IndraLab

Statements


USP22 deubiquitinates Histone. 9 / 9
| 9

reach
"USP22 deubiquitylates histone and non histone substrates and has been associated with cancer progression and spinocerebellar ataxia."

reach
"USP22 deubiquitinates histone H2Bub and H2Aub."

reach
"USP22 can deubiquitylate both histone and non‐histone substrates."

reach
"USP22 reverses the polycomb-catalyzed ubiquitination of histones, including H2A and H2B, as well as nonhistone protein TRF1 (TBP [TATA box-binding protein]-related factor 1) to regulate the transcript[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

reach
"In addition to histones, USP22 deubiquitinates TRF1, CCNB1, CCND1, and SIRT1, thereby regulating involvement in metabolism, cycling, and apoptosis."

reach
"Our studies indicate that USP22 acting as a histone deubiquitinase participates in deubiquitination of histone H2Bub on the promoter of VEGFA, co-activating ZEB1-mediated VEGFA transcription.It has been reported that ubiquitination modification on ZEB1 involved in maintenance of ZEB1 stability plays important roles in tumor progression."

reach
"However, the mechanisms by which miR-30e-5p regulates NSCLC pathogenesis remain unclear.Ubiquitin-specific peptidase 22 (USP22) is part of a multiprotein complex and regulates gene transcription withi[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

reach
"USP22 also deubiquitinates non histone proteins, including telomeric repeat binding factor 1 (TRF1), sirtuin 1 (SIRT1), cyclin B1 and others, leading to protein stabilization by preventing proteasome mediated degradation."

reach
"In addition, certain non histone proteins such as sirtuin 1 (Sirt1) and fructose-bisphosphatase 1 (FBP1) could be deubiquitinated by USP22."