|
actin lateral binding
|
GO_0003786 |
[Binding to an actin filament along its length.] |
|
actin monomer binding
|
GO_0003785 |
[Binding to monomeric actin, also known as G-actin.] |
|
obsolete barbed-end actin capping/severing activity
|
GO_0003784 |
[OBSOLETE. (Was not defined before being made obsolete).] |
|
obsolete barbed-end actin capping activity
|
GO_0003783 |
[OBSOLETE. (Was not defined before being made obsolete).] |
|
obsolete F-actin capping activity
|
GO_0003782 |
[OBSOLETE. (Was not defined before being made obsolete).] |
|
obsolete actin bundling activity
|
GO_0003781 |
[OBSOLETE. (Was not defined before being made obsolete).] |
|
obsolete actin cross-linking activity
|
GO_0003780 |
[OBSOLETE. Interacting selectively with two actin filaments to anchor them together.] |
|
obsolete dynactin motor
|
GO_0003778 |
[OBSOLETE. (Was not defined before being made obsolete).] |
|
obsolete muscle motor activity
|
GO_0003776 |
[OBSOLETE. (Was not defined before being made obsolete).] |
|
obsolete axonemal motor activity
|
GO_0003775 |
[OBSOLETE. (Was not defined before being made obsolete).] |
|
obsolete heat shock protein activity
|
GO_0003773 |
[OBSOLETE. Any of a group of specific proteins that are synthesized by both prokaryotic and eukaryotic cells after they have been exposed to a temperature that is higher than normal. Other stresses, e.g. free radical damage, have a similar effect. Many members of the hsp family are not induced but are present in all cells. They are characterized by their role as molecular chaperones.] |
|
obsolete co-chaperonin activity
|
GO_0003772 |
[OBSOLETE. Co-chaperonins are proteins that bind to chaperones and this complex then folds misfolded proteins. Co-chaperonins by themselves do not possess chaperone activity.] |
|
GO_0003771
|
GO_0003771 |
|
|
GO_0003770
|
GO_0003770 |
|
|
GO_0003769
|
GO_0003769 |
|
|
GO_0003768
|
GO_0003768 |
|
|
obsolete co-chaperone activity
|
GO_0003767 |
[OBSOLETE. Co-chaperones are proteins that bind to chaperones and this complex then folds misfolded proteins. Co-chaperones by themselves do not possess chaperone activity.] |
|
GO_0003766
|
GO_0003766 |
|
|
GO_0003765
|
GO_0003765 |
|
|
GO_0003764
|
GO_0003764 |
|