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

Mitogen-activated protein kinase HOG1 (MAP kinase HOG1) (EC 2.7.11.24) (High osmolarity glycerol response protein 1)

 HOG1_YEAST              Reviewed;         435 AA.
P32485; D6VYB1; Q06232; Q12294;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
25-OCT-2017, entry version 182.
RecName: Full=Mitogen-activated protein kinase HOG1;
Short=MAP kinase HOG1;
EC=2.7.11.24;
AltName: Full=High osmolarity glycerol response protein 1;
Name=HOG1; Synonyms=SSK3; OrderedLocusNames=YLR113W;
ORFNames=L2931, L9354.2;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7681220; DOI=10.1126/science.7681220;
Brewster J.L., de Valoir T., Dwyer N.D., Winter E., Gustin M.C.;
"An osmosensing signal transduction pathway in yeast.";
Science 259:1760-1763(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 90840 / EAY235 / FY23;
PubMed=9090053;
DOI=10.1002/(SICI)1097-0061(19970315)13:3<241::AID-YEA61>3.0.CO;2-#;
Verhasselt P., Volckaert G.;
"Sequence analysis of a 37.6 kbp cosmid clone from the right arm of
Saccharomyces cerevisiae chromosome XII, carrying YAP3, HOG1, SNR6,
tRNA-Arg3 and 23 new open reading frames, among which several
homologies to proteins involved in cell division control and to
mammalian growth factors and other animal proteins are found.";
Yeast 13:241-250(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
FUNCTION, PHOSPHORYLATION, AND MUTAGENESIS OF LYS-52; THR-174 AND
TYR-176.
PubMed=7523111;
Schueller C., Brewster J.L., Alexander M.R., Gustin M.C., Ruis H.;
"The HOG pathway controls osmotic regulation of transcription via the
stress response element (STRE) of the Saccharomyces cerevisiae CTT1
gene.";
EMBO J. 13:4382-4389(1994).
[6]
FUNCTION.
PubMed=8662716; DOI=10.1074/jbc.271.23.13875;
Norbeck J., Paehlman A.-K., Akhtar N., Blomberg A., Adler L.;
"Purification and characterization of two isoenzymes of DL-glycerol-3-
phosphatase from Saccharomyces cerevisiae. Identification of the
corresponding GPP1 and GPP2 genes and evidence for osmotic regulation
of Gpp2p expression by the osmosensing mitogen-activated protein
kinase signal transduction pathway.";
J. Biol. Chem. 271:13875-13881(1996).
[7]
FUNCTION, AND MUTAGENESIS OF LYS-52.
PubMed=8943326; DOI=10.1128/MCB.16.12.6715;
Hall J.P., Cherkasova V., Elion E., Gustin M.C., Winter E.;
"The osmoregulatory pathway represses mating pathway activity in
Saccharomyces cerevisiae: isolation of a FUS3 mutant that is
insensitive to the repression mechanism.";
Mol. Cell. Biol. 16:6715-6723(1996).
[8]
INTERACTION WITH PTP2, AND ENZYME REGULATION.
PubMed=9032256; DOI=10.1128/MCB.17.3.1289;
Wurgler-Murphy S.M., Maeda T., Witten E.A., Saito H.;
"Regulation of the Saccharomyces cerevisiae HOG1 mitogen-activated
protein kinase by the PTP2 and PTP3 protein tyrosine phosphatases.";
Mol. Cell. Biol. 17:1289-1297(1997).
[9]
INTERACTION WITH PTP2 AND PTP3, AND ENZYME REGULATION.
PubMed=9211927; DOI=10.1074/jbc.272.28.17749;
Jacoby T., Flanagan H., Faykin A., Seto A.G., Mattison C.P., Ota I.M.;
"Two protein-tyrosine phosphatases inactivate the osmotic stress
response pathway in yeast by targeting the mitogen-activated protein
kinase, Hog1.";
J. Biol. Chem. 272:17749-17755(1997).
[10]
FUNCTION.
PubMed=9744864; DOI=10.1101/gad.12.18.2874;
O'Rourke S.M., Herskowitz I.;
"The Hog1 MAPK prevents cross talk between the HOG and pheromone
response MAPK pathways in Saccharomyces cerevisiae.";
Genes Dev. 12:2874-2886(1998).
[11]
FUNCTION.
PubMed=9817752; DOI=10.1083/jcb.143.4.935;
Reynolds T.B., Hopkins B.D., Lyons M.R., Graham T.R.;
"The high osmolarity glycerol response (HOG) MAP kinase pathway
controls localization of a yeast Golgi glycosyltransferase.";
J. Cell Biol. 143:935-946(1998).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=10198063; DOI=10.1091/mbc.10.4.1147;
Reiser V., Ruis H., Ammerer G.;
"Kinase activity-dependent nuclear export opposes stress-induced
nuclear accumulation and retention of Hog1 mitogen-activated protein
kinase in the budding yeast Saccharomyces cerevisiae.";
Mol. Biol. Cell 10:1147-1161(1999).
