This gene belongs to the forkhead family of transcription factors which are characterized by a distinct forkhead domain. This gene likely functions as a trigger for apoptosis through expression of genes necessary for cell death. Translocation of this gene with the MLL gene is associated with secondary acute leukemia. Alternatively spliced transcript variants encoding the same protein have been observed. [provided by RefSeq, Jul 2008]

eIF4E, a protein modulates translation of maternal mRNAs in early embryos before the onset of zygotic transcription. eIF4E also influences the overall rate of translation. eIF4E binds to the 7 methyl GTP cap structure of eukaryotic mRNAs. Phosphorylation of eIF4E on serine 209 regulates the affinity of this protein for the 7 methyl GTP cap and/or RNA. Phosphorylation also enhances the interaction of eIF4E with eIF4G, which form a complex known as eIF4F. eIF4E phosphorylation is correlated with

p130 represents one of several known substrates for v-Crk encoded p47. p130 Cas (for Crk-associated substrate) exhibits a high level of tyrosine phosphorylation and is tightly associated with v-Crk, suggesting a role in v-Crk-mediated cell signaling. The molecular cloning of p130 Cas has shown it to represent a novel SH3 containing signaling molecule with a cluster of multiple putative SH2-binding motifs for v-Crk. By immunoprecipitation analysis, p130 Cas has been shown to be highly phosphory

The mitochondrial enzyme encoded by this gene catalyzes synthesis of carbamoyl phosphate from ammonia and bicarbonate. This reaction is the first committed step of the urea cycle, which is important in the removal of excess urea from cells. The encoded protein may also represent a core mitochondrial nucleoid protein. Three transcript variants encoding different isoforms have been found for this gene. The shortest isoform may not be localized to the mitochondrion. Mutations in this gene have be

The protein encoded by this gene can polymerize and depolymerize F-actin and G-actin in a pH-dependent manner. Increased phosphorylation of this protein by LIM kinase aids in Rho-induced reorganization of the actin cytoskeleton. Cofilin is a widely distributed intracellular actin-modulating protein that binds and depolymerizes filamentous F-actin and inhibits the polymerization of monomeric G-actin in a pH-dependent manner. It is involved in the translocation of actin-cofilin complex from c

PCK2 is a a member of the phosphoenolpyruvate carboxykinase (GTP) family. The protein is a mitochondrial enzyme that catalyzes the conversion of oxaloacetate to phosphoenolpyruvate in the presence of GTP. A cytosolic form encoded by a different gene has also been characterized and is the key enzyme of gluconeogenesis in the liver. The encoded protein may serve a similar function, although it is constitutively expressed and not modulated by hormones such as glucagon and insulin that regulate