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Epithelial discoidin domain-containing receptor 1 (Epithelial discoidin domain receptor 1) (EC 2.7.10.1) (CD167 antigen-like family member A) (Cell adhesion kinase) (Discoidin receptor tyrosine kinase) (HGK2) (Mammary carcinoma kinase 10) (MCK-10) (Protein-tyrosine kinase 3A) (Protein-tyrosine kinase RTK-6) (TRK E) (Tyrosine kinase DDR) (Tyrosine-protein kinase CAK) (CD antigen CD167a)

 DDR1_HUMAN              Reviewed;         913 AA.
Q08345; B5A975; B5A976; B7Z2K0; Q14196; Q16562; Q2L6H3; Q4LE50;
Q5ST11; Q5ST12; Q6NSK4; Q9UD35; Q9UD36; Q9UD37; Q9UD86; Q9UDL2;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
25-OCT-2017, entry version 197.
RecName: Full=Epithelial discoidin domain-containing receptor 1;
Short=Epithelial discoidin domain receptor 1;
EC=2.7.10.1;
AltName: Full=CD167 antigen-like family member A;
AltName: Full=Cell adhesion kinase;
AltName: Full=Discoidin receptor tyrosine kinase;
AltName: Full=HGK2;
AltName: Full=Mammary carcinoma kinase 10;
Short=MCK-10;
AltName: Full=Protein-tyrosine kinase 3A;
AltName: Full=Protein-tyrosine kinase RTK-6;
AltName: Full=TRK E;
AltName: Full=Tyrosine kinase DDR;
AltName: Full=Tyrosine-protein kinase CAK;
AltName: CD_antigen=CD167a;
Flags: Precursor;
Name=DDR1; Synonyms=CAK, EDDR1, NEP, NTRK4, PTK3A, RTK6, TRKE;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Brain, and Keratinocyte;
PubMed=8226977;
di Marco E., Cutuli N., Guerra L., Cancedda R., de Luca M.;
"Molecular cloning of trkE, a novel trk-related putative tyrosine
kinase receptor isolated from normal human keratinocytes and widely
expressed by normal human tissues.";
J. Biol. Chem. 268:24290-24295(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-833.
TISSUE=Placenta;
PubMed=8390675; DOI=10.1073/pnas.90.12.5677;
Johnson J.D., Edman J.C., Rutter W.J.;
"A receptor tyrosine kinase found in breast carcinoma cells has an
extracellular discoidin I-like domain.";
Proc. Natl. Acad. Sci. U.S.A. 90:5677-5681(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
TISSUE=Ovary;
PubMed=7848919;
Laval S., Butler R., Shelling A.N., Hanby A.M., Poulsom R.,
Ganesan T.S.;
"Isolation and characterization of an epithelial-specific receptor
tyrosine kinase from an ovarian cancer cell line.";
Cell Growth Differ. 5:1173-1183(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal liver;
PubMed=8302582;
Perez J.L., Shen X., Finkernagel S., Sciorra L., Jenkins N.A.,
Gilbert D.J., Copeland N.G., Wong T.W.;
"Identification and chromosomal mapping of a receptor tyrosine kinase
with a putative phospholipid binding sequence in its ectodomain.";
Oncogene 9:211-219(1994).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-833.
PubMed=8977099; DOI=10.1016/S0014-5793(96)01234-3;
Sakuma S., Tada M., Saya H., Sawamura Y., Shinohe Y., Abe H.;
"Receptor protein tyrosine kinase DDR is up-regulated by p53
protein.";
FEBS Lett. 398:165-169(1996).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8796349; DOI=10.1101/gr.6.7.620;
Playford M.P., Butler R.J., Wang X.C., Katso R.M., Cooke I.E.,
Ganesan T.S.;
"The genomic structure of discoidin receptor tyrosine kinase.";
Genome Res. 6:620-627(1996).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Lung;
PubMed=8622863;
Perez J.L., Jing S.Q., Wong T.W.;
"Identification of two isoforms of the Cak receptor kinase that are
coexpressed in breast tumor cell lines.";
Oncogene 12:1469-1477(1996).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE [MRNA]
OF 1-286 (ISOFORMS 1/2/4).
PubMed=18593464; DOI=10.1186/ar2447;
Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D.,
Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.;
"Novel splice variants derived from the receptor tyrosine kinase
superfamily are potential therapeutics for rheumatoid arthritis.";
Arthritis Res. Ther. 10:R73-R73(2008).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5).
TISSUE=Brain, and Placenta;
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).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M.,
Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.;
"Preparation of a set of expression-ready clones of mammalian long
cDNAs encoding large proteins by the ORF trap cloning method.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
TISSUE=Peripheral blood leukocyte;
PubMed=16702430; DOI=10.1534/genetics.106.057034;
Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M.,
Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K.,
Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y.,
Meyer A., Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K.,
Gojobori T., Inoko H., Bahram S.;
"Rapid evolution of major histocompatibility complex class I genes in
primates generates new disease alleles in humans via hitchhiking
diversity.";
Genetics 173:1555-1570(2006).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[13]
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.
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain, and Muscle;
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).
[15]
PROTEIN SEQUENCE OF 480-490; 515-525 AND 790-798, IDENTIFICATION BY
MASS SPECTROMETRY, SUBUNIT, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
TYR-484; TYR-513; TYR-520; TYR-792; TYR-796 AND TYR-797, GLYCOSYLATION
AT ASN-211 AND ASN-260, AND MUTAGENESIS OF ARG-105; ASN-211; SER-213;
ASN-260; ASN-371; THR-379; THR-393; ASN-394 AND LYS-655.
