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GTPase KRas (K-Ras 2) (Ki-Ras) (c-K-ras) (c-Ki-ras) [Cleaved into: GTPase KRas, N-terminally processed]

 RASK_HUMAN              Reviewed;         189 AA.
P01116; A8K8Z5; B0LPF9; P01118; Q96D10;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
25-OCT-2017, entry version 215.
RecName: Full=GTPase KRas;
AltName: Full=K-Ras 2;
AltName: Full=Ki-Ras;
AltName: Full=c-K-ras;
AltName: Full=c-Ki-ras;
Contains:
RecName: Full=GTPase KRas, N-terminally processed;
Flags: Precursor;
Name=KRAS; Synonyms=KRAS2, RASK2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2A AND 2B).
PubMed=6308466; DOI=10.1038/304501a0;
McGrath J.P., Capon D.J., Smith D.H., Chen E.Y., Seeburg P.H.,
Goeddel D.V., Levinson A.D.;
"Structure and organization of the human Ki-ras proto-oncogene and a
related processed pseudogene.";
Nature 304:501-506(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2A AND 2B).
TISSUE=Lung carcinoma;
PubMed=6308465; DOI=10.1038/304497a0;
Shimizu K., Birnbaum D., Ruley M.A., Fasano O., Suard Y., Edlund L.,
Taparowsky E., Goldfarb M., Wigler M.;
"Structure of the Ki-ras gene of the human lung carcinoma cell line
Calu-1.";
Nature 304:497-500(1983).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2A AND 2B).
TISSUE=Colon carcinoma, and Lung;
PubMed=6308467; DOI=10.1038/304507a0;
Capon D.J., Seeburg P.H., McGrath J.P., Hayflick J.S., Edman U.,
Levinson A.D., Goeddel D.V.;
"Activation of Ki-ras2 gene in human colon and lung carcinomas by two
different point mutations.";
Nature 304:507-513(1983).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2A AND 2B), AND VARIANT
COLON CANCER VAL-12.
TISSUE=Colon carcinoma;
PubMed=6092920; DOI=10.1128/MCB.4.8.1577;
McCoy M.S., Bargmann C.I., Weinberg R.A.;
"Human colon carcinoma Ki-ras2 oncogene and its corresponding proto-
oncogene.";
Mol. Cell. Biol. 4:1577-1582(1984).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2B).
PubMed=3310850;
Kahn S., Yamamoto F., Almoguera C., Winter E., Forrester K.,
Jordano J., Perucho M.;
"The c-K-ras gene and human cancer (review).";
Anticancer Res. 7:639-652(1987).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2B).
TISSUE=Brain;
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2B), AND VARIANT LUNG
CARCINOMA HIS-61.
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2B).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2B), AND VARIANT LUNG
CARCINOMA HIS-61.
TISSUE=Lung carcinoma;
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).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37, AND VARIANT LUNG CARCINOMA
CYS-12.
TISSUE=Lung carcinoma;
PubMed=6320174; DOI=10.1073/pnas.81.1.71;
Nakano H., Yamamoto F., Neville C., Evans D., Mizuno T., Perucho M.;
"Isolation of transforming sequences of two human lung carcinomas:
structural and functional analysis of the activated c-K-ras
oncogenes.";
Proc. Natl. Acad. Sci. U.S.A. 81:71-75(1984).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-96.
TISSUE=Pancreatic carcinoma;
PubMed=3855240; DOI=10.1016/S0006-291X(85)80140-6;
Hirai H., Okabe T., Anraku Y., Fujisawa M., Urabe A., Takaku F.;
"Activation of the c-K-ras oncogene in a human pancreas carcinoma.";
Biochem. Biophys. Res. Commun. 127:168-174(1985).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37, AND VARIANT GASC VAL-12.
PubMed=3034404;
Deng G., Lu Y., Chen S., Miao J., Lu G., Li H., Cai H., Xu X.,
Zheng E., Liu P.;
"Activated c-Ha-ras oncogene with a guanine to thymine transversion at
the twelfth codon in a human stomach cancer cell line.";
Cancer Res. 47:3195-3198(1987).
[15]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36, AND VARIANT BLADDER/LUNG
CANCER ARG-12.
TISSUE=Lung carcinoma;
PubMed=6695174; DOI=10.1126/science.6695174;
Santos E., Martin-Zanca D., Reddy P.E., Pierotti M.A., Porta G.,
Barbacid M.;
"Malignant activation of a K-ras oncogene in lung carcinoma but not in
normal tissue of the same patient.";
Science 223:661-664(1984).
[16]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37.
PubMed=3932274;
Sekiya T., Tokunaga A., Fushimi M.;
"Essential region for transforming activity of human c-Ha-ras-1.";
Jpn. J. Cancer Res. 76:787-791(1985).
[17]
PROTEIN SEQUENCE OF 1-41; 43-147 AND 150-161, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT MET-1 AND THR-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Cervix carcinoma;
Bienvenut W.V., Calvo F., Kolch W.;
Submitted (FEB-2008) to UniProtKB.
[18]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-96.
TISSUE=Lung carcinoma;
PubMed=6096811; DOI=10.1093/nar/12.23.8873;
Yamamoto F., Perucho M.;
"Activation of a human c-K-ras oncogene.";
Nucleic Acids Res. 12:8873-8885(1984).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
ACETYLATION AT LYS-104, VARIANT VAL-12, FUNCTION, AND ENZYME
REGULATION.
PubMed=22711838; DOI=10.1073/pnas.1201487109;
Yang M.H., Nickerson S., Kim E.T., Liot C., Laurent G., Spang R.,
Philips M.R., Shan Y., Shaw D.E., Bar-Sagi D., Haigis M.C.,
Haigis K.M.;
"Regulation of RAS oncogenicity by acetylation.";
Proc. Natl. Acad. Sci. U.S.A. 109:10843-10848(2012).
[21]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PDE6D.
PubMed=23698361; DOI=10.1038/nature12205;
Zimmermann G., Papke B., Ismail S., Vartak N., Chandra A.,
Hoffmann M., Hahn S.A., Triola G., Wittinghofer A., Bastiaens P.I.,
Waldmann H.;
"Small molecule inhibition of the KRAS-PDE? interaction impairs
oncogenic KRAS signalling.";
Nature 497:638-642(2013).
[22]
FUNCTION, AND CHARACTERIZATION OF VARIANT COLON CANCER VAL-12.
PubMed=24623306; DOI=10.7554/eLife.02313;
Serra R.W., Fang M., Park S.M., Hutchinson L., Green M.R.;
"A KRAS-directed transcriptional silencing pathway that mediates the
CpG island methylator phenotype.";
Elife 3:E02313-E02313(2014).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[24]
X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 1-164 IN COMPLEX WITH THE
GTP ANALOG GUANOSINE-5'-DIPHOSPHATE, AND ENZYME REGULATION.
