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

Serine/threonine-protein kinase STK11 (EC 2.7.11.1) (Liver kinase B1 homolog) (LKB1) (mLKB1)

 STK11_MOUSE             Reviewed;         436 AA.
Q9WTK7; B3VBP0; Q3TAE0;
28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
27-SEP-2017, entry version 152.
RecName: Full=Serine/threonine-protein kinase STK11;
EC=2.7.11.1;
AltName: Full=Liver kinase B1 homolog;
Short=LKB1;
Short=mLKB1;
Flags: Precursor;
Name=Stk11 {ECO:0000312|MGI:MGI:1341870};
Synonyms=Lkb1 {ECO:0000312|EMBL:AAD55368.1};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305, ECO:0000312|EMBL:AAD22100.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DEVELOPMENTAL STAGE.
PubMed=10381580; DOI=10.1016/S0925-4773(99)00050-7;
Luukko K., Ylikorkala A., Tiainen M., Makela T.P.;
"Expression of LKB1 and PTEN tumor suppressor genes during mouse
embryonic development.";
Mech. Dev. 83:187-190(1999).
[2] {ECO:0000305, ECO:0000312|EMBL:AAD55368.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND SUBCELLULAR
LOCATION.
STRAIN=129 {ECO:0000312|EMBL:AAD55368.1};
PubMed=10400995; DOI=10.1093/hmg/8.8.1479;
Smith D.P., Spicer J., Smith A., Swift S., Ashworth A.;
"The mouse Peutz-Jeghers syndrome gene Lkb1 encodes a nuclear protein
kinase.";
Hum. Mol. Genet. 8:1479-1485(1999).
[3] {ECO:0000305, ECO:0000312|EMBL:AAF21370.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, PALMITOYLATION AT CYS-422, PHOSPHORYLATION AT SER-431,
ISOPRENYLATION AT CYS-433, AND MUTAGENESIS OF SER-431 AND CYS-433.
PubMed=10642527; DOI=10.1042/bj3450673;
Collins S.P., Reoma J.L., Gamm D.M., Uhler M.D.;
"LKB1, a novel serine/threonine protein kinase and potential tumour
suppressor, is phosphorylated by cAMP-dependent protein kinase (PKA)
and prenylated in vivo.";
Biochem. J. 345:673-680(2000).
[4] {ECO:0000305, ECO:0000312|EMBL:BAA76749.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE, AND
DISRUPTION PHENOTYPE.
STRAIN=Swiss Webster / NIH {ECO:0000312|EMBL:BAA76749.1};
TISSUE=Embryo {ECO:0000312|EMBL:BAA76749.1};
PubMed=12060709; DOI=10.1073/pnas.122254599;
Jishage K., Nezu J., Kawase Y., Iwata T., Watanabe M., Miyoshi A.,
Ose A., Habu K., Kake T., Kamada N., Ueda O., Kinoshita M.,
Jenne D.E., Shimane M., Suzuki H.;
"Role of Lkb1, the causative gene of Peutz-Jegher's syndrome, in
embryogenesis and polyposis.";
Proc. Natl. Acad. Sci. U.S.A. 99:8903-8908(2002).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Ido Y., Lan F.;
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000305, ECO:0000312|EMBL:BAE42977.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=NOD {ECO:0000312|EMBL:BAE42977.1};
TISSUE=Spleen {ECO:0000312|EMBL:BAE42977.1};
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[7] {ECO:0000305, ECO:0000312|EMBL:AAH52379.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH52379.1};
TISSUE=Brain {ECO:0000312|EMBL:AAH52379.1};
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).
[8]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-431, ISOPRENYLATION AT
CYS-433, AND MUTAGENESIS OF SER-431 AND CYS-433.
PubMed=11297520; DOI=10.1074/jbc.M009953200;
Sapkota G.P., Kieloch A., Lizcano J.M., Lain S., Arthur J.S.,
Williams M.R., Morrice N., Deak M., Alessi D.R.;
"Phosphorylation of the protein kinase mutated in Peutz-Jeghers cancer
syndrome, LKB1/STK11, at Ser431 by p90(RSK) and cAMP-dependent protein
kinase, but not its farnesylation at Cys(433), is essential for LKB1
to suppress cell vrowth.";
J. Biol. Chem. 276:19469-19482(2001).
[9]
DISRUPTION PHENOTYPE.
PubMed=11509733; DOI=10.1126/science.1062074;
Ylikorkala A., Rossi D.J., Korsisaari N., Luukko K., Alitalo K.,
Henkemeyer M., Makela T.P.;
"Vascular abnormalities and deregulation of VEGF in Lkb1-deficient
mice.";
Science 293:1323-1326(2001).
[10]
SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT SER-31;
SER-325; THR-336 AND THR-366, ISOPRENYLATION AT CYS-433, METHYLATION
AT CYS-433, AND MUTAGENESIS OF SER-31; ASP-194; SER-325; THR-336;
THR-366 AND CYS-433.
PubMed=11853558; DOI=10.1042/0264-6021:3620481;
Sapkota G.P., Boudeau J., Deak M., Kieloch A., Morrice N.,
Alessi D.R.;
"Identification and characterization of four novel phosphorylation
sites (Ser31, Ser325, Thr336 and Thr366) on LKB1/STK11, the protein
kinase mutated in Peutz-Jeghers cancer syndrome.";
Biochem. J. 362:481-490(2002).
[11]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-366, AND MUTAGENESIS OF
THR-366.
PubMed=12234250; DOI=10.1042/BJ20021284;
Sapkota G.P., Deak M., Kieloch A., Morrice N., Goodarzi A.A.,
Smythe C., Shiloh Y., Lees-Miller S.P., Alessi D.R.;
"Ionizing radiation induces ataxia telangiectasia mutated kinase
(ATM)-mediated phosphorylation of LKB1/STK11 at Thr-366.";
Biochem. J. 368:507-516(2002).
[12]
DISRUPTION PHENOTYPE.
PubMed=11956081;
Miyoshi H., Nakau M., Ishikawa T.O., Seldin M.F., Oshima M.,
Taketo M.M.;
"Gastrointestinal hamartomatous polyposis in Lkb1 heterozygous
knockout mice.";
Cancer Res. 62:2261-2266(2002).
[13]
DISRUPTION PHENOTYPE.
PubMed=12226664; DOI=10.1038/nature01045;
Bardeesy N., Sinha M., Hezel A.F., Signoretti S., Hathaway N.A.,
Sharpless N.E., Loda M., Carrasco D.R., DePinho R.A.;
"Loss of the Lkb1 tumour suppressor provokes intestinal polyposis but
resistance to transformation.";
Nature 419:162-167(2002).
[14]
DISRUPTION PHENOTYPE.
PubMed=12218179; DOI=10.1073/pnas.192301399;
Rossi D.J., Ylikorkala A., Korsisaari N., Salovaara R., Luukko K.,
Launonen V., Henkemeyer M., Ristimaki A., Aaltonen L.A., Makela T.P.;
"Induction of cyclooxygenase-2 in a mouse model of Peutz-Jeghers
polyposis.";
Proc. Natl. Acad. Sci. U.S.A. 99:12327-12332(2002).
[15]
DISRUPTION PHENOTYPE.
PubMed=15480979; DOI=10.1053/j.gastro.2004.07.059;
Udd L., Katajisto P., Rossi D.J., Lepisto A., Lahesmaa A.M.,
Ylikorkala A., Jarvinen H.J., Ristimaki A.P., Makela T.P.;
"Suppression of Peutz-Jeghers polyposis by inhibition of
cyclooxygenase-2.";
Gastroenterology 127:1030-1037(2004).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[17]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16308421; DOI=10.1126/science.1120781;
Shaw R.J., Lamia K.A., Vasquez D., Koo S.-H., Bardeesy N.,
Depinho R.A., Montminy M., Cantley L.C.;
"The kinase LKB1 mediates glucose homeostasis in liver and therapeutic
effects of metformin.";
Science 310:1642-1646(2005).
[18]
FUNCTION, PHOSPHORYLATION AT SER-431, MUTAGENESIS OF SER-431,
SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND INTERACTION WITH
STRADA.
PubMed=17482548; DOI=10.1016/j.cell.2007.03.025;
Barnes A.P., Lilley B.N., Pan Y.A., Plummer L.J., Powell A.W.,
Raines A.N., Sanes J.R., Polleux F.;
"LKB1 and SAD kinases define a pathway required for the polarization
of cortical neurons.";
Cell 129:549-563(2007).
[19]
FUNCTION, PHOSPHORYLATION AT SER-431, AND MUTAGENESIS OF SER-431.
PubMed=17482549; DOI=10.1016/j.cell.2007.04.012;
Shelly M., Cancedda L., Heilshorn S., Sumbre G., Poo M.M.;
"LKB1/STRAD promotes axon initiation during neuronal polarization.";
Cell 129:565-577(2007).
[20]
ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), FUNCTION (ISOFORM 2), TISSUE
SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=18774945; DOI=10.1042/BJ20081447;
Towler M.C., Fogarty S., Hawley S.A., Pan D.A., Martin D.M.,
Morrice N.A., McCarthy A., Galardo M.N., Meroni S.B., Cigorraga S.B.,
Ashworth A., Sakamoto K., Hardie D.G.;
"A novel short splice variant of the tumour suppressor LKB1 is
required for spermiogenesis.";
Biochem. J. 416:1-14(2008).
[21]
ACETYLATION.
PubMed=18687677; DOI=10.1074/jbc.M805711200;
Lan F., Cacicedo J.M., Ruderman N., Ido Y.;
"SIRT1 modulation of the acetylation status, cytosolic localization,
and activity of LKB1. Possible role in AMP-activated protein kinase
activation.";
J. Biol. Chem. 283:27628-27635(2008).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[23]
ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
PubMed=18854309; DOI=10.1074/jbc.M806153200;
Denison F.C., Hiscock N.J., Carling D., Woods A.;
"Characterization of an alternative splice variant of LKB1.";
J. Biol. Chem. 284:67-76(2009).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Kidney, Liver, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[25]
FUNCTION, PHOSPHORYLATION AT THR-366, AND MUTAGENESIS OF THR-366.
PubMed=20864035; DOI=10.1016/j.molcel.2010.08.019;
Sherman M.H., Kuraishy A.I., Deshpande C., Hong J.S., Cacalano N.A.,
Gatti R.A., Manis J.P., Damore M.A., Pellegrini M., Teitell M.A.;
"AID-induced genotoxic stress promotes B cell differentiation in the
germinal center via ATM and LKB1 signaling.";
Mol. Cell 39:873-885(2010).
[26]
FUNCTION, INTERACTION WITH CDKN1A, PHOSPHORYLATION AT THR-366, AND
MUTAGENESIS OF THR-366.
PubMed=25329316; DOI=10.1371/journal.pgen.1004721;
Esteve-Puig R., Gil R., Gonzalez-Sanchez E., Bech-Serra J.J.,
Grueso J., Hernandez-Losa J., Moline T., Canals F., Ferrer B.,
Cortes J., Bastian B., Cajal S.R.Y., Martin-Caballero J., Flores J.M.,
Vivancos A., Garcia-Patos V., Recio J.A.;
"A mouse model uncovers LKB1 as an UVB-induced DNA damage sensor
mediating CDKN1A (p21WAF1/CIP1) degradation.";
PLoS Genet. 10:E1004721-E1004721(2014).
-!- FUNCTION: Tumor suppressor serine/threonine-protein kinase that
controls the activity of AMP-activated protein kinase (AMPK)
family members, thereby playing a role in various processes such
as cell metabolism, cell polarity, apoptosis and DNA damage
response. Acts by phosphorylating the T-loop of AMPK family
proteins, thus promoting their activity: phosphorylates PRKAA1,
PRKAA2, BRSK1, BRSK2, MARK1, MARK2, MARK3, MARK4, NUAK1, NUAK2,
SIK1, SIK2, SIK3 and SNRK but not MELK. Also phosphorylates non-
AMPK family proteins such as STRADA, PTEN and possibly p53/TP53.
Acts as a key upstream regulator of AMPK by mediating
phosphorylation and activation of AMPK catalytic subunits PRKAA1
and PRKAA2 and thereby regulates processes including: inhibition
of signaling pathways that promote cell growth and proliferation
when energy levels are low, glucose homeostasis in liver,
activation of autophagy when cells undergo nutrient deprivation,
and B-cell differentiation in the germinal center in response to
DNA damage. Also acts as a regulator of cellular polarity by
remodeling the actin cytoskeleton. Required for cortical neuron
polarization by mediating phosphorylation and activation of BRSK1
and BRSK2, leading to axon initiation and specification. Involved
in DNA damage response: interacts with p53/TP53 and recruited to
the CDKN1A/WAF1 promoter to participate in transcription
activation. Able to phosphorylate p53/TP53; the relevance of such
result in vivo is however unclear and phosphorylation may be
indirect and mediated by downstream STK11/LKB1 kinase NUAK1. Also
acts as a mediator of p53/TP53-dependent apoptosis via interaction
with p53/TP53: translocates to the mitochondrion during apoptosis
and regulates p53/TP53-dependent apoptosis pathways. In vein
endothelial cells, inhibits PI3K/Akt signaling activity and thus
induces apoptosis in response to the oxidant peroxynitrite.
Regulates UV radiation-induced DNA damage response mediated by
CDKN1A. In association with NUAK1, phosphorylates CDKN1A in
response to UV radiation and contributes to its degradation which
is necessary for optimal DNA repair (PubMed:25329316).