[13]
FUNCTION.
PubMed=10970855; DOI=10.1093/emboj/19.17.4623;
Raitt D.C., Posas F., Saito H.;
"Yeast Cdc42 GTPase and Ste20 PAK-like kinase regulate Sho1-dependent
activation of the Hog1 MAPK pathway.";
EMBO J. 19:4623-4631(2000).
[14]
SUBCELLULAR LOCATION.
PubMed=10817757;
Mattison C.P., Ota I.M.;
"Two protein tyrosine phosphatases, Ptp2 and Ptp3, modulate the
subcellular localization of the Hog1 MAP kinase in yeast.";
Genes Dev. 14:1229-1235(2000).
[15]
FUNCTION, AND INTERACTION WITH RCK2.
PubMed=10805732; DOI=10.1128/MCB.20.11.3887-3895.2000;
Bilsland-Marchesan E., Arino J., Saito H., Sunnerhagen P., Posas F.;
"Rck2 kinase is a substrate for the osmotic stress-activated mitogen-
activated protein kinase Hog1.";
Mol. Cell. Biol. 20:3887-3895(2000).
[16]
FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH SKO1.
PubMed=11230135; DOI=10.1093/emboj/20.5.1123;
Proft M., Pascual-Ahuir A., de Nadal E., Arino J., Serrano R.,
Posas F.;
"Regulation of the Sko1 transcriptional repressor by the Hog1 MAP
kinase in response to osmotic stress.";
EMBO J. 20:1123-1133(2001).
[17]
FUNCTION.
PubMed=11922108; DOI=10.1266/ggs.76.393;
Toh-e A., Oguchi T.;
"Defects in glycosylphosphatidylinositol (GPI) anchor synthesis
activate Hog1 kinase and confer copper-resistance in Saccharomyces
cerevisisae.";
Genes Genet. Syst. 76:393-410(2001).
[18]
FUNCTION, AND MUTAGENESIS OF TYR-68; ASP-170; ALA-314; PHE-318;
TRP-320; PHE-322; TRP-332 AND ASN-391.
PubMed=11309396; DOI=10.1074/jbc.M101818200;
Bell M., Capone R., Pashtan I., Levitzki A., Engelberg D.;
"Isolation of hyperactive mutants of the MAPK p38/Hog1 that are
independent of MAPK kinase activation.";
J. Biol. Chem. 276:25351-25358(2001).
[19]
FUNCTION.
PubMed=11336700; DOI=10.1016/S1097-2765(01)00221-0;
Alepuz P.M., Jovanovic A., Reiser V., Ammerer G.;
"Stress-induced map kinase Hog1 is part of transcription activation
complexes.";
Mol. Cell 7:767-777(2001).
[20]
ENZYME REGULATION.
PubMed=11113180; DOI=10.1128/MCB.21.1.51-60.2001;
Warmka J., Hanneman J., Lee J., Amin D., Ota I.M.;
"Ptc1, a type 2C Ser/Thr phosphatase, inactivates the HOG pathway by
dephosphorylating the mitogen-activated protein kinase Hog1.";
Mol. Cell. Biol. 21:51-60(2001).
[21]
FUNCTION.
PubMed=11136466; DOI=10.1046/j.1365-2958.2001.02242.x;
Kapteyn J.C., ter Riet B., Vink E., Blad S., De Nobel H.,
Van Den Ende H., Klis F.M.;
"Low external pH induces HOG1-dependent changes in the organization of
the Saccharomyces cerevisiae cell wall.";
Mol. Microbiol. 39:469-479(2001).
[22]
ENZYME REGULATION.
PubMed=12455951; DOI=10.1128/EC.1.2.163-173.2002;
Winkler A., Arkind C., Mattison C.P., Burkholder A., Knoche K.,
Ota I.M.;
"Heat stress activates the yeast high-osmolarity glycerol mitogen-
activated protein kinase pathway, and protein tyrosine phosphatases
are essential under heat stress.";
Eukaryot. Cell 1:163-173(2002).
[23]
ENZYME REGULATION.
PubMed=12477803; DOI=10.1128/EC.1.6.1032-1040.2002;
Young C., Mapes J., Hanneman J., Al-Zarban S., Ota I.M.;
"Role of Ptc2 type 2C Ser/Thr phosphatase in yeast high-osmolarity
glycerol pathway inactivation.";
Eukaryot. Cell 1:1032-1040(2002).
[24]
FUNCTION.
PubMed=11796711; DOI=10.1074/jbc.M108848200;
Uesono Y., Toh-e A.;
"Transient inhibition of translation initiation by osmotic stress.";
J. Biol. Chem. 277:13848-13855(2002).
[25]
FUNCTION.
PubMed=12086627; DOI=10.1016/S1097-2765(02)00557-9;
Proft M., Struhl K.;
"Hog1 kinase converts the Sko1-Cyc8-Tup1 repressor complex into an
activator that recruits SAGA and SWI/SNF in response to osmotic
stress.";
Mol. Cell 9:1307-1317(2002).
[26]
FUNCTION, AND INTERACTION WITH HOT1; KIN28; RBP1 AND SIN4.
PubMed=12743037; DOI=10.1093/emboj/cdg243;
Alepuz P.M., de Nadal E., Zapater M., Ammerer G., Posas F.;
"Osmostress-induced transcription by Hot1 depends on a Hog1-mediated
recruitment of the RNA Pol II.";
EMBO J. 22:2433-2442(2003).
[27]
PHOSPHORYLATION AT THR-174 AND TYR-176, AND MUTAGENESIS OF THR-174 AND
TYR-176.
PubMed=12637550; DOI=10.1074/jbc.C300006200;
Bell M., Engelberg D.;
"Phosphorylation of Tyr-176 of the yeast MAPK Hog1/p38 is not vital
for Hog1 biological activity.";
J. Biol. Chem. 278:14603-14606(2003).
[28]
FUNCTION, AND INTERACTION WITH SMP1.
PubMed=12482976; DOI=10.1128/MCB.23.1.229-237.2003;
de Nadal E., Casadome L., Posas F.;
"Targeting the MEF2-like transcription factor Smp1 by the stress-
activated Hog1 mitogen-activated protein kinase.";
Mol. Cell. Biol. 23:229-237(2003).
[29]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[30]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[31]
FUNCTION.
PubMed=14680476; DOI=10.1042/BJ20031127;
Nevitt T., Pereira J., Azevedo D., Guerreiro P., Rodrigues-Pousada C.;
"Expression of YAP4 in Saccharomyces cerevisiae under osmotic
stress.";
Biochem. J. 379:367-374(2004).
[32]
FUNCTION.
PubMed=15177185; DOI=10.1016/j.dnarep.2004.03.043;
Haghnazari E., Heyer W.-D.;
"The Hog1 MAP kinase pathway and the Mec1 DNA damage checkpoint
pathway independently control the cellular responses to hydrogen
peroxide.";
DNA Repair 3:769-776(2004).
[33]
FUNCTION, AND PHOSPHORYLATION.
PubMed=15060153; DOI=10.1128/MCB.24.8.3307-3323.2004;
Lawrence C.L., Botting C.H., Antrobus R., Coote P.J.;
"Evidence of a new role for the high-osmolarity glycerol mitogen-
activated protein kinase pathway in yeast: regulating adaptation to
citric acid stress.";
Mol. Cell. Biol. 24:3307-3323(2004).
[34]
FUNCTION, AND INTERACTION WITH RPD3.
PubMed=14737171; DOI=10.1038/nature02258;
De Nadal E., Zapater M., Alepuz P.M., Sumoy L., Mas G., Posas F.;
"The MAPK Hog1 recruits Rpd3 histone deacetylase to activate
osmoresponsive genes.";
Nature 427:370-374(2004).
[35]
FUNCTION, AND INTERACTION WITH SIC1.
PubMed=15448699; DOI=10.1038/ncb1174;
Escote X., Zapater M., Clotet J., Posas F.;
"Hog1 mediates cell-cycle arrest in G1 phase by the dual targeting of
Sic1.";
Nat. Cell Biol. 6:997-1002(2004).
[36]
SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=15707964; DOI=10.1016/j.bbrc.2005.01.039;
Sharma P., Mondal A.K.;
"Evidence that C-terminal non-kinase domain of Pbs2p has a role in
high osmolarity-induced nuclear localization of Hog1p.";
Biochem. Biophys. Res. Commun. 328:906-913(2005).
[37]
FUNCTION.
PubMed=16260593; DOI=10.1128/MCB.25.22.9753-9763.2005;
Vasudevan S., Garneau N., Tu Khounh D., Peltz S.W.;
"p38 mitogen-activated protein kinase/Hog1p regulates translation of
the AU-rich-element-bearing MFA2 transcript.";
Mol. Cell. Biol. 25:9753-9763(2005).
[38]
FUNCTION.
PubMed=15773992; DOI=10.1111/j.1365-2958.2005.04533.x;
Aguilera J., Rodriguez-Vargas S., Prieto J.A.;
"The HOG MAP kinase pathway is required for the induction of
methylglyoxal-responsive genes and determines methylglyoxal resistance
in Saccharomyces cerevisiae.";
Mol. Microbiol. 56:228-239(2005).
