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Histone deacetylase 6 (HD6) (EC 3.5.1.98) (Histone deacetylase mHDA2)

 HDAC6_MOUSE             Reviewed;        1149 AA.
Q9Z2V5; B1AUA6;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
25-OCT-2017, entry version 151.
RecName: Full=Histone deacetylase 6;
Short=HD6;
EC=3.5.1.98;
AltName: Full=Histone deacetylase mHDA2;
Name=Hdac6;
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 [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
INTERACTION WITH CBFA2T3.
PubMed=11533236; DOI=10.1128/MCB.21.19.6470-6483.2001;
Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N.,
Downing J.R., Meyers S., Hiebert S.W.;
"ETO, a target of t(8;21) in acute leukemia, makes distinct contacts
with multiple histone deacetylases and binds mSin3A through its
oligomerization domain.";
Mol. Cell. Biol. 21:6470-6483(2001).
[4]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=16933150; DOI=10.1007/s11064-006-9127-6;
Southwood C.M., Peppi M., Dryden S., Tainsky M.A., Gow A.;
"Microtubule deacetylases, SirT2 and HDAC6, in the nervous system.";
Neurochem. Res. 32:187-195(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-43 AND SER-1148,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
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).
[6]
FUNCTION, INTERACTION WITH CYLD AND MICROTUBULES, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=19893491; DOI=10.1038/emboj.2009.317;
Wickstrom S.A., Masoumi K.C., Khochbin S., Fassler R., Massoumi R.;
"CYLD negatively regulates cell-cycle progression by inactivating
HDAC6 and increasing the levels of acetylated tubulin.";
EMBO J. 29:131-144(2010).
[7]
INTERACTION WITH ZMYND15.
PubMed=20675388; DOI=10.1074/jbc.M110.116418;
Yan W., Si Y., Slaymaker S., Li J., Zheng H., Young D.L., Aslanian A.,
Saunders L., Verdin E., Charo I.F.;
"Zmynd15 encodes a histone deacetylase-dependent transcriptional
repressor essential for spermiogenesis and male fertility.";
J. Biol. Chem. 285:31418-31426(2010).
[8]
FUNCTION IN AUTOPHAGY, AND SUBCELLULAR LOCATION.
PubMed=22819792; DOI=10.1016/j.neuint.2012.07.010;
Gal J., Bang Y., Choi H.J.;
"SIRT2 interferes with autophagy-mediated degradation of protein
aggregates in neuronal cells under proteasome inhibition.";
Neurochem. Int. 61:992-1000(2012).
[9]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-32, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- 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 (By similarity).
Plays a central role in microtubule-dependent cell motility via
deacetylation of tubulin. {ECO:0000250,
ECO:0000269|PubMed:19893491, ECO:0000269|PubMed:22819792}.
-!- FUNCTION: In addition to its protein deacetylase activity, plays a
key role in the degradation of misfolded proteins: when misfolded
proteins are too abundant to be degraded by the chaperone
refolding system and the ubiquitin-proteasome, mediates the
transport of misfolded proteins to a cytoplasmic juxtanuclear
structure called aggresome. Probably acts as an adapter that
recognizes polyubiquitinated misfolded proteins and target them to
the aggresome, facilitating their clearance by autophagy (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
a histone to yield a deacetylated histone.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 3 Zn(2+) ions per subunit. {ECO:0000250};
-!- SUBUNIT: Interacts with BBIP10, DDIT3/CHOP, F-actin and HDAC11.
Interacts with SIRT2 (via both phosphorylated, unphosphorylated,
active or inactive forms); the interaction is necessary for the
complex to interact with alpha-tubulin. Under proteasome
impairment conditions, interacts with UBD via its histone
deacetylase 1 and UBP-type zinc-finger regions (By similarity).
Interacts with CBFA2T3, CYLD and ZMYND15. Interacts with RIPOR2;
this interaction occurs during early myogenic differentiation and
prevents HDAC6 to deacetylate tubulin (By similarity). Interacts
with DYSF; this interaction occurs during early myogenic
differentiation (By similarity). {ECO:0000250|UniProtKB:Q9UBN7,
ECO:0000269|PubMed:11533236, ECO:0000269|PubMed:19893491,
ECO:0000269|PubMed:20675388}.
-!- INTERACTION:
P62973:- (xeno); NbExp=2; IntAct=EBI-1009256, EBI-16124826;
Q80TQ2:Cyld; NbExp=3; IntAct=EBI-1009256, EBI-943859;
P21146:GRK2 (xeno); NbExp=2; IntAct=EBI-1009256, EBI-1036401;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Perikaryon. Cell
projection, dendrite. Cell projection, axon. Note=It is mainly
cytoplasmic, where it is associated with microtubules.
