Summary
| Name | CAPZA1View Modifications |
| Full Name | F-actin-capping protein subunit alpha-1 |
| Synonyms | CapZ alpha-1 |
| Primary ID | P52907 |
| Links | - - ![]() |
| Type | protein |
| Relations | 5 |
| Inhibitors | phosphatidylinositol bisphosphate; 1D-myo-inositol 1,4,5-trisphosphate |
| Function | F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. May play a role in the formation of epithelial cell junctions. |
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Modifications Tables
Relations
| Regulator | Mechanism | target | score ℹ | |
|---|---|---|---|---|
| + | CSNK2A1 | up-regulates
phosphorylation
|
CAPZA1 | 0.2 |
| Publications: | 1 | Organism: | Homo Sapiens | |
| + | RCSD1 | up-regulates
binding
|
CAPZA1 | 0.665 |
| Publications: | 1 | Organism: | In Vitro | |
| + | phosphatidylinositol bisphosphate | down-regulates activity
chemical inhibition
|
CAPZA1 | 0.8 |
| Publications: | 1 | Organism: | Homo Sapiens | |
| + | CAPZA1 | up-regulates quantity
binding
|
F-actin_assembly | 0.7 |
| Publications: | 1 | Organism: | Homo Sapiens | |
| + | 1D-myo-inositol 1,4,5-trisphosphate | down-regulates activity
chemical inhibition
|
CAPZA1 | 0.8 |
| Publications: | 1 | Organism: | Homo Sapiens | |
4.0
CAPZA1


phosphorylation
chemical inhibition