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Data suggest that ubiquitin-conjugating enzyme E2 variant 2 (Ube2V2) and ring finger protein 4 (RNF4) together induce an active conformation of the ubiquitin-conjugating enzyme Ubc13-ubiquitin (Ubc13~Ub) thioester.
Functional analysis of selected regulated proteins revealed that knockdown of HNRPD, PHB2 and UB2V2 can increase HCMV replication, while knockdown of A4 and KSRP resulted in decreased HCMV replication.
suppression of hMMS2 reverses L-OHP tolerance in differentiated human colorectal carcinoma cells by promoting apoptosis
Data show RING finger (RNF) E3 ubiquitin ligase RNF8 dimerizes and binds to E2 ubiquitin-conjugating complex Ubc13/Mms2 with formation of Lys-63 ubiquitin chains, whereas the RNF168 RING domain is a monomer and does not catalyze Lys-6 ubiquitylation.
the crystal structure of human OTUB1 in complex with human UBC13 and MMS2
entire coding region and splice junctions of RNF8, UBC13 and MMS2 genes were screened for mutations in affected index cases from 123 Northern Finnish breast cancer families
Ubc13-Mms2 and Lys63-polyubiquitin chains are associated with signaling cellular stress
UBE2v2 signalling through PCNA ubiquitination is not required for immunoglobulin diversification in DT40 cells.
The results in this study allowed identification of important residues of the Ubc13-Mms2 interface, determine a correlation between heterodimer formation and function, and conclude why Mms2 forms a specific complex with Ubc13 but not other Ubc proteins.
Insight into the influence of protein dynamics on the affinity of ubiquitin for Mms2.
Data demonstrate that divergent activities of Ubc13 rely on its pairing with either of two Uevs, Uev1A or Mms2.
Mms2 physical association with ubiquitin is correlated with its ability to promote Lys63-linked ubiquitin chain assembly
These results point to a high level of redundancy in the DNA damage tolerance pathway and suggest the existence of another hMMS2 variant (hMMSv) or complex that can compensate for its loss.
Ang II type 2 receptor signaling attenuates DNA damage and consequent vascular senescence at least in part through methyl methanesulfonate sensitive 2 (MMS2) transactivation.
Ubiquitin-conjugating enzyme E2 variant proteins constitute a distinct subfamily within the E2 protein family. They have sequence similarity to other ubiquitin-conjugating enzymes but lack the conserved cysteine residue that is critical for the catalytic activity of E2s. The protein encoded by this gene also shares homology with ubiquitin-conjugating enzyme E2 variant 1 and yeast MMS2 gene product. It may be involved in the differentiation of monocytes and enterocytes.
1 alpha,25-dihydroxyvitamin D3-inducible
, DDVit 1
, MMS2 homolog
, enterocyte differentiation promoting factor
, enterocyte differentiation-associated factor 1
, enterocyte differentiation-associated factor EDAF-1
, enterocyte differentiation-promoting factor 1
, methyl methanesulfonate sensitive 2, S. cerevisiae, homolog of
, vitamin D3-inducible protein
, ubiquitin-conjugating enzyme E2v2
, ubiquitin-conjugating enzyme variant MMS2
, methyl methanesulfonate sensitive 2
, ubc-like protein MMS2
, ubiquitin-conjugating enzyme E2 variant 2
, Ubiquitin-conjugating enzyme E2 variant 2
, TMEM189-UBE2V1 readthrough transcript