GRB10
entrez
2887
canonical
uniprot
Q13322
canonical
ensembl
ENSG00000106070
resolver
ensp
ENSP00000338543
resolver
ensp
ENSP00000349818
resolver
ensp
ENSP00000381790
resolver
ensp
ENSP00000381793
resolver
ensp
ENSP00000385189
resolver
ensp
ENSP00000385770
resolver
ensp
ENSP00000493728
resolver
ensp
ENSP00000495341
resolver
enst
ENST00000644879
resolver
genesymbol
GRB10
resolver
genesymbol_syn
GRBIR
resolver
genesymbol_syn
KIAA0207
resolver
hgnc
HGNC:4564
resolver
uniprot
A0A2R8YCL1
resolver
uniprot
A4D258
resolver
uniprot
A7VJ95
resolver
uniprot
A8K0E6
resolver
uniprot
D3DVM9
resolver
uniprot
O00427
resolver
uniprot
O00701
resolver
uniprot
O75222
resolver
uniprot
Q92606
resolver
uniprot
Q92907
resolver
uniprot
Q92948
resolver
uniprot_entry
A0A2R8YCL1_HUMAN
resolver
uniprot_entry
GRB10_HUMAN
resolver
uniprot_sec
A4D258
resolver
uniprot_sec
A7VJ95
resolver
uniprot_sec
A8K0E6
resolver
uniprot_sec
D3DVM9
resolver
uniprot_sec
O00427
resolver
uniprot_sec
O00701
resolver
uniprot_sec
O75222
resolver
uniprot_sec
Q92606
resolver
uniprot_sec
Q92907
resolver
uniprot_sec
Q92948
resolver
activity_regulation
ACTIVITY REGULATION: Phosphorylation by mTORC1 stabilizes and activates GRB10 constituting a feedback pathway by which mTORC1 inhibits INSR-dependent signaling. {ECO:0000269|PubMed:21659604}.
uniprot
proteins
amino_acid_sequence
MALAGCPDSFLHHPYYQDKVEQTPRSQQDPAGPGLPAQSDRLANHQEDDVDLEALVNDMNASLESLYSACSMQSDTVPLLQNGQHARSQPRASGPPRSIQPQVSPRQRVQRSQPVHILAVRRLQEEDQQFRTSSLPAIPNPFPELCGPGSPPVLTPGSLPPSQAAAKQDVKVFSEDGTSKVVEILADMTARDLCQLLVYKSHCVDDNSWTLVEHHPHLGLERCLEDHELVVQVESTMASESKFLFRKNYAKYEFFKNPMNFFPEQMVTWCQQSNGSQTQLLQNFLNSSSCPEIQGFLHVKELGKKSWKKLYVCLRRSGLYCSTKGTSKEPRHLQLLADLEDSNIFSLIAGRKQYNAPTDHGLCIKPNKVRNETKELRLLCAEDEQTRTCWMTAFRLLKYGMLLYQNYRIPQQRKALLSPFSTPVRSVSENSLVAMDFSGQTGRVIENPAEAQSAALEEGHAWRKRSTRMNILGSQSPLHPSTLSTVIHRTQHWFHGRISREESHRIIKQQGLVDGLFLLRDSQSNPKAFVLTLCHHQKIKNFQILPCEDDGQTFFSLDDGNTKFSDLIQLVDFYQLNKGVLPCKLKHHCIRVAL
uniprot
proteins
function
FUNCTION: Adapter protein which modulates coupling of a number of cell surface receptor kinases with specific signaling pathways. Binds to, and suppress signals from, activated receptors tyrosine kinases, including the insulin (INSR) and insulin-like growth factor (IGF1R) receptors. The inhibitory effect can be achieved by 2 mechanisms: interference with the signaling pathway and increased receptor degradation. Delays and reduces AKT1 phosphorylation in response to insulin stimulation. Blocks association between INSR and IRS1 and IRS2 and prevents insulin-stimulated IRS1 and IRS2 tyrosine phosphorylation. Recruits NEDD4 to IGF1R, leading to IGF1R ubiquitination, increased internalization and degradation by both the proteasomal and lysosomal pathways. May play a role in mediating insulin-stimulated ubiquitination of INSR, leading to proteasomal degradation. Negatively regulates Wnt signaling by interacting with LRP6 intracellular portion and interfering with the binding of AXIN1 to LRP6. Positive regulator of the KDR/VEGFR-2 signaling pathway. May inhibit NEDD4-mediated degradation of KDR/VEGFR-2. {ECO:0000269|PubMed:12493740, ECO:0000269|PubMed:15060076, ECO:0000269|PubMed:16434550, ECO:0000269|PubMed:17376403}.
