GRB7

The PH domain mediates interaction with membranes containing phosphoinositides.

Adapter protein that interacts with the cytoplasmic domain of numerous receptor kinases and modulates down-stream signaling. Promotes activation of down-stream protein kinases, including STAT3, AKT1, MAPK1 and/or MAPK3. Promotes activation of HRAS. Plays a role in signal transduction in response to EGF. Plays a role in the regulation of cell proliferation and cell migration. Plays a role in the assembly and stability of RNA stress granules. Binds to the 5'UTR of target mRNA molecules and represses translation of target mRNA species, when not phosphorylated. Phosphorylation impairs RNA binding and promotes stress granule disassembly during recovery after cellular stress (By similarity).

Phosphorylated on serine and threonine residues in response to heregulin. Phosphorylated on tyrosine residues by TEK/TIE2. Phosphorylated on tyrosine residues in response to NTN1 signaling. Phosphorylation promotes stress granule disassembly during recovery after cellular stress (By similarity). Phosphorylated on tyrosine residues by PTK2/FAK1, and possibly also other kinases. Phosphorylation is enhanced by activation of receptor kinases. Tyrosine phosphorylation is essential for activation of down-stream protein kinases.

Belongs to the GRB7/10/14 family.

• Cytoplasm
• Cell junction
• Focal adhesion
• Cell membrane
• Peripheral membrane protein
• Cytoplasmic side
• Cytoplasmic granule
• Cell projection
• Predominantly cytoplasmic. Detected in stress granules, where mRNA is stored under stress conditions.

Growth factor receptor-bound protein 7, B47, Epidermal growth factor receptor GRB-7, GRB7 adapter protein, GRB7

• entrezGene:2886
• omim:601522
• swissprot:Q14451

Proteins

Oncology

59681Da