node1 | node2 | node1 annotation | node2 annotation | score |
A0A074X3J6 | A0A074X3Z6 | F-actin-capping protein subunit beta; 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. | Cytoplasmic dynein intermediate chain. | 0.856 |
A0A074X3J6 | A0A074X5W5 | F-actin-capping protein subunit beta; 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. | Trimeric LpxA-like protein. | 0.973 |
A0A074X3J6 | A0A074XKD4 | F-actin-capping protein subunit beta; 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. | Uncharacterized protein. | 0.929 |
A0A074X3J6 | A0A074XRA1 | F-actin-capping protein subunit beta; 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. | Uncharacterized protein. | 0.976 |
A0A074X3J6 | A0A074XTX0 | F-actin-capping protein subunit beta; 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. | Ras-domain-containing protein. | 0.541 |
A0A074X3J6 | A0A074Y9Q7 | F-actin-capping protein subunit beta; 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. | CAP-Gly domain-containing protein. | 0.972 |
A0A074X3J6 | A0A074YCI8 | F-actin-capping protein subunit beta; 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. | Dynein heavy chain. | 0.856 |
A0A074X3J6 | A0A074YEV9 | F-actin-capping protein subunit beta; 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. | Robl_LC7 domain-containing protein. | 0.598 |
A0A074X3J6 | A0A074YJH3 | F-actin-capping protein subunit beta; 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. | Dynein light chain; Acts as one of several non-catalytic accessory components of the cytoplasmic dynein complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures. | 0.775 |
A0A074X3Z6 | A0A074X3J6 | Cytoplasmic dynein intermediate chain. | F-actin-capping protein subunit beta; 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. | 0.856 |
A0A074X3Z6 | A0A074X5W5 | Cytoplasmic dynein intermediate chain. | Trimeric LpxA-like protein. | 0.907 |
A0A074X3Z6 | A0A074XKD4 | Cytoplasmic dynein intermediate chain. | Uncharacterized protein. | 0.985 |
A0A074X3Z6 | A0A074XRA1 | Cytoplasmic dynein intermediate chain. | Uncharacterized protein. | 0.988 |
A0A074X3Z6 | A0A074XRG5 | Cytoplasmic dynein intermediate chain. | Dynein light chain, cytosolic. | 0.998 |
A0A074X3Z6 | A0A074Y9Q7 | Cytoplasmic dynein intermediate chain. | CAP-Gly domain-containing protein. | 0.983 |
A0A074X3Z6 | A0A074YCI8 | Cytoplasmic dynein intermediate chain. | Dynein heavy chain. | 0.995 |
A0A074X3Z6 | A0A074YEV9 | Cytoplasmic dynein intermediate chain. | Robl_LC7 domain-containing protein. | 0.998 |
A0A074X3Z6 | A0A074YJH3 | Cytoplasmic dynein intermediate chain. | Dynein light chain; Acts as one of several non-catalytic accessory components of the cytoplasmic dynein complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures. | 0.993 |
A0A074X5W5 | A0A074X3J6 | Trimeric LpxA-like protein. | F-actin-capping protein subunit beta; 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. | 0.973 |
A0A074X5W5 | A0A074X3Z6 | Trimeric LpxA-like protein. | Cytoplasmic dynein intermediate chain. | 0.907 |