FAK Antibody (YA5276)

Cell junction, focal adhesion; Cell membrane; Peripheral membrane protein; Cytoplasmic side; Cytoplasm, perinuclear region; Cytoplasm, cell cortex; Cytoplasm, cytoskeleton; Cytoplasm, cytoskeleton, microtubule organizing center, centrosome; Nucleus; Cytoplasm, cytoskeleton, cilium basal body; Cytoplasm

Tissue_specificity:Detectable in both B cells and T lymphocytes. Isomers 1 and 6 are detectable in lung fibroblasts (protein level) . Widely present. Expressed in epithelial cells (protein level) (PubMed:31630787)

Q05397 has 7 isomers: Q05397-1: 119233 Da (predicted); Q05397-2: 99358 Da (predicted); Q05397-3: 63201 Da (predicted); Q05397-4: 48967 Da (predicted); Q05397-5: 120900 Da (predicted); Q05397-6: 39874 Da (predicted); Q05397-7: 114253 Da (predicted).
Phosphorylated on tyrosine residues upon activation, e.g. upon integrin signaling. Tyr-397 is the major autophosphorylation site, but other kinases can also phosphorylate this residue. Phosphorylation at Tyr-397 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-576, Tyr-577 and at additional tyrosine residues. FGR promotes phosphorylation at Tyr-397 and Tyr-576. FER promotes phosphorylation at Tyr-577, Tyr-861 and Tyr-925, even when cells are not adherent. Tyr-397, Tyr-576 and Ser-722 are phosphorylated only when cells are adherent. Phosphorylation at Tyr-397 is important for interaction with BMX, PIK3R1 and SHC1. Phosphorylation at Tyr-925 is important for interaction with GRB2. Dephosphorylated by PTPN11; PTPN11 is recruited to PTK2 via EPHA2 (tyrosine phosphorylated). Microtubule-induced dephosphorylation at Tyr-397 is crucial for the induction of focal adhesion disassembly; this dephosphorylation could be catalyzed by PTPN11 and regulated by ZFYVE21. Phosphorylation on tyrosine residues is enhanced by NTN1 (By similarity);Sumoylated; this enhances autophosphorylation

Interacts (via first Pro-rich region) with CAS family members (via SH3 domain), including BCAR1, BCAR3, and CASS4. Interacts with NEDD9 (via SH3 domain) (PubMed:9360983). Interacts with GIT1. Interacts with SORBS1. Interacts with ARHGEF28. Interacts with SHB. Part of a complex composed of THSD1, PTK2/FAK1, TLN1 and VCL (PubMed:29069646). Interacts with PXN and TLN1. Interacts with STAT1. Interacts with DCC. Interacts with WASL. Interacts with ARHGEF7. Interacts with GRB2 and GRB7 (By similarity). Component of a complex that contains at least FER, CTTN and PTK2/FAK1. Interacts with BMX. Interacts with TGFB1I1. Interacts with STEAP4. Interacts with ZFYVE21. Interacts with ESR1. Interacts with PIK3R1 or PIK3R2. Interacts with SRC, FGR, FLT4 and RET. Interacts with EPHA2 in resting cells; activation of EPHA2 recruits PTPN11, leading to dephosphorylation of PTK2/FAK1 and dissociation of the complex. Interacts with EPHA1 (kinase activity-dependent). Interacts with CD4; this interaction requires the presence of HIV-1 gp120. Interacts with PIAS1. Interacts with ARHGAP26 and SHC1. Interacts with RB1CC1; this inhibits PTK2/FAK1 activity and activation of downstream signaling pathways. Interacts with P53/TP53 and MDM2. Interacts with LPXN (via LD motif 3). Interacts with MISP. Interacts with CIB1 isoform 2. Interacts with CD36. Interacts with EMP2; regulates PTK2 activation and localization (PubMed:19494199). Interacts with DSCAM (By similarity). Interacts with AMBRA1 (By similarity). Interacts (when tyrosine-phosphorylated) with tensin TNS1; the interaction is increased by phosphorylation of TNS1 (PubMed:20798394)

Q05397

FADK 1; FADK; FAK 1; FAK 1; FAK related non kinase polypeptide; FAK1; FAK1_HUMAN; Focal adhesion kinase 1; Focal adhesion kinase 1; Focal adhesion Kinase; Focal adhesion kinase isoform FAK Del33; Focal adhesion kinase related nonkinase; FRNK; p125FAK; pp125FAK; pp125FAK; PPP1R71; Protein phosphatase 1 regulatory subunit 71; Protein tyrosine kinase 2; Protein Tyrosine Kinase Cytoplasmic; Protein Tyrosine Kinase Cytoplasmic; Protein-tyrosine kinase 2; PTK 2; PTK 2; PTK2; PTK2 protein tyrosine kinase 2; PTK2 protein tyrosine kinase 2.