| + |
PRKACA | down-regulates activity 
phosphorylation
|
ADD1 |
0.316 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250329 |
Ser408 |
REKSKKYsDVEVPAS |
in vitro |
|
| pmid |
sentence |
| 8810272 |
Protein kinase A phosphorylates -adducin at three sites in the neck domain (Ser-408, ’436, and ’481) in addition to the MARCKS-related domain of both subunits. Phosphorylation by PKA, in contrast to PKC, reduced affinity of erythrocyte adducin for spectrin-F-actin complexes as well as activity of adducin in promoting binding of spectrin to F-actin. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250330 |
Ser436 |
TCSPLRHsFQKQQRE |
in vitro |
|
| pmid |
sentence |
| 8810272 |
Protein kinase A phosphorylates -adducin at three sites in the neck domain (Ser-408, ’436, and ’481) in addition to the MARCKS-related domain of both subunits. Phosphorylation by PKA, in contrast to PKC, reduced affinity of erythrocyte adducin for spectrin-F-actin complexes as well as activity of adducin in promoting binding of spectrin to F-actin. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250331 |
Ser481 |
KEDGHRTsTSAVPNL |
in vitro |
|
| pmid |
sentence |
| 8810272 |
Protein kinase A phosphorylates -adducin at three sites in the neck domain (Ser-408, ’436, and ’481) in addition to the MARCKS-related domain of both subunits. Phosphorylation by PKA, in contrast to PKC, reduced affinity of erythrocyte adducin for spectrin-F-actin complexes as well as activity of adducin in promoting binding of spectrin to F-actin. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
PRKCA | up-regulates 
phosphorylation
|
ADD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-43744 |
Ser726 |
KKKFRTPsFLKKSKK |
Homo sapiens |
|
| pmid |
sentence |
| 8810272 |
These data demonstrate that adducin is a significant in vivo substrate for pkc or other pma-activated kinases in a variety of cells, and that phosphorylation of adducin occurs in dendritic spines that are believed to respond to external signals by changes in morphology and reorganization of cytoskeletal structures. 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 common for pka and pkc. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-59229 |
Ser726 |
KKKFRTPsFLKKSKK |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 9679146 |
These data demonstrate that adducin is a significant in vivo substrate for pkc or other pma-activated kinases in a variety of cells, and that phosphorylation of adducin occurs in dendritic spines that are believed to respond to external signals by changes in morphology and reorganization of cytoskeletal structures. 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 common for pka and pkc. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney |
| + |
PRKCZ | up-regulates
phosphorylation
|
ADD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-59303 |
Ser726 |
KKKFRTPsFLKKSKK |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 9679146 |
These data demonstrate that adducin is a significant in vivo substrate for pkc or other pma-activated kinases in a variety of cells, and that phosphorylation of adducin occurs in dendritic spines that are believed to respond to external signals by changes in morphology and reorganization of cytoskeletal structures. 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 common for pka and pkc. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-43834 |
Ser726 |
KKKFRTPsFLKKSKK |
Homo sapiens |
|
| pmid |
sentence |
| 8810272 |
These data demonstrate that adducin is a significant in vivo substrate for pkc or other pma-activated kinases in a variety of cells, and that phosphorylation of adducin occurs in dendritic spines that are believed to respond to external signals by changes in morphology and reorganization of cytoskeletal structures. 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 common for pka and pkc. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney |
| + |
ROCK1 | up-regulates
phosphorylation
|
ADD1 |
0.384 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-66992 |
Thr445 |
QKQQREKtRWLNSGR |
Homo sapiens |
|
| pmid |
sentence |
| 10209029 |
Rho-associated kinase (rho- kinase), which is activated by the small guanosine triphosphatase rho, phosphorylates alpha-adducin and thereby enhances the f-actin-binding activity of alpha-adducin in vitro. Here we identified the sites of phosphorylation of alpha-adducin by rho-kinase as thr445 and thr480 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-66996 |
Thr480 |
TKEDGHRtSTSAVPN |
Homo sapiens |
|
| pmid |
sentence |
| 10209029 |
Rho-associated kinase (rho- kinase), which is activated by the small guanosine triphosphatase rho, phosphorylates alpha-adducin and thereby enhances the f-actin-binding activity of alpha-adducin in vitro. Here we identified the sites of phosphorylation of alpha-adducin by rho-kinase as thr445 and thr480 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney |
| + |
CDK5 | up-regulates activity
phosphorylation
|
ADD1 |
0.258 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277487 |
Thr724 |
KKKKKFRtPSFLKKS |
Homo sapiens |
MDA-MB-231 Cell |
| pmid |
sentence |
| 31548578 |
We found that Cdk5 directly phosphorylated the actin-binding protein adducin-1 (ADD1) at T724 in vitro and in intact cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ADD1 | form complex 
binding
|
4.1 complex |
0.341 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266037 |
|
|
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
ADD1
- 
- 