CBLC
entrez
23624
canonical
uniprot
Q9ULV8
canonical
ensembl
ENSG00000142273
resolver
ensp
ENSP00000340250
resolver
ensp
ENSP00000494162
resolver
ensp
ENSP00000667394
resolver
ensp
ENSP00000667397
resolver
ensp
ENSP00000724817
resolver
ensp
ENSP00000743308
resolver
genesymbol
CBLC
resolver
genesymbol_syn
CBL3
resolver
genesymbol_syn
RNF57
resolver
hgnc
HGNC:15961
resolver
uniprot
Q8N1E5
resolver
uniprot
Q9Y5Z2
resolver
uniprot
Q9Y5Z3
resolver
uniprot_entry
CBLC_HUMAN
resolver
uniprot_sec
Q8N1E5
resolver
uniprot_sec
Q9Y5Z2
resolver
uniprot_sec
Q9Y5Z3
resolver
activity_regulation
ACTIVITY REGULATION: Phosphorylation at Tyr-341 is necessary and sufficient for the activation of E3 activity. {ECO:0000269|PubMed:20525694}.
uniprot
proteins
amino_acid_sequence
MALAVAPWGRQWEEARALGRAVRMLQRLEEQCVDPRLSVSPPSLRDLLPRTAQLLREVAHSRRAAGGGGPGGPGGSGDFLLIYLANLEAKSRQVAALLPPRGRRSANDELFRAGSRLRRQLAKLAIIFSHMHAELHALFPGGKYCGHMYQLTKAPAHTFWRESCGARCVLPWAEFESLLGTCHPVEPGCTALALRTTIDLTCSGHVSIFEFDVFTRLFQPWPTLLKNWQLLAVNHPGYMAFLTYDEVQERLQACRDKPGSYIFRPSCTRLGQWAIGYVSSDGSILQTIPANKPLSQVLLEGQKDGFYLYPDGKTHNPDLTELGQAEPQQRIHVSEEQLQLYWAMDSTFELCKICAESNKDVKIEPCGHLLCSCCLAAWQHSDSQTCPFCRCEIKGWEAVSIYQFHGQATAEDSGNSSDQEGRELELGQVPLSAPPLPPRPDLPPRKPRNAQPKVRLLKGNSPPAALGPQDPAPA
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: 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. Functionally coupled with the E2 ubiquitin-protein ligases UB2D1, UB2D2 and UB2D3. Regulator of EGFR mediated signal transduction; upon EGF activation, ubiquitinates EGFR. Isoform 1, but not isoform 2, inhibits EGF stimulated MAPK1 activation. Promotes ubiquitination of SRC phosphorylated at 'Tyr-419'. In collaboration with CD2AP may act as regulatory checkpoint for Ret signaling by modulating the rate of RET degradation after ligand activation; CD2AP converts it from an inhibitor to a promoter of RET degradation; the function limits the potency of GDNF on neuronal survival. {ECO:0000269|PubMed:10362357, ECO:0000269|PubMed:14661060, ECO:0000269|PubMed:18753381, ECO:0000269|PubMed:20525694, ECO:0000269|PubMed:23145173}.
uniprot
proteins
mass_dalton
52456
uniprot
proteins
mutagenesis
MUTAGEN 244; /note="Y->A: Abolishes interaction with EGFR. Decreases interaction with SRC and abolishes SRC ubiquitination."; /evidence="ECO:0000269|PubMed:22888118"; MUTAGEN 244; /note="Y->F: No effect on interaction with EGFR and SRC as well as on SRC ubiquitination."; /evidence="ECO:0000269|PubMed:22888118"; MUTAGEN 264; /note="R->A: Abolishes interaction with EGFR. Decreases interaction with SRC and abolishes SRC ubiquitination."; /evidence="ECO:0000269|PubMed:22888118"; MUTAGEN 265; /note="P->L: Enhances interaction with EGFR and SRC as well as SRC ubiquitination."; /evidence="ECO:0000269|PubMed:22888118"; MUTAGEN 266; /note="S->A: Decreases interactions with EGFR and SRC as well as SRC ubiquitination."; /evidence="ECO:0000269|PubMed:22888118"; MUTAGEN 268; /note="T->A: Abolishes interaction with EGFR. Decreases interaction with and ubiquitination of SRC."; /evidence="ECO:0000269|PubMed:22888118"; MUTAGEN 276; /note="G->E: No effect on interaction with RET. Binds slightly to SRC, this interaction is independent of SRC phosphorylation. Strongly decreases SRC ubiquitination. Abolishes interaction with EGFR."; /evidence="ECO:0000269|PubMed:14661060, ECO:0000269|PubMed:18753381, ECO:0000269|PubMed:22888118"; MUTAGEN 341; /note="Y->E: Induces E3 activity and autoubiquitination. Releases ubiquitin-conjugating enzyme E2 UBE2D2 faster."; /evidence="ECO:0000269|PubMed:14661060, ECO:0000269|PubMed:20525694, ECO:0000269|PubMed:23145173"; MUTAGEN 341; /note="Y->F: Abolishes activation by EGF stimulation and enhancement by TGFB1I1 of E3 activity."; /evidence="ECO:0000269|PubMed:14661060, ECO:0000269|PubMed:20525694, ECO:0000269|PubMed:23145173"; MUTAGEN 341; /note="Missing: Abolishes E3 activity."; /evidence="ECO:0000269|PubMed:14661060, ECO:0000269|PubMed:20525694, ECO:0000269|PubMed:23145173"; MUTAGEN 351; /note="C->A: No effect on TGFB1I1 and SRC interactions. Abolishes SRC ubiquitination. Abolishes interaction with TGFB1I1; when associated with A-366. Abolishes interaction with RET and inhibition of RET degradation."; /evidence="ECO:0000269|PubMed:14661060, ECO:0000269|PubMed:18753381, ECO:0000269|PubMed:23145173"; MUTAGEN 366; /note="C->A: Abolishes interaction with TGFB1I1. Abolishes interaction with TGFB1I1; when associated with A-351."; /evidence="ECO:0000269|PubMed:23145173
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on multiple tyrosine residues by SRC. Isoform 1, but not isoform 2, is phosphorylated on tyrosines by EGFR.; PTM: Autoubiquitinated when phosphorylated at Tyr-341, enhanced by SRC; suggesting proteasomal degradation. {ECO:0000269|PubMed:14661060, ECO:0000269|PubMed:20525694, ECO:0000269|PubMed:23145173}.
uniprot
proteins
pubmed
10362357
uniprot
proteins
pubmed
10571044
uniprot
proteins
pubmed
14661060
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18753381
uniprot
proteins
pubmed
20525694
uniprot
proteins
pubmed
22888118
uniprot
proteins
pubmed
23145173
uniprot
proteins
sequence_length
474
uniprot
proteins