CBLC

Cbl proto-oncogene C, E3 ubiquitin protein ligase

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
3OP0, 3VRN, 3VRO, 3VRP, 3VRQ, 3VRR

Identifiers

Symbols

CBLC ; CBL-3; CBL-SL; RNF57

External IDs

OMIM: 608453 MGI: 1931457 HomoloGene: 8108 GeneCards: CBLC Gene

Gene ontology
Molecular function	• phosphotyrosine binding • signal transducer activity • epidermal growth factor receptor binding • calcium ion binding • zinc ion binding • ligase activity • SH3 domain binding • ubiquitin protein ligase activity
Cellular component	• nucleus • extracellular exosome
Biological process	• cell surface receptor signaling pathway • negative regulation of epidermal growth factor-activated receptor activity • protein ubiquitination • negative regulation of epidermal growth factor receptor signaling pathway • protein ubiquitination involved in ubiquitin-dependent protein catabolic process • negative regulation of MAP kinase activity
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 19:
44.78 – 44.8 Mb

Chr 7:
19.78 – 19.8 Mb

PubMed search

Signal transduction protein CBL-C is a protein that in humans is encoded by the CBLC gene.^[1]^[2]^[3]

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 (MIM 190090) homology-2 (SH2) and SH3 domains, CBL proteins modulate downstream cell signaling (Keane et al., 1999).[supplied by OMIM]^[3]

Interactions

CBLC has been shown to interact with FYN^[4] and Epidermal growth factor receptor.^[2]^[5]

References

↑ Keane MM, Ettenberg SA, Nau MM, Banerjee P, Cuello M, Penninger J, Lipkowitz S (Jun 1999). "cbl-3: a new mammalian cbl family protein". Oncogene 18 (22): 3365–75. doi:10.1038/sj.onc.1202753. PMID 10362357.
1 2 Kim M, Tezuka T, Suziki Y, Sugano S, Hirai M, Yamamoto T (Dec 1999). "Molecular cloning and characterization of a novel cbl-family gene, cbl-c". Gene 239 (1): 145–54. doi:10.1016/S0378-1119(99)00356-X. PMID 10571044.
1 2 "Entrez Gene: CBLC Cas-Br-M (murine) ecotropic retroviral transforming sequence c".
↑ Kim, M; Tezuka T; Suziki Y; Sugano S; Hirai M; Yamamoto T (Oct 1999). "Molecular cloning and characterization of a novel cbl-family gene, cbl-c". Gene (NETHERLANDS) 239 (1): 145–54. doi:10.1016/S0378-1119(99)00356-X. ISSN 0378-1119. PMID 10571044.
↑ Keane, M M; Ettenberg S A; Nau M M; Banerjee P; Cuello M; Penninger J; Lipkowitz S (Jun 1999). "cbl-3: a new mammalian cbl family protein". Oncogene (ENGLAND) 18 (22): 3365–75. doi:10.1038/sj.onc.1202753. ISSN 0950-9232. PMID 10362357.

Ollendorff V, Mattei M, Fournier E; et al. (1999). "A third human CBL gene is on chromosome 19". Int. J. Oncol. 13 (6): 1159–61. doi:10.3892/ijo.13.6.1159. PMID 9824625.
Irby RB, Mao W, Coppola D; et al. (1999). "Activating SRC mutation in a subset of advanced human colon cancers". Nat. Genet. 21 (2): 187–90. doi:10.1038/5971. PMID 9988270.
Ettenberg SA, Keane MM, Nau MM; et al. (1999). "Cbl-b inhibits epidermal growth factor receptor signaling". Oncogene 18 (10): 1855–66. doi:10.1038/sj.onc.1202499. PMID 10086340.
Loreto MP, Berry DM, McGlade CJ (2002). "Functional Cooperation between c-Cbl and Src-Like Adaptor Protein 2 in the Negative Regulation of T-Cell Receptor Signaling". Mol. Cell. Biol. 22 (12): 4241–55. doi:10.1128/MCB.22.12.4241-4255.2002. PMC 133880. PMID 12024036.
Szymkiewicz I, Kowanetz K, Soubeyran P; et al. (2002). "CIN85 participates in Cbl-b-mediated down-regulation of receptor tyrosine kinases". J. Biol. Chem. 277 (42): 39666–72. doi:10.1074/jbc.M205535200. PMID 12177062.
Courbard JR, Fiore F, Adélaïde J; et al. (2003). "Interaction between two ubiquitin-protein isopeptide ligases of different classes, CBLC and AIP4/ITCH". J. Biol. Chem. 277 (47): 45267–75. doi:10.1074/jbc.M206460200. PMID 12226085.
Wong ES, Fong CW, Lim J; et al. (2002). "Sprouty2 attenuates epidermal growth factor receptor ubiquitylation and endocytosis, and consequently enhances Ras/ERK signalling". EMBO J. 21 (18): 4796–808. doi:10.1093/emboj/cdf493. PMC 126289. PMID 12234920.
Taher TE, Tjin EP, Beuling EA; et al. (2002). "C-Cbl is involved in Met signaling in B cells and mediates hepatocyte growth factor-induced receptor ubiquitination". J. Immunol. 169 (7): 3793–800. doi:10.4049/jimmunol.169.7.3793. PMID 12244174.
Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Nau MM, Lipkowitz S (2003). "Comparative genomic organization of the cbl genes". Gene 308: 103–13. doi:10.1016/S0378-1119(03)00471-2. PMID 12711395.
Kim M, Tezuka T, Tanaka K, Yamamoto T (2004). "Cbl-c suppresses v-Src-induced transformation through ubiquitin-dependent protein degradation". Oncogene 23 (9): 1645–55. doi:10.1038/sj.onc.1207298. PMID 14661060.
Kassenbrock CK, Anderson SM (2004). "Regulation of ubiquitin protein ligase activity in c-Cbl by phosphorylation-induced conformational change and constitutive activation by tyrosine to glutamate point mutations". J. Biol. Chem. 279 (27): 28017–27. doi:10.1074/jbc.M404114200. PMID 15117950.
Beausoleil SA, Jedrychowski M, Schwartz D; et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
Rual JF, Venkatesan K, Hao T; et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.

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CBLC

Interactions

References

Further reading