IndraLab

Statements


UBE2D3 affects OTUB1
4 | 2 2
UBE2D3 binds OTUB1.
4 | 1 2
4 | 1

No evidence text available

No evidence text available

sparser
"These E2 enzymes have EC 50 values in the single digit micromolar range and lower the K M of OTUB1 for its substrate to 6.6 – 14 μM. Since the concentration of UBE2D3 alone has been reported to be 1.7 μM in MEF cells xref and the effective concentration of UBE2D3 needed to stimulate the DUB activity of OTUB1 is 1.6 μM ( xref ), it is likely that OTUB1:UBE2D3 form a stimulated DUB complex in cells."

No evidence text available

No evidence text available
UBE2D3-E2S binds OTUB1. 1 / 1
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reach
"To verify that the interactions observed in the crystal structure are also observed in solution, the binding of the E2s UbcH5c (closely related to UbcH5b and also targeted by OTUB1) and UBC13 to full-length OTUB1 was examined by NMR spectroscopy."
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sparser
"To verify that the interactions observed in the crystal structure are also observed in solution, the binding of the E2s UbcH5c (closely related to UbcH5b and also targeted by OTUB1) and UBC13 to full-length OTUB1 was examined by NMR spectroscopy."
UBE2D3 activates OTUB1.
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UBE2D3 activates OTUB1. 1 / 1
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reach
"Since the concentration of UBE2D3 alone has been reported to be 1.7 muM in MEF cells 19 and the effective concentration of UBE2D3 needed to stimulate the DUB activity of OTUB1 is 1.6 muM (XREF_FIG), it is likely that OTUB1 : UBE2D3 form a stimulated DUB complex in cells."
OTUB1 affects UBE2D3
4 | 2 2
OTUB1 binds UBE2D3.
4 | 1 2
4 | 1

No evidence text available

No evidence text available

sparser
"These E2 enzymes have EC 50 values in the single digit micromolar range and lower the K M of OTUB1 for its substrate to 6.6 – 14 μM. Since the concentration of UBE2D3 alone has been reported to be 1.7 μM in MEF cells xref and the effective concentration of UBE2D3 needed to stimulate the DUB activity of OTUB1 is 1.6 μM ( xref ), it is likely that OTUB1:UBE2D3 form a stimulated DUB complex in cells."

No evidence text available

No evidence text available
UBE2D3-E2S binds OTUB1. 1 / 1
| 1

reach
"To verify that the interactions observed in the crystal structure are also observed in solution, the binding of the E2s UbcH5c (closely related to UbcH5b and also targeted by OTUB1) and UBC13 to full-length OTUB1 was examined by NMR spectroscopy."
| 1

sparser
"To verify that the interactions observed in the crystal structure are also observed in solution, the binding of the E2s UbcH5c (closely related to UbcH5b and also targeted by OTUB1) and UBC13 to full-length OTUB1 was examined by NMR spectroscopy."
OTUB1 inhibits UBE2D3.
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OTUB1 inhibits UBE2D3. 1 / 1
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reach
"Interestingly, this non canonical mode of action by OTUB1 was found not to be unique to UBC13, as OTUB1 was also found to interact with and inhibit the E2 enzymes UBE2D2 and UBCH5B and UBE2D3 and UBCH[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
OTUB1 affects UBE2D1, UBE2D2, UBE2D3, UBE2E1, and UBE2N
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sparser
"To see if differences in relative stimulation of DUB activity can be attributed to variations in binding affinities, we determined equilibrium dissociation constants (K d ) for OTUB1 binding to UBE2D1, UBE2D2, UBE2D3, UBE2N, and UBE2E1 using isothermal titration calorimetry (ITC)."