-!- TISSUE SPECIFICITY: Expressed in neurons of the cortex. Expressed
in Purkinje cells. Detected in keratinocytes (at protein level).
{ECO:0000269|PubMed:16933150, ECO:0000269|PubMed:19893491}.
-!- PTM: Phosphorylated by AURKA. {ECO:0000250}.
-!- PTM: Ubiquitinated. Its polyubiquitination however does not lead
to its degradation (By similarity). {ECO:0000250}.
-!- PTM: Sumoylated in vitro. {ECO:0000250}.
-!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
subfamily. {ECO:0000305}.
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EMBL; AF006603; AAD09835.2; -; mRNA.
EMBL; AL670169; CAM17240.1; -; Genomic_DNA.
CCDS; CCDS40845.1; -.
PIR; T13964; T13964.
RefSeq; NP_001123888.1; NM_001130416.1.
RefSeq; NP_034543.3; NM_010413.3.
RefSeq; XP_006527630.1; XM_006527567.2.
RefSeq; XP_017173877.1; XM_017318388.1.
RefSeq; XP_017173878.1; XM_017318389.1.
UniGene; Mm.29854; -.
ProteinModelPortal; Q9Z2V5; -.
SMR; Q9Z2V5; -.
BioGrid; 200263; 41.
DIP; DIP-36461N; -.
IntAct; Q9Z2V5; 37.
MINT; MINT-220628; -.
STRING; 10090.ENSMUSP00000033501; -.
BindingDB; Q9Z2V5; -.
ChEMBL; CHEMBL2878; -.
iPTMnet; Q9Z2V5; -.
PhosphoSitePlus; Q9Z2V5; -.
EPD; Q9Z2V5; -.
MaxQB; Q9Z2V5; -.
PaxDb; Q9Z2V5; -.
PeptideAtlas; Q9Z2V5; -.
PRIDE; Q9Z2V5; -.
Ensembl; ENSMUST00000033501; ENSMUSP00000033501; ENSMUSG00000031161.
Ensembl; ENSMUST00000115642; ENSMUSP00000111306; ENSMUSG00000031161.
GeneID; 15185; -.
KEGG; mmu:15185; -.
UCSC; uc009snh.2; mouse.
CTD; 10013; -.
MGI; MGI:1333752; Hdac6.
eggNOG; KOG1343; Eukaryota.
eggNOG; COG0123; LUCA.
GeneTree; ENSGT00530000062809; -.
HOGENOM; HOG000004769; -.
HOVERGEN; HBG051894; -.
InParanoid; Q9Z2V5; -.
KO; K11407; -.
OMA; QPHGFCI; -.
OrthoDB; EOG091G0210; -.
TreeFam; TF106173; -.
BRENDA; 3.5.1.98; 3474.
Reactome; R-MMU-3371511; HSF1 activation.
Reactome; R-MMU-5617833; Cilium Assembly.
PRO; PR:Q9Z2V5; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000031161; -.
CleanEx; MM_HDAC6; -.
ExpressionAtlas; Q9Z2V5; baseline and differential.
Genevisible; Q9Z2V5; MM.
GO; GO:0016235; C:aggresome; ISO:MGI.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:0005901; C:caveola; ISO:MGI.
GO; GO:0044297; C:cell body; IDA:MGI.
GO; GO:0031252; C:cell leading edge; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; IDA:UniProtKB.
GO; GO:0030286; C:dynein complex; IEA:Ensembl.
GO; GO:0000118; C:histone deacetylase complex; ISO:MGI.
GO; GO:0016234; C:inclusion body; ISO:MGI.
GO; GO:0005874; C:microtubule; ISO:MGI.
GO; GO:0005875; C:microtubule associated complex; ISO:MGI.
GO; GO:0043005; C:neuron projection; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0043234; C:protein complex; IPI:MGI.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0043014; F:alpha-tubulin binding; ISO:MGI.
GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
GO; GO:0048487; F:beta-tubulin binding; IDA:MGI.
GO; GO:0001047; F:core promoter binding; ISO:MGI.
GO; GO:0070840; F:dynein complex binding; ISO:MGI.
GO; GO:0004407; F:histone deacetylase activity; IDA:MGI.
GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
GO; GO:0051879; F:Hsp90 protein binding; ISO:MGI.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0051787; F:misfolded protein binding; ISO:MGI.
GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISO:MGI.
GO; GO:0048156; F:tau protein binding; ISO:MGI.
GO; GO:0042903; F:tubulin deacetylase activity; IDA:UniProtKB.
GO; GO:0043130; F:ubiquitin binding; IDA:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0070842; P:aggresome assembly; IGI:MGI.
GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:MGI.
GO; GO:0071218; P:cellular response to misfolded protein; IMP:MGI.
GO; GO:0035967; P:cellular response to topologically incorrect protein; ISO:MGI.
GO; GO:0048668; P:collateral sprouting; IMP:MGI.
GO; GO:0060997; P:dendritic spine morphogenesis; IMP:MGI.
GO; GO:0016575; P:histone deacetylation; ISO:MGI.
GO; GO:0070846; P:Hsp90 deacetylation; IMP:MGI.
GO; GO:0006886; P:intracellular protein transport; ISO:MGI.
GO; GO:0032418; P:lysosome localization; ISO:MGI.
GO; GO:0051646; P:mitochondrion localization; IMP:ParkinsonsUK-UCL.
GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:MGI.
GO; GO:0043242; P:negative regulation of protein complex disassembly; ISO:MGI.
GO; GO:0045861; P:negative regulation of proteolysis; ISO:MGI.
GO; GO:0061734; P:parkin-mediated stimulation of mitophagy in response to mitochondrial depolarization; ISO:MGI.
GO; GO:0034983; P:peptidyl-lysine deacetylation; ISO:MGI.
GO; GO:0070845; P:polyubiquitinated misfolded protein transport; ISO:MGI.
GO; GO:0090035; P:positive regulation of chaperone-mediated protein complex assembly; ISO:MGI.
GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:MGI.
GO; GO:1901300; P:positive regulation of hydrogen peroxide-mediated programmed cell death; ISO:MGI.
GO; GO:0098779; P:positive regulation of mitophagy in response to mitochondrial depolarization; IGI:ParkinsonsUK-UCL.
GO; GO:0010870; P:positive regulation of receptor biosynthetic process; ISO:MGI.
GO; GO:0009967; P:positive regulation of signal transduction; ISO:MGI.
GO; GO:0043241; P:protein complex disassembly; IGI:MGI.
GO; GO:0006476; P:protein deacetylation; IDA:MGI.
GO; GO:0000209; P:protein polyubiquitination; IDA:MGI.
GO; GO:0006515; P:protein quality control by the ubiquitin-proteasome system; ISO:MGI.
GO; GO:0070201; P:regulation of establishment of protein localization; IMP:MGI.
GO; GO:0045598; P:regulation of fat cell differentiation; IMP:MGI.
GO; GO:0040029; P:regulation of gene expression, epigenetic; ISO:MGI.
GO; GO:0016241; P:regulation of macroautophagy; ISO:MGI.
GO; GO:0031647; P:regulation of protein stability; ISO:MGI.
GO; GO:0010469; P:regulation of receptor activity; ISO:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0070848; P:response to growth factor; ISO:MGI.
GO; GO:0051788; P:response to misfolded protein; ISO:MGI.
GO; GO:0010033; P:response to organic substance; ISO:MGI.
GO; GO:0009636; P:response to toxic substance; ISO:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0090042; P:tubulin deacetylation; IDA:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:MGI.
GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:MGI.
Gene3D; 3.30.40.10; -; 1.
Gene3D; 3.40.800.20; -; 2.
InterPro; IPR000286; His_deacetylse.
InterPro; IPR023801; His_deacetylse_dom.
InterPro; IPR037138; His_deacetylse_dom_sf.
InterPro; IPR023696; Ureohydrolase_domain.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR001607; Znf_UBP.
PANTHER; PTHR10625; PTHR10625; 4.
Pfam; PF00850; Hist_deacetyl; 2.
Pfam; PF02148; zf-UBP; 1.
PRINTS; PR01270; HDASUPER.
SMART; SM00290; ZnF_UBP; 1.
SUPFAM; SSF52768; SSF52768; 2.
PROSITE; PS50271; ZF_UBP; 1.
1: Evidence at protein level;
Actin-binding; Cell projection; Chromatin regulator;
Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Methylation;
Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
Transcription; Transcription regulation; Ubl conjugation; Zinc;
Zinc-finger.
CHAIN 1 1149 Histone deacetylase 6.
/FTId=PRO_0000114704.
ZN_FING 1065 1126 UBP-type. {ECO:0000255|PROSITE-
ProRule:PRU00502}.
