This gene encodes a complex I assembly factor protein. Complex I (NADH-ubiquinone oxidoreductase) catalyzes the transfer of electrons from NADH to ubiquinone (coenzyme Q) in the first step of the mitochondrial respiratory chain, resulting in the translocation of protons across the inner mitochondrial membrane. The encoded protein is required for assembly of complex I, and mutations in this gene are a cause of mitochondrial complex I deficiency. Alternatively spliced transcript variants have be

GNB2 belongs to the WD repeat G protein beta family. $nGuanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.

DNA replication, recombination and repair, all of which are necessary for genome stability, require the presence of exonucleases (1). In DNA replication, these enzymes are involved in the processing of Okazaki fragments, whereas in DNA repair, they function to excise damaged DNA fragments and correct recombinational mismatches (2). Exonucleases involved in these processes include DNA polymerases, including DNA pol ∂ and é. DNA pol ∂ consists of two subunits, p125 which interacts direc

This gene encodes a testis-specific, differentiation antigen, acrosomal vesicle protein 1, that arises within the acrosomal vesicle during spermatogenesis, and is associated with the acrosomal membranes and matrix of mature sperm. The acrosomal vesicle protein 1 may be involved in sperm-zona binding or penetration. Alternatively spliced transcript variants have been described. [provided by RefSeq, Nov 2010].

Cenexin1 is an isoform of ODF2, that unlike ODF2 is present in several somatic cell types. Cenexin1 acts as a general scaffold protein that is specifically localised to the distal/subdistal appendages of mother centrioles. Cenexin1 is required for proper localization of Plk1 to the centrosomes. This centrosomal localization of Plk1 is required for proper microtubule function. Cenexin1 recruits Plk1 via a C-terminal extension of cenexin1 that is not present in ODF2. Cenexin1 is required for prop