Cblb
entrez
208650
canonical
uniprot
Q3TTA7
canonical
ensembl
ENSMUSG00000022637
resolver
ensp
ENSMUSP00000110115
resolver
ensp
ENSMUSP00000153753
resolver
ensp
ENSMUSP00000153787
resolver
ensp
ENSMUSP00000154583
resolver
ensp
ENSMUSP00000154755
resolver
ensp
ENSMUSP00000228202
resolver
ensp
ENSMUSP00000228203
resolver
enst
ENSMUST00000114471
resolver
enst
ENSMUST00000227062
resolver
genesymbol
Cblb
resolver
uniprot
B9EKI5
resolver
uniprot
E9QMY2
resolver
uniprot
F7C621
resolver
uniprot_entry
B9EKI5_MOUSE
resolver
uniprot_entry
CBLB_MOUSE
resolver
uniprot_entry
F7C621_MOUSE
resolver
uniprot_sec
E9QMY2
resolver
amino_acid_sequence
MANSMNGRNPGGRGGNPRKGRILGIIDAIQDAVGPPKQAAADRRTVEKTWKLMDKVVRLCQNPKLQLKNSPPYILDILPDTYQHLRLILSKYDDNQKLAQLSENEYFKIYIDSLMKKSKRAIRLFKEGKERMYEEQSQDRRNLTKLSLIFSHMLAEIKAIFPNGQFQGDNFRITKADAAEFWRKFFGDKTIVPWKVFRQCLHEVHQISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPWGSILRNWNFLAVTHPGYMAFLTYDEVKARLQKYSTKPGSYIFRLSCTRLGQWAIGYVTGDGNILQTIPHNKPLFQALIDGSREGFYLYPDGRSYNPDLTGLCEPTPHDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTAWQESDGQGCPFCRCEIKGTEPIIVDPFDPRDEGSRCCSIIDPFSIPMLDLDDDDDREESLMMNRLASVRKCTDRQNSPVTSPGSSPLAQRRKPQPDPLQIPHLSLPPVPPRLDLIQKGIVRSPCGSPTGSPKSSPCMVRKQDKPLPAPPPPLRDPPPPPERPPPIPPDNRLSRHFHHGESVPSRDQPMPLEAWCPRDAFGTNQVMGCRILGDGSPKPGVTANSSLNGRHSRMGSEQVLMRKHRRHDLPSEGAKVFSNGHLATEEYDVPPRLSPPPPVTTLLPSIKCTGPLANCLSEKTRDTVEDDDDEYKIPSSHPVSLNSQPSHCHNVKAPVRSCDNGHCILNGTHGAPSEMKKSNIPDLGIYLKGGGSDSASDPVPLPPARPPPRDSPKHGSSVNRTPSDYDLLIPPLGEDAFDALPPSLPPPPPPARHSLIEHSKPPGSSSRPSSGQDLFLLPSDPFFDPTSGQVPLPPARRAAGDSGKANRASQDYDQLPSSSDGSQAPARPPKPRPRRTAPEIHHRKPHGPEAALENVDAKIAKLMGEGYAFEEVKRALEIAQNNVEVARSILREFAFPPPVSPRLNL
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome (PubMed:10646608, PubMed:10646609, PubMed:11070165). Negatively regulates TCR (T-cell receptor), BCR (B-cell receptor) and FCER1 (high affinity immunoglobulin epsilon receptor) signal transduction pathways (PubMed:10646608, PubMed:10646609, PubMed:11070165). In naive T-cells, inhibits VAV1 activation upon TCR engagement and imposes a requirement for CD28 costimulation for proliferation and IL-2 production (PubMed:10646608, PubMed:10646609, PubMed:11070165). Also acts by promoting PIK3R1/p85 ubiquitination, which impairs its recruitment to the TCR and subsequent activation (PubMed:11526404). In activated T-cells, inhibits PLCG1 activation and calcium mobilization upon restimulation and promotes anergy (PubMed:15308098). 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). In B-cells, acts by ubiquitinating SYK and promoting its proteasomal degradation (PubMed:12771181). Slightly promotes SRC ubiquitination (By similarity). May be involved in EGFR ubiquitination and internalization (By similarity). May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3 (By similarity). In association with CBL, 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:Q13191, ECO:0000269|PubMed:10646608, ECO:0000269|PubMed:10646609, ECO:0000269|PubMed:11070165, ECO:0000269|PubMed:11526404, ECO:0000269|PubMed:12771181, ECO:0000269|PubMed:15308098, ECO:0000269|PubMed:29237719}.
uniprot
proteins
mass_dalton
109092
uniprot
proteins
mutagenesis
MUTAGEN 257; /note="H->L: Homozygous mice display immune dysregulation with T and B cell hyperproliferation in response to antigen receptor cross-linking."; /evidence="ECO:0000269|PubMed:36006710
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination.
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on tyrosine and serine residues upon TCR or BCR activation. Phosphorylated on Tyr-664 and Tyr-708 in adipocytes following insulin stimulation. {ECO:0000269|PubMed:12771181, ECO:0000269|PubMed:12842890}.; PTM: Auto-ubiquitinated upon EGF-mediated cell activation or upon T-cell costimulation by CD28; which promotes proteasomal degradation. {ECO:0000269|PubMed:12193687}.
uniprot
proteins
pubmed
10646608
uniprot
proteins
pubmed
10646609
uniprot
proteins
pubmed
11070165
uniprot
proteins
pubmed
11526404
uniprot
proteins
pubmed
12193687
uniprot
proteins
pubmed
12771181
uniprot
proteins
pubmed
12842890
uniprot
proteins
pubmed
15308098
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
29237719
uniprot
proteins
pubmed
36006710
uniprot
proteins
sequence_length
982
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12842890}. Note=In adipocytes, translocates to the plasma membrane upon insulin stimulation.
uniprot
proteins