All terms in GO
| Label | Id | Description |
|---|---|---|
| obsolete unilateral process | GO_0007337 |
OBSOLETE. (Was not defined before being made obsolete).
|
| phosphatidylinositol-4,5-bisphosphate 3-kinase activity | GO_0046934 |
Catalysis of the reaction: 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + ATP = a 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + ADP + 2 H(+).
|
| phosphatidylinositol bisphosphate kinase activity | GO_0052813 |
Catalysis of the reaction: ATP + a phosphatidylinositol bisphosphate = ADP + a phosphatidylinositol trisphosphate.
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| obsolete bilateral process | GO_0007336 |
OBSOLETE. (Was not defined before being made obsolete).
|
| proton-transporting ATP synthase activity, rotational mechanism | GO_0046933 |
Enables the synthesis of ATP from ADP and phosphate by the transfer of protons from one side of a membrane to the other by a rotational mechanism driven by a gradient according to the reaction: ADP + H2O + phosphate + H+(in) -> ATP + H+(out).
|
| binding of sperm to zona pellucida | GO_0007339 |
The process in which the sperm binds to the zona pellucida glycoprotein layer of the egg. The process begins with the attachment of the sperm plasma membrane to the zona pellucida and includes attachment of the acrosome inner membrane to the zona pellucida after the acrosomal reaction takes place.
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| 2'-deoxyadenosine deaminase activity | GO_0046936 |
Catalysis of the reaction: 2'-deoxyadenosine + H2O = deoxyinosine + NH3.
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| single fertilization | GO_0007338 |
The union of male and female gametes to form a zygote.
|
| 1-phosphatidylinositol-3-kinase regulator activity | GO_0046935 |
Modulates the activity of the enzyme 1-phosphatidylinositol-3-kinase activity.
|
| GO_0140160 | GO_0140160 | |
| phytochelatin biosynthetic process | GO_0046938 |
The chemical reactions and pathways resulting in the formation of phytochelatins, any of a group of peptides that bind metals (Cd, Zn, Cu, Pb, Hg) in thiolate coordination complexes. The structure is of the type (gamma-glutamyl-cysteinyl)n-glycine, where n is 2 to 11.
|
| phytochelatin metabolic process | GO_0046937 |
The chemical reactions and pathways involving phytochelatins, any of a group of peptides that bind metals (Cd, Zn, Cu, Pb, Hg) in thiolate coordination complexes. The structure is of the type (gamma-glutamyl-cysteinyl)n-glycine, where n is 2 to 11.
|
| sodium-transporting ATP synthase activity, rotational mechanism | GO_0046932 |
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ADP + phosphate + Na+(out) => ATP + H2O + Na+(in), by a rotational mechanism.
|
| pore complex assembly | GO_0046931 |
The aggregation, arrangement and bonding together of a set of components to form a pore complex. A pore complex is a small opening in a membrane that allows the passage of liquids and/or gases.
|
| protein N-linked N-acetylglucosaminylation via asparagine | GO_0071903 |
A process of protein N-linked glycosylation via asparagine in which N-acetylglucosamine is added to the N4 of asparagine, forming an (S)-2-amino-4-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)amino-4-oxobutanoic acid residue.
|
| protein N-linked glycosylation via asparagine | GO_0018279 |
The glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine and N4 glucosyl asparagine also occur. This modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.
|
| protein N-linked glucosylation via asparagine | GO_0071905 |
A process of protein N-linked glycosylation via asparagine in which glucose is added to the N4 of asparagine, forming an (S)-2-amino-4-(D-glucopyranosyl)amino-4-oxobutanoic acid residue.
|
| protein N-linked N-acetylgalactosaminylation via asparagine | GO_0071904 |
A process of protein N-linked glycosylation via asparagine in which N-acetylgalactosamine is added to the N4 of asparagine, forming an (S)-2-amino-4-(2-acetamido-2-deoxy-beta-D-galactopyranosyl)amino-4-oxobutanoic acid residue.
|
| determination of digestive tract left/right asymmetry | GO_0071907 |
Determination of the asymmetric location of various parts of the digestive tract with respect to the left and right halves of the organism. The digestive tract is the anatomical structure through which food passes and is processed.
|
| CRD domain binding | GO_0071906 |
Binding to a CRD (context dependent regulatory) domain, a domain of about 130 residues that is the most divergent region among the LEF/TCF proteins.
|