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DDR1/MCK10/CD167  Protein, Antibody, ELISA Kit, cDNA Clone

Expression host: Baculovirus-Insect Cells  
10730-H20B1-50
10730-H20B1-20
50 µg 
20 µg 
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Expression host: Human Cells  
10730-H08H-50
10730-H08H-100
50 µg 
100 µg 
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Expression host: Human Cells  
50829-M02H-50
50829-M02H-100
50 µg 
100 µg 
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Expression host: Human Cells  
50829-M08H-50
50829-M08H-100
50 µg 
100 µg 
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  • Slide 1
Expression host: Baculovirus-Insect Cells  
50829-M20B1-50
50829-M20B1-20
50 µg 
20 µg 
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  • Slide 1
Expression host: Human Cells  
80440-R08H-50
80440-R08H-100
50 µg 
100 µg 
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Expression host: Human Cells  
80440-R02H-50
80440-R02H-100
50 µg 
100 µg 
Add to Cart
  • Slide 1

DDR1/MCK10/CD167 Related Area

DDR1/MCK10/CD167 Related Pathways

DDR1/MCK10/CD167 Summary & Protein Information

DDR1/MCK10/CD167 Background

Gene Summary: Receptor tyrosine kinases play a key role in the communication of cells with their microenvironment. These kinases are involved in the regulation of cell growth, differentiation and metabolism. The protein encoded by this gene belongs to a subfamily of tyrosine kinase receptors with homology to Dictyostelium discoideum protein discoidin I in their extracellular domain, and that are activated by various types of collagen. Expression of this protein is restricted to epithelial cells, particularly in the kidney, lung, gastrointestinal tract, and brain. In addition, it has been shown to be significantly overexpressed in several human tumors. Alternatively spliced transcript variants encoding different isoforms have been described for this gene.
General information above from NCBI
Catalytic activity: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-ProRule:PRU10028}.
Enzyme regulation: ENZYME REGULATION: Inhibited by the multi-targeted cancer drugs imatinib and ponatinib. {ECO:0000269|PubMed:24768818}.
Subunit structure: 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}.
Domain: The Gly/Pro-rich domains may be required for an unusual geometry of interaction with ligand or substrates.
Subcellular location: Isoform 1: Cell membrane; Single-pass type I membrane protein.; Isoform 2: Cell membrane; Single-pass type I membrane protein.; Isoform 3: Secreted {ECO:0000305}.; Isoform 4: Cell membrane; Single-pass type I membrane protein.
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}.
Post-translational: Autophosphorylated in response to fibrillar collagen binding.; 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}.
Sequence similarity: Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.; Contains 1 F5/8 type C domain. {ECO:0000255|PROSITE-ProRule:PRU00081}.; Contains 1 protein kinase domain. {ECO:0000255|PROSITE-ProRule:PRU00159}.
General information above from UniProt

Discoidin domain receptor family, member 1 (DDR1), also known as or CD167a (cluster of differentiation 167a), and Mammary carcinoma kinase 10 (MCK10), belongs to a subfamily of tyrosine kinase receptors with an extracellular domain homologous to Dictyostellium discoideum protein discoidin 1. Receptor tyrosine kinases play a key role in the communication of cells with their microenvironment. These kinases are involved in the regulation of cell growth, differentiation and metabolism. Expression of DDR1/MCK10/CD167 is restricted to epithelial cells, particularly in the kidney, lung, gastrointestinal tract, and brain. In addition, it has been shown to be significantly overexpressed in several human tumors. DDR1/MCK10/CD167 plays an important role in regulating attachment to collagen, chemotaxis, proliferation, and MMP production in smooth muscle cells. DDR1 functions in a feedforward loop to increase p53 levels and at least some of its effectors. Inhibition of DDR1 function resulted in strikingly increased apoptosis of wild-type p53-containing cells in response to genotoxic stress through a caspase-dependent pathway.

DDR1/MCK10/CD167 Alternative Name

NEP,CAK,DDR,HGK2,PTK3,RTK6,TRKE,CD167,EDDR1,MCK10,NTRK4,PTK3A, [homo-sapiens]
NEP,CAK,CD167,DAAP-278B20.1,DDR,DDR1,EDDR1,MCK10,NTRK4,PTK3,PTK3A,RTK6,TRKE, [human]
NEP,6030432F18,AI323681,Cak,CD167a,Ddr1,PTK3A, [mouse]
NEP,Cak,PTK3A,CD167a,AI323681,6030432F18, [mus-musculus]

DDR1/MCK10/CD167 Related Studies

  • Hou G, et al. (2001) The discoidin domain receptor tyrosine kinase DDR1 in arterial wound repair. J Clin Invest. 107(6): 727-35.
  • Ongusaha PP, et al. (2003) p53 induction and activation of DDR1 kinase counteract p53-mediated apoptosis and influence p53 regulation through a positive feedback loop. EMBO J. 22(6): 1289-301.
  • Jönsson M, et al. (2001) Repression of Wnt-5a impairs DDR1 phosphorylation and modifies adhesion and migration of mammary cells. J Cell Sci. 114(11): 2043-53.
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