PubMed=24509848; DOI=10.1074/jbc.M113.541102;
Fu H.L., Valiathan R.R., Payne L., Kumarasiri M., Mahasenan K.V.,
Mobashery S., Huang P., Fridman R.;
"Glycosylation at Asn211 regulates the activation state of the
discoidin domain receptor 1 (DDR1).";
J. Biol. Chem. 289:9275-9287(2014).
[16]
NUCLEOTIDE SEQUENCE [MRNA] OF 501-550 (ISOFORMS 1/4), NUCLEOTIDE
SEQUENCE [MRNA] OF 501-550 AND 651-694 (ISOFORM 2), NUCLEOTIDE
SEQUENCE [MRNA] OF 651-694 (ISOFORM 4), ALTERNATIVE SPLICING, AND
TISSUE SPECIFICITY.
TISSUE=Mammary carcinoma;
PubMed=7845687;
Alves F., Vogel W., Mossie K., Millauer B., Hoefler H., Ullrich A.;
"Distinct structural characteristics of discoidin I subfamily receptor
tyrosine kinases and complementary expression in human cancer.";
Oncogene 10:609-618(1995).
[17]
NUCLEOTIDE SEQUENCE [MRNA] OF 771-824 (ISOFORMS 1/2/4).
PubMed=7834423; DOI=10.1007/BF02303537;
Weiner T.M., Liu E.T., Craven R.J., Cance W.G.;
"Expression of growth factor receptors, the focal adhesion kinase, and
other tyrosine kinases in human soft tissue tumors.";
Ann. Surg. Oncol. 1:18-27(1994).
[18]
NUCLEOTIDE SEQUENCE [MRNA] OF 772-823 (ISOFORMS 1/2/4), AND TISSUE
SPECIFICITY.
TISSUE=Melanocyte;
PubMed=8247543;
Lee S.-T., Strunk K.M., Spritz R.A.;
"A survey of protein tyrosine kinase mRNAs expressed in normal human
melanocytes.";
Oncogene 8:3403-3410(1993).
[19]
FUNCTION AS COLLAGEN RECEPTOR, PHOSPHORYLATION AT TYR-513, INTERACTION
WITH SHC1, AUTOPHOSPHORYLATION, AND SUBCELLULAR LOCATION.
PubMed=9659899; DOI=10.1016/S1097-2765(00)80003-9;
Vogel W., Gish G.D., Alves F., Pawson T.;
"The discoidin domain receptor tyrosine kinases are activated by
collagen.";
Mol. Cell 1:13-23(1997).
[20]
FUNCTION.
PubMed=12065315; DOI=10.1161/01.RES.0000022166.74073.F8;
Hou G., Vogel W.F., Bendeck M.P.;
"Tyrosine kinase activity of discoidin domain receptor 1 is necessary
for smooth muscle cell migration and matrix metalloproteinase
expression.";
Circ. Res. 90:1147-1149(2002).
[21]
FUNCTION, INTERACTION WITH PTPN11 AND NCK2, PHOSPHORYLATION AT
TYR-740, AND MUTAGENESIS OF TYR-740.
PubMed=16337946; DOI=10.1016/j.febslet.2005.11.035;
Koo D.H., McFadden C., Huang Y., Abdulhussein R., Friese-Hamim M.,
Vogel W.F.;
"Pinpointing phosphotyrosine-dependent interactions downstream of the
collagen receptor DDR1.";
FEBS Lett. 580:15-22(2006).
[22]
FUNCTION.
PubMed=16234985; DOI=10.1007/s11060-005-6874-1;
Ram R., Lorente G., Nikolich K., Urfer R., Foehr E., Nagavarapu U.;
"Discoidin domain receptor-1a (DDR1a) promotes glioma cell invasion
and adhesion in association with matrix metalloproteinase-2.";
J. Neurooncol. 76:239-248(2006).
[23]
INTERACTION WITH WWC1 AND PRKCZ.
PubMed=18190796; DOI=10.1016/j.bbamcr.2007.12.007;
Hilton H.N., Stanford P.M., Harris J., Oakes S.R., Kaplan W.,
Daly R.J., Ormandy C.J.;
"KIBRA interacts with discoidin domain receptor 1 to modulate
collagen-induced signalling.";
Biochim. Biophys. Acta 1783:383-393(2008).
[24]
FUNCTION, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, AND INTERACTION
WITH MYH9.
PubMed=19401332; DOI=10.1242/jcs.046219;
Huang Y., Arora P., McCulloch C.A., Vogel W.F.;
"The collagen receptor DDR1 regulates cell spreading and motility by
associating with myosin IIA.";
J. Cell Sci. 122:1637-1646(2009).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[26]
FUNCTION, AND INTERACTION WITH CDH1.
PubMed=20432435; DOI=10.1002/jcp.22134;
Eswaramoorthy R., Wang C.K., Chen W.C., Tang M.J., Ho M.L.,
Hwang C.C., Wang H.M., Wang C.Z.;
"DDR1 regulates the stabilization of cell surface E-cadherin and E-
cadherin-mediated cell aggregation.";
J. Cell. Physiol. 224:387-397(2010).
[27]
FUNCTION, AND INTERACTION WITH SRC.
PubMed=20093046; DOI=10.1016/j.carpath.2009.12.006;
Lu K.K., Trcka D., Bendeck M.P.;
"Collagen stimulates discoidin domain receptor 1-mediated migration of
smooth muscle cells through Src.";
Cardiovasc. Pathol. 20:71-76(2011).
[28]
FUNCTION.
PubMed=20884741; DOI=10.1183/09031936.00039710;
Roberts M.E., Magowan L., Hall I.P., Johnson S.R.;
"Discoidin domain receptor 1 regulates bronchial epithelial repair and
matrix metalloproteinase production.";
Eur. Respir. J. 37:1482-1493(2011).
[29]
FUNCTION AS COLLAGEN RECEPTOR, AND AUTOPHOSPHORYLATION.
PubMed=21044884; DOI=10.1016/j.matbio.2010.10.004;
Xu H., Raynal N., Stathopoulos S., Myllyharju J., Farndale R.W.,
Leitinger B.;
"Collagen binding specificity of the discoidin domain receptors:
binding sites on collagens II and III and molecular determinants for
collagen IV recognition by DDR1.";
Matrix Biol. 30:16-26(2011).