PubMed=22566140; DOI=10.1002/anie.201201358;
Sun Q., Burke J.P., Phan J., Burns M.C., Olejniczak E.T.,
Waterson A.G., Lee T., Rossanese O.W., Fesik S.W.;
"Discovery of small molecules that bind to K-Ras and inhibit Sos-
mediated activation.";
Angew. Chem. Int. Ed. Engl. 51:6140-6143(2012).
[25]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-164 IN COMPLEX WITH GTP
ANALOGS AND MAGNESIUM, FUNCTION, ENZYME REGULATION, INTERACTION WITH
SOS1, AND SUBCELLULAR LOCATION.
PubMed=22431598; DOI=10.1073/pnas.1116510109;
Maurer T., Garrenton L.S., Oh A., Pitts K., Anderson D.J.,
Skelton N.J., Fauber B.P., Pan B., Malek S., Stokoe D., Ludlam M.J.,
Bowman K.K., Wu J., Giannetti A.M., Starovasnik M.A., Mellman I.,
Jackson P.K., Rudolph J., Wang W., Fang G.;
"Small-molecule ligands bind to a distinct pocket in Ras and inhibit
SOS-mediated nucleotide exchange activity.";
Proc. Natl. Acad. Sci. U.S.A. 109:5299-5304(2012).
[26] {ECO:0000244|PDB:5TAR, ECO:0000244|PDB:5TB5}
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-164, ISOPRENYLATION AT
CYS-186, AND METHYLATION AT CYS-186.
PubMed=27791178; DOI=10.1073/pnas.1615316113;
Dharmaiah S., Bindu L., Tran T.H., Gillette W.K., Frank P.H.,
Ghirlando R., Nissley D.V., Esposito D., McCormick F., Stephen A.G.,
Simanshu D.K.;
"Structural basis of recognition of farnesylated and methylated KRAS4b
by PDEdelta.";
Proc. Natl. Acad. Sci. U.S.A. 113:E6766-E6775(2016).
[27]
VARIANT BREAST CANCER ASP-13.
PubMed=3627975; DOI=10.1093/nar/15.15.5963;
Kozma S.C., Bogaard M.E., Buser K., Saurer S.M., Bos J.L., Groner B.,
Hynes N.E.;
"The human c-Kirsten ras gene is activated by a novel mutation in
codon 13 in the breast carcinoma cell line MDA-MB231.";
Nucleic Acids Res. 15:5963-5971(1987).
[28]
VARIANT BLADDER CANCER THR-59.
PubMed=1553789; DOI=10.1007/BF00296523;
Grimmond S.M., Raghavan D., Russell P.J.;
"Detection of a rare point mutation in Ki-ras of a human bladder
cancer xenograft by polymerase chain reaction and direct sequencing.";
Urol. Res. 20:121-126(1992).
[29]
VARIANTS PANCREATIC CARCINOMA ASP-12 AND VAL-12.
PubMed=8439212; DOI=10.1097/00000658-199302000-00007;
Motojima K., Urano T., Nagata Y., Shiku H., Tsurifune T.,
Kanematsu T.;
"Detection of point mutations in the Kirsten-ras oncogene provides
evidence for the multicentricity of pancreatic carcinoma.";
Ann. Surg. 217:138-143(1993).
[30]
VARIANTS GASC SER-12 AND ASP-12.
PubMed=7773929;
DOI=10.1002/1097-0142(19950615)75:12<2794::AID-CNCR2820751203>3.0.CO;2-F;
Lee K.H., Lee J.S., Suh C., Kim S.W., Kim S.B., Lee J.H., Lee M.S.,
Park M.Y., Sun H.S., Kim S.H.;
"Clinicopathologic significance of the K-ras gene codon 12 point
mutation in stomach cancer. An analysis of 140 cases.";
Cancer 75:2794-2801(1995).
[31]
INVOLVEMENT IN AML, VARIANT GLY-10 INS, AND CHARACTERIZATION OF
VARIANT GLY-10 INS.
PubMed=8955068; DOI=10.1074/jbc.271.51.32491;
Bollag G., Adler F., elMasry N., McCabe P.C., Conner E. Jr.,
Thompson P., McCormick F., Shannon K.;
"Biochemical characterization of a novel KRAS insertion mutation from
a human leukemia.";
J. Biol. Chem. 271:32491-32494(1996).
[32]
VARIANTS GASC ASN-5; VAL-12; ASP-13 AND THR-59.
PubMed=14534542; DOI=10.1038/sj.onc.1206749;
Lee S.H., Lee J.W., Soung Y.H., Kim H.S., Park W.S., Kim S.Y.,
Lee J.H., Park J.Y., Cho Y.G., Kim C.J., Nam S.W., Kim S.H., Lee J.Y.,
Yoo N.J.;
"BRAF and KRAS mutations in stomach cancer.";
Oncogene 22:6942-6945(2003).
[33]
VARIANT PYLOCYTIC ASTROCYTOMA ARG-13.
PubMed=16247081; DOI=10.1212/01.wnl.0000180409.78098.d7;
Sharma M.K., Zehnbauer B.A., Watson M.A., Gutmann D.H.;
"RAS pathway activation and an oncogenic RAS mutation in sporadic
pilocytic astrocytoma.";
Neurology 65:1335-1336(2005).
[34]
VARIANTS NS3 GLY-152 (ISOSORM 2) AND VAL-153 (ISOFORM 2).
PubMed=16773572; DOI=10.1086/504394;
Carta C., Pantaleoni F., Bocchinfuso G., Stella L., Vasta I.,
Sarkozy A., Digilio C., Palleschi A., Pizzuti A., Grammatico P.,
Zampino G., Dallapiccola B., Gelb B.D., Tartaglia M.;
"Germline missense mutations affecting KRAS Isoform B are associated
with a severe Noonan syndrome phenotype.";
Am. J. Hum. Genet. 79:129-135(2006).
[35]
VARIANTS LUNG CARCINOMA CYS-12; ASP-12; SER-12; VAL-12 AND HIS-61.
PubMed=16533793; DOI=10.1158/1078-0432.CCR-05-1981;
Tam I.Y.S., Chung L.P., Suen W.S., Wang E., Wong M.C.M., Ho K.K.,
Lam W.K., Chiu S.W., Girard L., Minna J.D., Gazdar A.F., Wong M.P.;
"Distinct epidermal growth factor receptor and KRAS mutation patterns
in non-small cell lung cancer patients with different tobacco exposure
and clinicopathologic features.";
Clin. Cancer Res. 12:1647-1653(2006).
[36]
VARIANT CFC2 ARG-60.
PubMed=16474404; DOI=10.1038/ng1749;
Niihori T., Aoki Y., Narumi Y., Neri G., Cave H., Verloes A.,
Okamoto N., Hennekam R.C.M., Gillessen-Kaesbach G., Wieczorek D.,
Kavamura M.I., Kurosawa K., Ohashi H., Wilson L., Heron D.,
Bonneau D., Corona G., Kaname T., Naritomi K., Baumann C.,
Matsumoto N., Kato K., Kure S., Matsubara Y.;
"Germline KRAS and BRAF mutations in cardio-facio-cutaneous
syndrome.";
Nat. Genet. 38:294-296(2006).
