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Histone deacetylase 4 (HD4) (EC 3.5.1.98)

 HDAC4_HUMAN             Reviewed;        1084 AA.
P56524; E9PGB9; F5GX36; Q86YH7; Q9UND6;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
22-SEP-2009, sequence version 3.
22-NOV-2017, entry version 186.
RecName: Full=Histone deacetylase 4;
Short=HD4;
EC=3.5.1.98;
Name=HDAC4; Synonyms=KIAA0288;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Leukemia;
PubMed=10220385; DOI=10.1073/pnas.96.9.4868;
Grozinger C.M., Hassig C.A., Schreiber S.L.;
"Three proteins define a class of human histone deacetylases related
to yeast Hda1p.";
Proc. Natl. Acad. Sci. U.S.A. 96:4868-4873(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9179496; DOI=10.1093/dnares/4.1.53;
Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N.,
Nomura N.;
"Construction and characterization of human brain cDNA libraries
suitable for analysis of cDNA clones encoding relatively large
proteins.";
DNA Res. 4:53-59(1997).
[3]
SEQUENCE REVISION TO N-TERMINUS.
Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N.,
Nomura N.;
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
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).
[7]
SUBCELLULAR LOCATION, AND INTERACTION WITH MEF2A.
PubMed=10487761; DOI=10.1093/emboj/18.18.5099;
Miska E.A., Karlsson C., Langley E., Nielsen S.J., Pines J.,
Kouzarides T.;
"HDAC4 deacetylase associates with and represses the MEF2
transcription factor.";
EMBO J. 18:5099-5107(1999).
[8]
FUNCTION, INTERACTION WITH MEF2C AND MEF2D, AND MUTAGENESIS OF
HIS-803.
PubMed=10523670; DOI=10.1128/MCB.19.11.7816;
Wang A.H., Bertos N.R., Vezmar M., Pelletier N., Crosato M.,
Heng H.H., Th'ng J., Han J., Yang X.-J.;
"HDAC4, a human histone deacetylase related to yeast HDA1, is a
transcriptional corepressor.";
Mol. Cell. Biol. 19:7816-7827(1999).
[9]
PHOSPHORYLATION AT SER-246; SER-467 AND SER-632, MUTAGENESIS OF
SER-246; SER-467 AND SER-632, AND INTERACTION WITH 14-3-3 PROTEINS.
PubMed=10958686; DOI=10.1128/MCB.20.18.6904-6912.2000;
Wang A.H., Kruhlak M.J., Wu J., Bertos N.R., Vezmar M., Posner B.I.,
Bazett-Jones D.P., Yang X.-J.;
"Regulation of histone deacetylase 4 by binding of 14-3-3 proteins.";
Mol. Cell. Biol. 20:6904-6912(2000).
[10]
SUBCELLULAR LOCATION, PHOSPHORYLATION, AND MUTAGENESIS OF SER-467 AND
SER-632.
PubMed=11470791; DOI=10.1074/jbc.M105086200;
Zhao X., Ito A., Kane C.D., Liao T.-S., Bolger T.A., Lemrow S.M.,
Means A.R., Yao T.-P.;
"The modular nature of histone deacetylase HDAC4 confers
phosphorylation-dependent intracellular trafficking.";
J. Biol. Chem. 276:35042-35048(2001).
[11]
NUCLEAR EXPORT SIGNAL, AND MUTAGENESIS OF VAL-1056 AND LEU-1062.
PubMed=11509672; DOI=10.1128/MCB.21.18.6312-6321.2001;
McKinsey T.A., Zhang C.-L., Olson E.N.;
"Identification of a signal-responsive nuclear export sequence in
class II histone deacetylases.";
Mol. Cell. Biol. 21:6312-6321(2001).
[12]
INTERACTION WITH NR2C1.
PubMed=11463856; DOI=10.1210/mend.15.8.0682;
Franco P.J., Farooqui M., Seto E., Wei L.-N.;
"The orphan nuclear receptor TR2 interacts directly with both class I
and class II histone deacetylases.";
Mol. Endocrinol. 15:1318-1328(2001).
[13]
HOMODIMERIZATION, SUMOYLATION AT LYS-559, AND MUTAGENESIS OF LYS-559.
PubMed=12032081; DOI=10.1093/emboj/21.11.2682;
Kirsh O., Seeler J.-S., Pichler A., Gast A., Mueller S., Miska E.,
Mathieu M., Harel-Bellan A., Kouzarides T., Melchior F., Dejean A.;
"The SUMO E3 ligase RanBP2 promotes modification of the HDAC4
deacetylase.";
EMBO J. 21:2682-2691(2002).
[14]
INTERACTION WITH KDM5B.
