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Histone deacetylase 5 (HD5) (EC 3.5.1.98) (Histone deacetylase mHDA1)

 HDAC5_MOUSE             Reviewed;        1113 AA.
Q9Z2V6; Q9JL73;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 2.
22-NOV-2017, entry version 144.
RecName: Full=Histone deacetylase 5;
Short=HD5;
EC=3.5.1.98;
AltName: Full=Histone deacetylase mHDA1;
Name=Hdac5;
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].
STRAIN=C57BL/6J; TISSUE=Fetus;
PubMed=9891014; DOI=10.1074/jbc.274.4.2440;
Verdel A., Khochbin S.;
"Identification of a new family of higher eukaryotic histone
deacetylases. Coordinate expression of differentiation-dependent
chromatin modifiers.";
J. Biol. Chem. 274:2440-2445(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH NCOR2.
STRAIN=C57BL/6J;
PubMed=10640276;
Kao H.-Y., Downes M., Ordentlich P., Evans R.M.;
"Isolation of a novel histone deacetylase reveals that class I and
class II deacetylases promote SMRT-mediated repression.";
Genes Dev. 14:55-66(2000).
[3]
INTERACTION WITH HDAC7, NUCLEAR EXPORT, AND MUTAGENESIS OF HIS-824 AND
HIS-884.
PubMed=10984530; DOI=10.1073/pnas.97.19.10330;
Downes M., Ordentlich P., Kao H.-Y., Alvarez J.G.A., Evans R.M.;
"Identification of a nuclear domain with deacetylase activity.";
Proc. Natl. Acad. Sci. U.S.A. 97:10330-10335(2000).
[4]
INTERACTION WITH CTBP1 AND HDAC9.
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).
[5]
INTERACTION WITH PHB2.
PubMed=15140878; DOI=10.1074/jbc.M312300200;
Kurtev V., Margueron R., Kroboth K., Ogris E., Cavailles V.,
Seiser C.;
"Transcriptional regulation by the repressor of estrogen receptor
activity via recruitment of histone deacetylases.";
J. Biol. Chem. 279:24834-24843(2004).
[6]
INTERACTION WITH NRIP1.
PubMed=15060175; DOI=10.1093/nar/gkh524;
Castet A., Boulahtouf A., Versini G., Bonnet S., Augereau P.,
Vignon F., Khochbin S., Jalaguier S., Cavailles V.;
"Multiple domains of the receptor-interacting protein 140 contribute
to transcription inhibition.";
Nucleic Acids Res. 32:1957-1966(2004).
[7]
INTERACTION WITH MYOCD.
PubMed=15601857; DOI=10.1128/MCB.25.1.364-376.2005;
Cao D., Wang Z., Zhang C.L., Oh J., Xing W., Li S., Richardson J.A.,
Wang D.Z., Olson E.N.;
"Modulation of smooth muscle gene expression by association of histone
acetyltransferases and deacetylases with myocardin.";
Mol. Cell. Biol. 25:364-376(2005).
[8]
PHOSPHORYLATION AT SER-250 AND SER-488, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF SER-250 AND SER-488.
PubMed=17468767; DOI=10.1038/nm1573;
Berdeaux R., Goebel N., Banaszynski L., Takemori H., Wandless T.,
Shelton G.D., Montminy M.;
"SIK1 is a class II HDAC kinase that promotes survival of skeletal
myocytes.";
Nat. Med. 13:597-603(2007).
[9]
INTERACTION WITH AHRR.
PubMed=17949687; DOI=10.1016/j.bbrc.2007.09.131;
Oshima M., Mimura J., Yamamoto M., Fujii-Kuriyama Y.;
"Molecular mechanism of transcriptional repression of AhR repressor
involving ANKRA2, HDAC4, and HDAC5.";
Biochem. Biophys. Res. Commun. 364:276-282(2007).
[10]
INTERACTION WITH GRK5, AND PHOSPHORYLATION.
PubMed=18711143; DOI=10.1073/pnas.0803153105;
Martini J.S., Raake P., Vinge L.E., DeGeorge B.R. Jr., Chuprun J.K.,
Harris D.M., Gao E., Eckhart A.D., Pitcher J.A., Koch W.J.;
"Uncovering G protein-coupled receptor kinase-5 as a histone
deacetylase kinase in the nucleus of cardiomyocytes.";
Proc. Natl. Acad. Sci. U.S.A. 105:12457-12462(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, and Lung;
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).