{ECO:0000269|PubMed:16308421, ECO:0000269|PubMed:17482548,
ECO:0000269|PubMed:17482549, ECO:0000269|PubMed:20864035,
ECO:0000269|PubMed:25329316}.
-!- FUNCTION: Isoform 2: Has a role in spermiogenesis.
{ECO:0000269|PubMed:18774945}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000250|UniProtKB:Q15831}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q15831};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000250|UniProtKB:Q15831};
-!- ENZYME REGULATION: Activated by forming a complex with STRAD
(STRADA or STRADB) and CAB39/MO25 (CAB39/MO25alpha or
CAB39L/MO25beta): STRADA (or STRADB)-binding promotes a
conformational change of STK11/LKB1 in an active conformation,
which is stabilized by CAB39/MO25alpha (or CAB39L/MO25beta)
interacting with the STK11/LKB1 activation loop. Sequestration in
the nucleus by NR4A1 prevents it from phosphorylating and
activating cytoplasmic AMPK (By similarity). {ECO:0000250}.
-!- SUBUNIT: Catalytic component of a trimeric complex composed of
STK11/LKB1, STRAD (STRADA or STRADB) and CAB39/MO25
(CAB39/MO25alpha or CAB39L/MO25beta): the complex tethers
STK11/LKB1 in the cytoplasm and stimulates its catalytic activity.
Found in a ternary complex composed of SMAD4, STK11/LKB1 and
STK11IP. Interacts with p53/TP53, SMAD4, STK11IP and WDR6.
Interacts with NR4A1 (By similarity). Interacts with NISCH; this
interaction may increase STK11 activity (By similarity). Interacts
with PTEN, leading to PTEN phosphorylation (By similarity).
Interacts with SIRT1; the interaction deacetylates STK11 (By
similarity). Interacts with CDKN1A. {ECO:0000250|UniProtKB:Q15831,
ECO:0000269|PubMed:17482548, ECO:0000269|PubMed:25329316}.
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Membrane. Mitochondrion
{ECO:0000250}. Note=Translocates to mitochondrion during apoptosis
(By similarity). A small fraction localizes at membranes.
Relocates to the cytoplasm when bound to STRAD (STRADA or STRADB)
and CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta). PTEN promotes
cytoplasmic localization (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 2: Nucleus {ECO:0000250}. Cytoplasm
{ECO:0000250}. Note=Relocates to the cytoplasm when bound to STRAD
(STRADA or STRADB) and CAB39/MO25 (CAB39/MO25alpha or
CAB39L/MO25beta). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1 {ECO:0000269|PubMed:10381580, ECO:0000269|PubMed:10400995,
ECO:0000269|PubMed:10642527, ECO:0000269|PubMed:12060709,
ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16141072};
Synonyms=LKB1(L);
IsoId=Q9WTK7-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:16141072}; Synonyms=LKB1(S);
IsoId=Q9WTK7-2; Sequence=VSP_052222, VSP_052223;
-!- TISSUE SPECIFICITY: Widely expressed. Isoform 2 is predominantly
expressed in testis (at protein level).
{ECO:0000269|PubMed:10642527, ECO:0000269|PubMed:18774945,
ECO:0000269|PubMed:18854309}.
-!- DEVELOPMENTAL STAGE: Ubiquitously expressed 7-11 dpc. Present in
nucleated embryonic blood cells from 9 dpc. Restricted to
gastrointestinal tract, testis and lung from days 15-19 dpc.
{ECO:0000269|PubMed:10381580, ECO:0000269|PubMed:12060709}.
-!- PTM: Phosphorylated by ATM at Thr-366 following ionizing radiation
(IR). Phosphorylation at Ser-431 by RPS6KA1 and/or some PKA is
required to inhibit cell growth. Phosphorylation at Ser-431 is
also required during neuronal polarization to mediate
phosphorylation of BRSK1 and BRSK2. Phosphorylation by PKC/PRKCZ
at Ser-428 promotes peroxynitrite-induced nuclear export of STK11,
leading to PTEN activation and subsequent inhibition of AKT
signaling. Phosphorylation by PKC/PRKCZ at Ser-399 in isoform 2
promotes metformin (or peroxynitrite)-induced nuclear export of
STK11 and activation of AMPK. UV radiation-induced phosphorylation
at Thr-366 mediates CDKN1A degradation.
{ECO:0000269|PubMed:10642527, ECO:0000269|PubMed:11297520,
ECO:0000269|PubMed:11853558, ECO:0000269|PubMed:12234250,
ECO:0000269|PubMed:17482548, ECO:0000269|PubMed:17482549,
ECO:0000269|PubMed:20864035, ECO:0000269|PubMed:25329316}.