REGION 87 403 Histone deacetylase 1.
REGION 481 799 Histone deacetylase 2.
REGION 1088 1090 Ubiquitin binding. {ECO:0000250}.
REGION 1116 1123 Ubiquitin binding. {ECO:0000250}.
COMPBIAS 455 460 Poly-Glu.
ACT_SITE 215 215 1. {ECO:0000250}.
ACT_SITE 610 610 2. {ECO:0000250}.
METAL 1047 1047 Zinc 1. {ECO:0000250}.
METAL 1049 1049 Zinc 1. {ECO:0000250}.
METAL 1067 1067 Zinc 3. {ECO:0000250}.
METAL 1070 1070 Zinc 3. {ECO:0000250}.
METAL 1079 1079 Zinc 2. {ECO:0000250}.
METAL 1082 1082 Zinc 2. {ECO:0000250}.
METAL 1087 1087 Zinc 3. {ECO:0000250}.
METAL 1094 1094 Zinc 3. {ECO:0000250}.
METAL 1098 1098 Zinc 2. {ECO:0000250}.
METAL 1104 1104 Zinc 2. {ECO:0000250}.
METAL 1117 1117 Zinc 1. {ECO:0000250}.
METAL 1120 1120 Zinc 1. {ECO:0000250}.
MOD_RES 21 21 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 32 32 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 43 43 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 958 958 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9UBN7}.
MOD_RES 961 961 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9UBN7}.
MOD_RES 967 967 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9UBN7}.
MOD_RES 971 971 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9UBN7}.
MOD_RES 975 975 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UBN7}.
MOD_RES 1148 1148 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CONFLICT 133 133 R -> W (in Ref. 1; AAD09835).
{ECO:0000305}.
CONFLICT 394 394 V -> I (in Ref. 1; AAD09835).
{ECO:0000305}.
CONFLICT 421 421 T -> I (in Ref. 1; AAD09835).
{ECO:0000305}.
CONFLICT 532 532 D -> G (in Ref. 1; AAD09835).
{ECO:0000305}.
CONFLICT 836 836 M -> S (in Ref. 1; AAD09835).
{ECO:0000305}.
CONFLICT 851 851 I -> V (in Ref. 1; AAD09835).
{ECO:0000305}.
CONFLICT 1126 1127 HE -> QD (in Ref. 1; AAD09835).
{ECO:0000305}.
SEQUENCE 1149 AA; 125787 MW; D5F73BA3F79AF520 CRC64;
MTSTGQDSST RQRKSRHNPQ SPLQESSATL KRGGKKCAVP HSSPNLAEVK KKGKMKKLSQ
PAEEDLVVGL QGLDLNPETR VPVGTGLVFD EQLNDFHCLW DDSFPESPER LHAIREQLIL
EGLLGRCVSF QARFAEKEEL MLVHSLEYID LMETTQYMNE GELRVLAETY DSVYLHPNSY
SCACLATGSV LRLVDALMGA EIRNGMAVIR PPGHHAQHNL MDGYCMFNHL AVAARYAQKK
HRIQRVLIVD WDVHHGQGTQ FIFDQDPSVL YFSIHRYEHG RFWPHLKASN WSTIGFGQGQ
GYTINVPWNQ TGMRDADYIA AFLHILLPVA SEFQPQLVLV AAGFDALHGD PKGEMAATPA
GFAHLTHLLM GLAGGKLILS LEGGYNLRAL AKGVSASLHT LLGDPCPMLE SCVVPCASAQ
TSIYCTLEAL EPFWEVLERS VETQEEDEVE EAVLEEEEEE GGWEATALPM DTWPLLQNRT
GLVYDEKMMS HCNLWDNHHP ETPQRILRIM CHLEEVGLAA RCLILPARPA LDSELLTCHS
AEYVEHLRTT EKMKTRDLHR EGANFDSIYI CPSTFACAKL ATGAACRLVE AVLSGEVLNG
IAVVRPPGHH AEPNAACGFC FFNSVAVAAR HAQIIAGRAL RILIVDWDVH HGNGTQHIFE
DDPSVLYVSL HRYDRGTFFP MGDEGASSQV GRDAGIGFTV NVPWNGPRMG DADYLAAWHR
LVLPIAYEFN PELVLISAGF DAAQGDPLGG CQVTPEGYAH LTHLLMGLAG GRIILILEGG
YNLASISESM AACTHSLLGD PPPQLTLLRP PQSGALVSIS EVIQVHRKYW RSLRLMKMED
KEECSSSRLV IKKLPPTASP VSAKEMTTPK GKVPEESVRK TIAALPGKES TLGQAKSKMA
KAVLAQGQSS EQAAKGTTLD LATSKETVGG ATTDLWASAA APENFPNQTT SVEALGETEP
TPPASHTNKQ TTGASPLQGV TAQQSLQLGV LSTLELSREA EEAHDSEEGL LGEAAGGQDM
NSLMLTQGFG DFNTQDVFYA VTPLSWCPHL MAVCPIPAAG LDVSQPCKTC GTVQENWVCL