[37]
VARIANTS NS3 ILE-14 AND ILE-58, VARIANT CFC2 ARG-34, AND
CHARACTERIZATION OF VARIANTS NS3 ILE-14 AND ILE-58.
PubMed=16474405; DOI=10.1038/ng1748;
Schubbert S., Zenker M., Rowe S.L., Boell S., Klein C., Bollag G.,
van der Burgt I., Musante L., Kalscheuer V., Wehner L.-E., Nguyen H.,
West B., Zhang K.Y.J., Sistermans E., Rauch A., Niemeyer C.M.,
Shannon K., Kratz C.P.;
"Germline KRAS mutations cause Noonan syndrome.";
Nat. Genet. 38:331-336(2006).
[38]
VARIANTS [LARGE SCALE ANALYSIS] ALA-12; ASP-12; SER-12; VAL-12;
ASP-13; ARG-61; ASN-117 AND THR-146.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[39]
VARIANTS JMML ASP-12; SER-12 AND ASP-13.
PubMed=17332249; DOI=10.1182/blood-2006-09-046649;
Matsuda K., Shimada A., Yoshida N., Ogawa A., Watanabe A., Yajima S.,
Iizuka S., Koike K., Yanai F., Kawasaki K., Yanagimachi M.,
Kikuchi A., Ohtsuka Y., Hidaka E., Yamauchi K., Tanaka M.,
Yanagisawa R., Nakazawa Y., Shiohara M., Manabe A., Kojima S.,
Koike K.;
"Spontaneous improvement of hematologic abnormalities in patients
having juvenile myelomonocytic leukemia with specific RAS mutations.";
Blood 109:5477-5480(2007).
[40]
VARIANT NS3 GLU-5.
PubMed=17468812; DOI=10.1007/s10038-007-0146-1;
Bertola D.R., Pereira A.C., Brasil A.S., Albano L.M., Kim C.A.,
Krieger J.E.;
"Further evidence of genetic heterogeneity in Costello syndrome:
involvement of the KRAS gene.";
J. Hum. Genet. 52:521-526(2007).
[41]
VARIANTS NS3 ILE-14; ARG-22; LEU-34; GLN-34; MET-36 AND VAL-153
(ISOFORM 2), VARIANT CFC2 GLU-22, VARIANT NS3/CFC2 ILE-156 (ISOFORM
2), AND VARIANTS ASN-5 AND LEU-156 (ISOFORM 2).
PubMed=17056636; DOI=10.1136/jmg.2006.046300;
Zenker M., Lehmann K., Schulz A.L., Barth H., Hansmann D., Koenig R.,
Korinthenberg R., Kreiss-Nachtsheim M., Meinecke P., Morlot S.,
Mundlos S., Quante A.S., Raskin S., Schnabel D., Wehner L.E.,
Kratz C.P., Horn D., Kutsche K.;
"Expansion of the genotypic and phenotypic spectrum in patients with
KRAS germline mutations.";
J. Med. Genet. 44:131-135(2007).
[42]
VARIANTS NS3 ILE-58 AND SER-60.
PubMed=19396835; DOI=10.1002/ajmg.a.32786;
Kratz C.P., Zampino G., Kriek M., Kant S.G., Leoni C., Pantaleoni F.,
Oudesluys-Murphy A.M., Di Rocco C., Kloska S.P., Tartaglia M.,
Zenker M.;
"Craniosynostosis in patients with Noonan syndrome caused by germline
KRAS mutations.";
Am. J. Med. Genet. A 149:1036-1040(2009).
[43]
CHARACTERIZATION OF VARIANTS NS3 ILE-14; ARG-22; LEU-34; ILE-58 AND
VAL-153 (ISOFORM 2), CHARACTERIZATION OF VARIANTS CFC2 GLU-22; ARG-34
AND ARG-60, AND CHARACTERIZATION OF VARIANTS ASN-5 AND LEU-156
(ISOFORM 2).
PubMed=20949621; DOI=10.1002/humu.21377;
Gremer L., Merbitz-Zahradnik T., Dvorsky R., Cirstea I.C., Kratz C.P.,
Zenker M., Wittinghofer A., Ahmadian M.R.;
"Germline KRAS mutations cause aberrant biochemical and physical
properties leading to developmental disorders.";
Hum. Mutat. 32:33-43(2011).
[44]
VARIANTS CFC2 HIS-71 AND GLU-147.
PubMed=21797849; DOI=10.1111/j.1399-0004.2011.01754.x;
Stark Z., Gillessen-Kaesbach G., Ryan M.M., Cirstea I.C., Gremer L.,
Ahmadian M.R., Savarirayan R., Zenker M.;
"Two novel germline KRAS mutations: expanding the molecular and
clinical phenotype.";
Clin. Genet. 81:590-594(2012).
-!- FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase
activity. Plays an important role in the regulation of cell
proliferation (PubMed:23698361, PubMed:22711838). Plays a role in
promoting oncogenic events by inducing transcriptional silencing
of tumor suppressor genes (TSGs) in colorectal cancer (CRC) cells
in a ZNF304-dependent manner (PubMed:24623306).
{ECO:0000269|PubMed:22711838, ECO:0000269|PubMed:23698361,
ECO:0000269|PubMed:24623306, ECO:0000305}.
-!- ENZYME REGULATION: Alternates between an inactive form bound to
GDP and an active form bound to GTP. Activated by a guanine
nucleotide-exchange factor (GEF) and inactivated by a GTPase-
activating protein (GAP). Interaction with SOS1 promotes exchange
of bound GDP by GTP. {ECO:0000269|PubMed:22431598,
ECO:0000269|PubMed:22566140, ECO:0000269|PubMed:22711838}.
-!- SUBUNIT: Interacts with PHLPP. Interacts (active GTP-bound form
preferentially) with RGS14 (By similarity). Interacts (when
farnesylated) with PDE6D; this promotes dissociation from the cell
membrane (PubMed:23698361). Interacts with SOS1 (PubMed:22431598).
{ECO:0000250|UniProtKB:P08644, ECO:0000269|PubMed:22431598,
ECO:0000269|PubMed:23698361}.
-!- INTERACTION:
Q96II5:ARAF; NbExp=3; IntAct=EBI-367415, EBI-9383168;
Q04631:Fnta (xeno); NbExp=3; IntAct=EBI-367427, EBI-602447;
P04049:RAF1; NbExp=3; IntAct=EBI-367427, EBI-365996;
P50749:RASSF2; NbExp=2; IntAct=EBI-367415, EBI-960081;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22431598,
ECO:0000269|PubMed:23698361}; Lipid-anchor
{ECO:0000305|PubMed:23698361}; Cytoplasmic side
{ECO:0000305|PubMed:23698361}. Cytoplasm, cytosol
{ECO:0000269|PubMed:23698361}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Isoforms differ in the C-terminal region which is
encoded by two alternative exons (IVA and IVB).;
Name=2A; Synonyms=K-Ras4A;
IsoId=P01116-1; Sequence=Displayed;
Name=2B; Synonyms=K-Ras4B;
IsoId=P01116-2, P01118-1;
Sequence=VSP_011140, VSP_011141;
Note=Variant in position: 152:V->G (in NS3). Variant in
position: 153:D->V (in CFC2 and NS3, exhibits only minor
alterations in its in vitro biochemical behavior compared to
wild-type protein). Variant in position: 156:F->I (in NS3/CFC2).