uniprot
proteins
mass_dalton
67231
uniprot
proteins
mutagenesis
MUTAGEN 104; /note="S->G: No effect on phosphorylation."; /evidence="ECO:0000269|PubMed:15952796"; MUTAGEN 134; /note="S->A: No effect on YWHAE-binding."; /evidence="ECO:0000269|PubMed:15722337"; MUTAGEN 136; /note="P->A: No effect on NEDD4-binding; when associated with A-139 and A-141."; /evidence="ECO:0000269|PubMed:15060076"; MUTAGEN 139; /note="P->A: No effect on NEDD4-binding; when associated with A-136 and A-141."; /evidence="ECO:0000269|PubMed:15060076"; MUTAGEN 141; /note="P->S: No effect on NEDD4-binding; when associated with A-136 and A-139."; /evidence="ECO:0000269|PubMed:15060076"; MUTAGEN 150; /note="S->I: Loss of phosphorylation."; /evidence="ECO:0000269|PubMed:15952796"; MUTAGEN 300; /note="K->A: 2-fold loss of inositide-binding."; /evidence="ECO:0000269|PubMed:19648926"; MUTAGEN 305; /note="K->A: 5-fold loss of inositide-binding."; /evidence="ECO:0000269|PubMed:19648926"; MUTAGEN 308; /note="K->A: 5-fold loss of inositide-binding."; /evidence="ECO:0000269|PubMed:19648926"; MUTAGEN 355; /note="N->G: 5-fold loss of inositide-binding."; /evidence="ECO:0000269|PubMed:19648926"; MUTAGEN 418; /note="S->A: No net loss of phosphorylation, this may be due to a compensatory phosphorylation of T-422 in vitro."; /evidence="ECO:0000269|PubMed:15952796"; MUTAGEN 428; /note="S->A: Impairs YWHAE-binding."; /evidence="ECO:0000269|PubMed:15722337"; MUTAGEN 476; /note="S->A: Loss of phosphorylation."; /evidence="ECO:0000269|PubMed:15952796"; MUTAGEN 520; /note="R->K: No effect on NEDD4-binding. No effect on the disruption of the interaction between INSR and IRS1 and IRS2."; /evidence="ECO:0000269|PubMed:12493740, ECO:0000269|PubMed:15060076
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on serine residues upon EGF, FGF and PDGF stimulation (By similarity). Phosphorylated at Tyr-67 by TEC. {ECO:0000250, ECO:0000269|PubMed:15722337, ECO:0000269|PubMed:15952796, ECO:0000269|PubMed:21659604, ECO:0000269|PubMed:9753425}.
uniprot
proteins
protein_family
GRB7/10/14 family
uniprot
proteins
pubmed
10856193
uniprot
proteins
pubmed
10861285
uniprot
proteins
pubmed
11527390
uniprot
proteins
pubmed
12493740
uniprot
proteins
pubmed
12551896
uniprot
proteins
pubmed
12690205
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
12853971
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15060076
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15722337
uniprot
proteins
pubmed
15952796
uniprot
proteins
pubmed
16434550
uniprot
proteins
pubmed
17376403
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19487367
uniprot
proteins
pubmed
19648926
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21659604
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
7479769
uniprot
proteins
pubmed
8798417
uniprot
proteins
pubmed
9006901
uniprot
proteins
pubmed
9039502
uniprot
proteins
pubmed
9360986
uniprot
proteins
pubmed
9553107
uniprot
proteins
pubmed
9753425
uniprot
proteins
pubmed
9881709
uniprot
proteins
sequence_length
594
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=When complexed with NEDD4 and IGF1R, follows IGF1R internalization, remaining associated with early endosomes. Uncouples from IGF1R-containing endosomes before the sorting of the receptor to the lysosomal compartment (By similarity). {ECO:0000250}.
uniprot
proteins