+ |
PRKCB |
phosphorylation
|
ANXA2 |
0.338 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248956 |
Ser2 |
sTVHEILC |
in vitro |
|
pmid |
sentence |
8898866 |
A comparison of the phosphorylation patterns obtained identified Ser-II as the protein kinase C site responsible for regulating the annexin II-p11 interaction. Ser-II lies within the sequence mediating p11 binding, i.e. amino-acid residues 1 to 14 of annexin II, and phosphorylation at this site most likely leads to a direct spatial interference with p11 binding. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
PRKCA |
phosphorylation
|
ANXA2 |
0.363 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248892 |
Ser26 |
TPPSAYGsVKAYTNF |
Homo sapiens |
Fibroblast |
pmid |
sentence |
2946940 |
The protein-tyrosine kinase substrate p36 is also a substrate for protein kinase C in vitro and in vivo. | We present evidence suggesting that protein kinase C mediates phosphorylation of serine 25. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SRC | up-regulates
phosphorylation
|
ANXA2 |
0.564 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-127872 |
Tyr24 |
HSTPPSAyGSVKAYT |
Homo sapiens |
|
pmid |
sentence |
15302870 |
Translocation requires the presence of the annexin 2 binding partner p11 (s100a10) and the phosphorylation of annexin 2 at tyr23 through a src-like tyrosine kinase-dependent mechanism both in vitro and in vivo. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
UBAP2 | down-regulates quantity
ubiquitination
|
ANXA2 |
0.348 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261314 |
|
|
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
27121050 |
UBAP2 formed a complex with Annexin A2 and promoted the degradation of Annexin A2 protein by ubiquitination |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CBLL1 | down-regulates quantity by destabilization
ubiquitination
|
ANXA2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271473 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
31952268 |
By immunoprecipitation, we present evidence that Hakai interacts with Hsp90 chaperone complex in several epithelial cells and demonstrate that is a novel Hsp90 client protein. Interestingly, by overexpressing and knocking-down experiments with Hakai, we identified Annexin A2 as a Hakai-regulated protein. Interestingly, geldanamycin-induced Hakai degradation is accompanied by an increased expression of E-cadherin and Annexin A2. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |