Grb7
entrez
14786
canonical
uniprot
Q03160
canonical
ensembl
ENSMUSG00000019312
resolver
ensp
ENSMUSP00000019456
resolver
ensp
ENSMUSP00000161169
resolver
enst
ENSMUST00000019456
resolver
genesymbol
Grb7
resolver
uniprot
Q3TH55
resolver
uniprot_entry
GRB7_MOUSE
resolver
uniprot_sec
Q3TH55
resolver
amino_acid_sequence
MELDLSPTHLSSSPEDVCPTPATPPETPPPPDNPPPGDVKRSQPLPIPSSRKLREEEFQATSLPSIPNPFPELCSPPSQKPILGGSSGARGLLPRDSSRLCVVKVYSEDGACRSVEVAAGATARHVCEMLVQRAHALSDESWGLVESHPYLALERGLEDHEFVVEVQEAWPVGGDSRFIFRKNFAKYELFKSPPHTLFPEKMVSSCLDAQTGISHEDLIQNFLNAGSFPEIQGFLQLRGSGRGSGRKLWKRFFCFLRRSGLYYSTKGTSKDPRHLQYVADVNESNVYVVTQGRKLYGMPTDFGFCVKPNKLRNGHKGLHIFCSEDEQSRTCWLAAFRLFKYGVQLYKNYQQAQSRHLRLSYLGSPPLRSVSDNTLVAMDFSGHAGRVIDNPREALSAAMEEAQAWRKKTNHRLSLPTTCSGSSLSAAIHRTQPWFHGRISREESQRLIGQQGLVDGVFLVRESQRNPQGFVLSLCHLQKVKHYLILPSEDEGCLYFSMDEGQTRFTDLLQLVEFHQLNRGILPCLLRHCCARVAL
uniprot
proteins
function
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 (By similarity). 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. {ECO:0000250, ECO:0000269|PubMed:17318180, ECO:0000269|PubMed:18273060}.
uniprot
proteins
mass_dalton
59959
uniprot
proteins
mutagenesis
MUTAGEN 262; /note="Y->F: Abolishes interaction with FHL2."; MUTAGEN 263; /note="Y->F: Abolishes interaction with FHL2."; MUTAGEN 287; /note="Y->F: Abolishes interaction with FHL2."; MUTAGEN 483; /note="Y->F: Strongly reduced tyrosine phosphorylation. Abolishes interaction with FHL2."; /evidence="ECO:0000269|PubMed:17318180"; MUTAGEN 495; /note="Y->F: Strongly reduced tyrosine phosphorylation. Abolishes interaction with FHL2."; /evidence="ECO:0000269|PubMed:17318180
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on serine and threonine residues in response to activation of receptor kinases. Phosphorylated on tyrosine residues by TEK/TIE2. 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 (By similarity). Phosphorylated on tyrosine residues in response to NTN1 signaling. Phosphorylation promotes stress granule disassembly during recovery after cellular stress. {ECO:0000250, ECO:0000269|PubMed:10521483, ECO:0000269|PubMed:17318180, ECO:0000269|PubMed:18273060}.
uniprot
proteins
protein_family
GRB7/10/14 family
uniprot
proteins
pubmed
10377264
uniprot
proteins
pubmed
10521483
uniprot
proteins
pubmed
1409582
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
17318180
uniprot
proteins
pubmed
18273060
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
8631863
uniprot
proteins
pubmed
8940081
uniprot
proteins
sequence_length
535
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18273060}. Cell projection {ECO:0000250|UniProtKB:Q14451}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q14451}. Cell membrane {ECO:0000250|UniProtKB:Q14451}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14451}; Cytoplasmic side {ECO:0000250|UniProtKB:Q14451}. Cytoplasmic granule {ECO:0000269|PubMed:18273060}. Note=Predominantly cytoplasmic. Detected in stress granules where mRNA is stored under stress conditions. {ECO:0000269|PubMed:18273060}.
uniprot
proteins