+ |
IKBKB | down-regulates activity
phosphorylation
|
COPS5 |
0.336 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275518 |
Ser201 |
KPPDEGPsEYQTIPL |
in vitro |
|
pmid |
sentence |
31950832 |
Overexpression of IKKalpha or IKKbeta leads to enhanced phosphorylation of CSN5, the catalytic subunit for CSN deneddylase activity. Mutational analyses have revealed that phosphorylation at serine 201 and threonine 205 of CSN5 impairs CSN-mediated deneddylation activity in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275519 |
Thr205 |
EGPSEYQtIPLNKIE |
in vitro |
|
pmid |
sentence |
31950832 |
Overexpression of IKKalpha or IKKbeta leads to enhanced phosphorylation of CSN5, the catalytic subunit for CSN deneddylase activity. Mutational analyses have revealed that phosphorylation at serine 201 and threonine 205 of CSN5 impairs CSN-mediated deneddylation activity in vitro. |
|
Publications: |
2 |
Organism: |
In Vitro |
+ |
CHUK | down-regulates activity
phosphorylation
|
COPS5 |
0.329 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275507 |
Ser201 |
KPPDEGPsEYQTIPL |
in vitro |
|
pmid |
sentence |
31950832 |
Overexpression of IKKalpha or IKKbeta leads to enhanced phosphorylation of CSN5, the catalytic subunit for CSN deneddylase activity. Mutational analyses have revealed that phosphorylation at serine 201 and threonine 205 of CSN5 impairs CSN-mediated deneddylation activity in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275508 |
Thr205 |
EGPSEYQtIPLNKIE |
in vitro |
|
pmid |
sentence |
31950832 |
Overexpression of IKKalpha or IKKbeta leads to enhanced phosphorylation of CSN5, the catalytic subunit for CSN deneddylase activity. Mutational analyses have revealed that phosphorylation at serine 201 and threonine 205 of CSN5 impairs CSN-mediated deneddylation activity in vitro. |
|
Publications: |
2 |
Organism: |
In Vitro |
+ |
COPS5 | form complex
binding
|
COP9 signalosome variant 2 |
0.933 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270761 |
|
|
Homo sapiens |
|
pmid |
sentence |
18850735 |
The COP9 signalosome (CSN) is a multiprotein complex that plays a critical role in diverse cellular and developmental processes in various eukaryotic organisms. we have performed a comprehensive proteomic analysis of the human CSN complex using a new purification method and quantitative mass spectrometry. Purification of the human CSN complex from a stable 293 cell line expressing N-terminal HBTH-tagged CSN5 subunit was achieved by high-affinity streptavidin binding with TEV cleavage elution. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
COPS5 | form complex
binding
|
COP9 signalosome variant 1 |
0.94 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270775 |
|
|
Homo sapiens |
|
pmid |
sentence |
18850735 |
The COP9 signalosome (CSN) is a multiprotein complex that plays a critical role in diverse cellular and developmental processes in various eukaryotic organisms. we have performed a comprehensive proteomic analysis of the human CSN complex using a new purification method and quantitative mass spectrometry. Purification of the human CSN complex from a stable 293 cell line expressing N-terminal HBTH-tagged CSN5 subunit was achieved by high-affinity streptavidin binding with TEV cleavage elution. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
COPS5 | down-regulates
ubiquitination
|
SMAD4 |
0.444 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-114697 |
|
|
Homo sapiens |
|
pmid |
sentence |
11818334 |
We report a novel mechanism of smad4 degradation. Jab1 interacts directly with smad4 and induces its ubiquitylation for degradation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
COPS5 | up-regulates quantity by stabilization
deubiquitination
|
CD274 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274977 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
27866850 |
The results suggested that TNF-α upregulates expression of CSN5, which interacts and deubiquitinates PD-L1 for protein stabilization. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |