+ |
AKT |
phosphorylation
|
CCT2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-244172 |
Ser260 |
GSRVRVDsTAKVAEI |
Homo sapiens |
|
pmid |
sentence |
19332537 |
Furthermore, ha-tagged akt can phosphorylate gst-cct_ protein in vitro |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPS6K | up-regulates
phosphorylation
|
CCT2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252780 |
Ser260 |
GSRVRVDsTAKVAEI |
Homo sapiens |
|
pmid |
sentence |
21440620 |
Furthermore, both the s260a and s260d mutants showed a decreased folding capacity as compared to cells expressing the wild-type cct_ subunit ( fig.?_5e), suggesting that a cyclic phosphorylation of the s260 site by s6k1 is likely to be important for chaperonin function and that mutation of this site interferes with this process. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPS6KA1 | up-regulates
phosphorylation
|
CCT2 |
0.251 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-172986 |
Ser260 |
GSRVRVDsTAKVAEI |
Homo sapiens |
|
pmid |
sentence |
21440620 |
Furthermore, both the s260a and s260d mutants showed a decreased folding capacity as compared to cells expressing the wild-type cct_ subunit ( fig.?_5e), suggesting that a cyclic phosphorylation of the s260 site by s6k1 is likely to be important for chaperonin function and that mutation of this site interferes with this process. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AKT1 |
phosphorylation
|
CCT2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-184922 |
Ser260 |
GSRVRVDsTAKVAEI |
Homo sapiens |
|
pmid |
sentence |
19332537 |
Furthermore, ha-tagged akt can phosphorylate gst-cct_ protein in vitro |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPS6KB1 |
phosphorylation
|
CCT2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-184926 |
Ser260 |
GSRVRVDsTAKVAEI |
Homo sapiens |
|
pmid |
sentence |
19332537 |
Mass spectrometry and mutagenesis analysis revealed that rsk and s6k1 phosphorylate cct_ ser-260 in vitro and in intact cells |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CCT2 | form complex
binding
|
TRiC |
0.746 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272860 |
|
|
Homo sapiens |
|
pmid |
sentence |
36185250 |
Mammalian cells contain an evolutionarily conserved type II chaperonin called chaperonin containing tailless complex polypeptide 1 (CCT) or tailless complex polypeptide 1 ring complex (TRiC). The CCT complex is composed of eight subunits [CCT1-8 (yeast) or CCTα-θ (mammals)] and folds substrates needed for cell invasion and proliferation, such as actin, tubulin, and cell division cycle protein 20 homolog (cdc20), as well as oncoproteins like signal transducer and activator of transcription 3 (STAT3), Kirsten rat sarcoma viral oncogene homolog (KRAS), and Myelocytomatosis (MYC). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |