Frs2
entrez
327826
canonical
uniprot
Q8C180
canonical
ensembl
ENSMUSG00000020170
resolver
ensp
ENSMUSP00000020381
resolver
ensp
ENSMUSP00000171856
resolver
ensp
ENSMUSP00000171857
resolver
ensp
ENSMUSP00000171858
resolver
ensp
ENSMUSP00000171859
resolver
ensp
ENSMUSP00000171860
resolver
ensp
ENSMUSP00000171863
resolver
ensp
ENSMUSP00000171864
resolver
ensp
ENSMUSP00000171865
resolver
ensp
ENSMUSP00000171866
resolver
enst
ENSMUST00000020381
resolver
genesymbol
Frs2
resolver
genesymbol_syn
Frs2a
resolver
uniprot_entry
FRS2_MOUSE
resolver
amino_acid_sequence
MGSCCSCPDKDTVPDNHRNKFKVINVDDDGNELGSGVMELTDTELILYTRKRDSVKWHYLCLRRYGYDSNLFSFESGRRCQTGQGIFAFKCARAEELFNMLQEIMQNNSINVVEEPVVERSSHQTELEVPRTPRTPTTPGLGAQNLPNGYPRYPSFGDASSHPSSRHPSVGSARLPSVGEESTHPLLVAEEQVHTYVNTTGVQEERKNRASVHVPPEARVSNAESNTPKEEPSNPEDRDPQVLLKPEGVRFVLGPTPVQKQLMEKEKLEQLGKDPVSGSGAGNTEWDTGYDSDERRDVPPVNKLVYENINGLSIPSASGVRRGRLTSTSTSDTQNINNSAQRRPALLNYENLPSLPPVWEARKLSRDEDDNLGPKTPSLNGYHNNLDPMHNYVNTENVTVPASAHKIDYSKRRDCTPTVFNFDIRRPSLEHRQLNYIQVDLEGGSDSDNPQTPKTPTTPLPQTPTRRTELYAVIDIERTAAMSNLQKALPRDDGTSRKTRHNSTDLPM
uniprot
proteins
function
FUNCTION: Adapter protein that links activated FGR and NGF receptors to downstream signaling pathways. Plays an important role in the activation of MAP kinases and in the phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, in response to ligand-mediated activation of FGFR1. Modulates signaling via SHC1 by competing for a common binding site on NTRK1. {ECO:0000269|PubMed:11353842, ECO:0000269|PubMed:11390647, ECO:0000269|PubMed:12181353, ECO:0000269|PubMed:9182757, ECO:0000269|PubMed:9632781}.
uniprot
proteins
mass_dalton
56794
uniprot
proteins
mutagenesis
MUTAGEN 2; /note="G->A: Abolishes myristoylation and membrane association."; /evidence="ECO:0000269|PubMed:9182757"; MUTAGEN 196; /note="Y->F: Abolishes tyrosine phosphorylation and interactions with GRB2 and PTPN11; when associated with F-306; F-349; F-392 and F-436."; /evidence="ECO:0000269|PubMed:9182757"; MUTAGEN 306; /note="Y->F: Abolishes tyrosine phosphorylation and interactions with GRB2 and PTPN11; when associated with F-196; F-349; F-392 and F-436."; /evidence="ECO:0000269|PubMed:9182757"; MUTAGEN 349; /note="Y->F: Abolishes tyrosine phosphorylation and interactions with GRB2 and PTPN11; when associated with F-196; F-306; F-392 and F-436."; /evidence="ECO:0000269|PubMed:9182757"; MUTAGEN 392; /note="Y->F: Abolishes tyrosine phosphorylation and interactions with GRB2 and PTPN11; when associated with F-196; F-306; F-349 and F-436."; /evidence="ECO:0000269|PubMed:9182757"; MUTAGEN 436; /note="Y->F: Abolishes tyrosine phosphorylation and interactions with GRB2 and PTPN11; when associated with F-196; F-306; F-349 and F-392."; /evidence="ECO:0000269|PubMed:9632781
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on tyrosine residues upon stimulation by FGF2 or NGFB. Phosphorylated by ULK2 (in vitro). Phosphorylated on tyrosine residues by activated ALK and FGFR1. Phosphorylated on tyrosine residues upon activation of FGFR2 and FGFR3. Phosphorylated on threonine residues by MAP kinases; this inhibits tyrosine phosphorylation, and thereby down-regulates FRS2-mediated activation of MAP kinases.; PTM: Ubiquitinated when tyrosine phosphorylated and in a complex with GRB2. The unphosphorylated form is not subject to ubiquitination. {ECO:0000269|PubMed:11997436}.
uniprot
proteins
pubmed
10629055
uniprot
proteins
pubmed
10851026
uniprot
proteins
pubmed
11353842
uniprot
proteins
pubmed
11390647
uniprot
proteins
pubmed
11433297
uniprot
proteins
pubmed
11997436
uniprot
proteins
pubmed
12181353
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16887332
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
18452557
uniprot
proteins
pubmed
19131326
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
20094046
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
8780727
uniprot
proteins
pubmed
9182757
uniprot
proteins
pubmed
9632781
uniprot
proteins
sequence_length
508
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:8780727}; Lipid-anchor {ECO:0000269|PubMed:8780727}.
uniprot
proteins