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OTUB2 deubiquitinates STAT1. 5 / 5
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"Previous IB results indicated that OTUB2 did not affect total STAT1 protein levels ( Figures 4 D and 4E), suggesting that deubiquitination of STAT1 by OTUB2 is atypical, regardless of protein stabilit[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"These results supported our conclusion that K173 and K637 are essential lysine sites that facilitate the deubiquitination of STAT1 by OTUB2 and the subsequent regulation of STAT1 dimerization and tran[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"In addition, OTUB2 deubiquitinates STAT1 to promote its phosphorylation and dimerization ."
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"Mechanistically, OTUB2 mediates the deubiquitination and phosphorylation of STAT1 and further promotes calmodulin-like protein 3 (CALML3) upregulation."
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"In contrast, Chang et al. [56] discovered that OTUB2 is missing in ESCC tissues, while OTUB2 can deubiquitinate STAT1 and phosphorylate it, thereby activating CALML3 transcription and phospholipid acetylserine synthesis to exert tumor suppressive effects."
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