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The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Additionally we are shipping Ubiquitin-Conjugating Enzyme E2G 1 Proteins (10) and many more products for this protein.
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Further study discovered that the gp78 (show AMFR Antibodies) CUE domain works as a proofreading machine during the growth of K48-linked polyubiquitin (show UBB Antibodies) chains to ensure the linkage specificity. Together, our studies uncover a novel mechanism underlying the linkage specificity determination of longer polyubiquitin (show UBB Antibodies) chains.
ubiquitin binding by the acidic loops of Ube2g1 and Ube2r1 (show CDC34 Antibodies) enzymes distinguishes their Lys (show LYZ Antibodies)-48-ubiquitylation activities
These results reveal an unanticipated mode of Ube2g2 self-association that allows Ube2g2 to effectively engage two ubiquitins to specifically synthesize Lys48-linked ubiquitin chains.
study reports that UBCH8 (show UBE2E2 Antibodies) and UBE2G1 and UBE2G2 (show UBE2G2 Antibodies) cooperate with CRL4Cdt2 in promoting the polyubiquitylation and subsequent degradation of p21 (show CDKN1A Antibodies) and Cdt1 (show CDT1 Antibodies), respectively
The presence of the AUP1 (show Aup1 Antibodies)-Ube2g2 (show UBE2G2 Antibodies) complex at LDs provides a direct molecular link between LDs and the cellular ubiquitination machinery.
Lys (show LYZ Antibodies)-48-linked polyubiquitin (show UBB Antibodies) chains may be designed to bind certain proteins like Ube2g2 (show UBE2G2 Antibodies) such that the terminal ubiquitin subunit carrying the reactive Lys (show LYZ Antibodies)-48 side chain can be positioned properly for chain elongation regardless of chain length.
Results report the solution structure and backbone dynamics of Ube2g2 (show UBE2G2 Antibodies) solved by nuclear magnetic resonance spectroscopy.
Ubc7 mediates inositol 1,4,5-trisphosphate receptor ubiquitination and is a component of the endoplasmic reticulum-associated degradation pathway
Structural comparison of human UBE2G2 (show UBE2G2 Antibodies) with yeast Ubc7 indicated that the overall structures are similar except for the long loop region and the C-terminal helix.
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. The encoded protein shares 100% sequence identity with the mouse counterpart. This gene is ubiquitously expressed, with high expression seen in adult muscle. Three alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.
ubiquitin-conjugating enzyme E2 G1
, Ubiquitin-conjugating enzyme E2 G1
, ubiquitin-conjugating enzyme e2 g1
, ubiquitin-conjugating enzyme E2G 1 (UBC7 homolog)
, ubiquitin-conjugating enzyme E2G 1 (UBC7 homolog, yeast)
, ubiquitin-conjugating enzyme E2G 1
, ubiquitin carrier protein G1
, ubiquitin-conjugating enzyme E2G 1 (UBC7 homolog, C. elegans)
, ubiquitin-conjugating enzyme E2G 1 (homologous to C. elegans UBC7)
, ubiquitin-protein ligase G1
, ubiquitin-conjugating enzyme UBC7
, ubiquitin carrier protein G2
, ubiquitin conjugating enzyme 7
, ubiquitin conjugating enzyme G2
, ubiquitin-conjugating enzyme E2 G2
, ubiquitin-conjugating enzyme E2G 2 (UBC7 homolog, yeast)
, ubiquitin-conjugating enzyme E2G 2 (homologous to yeast UBC7)
, ubiquitin-protein ligase G2