[12]
PHOSPHORYLATION AT SER-250 AND SER-488, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF SER-250 AND SER-488.
PubMed=21454484; DOI=10.1074/jbc.M110.199372;
Zhao J.X., Yue W.F., Zhu M.J., Du M.;
"AMP-activated protein kinase regulates beta-catenin transcription via
histone deacetylase 5.";
J. Biol. Chem. 286:16426-16434(2011).
-!- FUNCTION: Responsible for the deacetylation of lysine residues on
the N-terminal part of the core histones (H2A, H2B, H3 and H4).
Histone deacetylation gives a tag for epigenetic repression and
plays an important role in transcriptional regulation, cell cycle
progression and developmental events. Histone deacetylases act via
the formation of large multiprotein complexes. Involved in muscle
maturation by repressing transcription of myocyte enhancer MEF2C.
During muscle differentiation, it shuttles into the cytoplasm,
allowing the expression of myocyte enhancer factors (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
a histone to yield a deacetylated histone.
-!- SUBUNIT: Interacts with AHRR, BAHD1, BCOR, HDAC7, HDAC9, CTBP1,
MEF2C, NCOR2, NRIP1, PHB2 and a 14-3-3 chaperone protein.
Interacts with BCL6, DDIT3/CHOP, GRK5, KDM5B and MYOCD. Interacts
with EP300 in the presence of TFAP2C. Interacts with ANKRA2.
Interacts with CUL7 (as part of the 3M complex); negatively
regulated by ANKRA2. {ECO:0000250|UniProtKB:Q9UQL6,
ECO:0000269|PubMed:10640276, ECO:0000269|PubMed:10984530,
ECO:0000269|PubMed:11022042, ECO:0000269|PubMed:15060175,
ECO:0000269|PubMed:15140878, ECO:0000269|PubMed:15601857,
ECO:0000269|PubMed:17949687, ECO:0000269|PubMed:18711143}.
-!- INTERACTION:
P23242:Gja1; NbExp=2; IntAct=EBI-645339, EBI-298630;
Q64104:Nr2e1; NbExp=3; IntAct=EBI-645339, EBI-15658561;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between
the nucleus and the cytoplasm. In muscle cells, it shuttles into
the cytoplasm during myocyte differentiation. The export to
cytoplasm depends on the interaction with a 14-3-3 chaperone
protein and is due to its phosphorylation at Ser-250 and Ser-488
by AMPK, CaMK1 and SIK1.
-!- DOMAIN: The nuclear export sequence mediates the shuttling between
the nucleus and the cytoplasm.
-!- PTM: Phosphorylated by AMPK, CaMK1, SIK1 and PRKD1 at Ser-250 and
Ser-488. The phosphorylation is required for the export to the
cytoplasm and inhibition. Phosphorylated by the PKC kinases PKN1
and PKN2, impairing nuclear import (By similarity). Phosphorylated
by GRK5, leading to nuclear export of HDAC5 and allowing MEF2-
mediated transcription. {ECO:0000250, ECO:0000269|PubMed:17468767,
ECO:0000269|PubMed:18711143, ECO:0000269|PubMed:21454484}.
-!- PTM: Ubiquitinated. Polyubiquitination however does not lead to
its degradation (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF006602; AAD09834.2; -; mRNA.
EMBL; AF207748; AAF31418.1; -; mRNA.
UniGene; Mm.22665; -.
ProteinModelPortal; Q9Z2V6; -.
SMR; Q9Z2V6; -.
CORUM; Q9Z2V6; -.
DIP; DIP-40855N; -.
ELM; Q9Z2V6; -.
IntAct; Q9Z2V6; 6.
MINT; MINT-125422; -.
STRING; 10090.ENSMUSP00000102770; -.
BindingDB; Q9Z2V6; -.
ChEMBL; CHEMBL2768; -.
iPTMnet; Q9Z2V6; -.
PhosphoSitePlus; Q9Z2V6; -.
MaxQB; Q9Z2V6; -.
PaxDb; Q9Z2V6; -.
PRIDE; Q9Z2V6; -.
MGI; MGI:1333784; Hdac5.
eggNOG; KOG1343; Eukaryota.
eggNOG; COG0123; LUCA.
HOVERGEN; HBG057100; -.