[30]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 29-367 IN COMPLEX WITH
INHIBITORY ANTIBODY, SUBUNIT, CALCIUM-BINDING SITES, GLYCOSYLATION AT
ASN-211 AND ASN-260, AND DISULFIDE BONDS.
PubMed=22483115; DOI=10.1016/j.str.2012.02.011;
Carafoli F., Mayer M.C., Shiraishi K., Pecheva M.A., Chan L.Y.,
Nan R., Leitinger B., Hohenester E.;
"Structure of the discoidin domain receptor 1 extracellular region
bound to an inhibitory Fab fragment reveals features important for
signaling.";
Structure 20:688-697(2012).
[31]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 601-913 IN COMPLEX WITH
INHIBITOR, AUTOPHOSPHORYLATION, AND MUTAGENESIS OF GLY-707.
PubMed=23899692; DOI=10.1021/cb400430t;
Kim H.G., Tan L., Weisberg E.L., Liu F., Canning P., Choi H.G.,
Ezell S.A., Wu H., Zhao Z., Wang J., Mandinova A., Griffin J.D.,
Bullock A.N., Liu Q., Lee S.W., Gray N.S.;
"Discovery of a potent and selective DDR1 receptor tyrosine kinase
inhibitor.";
ACS Chem. Biol. 8:2145-2150(2013).
[32]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 601-913 IN COMPLEXES WITH
INHIBITORS IMATINIB AND PONATINIB, ENZYME REGULATION, AND
AUTOPHOSPHORYLATION.
PubMed=24768818; DOI=10.1016/j.jmb.2014.04.014;
Canning P., Tan L., Chu K., Lee S.W., Gray N.S., Bullock A.N.;
"Structural mechanisms determining inhibition of the collagen receptor
DDR1 by selective and multi-targeted type II kinase inhibitors.";
J. Mol. Biol. 426:2457-2470(2014).
[33]
VARIANTS [LARGE SCALE ANALYSIS] GLY-17; ALA-100; GLN-169; ASP-170;
TRP-306 AND ALA-496.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Tyrosine kinase that functions as cell surface receptor
for fibrillar collagen and regulates cell attachment to the
extracellular matrix, remodeling of the extracellular matrix, cell
migration, differentiation, survival and cell proliferation.
Collagen binding triggers a signaling pathway that involves SRC
and leads to the activation of MAP kinases. Regulates remodeling
of the extracellular matrix by up-regulation of the matrix
metalloproteinases MMP2, MMP7 and MMP9, and thereby facilitates
cell migration and wound healing. Required for normal blastocyst
implantation during pregnancy, for normal mammary gland
differentiation and normal lactation. Required for normal ear
morphology and normal hearing (By similarity). Promotes smooth
muscle cell migration, and thereby contributes to arterial wound
healing. Also plays a role in tumor cell invasion. Phosphorylates
PTPN11. {ECO:0000250, ECO:0000269|PubMed:12065315,
ECO:0000269|PubMed:16234985, ECO:0000269|PubMed:16337946,
ECO:0000269|PubMed:19401332, ECO:0000269|PubMed:20093046,
ECO:0000269|PubMed:20432435, ECO:0000269|PubMed:20884741,
ECO:0000269|PubMed:21044884, ECO:0000269|PubMed:9659899}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ENZYME REGULATION: Inhibited by the multi-targeted cancer drugs
imatinib and ponatinib. {ECO:0000269|PubMed:24768818}.
-!- SUBUNIT: Homodimer. Interacts (via PPxY motif) with WWC1 (via WW
domains) in a collagen-regulated manner. Forms a tripartite
complex with WWC1 and PRKCZ, but predominantly in the absence of
collagen. Interacts (tyrosine phosphorylated) with SHC1. Interacts
with SRC. Interacts with MYH9. Interacts with CDH1. Interacts with
PTPN11. Interacts with NCK2. {ECO:0000269|PubMed:16337946,
ECO:0000269|PubMed:18190796, ECO:0000269|PubMed:19401332,
ECO:0000269|PubMed:20093046, ECO:0000269|PubMed:20432435,
ECO:0000269|PubMed:22483115, ECO:0000269|PubMed:23899692,
ECO:0000269|PubMed:24509848, ECO:0000269|PubMed:9659899}.
-!- INTERACTION:
O43639:NCK2; NbExp=3; IntAct=EBI-711879, EBI-713635;
Q06124:PTPN11; NbExp=4; IntAct=EBI-711879, EBI-297779;
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
membrane protein.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Single-pass type I
membrane protein.
-!- SUBCELLULAR LOCATION: Isoform 3: Secreted {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 4: Cell membrane; Single-pass type I
membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=CAK I, DDR1b;
IsoId=Q08345-1; Sequence=Displayed;
Name=2; Synonyms=CAK II, DDR1a, Short;
IsoId=Q08345-2; Sequence=VSP_002953;
Name=3; Synonyms=DDR1d;
IsoId=Q08345-4; Sequence=VSP_036916, VSP_036917;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=4;
IsoId=Q08345-5; Sequence=VSP_038057;
Name=5;
IsoId=Q08345-6; Sequence=VSP_043582, VSP_002953;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in T-47D, MDA-MB-175 and HBL-100
breast carcinoma cells, A-431 epidermoid carcinoma cells, SW48 and
SNU-C2B colon carcinoma cells and Hs 294T melanoma cells (at
protein level). Expressed at low levels in most adult tissues and
is highest in the brain, lung, placenta and kidney. Lower levels
of expression are detected in melanocytes, heart, liver, skeletal
muscle and pancreas. Abundant in breast carcinoma cell lines. In
the colonic mucosa, expressed in epithelia but not in the
connective tissue of the lamina propria. In the thyroid gland,
expressed in the epithelium of the thyroid follicles. In pancreas,
expressed in the islets of Langerhans cells, but not in the
surrounding epithelial cells of the exocrine pancreas. In kidney,
expressed in the epithelia of the distal tubules. Not expressed in
connective tissue, endothelial cells, adipose tissue, muscle cells
or cells of hematopoietic origin. {ECO:0000269|PubMed:7845687,
ECO:0000269|PubMed:7848919, ECO:0000269|PubMed:8247543}.
