Cbl
entrez
12402
canonical
uniprot
P22682
canonical
ensembl
ENSMUSG00000034342
resolver
ensp
ENSMUSP00000041902
resolver
ensp
ENSMUSP00000146244
resolver
ensp
ENSMUSP00000258365
resolver
enst
ENSMUST00000037644
resolver
enst
ENSMUST00000206720
resolver
genesymbol
Cbl
resolver
uniprot
A0A0X1KG61
resolver
uniprot
Q3U527
resolver
uniprot
Q8CEA1
resolver
uniprot_entry
A0A0X1KG61_MOUSE
resolver
uniprot_entry
CBL_MOUSE
resolver
uniprot_sec
Q3U527
resolver
uniprot_sec
Q8CEA1
resolver
amino_acid_sequence
MAGNVKKSSGAGGGGSGGSGAGGLIGLMKDAFQPHHHHHHLSPHPPCTVDKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLRTVLSRYEGKMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQPRRNLTKLSLIFSHMLAELKGIFPSGLFQGDTFRITKADAAEFWRKAFGEKTIVPWKSFRQALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPWSSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIHKPGSYIFRLSCTRLGQWAIGYVTADGNILQTIPHNKPLFQALIDGFREGFYLFPDGRNQNPDLTGLCEPTPQDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTSWQESEGQGCPFCRCEIKGTEPIVVDPFDPRGSGSLLRQGAEGAPSPNYDDDDDERADDSLFMMKELAGAKVERPSSPFSMAPQASLPPVPPRLDLLQQRAPVPASTSVLGTASKAASGSLHKDKPLPIPPTLRDLPPPPPPDRPYSVGAETRPQRRPLPCTPGDCPSRDKLPPVPSSRPGDSWLSRPIPKVPVATPNPGDPWNGRELTNRHSLPFSLPSQMEPRADVPRLGSTFSLDTSMTMNSSPVAGPESEHPKIKPSSSANAIYSLAARPLPMPKLPPGEQGESEEDTEYMTPTSRPVGVQKPEPKRPLEATQSSRACDCDQQIDSCTYEAMYNIQSQALSVAENSASGEGNLATAHTSTGPEESENEDDGYDVPKPPVPAVLARRTLSDISNASSSFGWLSLDGDPTNFNEGSQVPERPPKPFPRRINSERKASSYQQGGGATANPVATAPSPQLSSEIERLMSQGYSYQDIQKALVIAHNNIEMAKNILREFVSISSPAHVAT
uniprot
proteins
disease_involvement
DISEASE: Note=Can be converted to an oncogenic protein by deletions or mutations that disturb its ability to down-regulate RTKs.
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: E3 ubiquitin-protein ligase that acts as a negative regulator of many signaling pathways by mediating ubiquitination of cell surface receptors (PubMed:10393178, PubMed:12649282, PubMed:19265199, PubMed:20100865, PubMed:9653117). Accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome (PubMed:12649282, PubMed:20100865). Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, CSF1R, EPHA8 and KDR and mediates their ubiquitination to terminate signaling (PubMed:19265199). Recognizes membrane-bound HCK, SRC and other kinases of the SRC family and mediates their ubiquitination and degradation (By similarity). Ubiquitinates EGFR and SPRY2 (By similarity). Involved in LAG3-mediated inhibition of TCR signaling: following ligand-binding to LAG3, catalyzes 'Lys-63'-linked ubiquitination of LAG3, unleashing the LAG3 C-terminus from the membrane, and initiating a signaling that prevents TCR activation (By similarity). Ubiquitinates NECTIN1 following association between NECTIN1 and herpes simplex virus 1/HHV-1 envelope glycoprotein D, leading to NECTIN1 removal from cell surface (By similarity). Participates in signal transduction in hematopoietic cells (By similarity). Plays an important role in the regulation of osteoblast differentiation and apoptosis (By similarity). Essential for osteoclastic bone resorption (By similarity). The 'Tyr-731' phosphorylated form induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function (By similarity). In association with CBLB, required for proper feedback inhibition of ciliary platelet-derived growth factor receptor-alpha (PDGFRA) signaling pathway via ubiquitination and internalization of PDGFRA (PubMed:29237719). {ECO:0000250|UniProtKB:P22681, ECO:0000269|PubMed:10393178, ECO:0000269|PubMed:12649282, ECO:0000269|PubMed:19265199, ECO:0000269|PubMed:20100865, ECO:0000269|PubMed:29237719, ECO:0000269|PubMed:9653117}.
uniprot
proteins
mass_dalton
100564
uniprot
proteins
mutagenesis
MUTAGEN 304; /note="G->E: Abolishes interaction with ZAP70, but does not affect interaction with SLA."; /evidence="ECO:0000269|PubMed:12024036
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:12649282, ECO:0000269|PubMed:20100865}.
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on tyrosine residues by ALK, EGFR, FGR, INSR, SYK, FYN and ZAP70. Phosphorylated on several tyrosine residues by constitutively activated FGFR3. Phosphorylated on tyrosine residues by activated PDGFRA and PDGFRB (By similarity). Phosphorylated on tyrosine residues in response to CSF1R, FLT1 and KIT signaling. Phosphorylated on tyrosine residues by HCK. {ECO:0000250, ECO:0000269|PubMed:10092522, ECO:0000269|PubMed:15001553, ECO:0000269|PubMed:17353186, ECO:0000269|PubMed:18034775, ECO:0000269|PubMed:19265199, ECO:0000269|PubMed:7782294, ECO:0000269|PubMed:8551236, ECO:0000269|PubMed:8798454}.; PTM: Ubiquitinated, leading to its degradation via the proteasome. Ubiquitination is negatively regulated by IFT20. {ECO:0000250|UniProtKB:P22681}.
uniprot
proteins
pubmed
10092522
uniprot
proteins
pubmed
10393178
uniprot
proteins
pubmed
12024036
uniprot
proteins
pubmed
12649282
uniprot
proteins
pubmed
12842890
uniprot
proteins
pubmed
15001553
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17353186
uniprot
proteins
pubmed
17620338
uniprot
proteins
pubmed
17947660
uniprot
proteins
pubmed
18034775
uniprot
proteins
pubmed
18602463
uniprot
proteins
pubmed
19265199
uniprot
proteins
pubmed
20100865
uniprot
proteins
pubmed
2030914
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21830225
uniprot
proteins
pubmed
23374343
uniprot
proteins
pubmed
29237719
uniprot
proteins
pubmed
29589748
uniprot
proteins
pubmed
7782294
uniprot
proteins
pubmed
8551236
uniprot
proteins
pubmed
8798454
uniprot
proteins
pubmed
9447983
uniprot
proteins
pubmed
9653117
uniprot
proteins
pubmed
9722576
uniprot
proteins
sequence_length
913
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000250}. Cell projection, cilium {ECO:0000269|PubMed:29237719}. Golgi apparatus {ECO:0000269|PubMed:29237719}. Note=Colocalizes with FGFR2 in lipid rafts at the cell membrane. {ECO:0000250}.
uniprot
proteins