InParanoid; Q9Z2V6; -.
ChiTaRS; Hdac5; mouse.
PRO; PR:Q9Z2V6; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_HDAC5; -.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0000118; C:histone deacetylase complex; TAS:UniProtKB.
GO; GO:0016604; C:nuclear body; IDA:MGI.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0016607; C:nuclear speck; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0090571; C:RNA polymerase II transcription repressor complex; IDA:BHF-UCL.
GO; GO:0001047; F:core promoter binding; ISO:MGI.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0004407; F:histone deacetylase activity; ISO:MGI.
GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
GO; GO:0033558; F:protein deacetylase activity; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
GO; GO:0070491; F:repressing transcription factor binding; ISO:MGI.
GO; GO:0001226; F:RNA polymerase II transcription corepressor binding; IPI:BHF-UCL.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; IPI:BHF-UCL.
GO; GO:0001025; F:RNA polymerase III transcription factor binding; ISO:MGI.
GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IMP:UniProtKB.
GO; GO:0042113; P:B cell activation; TAS:UniProtKB.
GO; GO:0030183; P:B cell differentiation; TAS:UniProtKB.
GO; GO:0071498; P:cellular response to fluid shear stress; IDA:UniProtKB.
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:0006954; P:inflammatory response; TAS:UniProtKB.
GO; GO:0033555; P:multicellular organismal response to stress; IMP:MGI.
GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; ISO:MGI.
GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
GO; GO:0010832; P:negative regulation of myotube differentiation; ISO:MGI.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:MGI.
GO; GO:0045843; P:negative regulation of striated muscle tissue development; TAS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; 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:0002076; P:osteoblast development; IMP:MGI.
GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IMP:BHF-UCL.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; ISO:MGI.
GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0006476; P:protein deacetylation; ISO:MGI.
GO; GO:0040029; P:regulation of gene expression, epigenetic; ISO:MGI.
GO; GO:0010830; P:regulation of myotube differentiation; IDA:UniProtKB.
GO; GO:0043393; P:regulation of protein binding; 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:0061333; P:renal tubule morphogenesis; IMP:UniProtKB.
GO; GO:0042220; P:response to cocaine; IDA:MGI.
Gene3D; 3.40.800.20; -; 1.
InterPro; IPR000286; His_deacetylse.
InterPro; IPR023801; His_deacetylse_dom.
InterPro; IPR037138; His_deacetylse_dom_sf.
InterPro; IPR024643; Hist_deacetylase_Gln_rich_N.
InterPro; IPR017320; Histone_deAcase_II_euk.
InterPro; IPR030703; Histone_deacetylase_5.
InterPro; IPR023696; Ureohydrolase_dom_sf.
PANTHER; PTHR10625; PTHR10625; 1.
PANTHER; PTHR10625:SF57; PTHR10625:SF57; 1.
Pfam; PF12203; HDAC4_Gln; 1.
Pfam; PF00850; Hist_deacetyl; 1.
PIRSF; PIRSF037911; HDAC_II_euk; 1.
PRINTS; PR01270; HDASUPER.
SUPFAM; SSF52768; SSF52768; 1.
1: Evidence at protein level;
Acetylation; Chromatin regulator; Complete proteome; Cytoplasm;
Hydrolase; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Repressor; Transcription;
Transcription regulation; Ubl conjugation; Zinc.
CHAIN 1 1113 Histone deacetylase 5.
/FTId=PRO_0000114702.
REGION 675 1019 Histone deacetylase.
MOTIF 1072 1113 Nuclear export signal. {ECO:0000250}.
COMPBIAS 47 52 Poly-Gly.
COMPBIAS 85 92 Poly-Gln.
COMPBIAS 577 588 Poly-Glu.
ACT_SITE 824 824 {ECO:0000250}.
METAL 687 687 Zinc. {ECO:0000250}.
METAL 689 689 Zinc. {ECO:0000250}.
METAL 695 695 Zinc. {ECO:0000250}.
METAL 772 772 Zinc. {ECO:0000250}.
MOD_RES 250 250 Phosphoserine; by AMPK, CaMK1, SIK1 and
PKD/PRKD1. {ECO:0000269|PubMed:17468767,
ECO:0000269|PubMed:21454484}.
MOD_RES 283 283 Phosphothreonine; by PKC.
{ECO:0000250|UniProtKB:Q9UQL6}.
MOD_RES 488 488 Phosphoserine; by AMPK, CaMK1, SIK1 and
PKD/PRKD1. {ECO:0000269|PubMed:17468767,
ECO:0000269|PubMed:21454484}.
MOD_RES 523 523 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9UQL6}.
MOD_RES 600 600 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQL6}.
MOD_RES 650 650 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQL6}.
MOD_RES 1099 1099 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQL6}.
CROSSLNK 35 35 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9UQL6}.
MUTAGEN 250 250 S->A: Abolishes phosphorylation by SIK1
and fails to promote beta-catenin
expression; when associated with A-488.
{ECO:0000269|PubMed:17468767,
ECO:0000269|PubMed:21454484}.
MUTAGEN 488 488 S->A: Abolishes phosphorylation by SIK1
and fails to promote beta-catenin
expression; when associated with A-250.
{ECO:0000269|PubMed:17468767,
ECO:0000269|PubMed:21454484}.
MUTAGEN 824 824 H->A: Abolishes deacetylase activity.
{ECO:0000269|PubMed:10984530}.
MUTAGEN 884 884 H->F: Disrupts the dot-like nuclear
pattern. {ECO:0000269|PubMed:10984530}.
CONFLICT 7 7 S -> SA (in Ref. 2; AAF31418).
{ECO:0000305}.
CONFLICT 18 18 G -> E (in Ref. 2; AAF31418).
{ECO:0000305}.
SEQUENCE 1113 AA; 120942 MW; 63071AF45B87815A CRC64;
MNSPNESDGM SGREPSLGIL PRTPLHSIPV AVEVKPVLPG AMPSSMGGGG GGSPSPVELR
GALAGPMDPA LREQQLQQEL LVLKQQQQLQ KQLLFAEFQK QHDHLTRQHE VQLQKHLKQQ
QEMLAAKRQQ ELEQQRQREQ QRQEELEKQR LEQQLLILRN KEKSKESAIA STEVKLRLQE
FLLSKSKEPT PGGLNHSLPQ HPKCWGAHHA SLDQSSPPQS GPPGTPPSYK LPLLGPYDSR
DDFPLRKTAS EPNLKVRSRL KQKVAERRSS PLLRRKDGTV ISTFKKRAVE ITGTGPGVSS
VCNSAPGSGP SSPNSSHSTI AENGFTGSVP NIPTEMIPQH RALPLDSSPN QFSLYTSPSL
PNISLGLQAT VTVTNSHLTA SPKLSTQQEA ERQALQSLRQ GGTLTGKFMS TSSIPGCLLG
VALEGDTSPH GHASLLQHVC SWTGRQQSTL IAVPLHGQSP LVTGERVATS MRTVGKLPRH
RPLSRTQSSP LPQSPQALQQ LVMQQQHQQF LEKQKQQQMQ LGKILTKTGE LSRQPTTHPE
ETEEELTEQQ EALLGEGALT IPREGSTESE STQEDLEEEE EEEEEEEEDC IQVKDEDGES
GPDEGPDLEE SSAGYKKLFA DAQQLQPLQV YQAPLSLATV PHQALGRTQS SPAAPGSMKS
PTDQPTVVKH LFTTGVVYDT FMLKHQCMCG NTHVHPEHAG RIQSIWSRLQ ETGLLGKCER
IRGRKATLDE IQTVHSEYHT LLYGTSPLNR QKLDSKKLLG PISQKMYAML PCGGIGVDSD
TVWNEMHSSS AVRMAVGCLV ELAFKVAAGE LKNGFAIIRP PGHHAEESTA MGFCFFNSVA
ITAKLLQQKL SVGKVLIVDW DIHHGNGTQQ AFYNDPSVLY ISLHRYDNGN FFPGSGAPEE
VGGGPGVGYN VNVAWTGGVD PPIGDVEYLT AFRTVVMPIA QEFSPDVVLV SAGFDAVEGH
LSPLGGYSVT ARCFGHLTRQ LMTLAGGRVV LALEGGHDLT AICDASEACV SALLSVELQP
LDEAVLQQKP SVNAVATLEK VIEIQSKHWS CVQRFAAGLG CSLREAQTGE KEEAETVSAM
ALLSVGAEQA QAVATQEHSP RPAEEPMEQE PAL


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San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




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