IndraLab

Statements


13 | 10 4

No evidence text available

sparser
"Taken together, these data show that USP15 interacts with SART3 directly through the DUSP-UBL domains."

No evidence text available

sparser
"As shown in xref , SART3 interacted with USP15 1–226 but not with USP15 230–952 ."

reach
"Moreover, as a substrate recruiting factor of USP15 either, SART3 can simultaneously bind USP4 and USP15, serving as a platform to deubiquitinate PRP31 and PRP3."

sparser
"USP15 interacts with SART3."

reach
"We next examined whether SART3 forms a complex with USP15 and USP4 simultaneously using sequential immunoprecipitation."

reach
"Moreover, it was reported that Sart3, Usp4 and Usp15 form a complex in order to de-ubiquitinate Prp3 and Prp31 simultaneously."
| PMC

reach
"USP15 interacts with SART3."

No evidence text available

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reach
"The U4/U6 recycling factor SART3 has histone chaperone activity and associates with USP15 to regulate H2B deubiquitination."

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reach
"Therefore, the interaction between SART3 and USP15 in the cells was examined."

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sparser
"Therefore, the interaction between SART3 and USP15 in the cells was examined."

reach
"As shown in XREF_SUPPLEMENTARY, SART3 interacted with USP15 1-226 but not with USP15 230-952."

No evidence text available

reach
"USP15 and USP4 form a complex with SART3."

reach
"Indeed, USP15 specifically binds to SART3 (also known as Tip110) via DUSP domain and removes ubiquitin from both SART3 and its binding partner, histone H2B XREF_BIBR XREF_BIBR XREF_BIBR."

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reach
"These findings suggest SART3 binds to both USP15 and USP4, and this may lead to deubiquitination of PRP31 and PRP3 simultaneously."

No evidence text available

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