PubMed=17373667; DOI=10.1002/ijc.22673;
Barrett A., Santangelo S., Tan K., Catchpole S., Roberts K.,
Spencer-Dene B., Hall D., Scibetta A., Burchell J., Verdin E.,
Freemont P., Taylor-Papadimitriou J.;
"Breast cancer associated transcriptional repressor PLU-1/JARID1B
interacts directly with histone deacetylases.";
Int. J. Cancer 121:265-275(2007).
[15]
PHOSPHORYLATION BY CAMK2D.
PubMed=17179159; DOI=10.1074/jbc.M604281200;
Little G.H., Bai Y., Williams T., Poizat C.;
"Nuclear calcium/calmodulin-dependent protein kinase IIdelta
preferentially transmits signals to histone deacetylase 4 in cardiac
cells.";
J. Biol. Chem. 282:7219-7231(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-632 AND SER-633, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
INVOLVEMENT IN BDMR.
PubMed=20691407; DOI=10.1016/j.ajhg.2010.07.011;
Williams S.R., Aldred M.A., Der Kaloustian V.M., Halal F., Gowans G.,
McLeod D.R., Zondag S., Toriello H.V., Magenis R.E., Elsea S.H.;
"Haploinsufficiency of HDAC4 causes brachydactyly mental retardation
syndrome, with brachydactyly type E, developmental delays, and
behavioral problems.";
Am. J. Hum. Genet. 87:219-228(2010).
[19]
INTERACTION WITH MORC2.
PubMed=20110259; DOI=10.1093/nar/gkq006;
Shao Y., Li Y., Zhang J., Liu D., Liu F., Zhao Y., Shen T., Li F.;
"Involvement of histone deacetylation in MORC2-mediated down-
regulation of carbonic anhydrase IX.";
Nucleic Acids Res. 38:2813-2824(2010).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[22]
INVOLVEMENT IN BDMR.
PubMed=23188045; DOI=10.1038/ejhg.2012.240;
Villavicencio-Lorini P., Klopocki E., Trimborn M., Koll R.,
Mundlos S., Horn D.;
"Phenotypic variant of Brachydactyly-mental retardation syndrome in a
family with an inherited interstitial 2q37.3 microdeletion including
HDAC4.";
Eur. J. Hum. Genet. 21:743-748(2013).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-632, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[24]
FUNCTION, AND INTERACTION WITH EP300.
PubMed=24413532; DOI=10.1158/0008-5472.CAN-13-2020;
Kang H.J., Lee M.H., Kang H.L., Kim S.H., Ahn J.R., Na H., Na T.Y.,
Kim Y.N., Seong J.K., Lee M.O.;
"Differential regulation of estrogen receptor alpha expression in
breast cancer cells by metastasis-associated protein 1.";
Cancer Res. 74:1484-1494(2014).
[25]
INVOLVEMENT IN BDMR.
PubMed=24715439; DOI=10.1002/ajmg.a.36542;
Wheeler P.G., Huang D., Dai Z.;
"Haploinsufficiency of HDAC4 does not cause intellectual disability in
all affected individuals.";
Am. J. Med. Genet. A 164A:1826-1829(2014).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-632, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[27]
INTERACTION WITH CUL7 AND ANKRA2, AND MUTAGENESIS OF PRO-349 AND
ILE-354.
PubMed=25752541; DOI=10.1016/j.str.2015.02.001;
Nie J., Xu C., Jin J., Aka J.A., Tempel W., Nguyen V., You L.,
Weist R., Min J., Pawson T., Yang X.J.;
"Ankyrin repeats of ANKRA2 recognize a PxLPxL motif on the 3M syndrome
protein CCDC8.";
Structure 23:700-712(2015).
[28]
FUNCTION, AND INTERACTION WITH HSPA1A AND HSPA1B.
PubMed=27708256; DOI=10.1038/ncomms12882;
Seo J.H., Park J.H., Lee E.J., Vo T.T., Choi H., Kim J.Y., Jang J.K.,
Wee H.J., Lee H.S., Jang S.H., Park Z.Y., Jeong J., Lee K.J.,
Seok S.H., Park J.Y., Lee B.J., Lee M.N., Oh G.T., Kim K.W.;
"ARD1-mediated Hsp70 acetylation balances stress-induced protein
refolding and degradation.";
Nat. Commun. 7:12882-12882(2016).
[29]
X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 343-359 IN COMPLEX WITH
ANKRA2, PHOSPHORYLATION AT SER-350, MOTIF, AND MUTAGENESIS OF LEU-345;
TYR-346; THR-347; SER-348; PRO-349; SER-350; LEU-351; PRO-352;
ASN-353; ILE-354; THR-355 AND LEU-356.
