GRB7
entrez
2886
canonical
uniprot
Q14451
canonical
ensembl
ENSG00000141738
resolver
ensp
ENSP00000310771
resolver
ensp
ENSP00000377754
resolver
ensp
ENSP00000377759
resolver
ensp
ENSP00000377761
resolver
ensp
ENSP00000403459
resolver
ensp
ENSP00000593485
resolver
genesymbol
GRB7
resolver
hgnc
HGNC:4567
resolver
uniprot
A0A0S2Z4F6
resolver
uniprot
B2RAV1
resolver
uniprot
B3KNL0
resolver
uniprot
B3KWP9
resolver
uniprot
B7WP75
resolver
uniprot
J3KQM4
resolver
uniprot
Q53YD3
resolver
uniprot
Q92568
resolver
uniprot
Q96DF9
resolver
uniprot
Q9Y220
resolver
uniprot_entry
A0A0S2Z4F6_HUMAN
resolver
uniprot_entry
GRB7_HUMAN
resolver
uniprot_sec
B2RAV1
resolver
uniprot_sec
B3KNL0
resolver
uniprot_sec
B3KWP9
resolver
uniprot_sec
B7WP75
resolver
uniprot_sec
J3KQM4
resolver
uniprot_sec
Q53YD3
resolver
uniprot_sec
Q92568
resolver
uniprot_sec
Q96DF9
resolver
uniprot_sec
Q9Y220
resolver
amino_acid_sequence
MELDLSPPHLSSSPEDLCPAPGTPPGTPRPPDTPLPEEVKRSQPLLIPTTGRKLREEERRATSLPSIPNPFPELCSPPSQSPILGGPSSARGLLPRDASRPHVVKVYSEDGACRSVEVAAGATARHVCEMLVQRAHALSDETWGLVECHPHLALERGLEDHESVVEVQAAWPVGGDSRFVFRKNFAKYELFKSSPHSLFPEKMVSSCLDAHTGISHEDLIQNFLNAGSFPEIQGFLQLRGSGRKLWKRFFCFLRRSGLYYSTKGTSKDPRHLQYVADVNESNVYVVTQGRKLYGMPTDFGFCVKPNKLRNGHKGLRIFCSEDEQSRTCWLAAFRLFKYGVQLYKNYQQAQSRHLHPSCLGSPPLRSASDNTLVAMDFSGHAGRVIENPREALSVALEEAQAWRKKTNHRLSLPMPASGTSLSAAIHRTQLWFHGRISREESQRLIGQQGLVDGLFLVRESQRNPQGFVLSLCHLQKVKHYLILPSEEEGRLYFSMDDGQTRFTDLLQLVEFHQLNRGILPCLLRHCCTRVAL
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. 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). {ECO:0000250, ECO:0000269|PubMed:10893408, ECO:0000269|PubMed:12021278, ECO:0000269|PubMed:12223469, ECO:0000269|PubMed:20622016}.
uniprot
proteins
mass_dalton
59681
uniprot
proteins
mutagenesis
MUTAGEN 188; /note="Y->F: Abolishes Ras activity increase and ERK1/2 phosphorylation."; /evidence="ECO:0000269|PubMed:20622016"; MUTAGEN 239; /note="R->L: Abolishes phosphoinositide binding."; /evidence="ECO:0000269|PubMed:12021278"; MUTAGEN 259; /note="Y->F: Global loss of tyrosine phosphorylation. Abolishes interaction with FHL2 and HAX1."; /evidence="ECO:0000269|PubMed:18853468, ECO:0000269|PubMed:20665473"; MUTAGEN 260; /note="Y->F: Global loss of tyrosine phosphorylation. Abolishes interaction with FHL2 and HAX1."; /evidence="ECO:0000269|PubMed:18853468, ECO:0000269|PubMed:20665473"; MUTAGEN 284; /note="Y->F: Global loss of tyrosine phosphorylation. Abolishes interaction with FHL2 and HAX1."; /evidence="ECO:0000269|PubMed:18853468, ECO:0000269|PubMed:20665473"; MUTAGEN 338; /note="Y->F: Abolishes Ras activity increase and ERK1/2 phosphorylation."; /evidence="ECO:0000269|PubMed:20622016"; MUTAGEN 458; /note="R->L: Impairs phosphotyrosine binding by SH2 domain."; MUTAGEN 480; /note="Y->F: Global loss of tyrosine phosphorylation. Abolishes interaction with FHL2 and HAX1."; /evidence="ECO:0000269|PubMed:18853468, ECO:0000269|PubMed:20665473"; MUTAGEN 492; /note="Y->F: Global loss of tyrosine phosphorylation. Abolishes interaction with FHL2 and HAX1."; /evidence="ECO:0000269|PubMed:18853468, ECO:0000269|PubMed:20665473"; MUTAGEN 511; /note="F->R: Abolishes dimerization. Abolishes activation of HRAS."; /evidence="ECO:0000269|PubMed:15841400
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000250, ECO:0000269|PubMed:10893408, ECO:0000269|PubMed:12223469, ECO:0000269|PubMed:19473962, ECO:0000269|PubMed:20622016}.
uniprot
proteins
protein_family
GRB7/10/14 family
uniprot
proteins
pubmed
10664463
uniprot
proteins
pubmed
10803466
uniprot
proteins
pubmed
10893408
uniprot
proteins
pubmed
12021278
uniprot
proteins
pubmed
12223469
uniprot
proteins
pubmed
12975581
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15526160
uniprot
proteins
pubmed
15841400
uniprot
proteins
pubmed
16129412
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
17894853
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18853468
uniprot
proteins
pubmed
19473962
uniprot
proteins
pubmed
20622016
uniprot
proteins
pubmed
20665473
uniprot
proteins
pubmed
8988034
uniprot
proteins
pubmed
9125150
uniprot
proteins
pubmed
9516479
uniprot
proteins
pubmed
9710451
uniprot
proteins
sequence_length
532
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10893408, ECO:0000269|PubMed:12021278, ECO:0000269|PubMed:18853468}. Cell junction, focal adhesion {ECO:0000269|PubMed:10893408, ECO:0000269|PubMed:12021278}. Cell membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:10893408, ECO:0000269|PubMed:12021278, ECO:0000269|PubMed:18853468}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q03160}. Cell projection {ECO:0000269|PubMed:18853468}. Note=Predominantly cytoplasmic. Detected in stress granules, where mRNA is stored under stress conditions. {ECO:0000250|UniProtKB:Q03160}.
uniprot
proteins