Aliases for TBC1D4 Gene
External Ids for TBC1D4 Gene
Previous GeneCards Identifiers for TBC1D4 Gene
This gene is a member of the Tre-2/BUB2/CDC16 domain family. The protein encoded by this gene is a Rab-GTPase-activating protein, and contains two phopshotyrosine-binding domains (PTB1 and PTB2), a calmodulin-binding domain (CBD), a Rab-GTPase domain, and multiple AKT phosphomotifs. This protein is thought to play an important role in glucose homeostasis by regulating the insulin-dependent trafficking of the glucose transporter 4 (GLUT4), important for removing glucose from the bloodstream into skeletal muscle and fat tissues. Reduced expression of this gene results in an increase in GLUT4 levels at the plasma membrane, suggesting that this protein is important in intracellular retention of GLUT4 under basal conditions. When exposed to insulin, this protein is phosphorylated, dissociates from GLUT4 vesicles, resulting in increased GLUT4 at the cell surface, and enhanced glucose transport. Phosphorylation of this protein by AKT is required for proper translocation of GLUT4 to the cell surface. Individuals homozygous for a mutation in this gene are at higher risk for type 2 diabetes and have higher levels of circulating glucose and insulin levels after glucose ingestion. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Aug 2015]
GeneCards Summary for TBC1D4 Gene
TBC1D4 (TBC1 Domain Family Member 4) is a Protein Coding gene. Diseases associated with TBC1D4 include diabetes mellitus, noninsulin-dependent, 5 and lipodystrophy, familial partial, type 5. Among its related pathways are Translation Insulin regulation of translation and Thyroid hormone signaling pathway. GO annotations related to this gene include GTPase activator activity. An important paralog of this gene is EVI5L.
UniProtKB/Swiss-Prot for TBC1D4 Gene
May act as a GTPase-activating protein for RAB2A, RAB8A, RAB10 and RAB14. Isoform 2 promotes insulin-induced glucose transporter SLC2A4/GLUT4 translocation at the plasma membrane, thus increasing glucose uptake.