[39]
FUNCTION.
PubMed=16321140; DOI=10.1042/BJ20051243;
Prick T., Thumm M., Koehrer K., Haeussinger D., Vom Dahl S.;
"In yeast, loss of Hog1 leads to osmosensitivity of autophagy.";
Biochem. J. 394:153-161(2006).
[40]
FUNCTION.
PubMed=16688223; DOI=10.1038/sj.emboj.7601095;
Clotet J., Escote X., Adrover M.A., Yaakov G., Gari E., Aldea M.,
de Nadal E., Posas F.;
"Phosphorylation of Hsl1 by Hog1 leads to a G2 arrest essential for
cell survival at high osmolarity.";
EMBO J. 25:2338-2346(2006).
[41]
PHOSPHORYLATION.
PubMed=16467474; DOI=10.1128/EC.5.2.330-346.2006;
Chasse S.A., Flanary P., Parnell S.C., Hao N., Cha J.Y.,
Siderovski D.P., Dohlman H.G.;
"Genome-scale analysis reveals Sst2 as the principal regulator of
mating pheromone signaling in the yeast Saccharomyces cerevisiae.";
Eukaryot. Cell 5:330-346(2006).
[42]
FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
LYS-52 AND ASP-144.
PubMed=16896207; DOI=10.1128/EC.00037-06;
Westfall P.J., Thorner J.;
"Analysis of mitogen-activated protein kinase signaling specificity in
response to hyperosmotic stress: use of an analog-sensitive HOG1
allele.";
Eukaryot. Cell 5:1215-1228(2006).
[43]
FUNCTION, AND PHOSPHORYLATION.
PubMed=16920868; DOI=10.1128/EC.00225-06;
Sotelo J., Rodriguez-Gabriel M.A.;
"Mitogen-activated protein kinase Hog1 is essential for the response
to arsenite in Saccharomyces cerevisiae.";
Eukaryot. Cell 5:1826-1830(2006).
[44]
FUNCTION, AND PHOSPHORYLATION.
PubMed=16371351; DOI=10.1074/jbc.M512736200;
Panadero J., Pallotti C., Rodriguez-Vargas S., Randez-Gil F.,
Prieto J.A.;
"A downshift in temperature activates the high osmolarity glycerol
(HOG) pathway, which determines freeze tolerance in Saccharomyces
cerevisiae.";
J. Biol. Chem. 281:4638-4645(2006).
[45]
FUNCTION, INDUCTION, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
PubMed=16790423; DOI=10.1074/jbc.M603753200;
Marques J.M., Rodrigues R.J., de Magalhaes-Sant'ana A.C.,
Goncalves T.;
"Saccharomyces cerevisiae Hog1 protein phosphorylation upon exposure
to bacterial endotoxin.";
J. Biol. Chem. 281:24687-24694(2006).
[46]
FUNCTION, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
PubMed=16885417; DOI=10.1091/mbc.E06-04-0315;
Thorsen M., Di Y., Taengemo C., Morillas M., Ahmadpour D.,
Van der Does C., Wagner A., Johansson E., Boman J., Posas F.,
Wysocki R., Tamas M.J.;
"The MAPK Hog1p modulates Fps1p-dependent arsenite uptake and
tolerance in yeast.";
Mol. Biol. Cell 17:4400-4410(2006).
[47]
FUNCTION, AND INTERACTION WITH RPB1.
PubMed=16857590; DOI=10.1016/j.molcel.2006.05.031;
Proft M., Mas G., de Nadal E., Vendrell A., Noriega N., Struhl K.,
Posas F.;
"The stress-activated Hog1 kinase is a selective transcriptional
elongation factor for genes responding to osmotic stress.";
Mol. Cell 23:241-250(2006).
[48]
FUNCTION, AND MUTAGENESIS OF LYS-52.
PubMed=17363249; DOI=10.1016/j.cub.2007.02.044;
Hao N., Behar M., Parnell S.C., Torres M.P., Borchers C.H.,
Elston T.C., Dohlman H.G.;
"A systems-biology analysis of feedback inhibition in the Sho1
osmotic-stress-response pathway.";
Curr. Biol. 17:659-667(2007).
[49]
FUNCTION, INTERACTION WITH CDC37, AND PHOSPHORYLATION.
PubMed=17220467; DOI=10.1128/EC.00343-06;
Hawle P., Horst D., Bebelman J.-P., Yang X.X., Siderius M.,
van der Vies S.M.;
"Cdc37p is required for stress-induced high-osmolarity glycerol and
protein kinase C mitogen-activated protein kinase pathway
functionality by interaction with Hog1p and Slt2p (Mpk1p).";
Eukaryot. Cell 6:521-532(2007).
[50]
FUNCTION, AND PHOSPHORYLATION.