-!- PTM: Acetylated. Deacetylation at Lys-48 enhances cytoplasmic
localization and kinase activity in vitro.
{ECO:0000269|PubMed:18687677}.
-!- DISRUPTION PHENOTYPE: Mice die in utero 8.5 to 9.5 dpc due to
severe defects in their vasculature: embryos show neural tube
defects, mesenchymal cell death, and vascular abnormalities.
Extraembryonic development is also severely affected; the mutant
placentas exhibit defective labyrinth layer development and the
fetal vessels fail to invade the placenta. Male mice specifically
lacking isoform 2 are sterile (PubMed:18774945). A specifically
deletion in liver results in hyperglycemia with increased
gluconeogenic and lipogenic gene expression due to loss of AMPK
phosphorylation and subsequent dephosphorylation of CRTC2/TORC2
(PubMed:16308421). Use of a conditional allele, leads to defects
in defects in axon formation with a thinner cortical wall and
larger lateral ventricles in the brain cortex (PubMed:17482548).
Heterozygous mice develop multiple gastric adenomatous polyps,
with polyps remarkably similar to hamartomas of PJS patients both
macroscopically and histologically. Polyps in the heterozygous
mice are detected at 5 months, and cause premature lethality
progressively from 8 months onwards. Polyps are most frequently
observed in the stomach where they typically concentrate close to
the pylorus. Polyps in the small and large intestine are
significantly less frequent. The histology of the polyps in the
heterozygous mice is remarkably similar to PJS polyps including
the relative contribution of well-differentiated epithelium, and a
prominent smooth muscle component. Ptgs2/Cox2 is highly up-
regulated in heterozygous mice polyps concomitantly with
activation of the extracellular signal-regulated kinases
Mapk1/Erk2 and Mapk3/Erk1: treatment with celecoxib Ptgs2/Cox2
inhibitor significantly reduces the total polyp burden.
{ECO:0000269|PubMed:11509733, ECO:0000269|PubMed:11956081,
ECO:0000269|PubMed:12060709, ECO:0000269|PubMed:12218179,
ECO:0000269|PubMed:12226664, ECO:0000269|PubMed:15480979,
ECO:0000269|PubMed:16308421, ECO:0000269|PubMed:17482548,
ECO:0000269|PubMed:18774945}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. LKB1 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF129870; AAD22100.1; -; mRNA.
EMBL; AF145287; AAD31044.1; -; mRNA.
EMBL; EU730638; ACE73833.1; -; mRNA.
EMBL; AF145296; AAD55368.1; -; Genomic_DNA.
EMBL; AF145288; AAD55368.1; JOINED; Genomic_DNA.
EMBL; AF145289; AAD55368.1; JOINED; Genomic_DNA.
EMBL; AF145290; AAD55368.1; JOINED; Genomic_DNA.
EMBL; AF145291; AAD55368.1; JOINED; Genomic_DNA.
EMBL; AF145292; AAD55368.1; JOINED; Genomic_DNA.
EMBL; AF145293; AAD55368.1; JOINED; Genomic_DNA.
EMBL; AF145294; AAD55368.1; JOINED; Genomic_DNA.
EMBL; AF145295; AAD55368.1; JOINED; Genomic_DNA.
EMBL; AF151711; AAF21370.1; -; mRNA.
EMBL; AB015801; BAA76749.1; -; mRNA.
EMBL; AK171909; BAE42728.1; -; mRNA.
EMBL; AK172528; BAE43050.1; -; mRNA.
EMBL; AK172385; BAE42977.1; -; mRNA.
EMBL; BC052379; AAH52379.1; -; mRNA.
CCDS; CCDS35974.1; -. [Q9WTK7-1]
CCDS; CCDS78854.1; -. [Q9WTK7-2]
RefSeq; NP_001288782.1; NM_001301853.1. [Q9WTK7-2]
RefSeq; NP_001288783.1; NM_001301854.1.
RefSeq; NP_035622.1; NM_011492.4. [Q9WTK7-1]
UniGene; Mm.44231; -.
ProteinModelPortal; Q9WTK7; -.
SMR; Q9WTK7; -.
BioGrid; 203541; 4.
CORUM; Q9WTK7; -.
DIP; DIP-60722N; -.
ELM; Q9WTK7; -.
IntAct; Q9WTK7; 3.
STRING; 10090.ENSMUSP00000003152; -.
ChEMBL; CHEMBL3734644; -.
iPTMnet; Q9WTK7; -.
