Discoidin domain-containing receptor 2

Discoidin domain receptor tyrosine kinase 2
Rendering based on PDB 2WUH.
Available structures PDB 2WUH, 2Z4F
Identifiers
Symbols	DDR2; MIG20a; NTRKR3; TKT; TYRO10
External IDs	OMIM: 191311 MGI: 1345277 HomoloGene: 68505 GeneCards: DDR2 Gene
EC number	2.7.10.1
Gene Ontology Molecular function • nucleotide binding • transmembrane receptor protein tyrosine kinase activity • receptor activity • collagen binding • ATP binding Cellular component • integral to plasma membrane • membrane • apical plasma membrane Biological process • cell adhesion • signal transduction • transmembrane receptor protein tyrosine kinase signaling pathway • positive regulation of cell proliferation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	4921	18214
Ensembl	ENSG00000162733	ENSMUSG00000026674
UniProt	Q16832	Q62371
RefSeq (mRNA)	NM_001014796.1	NM_022563.2
RefSeq (protein)	NP_001014796.1	NP_072075.2
Location (UCSC)	Chr 1: 162.6 – 162.75 Mb	Chr 1: 171.9 – 172.04 Mb
PubMed search	[1]	[2]

Discoidin domain receptor family, member 2, also known as DDR2 or CD167b (cluster of differentiation 167b), is a human gene.^[1]

Receptor tyrosine kinases (RTKs) play a key role in the communication of cells with their microenvironment. These molecules are involved in the regulation of cell growth, differentiation, and metabolism. In several cases the biochemical mechanism by which RTKs transduce signals across the membrane has been shown to be ligand induced receptor oligomerization and subsequent intracellular phosphorylation. This autophosphorylation leads to phosphorylation of cytosolic targets as well as association with other molecules, which are involved in pleiotropic effects of signal transduction. RTKs have a tripartite structure with extracellular, transmembrane, and cytoplasmic regions. This gene encodes a member of a novel subclass of RTKs and contains a distinct extracellular region encompassing a factor VIII-like domain. Alternative splicing in the 5' UTR results in multiple transcript variants encoding the same protein.^[1]

Interactions

DDR2 (gene) has been shown to interact with SHC1.^[2]

References

1. ^ ^{a b} "Entrez Gene: DDR2 discoidin domain receptor family, member 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4921. 
2. ^ Ikeda, Kazuo; Wang Li-Hsien, Torres Richard, Zhao Hong, Olaso Elvira, Eng Francis J, Labrador Pablo, Klein Rudiger, Lovett David, Yancopoulos George D, Friedman Scott L, Lin Hsin Chieh (May. 2002). "Discoidin domain receptor 2 interacts with Src and Shc following its activation by type I collagen". J. Biol. Chem. (United States) 277 (21): 19206–12. doi:10.1074/jbc.M201078200. ISSN 0021-9258. PMID 11884411. 