Variant in position: 156:F->L (found in a patient with Costello
syndrome, exhibits an increase in intrinsic and guanine
nucleotide exchange factor catalyzed nucleotide exchange in
combination with an impaired GTPase-activating
protein-stimulated GTP hydrolysis but functional in interaction
with effectors).;
-!- PTM: Acetylation at Lys-104 prevents interaction with guanine
nucleotide exchange factors (GEFs). {ECO:0000269|PubMed:22711838,
ECO:0000269|Ref.17}.
-!- DISEASE: Leukemia, acute myelogenous (AML) [MIM:601626]: A subtype
of acute leukemia, a cancer of the white blood cells. AML is a
malignant disease of bone marrow characterized by maturational
arrest of hematopoietic precursors at an early stage of
development. Clonal expansion of myeloid blasts occurs in bone
marrow, blood, and other tissue. Myelogenous leukemias develop
from changes in cells that normally produce neutrophils,
basophils, eosinophils and monocytes.
{ECO:0000269|PubMed:8955068}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Leukemia, juvenile myelomonocytic (JMML) [MIM:607785]: An
aggressive pediatric myelodysplastic syndrome/myeloproliferative
disorder characterized by malignant transformation in the
hematopoietic stem cell compartment with proliferation of
differentiated progeny. Patients have splenomegaly, enlarged lymph
nodes, rashes, and hemorrhages. {ECO:0000269|PubMed:17332249}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Noonan syndrome 3 (NS3) [MIM:609942]: A form of Noonan
syndrome, a disease characterized by short stature, facial
dysmorphic features such as hypertelorism, a downward eyeslant and
low-set posteriorly rotated ears, and a high incidence of
congenital heart defects and hypertrophic cardiomyopathy. Other
features can include a short neck with webbing or redundancy of
skin, deafness, motor delay, variable intellectual deficits,
multiple skeletal defects, cryptorchidism, and bleeding diathesis.
Individuals with Noonan syndrome are at risk of juvenile
myelomonocytic leukemia, a myeloproliferative disorder
characterized by excessive production of myelomonocytic cells.
{ECO:0000269|PubMed:16474405, ECO:0000269|PubMed:16773572,
ECO:0000269|PubMed:17056636, ECO:0000269|PubMed:17468812,
ECO:0000269|PubMed:19396835, ECO:0000269|PubMed:20949621}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Gastric cancer (GASC) [MIM:613659]: A malignant disease
which starts in the stomach, can spread to the esophagus or the
small intestine, and can extend through the stomach wall to nearby
lymph nodes and organs. It also can metastasize to other parts of
the body. The term gastric cancer or gastric carcinoma refers to
adenocarcinoma of the stomach that accounts for most of all
gastric malignant tumors. Two main histologic types are
recognized, diffuse type and intestinal type carcinomas. Diffuse
tumors are poorly differentiated infiltrating lesions, resulting
in thickening of the stomach. In contrast, intestinal tumors are
usually exophytic, often ulcerating, and associated with
intestinal metaplasia of the stomach, most often observed in
sporadic disease. {ECO:0000269|PubMed:14534542,
ECO:0000269|PubMed:3034404, ECO:0000269|PubMed:7773929}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Note=Defects in KRAS are a cause of pylocytic astrocytoma
(PA). Pylocytic astrocytomas are neoplasms of the brain and spinal
cord derived from glial cells which vary from histologically
benign forms to highly anaplastic and malignant tumors.
{ECO:0000269|PubMed:16247081}.
-!- DISEASE: Cardiofaciocutaneous syndrome 2 (CFC2) [MIM:615278]: A
form of cardiofaciocutaneous syndrome, a multiple congenital
anomaly disorder characterized by a distinctive facial appearance,
heart defects and mental retardation. Heart defects include
pulmonic stenosis, atrial septal defects and hypertrophic
cardiomyopathy. Some affected individuals present with ectodermal
abnormalities such as sparse, friable hair, hyperkeratotic skin
lesions and a generalized ichthyosis-like condition. Typical
facial features are similar to Noonan syndrome. They include high
forehead with bitemporal constriction, hypoplastic supraorbital
ridges, downslanting palpebral fissures, a depressed nasal bridge,
and posteriorly angulated ears with prominent helices. CFC2
patients often do not have the skin abnormalities, such as
ichthyosis, hyperkeratosis, and hemangioma observed in CFC1.
{ECO:0000269|PubMed:16474404, ECO:0000269|PubMed:16474405,
ECO:0000269|PubMed:17056636, ECO:0000269|PubMed:20949621,
ECO:0000269|PubMed:21797849}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=KRAS mutations are involved in cancer development.
{ECO:0000269|PubMed:14534542, ECO:0000269|PubMed:1553789,
ECO:0000269|PubMed:16533793, ECO:0000269|PubMed:24623306,
ECO:0000269|PubMed:3034404, ECO:0000269|PubMed:3627975,
ECO:0000269|PubMed:6092920, ECO:0000269|PubMed:6695174,
ECO:0000269|PubMed:7773929}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/KRASID91.html";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=KRAS";
-----------------------------------------------------------------------
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EMBL; L00049; AAB59444.1; -; Genomic_DNA.
EMBL; L00045; AAB59444.1; JOINED; Genomic_DNA.
EMBL; L00046; AAB59444.1; JOINED; Genomic_DNA.
EMBL; L00047; AAB59444.1; JOINED; Genomic_DNA.
EMBL; L00048; AAB59445.1; -; Genomic_DNA.
EMBL; L00045; AAB59445.1; JOINED; Genomic_DNA.
EMBL; L00046; AAB59445.1; JOINED; Genomic_DNA.
EMBL; L00047; AAB59445.1; JOINED; Genomic_DNA.
EMBL; M54968; AAB41942.1; -; mRNA.
EMBL; AF493917; AAM12631.1; -; mRNA.
EMBL; BT007153; AAP35817.1; -; mRNA.
EMBL; AK292510; BAF85199.1; -; mRNA.
EMBL; CH471094; EAW96511.1; -; Genomic_DNA.
EMBL; CH471094; EAW96512.1; -; Genomic_DNA.
EMBL; EU332849; ABY87538.1; -; Genomic_DNA.
EMBL; BC013572; AAH13572.1; -; mRNA.
EMBL; K01519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; K01520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M25876; AAA35683.1; -; Genomic_DNA.
