Aliases for PTK2 Gene
External Ids for PTK2 Gene
This gene encodes a cytoplasmic protein tyrosine kinase which is found concentrated in the focal adhesions that form between cells growing in the presence of extracellular matrix constituents. The encoded protein is a member of the FAK subfamily of protein tyrosine kinases but lacks significant sequence similarity to kinases from other subfamilies. Activation of this gene may be an important early step in cell growth and intracellular signal transduction pathways triggered in response to certain neural peptides or to cell interactions with the extracellular matrix. Several transcript variants encoding different isoforms have been found for this gene, but the full-length natures of only three of them have been determined. [provided by RefSeq, Dec 2010]
GeneCards Summary for PTK2 Gene
PTK2 (Protein Tyrosine Kinase 2) is a Protein Coding gene. Diseases associated with PTK2 include scar contracture and breast cancer. Among its related pathways are PI3K-Akt signaling pathway and Signaling by GPCR. GO annotations related to this gene include actin binding and signal transducer activity. An important paralog of this gene is TNK1.
UniProtKB/Swiss-Prot for PTK2 Gene
Non-receptor protein-tyrosine kinase that plays an essential role in regulating cell migration, adhesion, spreading, reorganization of the actin cytoskeleton, formation and disassembly of focal adhesions and cell protrusions, cell cycle progression, cell proliferation and apoptosis. Required for early embryonic development and placenta development. Required for embryonic angiogenesis, normal cardiomyocyte migration and proliferation, and normal heart development. Regulates axon growth and neuronal cell migration, axon branching and synapse formation; required for normal development of the nervous system. Plays a role in osteogenesis and differentiation of osteoblasts. Functions in integrin signal transduction, but also in signaling downstream of numerous growth factor receptors, G-protein coupled receptors (GPCR), EPHA2, netrin receptors and LDL receptors. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascade. Promotes activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling cascade. Promotes localized and transient activation of guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and thereby modulates the activity of Rho family GTPases. Signaling via CAS family members mediates activation of RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ACTN1, ARHGEF7, GRB7, RET and WASL. Promotes phosphorylation of PXN and STAT1; most likely PXN and STAT1 are phosphorylated by a SRC family kinase that is recruited to autophosphorylated PTK2/FAK1, rather than by PTK2/FAK1 itself. Promotes phosphorylation of BCAR1; GIT2 and SHC1; this requires both SRC and PTK2/FAK1. Promotes phosphorylation of BMX and PIK3R1. Isoform 6 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription.
Focal adhesion kinase (FAK), a non-receptor tyrosine kinase, is the first intracellular step in the signal transduction cascade initiated by the attachment of an integrin to the extracellular matrix at points known as focal adhesions. Therefore, FAK is plays a key role in cellular migration and motility. FAK has 3 functional domains: a focal adhesion targeting domain (FAT), a catalytic domain and a FERM domain, which mediates interactions with the cytoplasmic domains of integrins and growth factor receptors. FAK has multiple phosphorylation sites that are required for binding to adaptor proteins containing SH2 domains (e.g. Src and SH3 domains (e.g. CAS, GRAF)). Key amongst these phosphorylation sites is Tyr397, which is important for the interaction of FAK with downstream signaling molecules such as PI 3-K, PLCgamma and Rho kinase. Overexpression of FAK has been associated with several types of cancer.