PubMed=22649097; DOI=10.1126/scisignal.2002979;
Xu C., Jin J., Bian C., Lam R., Tian R., Weist R., You L., Nie J.,
Bochkarev A., Tempel W., Tan C.S., Wasney G.A., Vedadi M., Gish G.D.,
Arrowsmith C.H., Pawson T., Yang X.J., Min J.;
"Sequence-specific recognition of a PxLPxI/L motif by an ankyrin
repeat tumbler lock.";
Sci. Signal. 5:RA39-RA39(2012).
[30]
VARIANT [LARGE SCALE ANALYSIS] ARG-727.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[31]
VARIANT ILE-754.
PubMed=24169519; DOI=10.1038/ejhg.2013.243;
Piton A., Poquet H., Redin C., Masurel A., Lauer J., Muller J.,
Thevenon J., Herenger Y., Chancenotte S., Bonnet M., Pinoit J.M.,
Huet F., Thauvin-Robinet C., Jaeger A.S., Le Gras S., Jost B.,
Gerard B., Peoc'h K., Launay J.M., Faivre L., Mandel J.L.;
"20 ans apres: a second mutation in MAOA identified by targeted high-
throughput sequencing in a family with altered behavior and
cognition.";
Eur. J. Hum. Genet. 22:776-783(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. Involved in muscle
maturation via its interaction with the myocyte enhancer factors
such as MEF2A, MEF2C and MEF2D. Involved in the MTA1-mediated
epigenetic regulation of ESR1 expression in breast cancer.
Deacetylates HSPA1A and HSPA1B at 'Lys-77' leading to their
preferential binding to co-chaperone STUB1 (PubMed:27708256).
{ECO:0000269|PubMed:10523670, ECO:0000269|PubMed:24413532,
ECO:0000269|PubMed:27708256}.
-!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
a histone to yield a deacetylated histone.
-!- SUBUNIT: Homodimer. Homodimerization via its N-terminal domain
(PubMed:12032081). Interacts with MEF2A (PubMed:10487761).
Interacts with MEF2C and MEF2D (PubMed:10523670). Interacts with
AHRR (By similarity). Interacts with NR2C1 (PubMed:11463856).
Interacts with HDAC7 (By similarity). Interacts with a 14-3-3
chaperone protein in a phosphorylation dependent manner
(PubMed:10958686). Interacts with BTBD14B (By similarity).
Interacts with KDM5B (PubMed:17373667). Interacts with MYOCD (By
similarity). Interacts with MORC2 (PubMed:20110259). Interacts
(via PxLPxI/L motif) with ANKRA2 (via ankyrin repeats). Interacts
with CUL7 (as part of the 3M complex); negatively regulated by
ANKRA2 (PubMed:25752541). Interacts with EP300 in the presence of
TFAP2C (PubMed:24413532). Interacts with HSPA1A and HSPA1B leading
to their deacetylation at 'Lys-77' (PubMed:27708256).
{ECO:0000250|UniProtKB:Q6NZM9, ECO:0000250|UniProtKB:Q99P99,
ECO:0000269|PubMed:10487761, ECO:0000269|PubMed:10523670,
ECO:0000269|PubMed:10958686, ECO:0000269|PubMed:11463856,
ECO:0000269|PubMed:17373667, ECO:0000269|PubMed:20110259,
ECO:0000269|PubMed:22649097, ECO:0000269|PubMed:24413532,
ECO:0000269|PubMed:25752541, ECO:0000269|PubMed:27708256}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-308629, EBI-308629;
Q9H9E1:ANKRA2; NbExp=3; IntAct=EBI-308629, EBI-10215533;
P10275:AR; NbExp=4; IntAct=EBI-308629, EBI-608057;
P15336:ATF2; NbExp=2; IntAct=EBI-308629, EBI-1170906;
P41182:BCL6; NbExp=3; IntAct=EBI-308629, EBI-765407;
Q9HCU9:BRMS1; NbExp=2; IntAct=EBI-308629, EBI-714781;
Q96JN2-2:CCDC136; NbExp=3; IntAct=EBI-308629, EBI-10171416;
Q01850:CDR2; NbExp=3; IntAct=EBI-308629, EBI-1181367;
O54946-2:Dnajb6 (xeno); NbExp=2; IntAct=EBI-308629, EBI-13941040;
Q8AZK7:EBNA-LP (xeno); NbExp=5; IntAct=EBI-308629, EBI-1185167;
O95967:EFEMP2; NbExp=3; IntAct=EBI-308629, EBI-743414;
Q08379:GOLGA2; NbExp=3; IntAct=EBI-308629, EBI-618309;
P08393:ICP0 (xeno); NbExp=3; IntAct=EBI-308629, EBI-6148881;
Q15323:KRT31; NbExp=3; IntAct=EBI-308629, EBI-948001;
O76015:KRT38; NbExp=3; IntAct=EBI-308629, EBI-1047263;
Q6A162:KRT40; NbExp=3; IntAct=EBI-308629, EBI-10171697;
O95751:LDOC1; NbExp=3; IntAct=EBI-308629, EBI-740738;
A9UHW6:MIF4GD; NbExp=4; IntAct=EBI-308629, EBI-373498;
Q5JR59:MTUS2; NbExp=3; IntAct=EBI-308629, EBI-742948;
Q8ND90:PNMA1; NbExp=3; IntAct=EBI-308629, EBI-302345;
Q6NUQ1:RINT1; NbExp=3; IntAct=EBI-308629, EBI-726876;
Q13761:RUNX3; NbExp=9; IntAct=EBI-308629, EBI-925990;
P31947:SFN; NbExp=4; IntAct=EBI-308629, EBI-476295;
P63279:UBE2I; NbExp=3; IntAct=EBI-308629, EBI-80168;
P31946:YWHAB; NbExp=3; IntAct=EBI-308629, EBI-359815;
P62258:YWHAE; NbExp=4; IntAct=EBI-308629, EBI-356498;
P61981:YWHAG; NbExp=7; IntAct=EBI-308629, EBI-359832;
Q04917:YWHAH; NbExp=4; IntAct=EBI-308629, EBI-306940;
P63104:YWHAZ; NbExp=5; IntAct=EBI-308629, EBI-347088;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between
the nucleus and the cytoplasm. Upon muscle cells differentiation,
it accumulates in the nuclei of myotubes, suggesting a positive
role of nuclear HDAC4 in muscle differentiation. The export to
cytoplasm depends on the interaction with a 14-3-3 chaperone
protein and is due to its phosphorylation at Ser-246, Ser-467 and
Ser-632 by CaMK4 and SIK1. The nuclear localization probably
depends on sumoylation.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P56524-1; Sequence=Displayed;
Name=2;
IsoId=P56524-2; Sequence=VSP_057290, VSP_057291;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- DOMAIN: The nuclear export sequence mediates the shuttling between
the nucleus and the cytoplasm.
-!- DOMAIN: The PxLPxI/L motif mediates interaction with ankyrin
repeats of ANKRA2. {ECO:0000269|PubMed:22649097}.
-!- PTM: Phosphorylated by CaMK4 at Ser-246, Ser-467 and Ser-632.
Phosphorylation at other residues by CaMK2D is required for the
interaction with 14-3-3. Phosphorylation at Ser-350, within the
PxLPxI/L motif, impairs the binding of ANKRA2 but generates a
high-affinity docking site for 14-3-3.
{ECO:0000269|PubMed:10958686, ECO:0000269|PubMed:22649097}.
-!- PTM: Sumoylation on Lys-559 is promoted by the E3 SUMO-protein
ligase RANBP2, and prevented by phosphorylation by CaMK4.
{ECO:0000269|PubMed:12032081}.
-!- DISEASE: Brachydactyly-mental retardation syndrome (BDMR)
[MIM:600430]: A syndrome resembling the physical anomalies found
in Albright hereditary osteodystrophy. Common features are mild
facial dysmorphism, congenital heart defects, distinct
brachydactyly type E, mental retardation, developmental delay,
seizures, autism spectrum disorder, and stocky build. Soft tissue
ossification is absent, and there are no abnormalities in
parathyroid hormone or calcium metabolism.
{ECO:0000269|PubMed:20691407, ECO:0000269|PubMed:23188045,
ECO:0000269|PubMed:24715439}. Note=The gene represented in this
entry is involved in disease pathogenesis. HDAC4 point mutations
and chromosomal microdeletions encompassing this gene have been
found in BDMR patients (PubMed:20691407, PubMed:24715439,
PubMed:23188045). However, HDAC4 haploinsufficiency is not fully
penetrant and multiple genes may contribute to manifestation of
the full phenotypic spectrum (PubMed:24715439, PubMed:23188045).
{ECO:0000269|PubMed:20691407, ECO:0000269|PubMed:23188045,
ECO:0000269|PubMed:24715439}.
-!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA22957.2; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF132607; AAD29046.1; -; mRNA.
EMBL; AB006626; BAA22957.2; ALT_INIT; mRNA.
EMBL; AC017028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC062017; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; KF510800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; KF510801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471063; EAW71165.1; -; Genomic_DNA.
EMBL; BC039904; AAH39904.1; -; mRNA.
CCDS; CCDS2529.1; -. [P56524-1]
RefSeq; NP_006028.2; NM_006037.3. [P56524-1]
UniGene; Hs.20516; -.
PDB; 2H8N; X-ray; 2.60 A; A/B/C/D=62-153.
PDB; 2O94; X-ray; 3.00 A; A/B/C/D=62-153.
PDB; 2VQJ; X-ray; 2.10 A; A=648-1057.
PDB; 2VQM; X-ray; 1.80 A; A=648-1057.
PDB; 2VQO; X-ray; 2.15 A; A/B=648-1057.
