Q9Z1S8
uniprot
Q9Z1S8
canonical
amino_acid_sequence
MSGGGGDDVVCTGWLRKSPPEKKLRRYAWKKRWFILRSGRMSGDPDVLEYYKNEHSKKPLRIINLNLCEQVDAGLTFNKKELQDSFVFDIKTSERTFYLVAETEADMNKWVQSICQICGFNQAEESTDSLRNLSSASHGPRSSPAEFSSSQHLLRERKSSAPSHSSQPTLFTFEPPVSSHMQPTLSTSAPQEYLYLHQCISRRTENARSASFSQGTRQKSDTAVQKLAQSNGHCINGVGGQVHGFYSLPKPSRHNTEFKDSTYDLPRSLASHGHTKSSLTGSETDNEDVYTFKMPSNTLCRELGDLLVDNMDVPTTPLSAYQIPRTFTLDKNHNAMTVATPGDSAIAPPPRPPKPSQAETSQWGSIQQRPPISENSRSVAATIPRRNTLPAMDNSRLHRASSCETYEYPARGSGESASWSAEPPGKTAVGRSNSASSDDNYVPMNPGSSTLLAMERPGDNSQSVYIPMSPGPHHFDPLGYPSTALPIHRGPSRGSEIQPPPVNRNLKPDRKAKPTPLDLRNNTVIDELPFKSPVTKSWSRINHTFNSSSSQYCRPISTQSITSTDSGDSEENYVPMQNPVSASPVPSGTNSPAPKKSTGSVDYLALDFQPGSPSPHRKPSTSSVTSDEKVDYVQVDKEKTQALQNTMQEWTDVRQSSEPSKGAKL
uniprot
proteins
function
FUNCTION: Adapter protein which acts downstream of several membrane receptors including cytokine, antigen, hormone, cell matrix and growth factor receptors to regulate multiple signaling pathways. Regulates osteoclast differentiation mediating the TNFRSF11A/RANK signaling (PubMed:15750601). In allergic response, it plays a role in mast cells activation and degranulation through PI-3-kinase regulation. Also involved in the regulation of cell proliferation and hematopoiesis. {ECO:0000269|PubMed:10068651, ECO:0000269|PubMed:11449275, ECO:0000269|PubMed:15750601, ECO:0000269|PubMed:17374739, ECO:0000269|PubMed:9885561}.
uniprot
proteins
mass_dalton
73208
uniprot
proteins
mutagenesis
MUTAGEN 32; /note="R->C: Impairs EGF-induced phosphorylation at S-211 and T-388 and binding to phosphatidylinositol 3,4,5-trisphosphate and phosphatidylinositol 3,4-bisphosphate."; /evidence="ECO:0000269|PubMed:16456001, ECO:0000269|PubMed:19172738
uniprot
proteins
post_translational_modification
PTM: Phosphorylated upon EGF stimulation. Phosphorylated on tyrosine residues by HCK upon IL6 signaling (By similarity). Phosphorylated on tyrosine residue(s) by the thrombopoietin receptor (TPOR), stem cell factor receptor (SCFR), and T-cell and B-cell antigen receptors, gp130, IL-2R and IL-3R. Phosphorylated upon stimulation of TNFRSF11A/RANK by TNFSF11/RANKL. {ECO:0000250, ECO:0000269|PubMed:10068651, ECO:0000269|PubMed:15750601, ECO:0000269|PubMed:19172738, ECO:0000269|PubMed:9885561}.; PTM: Dephosphorylated by PTPN11.
uniprot
proteins
protein_family
GAB family
uniprot
proteins
pubmed
10068651
uniprot
proteins
pubmed
11449275
uniprot
proteins
pubmed
15750601
uniprot
proteins
pubmed
16456001
uniprot
proteins
pubmed
17374739
uniprot
proteins
pubmed
17947660
uniprot
proteins
pubmed
19172738
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23478294
uniprot
proteins
pubmed
9885561
uniprot
proteins
sequence_length
665
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UQC2}. Cell membrane {ECO:0000250|UniProtKB:Q9UQC2}. Membrane raft {ECO:0000269|PubMed:23478294}.
uniprot
proteins