PhosphoSitePlus; Q9WTK7; -.
EPD; Q9WTK7; -.
PaxDb; Q9WTK7; -.
PeptideAtlas; Q9WTK7; -.
PRIDE; Q9WTK7; -.
Ensembl; ENSMUST00000003152; ENSMUSP00000003152; ENSMUSG00000003068. [Q9WTK7-1]
Ensembl; ENSMUST00000144883; ENSMUSP00000114195; ENSMUSG00000003068. [Q9WTK7-2]
Ensembl; ENSMUST00000213772; ENSMUSP00000150488; ENSMUSG00000003068. [Q9WTK7-2]
GeneID; 20869; -.
KEGG; mmu:20869; -.
UCSC; uc007gbt.2; mouse. [Q9WTK7-1]
CTD; 6794; -.
MGI; MGI:1341870; Stk11.
eggNOG; KOG0583; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00530000063214; -.
HOGENOM; HOG000007002; -.
HOVERGEN; HBG054467; -.
InParanoid; Q9WTK7; -.
KO; K07298; -.
OMA; DPQQLGM; -.
OrthoDB; EOG091G0BNP; -.
PhylomeDB; Q9WTK7; -.
TreeFam; TF105322; -.
Reactome; R-MMU-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
PRO; PR:Q9WTK7; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000003068; -.
CleanEx; MM_STK11; -.
ExpressionAtlas; Q9WTK7; baseline and differential.
Genevisible; Q9WTK7; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0036398; C:TCR signalosome; IDA:MGI.
GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
GO; GO:0030275; F:LRR domain binding; IPI:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
GO; GO:0002039; F:p53 binding; ISS:UniProtKB.
GO; GO:0030295; F:protein kinase activator activity; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0032147; P:activation of protein kinase activity; IDA:MGI.
GO; GO:0043276; P:anoikis; ISO:MGI.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0007409; P:axonogenesis; IMP:UniProtKB.
GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:MGI.
GO; GO:0007050; P:cell cycle arrest; ISS:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
GO; GO:0071493; P:cellular response to UV-B; IDA:UniProtKB.
GO; GO:0097484; P:dendrite extension; IMP:MGI.
GO; GO:0030010; P:establishment of cell polarity; IMP:UniProtKB.
GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB.
GO; GO:0051645; P:Golgi localization; IMP:MGI.
GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; ISS:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0060770; P:negative regulation of epithelial cell proliferation involved in prostate gland development; IMP:MGI.
GO; GO:0051055; P:negative regulation of lipid biosynthetic process; IMP:MGI.
GO; GO:1904262; P:negative regulation of TORC1 signaling; ISO:MGI.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
GO; GO:0010508; P:positive regulation of autophagy; ISO:MGI.
GO; GO:0050772; P:positive regulation of axonogenesis; IGI:MGI.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:MGI.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IMP:MGI.
GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0045059; P:positive thymic T cell selection; IMP:MGI.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0001558; P:regulation of cell growth; IDA:UniProtKB.
GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:MGI.
GO; GO:0051896; P:regulation of protein kinase B signaling; IMP:MGI.
GO; GO:0030111; P:regulation of Wnt signaling pathway; IMP:MGI.
GO; GO:0010212; P:response to ionizing radiation; IDA:UniProtKB.
GO; GO:0007286; P:spermatid development; IMP:UniProtKB.
GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
GO; GO:0050852; P:T cell receptor signaling pathway; IMP:MGI.
GO; GO:0036399; P:TCR signalosome assembly; IMP:MGI.
GO; GO:0001894; P:tissue homeostasis; IMP:MGI.
GO; GO:0001944; P:vasculature development; IMP:UniProtKB.
InterPro; IPR020636; Ca/CaM-dep_Ca-dep_prot_Kinase.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR24347; PTHR24347; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 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; Alternative splicing; Apoptosis; ATP-binding; Autophagy;
Cell cycle; Complete proteome; Cytoplasm; Differentiation; DNA damage;
Kinase; Lipoprotein; Magnesium; Manganese; Membrane; Metal-binding;
Methylation; Mitochondrion; Nucleotide-binding; Nucleus; Palmitate;
Phosphoprotein; Prenylation; Reference proteome;
Serine/threonine-protein kinase; Spermatogenesis; Transferase;
Tumor suppressor.
CHAIN 1 433 Serine/threonine-protein kinase STK11.
/FTId=PRO_0000260032.
PROPEP 434 436 Removed in mature form.
/FTId=PRO_0000422301.