PDB; 2VQQ; X-ray; 1.90 A; A/B=648-1057.
PDB; 2VQV; X-ray; 3.30 A; A/B=648-1057.
PDB; 2VQW; X-ray; 3.00 A; G=648-1057.
PDB; 3UXG; X-ray; 1.85 A; B=343-359.
PDB; 3UZD; X-ray; 1.86 A; B=343-359.
PDB; 3V31; X-ray; 1.57 A; B=343-359.
PDB; 4CBT; X-ray; 3.03 A; A/B/C=648-1033.
PDB; 4CBY; X-ray; 2.72 A; A/B/C/D=648-1033.
PDB; 5A2S; X-ray; 2.65 A; A/B=648-1033.
PDBsum; 2H8N; -.
PDBsum; 2O94; -.
PDBsum; 2VQJ; -.
PDBsum; 2VQM; -.
PDBsum; 2VQO; -.
PDBsum; 2VQQ; -.
PDBsum; 2VQV; -.
PDBsum; 2VQW; -.
PDBsum; 3UXG; -.
PDBsum; 3UZD; -.
PDBsum; 3V31; -.
PDBsum; 4CBT; -.
PDBsum; 4CBY; -.
PDBsum; 5A2S; -.
ProteinModelPortal; P56524; -.
SMR; P56524; -.
BioGrid; 115106; 195.
CORUM; P56524; -.
DIP; DIP-34565N; -.
ELM; P56524; -.
IntAct; P56524; 81.
MINT; MINT-104901; -.
STRING; 9606.ENSP00000264606; -.
BindingDB; P56524; -.
ChEMBL; CHEMBL3524; -.
DrugBank; DB05015; Belinostat.
DrugBank; DB06603; Panobinostat.
DrugBank; DB06176; Romidepsin.
GuidetoPHARMACOLOGY; 2659; -.
iPTMnet; P56524; -.
PhosphoSitePlus; P56524; -.
BioMuta; HDAC4; -.
DMDM; 259016348; -.
EPD; P56524; -.
MaxQB; P56524; -.
PaxDb; P56524; -.
PeptideAtlas; P56524; -.
PRIDE; P56524; -.
Ensembl; ENST00000345617; ENSP00000264606; ENSG00000068024. [P56524-1]
Ensembl; ENST00000543185; ENSP00000440481; ENSG00000068024. [P56524-2]
GeneID; 9759; -.
KEGG; hsa:9759; -.
UCSC; uc002vyk.4; human. [P56524-1]
CTD; 9759; -.
DisGeNET; 9759; -.
EuPathDB; HostDB:ENSG00000068024.16; -.
GeneCards; HDAC4; -.
GeneReviews; HDAC4; -.
HGNC; HGNC:14063; HDAC4.
HPA; CAB004431; -.
HPA; HPA048723; -.
MalaCards; HDAC4; -.
MIM; 600430; phenotype.
MIM; 605314; gene.
neXtProt; NX_P56524; -.
OpenTargets; ENSG00000068024; -.
Orphanet; 1001; 2q37 microdeletion syndrome.
PharmGKB; PA29229; -.
eggNOG; KOG1343; Eukaryota.
eggNOG; COG0123; LUCA.
GeneTree; ENSGT00530000062809; -.
HOGENOM; HOG000232065; -.
HOVERGEN; HBG057100; -.
InParanoid; P56524; -.
KO; K11406; -.
OMA; KCENEEA; -.
OrthoDB; EOG091G0EQO; -.
PhylomeDB; P56524; -.
TreeFam; TF106174; -.
BRENDA; 3.5.1.98; 2681.
Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
Reactome; R-HSA-8941284; RUNX2 regulates chondrocyte maturation.
Reactome; R-HSA-8951936; RUNX3 regulates p14-ARF.
SIGNOR; P56524; -.
ChiTaRS; HDAC4; human.
EvolutionaryTrace; P56524; -.
GeneWiki; HDAC4; -.
GenomeRNAi; 9759; -.
PRO; PR:P56524; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000068024; -.
CleanEx; HS_HDAC4; -.
ExpressionAtlas; P56524; baseline and differential.
Genevisible; P56524; HS.
GO; GO:0031672; C:A band; IEA:Ensembl.
GO; GO:0042641; C:actomyosin; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0000118; C:histone deacetylase complex; IDA:BHF-UCL.
GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0017053; C:transcriptional repressor complex; IDA:BHF-UCL.
GO; GO:0030018; C:Z disc; IEA:Ensembl.
GO; GO:0033613; F:activating transcription factor binding; IPI:BHF-UCL.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0001047; F:core promoter binding; IDA:UniProtKB.
GO; GO:0004407; F:histone deacetylase activity; IDA:BHF-UCL.
GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
GO; GO:0030955; F:potassium ion binding; IDA:BHF-UCL.