EMBL; M34904; AAA36149.1; -; Genomic_DNA.
EMBL; M30539; AAA36557.1; -; Genomic_DNA.
EMBL; X01669; CAA25828.1; -; Genomic_DNA.
EMBL; X02825; CAA26593.1; -; Genomic_DNA.
EMBL; K03210; AAA36554.1; -; Genomic_DNA.
EMBL; K03209; AAA36554.1; JOINED; Genomic_DNA.
CCDS; CCDS8702.1; -. [P01116-2]
CCDS; CCDS8703.1; -. [P01116-1]
PIR; A93311; TVHUK.
PIR; B93311; TVHU2K.
RefSeq; NP_004976.2; NM_004985.4. [P01116-2]
RefSeq; NP_203524.1; NM_033360.3. [P01116-1]
RefSeq; XP_006719132.1; XM_006719069.3. [P01116-1]
RefSeq; XP_011518955.1; XM_011520653.2. [P01116-2]
UniGene; Hs.37003; -.
UniGene; Hs.505033; -.
PDB; 1D8D; X-ray; 2.00 A; P=178-188.
PDB; 1D8E; X-ray; 3.00 A; P=178-188.
PDB; 1KZO; X-ray; 2.20 A; C=169-173.
PDB; 1KZP; X-ray; 2.10 A; C=169-173.
PDB; 1N4P; X-ray; 2.65 A; M/N=185-189.
PDB; 1N4Q; X-ray; 2.40 A; M/N/O/P/Q/R=185-189.
PDB; 1N4R; X-ray; 2.80 A; M/N/O/P/Q/R=185-189.
PDB; 1N4S; X-ray; 2.60 A; M/N/O/P/Q/R=185-189.
PDB; 3GFT; X-ray; 2.27 A; A/B/C/D/E/F=1-164.
PDB; 4DSN; X-ray; 2.03 A; A=2-164.
PDB; 4DSO; X-ray; 1.85 A; A=2-164.
PDB; 4EPR; X-ray; 2.00 A; A=1-164.
PDB; 4EPT; X-ray; 2.00 A; A=1-164.
PDB; 4EPV; X-ray; 1.35 A; A=1-164.
PDB; 4EPW; X-ray; 1.70 A; A=1-164.
PDB; 4EPX; X-ray; 1.76 A; A=1-164.
PDB; 4EPY; X-ray; 1.80 A; A=1-164.
PDB; 4L8G; X-ray; 1.52 A; A=1-169.
PDB; 4LDJ; X-ray; 1.15 A; A=1-164.
PDB; 4LPK; X-ray; 1.50 A; A/B=1-169.
PDB; 4LRW; X-ray; 2.15 A; A/B=1-169.
PDB; 4LUC; X-ray; 1.29 A; A/B=1-169.
PDB; 4LV6; X-ray; 1.50 A; A/B=1-169.
PDB; 4LYF; X-ray; 1.57 A; A/B/C=1-169.
PDB; 4LYH; X-ray; 1.37 A; A/B/C=1-169.
PDB; 4LYJ; X-ray; 1.93 A; A=1-169.
PDB; 4M1O; X-ray; 1.57 A; A/B/C=1-169.
PDB; 4M1S; X-ray; 1.55 A; A/B/C=1-169.
PDB; 4M1T; X-ray; 1.70 A; A/B/C=1-169.
PDB; 4M1W; X-ray; 1.58 A; A/B/C=1-169.
PDB; 4M1Y; X-ray; 1.49 A; A/B/C=1-169.
PDB; 4M21; X-ray; 1.94 A; A/B/C=1-169.
PDB; 4M22; X-ray; 2.09 A; A/B/C=1-169.
PDB; 4NMM; X-ray; 1.89 A; A=1-164.
PDB; 4OBE; X-ray; 1.24 A; A/B=1-164.
PDB; 4PZY; X-ray; 1.88 A; A/B=1-164.
PDB; 4PZZ; X-ray; 1.40 A; A=1-164.
PDB; 4Q01; X-ray; 1.29 A; A/B=1-164.
PDB; 4Q02; X-ray; 1.70 A; A=1-164.
PDB; 4Q03; X-ray; 1.20 A; A=1-164.
PDB; 4QL3; X-ray; 1.04 A; A=1-11, A=13-164.
PDB; 4TQ9; X-ray; 1.49 A; A/B=1-164.
PDB; 4TQA; X-ray; 1.13 A; A/B=1-164.
PDB; 4WA7; X-ray; 1.99 A; A=1-164.
PDB; 5F2E; X-ray; 1.40 A; A=1-169.
PDB; 5KYK; X-ray; 2.70 A; A/B/C=1-167.
PDB; 5O2S; X-ray; 3.22 A; A/C/E/G=1-166.
PDB; 5O2T; X-ray; 2.19 A; A=1-166.
PDB; 5TAR; X-ray; 1.90 A; A=2-164.
PDB; 5TB5; X-ray; 2.00 A; A/C=2-164.
PDB; 5UFE; X-ray; 2.30 A; A=1-166.
PDB; 5UFQ; X-ray; 2.20 A; A/B=1-166.
PDB; 5UQW; X-ray; 1.50 A; A/B=1-164.
PDB; 5US4; X-ray; 1.83 A; A/B=1-164.
PDB; 5USJ; X-ray; 1.94 A; A/B/C/D/E/F=1-164.
PDB; 5V6S; X-ray; 1.70 A; A=1-169.
PDB; 5V6V; X-ray; 1.72 A; A/B=1-169.
PDB; 5V71; X-ray; 2.23 A; A/B/C/D/E/F=1-167.
PDB; 5V9L; X-ray; 1.98 A; A/B/C=1-167.
PDB; 5V9O; X-ray; 1.56 A; A=1-167.
PDB; 5XCO; X-ray; 1.25 A; A=1-169.
PDBsum; 1D8D; -.
PDBsum; 1D8E; -.
PDBsum; 1KZO; -.
PDBsum; 1KZP; -.
PDBsum; 1N4P; -.
PDBsum; 1N4Q; -.
PDBsum; 1N4R; -.
PDBsum; 1N4S; -.
PDBsum; 3GFT; -.
PDBsum; 4DSN; -.
PDBsum; 4DSO; -.
PDBsum; 4EPR; -.
PDBsum; 4EPT; -.
PDBsum; 4EPV; -.
PDBsum; 4EPW; -.
PDBsum; 4EPX; -.
PDBsum; 4EPY; -.
PDBsum; 4L8G; -.
PDBsum; 4LDJ; -.
PDBsum; 4LPK; -.
PDBsum; 4LRW; -.
PDBsum; 4LUC; -.
PDBsum; 4LV6; -.
PDBsum; 4LYF; -.
PDBsum; 4LYH; -.
PDBsum; 4LYJ; -.
PDBsum; 4M1O; -.
PDBsum; 4M1S; -.
PDBsum; 4M1T; -.
PDBsum; 4M1W; -.
