CBLC

Description

The CBLC (Cbl proto-oncogene C) is a protein-coding gene located on chromosome 19.

CBL-C is a signal transduction protein encoded by the CBLC gene in humans. CBL proteins, including CBL-C, are phosphorylated when activated by receptors that signal through protein tyrosine kinases. These proteins interact with other proteins containing SH2 and SH3 domains, influencing downstream cell signaling. CBL-C specifically interacts with FYN and the Epidermal Growth Factor Receptor.

CBL-C is an E3 ubiquitin ligase that attaches ubiquitin to proteins, marking them for degradation by the proteasome. It works with the E2 enzymes UB2D1, UB2D2, and UB2D3. CBL-C regulates EGFR signaling by ubiquitinating EGFR after EGF activation. Isoform 1, but not isoform 2, blocks EGF-induced MAPK1 activation. It also promotes the ubiquitination of SRC when it is phosphorylated at tyrosine 419. Along with CD2AP, CBL-C acts as a checkpoint in Ret signaling by controlling how quickly RET is broken down after ligand activation. CD2AP changes CBL-C from an inhibitor to a promoter of RET degradation, limiting the effects of GDNF on nerve cell survival.

CBLC is also known as CBL-3, CBL-SL, RNF57.

Associated Diseases

WES Whole Exome Sequencing