Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Histone deacetylase 1 (HD1) (EC 3.5.1.98)

 HDAC1_MOUSE             Reviewed;         482 AA.
O09106; P97476;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
27-SEP-2017, entry version 183.
RecName: Full=Histone deacetylase 1;
Short=HD1;
EC=3.5.1.98;
Name=Hdac1;
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].
TISSUE=Fibroblast;
PubMed=9271381; DOI=10.1128/MCB.17.9.5033;
Bartl S., Taplick J., Lagger G., Khier H., Kuchler K., Seiser C.;
"Identification of mouse histone deacetylase 1 as a growth factor-
inducible gene.";
Mol. Cell. Biol. 17:5033-5043(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Johnson C.A.;
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[3]
INTERACTION WITH SAP30.
PubMed=9702189; DOI=10.1016/S1097-2765(00)80111-2;
Laherty C.D., Billin A.N., Lavinsky R.M., Yochum G.S., Bush A.C.,
Sun J.-M., Mullen T.-M., Davie J.R., Rose D.W., Glass C.K.,
Rosenfeld M.G., Ayer D.E., Eisenman R.N.;
"SAP30, a component of the mSin3 corepressor complex involved in N-
CoR-mediated repression by specific transcription factors.";
Mol. Cell 2:33-42(1998).
[4]
INTERACTION WITH DNMT1.
PubMed=10615135; DOI=10.1038/71750;
Fuks F., Burgers W.A., Brehm A., Hughes-Davies L., Kouzarides T.;
"DNA methyltransferase Dnmt1 associates with histone deacetylase
activity.";
Nat. Genet. 24:88-91(2000).
[5]
INTERACTION WITH HDAC7.
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).
[6]
INTERACTION WITH 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).
[7]
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).
[8]
INTERACTION WITH BAZ2A.
PubMed=12198165; DOI=10.1093/emboj/cdf460;
Zhou Y., Santoro R., Grummt I.;
"The chromatin remodeling complex NoRC targets HDAC1 to the ribosomal
gene promoter and represses RNA polymerase I transcription.";
EMBO J. 21:4632-4640(2002).
[9]
INTERACTION WITH SIN3B.
PubMed=11909966; DOI=10.1128/MCB.22.8.2743-2750.2002;
Alland L., David G., Shen-Li H., Potes J., Muhle R., Lee H.-C.,
Hou H. Jr., Chen K., DePinho R.A.;
"Identification of mammalian Sds3 as an integral component of the
Sin3/histone deacetylase corepressor complex.";
Mol. Cell. Biol. 22:2743-2750(2002).
[10]
INTERACTION WITH SUV39H1.
PubMed=11788710; DOI=10.1093/nar/30.2.475;
Vaute O., Nicolas E., Vandel L., Trouche D.;
"Functional and physical interaction between the histone methyl
transferase Suv39H1 and histone deacetylases.";
Nucleic Acids Res. 30:475-481(2002).
[11]
INTERACTION WITH SETDB1.
PubMed=12398767; DOI=10.1042/BJ20020854;
Yang L., Mei Q., Zielinska-Kwiatkowska A., Matsui Y., Blackburn M.L.,
Benedetti D., Krumm A.A., Taborsky G.J. Jr., Chansky H.A.;
"An ERG (ets-related gene)-associated histone methyltransferase
interacts with histone deacetylases 1/2 and transcription co-
repressors mSin3A/B.";
Biochem. J. 369:651-657(2003).
[12]
IDENTIFICATION IN A COMPLEX WITH DNMT3A.
PubMed=12616525; DOI=10.1002/jcb.10457;
Datta J., Ghoshal K., Sharma S.M., Tajima S., Jacob S.T.;
"Biochemical fractionation reveals association of DNA
methyltransferase (Dnmt) 3b with Dnmt1 and that of Dnmt 3a with a
histone H3 methyltransferase and Hdac1.";
J. Cell. Biochem. 88:855-864(2003).
[13]
INTERACTION WITH RERE.
PubMed=14645126; DOI=10.1242/dev.00908;
Zoltewicz J.S., Stewart N.J., Leung R., Peterson A.S.;
"Atrophin 2 recruits histone deacetylase and is required for the
function of multiple signaling centers during mouse embryogenesis.";
Development 131:3-14(2004).
