TRIM23 siRNA – E3 Ubiquitin-Protein Ligase TRIM23 Isoform Alpha (Human)

The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This protein is also a member of the ADP ribosylation factor family of guanine nucleotide-binding family of proteins. Its carboxy terminus contains an ADP-ribosylation factor domain and a guanine nucleotide binding site, while the amino terminus contains a GTPase activating protein domain which acts on the guanine nucleotide binding site. The protein localizes to lysosomes and the Golgi apparatus. It plays a role in the formation of intracellular transport vesicles, their movement from one compartment to another, and phopholipase D activation. Three alternatively spliced transcript variants for this gene have been described. [provided by RefSeq, Jul 2008]

TRIM23: Acts as an E3 ubiquitin-protein ligase. In the presence of the human cytomegalovirus (HCMV) protein UL144, participates in 'Lys-63'-linked auto-ubiquitination of TRAF6 resulting in the virally controlled activation of NF-kappa-B at early time of infection. The C-terminus can act as an allosteric activator of the cholera toxin catalytic subunit. 3 isoforms of the human protein are produced by alternative splicing.

Protein type: Ubiquitin ligase; Ubiquitin conjugating system; Ligase; EC 6.3.2.-

Chromosomal Location of Human Ortholog: 5q12.3

Cellular Component: Golgi membrane; lysosomal membrane; nucleus

Molecular Function: GTPase activity; identical protein binding; protein binding; GDP binding; GTP binding; zinc ion binding; enzyme activator activity; ubiquitin-protein ligase activity; ligase activity

Biological Process: positive regulation of catalytic activity; viral reproduction; small GTPase mediated signal transduction; protein ubiquitination