UniProt functional annotation for P27870

UniProt code: P27870.

Organism: Mus musculus (Mouse).
Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.
 
Function: Couples tyrosine kinase signals with the activation of the Rho/Rac GTPases, thus leading to cell differentiation and/or proliferation.
 
Subunit: Interacts with SHB (By similarity). Interacts with APS, DOCK2, GRB2, GRB3, DOCK2, SLA, TEC and ZNF655/VIK. Interacts with SIAH2; without leading to its degradation. Associates with BLNK, PLCG1, GRB2 and NCK1 in a B-cell antigen receptor-dependent fashion. Interacts with CBLB; which inhibits tyrosine phosphorylation and down-regulates activity (PubMed:10646609, PubMed:10646608). May interact with CCPG1 (PubMed:17000758). Interacts with CLNK (PubMed:11463797). Interacts with THEMIS2 (PubMed:20644716). Interacts with NEK3 and this interaction is prolactin-dependent. Interacts with ITK. Interacts with PTK2B/PYK2 (By similarity). Interacts with HCK. Interacts with PTK2B/PYK2. Interacts (via SH2 domain) with SYK (By similarity). Interacts with ANKRD54 (PubMed:19064729). Interacts with CD6 (PubMed:24584089). Interacts with isoform 2 of CRACR2A (By similarity). {ECO:0000250|UniProtKB:P15498, ECO:0000269|PubMed:10646608, ECO:0000269|PubMed:10646609, ECO:0000269|PubMed:10662792, ECO:0000269|PubMed:11463797, ECO:0000269|PubMed:19064729, ECO:0000269|PubMed:20644716, ECO:0000269|PubMed:24584089, ECO:0000269|PubMed:8877094, ECO:0000269|PubMed:9400828}.
Tissue specificity: Widely expressed in hematopoietic cells but not in other cell types. Found in the spleen and lung. {ECO:0000269|PubMed:2069873}.
Domain: The DH domain is involved in interaction with CCPG1.
Ptm: Phosphorylated by FYN (By similarity). Phosphorylated on tyrosine residues by HCK in response to IFNG and bacterial lipopolysaccharide (LPS). {ECO:0000250, ECO:0000269|PubMed:10646608, ECO:0000269|PubMed:10646609, ECO:0000269|PubMed:9400828}.

Annotations taken from UniProtKB at the EBI.