GO; GO:0033558; F:protein deacetylase activity; IDA:BHF-UCL.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0070491; F:repressing transcription factor binding; IPI:BHF-UCL.
GO; GO:0001025; F:RNA polymerase III transcription factor binding; IPI:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL.
GO; GO:0008270; F:zinc ion binding; IDA:BHF-UCL.
GO; GO:0042113; P:B cell activation; TAS:UniProtKB.
GO; GO:0030183; P:B cell differentiation; TAS:UniProtKB.
GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; TAS:BHF-UCL.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IEA:Ensembl.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0006338; P:chromatin remodeling; IDA:BHF-UCL.
GO; GO:0016575; P:histone deacetylation; IDA:BHF-UCL.
GO; GO:0070932; P:histone H3 deacetylation; IDA:BHF-UCL.
GO; GO:0070933; P:histone H4 deacetylation; IDA:BHF-UCL.
GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0045820; P:negative regulation of glycolytic process; ISS:BHF-UCL.
GO; GO:0010832; P:negative regulation of myotube differentiation; IMP:BHF-UCL.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; IEA:Ensembl.
GO; GO:1902894; P:negative regulation of pri-miRNA transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IMP:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0007399; P:nervous system development; TAS:UniProtKB.
GO; GO:0002076; P:osteoblast development; IEA:Ensembl.
GO; GO:0034983; P:peptidyl-lysine deacetylation; IDA:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:BHF-UCL.
GO; GO:0010592; P:positive regulation of lamellipodium assembly; IEA:Ensembl.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0033235; P:positive regulation of protein sumoylation; IDA:UniProtKB.
GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IEA:Ensembl.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IMP:BHF-UCL.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IEA:Ensembl.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:BHF-UCL.
GO; GO:0006476; P:protein deacetylation; IDA:UniProtKB.
GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; IEA:Ensembl.
GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:UniProtKB.
GO; GO:0043393; P:regulation of protein binding; IMP:BHF-UCL.
GO; GO:0048742; P:regulation of skeletal muscle fiber development; IEA:Ensembl.
GO; GO:0014894; P:response to denervation involved in regulation of muscle adaptation; ISS:BHF-UCL.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0070555; P:response to interleukin-1; IMP:BHF-UCL.
GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.40.800.20; -; 1.
InterPro; IPR033660; HDAC4.
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; IPR023696; Ureohydrolase_dom_sf.
PANTHER; PTHR10625; PTHR10625; 1.
PANTHER; PTHR10625:SF100; PTHR10625:SF100; 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;
3D-structure; Alternative splicing; Autism spectrum disorder;
Chromatin regulator; Coiled coil; Complete proteome; Cytoplasm;
Hydrolase; Isopeptide bond; Mental retardation; Metal-binding;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repressor;
Transcription; Transcription regulation; Ubl conjugation; Zinc.
CHAIN 1 1084 Histone deacetylase 4.
/FTId=PRO_0000114699.
REGION 118 313 Interaction with MEF2A.
{ECO:0000269|PubMed:10487761}.
REGION 655 1084 Histone deacetylase.
COILED 67 177 {ECO:0000255}.
MOTIF 349 354 PxLPxI/L motif; mediates interaction with
ANKRA2 and 14-3-3 proteins.
{ECO:0000269|PubMed:22649097}.
MOTIF 1051 1084 Nuclear export signal. {ECO:0000250}.
ACT_SITE 803 803 {ECO:0000250}.
METAL 667 667 Zinc. {ECO:0000250}.
METAL 669 669 Zinc. {ECO:0000250}.
METAL 675 675 Zinc. {ECO:0000250}.
METAL 751 751 Zinc. {ECO:0000250}.
MOD_RES 210 210 Phosphoserine.
{ECO:0000250|UniProtKB:Q6NZM9}.
MOD_RES 246 246 Phosphoserine; by CaMK4 and SIK1.
{ECO:0000269|PubMed:10958686}.
MOD_RES 350 350 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:22649097}.
MOD_RES 467 467 Phosphoserine; by CaMK4 and SIK1.
{ECO:0000269|PubMed:10958686}.
MOD_RES 565 565 Phosphoserine.
{ECO:0000250|UniProtKB:Q6NZM9}.
MOD_RES 632 632 Phosphoserine; by CaMK4.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:10958686}.
MOD_RES 633 633 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
CROSSLNK 559 559 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:12032081}.
VAR_SEQ 1 117 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_057290.
VAR_SEQ 431 431 T -> TDWYLS (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_057291.
VARIANT 727 727 P -> R (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036042.
VARIANT 754 754 V -> I (in dbSNP:rs151043798).
{ECO:0000269|PubMed:24169519}.
/FTId=VAR_071965.
MUTAGEN 246 246 S->A: Reduces phosphorylation and its
subsequent nuclear export.
{ECO:0000269|PubMed:10958686}.