[14]
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).
[15]
FUNCTION IN CIRCADIAN CLOCK, AND INTERACTION WITH CRY1.
PubMed=15226430; DOI=10.1128/MCB.24.14.6278-6287.2004;
Naruse Y., Oh-hashi K., Iijima N., Naruse M., Yoshioka H., Tanaka M.;
"Circadian and light-induced transcription of clock gene Per1 depends
on histone acetylation and deacetylation.";
Mol. Cell. Biol. 24:6278-6287(2004).
[16]
INTERACTION WITH KLF1, AND FUNCTION.
PubMed=15542849; DOI=10.1128/MCB.24.23.10416-10424.2004;
Chen X., Bieker J.J.;
"Stage-specific repression by the EKLF transcriptional activator.";
Mol. Cell. Biol. 24:10416-10424(2004).
[17]
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).
[18]
INTERACTION WITH BAZ2A.
PubMed=16085498; DOI=10.1016/j.cub.2005.06.057;
Zhou Y., Grummt I.;
"The PHD finger/bromodomain of NoRC interacts with acetylated histone
H4K16 and is sufficient for rDNA silencing.";
Curr. Biol. 15:1434-1438(2005).
[19]
INTERACTION WITH H2AFY.
PubMed=16107708; DOI=10.1128/MCB.25.17.7616-7624.2005;
Chakravarthy S., Gundimella S.K., Caron C., Perche P.-Y.,
Pehrson J.R., Khochbin S., Luger K.;
"Structural characterization of the histone variant macroH2A.";
Mol. Cell. Biol. 25:7616-7624(2005).
[20]
INTERACTION WITH BANP.
PubMed=16166625; DOI=10.1128/MCB.25.19.8415-8429.2005;
Rampalli S., Pavithra L., Bhatt A., Kundu T.K., Chattopadhyay S.;
"Tumor suppressor SMAR1 mediates cyclin D1 repression by recruitment
of the SIN3/histone deacetylase 1 complex.";
Mol. Cell. Biol. 25:8415-8429(2005).
[21]
INTERACTION WITH HDAC9, AND TISSUE SPECIFICITY.
PubMed=15711539; DOI=10.1038/nn1408;
Mejat A., Ramond F., Bassel-Duby R., Khochbin S., Olson E.N.,
Schaeffer L.;
"Histone deacetylase 9 couples neuronal activity to muscle chromatin
acetylation and gene expression.";
Nat. Neurosci. 8:313-321(2005).
[22]
INTERACTION WITH SMYD2.
PubMed=16805913; DOI=10.1186/1476-4598-5-26;
Brown M.A., Sims R.J. III, Gottlieb P.D., Tucker P.W.;
"Identification and characterization of Smyd2: a split SET/MYND
domain-containing histone H3 lysine 36-specific methyltransferase that
interacts with the Sin3 histone deacetylase complex.";
Mol. Cancer 5:26-26(2006).
[23]
INTERACTION WITH PRDM6.
PubMed=16537907; DOI=10.1128/MCB.26.7.2626-2636.2006;
Davis C.A., Haberland M., Arnold M.A., Sutherland L.B., McDonald O.G.,
Richardson J.A., Childs G., Harris S., Owens G.K., Olson E.N.;
"PRISM/PRDM6, a transcriptional repressor that promotes the
proliferative gene program in smooth muscle cells.";
Mol. Cell. Biol. 26:2626-2636(2006).
[24]
INTERACTION WITH HDAC9.
PubMed=16611996; DOI=10.1128/MCB.26.9.3550-3564.2006;
Morrison B.E., Majdzadeh N., Zhang X., Lyles A., Bassel-Duby R.,
Olson E.N., D'Mello S.R.;
"Neuroprotection by histone deacetylase-related protein.";
Mol. Cell. Biol. 26:3550-3564(2006).
[25]
IDENTIFICATION BY MASS SPECTROMETRY AS A COMPONENT OF A
GFI-RCOR-KDM1A-HDAC COMPLEX, INTERACTION WITH GFI1 AND GFI1B, AND
FUNCTION.