-!- DOMAIN: The Gly/Pro-rich domains may be required for an unusual
geometry of interaction with ligand or substrates.
-!- PTM: Autophosphorylated in response to fibrillar collagen binding.
-!- PTM: Glycosylation of Asn-211, but apparently not of Asn-260, Asn-
371, or Asn-394, prevents autophosphorylation from occurring in
the absence of collagen. {ECO:0000269|PubMed:22483115,
ECO:0000269|PubMed:24509848}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- CAUTION: The mutant Gln-371 studied is still likely to be
glycosylated at Asn-370, but study did not include mutagenesis of
Asn-370. {ECO:0000305|PubMed:24509848}.
-!- SEQUENCE CAUTION:
Sequence=ACF47649.1; Type=Erroneous termination; Positions=287; Note=Translated as Cys.; Evidence={ECO:0000305};
Sequence=BAE06103.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/DDR1ID40280ch6p21.html";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X74979; CAA52915.1; -; mRNA.
EMBL; L11315; AAA02866.1; -; mRNA.
EMBL; Z29093; CAA82335.1; -; mRNA.
EMBL; L20817; AAA18019.1; -; mRNA.
EMBL; U48705; AAC50917.1; -; Genomic_DNA.
EMBL; X98208; CAA66871.1; -; Genomic_DNA.
EMBL; X99023; CAA66871.1; JOINED; Genomic_DNA.
EMBL; X99024; CAA66871.1; JOINED; Genomic_DNA.
EMBL; X99025; CAA66871.1; JOINED; Genomic_DNA.
EMBL; X99026; CAA66871.1; JOINED; Genomic_DNA.
EMBL; X99027; CAA66871.1; JOINED; Genomic_DNA.
EMBL; X99028; CAA66871.1; JOINED; Genomic_DNA.
EMBL; X99029; CAA66871.1; JOINED; Genomic_DNA.
EMBL; X99030; CAA66871.1; JOINED; Genomic_DNA.
EMBL; X99031; CAA66871.1; JOINED; Genomic_DNA.
EMBL; X99032; CAA66871.1; JOINED; Genomic_DNA.
EMBL; X99033; CAA66871.1; JOINED; Genomic_DNA.
EMBL; X99034; CAA66871.1; JOINED; Genomic_DNA.
EMBL; L57508; AAB05208.1; -; mRNA.
EMBL; EU826613; ACF47649.1; ALT_SEQ; mRNA.
EMBL; EU826614; ACF47650.1; -; mRNA.
EMBL; AK291621; BAF84310.1; -; mRNA.
EMBL; AK294793; BAH11886.1; -; mRNA.
EMBL; AB210021; BAE06103.1; ALT_INIT; mRNA.
EMBL; BA000025; BAB63318.1; -; Genomic_DNA.
EMBL; CR759747; CAQ06757.1; -; Genomic_DNA.
EMBL; CR759747; CAQ06756.1; -; Genomic_DNA.
EMBL; AB088102; BAC54935.1; -; Genomic_DNA.
EMBL; AB103608; BAF31270.1; -; Genomic_DNA.
EMBL; AL662854; CAI17434.1; -; Genomic_DNA.
EMBL; AL662870; CAI18441.1; -; Genomic_DNA.
EMBL; AL773541; CAI18450.1; -; Genomic_DNA.
EMBL; AL773589; CAI18450.1; JOINED; Genomic_DNA.
EMBL; AL773589; CAI18534.1; -; Genomic_DNA.
EMBL; AL773541; CAI18534.1; JOINED; Genomic_DNA.
EMBL; AL662854; CAI17433.1; -; Genomic_DNA.
EMBL; AL662870; CAI18442.1; -; Genomic_DNA.
EMBL; AL773541; CAI18451.1; -; Genomic_DNA.
EMBL; AL773589; CAI18451.1; JOINED; Genomic_DNA.
EMBL; AL773589; CAI18533.1; -; Genomic_DNA.
EMBL; AL773541; CAI18533.1; JOINED; Genomic_DNA.
EMBL; AB202100; BAE78621.1; -; Genomic_DNA.
EMBL; BX927194; CAQ09768.1; -; Genomic_DNA.
EMBL; BX927194; CAQ09767.1; -; Genomic_DNA.
EMBL; CH471081; EAX03335.1; -; Genomic_DNA.
EMBL; CH471081; EAX03338.1; -; Genomic_DNA.
EMBL; BC008716; AAH08716.1; -; mRNA.
EMBL; BC013400; AAH13400.1; -; mRNA.
EMBL; BC070070; AAH70070.1; -; mRNA.
CCDS; CCDS34385.1; -. [Q08345-1]
CCDS; CCDS4690.1; -. [Q08345-2]
CCDS; CCDS47396.1; -. [Q08345-5]
CCDS; CCDS56411.1; -. [Q08345-6]
PIR; A48280; A48280.
PIR; A49508; A49508.
RefSeq; NP_001189450.1; NM_001202521.1.
RefSeq; NP_001189451.1; NM_001202522.1.
RefSeq; NP_001189452.1; NM_001202523.1. [Q08345-6]
RefSeq; NP_001284581.1; NM_001297652.1. [Q08345-2]
RefSeq; NP_001284582.1; NM_001297653.1. [Q08345-2]
RefSeq; NP_001284583.1; NM_001297654.1. [Q08345-1]
RefSeq; NP_001945.3; NM_001954.4. [Q08345-2]
RefSeq; NP_054699.2; NM_013993.2. [Q08345-1]
RefSeq; NP_054700.2; NM_013994.2. [Q08345-5]
UniGene; Hs.631988; -.
PDB; 3ZOS; X-ray; 1.92 A; A/B=601-913.
PDB; 4AG4; X-ray; 2.80 A; A=29-367.
PDB; 4BKJ; X-ray; 1.70 A; A/B=601-913.