DOMAIN 49 309 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 55 63 ATP. {ECO:0000250|UniProtKB:P28523,
ECO:0000255|PROSITE-ProRule:PRU00159}.
REGION 45 90 Sufficient for interaction with SIRT1.
{ECO:0000250}.
ACT_SITE 176 176 Proton acceptor.
{ECO:0000250|UniProtKB:P28523,
ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10027}.
BINDING 78 78 ATP. {ECO:0000305}.
MOD_RES 31 31 Phosphoserine.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:11853558}.
MOD_RES 44 44 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q15831}.
MOD_RES 48 48 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q15831}.
MOD_RES 96 96 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q15831}.
MOD_RES 97 97 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q15831}.
MOD_RES 189 189 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:Q15831}.
MOD_RES 296 296 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q15831}.
MOD_RES 311 311 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q15831}.
MOD_RES 325 325 Phosphoserine.
{ECO:0000269|PubMed:11853558}.
MOD_RES 336 336 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:11853558}.
MOD_RES 366 366 Phosphothreonine; by ATM and
autocatalysis.
{ECO:0000269|PubMed:11853558,
ECO:0000269|PubMed:12234250,
ECO:0000269|PubMed:20864035,
ECO:0000269|PubMed:25329316}.
MOD_RES 403 403 Phosphoserine.
{ECO:0000250|UniProtKB:Q15831}.
MOD_RES 420 420 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q15831}.
MOD_RES 426 426 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q15831}.
MOD_RES 431 431 Phosphoserine; by autocatalysis, PKA,
PKC/PRKCZ and RPS6KA1.
{ECO:0000269|PubMed:10642527,
ECO:0000269|PubMed:11297520,
ECO:0000269|PubMed:17482548,
ECO:0000269|PubMed:17482549}.
MOD_RES 433 433 Cysteine methyl ester.
{ECO:0000269|PubMed:11853558}.
MOD_RES 434 434 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q15831}.
LIPID 422 422 S-palmitoyl cysteine.
{ECO:0000269|PubMed:10642527}.
LIPID 433 433 S-farnesyl cysteine.
{ECO:0000269|PubMed:10642527,
ECO:0000269|PubMed:11297520,
ECO:0000269|PubMed:11853558}.
VAR_SEQ 374 415 QVLEEEVGQNGQSHSLPKAVCVNGTEPQLSSKVKPEGRPGT
A -> VEEAAEAGLSEDACDTCMWKSQGAGLPGEEPEEGFG
ALV (in isoform 2).
{ECO:0000303|PubMed:16141072,
ECO:0000303|Ref.5}.
/FTId=VSP_052222.
VAR_SEQ 416 436 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072,
ECO:0000303|Ref.5}.
/FTId=VSP_052223.
MUTAGEN 31 31 S->A: No change in kinase activity; when
associated with A-325; A-336 and A-366.
{ECO:0000269|PubMed:11853558}.
MUTAGEN 78 78 K->I: Loss of kinase activity.
MUTAGEN 194 194 D->A: Loss of kinase activity and
descreased phosphorylation.
{ECO:0000269|PubMed:11853558}.
MUTAGEN 325 325 S->A: No change in kinase activity; when
associated with A-31; A-336 and A-366.
{ECO:0000269|PubMed:11853558}.
MUTAGEN 336 336 T->A: Abolishes ability to suppress cell
growth. Decreased phosphorylation; when
associated with A-366. No change in
kinase activity; when associated with A-
31; A-325 and A-366.
{ECO:0000269|PubMed:11853558}.
MUTAGEN 366 366 T->A: Diminished interaction with CDKN1A
and impaired ability to repair UV-induced
DNA damage by affecting CDKN1A UV-induced
degradation. Decreased phosphorylation;
when associated with A-336. No change in
kinase activity; when associated with A-
31; A-325 and A-336.
{ECO:0000269|PubMed:11853558,
ECO:0000269|PubMed:12234250,
ECO:0000269|PubMed:20864035,
ECO:0000269|PubMed:25329316}.
MUTAGEN 431 431 S->A: Does not prevent S-farnesylation.
Defects in neuron polarization.
{ECO:0000269|PubMed:10642527,
ECO:0000269|PubMed:11297520,
ECO:0000269|PubMed:17482548,
ECO:0000269|PubMed:17482549}.
MUTAGEN 433 433 C->A: Does not affect nuclear
localization. Does not prevent
phosphorylation at S-431.
{ECO:0000269|PubMed:10642527,
ECO:0000269|PubMed:11297520,
ECO:0000269|PubMed:11853558}.
CONFLICT 95 95 V -> L (in Ref. 2; BAE42728).
{ECO:0000305}.
