IndraLab

Statements


CK2 phosphorylates OTUB1 on S16. 12 / 12
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sparser
"Indeed, we provided biochemical, pharmacological and genetic evidence to establish that CK2 phosphorylates OTUB1 at Ser 16 ."

sparser
"CK2 phosphorylation of cytosolic Otub1 at ser16 induces nuclear translocation [ xref ]."

sparser
"CK2 phosphorylates OTUB1 at Ser 16 in vitro."

reach
"Casein kinase 2 (CK2)-dependent phosphorylation of OTUB1 at Ser16 played a critical role in ODN- and cathepsin K siRNA-mediated p53 stabilization."

sparser
"As reported previously, phosphorylation of OTUB1 at Serine 16 by Casein kinase 2 causes nuclear accumulation of OTUB1 ( xref ), we sought to know whether SET7-mediated methylation of OTUB1 at K122 could alter subcellular localization of OTUB1."

reach
"ODN-induced p53 stabilization is attributed to casein kinase 2 (CK2)-mediated phosphorylation of OTUB1 at Ser 16 [10]."

reach
"Casein kinase 2 (CK2) phosphorylates the deubiquitylase OTUB1 at Ser16 to trigger its nuclear localization."

sparser
"In osteosarcoma U2OS cells, casein kinase 2 (CK2) phosphorylates OTUB1 at Ser16 of the deubiquitinase, leading to its phosphorylation without altering its catalytic activity but promoting its translocation from the cytoplasm to the nucleus."

sparser
"Now that we have established that CK2 phosphorylates OTUB1 at Ser 16 , it would be interesting to explore whether small molecule inhibitors of CK2 potentially decrease the infection of host cells by Yersinia."

sparser
"ODN-induced p53 stabilization is attributed to casein kinase 2 (CK2)-mediated phosphorylation of OTUB1 at Ser 16 [ xref ]."

reach
"CK2 phosphorylation of cytosolic Otub1 at ser16 induces nuclear translocation [76]."

sparser
"In this study, we demonstrated that CK2 phosphorylated OTUB1 at Ser 16 in vitro and in cells, making OTUB1 a bona fide substrate for CK2."