PDB; 4CKR; X-ray; 2.20 A; A=601-913.
PDB; 5BVK; X-ray; 2.29 A; A=595-913.
PDB; 5BVN; X-ray; 2.21 A; A=595-913.
PDB; 5BVO; X-ray; 1.98 A; A=595-913.
PDB; 5BVW; X-ray; 1.94 A; A=595-913.
PDB; 5FDP; X-ray; 2.25 A; A=601-913.
PDB; 5FDX; X-ray; 2.65 A; A/B=601-913.
PDBsum; 3ZOS; -.
PDBsum; 4AG4; -.
PDBsum; 4BKJ; -.
PDBsum; 4CKR; -.
PDBsum; 5BVK; -.
PDBsum; 5BVN; -.
PDBsum; 5BVO; -.
PDBsum; 5BVW; -.
PDBsum; 5FDP; -.
PDBsum; 5FDX; -.
ProteinModelPortal; Q08345; -.
SMR; Q08345; -.
BioGrid; 107234; 16.
CORUM; Q08345; -.
DIP; DIP-39698N; -.
IntAct; Q08345; 14.
MINT; MINT-1383336; -.
STRING; 9606.ENSP00000365759; -.
BindingDB; Q08345; -.
ChEMBL; CHEMBL5319; -.
DrugBank; DB00619; Imatinib.
GuidetoPHARMACOLOGY; 1843; -.
iPTMnet; Q08345; -.
PhosphoSitePlus; Q08345; -.
BioMuta; DDR1; -.
DMDM; 729008; -.
MaxQB; Q08345; -.
PaxDb; Q08345; -.
PeptideAtlas; Q08345; -.
PRIDE; Q08345; -.
DNASU; 780; -.
Ensembl; ENST00000259875; ENSP00000259875; ENSG00000137332. [Q08345-2]
Ensembl; ENST00000324771; ENSP00000318217; ENSG00000204580. [Q08345-1]
Ensembl; ENST00000376567; ENSP00000365751; ENSG00000204580. [Q08345-2]
Ensembl; ENST00000376568; ENSP00000365752; ENSG00000204580. [Q08345-1]
Ensembl; ENST00000376569; ENSP00000365753; ENSG00000204580. [Q08345-2]
Ensembl; ENST00000376570; ENSP00000365754; ENSG00000204580. [Q08345-2]
Ensembl; ENST00000376575; ENSP00000365759; ENSG00000204580. [Q08345-4]
Ensembl; ENST00000383377; ENSP00000372868; ENSG00000137332. [Q08345-1]
Ensembl; ENST00000400410; ENSP00000383261; ENSG00000137332. [Q08345-2]
Ensembl; ENST00000400411; ENSP00000383262; ENSG00000137332. [Q08345-2]
Ensembl; ENST00000400414; ENSP00000383265; ENSG00000137332. [Q08345-1]
Ensembl; ENST00000400486; ENSP00000383334; ENSG00000215522. [Q08345-2]
Ensembl; ENST00000400488; ENSP00000383336; ENSG00000215522. [Q08345-2]
Ensembl; ENST00000400489; ENSP00000383337; ENSG00000215522. [Q08345-2]
Ensembl; ENST00000400491; ENSP00000383338; ENSG00000215522. [Q08345-1]
Ensembl; ENST00000400492; ENSP00000383339; ENSG00000215522. [Q08345-1]
Ensembl; ENST00000412329; ENSP00000391805; ENSG00000230456. [Q08345-1]
Ensembl; ENST00000415092; ENSP00000405540; ENSG00000230456. [Q08345-2]
Ensembl; ENST00000418800; ENSP00000407699; ENSG00000204580. [Q08345-2]
Ensembl; ENST00000419412; ENSP00000416183; ENSG00000234078. [Q08345-2]
Ensembl; ENST00000421229; ENSP00000415730; ENSG00000234078. [Q08345-2]
Ensembl; ENST00000427053; ENSP00000416145; ENSG00000230456. [Q08345-2]
Ensembl; ENST00000429699; ENSP00000401397; ENSG00000234078. [Q08345-1]
Ensembl; ENST00000430933; ENSP00000397769; ENSG00000234078. [Q08345-1]
Ensembl; ENST00000449518; ENSP00000414285; ENSG00000230456. [Q08345-1]
Ensembl; ENST00000452441; ENSP00000405039; ENSG00000204580. [Q08345-1]
Ensembl; ENST00000453510; ENSP00000401208; ENSG00000230456. [Q08345-2]
Ensembl; ENST00000454612; ENSP00000406091; ENSG00000204580. [Q08345-2]
Ensembl; ENST00000454774; ENSP00000400393; ENSG00000234078. [Q08345-2]
Ensembl; ENST00000482873; ENSP00000421978; ENSG00000204580. [Q08345-4]
Ensembl; ENST00000508312; ENSP00000422442; ENSG00000204580. [Q08345-6]
Ensembl; ENST00000513240; ENSP00000427552; ENSG00000204580. [Q08345-5]
Ensembl; ENST00000548133; ENSP00000449611; ENSG00000230456. [Q08345-1]
Ensembl; ENST00000548962; ENSP00000448115; ENSG00000230456. [Q08345-6]
Ensembl; ENST00000549026; ENSP00000449238; ENSG00000215522. [Q08345-6]
Ensembl; ENST00000550384; ENSP00000447474; ENSG00000234078. [Q08345-6]
Ensembl; ENST00000550395; ENSP00000449255; ENSG00000215522. [Q08345-1]
Ensembl; ENST00000552068; ENSP00000449190; ENSG00000234078. [Q08345-1]
Ensembl; ENST00000552721; ENSP00000449307; ENSG00000137332. [Q08345-6]
Ensembl; ENST00000553015; ENSP00000448377; ENSG00000137332. [Q08345-1]
Ensembl; ENST00000617572; ENSP00000479195; ENSG00000215522. [Q08345-4]
Ensembl; ENST00000618059; ENSP00000479204; ENSG00000234078. [Q08345-4]
Ensembl; ENST00000620318; ENSP00000484588; ENSG00000137332. [Q08345-4]
Ensembl; ENST00000621544; ENSP00000484013; ENSG00000230456. [Q08345-4]
GeneID; 780; -.
