disease:Can be converted to an oncogenic protein by deletions or mutations that disturb its ability to down-regulate RTKs.,domain:The N-terminus is composed of the phosphotyrosine binding (PTB) domain, a short linker region and the RING-type zinc finger. The PTB domain, which is also called TKB (tyrosine kinase binding) domain, is composed of three different subdomains: a four-helix bundle (4H), a calcium-binding EF hand and a divergent SH2 domain.,domain:The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme.,function:Participates in signal transduction in hematopoietic cells. Adapter protein that functions as a negative regulator of many signaling pathways that start from receptors at the cell surface. Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Recognizes activated receptor tyrosine kinases, including PDGFA, EGF and CSF1, and terminates signaling.,miscellaneous:This protein has one functional calcium-binding site.,pathway:Protein modification; protein ubiquitination.,PTM:Phosphorylated on tyrosine residues by EGFR, SYK, FYN and ZAP70 (By similarity). Phosphorylated on tyrosine residues by INSR.,similarity:Contains 1 CBL N-terminal domain.,similarity:Contains 1 RING-type zinc finger.,similarity:Contains 1 SH2 domain.,similarity:Contains 1 UBA domain.,similarity:Contains 2 EF-hand-like domains.,subunit:Associates with NCK via its SH3 domain. The phosphorylated C-terminus interacts with CD2AP via its second SH3 domain. Binds to UBE2L3. Interacts with adapters SLA, SLA2 and with the phosphorylated C-terminus of SH2B2. Interacts with EGFR, SYK and ZAP70 via the highly conserved Cbl-N region. Also interacts with SORBS1 and INPPL1/SHIP2. Interacts with phosphorylated LAT2. May interact with CBLB.,
show all