IndraLab

Statements


CHEK2 affects USP28
| 6 8
CHEK2 binds USP28.
| 4 7
| 4 1

sparser
"It was previously shown that USP28 interacts with CHK2 [ xref ]."
| PMC

reach
"USP28 forms a complex with PIRH2 and CHK2 and antagonizes PIRH2 mediated polyubiquitylation and proteasomal degradation of CHK2 [XREF_BIBR]."

reach
"Similar to FBXW7, USP28 forms a complex with PIRH2 and CHK2, thus antagonizing the ubiquitination of CHK2 by PIRH2.The protein PIRH2 (also called RCHY1) is a promising candidate for maintaining the previously demonstrated USP28 “piggyback” model."
| PMC

reach
"We show that the deubiquitylating enzyme USP28 forms a complex with PIRH2 and CHK2 and antagonizes PIRH2 mediated polyubiquitylation and proteasomal degradation of CHK2."

reach
"USP28 forms a complex with PIRH2 and CHK2 and counteracts the negative regulation of PIRH2 on CHK2 21."
| 5

sparser
"Similar to FBXW7, USP28 forms a complex with PIRH2 and CHK2, thus antagonizing the ubiquitination of CHK2 by PIRH2."
| PMC

sparser
"We show that the deubiquitylating enzyme USP28 forms a complex with PIRH2 and CHK2 and antagonizes PIRH2-mediated polyubiquitylation and proteasomal degradation of CHK2."

sparser
"USP28 forms a complex with PIRH2 and CHK2 and counteracts the negative regulation of PIRH2 on CHK221."

sparser
"USP28 forms a complex with PIRH2 and CHK2 and antagonizes PIRH2-mediated polyubiquitylation and proteasomal degradation of CHK2 [ xref ]."

sparser
"USP28 forms a complex with PIRH2 and CHK2 and counteracts the negative regulation of PIRH2 on CHK2 xref ."

sparser
"Another potential candidate is UBR5, an E3 ligase that interacts with several reported USP28 substrates such as CHK2, p53, and c-MYC [ xref , xref , xref , xref ]."
| PMC
CHEK2 phosphorylates USP28.
| 2 1
CHEK2 phosphorylates USP28. 3 / 3
| 2 1

reach
"However, analyses of the USP28 sequence did not reveal any CHK2 phosphorylation motif, suggesting that USP28 cannot be phosphorylated by CHK2."
| PMC

sparser
"However, analyses of the USP28 sequence did not reveal any CHK2 phosphorylation motif, suggesting that USP28 cannot be phosphorylated by CHK2."
| PMC

reach
"The downstream ATM kinase CHK2 could be a potential candidate to phosphorylates USP28 following DNA damage."
| PMC
USP28 affects CHEK2
1 | 5 7
USP28 binds CHEK2.
| 4 7
| 4 1

sparser
"It was previously shown that USP28 interacts with CHK2 [ xref ]."
| PMC

reach
"USP28 forms a complex with PIRH2 and CHK2 and antagonizes PIRH2 mediated polyubiquitylation and proteasomal degradation of CHK2 [XREF_BIBR]."

reach
"Similar to FBXW7, USP28 forms a complex with PIRH2 and CHK2, thus antagonizing the ubiquitination of CHK2 by PIRH2.The protein PIRH2 (also called RCHY1) is a promising candidate for maintaining the previously demonstrated USP28 “piggyback” model."
| PMC

reach
"We show that the deubiquitylating enzyme USP28 forms a complex with PIRH2 and CHK2 and antagonizes PIRH2 mediated polyubiquitylation and proteasomal degradation of CHK2."

reach
"USP28 forms a complex with PIRH2 and CHK2 and counteracts the negative regulation of PIRH2 on CHK2 21."
| 5

sparser
"Similar to FBXW7, USP28 forms a complex with PIRH2 and CHK2, thus antagonizing the ubiquitination of CHK2 by PIRH2."
| PMC

sparser
"We show that the deubiquitylating enzyme USP28 forms a complex with PIRH2 and CHK2 and antagonizes PIRH2-mediated polyubiquitylation and proteasomal degradation of CHK2."

sparser
"USP28 forms a complex with PIRH2 and CHK2 and counteracts the negative regulation of PIRH2 on CHK221."

sparser
"USP28 forms a complex with PIRH2 and CHK2 and antagonizes PIRH2-mediated polyubiquitylation and proteasomal degradation of CHK2 [ xref ]."

sparser
"USP28 forms a complex with PIRH2 and CHK2 and counteracts the negative regulation of PIRH2 on CHK2 xref ."

sparser
"Another potential candidate is UBR5, an E3 ligase that interacts with several reported USP28 substrates such as CHK2, p53, and c-MYC [ xref , xref , xref , xref ]."
| PMC
USP28 deubiquitinates CHEK2.
1 |
USP28 deubiquitinates CHEK2. 1 / 1
1 |
USP28 activates CHEK2.
| 1
USP28 activates CHEK2. 1 / 1
| 1

reach
"Interestingly, in another study, CHK2 is shown to be directly regulated by USP28."