KEGG; hsa:780; -.
UCSC; uc003nrq.4; human. [Q08345-1]
CTD; 780; -.
DisGeNET; 780; -.
EuPathDB; HostDB:ENSG00000204580.11; -.
GeneCards; DDR1; -.
HGNC; HGNC:2730; DDR1.
HPA; CAB010162; -.
HPA; CAB025656; -.
HPA; HPA057194; -.
MIM; 600408; gene.
neXtProt; NX_Q08345; -.
OpenTargets; ENSG00000204580; -.
PharmGKB; PA24348; -.
eggNOG; KOG1094; Eukaryota.
eggNOG; ENOG410XQAI; LUCA.
GeneTree; ENSGT00760000118818; -.
HOGENOM; HOG000043102; -.
HOVERGEN; HBG005461; -.
InParanoid; Q08345; -.
KO; K05124; -.
OrthoDB; EOG091G05Y8; -.
PhylomeDB; Q08345; -.
TreeFam; TF317840; -.
BRENDA; 2.7.10.1; 2681.
Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
SignaLink; Q08345; -.
SIGNOR; Q08345; -.
ChiTaRS; DDR1; human.
GeneWiki; DDR1; -.
GenomeRNAi; 780; -.
PMAP-CutDB; Q2L6H3; -.
PRO; PR:Q08345; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000204580; -.
CleanEx; HS_DDR1; -.
ExpressionAtlas; Q08345; baseline and differential.
Genevisible; Q08345; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005518; F:collagen binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0038062; F:protein tyrosine kinase collagen receptor activity; IDA:UniProtKB.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; TAS:ProtInc.
GO; GO:0061564; P:axon development; IEA:Ensembl.
GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; IEA:Ensembl.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IDA:UniProtKB.
GO; GO:0043583; P:ear development; IEA:Ensembl.
GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0007595; P:lactation; IEA:UniProtKB-KW.
GO; GO:0060749; P:mammary gland alveolus development; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:1990138; P:neuron projection extension; IEA:Ensembl.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IDA:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0001558; P:regulation of cell growth; IEA:Ensembl.
GO; GO:0001952; P:regulation of cell-matrix adhesion; IEA:Ensembl.
GO; GO:0010715; P:regulation of extracellular matrix disassembly; IMP:UniProtKB.
GO; GO:0014909; P:smooth muscle cell migration; IMP:UniProtKB.
GO; GO:0061302; P:smooth muscle cell-matrix adhesion; IMP:UniProtKB.
GO; GO:0044319; P:wound healing, spreading of cells; IMP:UniProtKB.
Gene3D; 2.60.120.260; -; 1.
InterPro; IPR029553; DDR1.
InterPro; IPR000421; FA58C.
InterPro; IPR008979; Galactose-bd-like.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
PANTHER; PTHR24416:SF333; PTHR24416:SF333; 1.
Pfam; PF00754; F5_F8_type_C; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00231; FA58C; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS01285; FA58C_1; 1.
PROSITE; PS01286; FA58C_2; 1.
PROSITE; PS50022; FA58C_3; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Calcium;
Cell membrane; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Kinase; Lactation; Membrane;
Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism;
Pregnancy; Receptor; Reference proteome; Secreted; Signal;
Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 913 Epithelial discoidin domain-containing
receptor 1.
/FTId=PRO_0000016742.
TOPO_DOM 21 417 Extracellular. {ECO:0000255}.
TRANSMEM 418 438 Helical. {ECO:0000255}.
TOPO_DOM 439 913 Cytoplasmic. {ECO:0000255}.
DOMAIN 31 185 F5/8 type C. {ECO:0000255|PROSITE-
ProRule:PRU00081}.
DOMAIN 610 905 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 616 624 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 192 367 DS-like domain.
MOTIF 481 484 PPxY motif.
COMPBIAS 377 415 Gly/Pro-rich.
COMPBIAS 476 601 Gly/Pro-rich.
ACT_SITE 766 766 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
METAL 211 211 Calcium 1; via carbonyl oxygen.
METAL 230 230 Calcium 1.
METAL 230 230 Calcium 2; via carbonyl oxygen.
METAL 233 233 Calcium 2.
METAL 235 235 Calcium 2; via carbonyl oxygen.
METAL 253 253 Calcium 1; via carbonyl oxygen.
METAL 255 255 Calcium 1; via carbonyl oxygen.
METAL 360 360 Calcium 2; via carbonyl oxygen.
METAL 361 361 Calcium 2.
BINDING 655 655 ATP.
MOD_RES 484 484 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:24509848}.
MOD_RES 513 513 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:24509848,
ECO:0000269|PubMed:9659899}.
MOD_RES 520 520 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:24509848}.
MOD_RES 631 631 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 740 740 Phosphotyrosine; by autocatalysis.
{ECO:0000305|PubMed:16337946}.
MOD_RES 792 792 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:24509848}.
MOD_RES 796 796 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:24509848}.
MOD_RES 797 797 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:24509848}.
CARBOHYD 211 211 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22483115,
ECO:0000269|PubMed:24509848}.
CARBOHYD 260 260 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22483115,
ECO:0000269|PubMed:24509848}.
CARBOHYD 370 370 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 371 371 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 394 394 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 31 185 {ECO:0000255|PROSITE-ProRule:PRU00081,
ECO:0000269|PubMed:22483115}.
DISULFID 74 177 {ECO:0000255|PROSITE-ProRule:PRU00081,
ECO:0000269|PubMed:22483115}.
DISULFID 303 348 {ECO:0000255|PROSITE-ProRule:PRU00081,
ECO:0000269|PubMed:22483115}.
VAR_SEQ 1 1 M -> MSLPRCCPHPLRPEGSGAM (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043582.