PubMed=17707228; DOI=10.1016/j.molcel.2007.06.039;
Saleque S., Kim J., Rooke H.M., Orkin S.H.;
"Epigenetic regulation of hematopoietic differentiation by Gfi-1 and
Gfi-1b is mediated by the cofactors CoREST and LSD1.";
Mol. Cell 27:562-572(2007).
[26]
INTERACTION WITH ZNF541.
PubMed=18849567; DOI=10.1074/jbc.M805590200;
Choi E., Han C., Park I., Lee B., Jin S., Choi H., Kim do H.,
Park Z.Y., Eddy E.M., Cho C.;
"A novel germ cell-specific protein, SHIP1, forms a complex with
chromatin remodeling activity during spermatogenesis.";
J. Biol. Chem. 283:35283-35294(2008).
[27]
INTERACTION WITH NR4A2.
PubMed=19144721; DOI=10.1242/dev.029769;
Jacobs F.M., van Erp S., van der Linden A.J., von Oerthel L.,
Burbach J.P., Smidt M.P.;
"Pitx3 potentiates Nurr1 in dopamine neuron terminal differentiation
through release of SMRT-mediated repression.";
Development 136:531-540(2009).
[28]
INTERACTION WITH SAMSN1.
PubMed=20478393; DOI=10.1016/j.biocel.2010.05.004;
Brandt S., Ellwanger K., Beuter-Gunia C., Schuster M., Hausser A.,
Schmitz I., Beer-Hammer S.;
"SLy2 targets the nuclear SAP30/HDAC1 complex.";
Int. J. Biochem. Cell Biol. 42:1472-1481(2010).
[29]
INTERACTION WITH TSC22D3.
STRAIN=DBA/2J; TISSUE=Myoblast;
PubMed=20124407; DOI=10.1074/jbc.M109.070136;
Bruscoli S., Donato V., Velardi E., Di Sante M., Migliorati G.,
Donato R., Riccardi C.;
"Glucocorticoid-induced leucine zipper (GILZ) and long GILZ inhibit
myogenic differentiation and mediate anti-myogenic effects of
glucocorticoids.";
J. Biol. Chem. 285:10385-10396(2010).
[30]
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).
[31]
INTERACTION WITH C10ORF90/FATS AND CDKN1A/P21.
PubMed=20154723; DOI=10.1038/onc.2010.19;
Li Z., Zhang Q., Mao J.H., Weise A., Mrasek K., Fan X., Zhang X.,
Liehr T., Lu K.H., Balmain A., Cai W.W.;
"An HDAC1-binding domain within FATS bridges p21 turnover to
radiation-induced tumorigenesis.";
Oncogene 29:2659-2671(2010).
[32]
INTERACTION WITH DDIT3.
PubMed=22242125; DOI=10.1371/journal.pone.0029498;
Alter J., Bengal E.;
"Stress-induced C/EBP homology protein (CHOP) represses MyoD
transcription to delay myoblast differentiation.";
PLoS ONE 6:E29498-E29498(2011).
[33]
INTERACTION WITH ZNF431.
PubMed=21177534; DOI=10.1074/jbc.M110.178780;
He Z., Cai J., Lim J.W., Kroll K., Ma L.;
"A novel KRAB domain-containing zinc finger transcription factor
ZNF431 directly represses Patched1 transcription.";
J. Biol. Chem. 286:7279-7289(2011).
[34]
IDENTIFICATION IN A COMPLEX WITH YY1; SIN3A AND GON4L, AND SUBCELLULAR
LOCATION.
PubMed=21454521; DOI=10.1074/jbc.M110.133603;
Lu P., Hankel I.L., Hostager B.S., Swartzendruber J.A., Friedman A.D.,
Brenton J.L., Rothman P.B., Colgan J.D.;
"The developmental regulator protein Gon4l associates with protein
YY1, co-repressor Sin3a, and histone deacetylase 1 and mediates
transcriptional repression.";
J. Biol. Chem. 286:18311-18319(2011).
[35]
FUNCTION, AND INTERACTION WITH KDM5A.
PubMed=21960634; DOI=10.1126/science.1206022;
DiTacchio L., Le H.D., Vollmers C., Hatori M., Witcher M., Secombe J.,
Panda S.;
"Histone lysine demethylase JARID1a activates CLOCK-BMAL1 and
influences the circadian clock.";
Science 333:1881-1885(2011).
[36]
INTERACTION WITH INSM1.
PubMed=24227653; DOI=10.1242/dev.097642;
Welcker J.E., Hernandez-Miranda L.R., Paul F.E., Jia S., Ivanov A.,
Selbach M., Birchmeier C.;
"Insm1 controls development of pituitary endocrine cells and requires
a SNAG domain for function and for recruitment of histone-modifying
factors.";
Development 140:4947-4958(2013).
[37]
IDENTIFICATION IN A LARGE PER COMPLEX.
PubMed=24413057; DOI=10.1038/nsmb.2746;
Duong H.A., Weitz C.J.;
"Temporal orchestration of repressive chromatin modifiers by circadian
clock Period complexes.";
Nat. Struct. Mol. Biol. 21:126-132(2014).
[38]
FUNCTION, AND INTERACTION WITH CIART.
PubMed=24736997; DOI=10.1371/journal.pbio.1001839;
Goriki A., Hatanaka F., Myung J., Kim J.K., Yoritaka T., Tanoue S.,
Abe T., Kiyonari H., Fujimoto K., Kato Y., Todo T., Matsubara A.,
Forger D., Takumi T.;
"A novel protein, CHRONO, functions as a core component of the
mammalian circadian clock.";
PLoS Biol. 12:E1001839-E1001839(2014).
[39]
IDENTIFICATION IN A COMPLEX WITH SIN3A; FAM60A; SAP30; RBBP4; OGT AND
TET1, AND INTERACTION WITH SIN3A.
PubMed=28554894; DOI=10.15252/embj.201696307;
Streubel G., Fitzpatrick D.J., Oliviero G., Scelfo A., Moran B.,
Das S., Munawar N., Watson A., Wynne K., Negri G.L., Dillon E.T.,
Jammula S., Hokamp K., O'Connor D.P., Pasini D., Cagney G.,
Bracken A.P.;
"Fam60a defines a variant Sin3a-Hdac complex in embryonic stem cells
required for self-renewal.";
EMBO J. 0:0-0(2017).
-!- 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. Deacetylates SP
proteins, SP1 and SP3, and regulates their function. Component of
the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-
mediated transcription in resting neurons. Upon calcium
stimulation, HDAC1 is released from the complex and CREBBP is
recruited, which facilitates transcriptional activation.
Deacetylates TSHZ3 and regulates its transcriptional repressor
activity. Deacetylates 'Lys-310' in RELA and thereby inhibits the
transcriptional activity of NF-kappa-B. Deacetylates NR1D2 and
abrogates the effect of KAT5-mediated relieving of NR1D2
transcription repression activity. Component of a
RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone
deacetylase (HDAC) recruitment, a number of genes implicated in
multilineage blood cell development. Involved in CIART-mediated
transcriptional repression of the circadian transcriptional
activator: CLOCK-ARNTL/BMAL1 heterodimer. Required for the
transcriptional repression of circadian target genes, such as
PER1, mediated by the large PER complex or CRY1 through histone
deacetylation. {ECO:0000269|PubMed:15226430,
ECO:0000269|PubMed:15542849, ECO:0000269|PubMed:17707228,
ECO:0000269|PubMed:21960634, ECO:0000269|PubMed:24736997}.
-!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
a histone to yield a deacetylated histone.
-!- SUBUNIT: Part of the core histone deacetylase (HDAC) complex
composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core complex
associates with MTA2, MBD2, MBD3, MTA1L1, CHD3 and CHD4 to form
the nucleosome remodeling and histone deacetylation (NuRD)
complex, or with SIN3, SAP18 and SAP30 to form the SIN3 HDAC
complex. Component of a BHC histone deacetylase complex that
contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST and
PHF21A/BHC80. The BHC complex may also contain ZMYM2, ZNF217,
ZMYM3, GSE1 and GTF2I. Component of a mSin3A corepressor complex
that contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and
HDAC2. Found in a trimeric complex with APBB1 and TSHZ3; the
interaction between HDAC1 and APBB1 is mediated by TSHZ3.
Component of a RCOR/GFI/KDM1A/HDAC complex. Part of a complex
composed of TRIM28, HDAC1, HDAC2 and EHMT2. Part of a complex
containing at least CDYL, MIER1, MIER2, HDAC1 and HDAC2. The large
PER complex involved in the histone deacetylation is composed of
at least HDAC1, PER2, SFPQ and SIN3A. Associates with the 9-1-1
complex; interacts with HUS1. Found in a complex with DNMT3A and
HDAC7. Interacts with the non-histone region of H2AFY. Interacts
with TRIM28; the interaction recruits HDAC1 to E2F1 and inhibits
its acetylation. Interacts with SP1; the interaction deacetylates
SP1 and regulates its transcriptional activity. Interacts with
SP3; the interaction deacetylates SP3 and regulates its
transcriptional activity. In vitro, C(18) ceramides increase this
interaction and the subsequent SP3 deacetylation and SP3-mediated
repression of the TERT promoter. Interacts with TSHZ3 (via N-
terminus); the interaction is direct. Interacts with APEX1; the
interaction is not dependent on the acetylated status of APEX1.
Interacts with DNTTIP1 (By similarity). Identified in a histone
deacetylase complex that contains DNTTIP1, HDAC1 and ELMSAN1; this
complex assembles into a tetramer that contains four copies of
each protein chain (By similarity). Interacts with C10orf90/FATS
(via its N-terminal); the interaction prevents binding of HDAC1 to
CDKN1A/p21 and facilitates the acetylation and stabilization of
CDKN1A/p21. Interacts with CDKN1A/p21. Interacts with CDK5
complexed to CDK5R1 (p25). Interacts directly with GFI1 and GFI1B.
Interacts with NR1D2 (via C-terminus). Interacts with TSC22D3
isoform 1; this interaction affects HDAC1 activity on MYOG
promoter and thus inhibits MYOD1 transcriptional activity.
Interacts with BAZ2A/TIP5, BANP, BCL6, BCOR, BHLHE40/DEC1, BRMS1,
BRMS1L, CBFA2T3, CHFR, CIART, CRY1, DAXX, DDIT3/CHOP, DDX5, DNMT1,
E4F1, EP300, HCFC1, HDAC9, INSM1, NFE4, NR4A2/NURR1, MIER1, KDM4A,
KDM5B, KLF1, MINT, NRIP1, PCAF, PHB2, PRDM6, PRDM16, RB1, RERE,
SAMSN1, SAP30L, SETDB1, SMAD3, SMARCA4/BRG1, SMYD2, SUV39H1, TGIF,
TGIF2, TRAF6, UHRF1, UHRF2, ZMYND15, ZNF431 and ZNF541. Interacts
with KDM5A. Interacts with CCAR2 (By similarity). Interacts with
PPHLN1 (By similarity). Found in a complex with YY1, SIN3A and
GON4L (PubMed:21454521). Interacts with CHD4 (By similarity).
Found in a complex composed of at least FAM60A, SIN3A, HDAC1,
SAP30, RBBP4, OGT and TET1 (PubMed:28554894). Interacts with SIN3A
(PubMed:28554894). {ECO:0000250|UniProtKB:Q13547,
ECO:0000269|PubMed:10615135, ECO:0000269|PubMed:10984530,
ECO:0000269|PubMed:11022042, ECO:0000269|PubMed:11533236,
ECO:0000269|PubMed:11788710, ECO:0000269|PubMed:11909966,
ECO:0000269|PubMed:12198165, ECO:0000269|PubMed:12398767,
ECO:0000269|PubMed:12616525, ECO:0000269|PubMed:14645126,
ECO:0000269|PubMed:15060175, ECO:0000269|PubMed:15140878,
ECO:0000269|PubMed:15226430, ECO:0000269|PubMed:15542849,
ECO:0000269|PubMed:15711539, ECO:0000269|PubMed:16085498,
ECO:0000269|PubMed:16107708, ECO:0000269|PubMed:16166625,
ECO:0000269|PubMed:16537907, ECO:0000269|PubMed:16611996,
ECO:0000269|PubMed:16805913, ECO:0000269|PubMed:17707228,
ECO:0000269|PubMed:18849567, ECO:0000269|PubMed:19144721,
ECO:0000269|PubMed:20124407, ECO:0000269|PubMed:20154723,
ECO:0000269|PubMed:20478393, ECO:0000269|PubMed:20675388,
ECO:0000269|PubMed:21177534, ECO:0000269|PubMed:21454521,
ECO:0000269|PubMed:21960634, ECO:0000269|PubMed:22242125,
ECO:0000269|PubMed:24227653, ECO:0000269|PubMed:24413057,
ECO:0000269|PubMed:24736997, ECO:0000269|PubMed:28554894,
ECO:0000269|PubMed:9702189}.
-!- INTERACTION:
P27699:Crem; NbExp=3; IntAct=EBI-301912, EBI-8744406;
P13864:Dnmt1; NbExp=3; IntAct=EBI-301912, EBI-301927;
Q02591:Gsc; NbExp=2; IntAct=EBI-301912, EBI-7457485;
P25799:Nfkb1; NbExp=2; IntAct=EBI-301912, EBI-643958;
Q04207:Rela; NbExp=2; IntAct=EBI-301912, EBI-644400;
O88939:Zbtb7a; NbExp=2; IntAct=EBI-301912, EBI-595063;
E9QAG8:Znf431; NbExp=3; IntAct=EBI-301912, EBI-9549639;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21454521}.
-!- TISSUE SPECIFICITY: Widely expressed with higher levels in thymus
and testis and lower levels in liver. Present in muscle (at
protein level). {ECO:0000269|PubMed:15711539}.
-!- INDUCTION: By interleukin-2.
-!- PTM: Sumoylated on Lys-444 and Lys-476; which promotes enzymatic
activity. Desumoylated by SENP1. {ECO:0000250|UniProtKB:Q13547}.
-!- PTM: Phosphorylation on Ser-421 and Ser-423 promotes enzymatic
activity and interactions with NuRD and SIN3 complexes.
Phosphorylated by CDK5. {ECO:0000250|UniProtKB:Q13547}.
-!- PTM: Ubiquitinated by CHFR and KCTD11, leading to its degradation
by the proteasome. {ECO:0000250|UniProtKB:Q13547}.
-!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X98207; CAA66870.1; -; mRNA.
EMBL; U80780; AAB68398.1; -; mRNA.
CCDS; CCDS18696.1; -.
RefSeq; NP_032254.1; NM_008228.2.
UniGene; Mm.202504; -.
UniGene; Mm.391033; -.
ProteinModelPortal; O09106; -.
SMR; O09106; -.
BioGrid; 241423; 91.
CORUM; O09106; -.
DIP; DIP-31499N; -.
IntAct; O09106; 35.
MINT; MINT-2568222; -.
STRING; 10090.ENSMUSP00000099657; -.
BindingDB; O09106; -.
ChEMBL; CHEMBL4001; -.
iPTMnet; O09106; -.
PhosphoSitePlus; O09106; -.
EPD; O09106; -.
PaxDb; O09106; -.
PeptideAtlas; O09106; -.
PRIDE; O09106; -.
Ensembl; ENSMUST00000102597; ENSMUSP00000099657; ENSMUSG00000028800.
GeneID; 433759; -.
KEGG; mmu:433759; -.
UCSC; uc008uxg.1; mouse.
CTD; 3065; -.
MGI; MGI:108086; Hdac1.
eggNOG; KOG1342; Eukaryota.
eggNOG; COG0123; LUCA.
GeneTree; ENSGT00530000062889; -.
HOGENOM; HOG000225180; -.
HOVERGEN; HBG057112; -.
InParanoid; O09106; -.
KO; K06067; -.
OMA; QNTNDYL; -.
OrthoDB; EOG091G067J; -.
PhylomeDB; O09106; -.
TreeFam; TF106171; -.
Reactome; R-MMU-1362277; Transcription of E2F targets under negative control by DREAM complex.
Reactome; R-MMU-1362300; Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1.
Reactome; R-MMU-1538133; G0 and Early G1.
Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-MMU-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
Reactome; R-MMU-3769402; Deactivation of the beta-catenin transactivating complex.
Reactome; R-MMU-427413; NoRC negatively regulates rRNA expression.
Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
Reactome; R-MMU-539107; Activation of E2F1 target genes at G1/S.
Reactome; R-MMU-573389; NoRC negatively regulates rRNA expression.
Reactome; R-MMU-6804758; Regulation of TP53 Activity through Acetylation.
Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-MMU-8943724; Regulation of PTEN gene transcription.
SABIO-RK; O09106; -.
PRO; PR:O09106; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000028800; -.
CleanEx; MM_HDAC1; -.
ExpressionAtlas; O09106; baseline and differential.
Genevisible; O09106; MM.
GO; GO:0000785; C:chromatin; ISO:MGI.
GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0000792; C:heterochromatin; IDA:MGI.
GO; GO:0000118; C:histone deacetylase complex; IPI:MGI.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0016581; C:NuRD complex; IDA:MGI.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0016580; C:Sin3 complex; ISO:MGI.
GO; GO:0005667; C:transcription factor complex; IDA:UniProtKB.
GO; GO:0017053; C:transcriptional repressor complex; IPI:MGI.
GO; GO:0033613; F:activating transcription factor binding; ISO:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0001047; F:core promoter binding; IDA:UniProtKB.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISO:MGI.
GO; GO:0019213; F:deacetylase activity; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0004407; F:histone deacetylase activity; IDA:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
GO; GO:0035851; F:Krueppel-associated box domain binding; IPI:UniProtKB.
GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
GO; GO:0051059; F:NF-kappaB binding; ISO:MGI.
GO; GO:0002039; F:p53 binding; ISO:MGI.
GO; GO:1990841; F:promoter-specific chromatin binding; IDA:MGI.
GO; GO:0033558; F:protein deacetylase activity; ISO:MGI.
GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
GO; GO:0070491; F:repressing transcription factor binding; ISO:MGI.
GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IPI:MGI.
GO; GO:0001106; F:RNA polymerase II transcription corepressor activity; ISO:MGI.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; ISO:MGI.
GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:MGI.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISO:MGI.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0043044; P:ATP-dependent chromatin remodeling; ISO:MGI.
GO; GO:0006325; P:chromatin organization; TAS:UniProtKB.
GO; GO:0000183; P:chromatin silencing at rDNA; TAS:Reactome.
GO; GO:0032922; P:circadian regulation of gene expression; IDA:UniProtKB.
GO; GO:0007623; P:circadian rhythm; IDA:UniProtKB.
GO; GO:0042733; P:embryonic digit morphogenesis; IGI:BHF-UCL.
GO; GO:0007492; P:endoderm development; IDA:MGI.
GO; GO:0009913; P:epidermal cell differentiation; IGI:BHF-UCL.
GO; GO:0061029; P:eyelid development in camera-type eye; IGI:BHF-UCL.
GO; GO:0061198; P:fungiform papilla formation; IGI:BHF-UCL.
GO; GO:0060789; P:hair follicle placode formation; IGI:BHF-UCL.
GO; GO:0021766; P:hippocampus development; IGI:MGI.
GO; GO:0016575; P:histone deacetylation; ISO:MGI.
GO; GO:0070932; P:histone H3 deacetylation; IDA:UniProtKB.
GO; GO:0070933; P:histone H4 deacetylation; IDA:UniProtKB.
GO; GO:0006346; P:methylation-dependent chromatin silencing; ISO:MGI.
GO; GO:0043922; P:negative regulation by host of viral transcription; ISO:MGI.
GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; ISO:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IGI:BHF-UCL.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IGI:MGI.
GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IGI:MGI.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IGI:MGI.
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:UniProtKB.
GO; GO:0030182; P:neuron differentiation; IGI:MGI.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IGI:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IGI:BHF-UCL.
GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IGI:MGI.
GO; GO:0010870; P:positive regulation of receptor biosynthetic process; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0006476; P:protein deacetylation; ISO:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.40.800.20; -; 1.
InterPro; IPR000286; His_deacetylse.
InterPro; IPR003084; His_deacetylse_1.
InterPro; IPR023801; His_deacetylse_dom.
PANTHER; PTHR10625; PTHR10625; 1.
Pfam; PF00850; Hist_deacetyl; 1.
PIRSF; PIRSF037913; His_deacetylse_1; 1.
PRINTS; PR01270; HDASUPER.
PRINTS; PR01271; HISDACETLASE.
1: Evidence at protein level;
Acetylation; Biological rhythms; Chromatin regulator;
Complete proteome; Hydrolase; Isopeptide bond; Methylation; Nucleus;
Phosphoprotein; Reference proteome; Repressor; S-nitrosylation;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 482 Histone deacetylase 1.