PubMed=17346711; DOI=10.1016/j.febslet.2007.02.032;
Kim S., Shah K.;
"Dissecting yeast Hog1 MAP kinase pathway using a chemical genetic
approach.";
FEBS Lett. 581:1209-1216(2007).
[51]
FUNCTION.
PubMed=17429070; DOI=10.1091/mbc.E06-10-0946;
Guha N., Desai P., Vancura A.;
"Plc1p is required for SAGA recruitment and derepression of Sko1p-
regulated genes.";
Mol. Biol. Cell 18:2419-2428(2007).
[52]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[53]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-176, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[54]
ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- FUNCTION: Mitogen-activated protein kinase involved in a signal
transduction pathway that is activated by changes in the
osmolarity of the extracellular environment. Controls osmotic
regulation of transcription via the stress response element (STRE)
in promoters of target genes. Upon osmotic shock, associates with
the SKO1-SSN6-TUP1 complex, phosphorylates SKO1, and converts it
into an activator that subsequently recruits Swi/Snf and SAGA
complexes. Activates the SMP1 transcription factor and the RCK2
kinase, both also involved in the regulation of the expression of
a subset of osmotic stress-related genes. Phosphorylation of HSL1
by HOG1 leads to a G2 arrest essential for cell survival at high
osmolarity. Mediates also cell-cycle arrest in G1 phase by the
dual targeting of SIC1. Regulates MFA2 ARE-mediated translation in
response to carbon source. Targets RDP3 histone deacetylase to
osmoresponsive promoters to induce gene expression on stress.
Plays an essential role in maintaining water homeostasis, arsenite
detoxification, copper-resistance, hydrogen peroxide response,
adaptation to citric acid stress, and repression of the mating
pathway activity. Required for the Golgi apparatus localization of
MNN1. {ECO:0000269|PubMed:10198063, ECO:0000269|PubMed:10805732,
ECO:0000269|PubMed:10970855, ECO:0000269|PubMed:11136466,
ECO:0000269|PubMed:11230135, ECO:0000269|PubMed:11309396,
ECO:0000269|PubMed:11336700, ECO:0000269|PubMed:11796711,
ECO:0000269|PubMed:11922108, ECO:0000269|PubMed:12086627,
ECO:0000269|PubMed:12482976, ECO:0000269|PubMed:12743037,
ECO:0000269|PubMed:14680476, ECO:0000269|PubMed:14737171,
ECO:0000269|PubMed:15060153, ECO:0000269|PubMed:15177185,
ECO:0000269|PubMed:15448699, ECO:0000269|PubMed:15773992,
ECO:0000269|PubMed:16260593, ECO:0000269|PubMed:16321140,
ECO:0000269|PubMed:16371351, ECO:0000269|PubMed:16688223,
ECO:0000269|PubMed:16790423, ECO:0000269|PubMed:16857590,
ECO:0000269|PubMed:16885417, ECO:0000269|PubMed:16896207,
ECO:0000269|PubMed:16920868, ECO:0000269|PubMed:17220467,
ECO:0000269|PubMed:17346711, ECO:0000269|PubMed:17363249,
ECO:0000269|PubMed:17429070, ECO:0000269|PubMed:7523111,
ECO:0000269|PubMed:8662716, ECO:0000269|PubMed:8943326,
ECO:0000269|PubMed:9744864, ECO:0000269|PubMed:9817752}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Activated by tyrosine and threonine
phosphorylation. Is phosphorylated on Tyr-176 by PBS2. Inactivated
by dephosphorylation by NBP2 after adaptation to osmotic stress.
PTP2 and PTP3 inactivate HOG1 by dephosphorylating Tyr-176, while
the PP2Cs PTC1 and PTC2 or PTC3 dephosphorylate Thr-174 in the
activation loop. {ECO:0000269|PubMed:11113180,
ECO:0000269|PubMed:12455951, ECO:0000269|PubMed:12477803,
ECO:0000269|PubMed:9032256, ECO:0000269|PubMed:9211927}.
-!- SUBUNIT: Interacts with CDC37, HOT1, KIN28, PTP2, PTP3, RBP1,
RCK2, RPD3, SIC1, SMP1 and SIN4. {ECO:0000269|PubMed:10805732,
ECO:0000269|PubMed:11230135, ECO:0000269|PubMed:12482976,
ECO:0000269|PubMed:12743037, ECO:0000269|PubMed:14737171,
ECO:0000269|PubMed:15448699, ECO:0000269|PubMed:16857590,
ECO:0000269|PubMed:17220467, ECO:0000269|PubMed:9032256,
ECO:0000269|PubMed:9211927}.
