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CBLB (E3 ubiquitin-protein ligase CBL-B) is a gene that drives cell growth when it is altered. The public catalogues list it as an oncogene driver and a biomarker, and clinical evidence ties its variants to diagnosis, prognosis or drug response. Tied to Lung cancer, Skin cancer, Breast cancer and 2 more.
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. Negatively regulates TCR (T-cell receptor), BCR (B-cell receptor) and FCER1 (high affinity immunoglobulin epsilon receptor) signal transduction pathways. In naive T-cells, inhibits VAV1 activation upon TCR engagement and imposes a requirement for CD28 costimulation for proliferation and IL-2 production.
CIViC holds 1 clinical evidence item and 0 assertions across 1 variant. Open Targets scores its association with cancer at 0.69 (direct and indirect evidence; datatypes literature 0.94, genetic association 0.36, somatic mutation 0.85). IntOGen calls it a driver in 2 cohorts (2 activating, 0 loss-of-function), covering Lung Adenocarcinoma, Non-Small Cell Lung Cancer.
In plain words · CBLB (E3 ubiquitin-protein ligase CBL-B) is a gene that drives cell growth when it is altered. The public catalogues list it as an oncogene driver and a biomarker, and clinical evidence ties its variants to diagnosis, prognosis or drug response. Tied to Lung cancer, Skin cancer, Breast cancer and 2 more.
CBLB (E3 ubiquitin-protein ligase CBL-B) is a gene that drives cell growth when it is altered. The public catalogues list it as an oncogene driver and a biomarker, and clinical evidence ties its variants to diagnosis, prognosis or drug response. Tied to Lung cancer, Skin cancer, Breast cancer and 2 more.
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.
No product in this corpus aims at CBLB yet. Drugs fit a pocket that exists only in one shape of the mutant protein and hold it there, off.
Tumour-specific alteration: the catalogues call it an oncogene driver (IntOGen cohort analysis finds it activated more often than chance); what a medicine would aim at or exploit is the altered form or its loss, absent from normal cells; no corpus medicine is aimed at it yet. HPA CBLB: RNA low tissue specificity; high antibody staining in 13 normal tissues; highest cancer staining liver cancer (5 of 11 high). Distribution: 3 cancer families in the corpus carry a prevalence row, label threshold or catalogue link for it (Lung cancer (all types), Skin cancer (all types), Breast cancer (all types)); Open Targets associates it with 0 specific cancer types at or above 0.5. (Rule 6 of scripts/fetch-target-specificity.ts.)
Sources: UniProt Q13191; CIViC gene CBLB; IntOGen CBLB; Human Protein Atlas CBLB tissue; Open Targets ENSG00000114423 associations
First described 1995. Earliest sequence paper UniProt cites for the protein: Keane M.M. et al, Oncogene, 1995, "Cloning and characterization of cbl-b: a SH3 binding protein with homology to the c-cbl proto-oncogene". Source.
Sources: HGNC HGNC:1542 (approved symbol, name, aliases, locus and cross-references (hgnc_complete_set.txt)); UniProt Q13191 (protein name, function text, keywords and locations (REST API)); CIViC gene CBLB (1 evidence items, 0 assertions, 1 variants; diseases: Lung Non-small Cell Carcinoma (GraphQL API, CC0)); Open Targets ENSG00000114423 (association with cancer (MONDO_0004992) 0.69; per-cancer scores at or above 0.5: melanoma 0.56, skin cancer 0.56, breast cancer 0.53, lung cancer 0.57 (GraphQL API, CC0)); IntOGen CBLB (driver in 2 cohorts (Act 2, LoF 0); Compendium_Cancer_Genes.tsv release 20240920, CC0 1.0)
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. Negatively regulates TCR (T-cell receptor), BCR (B-cell receptor) and FCER1 (high affinity immunoglobulin epsilon receptor) signal transduction pathways. In naive T-cells, inhibits VAV1 activation upon TCR engagement and imposes a requirement for CD28 costimulation for proliferation and IL-2 production. Also acts by promoting PIK3R1/p85 ubiquitination, which impairs its recruitment to the TCR and subsequent activation. In activated T-cells, inhibits PLCG1 activation and calcium mobilisation upon restimulation and promotes anergy. Involved in LAG3-mediated inhibition of TCR signalling: following ligand-binding to LAG3, catalyses 'Lys-63'-linked ubiquitination of LAG3, unleashing the LAG3 C-terminus from the membrane, and initiating a signalling that prevents TCR activation. Location: Cytoplasm (UniProt). Locus 3q13.11 (HGNC).
RNA: low tissue specificity, detected in all normal tissues.
Medium: Appendix, Breast, Caudate, Cervix, Gallbladder, Hippocampus, Kidney, Liver.
Medium only: carcinoid, colorectal cancer, endometrial cancer, lung cancer.
Human Protein Atlas version 25.1, antibody staining at reliability approved, enhanced or supported; used under CC BY-SA 3.0. Staining counts are patients per level in the atlas cohort, not population prevalence.
Query for this target: (TITLE:"CBLB" OR ABSTRACT:"CBLB" OR TITLE:"Cbl proto-oncogene B" OR ABSTRACT:"Cbl proto-oncogene B" OR TITLE:"E3 ubiquitin-protein ligase CBL-B" OR ABSTRACT:"E3 ubiquitin-protein ligase CBL-B" OR TITLE:"RNF56" OR ABSTRACT:"RNF56" OR TITLE:"Cbl-b" OR ABSTRACT:"Cbl-b") AND (cancer OR tumor OR tumour OR oncology OR carcinoma OR lymphoma OR leukemia OR leukaemia OR myeloma OR sarcoma OR melanoma OR glioma). Results are unfiltered search hits about CBLB, not a curated reading list.