Summary
Name | CAPZA1 View Modifications |
Full Name | F-actin-capping protein subunit alpha-1 |
Synonyms | CapZ alpha-1 |
Primary ID | P52907 |
Links | - - |
Type | protein |
Relations | 5 |
Inhibitors | 1D-myo-inositol 1,4,5-trisphosphate; phosphatidylinositol bisphosphate |
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. |
Viewer
Search Tools
Refine search:
- by mechanism
- by effect
- by organism:
- by tissue:
- by cell-line
Modifications Tables
Relations
Regulator | Mechanism | target | score ℹ | |
---|---|---|---|---|
+ | CSNK2A1 | up-regulates phosphorylation | CAPZA1 | 0.2 |
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 | |
+ | phosphatidylinositol bisphosphate | down-regulates activity chemical inhibition | CAPZA1 | 0.8 |
Publications: | 1 | Organism: | Homo Sapiens | |
+ | RCSD1 | up-regulates binding | CAPZA1 | 0.689 |
Publications: | 1 | Organism: | In Vitro | |