UMLS. CSP-HL7-ICD9CM-NCI-NDFRT-RXNORM
%
A B C D E F G H I J K L M N O P Q R S T U V W X Y Z
C C- C1 C3 C5 C6 C7 CA CB CC CD CE CF CG CH CI CJ CK CL CM CN CO CP CQ CR CS CT CU CV CW CX CY CZ
CB CB- CB1 CBA CBE CBF CBL CBM CBR CBT
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1. C57BL
(UMLS (NCI) C0025921) =Mammal ;
3. CBLB
[Cass-Br-M (Murine) Ecotropic Retroviral Transforming Sequence B (CBLB), encoded by the CALB gene, is a member of the CBL family of E3 ubiquitin ligases, which are critical negative regulators of tyrosine kinase signaling pathways in the immune system. Impairment of the CBLB signaling pathway may contribute to human autoimmune diseases, including type 1 diabetes. CBLB contains putative nuclear localization signal, zinc finger, leucine zipper, and proline-rich domains. It associates with three SH3 domain proteins FYN, FGR, and PLCG1. Three isoforms (a long form, truncated isoform 1, truncated isoform 2) are produced by alternative splicing. (From OMIM, PMID and NCI) ( NCI )] (UMLS (NCI) C1335961) Signal Transduction Protein CBLB =Amino Acid, Peptide, or Protein; Enzyme
2. CBL
[The cellular homologue of v-cbl, CBL protein is expressed in a range of hemopoietic lineages. Malignancies are associated with translocations of the CBL gene. Adaptor protein CBL2, containing a RING finger and multiple SH3 domains, encodes a protein similar to SLI1, a negative regulator of an EGF receptor tyrosine kinase homologue. Through its SH2 domain, CBL regulates activated tyrosine-phosphorylated receptor PTK ubiquitination as an E3 ubiquitin ligase and recruits, and activates, an E2 ubiquitin-conjugating enzyme through its RING domain. CBL is recruited to the tyrosine kinase insulin receptor by CAP adaptor protein, through a CAP SH3 domain. Upon CBL phosphorylation, CAP/CBL dissociates from the receptor to complex with caveolar flotillin and localize to plasma membrane lipid rafts. (from OMIM 165360 and NCI) ( NCI )] (UMLS (NCI) C1367374) CBL Gene Product;
CBL Protein;
CBL2 Gene Product =Amino Acid, Peptide, or Protein; Biologically Active Substance

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