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. Belongs to the protein kinase superfamily. Tyr protein kinase family. FAK subfamily. Detected in B and T-lymphocytes. Isoform 1 and isoform 6 are detected in lung fibroblasts (at protein level). Ubiquitous. 7 human isoforms generated by alternative promoter usage or alternative splicing have been reported. Note: This description may include information from UniProtKB.
Protein type: EC 220.127.116.11; Fak family; Kinase, protein; Protein kinase, TK; Protein kinase, tyrosine (non-receptor); TK group
Cellular Component: cell; cytoplasm; dendritic spine; focal adhesion; microtubule organizing center; nucleus; perinuclear region of cytoplasm; sarcolemma
Molecular Function: ATP binding; calcium-dependent cysteine-type endopeptidase activity; identical protein binding; non-membrane spanning protein tyrosine kinase activity; protease binding; protein binding; protein tyrosine kinase activity
Biological Process: actin filament organization; angiogenesis; angiogenesis involved in wound healing; cell differentiation; epidermal growth factor receptor signaling pathway; negative regulation of anoikis; negative regulation of cell-substrate adhesion; negative regulation of protein autophosphorylation; peptidyl-tyrosine autophosphorylation; positive regulation of cell proliferation; positive regulation of focal adhesion assembly; positive regulation of protein binding; positive regulation of protein tyrosine kinase activity; positive regulation of substrate-dependent cell migration, cell attachment to substrate; protein autophosphorylation; proteolysis; pyramidal neuron migration; regulation of cell adhesion; regulation of cell proliferation; response to muscle stretch; response to pH; signal complex assembly; wound healing, spreading of cells