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.
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.
2'-deoxyadenosine deaminase activity GO_0046936
Catalysis of the reaction: 2'-deoxyadenosine + H2O = deoxyinosine + NH3.
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.