TCYQVYCSRY VNAHMVCHHE ASEHPLVLSC VDLSTWCYVC QAYVHHEDLQ DVKNAAHQNK
FGEDMPHSH


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MCA5048Z MOUSE ANTI HUMAN HISTONE DEACETYLASE 4 Azide free, Product Type Monoclonal Antibody, Specificity HISTONE DEACETYLASE 4, Target Species Human, Host Mouse, Format Azide Free, Isotypes IgG2a, Appli 0.1 mg
MCA4831Z MOUSE ANTI HUMAN HISTONE DEACETYLASE 3 Azide free, Product Type Monoclonal Antibody, Specificity HISTONE DEACETYLASE 3, Target Species Human, Host Mouse, Format Azide Free, Isotypes IgG2a, Appli 0.1 mg
MCA3659Z MOUSE ANTI HUMAN HISTONE DEACETYLASE 6 Azide Free, Product Type Monoclonal Antibody, Specificity HISTONE DEACETYLASE 6, Target Species Human, Host Mouse, Format Azide Free, Isotypes IgG1, Applic 0.1 mg
MCA3883Z MOUSE ANTI HUMAN HISTONE DEACETYLASE 8 Azide Free, Product Type Monoclonal Antibody, Specificity HISTONE DEACETYLASE 8, Target Species Human, Host Mouse, Format Azide Free, Isotypes IgG2b, Appli 0.1 mg
MCA3162Z MOUSE ANTI HUMAN HISTONE DEACETYLASE 1 Azide Free, Product Type Monoclonal Antibody, Specificity HISTONE DEACETYLASE 1, Target Species Human, Host Mouse, Format Azide Free, Isotypes IgG1, Applic 0.1 mg
MCA3587Z MOUSE ANTI HUMAN HISTONE DEACETYLASE 3 Azide Free, Product Type Monoclonal Antibody, Specificity HISTONE DEACETYLASE 3, Target Species Human, Host Mouse, Format Azide Free, Isotypes IgG2a, Appli 0.1 mg
MCA3843Z MOUSE ANTI HUMAN HISTONE DEACETYLASE 7 Azide Free, Product Type Monoclonal Antibody, Specificity HISTONE DEACETYLASE 7, Target Species Human, Host Mouse, Format Azide Free, Isotypes IgG2b, Appli 0.1 mg
MCA3933Z MOUSE ANTI HUMAN HISTONE DEACETYLASE 11 Azide Free, Product Type Monoclonal Antibody, Specificity HISTONE DEACETYLASE 11, Target Species Human, Host Mouse, Format Azide Free, Isotypes IgG1, Appl 0.1 mg
orb61320 CI-994 CI-994 is a histone deacetylase (HDAC) inhibitor and induces histone hyperacetylation in living cells. CI-994 inhibited HDAC-1 and HDAC-2 but not the prototypical histone acetyltransferase GCN5 500 mg
26-515 SPOP may modulate the transcriptional repression activities of death-associated protein 6 (DAXX), which interacts with histone deacetylase, core histones, and other histone-associated proteins. In mou 0.05 mg
28-996 SAP30BP is a component of a histone deacetylase complex conserved among eukaryotic organisms. This complex is active in deacetylating core histone octamers, but inactive in deacetylating nucleosomal h 0.1 mg
28-051 SAP30BP is a component of a histone deacetylase complex conserved among eukaryotic organisms. This complex is active in deacetylating core histone octamers, but inactive in deacetylating nucleosomal h 0.05 mg
49-395 Histone Deacetylase 1 Antibody 0.05 mg
E02H0234 Rat Histone Deacetylase 96 Tests/kit
48-490 Histone Deacetylase 2 Antibody 0.05 mg
48-700 Histone Deacetylase 2 Antibody 0.05 mg
48-701 Histone Deacetylase 4 Antibody 0.05 mg
49-282 Histone Deacetylase 4 Antibody 0.05 mg


 

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