PDBsum; 4M1Y; -.
PDBsum; 4M21; -.
PDBsum; 4M22; -.
PDBsum; 4NMM; -.
PDBsum; 4OBE; -.
PDBsum; 4PZY; -.
PDBsum; 4PZZ; -.
PDBsum; 4Q01; -.
PDBsum; 4Q02; -.
PDBsum; 4Q03; -.
PDBsum; 4QL3; -.
PDBsum; 4TQ9; -.
PDBsum; 4TQA; -.
PDBsum; 4WA7; -.
PDBsum; 5F2E; -.
PDBsum; 5KYK; -.
PDBsum; 5O2S; -.
PDBsum; 5O2T; -.
PDBsum; 5TAR; -.
PDBsum; 5TB5; -.
PDBsum; 5UFE; -.
PDBsum; 5UFQ; -.
PDBsum; 5UQW; -.
PDBsum; 5US4; -.
PDBsum; 5USJ; -.
PDBsum; 5V6S; -.
PDBsum; 5V6V; -.
PDBsum; 5V71; -.
PDBsum; 5V9L; -.
PDBsum; 5V9O; -.
PDBsum; 5XCO; -.
ProteinModelPortal; P01116; -.
SMR; P01116; -.
BioGrid; 110043; 449.
CORUM; P01116; -.
DIP; DIP-33951N; -.
IntAct; P01116; 69.
MINT; MINT-131580; -.
STRING; 9606.ENSP00000256078; -.
BindingDB; P01116; -.
ChEMBL; CHEMBL2189121; -.
DrugBank; DB07780; FARNESYL DIPHOSPHATE.
GuidetoPHARMACOLOGY; 2824; -.
iPTMnet; P01116; -.
PhosphoSitePlus; P01116; -.
SwissPalm; P01116; -.
BioMuta; KRAS; -.
DMDM; 131875; -.
EPD; P01116; -.
MaxQB; P01116; -.
PaxDb; P01116; -.
PeptideAtlas; P01116; -.
PRIDE; P01116; -.
DNASU; 3845; -.
Ensembl; ENST00000256078; ENSP00000256078; ENSG00000133703. [P01116-1]
Ensembl; ENST00000311936; ENSP00000308495; ENSG00000133703. [P01116-2]
GeneID; 3845; -.
KEGG; hsa:3845; -.
UCSC; uc001rgp.3; human. [P01116-1]
CTD; 3845; -.
DisGeNET; 3845; -.
EuPathDB; HostDB:ENSG00000133703.11; -.
GeneCards; KRAS; -.
GeneReviews; KRAS; -.
HGNC; HGNC:6407; KRAS.
HPA; HPA049830; -.
MalaCards; KRAS; -.
MIM; 190070; gene.
MIM; 601626; phenotype.
MIM; 607785; phenotype.
MIM; 609942; phenotype.
MIM; 613659; phenotype.
MIM; 615278; phenotype.
neXtProt; NX_P01116; -.
OpenTargets; ENSG00000133703; -.
Orphanet; 1340; Cardiofaciocutaneous syndrome.
Orphanet; 1333; Familial pancreatic carcinoma.
Orphanet; 144; Hereditary nonpolyposis colon cancer.
Orphanet; 86834; Juvenile myelomonocytic leukemia.
Orphanet; 2612; Linear nevus sebaceus syndrome.
Orphanet; 648; Noonan syndrome.
Orphanet; 251612; Pilocytic astrocytoma.
Orphanet; 268114; RAS-associated autoimmune leukoproliferative disease.
Orphanet; 357194; Selection of therapeutic option in colorectal cancer.
Orphanet; 357191; Selection of therapeutic option in non-small cell lung carcinoma.
PharmGKB; PA30196; -.
eggNOG; KOG0395; Eukaryota.
eggNOG; COG1100; LUCA.
GeneTree; ENSGT00860000133672; -.
HOGENOM; HOG000233973; -.
HOVERGEN; HBG009351; -.
InParanoid; P01116; -.
KO; K07827; -.
OMA; QSWAVNM; -.
OrthoDB; EOG091G0UAU; -.
PhylomeDB; P01116; -.
TreeFam; TF312796; -.
Reactome; R-HSA-112412; SOS-mediated signalling.
Reactome; R-HSA-1169092; Activation of RAS in B cells.
Reactome; R-HSA-1236382; Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
Reactome; R-HSA-1250196; SHC1 events in ERBB2 signaling.
Reactome; R-HSA-1250347; SHC1 events in ERBB4 signaling.
Reactome; R-HSA-1433557; Signaling by SCF-KIT.
Reactome; R-HSA-167044; Signalling to RAS.
Reactome; R-HSA-171007; p38MAPK events.
Reactome; R-HSA-179812; GRB2 events in EGFR signaling.
Reactome; R-HSA-180336; SHC1 events in EGFR signaling.
Reactome; R-HSA-186763; Downstream signal transduction.
Reactome; R-HSA-1963640; GRB2 events in ERBB2 signaling.
Reactome; R-HSA-210993; Tie2 Signaling.
Reactome; R-HSA-2179392; EGFR Transactivation by Gastrin.
Reactome; R-HSA-2424491; DAP12 signaling.
Reactome; R-HSA-2428933; SHC-related events triggered by IGF1R.
Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
Reactome; R-HSA-375165; NCAM signaling for neurite out-growth.
Reactome; R-HSA-5218921; VEGFR2 mediated cell proliferation.
Reactome; R-HSA-5621575; CD209 (DC-SIGN) signaling.
Reactome; R-HSA-5637810; Constitutive Signaling by EGFRvIII.
Reactome; R-HSA-5654688; SHC-mediated cascade:FGFR1.
Reactome; R-HSA-5654693; FRS-mediated FGFR1 signaling.
Reactome; R-HSA-5654699; SHC-mediated cascade:FGFR2.
Reactome; R-HSA-5654700; FRS-mediated FGFR2 signaling.
Reactome; R-HSA-5654704; SHC-mediated cascade:FGFR3.
Reactome; R-HSA-5654706; FRS-mediated FGFR3 signaling.
Reactome; R-HSA-5654712; FRS-mediated FGFR4 signaling.
Reactome; R-HSA-5654719; SHC-mediated cascade:FGFR4.
Reactome; R-HSA-5655253; Signaling by FGFR2 in disease.
Reactome; R-HSA-5655291; Signaling by FGFR4 in disease.
Reactome; R-HSA-5655302; Signaling by FGFR1 in disease.
Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
Reactome; R-HSA-5673000; RAF activation.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-5674135; MAP2K and MAPK activation.
Reactome; R-HSA-5675221; Negative regulation of MAPK pathway.
Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants.
Reactome; R-HSA-6802949; Signaling by RAS mutants.
Reactome; R-HSA-6802952; Signaling by BRAF and RAF fusions.
Reactome; R-HSA-6802953; RAS signaling downstream of NF1 loss-of-function variants.
Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
Reactome; R-HSA-74751; Insulin receptor signalling cascade.
Reactome; R-HSA-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
Reactome; R-HSA-8851805; MET activates RAS signaling.
Reactome; R-HSA-8853334; Signaling by FGFR3 fusions in cancer.
Reactome; R-HSA-8853338; Signaling by FGFR3 point mutants in cancer.
Reactome; R-HSA-8951936; RUNX3 regulates p14-ARF.
SignaLink; P01116; -.
SIGNOR; P01116; -.
ChiTaRS; KRAS; human.
EvolutionaryTrace; P01116; -.
GeneWiki; KRAS; -.
GenomeRNAi; 3845; -.
PRO; PR:P01116; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000133703; -.
CleanEx; HS_KRAS; -.
ExpressionAtlas; P01116; baseline and differential.
Genevisible; P01116; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0019003; F:GDP binding; IEA:Ensembl.
GO; GO:0019002; F:GMP binding; IEA:Ensembl.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0030275; F:LRR domain binding; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IDA:MGI.
GO; GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IEA:Ensembl.
GO; GO:0038002; P:endocrine signaling; IEA:Ensembl.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEA:Ensembl.
GO; GO:0038128; P:ERBB2 signaling pathway; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
GO; GO:0021897; P:forebrain astrocyte development; IEA:Ensembl.
GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0001889; P:liver development; IEA:Ensembl.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0045596; P:negative regulation of cell differentiation; IEA:Ensembl.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:2000774; P:positive regulation of cellular senescence; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IEA:Ensembl.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IEA:Ensembl.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:BHF-UCL.
GO; GO:0035022; P:positive regulation of Rac protein signal transduction; IEA:Ensembl.
GO; GO:0007265; P:Ras protein signal transduction; TAS:Reactome.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; IEA:Ensembl.
GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
GO; GO:0035900; P:response to isolation stress; IEA:Ensembl.
GO; GO:0051385; P:response to mineralocorticoid; IEA:Ensembl.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0051146; P:striated muscle cell differentiation; IEA:Ensembl.
GO; GO:0008542; P:visual learning; IEA:Ensembl.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
InterPro; IPR020849; Small_GTPase_Ras.
PANTHER; PTHR24070; PTHR24070; 1.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51421; RAS; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cardiomyopathy;
Cell membrane; Complete proteome; Cytoplasm; Deafness;
Direct protein sequencing; Disease mutation; Ectodermal dysplasia;
GTP-binding; Lipoprotein; Membrane; Mental retardation; Methylation;
Nucleotide-binding; Palmitate; Polymorphism; Prenylation;
Proto-oncogene; Reference proteome; S-nitrosylation.
CHAIN 1 186 GTPase KRas.
/FTId=PRO_0000082641.
INIT_MET 1 1 Removed; alternate. {ECO:0000269|Ref.17}.
CHAIN 2 186 GTPase KRas, N-terminally processed.
/FTId=PRO_0000326480.
PROPEP 187 189 Removed in mature form.
/FTId=PRO_0000281291.
NP_BIND 10 18 GTP. {ECO:0000269|PubMed:22431598,
ECO:0000269|PubMed:22566140}.
NP_BIND 29 35 GTP. {ECO:0000269|PubMed:22431598,
ECO:0000269|PubMed:22566140}.
NP_BIND 59 60 GTP. {ECO:0000269|PubMed:22431598,
ECO:0000269|PubMed:22566140}.
NP_BIND 116 119 GTP. {ECO:0000269|PubMed:22431598,
ECO:0000269|PubMed:22566140}.
REGION 166 185 Hypervariable region.
MOTIF 32 40 Effector region.
MOD_RES 1 1 N-acetylmethionine; in GTPase KRas;
alternate. {ECO:0000269|Ref.17}.
MOD_RES 2 2 N-acetylthreonine; in GTPase KRas, N-
terminally processed.
{ECO:0000269|Ref.17}.
MOD_RES 104 104 N6-acetyllysine.
{ECO:0000269|PubMed:22711838}.
MOD_RES 118 118 S-nitrosocysteine.
{ECO:0000250|UniProtKB:P01112}.
MOD_RES 186 186 Cysteine methyl ester.
{ECO:0000244|PDB:5TAR,
ECO:0000244|PDB:5TB5,
ECO:0000269|PubMed:27791178}.
LIPID 180 180 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 186 186 S-farnesyl cysteine.
{ECO:0000244|PDB:5TAR,
ECO:0000244|PDB:5TB5,
ECO:0000269|PubMed:27791178}.
VAR_SEQ 151 153 RVE -> GVD (in isoform 2B).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:3310850,
ECO:0000303|Ref.6, ECO:0000303|Ref.7}.
/FTId=VSP_011140.
VAR_SEQ 165 189 QYRLKKISKEEKTPGCVKIKKCIIM -> KHKEKMSKDGKK
KKKKSKTKCVIM (in isoform 2B).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:3310850,
ECO:0000303|Ref.6, ECO:0000303|Ref.7}.
/FTId=VSP_011141.
VARIANT 5 5 K -> E (in NS3; dbSNP:rs193929331).
{ECO:0000269|PubMed:17468812}.
/FTId=VAR_065144.
VARIANT 5 5 K -> N (in GASC; found also in a patient
with Costello syndrome; exhibits only
minor alterations in its in vitro
biochemical behavior compared to wild-
type protein; dbSNP:rs104894361).
{ECO:0000269|PubMed:14534542}.
/FTId=VAR_064849.
VARIANT 10 10 G -> GG (in AML; expression in 3T3 cell
causes cellular transformation;
expression in COS cells activates the
Ras-MAPK signaling pathway; lower GTPase
activity; faster GDP dissociation rate).
{ECO:0000269|PubMed:8955068}.
/FTId=VAR_034601.
VARIANT 12 12 G -> A (in a colorectal cancer sample;
somatic mutation; dbSNP:rs121913529).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036305.
VARIANT 12 12 G -> C (in lung carcinoma; somatic
mutation; dbSNP:rs121913530).
{ECO:0000269|PubMed:16533793,
ECO:0000269|PubMed:6320174}.
/FTId=VAR_006839.
VARIANT 12 12 G -> D (in GASC and JMML; also found in
pancreatic carcinoma and lung carcinoma;
somatic mutation; dbSNP:rs121913529).
{ECO:0000269|PubMed:16533793,
ECO:0000269|PubMed:16959974,
ECO:0000269|PubMed:17332249,
ECO:0000269|PubMed:7773929,
ECO:0000269|PubMed:8439212}.
/FTId=VAR_016026.
VARIANT 12 12 G -> R (in lung cancer and bladder
cancer; somatic mutation;
dbSNP:rs121913530).
{ECO:0000269|PubMed:6695174}.
/FTId=VAR_016027.
VARIANT 12 12 G -> S (in GASC and JMML; also found in
lung carcinoma; somatic mutation;
dbSNP:rs121913530).