VAR_SEQ 190 243 GLLSYTAPVGQTMYLSEAVYLNDSTYDGHTVGGLQYGGLGQ
LADGVVGLDDFRK -> CSMGVWASWQMVWWGWMTLGRVRS
CGSGQAMTMWDGATTASPVAMWRWSLSLTG (in
isoform 3).
{ECO:0000303|PubMed:18593464}.
/FTId=VSP_036916.
VAR_SEQ 244 913 Missing (in isoform 3).
{ECO:0000303|PubMed:18593464}.
/FTId=VSP_036917.
VAR_SEQ 506 542 Missing (in isoform 2 and isoform 5).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7845687,
ECO:0000303|PubMed:7848919,
ECO:0000303|PubMed:8226977,
ECO:0000303|PubMed:8622863,
ECO:0000303|Ref.10}.
/FTId=VSP_002953.
VAR_SEQ 665 665 A -> ASFSLFS (in isoform 4).
{ECO:0000303|PubMed:7845687}.
/FTId=VSP_038057.
VARIANT 17 17 S -> G (in dbSNP:rs55901302).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041492.
VARIANT 100 100 V -> A (in dbSNP:rs34544756).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041493.
VARIANT 169 169 R -> Q (in dbSNP:rs55980643).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041494.
VARIANT 170 170 A -> D (in dbSNP:rs56231803).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041495.
VARIANT 306 306 R -> W (in dbSNP:rs56024191).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041496.
VARIANT 496 496 S -> A (in a lung squamous cell carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041497.
VARIANT 833 833 L -> V (in dbSNP:rs2524235).
{ECO:0000269|PubMed:8390675,
ECO:0000269|PubMed:8977099}.
/FTId=VAR_049716.
MUTAGEN 105 105 R->A: Inhibits collagen-induced
phosphorylation.
{ECO:0000269|PubMed:24509848}.
MUTAGEN 211 211 N->A: Phosphorylates regardless of
collagen presence, collagen addition does
not alter significantly the levels of
constitutive phosphorylation.
{ECO:0000269|PubMed:24509848}.
MUTAGEN 211 211 N->Q: Sustained phosphorylation
regardless of collagen presence, collagen
addition does not alter significantly the
levels of constitutive phosphorylation.
Located intracellularly and at the cell
surface. Displays a reduced rate of
receptor internalization, which is not
altered in the presence of collagen. Able
to bind collagen as wild-type. Exhibits
enhanced collagen-independent receptor
dimerization. Complete loss of the
collagen-independent constitutive
activation; when associated with A-655.
{ECO:0000269|PubMed:24509848}.
MUTAGEN 213 213 S->A: Phosphorylates regardless of
collagen presence, collagen addition does
not alter significantly the levels of
constitutive phosphorylation.
{ECO:0000269|PubMed:24509848}.
MUTAGEN 260 260 N->Q: Phosphorylates in response to
collagen, but at lower levels compared to
wild-type. No activation in the absence
of collagen.
{ECO:0000269|PubMed:24509848}.
MUTAGEN 371 371 N->Q: Phosphorylates in response to
collagen, but at lower levels compared to
wild-type. No activation in the absence
of collagen.
{ECO:0000269|PubMed:24509848}.
MUTAGEN 379 379 T->A: Phosphorylates in response to
collagen, but at lower levels compared to
wild-type. Phosphorylates in response to
collagen, but at lower levels compared to
wild-type; when associated with A-393.
{ECO:0000269|PubMed:24509848}.
MUTAGEN 393 393 T->A: Phosphorylates in response to
collagen, but at lower levels compared to
wild-type. Phosphorylates in response to
collagen, but at lower levels compared to
wild-type; when associated with A-379.
{ECO:0000269|PubMed:24509848}.
MUTAGEN 394 394 N->Q: Phosphorylates in response to
collagen, but at lower levels compared to
wild-type. No activation in the absence
of collagen.
{ECO:0000269|PubMed:24509848}.
MUTAGEN 655 655 K->A: Loss of kinase activity. Complete
loss of the collagen-independent
constitutive activation; when associated
with Q-211.
{ECO:0000269|PubMed:24509848}.
MUTAGEN 707 707 G->A: Confers over 20-fold resistance to
the ability of an inhibitor to inhibit
autophosphorylation.
{ECO:0000269|PubMed:23899692}.
MUTAGEN 740 740 Y->F: Abolishes interaction with PTPN11.
{ECO:0000269|PubMed:16337946}.
CONFLICT 94 94 L -> V (in Ref. 2; AAA02866 and 5;
AAC50917). {ECO:0000305}.
CONFLICT 165 165 R -> H (in Ref. 14; AAH70070).
{ECO:0000305}.
CONFLICT 285 286 VH -> MW (in Ref. 8; ACF47649).
{ECO:0000305}.
CONFLICT 741 741 P -> Q (in Ref. 14; AAH70070).
{ECO:0000305}.
CONFLICT 847 867 QLTDEQVIENAGEFFRDQGRQ -> SAHRRAGHRERGGVLP
GPGPA (in Ref. 6; CAA66871).
{ECO:0000305}.
TURN 37 39 {ECO:0000244|PDB:4AG4}.
HELIX 44 46 {ECO:0000244|PDB:4AG4}.
STRAND 47 50 {ECO:0000244|PDB:4AG4}.
HELIX 55 57 {ECO:0000244|PDB:4AG4}.
HELIX 59 61 {ECO:0000244|PDB:4AG4}.
TURN 68 70 {ECO:0000244|PDB:4AG4}.
STRAND 71 73 {ECO:0000244|PDB:4AG4}.
STRAND 87 103 {ECO:0000244|PDB:4AG4}.
HELIX 107 109 {ECO:0000244|PDB:4AG4}.
STRAND 116 127 {ECO:0000244|PDB:4AG4}.
STRAND 129 131 {ECO:0000244|PDB:4AG4}.
STRAND 145 148 {ECO:0000244|PDB:4AG4}.
STRAND 151 169 {ECO:0000244|PDB:4AG4}.
STRAND 171 173 {ECO:0000244|PDB:4AG4}.
STRAND 178 186 {ECO:0000244|PDB:4AG4}.
STRAND 191 197 {ECO:0000244|PDB:4AG4}.
STRAND 204 206 {ECO:0000244|PDB:4AG4}.
STRAND 217 220 {ECO:0000244|PDB:4AG4}.
STRAND 223 226 {ECO:0000244|PDB:4AG4}.
HELIX 230 232 {ECO:0000244|PDB:4AG4}.
STRAND 245 248 {ECO:0000244|PDB:4AG4}.
TURN 251 254 {ECO:0000244|PDB:4AG4}.
STRAND 256 259 {ECO:0000244|PDB:4AG4}.
HELIX 260 262 {ECO:0000244|PDB:4AG4}.
STRAND 266 287 {ECO:0000244|PDB:4AG4}.
HELIX 291 293 {ECO:0000244|PDB:4AG4}.
STRAND 299 306 {ECO:0000244|PDB:4AG4}.
STRAND 308 312 {ECO:0000244|PDB:4AG4}.
STRAND 314 316 {ECO:0000244|PDB:4AG4}.
STRAND 318 321 {ECO:0000244|PDB:4AG4}.
STRAND 332 351 {ECO:0000244|PDB:4AG4}.
STRAND 353 367 {ECO:0000244|PDB:4AG4}.
HELIX 607 609 {ECO:0000244|PDB:4BKJ}.
STRAND 610 619 {ECO:0000244|PDB:4BKJ}.
STRAND 622 631 {ECO:0000244|PDB:4BKJ}.
HELIX 632 634 {ECO:0000244|PDB:4BKJ}.
STRAND 637 639 {ECO:0000244|PDB:4BKJ}.
STRAND 651 657 {ECO:0000244|PDB:4BKJ}.
HELIX 663 678 {ECO:0000244|PDB:4BKJ}.
STRAND 687 691 {ECO:0000244|PDB:4BKJ}.
STRAND 693 696 {ECO:0000244|PDB:4BKJ}.
STRAND 698 702 {ECO:0000244|PDB:4BKJ}.
HELIX 709 714 {ECO:0000244|PDB:4BKJ}.
HELIX 740 759 {ECO:0000244|PDB:4BKJ}.
HELIX 769 771 {ECO:0000244|PDB:4BKJ}.
STRAND 772 774 {ECO:0000244|PDB:4BKJ}.
HELIX 776 778 {ECO:0000244|PDB:4BKJ}.
STRAND 780 782 {ECO:0000244|PDB:4BKJ}.
HELIX 790 795 {ECO:0000244|PDB:4BKJ}.
STRAND 797 800 {ECO:0000244|PDB:3ZOS}.
STRAND 803 805 {ECO:0000244|PDB:3ZOS}.
HELIX 807 809 {ECO:0000244|PDB:4BKJ}.
HELIX 812 817 {ECO:0000244|PDB:4BKJ}.
HELIX 822 837 {ECO:0000244|PDB:4BKJ}.
TURN 838 840 {ECO:0000244|PDB:4BKJ}.
TURN 844 847 {ECO:0000244|PDB:4BKJ}.
HELIX 850 862 {ECO:0000244|PDB:4BKJ}.
HELIX 878 887 {ECO:0000244|PDB:4BKJ}.
HELIX 892 894 {ECO:0000244|PDB:4BKJ}.
HELIX 898 906 {ECO:0000244|PDB:4BKJ}.
TURN 907 909 {ECO:0000244|PDB:4BKJ}.
HELIX 910 912 {ECO:0000244|PDB:4BKJ}.
SEQUENCE 913 AA; 101128 MW; C96913EA906C481E CRC64;
MGPEALSSLL LLLLVASGDA DMKGHFDPAK CRYALGMQDR TIPDSDISAS SSWSDSTAAR
HSRLESSDGD GAWCPAGSVF PKEEEYLQVD LQRLHLVALV GTQGRHAGGL GKEFSRSYRL
RYSRDGRRWM GWKDRWGQEV ISGNEDPEGV VLKDLGPPMV ARLVRFYPRA DRVMSVCLRV
ELYGCLWRDG LLSYTAPVGQ TMYLSEAVYL NDSTYDGHTV GGLQYGGLGQ LADGVVGLDD
FRKSQELRVW PGYDYVGWSN HSFSSGYVEM EFEFDRLRAF QAMQVHCNNM HTLGARLPGG
VECRFRRGPA MAWEGEPMRH NLGGNLGDPR ARAVSVPLGG RVARFLQCRF LFAGPWLLFS
EISFISDVVN NSSPALGGTF PPAPWWPPGP PPTNFSSLEL EPRGQQPVAK AEGSPTAILI
GCLVAIILLL LLIIALMLWR LHWRRLLSKA ERRVLEEELT VHLSVPGDTI LINNRPGPRE
PPPYQEPRPR GNPPHSAPCV PNGSALLLSN PAYRLLLATY ARPPRGPGPP TPAWAKPTNT
QAYSGDYMEP EKPGAPLLPP PPQNSVPHYA EADIVTLQGV TGGNTYAVPA LPPGAVGDGP
PRVDFPRSRL RFKEKLGEGQ FGEVHLCEVD SPQDLVSLDF PLNVRKGHPL LVAVKILRPD
ATKNARNDFL KEVKIMSRLK DPNIIRLLGV CVQDDPLCMI TDYMENGDLN QFLSAHQLED
KAAEGAPGDG QAAQGPTISY PMLLHVAAQI ASGMRYLATL NFVHRDLATR NCLVGENFTI
KIADFGMSRN LYAGDYYRVQ GRAVLPIRWM AWECILMGKF TTASDVWAFG VTLWEVLMLC
RAQPFGQLTD EQVIENAGEF FRDQGRQVYL SRPPACPQGL YELMLRCWSR ESEQRPPFSQ
LHRFLAEDAL NTV


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