SEQUENCE 436 AA; 49267 MW; CCD9BCF94CF5CC9C CRC64;
MDVADPEPLG LFSEGELMSV GMDTFIHRID STEVIYQPRR KRAKLIGKYL MGDLLGEGSY
GKVKEVLDSE TLCRRAVKIL KKKKLRRIPN GEANVKKEIQ LLRRLRHRNV IQLVDVLYNE
EKQKMYMVME YCVCGMQEML DSVPEKRFPV CQAHGYFRQL IDGLEYLHSQ GIVHKDIKPG
NLLLTTNGTL KISDLGVAEA LHPFAVDDTC RTSQGSPAFQ PPEIANGLDT FSGFKVDIWS
AGVTLYNITT GLYPFEGDNI YKLFENIGRG DFTIPCDCGP PLSDLLRGML EYEPAKRFSI
RQIRQHSWFR KKHPLAEALV PIPPSPDTKD RWRSMTVVPY LEDLHGRAEE EEEEDLFDIE
DGIIYTQDFT VPGQVLEEEV GQNGQSHSLP KAVCVNGTEP QLSSKVKPEG RPGTANPARK
VCSSNKIRRL SACKQQ


Related products :

Catalog number Product name Quantity
EIAAB40295 Liver kinase B1 homolog,LKB1,Lkb1,mLKB1,Mouse,Mus musculus,Serine_threonine-protein kinase STK11,Stk11
EIAAB40294 Liver kinase B1 homolog,LKB1,Lkb1,Rat,Rattus norvegicus,Serine_threonine-protein kinase STK11,Stk11
EIAAB40297 hLKB1,Homo sapiens,Human,Liver kinase B1,LKB1,LKB1,PJS,Renal carcinoma antigen NY-REN-19,Serine_threonine-protein kinase STK11,STK11
EIAAB40296 Chicken,Gallus gallus,Liver kinase B1 homolog,LKB1,Serine_threonine-protein kinase STK11,STK11
X1713P Human LKB1 per STK11 Serine per Threonine Kinase Polyclonal Antibody 100
X1713P LKB1 STK11 Serine Threonine Kinase type: Polyclonal Antibody host: Rabbit Isotype: IgG 100
STK11_RAT ELISA Kit FOR Serine per threonine-protein kinase STK11; organism: Rat; gene name: Stk11 96T
STK11_MOUSE ELISA Kit FOR Serine per threonine-protein kinase STK11; organism: Mouse; gene name: Stk11 96T
ER501 Serine per threonine-protein kinase STK11 Elisa Kit 96T
G9792 Serine threonine-protein kinase 11 (STK11), Mouse, ELISA Kit 96T
G9791 Serine threonine-protein kinase 11 (STK11), Human, ELISA Kit 96T
G9790 Serine threonine-protein kinase 11 (STK11), Chicken, ELISA Kit 96T
EIAAB31334 Bos taurus,Bovine,PKN,PKN1,PRK1,PRKCL1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein kinase PKN-alpha,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine
EIAAB31332 Mouse,Mus musculus,Pkn,Pkn1,Prk1,Prkcl1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine protein kinase N
GWB-24F765 Serine Threonine Protein Kinase 11 (STK11) Rabbit anti-Human Polyclonal (N-Terminus) Antibody
GWB-899C1C Anti- STK11 (serine threonine kinase 11) Antibody
G9785 Serine Threonine Kinase 11 (STK11), Mouse, ELISA Kit 96T
GWB-5BE1E2 Serine threonine-protein kinase SNF1-like kinase 2 (SNF1LK2) Salt-inducible protein kinase 2 (SIK2) Mouse anti-Human Monoclonal
GWB-CEE83D Serine threonine-protein kinase SNF1-like kinase 2 (SNF1LK2) Salt-inducible protein kinase 2 (SIK2) Rabbit anti-Human Polyclonal
E0071m Mouse ELISA Kit FOR Serine per threonine-protein kinase PRP4 homolog 96T
TM141_MOUSE Mouse ELISA Kit FOR Serine per threonine-protein kinase PRP4 homolog 96T
H0317 Serine threonine-protein kinase PRP4 homolog (PRPF4B), Rat, ELISA Kit 96T
CCD23_BOVIN Mouse ELISA Kit FOR Serine per threonine-protein kinase PRP4 homolog 96T
PRP4B_HUMAN Human ELISA Kit FOR Serine per threonine-protein kinase PRP4 homolog 96T
H0314 Serine threonine-protein kinase PRP4 homolog (PRPF4B), Bovine, ELISA Kit 96T


 

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