Ubiquitin-Conjugating Enzyme E2 (UBE2J2) Human Recombinant Protein

The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is located in the membrane of the endoplasmic reticulum. Multiple alternatively spliced transcript variants have been found for this gene, but the full-length nature of some variants has not been defined. [provided by RefSeq, Jul 2008]

UBE2J2: Catalyzes the covalent attachment of ubiquitin to other proteins. Seems to function in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum. Belongs to the ubiquitin-conjugating enzyme family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Ubiquitin conjugating system; Ligase; EC 6.3.2.19; Ubiquitin ligase; Membrane protein, integral; Endoplasmic reticulum

Chromosomal Location of Human Ortholog: 1p36.33

Cellular Component: endoplasmic reticulum membrane; endoplasmic reticulum; integral to membrane

Molecular Function: small conjugating protein ligase activity; ubiquitin protein ligase binding; ATP binding; ligase activity

Biological Process: ER-associated protein catabolic process; protein polyubiquitination; response to unfolded protein