MUTAGEN 345 345 L->A: No effect on interaction with
ANKRA2. {ECO:0000269|PubMed:22649097}.
MUTAGEN 346 346 Y->A: No effect on interaction with
ANKRA2. {ECO:0000269|PubMed:22649097}.
MUTAGEN 347 347 T->A: No effect on interaction with
ANKRA2. {ECO:0000269|PubMed:22649097}.
MUTAGEN 348 348 S->A: No effect on interaction with
ANKRA2. {ECO:0000269|PubMed:22649097}.
MUTAGEN 349 349 P->A: May affect interaction with ANKRA2.
{ECO:0000269|PubMed:22649097,
ECO:0000269|PubMed:25752541}.
MUTAGEN 349 349 P->G: Decreased interaction with ANKRA2.
{ECO:0000269|PubMed:22649097}.
MUTAGEN 350 350 S->A: No effect on interaction with
ANKRA2. {ECO:0000269|PubMed:22649097}.
MUTAGEN 351 351 L->A,G: Loss of interaction with ANKRA2.
{ECO:0000269|PubMed:22649097}.
MUTAGEN 352 352 P->A: Loss of interaction with ANKRA2.
{ECO:0000269|PubMed:22649097}.
MUTAGEN 353 353 N->A: No effect on interaction with
ANKRA2. {ECO:0000269|PubMed:22649097}.
MUTAGEN 354 354 I->A: May affect interaction with ANKRA2.
{ECO:0000269|PubMed:22649097,
ECO:0000269|PubMed:25752541}.
MUTAGEN 354 354 I->G: Loss of interaction with ANKRA2.
{ECO:0000269|PubMed:22649097}.
MUTAGEN 355 355 T->A: No effect on interaction with
ANKRA2. {ECO:0000269|PubMed:22649097}.
MUTAGEN 356 356 L->A: No effect on interaction with
ANKRA2. {ECO:0000269|PubMed:22649097}.
MUTAGEN 467 467 S->A: Reduces phosphorylation and its
subsequent nuclear export.
{ECO:0000269|PubMed:10958686,
ECO:0000269|PubMed:11470791}.
MUTAGEN 559 559 K->R: Abolishes sumoylation and reduces
the histone deacetylase activity.
{ECO:0000269|PubMed:12032081}.
MUTAGEN 632 632 S->A: Reduces phosphorylation and its
subsequent nuclear export.
{ECO:0000269|PubMed:10958686,
ECO:0000269|PubMed:11470791}.
MUTAGEN 803 803 H->L: Abolishes histone deacetylase
activity. {ECO:0000269|PubMed:10523670}.
MUTAGEN 1056 1056 V->A: Reduces CaMK-dependent nuclear
export. {ECO:0000269|PubMed:11509672}.
MUTAGEN 1062 1062 L->A: Reduces CaMK-dependent nuclear
export. {ECO:0000269|PubMed:11509672}.
CONFLICT 373 373 A -> T (in Ref. 1; AAD29046 and 2;
BAA22957). {ECO:0000305}.
HELIX 64 112 {ECO:0000244|PDB:2H8N}.
HELIX 115 121 {ECO:0000244|PDB:2H8N}.
TURN 122 125 {ECO:0000244|PDB:2H8N}.
HELIX 126 128 {ECO:0000244|PDB:2H8N}.
TURN 354 357 {ECO:0000244|PDB:3UXG}.
STRAND 652 657 {ECO:0000244|PDB:2VQM}.
HELIX 660 662 {ECO:0000244|PDB:2VQM}.
STRAND 673 675 {ECO:0000244|PDB:2VQJ}.
HELIX 681 691 {ECO:0000244|PDB:2VQM}.
HELIX 694 697 {ECO:0000244|PDB:2VQM}.
STRAND 698 701 {ECO:0000244|PDB:2VQM}.
HELIX 708 711 {ECO:0000244|PDB:2VQM}.
TURN 712 714 {ECO:0000244|PDB:2VQM}.
HELIX 717 724 {ECO:0000244|PDB:2VQM}.
HELIX 727 730 {ECO:0000244|PDB:2VQM}.
HELIX 737 745 {ECO:0000244|PDB:2VQM}.
STRAND 746 748 {ECO:0000244|PDB:2VQM}.
STRAND 754 756 {ECO:0000244|PDB:2VQM}.
HELIX 762 786 {ECO:0000244|PDB:2VQM}.
STRAND 789 795 {ECO:0000244|PDB:2VQM}.
STRAND 813 815 {ECO:0000244|PDB:2VQM}.
HELIX 817 828 {ECO:0000244|PDB:2VQM}.
STRAND 834 838 {ECO:0000244|PDB:2VQM}.
STRAND 840 842 {ECO:0000244|PDB:2VQM}.
