Ring Finger Protein 57 (RNF57)

CBL proteins, such as CBLC, are phosphorylated upon activation of a variety of receptors that signal via protein tyrosine kinases. Through interactions with proteins containing SRC homology-2 (SH2) and SH3 domains, CBL proteins modulate downstream cell signaling. The deduced 474-amino acid protein has a calculated molecular mass of 52.5 kD. CBLC contains an N-terminal phosphotyrosine-binding domain, a conserved C3HC4 zinc finger motif, and a short proline-rich region near the C terminus. CBLC lacks the extensive proline-rich domain and leucine zipper motif found in CBL and CBLB. RNA dot blot analysis detected low but ubiquitous expression, with highest levels in adrenal gland and salivary gland in addition to the tissues identified by Northern blot analysis.