| receptor protein-tyrosine kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifiers | |||||||||
| EC no. | 2.7.10.1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Symbol | Pkinase_Tyr | ||||||||
| Pfam | PF07714 | ||||||||
| OPM superfamily | 186 | ||||||||
| OPM protein | 2k1k | ||||||||
| Membranome | 3 | ||||||||
| |||||||||
Receptor tyrosine kinases (RTKs) are the high-affinity cell surface receptors for many polypeptide growth factors, cytokines, and hormones. Of the 90 unique tyrosine kinase genes identified in the human genome, 58 encode receptor tyrosine kinase proteins.[1] Receptor tyrosine kinases have been shown not only to be key regulators of normal cellular processes but also to have a critical role in the development and progression of many types of cancer.[2] Mutations in receptor tyrosine kinases lead to activation of a series of signalling cascades which have numerous effects on protein expression.[3] The receptors are generally activated by dimerization and substrate presentation. Receptor tyrosine kinases are part of the larger family of protein tyrosine kinases, encompassing the receptor tyrosine kinase proteins which contain a transmembrane domain, as well as the non-receptor tyrosine kinases which do not possess transmembrane domains.[4]
- ^ Robinson DR, Wu YM, Lin SF (November 2000). "The protein tyrosine kinase family of the human genome". Oncogene. 19 (49): 5548–57. doi:10.1038/sj.onc.1203957. PMID 11114734.
- ^ Zwick E, Bange J, Ullrich A (September 2001). "Receptor tyrosine kinase signalling as a target for cancer intervention strategies". Endocrine-Related Cancer. 8 (3): 161–73. doi:10.1677/erc.0.0080161. PMID 11566607.
- ^ Cite error: The named reference
:0was invoked but never defined (see the help page). - ^ Hubbard SR, Till JH (2000). "Protein tyrosine kinase structure and function". Annual Review of Biochemistry. 69: 373–98. doi:10.1146/annurev.biochem.69.1.373. PMID 10966463.