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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Ubiquitin-conjugating enzyme E2, J2

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] (from NCBI)
Top mentioned proteins: Ubiquitin, UBC6
Papers on NCUBE2
The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines.
Navon et al., Israel. In J Biol Chem, 2010
analysis of involvement of E2 enzymes in specifying polyubiquitin chain assembly
Identification of a family of noncanonical ubiquitin-conjugating enzymes structurally related to yeast UBC6.
Houston et al., United Kingdom. In Biochem Biophys Res Commun, 2000
Database searches identified other related proteins; the human and mouse orthologues of NCUBE1, a second human homologue of yeast UBC6 (NCUBE2), and related proteins from S. pombe, C. elegans, and P. mariana.
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