GRB7: 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. Homodimer. Interacts (via SH2 domain) with EGFR, ERBB2, ERBB3 (when phosphorylated), ERBB4 (when phosphorylated), EPHB1, INSR, FGFR1, PDGFRA (tyrosine phosphorylated) and PDGFRB (tyrosine phosphorylated). Interacts with SHC1. Interacts with RND1. Interacts (when tyrosine phosphorylated) with FHL2 and HAX1. Interacts (via SH2 domain) with RET and PTK2/FAK1. Interacts (when not phosphorylated) with ELAVL1. In stressed cells, but not in normal cells, part of a complex that contains at least GRB7, PTK2/FAK1, STAU1, ELAVL1 and TIA1. Interacts (via SH2 domain) with KIT (phosphorylated). Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated). Belongs to the GRB7/10/14 family. 4 isoforms of the human protein are produced by alternative splicing.
Protein type: Motility/polarity/chemotaxis; Adaptor/scaffold
Chromosomal Location of Human Ortholog: 17q12
Cellular Component: cell projection; focal adhesion; stress granule; plasma membrane; cytosol
Molecular Function: identical protein binding; protein binding; SH3/SH2 adaptor activity; RNA binding; protein kinase binding; phosphoinositide binding
Biological Process: epidermal growth factor receptor signaling pathway; stress granule assembly; positive regulation of signal transduction; negative regulation of translation; blood coagulation; leukocyte migration; positive regulation of cell migration
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