+ |
CSNK2A1 |
phosphorylation
|
PSMA3 |
0.389 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250938 |
Ser243 |
AEKYAKEsLKEEDES |
in vitro |
|
pmid |
sentence |
8619999 |
Several C8 protein constructs allow the location of the CKII phosphorylation sites to be the COOH terminal portion of the protein, and direct mutational analyses show that Ser-243 and Ser-250 are the residues of the C8 subunit phosphorylated by CKII. The in vitro phosphorylation of the proteasome by CKII does not affect its proteolytic activity (on proteins or fluorogenic synthetic peptides), therefore suggesting its involvement in the interaction of the proteasome with other cellular proteins, i.e. in the formation of the 26S complex and/or in the interaction with the nuclear translocation machinery. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250939 |
Ser250 |
SLKEEDEsDDDNM |
in vitro |
|
pmid |
sentence |
8619999 |
Several C8 protein constructs allow the location of the CKII phosphorylation sites to be the COOH terminal portion of the protein, and direct mutational analyses show that Ser-243 and Ser-250 are the residues of the C8 subunit phosphorylated by CKII. The in vitro phosphorylation of the proteasome by CKII does not affect its proteolytic activity (on proteins or fluorogenic synthetic peptides), therefore suggesting its involvement in the interaction of the proteasome with other cellular proteins, i.e. in the formation of the 26S complex and/or in the interaction with the nuclear translocation machinery. |
|
Publications: |
2 |
Organism: |
In Vitro |
+ |
PSMA3 | form complex
binding
|
26S Proteasome |
0.846 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263362 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
29636472 |
Here, we report near-atomic resolution cryo-EM structures of the activated human proteasome|The proteasome is composed of a 28-subunit barrel-shaped core particle (CP) and two 19- subunit regulatory particles (RP)5–8 capped at both sides of the CP|Human proteasomes were purified through affinity chromatography on a large scale from a stable HEK293 cell line |
|
Publications: |
1 |
Organism: |
Homo Sapiens |