Browse our anti-Ubiquitin-Conjugating Enzyme E2I (UBE2I) Antibodies

Human Ubiquitin-Conjugating Enzyme E2I (UBE2I) interaction partners

1. It demonstrates the enzyme/substrate nature of Ubc9/CRMP2 binding and identify hot spots on CRMP2 that may form the basis of future drug discovery campaigns disrupting the CRMP2-Ubc9 interaction to recapitulate allosteric regulation of NaV1.7 for pain relief.

2. Detailed structural, thermodynamic, and kinetics results of the interactions between Ubc9 and its K65 acetylated variant (Ac-Ubc9(K65)) with three NDSMs derived from Elk1, CBP, and Calpain2 were shown to rationalize the mechanism beneath this reduced binding.

3. Findings suggest that nuclear DNA leakage activates nucleophagy through UBC9-mediated SUMOylation of lamin A/C, leading to degradation of nuclear components including lamin A/C and leaked nuclear DNA.

4. Study demonstrated overexpression of Ubc9 protein in osteosarcoma. Silencing Ubc9 in osteosarcoma cell lines induced decoupling of SUMO1 from Cx43, generating increased free Cx43 levels, which is important for reconstructing gap junction intercellular communication and recovering cellular functions.

5. Data show that the forkhead Box Protein P3 (FOXP3) response element at the -310 bp region, but not the -2182 bp region, is mainly required for ubiquitin conjugating enzyme 9 (UBC9) activation by FOXP3.

6. Study provides an insight into the role of the RNF4 to balance the role of SUMO signaling by directly targeting Ubc9 and SUMO E3 ligases.

7. The SUMO1/UBC9 axis may regulate Nox1mediated diabetic retinopathy by inhibiting reactive oxygen species generation and apoptosis.

8. our results indicate that down-regulation of UBC9 sensitizes cells to anticancer drugs, is possibly associated with the regulation of ERK1/2 and P38 activation and interacts with the intrinsic apoptosis pathway.

9. 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.

10. NUSAP1 contributes to accurate chromosome segregation by acting as a co-factor for RanBP2-RanGAP1-UBC9 during cell division.

11. Listeriolysin O -induced down-regulation of Ubc9 is independent of Ubc9-SUMO interaction, however, it may involve phosphorylation signaling.

12. Sumoylation of PML with SUMO2 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. (PML = promyelocytic leukemia protein; SUMO2 = small ubiquitin-like modifier 2; UBC9/UBE2I = ubiquitin-conjugating enzyme UBC9/UBE2I)

13. The role of Transthyretin in the regulation of Ubc9 SUMOylation

14. These findings point to UBC9 and autophagy as novel hallmarks of human papillomavirus oncogenesis

15. These findings reveal that SUMO E1~E2 oxidation is an essential redox switch in oxidative stress.

16. the mRNA and protein expression of Ubc9 are regulated by the microRNA miRNA-30a (miR-30a) in human subcutaneous adipocytes.

17. miR-30e in VSMCs exerted an anti-atherosclerosis effect via inhibiting proliferation and migration, and promoting apoptosis of VSMCs. More specifically, it was demonstrated that miR-30e exhibited these effects on VSMCs partially through targeting Ube2i and downregulating the IkappaBalpha/NFkappaB signaling pathway.

18. Ubc9 plays different roles of action in antitumor agents in chemotherapy. The process requires bleomycin hydrolase and poly(ADP-ribose) polymerase-1. The results are beneficial to deeply understanding of Ubc9 functions and for precise prediction of chemotherapy outcomes in tumors.

19. Suggest a novel role of PCGF2 in arsenic trioxide-mediated degradation of PML-RARA that PCGF2 might act as a negative regulator of UBE2I via direct interaction.

20. Akt directly phosphorylates Ubc9 at Thr35 and phosphorylates SUMO1 at Thr76. Ubc9 phosphorylation at Thr35 promotes Ubc9 thioester bond formation and SUMO1 phosphorylation at Thr76 stabilizes the SUMO1 protein.

Zebrafish Ubiquitin-Conjugating Enzyme E2I (UBE2I) interaction partners

1. These data indicate an in vivo requirement of Ubc9 for G2/M transition and/or progression through mitosis during vertebrate organogenesis.

Mouse (Murine) Ubiquitin-Conjugating Enzyme E2I (UBE2I) interaction partners

1. SUMO-conjugating enzyme Ubc9 interacts with a conserved GKAE motif in ROR-gammat to induce SUMOylation of ROR-gammat and suppress IL-17 expression.

2. Ubc9 transgenic mice, but also SUMO1 knockout mice were protected from ischemia/reperfusion injury as evidenced by better preserved barrier function and blunted inflammatory responses

3. 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.

4. this study shows that loss of Ubc9 results in a significant reduction of CD4 and CD8 single-positive lymphocytes in both thymus and periphery

5. 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.

6. The study reveals a function of SUMO protein modification as a Ubiquitin-independent ESCRT sorting signal, regulating the extracellular vesicle release of alpha-Synuclein.

7. 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.

8. UBC9 has a role in promoting proliferation and migration of fibroblast-like synoviocytes in rheumatoid arthritis

9. the sole SUMO E2 enzyme Ubc9 plays a critical role in reprogramming fibroblasts to iPS cells and maintaining ESC pluripotency.

10. Data indicate that knockdown of ubiquitin-conjugating enzyme 9 (UBC9) by small interfering RNA caused significant accumulations of aggregated protein.

11. Ubc9 negatively regulates osteoblastic differentiation induced by BMP.

12. expressed Ubc9 at modestly increased levels showed robust resistance to brain ischemia compared to wild type mice

13. Ubiquitous loss of sumoylation due to loss of UBC9 led to immediate fatal failure of intestinal function. Sumoylation was required for nucleus positioning and polarized organization of actin in the enterocytes.

14. FOXL2 interacts with PIAS1 and UBC9, and sumoylated in both human and mouse

15. The temporal profile of UBC9 induction and its ability to affect C/EBPdelta mRNA induction support a role for this protein during early adipogenesis

16. Our data indicate that DeltaNp63alpha is ubiquitinated in a Nedd4- and sumoylated in a Ubc9-dependent fashion, and that these modifications can regulate DeltaNp63alpha stability in the zebrafish ectoderm.

17. Knockdown of the SUMO-conjugating enzyme, Ubc9, severely compromises C2C12 muscle cell terminal differentiation. However, it does not affect the expression, the localization and the activation of MyoD and myogenin.

18. Noncovalent interaction between Ubc9 and SUMO promotes SUMO chain formation.

19. Ubc9 regulates GLUT4 turnover and targeting to GLUT4 storage compartment by a mechanism independent of its catalytic activity

20. Transcriptionally quiescent, fully grown, GV-intact oocytes have larger UBE2I-containing bodies than transcriptionally active, meiotically incompetent, growing oocytes.

Cow (Bovine) Ubiquitin-Conjugating Enzyme E2I (UBE2I) interaction partners

1. Chromosomal assignment of the bovine ubiquitin-conjugating enzyme E2I (UBE2I ) gene to BTA6q34 defines a new fragment of conserved synteny with human chromosome 16.

Pig (Porcine) Ubiquitin-Conjugating Enzyme E2I (UBE2I) interaction partners

1. Analysis of protein interactions showed that K179A, K180A, and K221A substitutions of classical swine fever virus core protein disrupt core-SUMO-1 binding, while K220A substitution precludes core-UBC9 binding.