| + |
PRKCZ | down-regulates 
phosphorylation
|
ADD2 |
0.279 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-139914 |
Ser713 |
KKKFRTPsFLKKSKK |
Homo sapiens |
|
| pmid |
sentence |
| 16116087 |
We now demonstrate that ptn stimulates the phosphorylation of serines 713 and 726 in the myristoylated alanine-rich protein kinase (pk) c substrate domain of beta-adducin through activation of either pkc alpha or beta. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCA | down-regulates
phosphorylation
|
ADD2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-59299 |
Ser713 |
KKKFRTPsFLKKSKK |
Homo sapiens |
|
| pmid |
sentence |
| 9679146 |
Pkc phosphorylation of native and recombinant adducin inhibited actin capping measured using pyrene-actin polymerization and abolished activity of adducin in recruiting spectrin to ends and sides of actin filaments |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-139870 |
Ser713 |
KKKFRTPsFLKKSKK |
Homo sapiens |
|
| pmid |
sentence |
| 16116087 |
We now demonstrate that ptn stimulates the phosphorylation of serines 713 and 726 in the myristoylated alanine-rich protein kinase (pk) c substrate domain of beta-adducin through activation of either pkc alpha or beta. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCD |
phosphorylation
|
ADD2 |
0.288 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248952 |
Ser713 |
KKKFRTPsFLKKSKK |
in vitro |
|
| pmid |
sentence |
| 8810272 |
Ser-726 and Ser-713 in the C-terminal MARCKS-related domains of alpha- and beta-adducin, respectively, were identified as the major phosphorylation sites for PKC. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248953 |
Ser726 |
KKKEKVEs |
in vitro |
|
| pmid |
sentence |
| 8810272 |
Ser-726 and Ser-713 in the C-terminal MARCKS-related domains of alpha- and beta-adducin, respectively, were identified as the major phosphorylation sites for PKC. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PRKACA | down-regulates activity
phosphorylation
|
ADD2 |
0.286 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250332 |
Ser713 |
KKKFRTPsFLKKSKK |
in vitro |
|
| pmid |
sentence |
| 8810272 |
Ser-726 and Ser-713 in the C-terminal MARCKS-related domains of - and -adducin, respectively, were identified as the major phosphorylation sites common for PKA and PKC. Phosphorylation by PKA, but not PKC, reduced the affinity of adducin for spectrin-F-actin complexes as well as the activity of adducin in promoting binding of spectrin to F-actin. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250333 |
Ser726 |
KKKEKVEs |
in vitro |
|
| pmid |
sentence |
| 8810272 |
Ser-726 and Ser-713 in the C-terminal MARCKS-related domains of - and -adducin, respectively, were identified as the major phosphorylation sites common for PKA and PKC. Phosphorylation by PKA, but not PKC, reduced the affinity of adducin for spectrin-F-actin complexes as well as the activity of adducin in promoting binding of spectrin to F-actin. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
ADD2 | form complex 
binding
|
4.1 complex |
0.377 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266039 |
|
|
Homo sapiens |
Erythrocyte |
| pmid |
sentence |
| 33187473 |
The cytoskeleton plays a key role in maintaining the morphology and function of erythrocyte membranes. Many proteins, such as ankyrin, spectrin alpha- and beta-chains, proteins 4.1, or 4.1R and actin, cover the inner surface of the erythrocyte membrane to form two protein complexes, the ankyrin and protein 4.1 complex| the latter consists of Band 3 dimers binding Adducins alpha and beta, Glycophorin C, GLUT1 and Stomatin [15, 16] |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
ADD2
- 
- 