-!- INTERACTION:
Q03213:HOT1; NbExp=4; IntAct=EBI-8437, EBI-27376;
P34244:HSL1; NbExp=2; IntAct=EBI-8437, EBI-9771;
P25588:MRC1; NbExp=4; IntAct=EBI-8437, EBI-412442;
P38623:RCK2; NbExp=4; IntAct=EBI-8437, EBI-14885;
P38634:SIC1; NbExp=4; IntAct=EBI-8437, EBI-17127;
P06784:STE7; NbExp=2; IntAct=EBI-8437, EBI-18389;
Q01477:UBP3; NbExp=3; IntAct=EBI-8437, EBI-19834;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly
cytoplasmic in unstressed cells but rapidly concentrates within
the nucleus in response to hyperosmotic conditions and
phosphorylation.
-!- INDUCTION: By osmotic stress, cold stress, citric acid, and in
presence of bacterial lipopolysaccharides (LPS).
{ECO:0000269|PubMed:16790423}.
-!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
whose phosphorylation activates the MAP kinases.
-!- PTM: Dually phosphorylated on Thr-174 and Tyr-176, which activates
the enzyme. {ECO:0000269|PubMed:10198063,
ECO:0000269|PubMed:11230135, ECO:0000269|PubMed:12637550,
ECO:0000269|PubMed:15060153, ECO:0000269|PubMed:15707964,
ECO:0000269|PubMed:16371351, ECO:0000269|PubMed:16467474,
ECO:0000269|PubMed:16790423, ECO:0000269|PubMed:16885417,
ECO:0000269|PubMed:16896207, ECO:0000269|PubMed:16920868,
ECO:0000269|PubMed:17220467, ECO:0000269|PubMed:17346711,
ECO:0000269|PubMed:7523111}.
-!- MISCELLANEOUS: Present with 6780 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. MAP kinase subfamily. HOG1 sub-subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L06279; AAA34680.1; -; Genomic_DNA.
EMBL; U53878; AAB67558.1; -; Genomic_DNA.
EMBL; Z73285; CAA97680.1; -; Genomic_DNA.
EMBL; X89514; CAA61691.1; -; Genomic_DNA.
EMBL; BK006945; DAA09427.1; -; Genomic_DNA.
PIR; S64950; S64950.
RefSeq; NP_013214.1; NM_001182000.1.
ProteinModelPortal; P32485; -.
SMR; P32485; -.
BioGrid; 31384; 465.
DIP; DIP-1558N; -.
ELM; P32485; -.
IntAct; P32485; 32.
MINT; MINT-404719; -.
STRING; 4932.YLR113W; -.
iPTMnet; P32485; -.
MaxQB; P32485; -.
PRIDE; P32485; -.
EnsemblFungi; YLR113W; YLR113W; YLR113W.
GeneID; 850803; -.
KEGG; sce:YLR113W; -.
EuPathDB; FungiDB:YLR113W; -.
SGD; S000004103; HOG1.
GeneTree; ENSGT00550000074271; -.
HOGENOM; HOG000233024; -.
InParanoid; P32485; -.
KO; K04441; -.
OMA; EQFQQVY; -.
OrthoDB; EOG092C2FL8; -.
BioCyc; YEAST:G3O-32258-MONOMER; -.
BRENDA; 2.7.11.24; 984.
Reactome; R-SCE-168638; NOD1/2 Signaling Pathway.
Reactome; R-SCE-171007; p38MAPK events.
Reactome; R-SCE-193648; NRAGE signals death through JNK.
Reactome; R-SCE-198753; ERK/MAPK targets.
Reactome; R-SCE-2559580; Oxidative Stress Induced Senescence.
Reactome; R-SCE-2871796; FCERI mediated MAPK activation.
Reactome; R-SCE-375170; CDO in myogenesis.
Reactome; R-SCE-418592; ADP signalling through P2Y purinoceptor 1.
Reactome; R-SCE-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-SCE-450302; activated TAK1 mediates p38 MAPK activation.
Reactome; R-SCE-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
Reactome; R-SCE-6798695; Neutrophil degranulation.
PRO; PR:P32485; -.
Proteomes; UP000002311; Chromosome XII.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005516; F:calmodulin binding; IPI:SGD.
GO; GO:0003682; F:chromatin binding; IDA:SGD.
GO; GO:0004707; F:MAP kinase activity; IDA:SGD.
GO; GO:0034605; P:cellular response to heat; IMP:SGD.
GO; GO:0071310; P:cellular response to organic substance; IBA:GO_Central.
GO; GO:0071470; P:cellular response to osmotic stress; IMP:SGD.
GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IBA:GO_Central.
GO; GO:0006972; P:hyperosmotic response; IMP:SGD.
GO; GO:0007231; P:osmosensory signaling pathway; IMP:SGD.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:SGD.
GO; GO:0061393; P:positive regulation of transcription from RNA polymerase II promoter in response to osmotic stress; IMP:SGD.
