CBLB (gene)

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Cbl proto-oncogene B, E3 ubiquitin protein ligase
Protein CBLB PDB 2ooa.png
PDB rendering based on 2ooa.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols CBLB ; Cbl-b; RNF56
External IDs OMIM604491 MGI2146430 HomoloGene15856 GeneCards: CBLB Gene
RNA expression pattern
PBB GE CBLB 209682 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 868 208650
Ensembl ENSG00000114423 ENSMUSG00000022637
UniProt Q13191 Q3TTA7
RefSeq (mRNA) NM_170662 NM_001033238
RefSeq (protein) NP_733762 NP_001028410
Location (UCSC) Chr 3:
105.37 – 105.59 Mb
Chr 16:
52.03 – 52.21 Mb
PubMed search [1] [2]

CBL-B is an E3 ubiquitin-protein ligase that in humans is encoded by the CBLB gene.[1][2] CBLB is a member of the CBL gene family.

Function[edit]

CBL-B functions as a negative regulator of T-cell activation.[3]

Clinical significance[edit]

Mutation of the CBLB gene has been associated with autoimmune conditions such as type 1 diabetes.[4][5]

Interactions[edit]

CBLB has been shown to interact with:

References[edit]

  1. ^ Keane MM, Rivero-Lezcano OM, Mitchell JA, Robbins KC, Lipkowitz S (July 1995). "Cloning and characterization of cbl-b: a SH3 binding protein with homology to the c-cbl proto-oncogene". Oncogene 10 (12): 2367–77. PMID 7784085. 
  2. ^ "Entrez Gene: CBLB Cas-Br-M (murine) ecotropic retroviral transforming sequence b". 
  3. ^ Wallner S, Gruber T, Baier G, Wolf D (2012). "Releasing the brake: targeting Cbl-b to enhance lymphocyte effector functions". Clin. Dev. Immunol. 2012: 692639. doi:10.1155/2012/692639. PMC 3328896. PMID 22550535. 
  4. ^ Hoyne GF, Flening E, Yabas M, Teh C, Altin JA, Randall K, Thien CB, Langdon WY, Goodnow CC (February 2011). "Visualizing the role of Cbl-b in control of islet-reactive CD4 T cells and susceptibility to type 1 diabetes". J. Immunol. 186 (4): 2024–32. doi:10.4049/jimmunol.1002296. PMID 21248249. 
  5. ^ Yokoi N, Fujiwara Y, Wang HY, Kitao M, Hayashi C, Someya T, Kanamori M, Oiso Y, Tajima N, Yamada Y, Seino Y, Ikegami H, Seino S (March 2008). "Identification and functional analysis of CBLB mutations in type 1 diabetes". Biochem. Biophys. Res. Commun. 368 (1): 37–42. doi:10.1016/j.bbrc.2008.01.032. PMID 18201552. 
  6. ^ a b c Elly C, Witte S, Zhang Z, Rosnet O, Lipkowitz S, Altman A, Liu YC (February 1999). "Tyrosine phosphorylation and complex formation of Cbl-b upon T cell receptor stimulation". Oncogene 18 (5): 1147–56. doi:10.1038/sj.onc.1202411. PMID 10022120. 
  7. ^ Schulze WX, Deng L, Mann M (2005). "Phosphotyrosine interactome of the ErbB-receptor kinase family". Mol. Syst. Biol. 1: 2005.0008. doi:10.1038/msb4100012. PMC 1681463. PMID 16729043. 
  8. ^ Ettenberg SA, Keane MM, Nau MM, Frankel M, Wang LM, Pierce JH, Lipkowitz S (March 1999). "cbl-b inhibits epidermal growth factor receptor signaling". Oncogene 18 (10): 1855–66. doi:10.1038/sj.onc.1202499. PMID 10086340. 
  9. ^ a b Lavagna-Sévenier C, Marchetto S, Birnbaum D, Rosnet O (June 1998). "The CBL-related protein CBLB participates in FLT3 and interleukin-7 receptor signal transduction in pro-B cells". J. Biol. Chem. 273 (24): 14962–7. doi:10.1074/jbc.273.24.14962. PMID 9614102. 
  10. ^ Magnifico A, Ettenberg S, Yang C, Mariano J, Tiwari S, Fang S, Lipkowitz S, Weissman AM (October 2003). "WW domain HECT E3s target Cbl RING finger E3s for proteasomal degradation". J. Biol. Chem. 278 (44): 43169–77. doi:10.1074/jbc.M308009200. PMID 12907674. 
  11. ^ Szymkiewicz I, Kowanetz K, Soubeyran P, Dinarina A, Lipkowitz S, Dikic I (October 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. 

Further reading[edit]