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The SUMO1 (show SUMO1 Proteins)/UBC9 axis may regulate Nox1mediated diabetic retinopathy by inhibiting reactive oxygen species generation and apoptosis.
our results indicate that down-regulation of UBC9 sensitizes cells to anticancer drugs, is possibly associated with the regulation of ERK1/2 and P38 (show CRK Proteins) activation and interacts with the intrinsic apoptosis pathway.
Ubc9 is an essential regulator of ADAP where it is required for TCR-induced membrane recruitment of the small GTPase Rap1 and its effector protein RapL and for activation of the small GTPase Rac1 in T cell adhesion.
NUSAP1 (show NUSAP1 Proteins) contributes to accurate chromosome segregation by acting as a co-factor for RanBP2-RanGAP1 (show RANGAP1 Proteins)-UBC9 during cell division.
Listeriolysin O -induced down-regulation of Ubc9 is independent of Ubc9-SUMO interaction, however, it may involve phosphorylation signaling.
Sumoylation of PML (show PML Proteins) with SUMO2 (show SUMO2 Proteins) by UBC9/UBE2I can lead to formation of polymeric SUMO chains. Data suggest that coordination of growing poly-SUMO chain with "back side" binding site on UBC9/UBE2I appears to be required for SUMO chain elongation on PML (show PML Proteins). (PML (show PML Proteins) = promyelocytic leukemia protein (show PML Proteins); SUMO2 (show SUMO2 Proteins) = small ubiquitin-like modifier 2 (show SUMO2 Proteins); UBC9/UBE2I = ubiquitin-conjugating enzyme (show Ube2t Proteins) UBC9/UBE2I)
The role of Transthyretin (show TTR Proteins) in the regulation of Ubc9 SUMOylation
These findings point to UBC9 and autophagy as novel hallmarks of human papillomavirus oncogenesis
These findings reveal that SUMO E1~E2 oxidation is an essential redox switch in oxidative stress.
the mRNA and protein expression of Ubc9 are regulated by the microRNA miRNA-30a (miR (show MLXIP Proteins)-30a) in human subcutaneous adipocytes.
These data indicate an in vivo requirement of Ubc9 for G2/M transition and/or progression through mitosis during vertebrate organogenesis.
These findings suggest that the UBC9/PML/RNF4 axis plays a critical role as an important SUMO pathway in cardiac fibrosis. Modulating the protein levels of the pathway provides an attractive therapeutic target for the treatment of cardiac fibrosis and heart failure.
this study shows that loss of Ubc9 results in a significant reduction of CD4 (show CD4 Proteins) and CD8 (show CD8A Proteins) single-positive lymphocytes in both thymus and periphery
Increased UBC9-mediated SUMOylation is sufficient to upregulate cardiac autophagy. UBC9 overexpression reduced aggregate formation, decreased fibrosis, reduced hypertrophy, and improved cardiac function and survival.
The study reveals a function of SUMO protein modification as a Ubiquitin-independent ESCRT sorting signal, regulating the extracellular vesicle release of alpha-Synuclein.
Synaptic trapping of Ubc9 through a PKC phosphorylation-dependent increase of Ubc9 recognition to phosphorylated substrates and consequently leads to the modulation of synaptic sumoylation.
UBC9 has a role in promoting proliferation and migration of fibroblast-like synoviocytes in rheumatoid arthritis
the sole SUMO E2 enzyme Ubc9 plays a critical role in reprogramming fibroblasts to iPS cells and maintaining ESC pluripotency.
Data indicate that knockdown of ubiquitin-conjugating enzyme 9 (UBC9) by small interfering RNA caused significant accumulations of aggregated protein.
Ubc9 negatively regulates osteoblastic differentiation induced by BMP.
expressed Ubc9 at modestly increased levels showed robust resistance to brain ischemia compared to wild type mice
Chromosomal assignment of the bovine ubiquitin-conjugating enzyme E2I (UBE2I ) gene to BTA6q34 defines a new fragment of conserved synteny with human chromosome 16.
Analysis of protein interactions showed that K179A, K180A, and K221A substitutions of classical swine fever virus core protein disrupt core-SUMO-1 (show SUMO1 Proteins) binding, while K220A substitution precludes core-UBC9 binding.
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. Four alternatively spliced transcript variants encoding the same protein have been found for this gene.
, SUMO-conjugating enzyme UBC9
, SUMO-protein ligase
, ubiquitin carrier protein 9
, ubiquitin carrier protein I
, ubiquitin conjugating enzyme 9
, ubiquitin-conjugating enzyme E2I (UBC9 homolog, yeast)
, ubiquitin-conjugating enzyme E2I (homologous to yeast UBC9)
, ubiquitin-conjugating enzyme UbcE2A
, ubiquitin-like protein SUMO-1 conjugating enzyme
, ubiquitin-protein ligase E2I
, ubiquitin-protein ligase I
, SUMO-conjugating enzyme UBC9-A
, SUMO-protein ligase A
, ubiquitin carrier protein 9-A
, ubiquitin carrier protein I-A
, ubiquitin-conjugating enzyme 9
, ubiquitin-conjugating enzyme E2 I-A
, ubiquitin-protein ligase I-A
, ubiquitin-conjugating enzyme E2L
, ubiquitin-conjugating enzyme E2I
, SUMO-1 conjugating enzyme
, Ubiquitin conjugating enzyme E2I (homologous to yeast UBC9)
, ubiquitin-conjugating enzyme E2 I
, ubiquitin-conjugating enzyme E2I (UBC9 homolog)
, Ubiquitin carrier protein 9
, Ubiquitin carrier protein I
, Ubiquitin-conjugating enzyme E2 I
, Ubiquitin-protein ligase I
, ubiquitin conjugating enzyme
, RING-type E3 SUMO transferase UBC9