GO; GO:0006468; P:protein phosphorylation; IDA:SGD.
GO; GO:0016241; P:regulation of macroautophagy; IMP:SGD.
GO; GO:0033262; P:regulation of nuclear cell cycle DNA replication; IDA:SGD.
GO; GO:0061392; P:regulation of transcription from RNA polymerase II promoter in response to osmotic stress; IDA:SGD.
GO; GO:0046685; P:response to arsenic-containing substance; IMP:SGD.
GO; GO:0051403; P:stress-activated MAPK cascade; IBA:GO_Central.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR003527; MAP_kinase_CS.
InterPro; IPR008352; MAPK_p38.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
PRINTS; PR01773; P38MAPKINASE.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS01351; MAPK; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Acetylation; Activator; ATP-binding; Complete proteome; Cytoplasm;
Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Transcription;
Transcription regulation; Transferase.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 435 Mitogen-activated protein kinase HOG1.
/FTId=PRO_0000186331.
DOMAIN 23 302 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 29 37 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 174 176 TXY.
COMPBIAS 364 379 Ala-rich.
ACT_SITE 144 144 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 52 52 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2 2 N-acetylthreonine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 174 174 Phosphothreonine.
{ECO:0000269|PubMed:12637550}.
MOD_RES 176 176 Phosphotyrosine.
{ECO:0000244|PubMed:19779198,
ECO:0000269|PubMed:12637550}.
MUTAGEN 52 52 K->R: Impairs catalytic activity, nuclear
translocation, expression of CTT1 and
increases sensitivity to osmotic shock.
{ECO:0000269|PubMed:16896207,
ECO:0000269|PubMed:17363249,
ECO:0000269|PubMed:7523111,
ECO:0000269|PubMed:8943326}.
MUTAGEN 68 68 Y->H: Activates HOG1 in a constitutive
manner, without the need of a stimulating
stress. {ECO:0000269|PubMed:11309396}.
MUTAGEN 144 144 D->A: Impairs catalytic activity and
nuclear translocation.
{ECO:0000269|PubMed:16896207}.
MUTAGEN 170 170 D->A: Activates HOG1 in a constitutive
manner, without the need of a stimulating
stress. {ECO:0000269|PubMed:11309396}.
MUTAGEN 174 174 T->A: Impairs catalytic activity,
expression of CTT1 and increases
sensitivity to osmotic shock.
{ECO:0000269|PubMed:12637550,
ECO:0000269|PubMed:7523111}.
MUTAGEN 176 176 Y->F: Impairs expression of CTT1 and
increases sensitivity to osmotic shock.
{ECO:0000269|PubMed:12637550,
ECO:0000269|PubMed:7523111}.
MUTAGEN 314 314 A->T: Activates HOG1 in a constitutive
manner, without the need of a stimulating
stress. {ECO:0000269|PubMed:11309396}.
MUTAGEN 318 318 F->L,S: Activates HOG1 in a constitutive
manner, without the need of a stimulating
stress. {ECO:0000269|PubMed:11309396}.
MUTAGEN 320 320 W->R: Activates HOG1 in a constitutive
manner, without the need of a stimulating
stress. {ECO:0000269|PubMed:11309396}.
MUTAGEN 322 322 F->L: Activates HOG1 in a constitutive
manner, without the need of a stimulating
stress. {ECO:0000269|PubMed:11309396}.
MUTAGEN 332 332 W->R: Activates HOG1 in a constitutive
manner, without the need of a stimulating
stress. {ECO:0000269|PubMed:11309396}.
MUTAGEN 391 391 N->D: Activates HOG1 in a constitutive
manner, without the need of a stimulating
stress. {ECO:0000269|PubMed:11309396}.
CONFLICT 9 9 R -> G (in Ref. 2; AAB67558).
{ECO:0000305}.
CONFLICT 409 435 VSDHVAANDTITDYGNQAIQYANEFQQ -> GQRSCSCK
(in Ref. 1; AAA34680). {ECO:0000305}.
