Statements in which the resource exists as a subject.
PredicateObject
rdf:type
http://www.biopax.org/relea...
http://www.biopax.org/relea...
Growth factor receptor-bound protein 7, Growth factor receptor-bound protein 7
http://www.biopax.org/relea...
GRB7_HUMAN, GRB7_HUMAN
http://www.biopax.org/relea...
http://www.biopax.org/relea...
B47, B47, Epidermal growth factor receptor GRB-7, Epidermal growth factor receptor GRB-7, GRB7 adapter protein, GRB7 adapter protein
http://www.biopax.org/relea...
FUNCTION: 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). SUBUNIT: Homodimer. Interacts (via SH2 domain) with EGFR, ERBB2, ERBB3 (when phosphorylated), ERBB4 (when phosphorylated), EPHB1, INSR, FGFR1 and PDGFRB (when phosphorylated). Interacts with RND1. Interacts (when tyrosine phosphorylated) with FHL2 and HAX1. Interacts (via SH2 domain) with RET and FAK1. Interacts (when not phosphorylated) with ELAVL1. In stressed cells, but not in normal cells, part of a complex that contains at least GRB7, FAK1, STAU1, ELAVL1 and TIA1 (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Cell junction, focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic granule (By similarity). Cell projection. Note=Predominantly cytoplasmic. Detected in stress granules, where mRNA is stored under stress conditions (By similarity). ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=4; Comment=At least 2 isoforms are produced; Name=1; IsoId=Q14451-1; Sequence=Displayed; Name=2; Synonyms=Grb7V; IsoId=Q14451-2; Sequence=VSP_035500, VSP_035501; Name=3; IsoId=Q14451-3; Sequence=VSP_041665; Name=4; IsoId=Q14451-4; Sequence=VSP_041666; DOMAIN: The PH domain mediates interaction with membranes containing phosphoinositides. PTM: Phosphorylated on serine and threonine residues in response to heregulin. 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 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. SIMILARITY: Belongs to the GRB7/10/14 family. SIMILARITY: Contains 1 PH domain. SIMILARITY: Contains 1 Ras-associating domain. SIMILARITY: Contains 1 SH2 domain. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License., FUNCTION: 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). SUBUNIT: Homodimer. Interacts (via SH2 domain) with EGFR, ERBB2, ERBB3 (when phosphorylated), ERBB4 (when phosphorylated), EPHB1, INSR, FGFR1 and PDGFRB (when phosphorylated). Interacts with RND1. Interacts (when tyrosine phosphorylated) with FHL2 and HAX1. Interacts (via SH2 domain) with RET and FAK1. Interacts (when not phosphorylated) with ELAVL1. In stressed cells, but not in normal cells, part of a complex that contains at least GRB7, FAK1, STAU1, ELAVL1 and TIA1 (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Cell junction, focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic granule (By similarity). Cell projection. Note=Predominantly cytoplasmic. Detected in stress granules, where mRNA is stored under stress conditions (By similarity). ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=4; Comment=At least 2 isoforms are produced; Name=1; IsoId=Q14451-1; Sequence=Displayed; Name=2; Synonyms=Grb7V; IsoId=Q14451-2; Sequence=VSP_035500, VSP_035501; Name=3; IsoId=Q14451-3; Sequence=VSP_041665; Name=4; IsoId=Q14451-4; Sequence=VSP_041666; DOMAIN: The PH domain mediates interaction with membranes containing phosphoinositides. PTM: Phosphorylated on serine and threonine residues in response to heregulin. 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 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. SIMILARITY: Belongs to the GRB7/10/14 family. SIMILARITY: Contains 1 PH domain. SIMILARITY: Contains 1 Ras-associating domain. SIMILARITY: Contains 1 SH2 domain. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
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