HELIX 845 851 {ECO:0000244|PDB:2VQM}.
STRAND 857 864 {ECO:0000244|PDB:2VQM}.
HELIX 866 868 {ECO:0000244|PDB:2VQM}.
STRAND 870 872 {ECO:0000244|PDB:4CBT}.
HELIX 883 885 {ECO:0000244|PDB:2VQM}.
STRAND 889 894 {ECO:0000244|PDB:2VQM}.
STRAND 898 900 {ECO:0000244|PDB:2VQM}.
HELIX 904 913 {ECO:0000244|PDB:2VQM}.
HELIX 915 922 {ECO:0000244|PDB:2VQM}.
STRAND 925 931 {ECO:0000244|PDB:2VQM}.
STRAND 936 938 {ECO:0000244|PDB:2VQM}.
TURN 940 943 {ECO:0000244|PDB:2VQM}.
HELIX 950 961 {ECO:0000244|PDB:2VQM}.
HELIX 964 966 {ECO:0000244|PDB:2VQM}.
STRAND 968 972 {ECO:0000244|PDB:2VQM}.
HELIX 978 992 {ECO:0000244|PDB:2VQM}.
HELIX 1002 1006 {ECO:0000244|PDB:2VQM}.
HELIX 1011 1025 {ECO:0000244|PDB:2VQM}.
HELIX 1029 1031 {ECO:0000244|PDB:2VQM}.
HELIX 1042 1047 {ECO:0000244|PDB:2VQM}.
SEQUENCE 1084 AA; 119040 MW; BB7FD37652D12398 CRC64;
MSSQSHPDGL SGRDQPVELL NPARVNHMPS TVDVATALPL QVAPSAVPMD LRLDHQFSLP
VAEPALREQQ LQQELLALKQ KQQIQRQILI AEFQRQHEQL SRQHEAQLHE HIKQQQEMLA
MKHQQELLEH QRKLERHRQE QELEKQHREQ KLQQLKNKEK GKESAVASTE VKMKLQEFVL
NKKKALAHRN LNHCISSDPR YWYGKTQHSS LDQSSPPQSG VSTSYNHPVL GMYDAKDDFP
LRKTASEPNL KLRSRLKQKV AERRSSPLLR RKDGPVVTAL KKRPLDVTDS ACSSAPGSGP
SSPNNSSGSV SAENGIAPAV PSIPAETSLA HRLVAREGSA APLPLYTSPS LPNITLGLPA
TGPSAGTAGQ QDAERLTLPA LQQRLSLFPG THLTPYLSTS PLERDGGAAH SPLLQHMVLL
EQPPAQAPLV TGLGALPLHA QSLVGADRVS PSIHKLRQHR PLGRTQSAPL PQNAQALQHL
VIQQQHQQFL EKHKQQFQQQ QLQMNKIIPK PSEPARQPES HPEETEEELR EHQALLDEPY
LDRLPGQKEA HAQAGVQVKQ EPIESDEEEA EPPREVEPGQ RQPSEQELLF RQQALLLEQQ
RIHQLRNYQA SMEAAGIPVS FGGHRPLSRA QSSPASATFP VSVQEPPTKP RFTTGLVYDT
LMLKHQCTCG SSSSHPEHAG RIQSIWSRLQ ETGLRGKCEC IRGRKATLEE LQTVHSEAHT
LLYGTNPLNR QKLDSKKLLG SLASVFVRLP CGGVGVDSDT IWNEVHSAGA ARLAVGCVVE
LVFKVATGEL KNGFAVVRPP GHHAEESTPM GFCYFNSVAV AAKLLQQRLS VSKILIVDWD
VHHGNGTQQA FYSDPSVLYM SLHRYDDGNF FPGSGAPDEV GTGPGVGFNV NMAFTGGLDP
PMGDAEYLAA FRTVVMPIAS EFAPDVVLVS SGFDAVEGHP TPLGGYNLSA RCFGYLTKQL
MGLAGGRIVL ALEGGHDLTA ICDASEACVS ALLGNELDPL PEKVLQQRPN ANAVRSMEKV
MEIHSKYWRC LQRTTSTAGR SLIEAQTCEN EEAETVTAMA SLSVGVKPAE KRPDEEPMEE
EPPL


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SCH-AHP595 RABBIT ANTI HUMAN HISTONE DEACETYLASE 1, Product Type Polyclonal Antibody, Specificity HISTONE DEACETYLASE 1, Target Species Human, Host Rabbit, Format Purified, Isotypes Polyclonal IgG, Applica 50 µg
MCA3660Z MOUSE ANTI HUMAN HISTONE DEACETYLASE 5 Azide Free, Product Type Monoclonal Antibody, Specificity HISTONE DEACETYLASE 5, Target Species Human, Host Mouse, Format Azide Free, Isotypes IgG1, Applic 0.1 mg
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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