SEQUENCE 435 AA; 48858 MW; D95A20242587CE06 CRC64;
MTTNEEFIRT QIFGTVFEIT NRYNDLNPVG MGAFGLVCSA TDTLTSQPVA IKKIMKPFST
AVLAKRTYRE LKLLKHLRHE NLICLQDIFL SPLEDIYFVT ELQGTDLHRL LQTRPLEKQF
VQYFLYQILR GLKYVHSAGV IHRDLKPSNI LINENCDLKI CDFGLARIQD PQMTGYVSTR
YYRAPEIMLT WQKYDVEVDI WSAGCIFAEM IEGKPLFPGK DHVHQFSIIT DLLGSPPKDV
INTICSENTL KFVTSLPHRD PIPFSERFKT VEPDAVDLLE KMLVFDPKKR ITAADALAHP
YSAPYHDPTD EPVADAKFDW HFNDADLPVD TWRVMMYSEI LDFHKIGGSD GQIDISATFD
DQVAAATAAA AQAQAQAQAQ VQLNMAAHSH NGAGTTGNDH SDIAGGNKVS DHVAANDTIT
DYGNQAIQYA NEFQQ


Related products :

Catalog number Product name Quantity
10-782-55060 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.05 mg
10-782-55060 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.02 mg
10-782-55059 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.02 mg
10-782-55059 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.01 mg
10-782-55059 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.005 mg
10-782-55059 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.001 mg
EIAAB24970 Leucine zipper- and sterile alpha motif kinase ZAK,Mitogen-activated protein kinase kinase kinase MLT,Mixed lineage kinase-related kinase,MLK-like mitogen-activated protein triple kinase,MLK-related k
EIAAB24870 Homo sapiens,Human,MAP kinase 13,MAP kinase p38 delta,MAPK 13,MAPK13,Mitogen-activated protein kinase 13,Mitogen-activated protein kinase p38 delta,PRKM13,SAPK4,Stress-activated protein kinase 4
EIAAB24864 Homo sapiens,Human,MAP kinase 11,MAP kinase p38 beta,MAPK 11,MAPK11,Mitogen-activated protein kinase 11,Mitogen-activated protein kinase p38 beta,p38-2,p38b,PRKM11,SAPK2,Stress-activated protein kinas
EIAAB24872 MAP kinase 13,MAP kinase p38 delta,MAPK 13,Mapk13,Mitogen-activated protein kinase 13,Mitogen-activated protein kinase p38 delta,Mouse,Mus musculus,Serk4,Stress-activated protein kinase 4
U1206b CLIA Bos taurus,Bovine,ERK2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAPK 1,MAPK 2,MAPK1,Mitogen-activated protein kinase 1,Mitogen-activated protein kinase 2,PRKM1 96T
E1206b ELISA Bos taurus,Bovine,ERK2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAPK 1,MAPK 2,MAPK1,Mitogen-activated protein kinase 1,Mitogen-activated protein kinase 2,PRKM 96T
EIAAB24867 ERK6,ERK-6,Extracellular signal-regulated kinase 6,Homo sapiens,Human,MAP kinase 12,MAP kinase p38 gamma,MAPK 12,MAPK12,Mitogen-activated protein kinase 12,Mitogen-activated protein kinase p38 gamma,S
E1206b ELISA kit Bos taurus,Bovine,ERK2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAPK 1,MAPK 2,MAPK1,Mitogen-activated protein kinase 1,Mitogen-activated protein kinase 2 96T
EIAAB24866 ERK-6,Extracellular signal-regulated kinase 6,MAP kinase 12,MAP kinase p38 gamma,MAPK 12,Mapk12,Mitogen-activated protein kinase 12,Mitogen-activated protein kinase p38 gamma,Mouse,Mus musculus,Sapk3,
EIAAB24869 MAP kinase 13,MAP kinase p38 delta,MAPK 13,Mapk13,Mitogen-activated protein kinase 13,Mitogen-activated protein kinase p38 delta,Rat,Rattus norvegicus,Stress-activated protein kinase 4
EIAAB24868 ERK-6,Extracellular signal-regulated kinase 6,MAP kinase 12,MAP kinase p38 gamma,MAPK 12,Mapk12,Mitogen-activated protein kinase 12,Mitogen-activated protein kinase p38 gamma,Rat,Rattus norvegicus,Sap
U1206m CLIA Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protein kina 96T
U1206r CLIA Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protein kina 96T
EIAAB41234 Homo sapiens,Human,MAP3K7IP3,Mitogen-activated protein kinase kinase kinase 7-interacting protein 3,NF-kappa-B-activating protein 1,TAB3,TAB-3,TAK1-binding protein 3,TGF-beta-activated kinase 1 and MA
E1206m ELISA Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protein kin 96T
E1206r ELISA Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protein kin 96T
EIAAB25244 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,JNK kinase 2,JNK-activating kinase 2,JNKK 2,MAP kinase kinase 7,Map2k7,MAPK_ERK kinase 7,MAPKK 7,MEK 7,Mkk7,
EIAAB25239 C-JUN N-terminal kinase kinase 1,Dual specificity mitogen-activated protein kinase kinase 4,JNK kinase 1,JNK-activating kinase 1,JNKK 1,Jnkk1,MAP kinase kinase 4,Map2k4,MAPK_ERK kinase 4,MAPKK 4,MEK 4
EIAAB25245 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,JNK kinase 2,JNK-activating kinase 2,JNKK 2,MAP kinase kinase 7,Map2k7,MAPK_ERK kinase 7,MAPKK 7,MEK 7,Rat,R


 

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