IndraLab

Statements


USP37 is phosphorylated on S628. 7 / 7
| 5 2

sparser
"In G1/S, Ser628 of USP37 is phosphorylated by either CDK2/cyclin E or CDK2/cyclin A, and this triggers USP37 full DUB activity."

sparser
"In vivo deubiquitination assays and in vitro kinase assays indicated that phosphorylation of USP37 at Ser628 had no regulatory effect on targeting SND1 for deubiquitination ( xref ), and CDK2-mediated phosphorylation of USP37 at Ser628 did not mediate the phosphorylation of USP37 at Thr631 ( xref )."

sparser
"Ser 628 of USP37 was phosphorylated in G1/S, but not mitosis ( Figure 7 E)."

sparser
"Hence, we sought to determine whether phosphorylation of USP37 at Ser628 enhances targeting for deubiquitination of SND1 and whether CDK2 could also mediate phosphorylation of USP37 at Thr631."

rlimsp
"The USP37 protein becomes fully functional upon its Cyclin A/CDK2-mediated phosphorylation at Ser-628 residue [6] and remains active throughout the S phase upto G2/M boundary."

sparser
"Dixit et al. xref reported that CDK2 mediates the phosphorylation of USP37 at Ser628."

rlimsp
"A recent study implicates the phosphorylation of Ser-628 of USP37 to protect it from CDH1 mediated ubiquitination [6]."