|
obsolete [pyruvate dehydrogenase (lipoamide)] phosphatase regulator activity
|
GO_0019909 |
[OBSOLETE. Binds to and modulates of the activity of [pyruvate dehydrogenase (lipoamide)] phosphatase.] |
|
kinase binding
|
GO_0019900 |
[Binding to a kinase, any enzyme that catalyzes the transfer of a phosphate group.] |
|
phosphatase binding
|
GO_0019902 |
[Binding to a phosphatase.] |
|
obsolete peptidyl-D-alanine racemization via peptidyl-L-serine
|
GO_0019917 |
[OBSOLETE. The dehydration of peptidyl-serine, followed by hydrogenation to produce peptidyl-D-alanine.] |
|
peptidyl-arginine methylation, to symmetrical-dimethyl arginine
|
GO_0019918 |
[The process of methylation of peptidyl-arginine to form peptidyl-N(omega),N'(omega)-dimethyl-L-arginine.] |
|
peptidyl-arginine methylation, to asymmetrical-dimethyl arginine
|
GO_0019919 |
[The process of methylation of peptidyl-arginine to form peptidyl-N(omega),N(omega)-dimethyl-L-arginine.] |
|
mitochondrial pyruvate dehydrogenase (lipoamide) phosphatase complex
|
GO_0019910 |
[A mitochondrial complex of a regulatory and catalytic subunit that catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex. An example of this component is found in Mus musculus.] |
|
structural constituent of myelin sheath
|
GO_0019911 |
[The action of a molecule that contributes to the structural integrity of the myelin sheath of a nerve.] |
|
obsolete cyclin-dependent protein kinase activating kinase activity
|
GO_0019912 |
[OBSOLETE. Catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein; increases the activity of a cyclin-dependent protein kinase (CDK).] |
|
GO_0019913
|
GO_0019913 |
|
|
cyclin-dependent protein kinase regulator activity
|
GO_0019914 |
[Modulation of the activity of the enzyme cyclin-dependent protein kinase activating kinase.] |
|
nutrient storage
|
GO_0170062 |
[The accumulation and maintenance in cells or tissues of a nutrient, a substance that is used by an organism to survive, to grow, and to reproduce; such as proteins, vitamins, and minerals. Nutrient reserves can be accumulated for mobilization and utilization when needed.] |
|
obsolete peptidyl-D-alanine racemization, direct
|
GO_0019916 |
[OBSOLETE. The racemization of peptidyl-alanine.] |
|
obsolete peptide cross-linking via 3-(S-L-cysteinyl)-L-aspartic acid
|
GO_0019928 |
[OBSOLETE. The cross-linking of a cysteine residue to an aspartic acid residue to form 3-(S-L-cysteinyl)-L-aspartic acid.] |
|
obsolete peptide cross-linking via 4-(S-L-cysteinyl)-L-glutamic acid
|
GO_0019929 |
[OBSOLETE. The cross-linking of a cysteine residue to a glutamic acid residue to form 4-(S-L-cysteinyl)-L-glutamic acid.] |
|
obsolete peptidyl-1-thioglycine biosynthetic process, internal
|
GO_0019920 |
[OBSOLETE. The chemical reactions and pathways resulting in the formation of internal peptidyl-1-thioglycine, which has an internal C=S bond, instead of an internal C=O bond, in the peptide.] |
|
obsolete peptidyl-1-thioglycine biosynthetic process, carboxy-terminal
|
GO_0019921 |
[OBSOLETE. The chemical reactions and pathways resulting in the formation of carboxy-terminal peptidyl-1-thioglycine, which has a carboxy-terminal thiocarboxy-C(=O)-SH bond.] |
|
obsolete protein-chromophore linkage via peptidyl-cysteine
|
GO_0019922 |
[OBSOLETE. The covalent linking of a chromophore to a protein via peptidyl-cysteines.] |
|
obsolete alpha-1-microglobulin-chromophore linkage
|
GO_0019923 |
[OBSOLETE. The covalent linking of the alpha-1-microglobulin chromophore to the protein; the structure of the chromophore is not known. It is probably heterogeneous and involving two cysteines in thioether bonds.] |
|
GO_0019924
|
GO_0019924 |
|