IndraLab

Statements

SELENBP1 binds USP33. 4 / 8
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reach
"The interaction between USP33 and SELENBP1 was detected by a two-hybrid assay in human prostate cancer cells (Jeong et al., 2009), indicating SELENBP1 may play a role in epigenetics regulation."
36386843
sparser
"SELENBP1 has also been implicated in ubiquitination from a study demonstrating the binding of SELENBP1 to von Hippel- Lindau protein (pVHL)- interacting deubiquitinating enzyme 1 (VDU1) that was abolished with the incubation of β-mercaptoethanol, which dissociates selenium (Jeong et al., xref ), suggesting a selenium dependent interaction of SELENBP1 and VDU1."
23805071
reach
"SELENBP1 has also been implicated in ubiquitination from a study demonstrating the binding of SELENBP1 to von Hippel- Lindau protein (pVHL) - interacting deubiquitinating enzyme 1 (VDU1) that was abolished with the incubation of beta-mercaptoethanol, which dissociates selenium, suggesting a selenium dependent interaction of SELENBP1 and VDU1."
23805071
sparser
"The interaction between USP33 and SELENBP1 was detected by a two-hybrid assay in human prostate cancer cells ( xref ), indicating SELENBP1 may play a role in epigenetics regulation."
36386843