All terms in GO
| Label | Id | Description |
|---|---|---|
| P-type zinc transporter activity | GO_0016463 |
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Zn2+(in) -> ADP + phosphate + Zn2+(out).
|
| GO_0016478 | GO_0016478 | |
| detection of nuclear:cytoplasmic ratio | GO_0016475 |
The process in which the size of the nucleus with respect to its cytoplasm is sensed by a cell.
|
| sodium ion-transporting V-type ATPase complex | GO_0016474 |
A sodium ion-transporting two-sector ATPase complex that couples ATP hydrolysis to the transport of sodium ions across a concentration gradient. The complex comprises a membrane sector (V0) that carries out proton transport and a cytoplasmic compartment sector (V1) that catalyzes ATP hydrolysis.
|
| sodium ion-transporting two-sector ATPase complex | GO_0016472 |
A large protein complex that catalyzes the synthesis or hydrolysis of ATP by a rotational mechanism, coupled to the transport of sodium ions across a membrane. The complex comprises a membrane sector (F0 or V0) that carries out ion transport and a cytoplasmic compartment sector (F1 or V1) that catalyzes ATP synthesis or hydrolysis.
|
| sodium ion-transporting F-type ATPase complex | GO_0016473 |
A sodium ion-transporting two-sector ATPase complex that catalyzes the phosphorylation of ADP to ATP. The complex comprises a membrane sector (F0) that carries out proton transport and a cytoplasmic compartment sector (F1) that catalyzes ATP synthesis by a rotational mechanism.
|
| GO_0016470 | GO_0016470 | |
| nuclear matrix | GO_0016363 |
The dense fibrillar network lying on the inner side of the nuclear membrane.
|
| activin receptor activity, type II | GO_0016362 |
Combining with activin to initiate a change in cell activity; upon ligand binding, binds to and catalyses the phosphorylation of a type I activin receptor.
|
| activin receptor activity, type I | GO_0016361 |
Combining with activin-bound type II activin receptor to initiate a change in cell activity; upon binding, acts as a downstream transducer of activin signals.
|
| sensory organ precursor cell fate determination | GO_0016360 |
The process in which a cell becomes capable of differentiating autonomously into a sensory organ precursor cell regardless of its environment; upon determination, the cell fate cannot be reversed.
|
| mRNA export from nucleus in response to heat stress | GO_0031990 |
The directed movement of mRNA from the nucleus to the cytoplasm during a heat stimulus, a temperature stimulus above the optimal temperature for the organism; in particular, a process that enables an organism withstand exposure to temperatures that would otherwise lethally impair poly(A)+ mRNA-nucleus export.
|
| energy transducer activity | GO_0031992 |
The biological transducer activity that accepts energy and converts it to another form, often by transfer to another molecule within the cell.
|
| regulation of actomyosin contractile ring contraction | GO_0031991 |
Any process that modulates the frequency, rate or extent of contraction of the actomyosin ring involved in cytokinesis that takes place as part of a cell cycle.
|
| insulin-like growth factor I binding | GO_0031994 |
Binding to insulin-like growth factor I.
|
| light transducer activity | GO_0031993 |
Absorbing energy from one or more photons and transferring their energy to another molecule, usually a protein, within the cell.
|
| thioesterase binding | GO_0031996 |
Binding to a thioesterase.
|
| insulin-like growth factor II binding | GO_0031995 |
Binding to insulin-like growth factor II.
|
| N-terminal myristoylation domain binding | GO_0031997 |
Binding to the N-terminus of a protein that has the potential to be, or has been, modified by N-terminal myristoylation. Binding affinity is typically altered by myristoylation; for example, N-terminal myristoylation of HIV Nef increases its affinity for calmodulin.
|
| protein N-terminus binding | GO_0047485 |
Binding to a protein N-terminus, the end of any peptide chain at which the 2-amino (or 2-imino) function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue.
|