Further reading

• Lapsys NM, Layfield R, Baker E, et al. (1993). "Chromosomal location of the human transketolase gene.". Cytogenet. Cell Genet. 61 (4): 274–5. doi:10.1159/000133421. PMID 1486804. 
• Abedinia M, Layfield R, Jones SM, et al. (1992). "Nucleotide and predicted amino acid sequence of a cDNA clone encoding part of human transketolase.". Biochem. Biophys. Res. Commun. 183 (3): 1159–66. doi:10.1016/S0006-291X(05)80312-2. PMID 1567394. 
• Edelhoff S, Sweetser DA, Disteche CM (1995). "Mapping of the NEP receptor tyrosine kinase gene to human chromosome 6p21.3 and mouse chromosome 17C.". Genomics 25 (1): 309–11. doi:10.1016/0888-7543(95)80144-B. PMID 7774938. 
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• Karn T, Holtrich U, Bräuninger A, et al. (1993). "Structure, expression and chromosomal mapping of TKT from man and mouse: a new subclass of receptor tyrosine kinases with a factor VIII-like domain.". Oncogene 8 (12): 3433–40. PMID 8247548. 
• Hillier LD, Lennon G, Becker M, et al. (1997). "Generation and analysis of 280,000 human expressed sequence tags.". Genome Res. 6 (9): 807–28. doi:10.1101/gr.6.9.807. PMID 8889549. 
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
• Vogel W, Gish GD, Alves F, Pawson T (1998). "The discoidin domain receptor tyrosine kinases are activated by collagen.". Mol. Cell 1 (1): 13–23. doi:10.1016/S1097-2765(00)80003-9. PMID 9659899. 
• Mohan RR, Mohan RR, Wilson SE (2001). "Discoidin domain receptor (DDR) 1 and 2: collagen-activated tyrosine kinase receptors in the cornea.". Exp. Eye Res. 72 (1): 87–92. doi:10.1006/exer.2000.0932. PMID 11133186. 
• Ikeda K, Wang LH, Torres R, et al. (2002). "Discoidin domain receptor 2 interacts with Src and Shc following its activation by type I collagen.". J. Biol. Chem. 277 (21): 19206–12. doi:10.1074/jbc.M201078200. PMID 11884411. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Faraci E, Eck M, Gerstmayer B, et al. (2004). "An extracellular matrix-specific microarray allowed the identification of target genes downstream of discoidin domain receptors.". Matrix Biol. 22 (4): 373–81. doi:10.1016/S0945-053X(03)00053-2. PMID 12935821. 
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
• Ferri N, Carragher NO, Raines EW (2004). "Role of discoidin domain receptors 1 and 2 in human smooth muscle cell-mediated collagen remodeling: potential implications in atherosclerosis and lymphangioleiomyomatosis.". Am. J. Pathol. 164 (5): 1575–85. PMC 1615659. PMID 15111304. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1615659. 
• Leitinger B, Steplewski A, Fertala A (2005). "The D2 period of collagen II contains a specific binding site for the human discoidin domain receptor, DDR2.". J. Mol. Biol. 344 (4): 993–1003. doi:10.1016/j.jmb.2004.09.089. PMID 15544808. 
• Wall SJ, Werner E, Werb Z, DeClerck YA (2006). "Discoidin domain receptor 2 mediates tumor cell cycle arrest induced by fibrillar collagen.". J. Biol. Chem. 280 (48): 40187–94. doi:10.1074/jbc.M508226200. PMC 2768768. PMID 16186104. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2768768. 
• Yang K, Kim JH, Kim HJ, et al. (2006). "Tyrosine 740 phosphorylation of discoidin domain receptor 2 by Src stimulates intramolecular autophosphorylation and Shc signaling complex formation.". J. Biol. Chem. 280 (47): 39058–66. doi:10.1074/jbc.M506921200. PMID 16186108. 
• Leitinger B, Kwan AP (2007). "The discoidin domain receptor DDR2 is a receptor for type X collagen.". Matrix Biol. 25 (6): 355–64. doi:10.1016/j.matbio.2006.05.006. PMID 16806867. 
• Zhang W, Ding T, Zhang J, et al. (2007). "Expression of discoidin domain receptor 2 (DDR2) extracellular domain in pichia pastoris and functional analysis in synovial fibroblasts and NIT3T3 cells.". Mol. Cell. Biochem. 290 (1-2): 43–53. doi:10.1007/s11010-006-9136-4. PMID 16967187. 
• Ford CE, Lau SK, Zhu CQ, et al. (2007). "Expression and mutation analysis of the discoidin domain receptors 1 and 2 in non-small cell lung carcinoma.". Br. J. Cancer 96 (5): 808–14. doi:10.1038/sj.bjc.6603614. PMC 2360060. PMID 17299390. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2360060. 
• Xu L, Servais J, Li Y, et al. (2010). "Attenuation of Osteoarthritis Progression by Reduction of Discoidin Domain Receptor 2 in Mice". Arthritis & Rheumatism 62 (9): 2736–2744. doi:10.1002/art.27582. PMID 20518074. 

EPH receptor family

EPHA1 · EPHA2 · EPHA3 · EPHA4 · EPHA5 · EPHA6 · EPHA7 · EPHA8 · EPHB1 · EPHB2 · EPHB3 · EPHB4 · EPHB5 · EPHB6 · EPHX

LTK receptor family

LTK · ALK

TIE receptor family

TIE · TEK

ROR receptor family

ROR1 · ROR2

DDR receptor family

DDR1 · DDR2

PTK7 receptor family

PTK7

RYK receptor family

RYK

MuSK receptor family

MUSK

ROS receptor family

ROS1

AATYK receptor family

AATYK · AATYK2 · AATYK3

AXL receptor family

AXL · MER · TYRO3

RET receptor family

RET

uncatagorised

STYK1

Non-receptor tyrosine kinases (EC 2.7.10.2)
ABL family ABL1 · ARG ACK family ACK1 · TNK1 CSK family CSK · MATK FAK family FAK · PYK2 FES family FES · FER FRK family FRK · BRK · SRMS JAK family JAK1 · JAK2 · JAK3 · TYK2 SRC-A family SRC · FGR · FYN · YES1 SRC-B family BLK · HCK · LCK · LYN TEC family TEC · BMX · BTK · ITK · TXK SYK family SYK · ZAP70

B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6