{ECO:0000269|PubMed:16533793,
ECO:0000269|PubMed:16959974,
ECO:0000269|PubMed:17332249,
ECO:0000269|PubMed:7773929}.
/FTId=VAR_016028.
VARIANT 12 12 G -> V (in GASC; also found in lung
carcinoma, pancreatic carcinoma and colon
cancer; somatic mutation; it is
constitutively activated and stimulates
transcription activation of tumor
suppressor genes in non-transformed
fibroblasts; dbSNP:rs121913529).
{ECO:0000269|PubMed:14534542,
ECO:0000269|PubMed:16533793,
ECO:0000269|PubMed:16959974,
ECO:0000269|PubMed:22711838,
ECO:0000269|PubMed:24623306,
ECO:0000269|PubMed:3034404,
ECO:0000269|PubMed:6092920,
ECO:0000269|PubMed:8439212}.
/FTId=VAR_006840.
VARIANT 13 13 G -> D (in GASC and JMML; also found in a
breast carcinoma cell line; somatic
mutation; dbSNP:rs112445441).
{ECO:0000269|PubMed:14534542,
ECO:0000269|PubMed:16959974,
ECO:0000269|PubMed:17332249,
ECO:0000269|PubMed:3627975}.
/FTId=VAR_016029.
VARIANT 13 13 G -> R (in pylocytic astrocytoma; somatic
mutation; increase activation of the Ras
pathway; dbSNP:rs121913535).
{ECO:0000269|PubMed:16247081}.
/FTId=VAR_065145.
VARIANT 14 14 V -> I (in NS3; affects activity and
impairs responsiveness to GTPase
activating proteins; characterized by a
strong increase of both intrinsic and
guanine nucleotide exchanged factor-
catalyzed nucleotide exchange leading to
an increased level of the activated
state; dbSNP:rs104894365).
{ECO:0000269|PubMed:16474405}.
/FTId=VAR_026109.
VARIANT 22 22 Q -> E (in CFC2; exhibits an increase in
intrinsic and guanine nucleotide exchange
factor catalyzed nucleotide exchange in
combination with an impaired GTPase-
activating protein-stimulated GTP
hydrolysis but functional in interaction
with effectors).
{ECO:0000269|PubMed:17056636,
ECO:0000269|PubMed:20949621}.
/FTId=VAR_064850.
VARIANT 22 22 Q -> R (in NS3; impairs GTPase-activating
protein stimulated GTP hydrolysis with
unaffected intrinsic functions and a
virtually functional effector
interaction; dbSNP:rs727503110).
/FTId=VAR_064851.
VARIANT 34 34 P -> L (in NS3; characterized by a
defective GTPase-activating protein
sensitivity and a strongly reduced
interaction with effectors;
dbSNP:rs104894366).
/FTId=VAR_064852.
VARIANT 34 34 P -> Q (in NS3).
/FTId=VAR_064853.
VARIANT 34 34 P -> R (in CFC2; characterized by a
defective GTPase-activating protein
sensitivity and a strongly reduced
interaction with effectors;
dbSNP:rs104894366).
{ECO:0000269|PubMed:16474405,
ECO:0000269|PubMed:20949621}.
/FTId=VAR_026110.
VARIANT 36 36 I -> M (in NS3; dbSNP:rs727503109).
/FTId=VAR_064854.
VARIANT 58 58 T -> I (in NS3; affects activity and
impairs responsiveness to GTPase
activating proteins; exhibits only minor
alterations in its in vitro biochemical
behavior compared to wild-type protein;
dbSNP:rs104894364).
{ECO:0000269|PubMed:16474405,
ECO:0000269|PubMed:19396835}.
/FTId=VAR_026111.
VARIANT 59 59 A -> T (in GASC; also found in bladder
cancer; somatic mutation;
dbSNP:rs121913528).
{ECO:0000269|PubMed:14534542,
ECO:0000269|PubMed:1553789}.
/FTId=VAR_016030.
VARIANT 60 60 G -> R (in CFC2; characterized by a
defective GTPase-activating protein
sensitivity and a strongly reduced
interaction with effectors;
dbSNP:rs104894359).
{ECO:0000269|PubMed:16474404,
ECO:0000269|PubMed:20949621}.
/FTId=VAR_026112.
VARIANT 60 60 G -> S (in NS3; dbSNP:rs104894359).
{ECO:0000269|PubMed:19396835}.
/FTId=VAR_065146.
VARIANT 61 61 Q -> H (in lung carcinoma;
dbSNP:rs17851045).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16533793,
ECO:0000269|Ref.7}.
/FTId=VAR_006841.
VARIANT 61 61 Q -> R (in a colorectal cancer sample;
somatic mutation; dbSNP:rs121913240).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036306.
VARIANT 71 71 Y -> H (in CFC2; dbSNP:rs387907205).
{ECO:0000269|PubMed:21797849}.
/FTId=VAR_069784.
VARIANT 117 117 K -> N (in a colorectal cancer sample;
somatic mutation; dbSNP:rs770248150).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036307.
VARIANT 146 146 A -> T (in a colorectal cancer sample;
somatic mutation; dbSNP:rs121913527).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036308.
VARIANT 147 147 K -> E (in CFC2; dbSNP:rs387907206).
{ECO:0000269|PubMed:21797849}.
/FTId=VAR_069785.
MUTAGEN 164 164 R->A: Loss of GTP-binding activity.
STRAND 3 9 {ECO:0000244|PDB:4QL3}.
HELIX 16 25 {ECO:0000244|PDB:4QL3}.
STRAND 38 46 {ECO:0000244|PDB:4QL3}.
STRAND 49 57 {ECO:0000244|PDB:4QL3}.
HELIX 60 62 {ECO:0000244|PDB:4Q01}.
HELIX 65 74 {ECO:0000244|PDB:4QL3}.
STRAND 76 83 {ECO:0000244|PDB:4QL3}.
HELIX 87 91 {ECO:0000244|PDB:4QL3}.
HELIX 93 104 {ECO:0000244|PDB:4QL3}.
STRAND 111 116 {ECO:0000244|PDB:4QL3}.
STRAND 120 122 {ECO:0000244|PDB:4OBE}.
HELIX 127 137 {ECO:0000244|PDB:4QL3}.
STRAND 141 143 {ECO:0000244|PDB:4QL3}.
TURN 146 148 {ECO:0000244|PDB:4QL3}.
HELIX 152 167 {ECO:0000244|PDB:4QL3}.
HELIX 169 173 {ECO:0000244|PDB:4DSO}.
STRAND 175 177 {ECO:0000244|PDB:4DSN}.
STRAND 182 184 {ECO:0000244|PDB:5TB5}.
SEQUENCE 189 AA; 21656 MW; 973547B2E11C2C81 CRC64;
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHHYREQI KRVKDSEDVP MVLVGNKCDL
PSRTVDTKQA QDLARSYGIP FIETSAKTRQ RVEDAFYTLV REIRQYRLKK ISKEEKTPGC
VKIKKCIIM


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