/FTId=PRO_0000114688.
REGION 9 321 Histone deacetylase.
ACT_SITE 141 141 {ECO:0000250}.
MOD_RES 74 74 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q13547}.
MOD_RES 220 220 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q13547}.
MOD_RES 261 261 S-nitrosocysteine.
{ECO:0000250|UniProtKB:P70288}.
MOD_RES 273 273 S-nitrosocysteine.
{ECO:0000250|UniProtKB:P70288}.
MOD_RES 393 393 Phosphoserine.
{ECO:0000250|UniProtKB:Q13547}.
MOD_RES 406 406 Phosphoserine.
{ECO:0000250|UniProtKB:Q92769}.
MOD_RES 409 409 Phosphoserine.
{ECO:0000250|UniProtKB:Q13547}.
MOD_RES 421 421 Phosphoserine.
{ECO:0000250|UniProtKB:Q13547}.
MOD_RES 423 423 Phosphoserine.
{ECO:0000250|UniProtKB:Q13547}.
MOD_RES 432 432 N6-methylated lysine; by EHMT2.
{ECO:0000250|UniProtKB:Q13547}.
CROSSLNK 74 74 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q92769}.
CROSSLNK 438 438 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13547}.
CROSSLNK 444 444 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
{ECO:0000250|UniProtKB:Q13547}.
CROSSLNK 444 444 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q13547}.
CROSSLNK 456 456 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q92769}.
CROSSLNK 457 457 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13547}.
CROSSLNK 473 473 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q92769}.
CROSSLNK 476 476 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
{ECO:0000250|UniProtKB:Q13547}.
CROSSLNK 476 476 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q13547}.
CROSSLNK 480 480 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13547}.
SEQUENCE 482 AA; 55075 MW; 7F64D3C17F5E4844 CRC64;
MAQTQGTKRK VCYYYDGDVG NYYYGQGHPM KPHRIRMTHN LLLNYGLYRK MEIYRPHKAN
AEEMTKYHSD DYIKFLRSIR PDNMSEYSKQ MQRFNVGEDC PVFDGLFEFC QLSTGGSVAS
AVKLNKQQTD IAVNWAGGLH HAKKSEASGF CYVNDIVLAI LELLKYHQRV LYIDIDIHHG
DGVEEAFYTT DRVMTVSFHK YGEYFPGTGD LRDIGAGKGK YYAVNYPLRD GIDDESYEAI
FKPVMSKVME MFQPSAVVLQ CGSDSLSGDR LGCFNLTIKG HAKCVEFVKS FNLPMLMLGG
GGYTIRNVAR CWTYETAVAL DTEIPNELPY NDYFEYFGPD FKLHISPSNM TNQNTNEYLE
KIKQRLFENL RMLPHAPGVQ MQAIPEDAIP EESGDEDEED PDKRISICSS DKRIACEEEF
SDSDEEGEGG RKNSSNFKKA KRVKTEDEKE KDPEEKKEVT EEEKTKEEKP EAKGVKEEVK
LA


Related products :

Catalog number Product name Quantity
AHP1420 RABBIT ANTI HISTONE DEACETYLASE 1, Product Type Polyclonal Antibody, Specificity HISTONE DEACETYLASE 1, Target Species Human, Host Rabbit, Format Purified, Isotypes Polyclonal IgG, Applications 50 µg
SCH-AHP1420 RABBIT ANTI HISTONE DEACETYLASE 1, Product Type Polyclonal Antibody, Specificity HISTONE DEACETYLASE 1, Target Species Human, Host Rabbit, Format Purified, Isotypes Polyclonal IgG, Applications 50 µg
AHP596 RABBIT ANTI HISTONE DEACETYLASE 3, Product Type Polyclonal Antibody, Specificity HISTONE DEACETYLASE 3, Target Species Human, Host Rabbit, Format Purified, Isotypes Polyclonal IgG, Applications 50 µg
SCH-AHP596 RABBIT ANTI HISTONE DEACETYLASE 3, Product Type Polyclonal Antibody, Specificity HISTONE DEACETYLASE 3, Target Species Human, Host Rabbit, Format Purified, Isotypes Polyclonal IgG, Applications 50 µg
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
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


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
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




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur