEAETVTA MASLSVGVKP AEKRSEEEPM EEEPPL
//
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