Any process that modulates the frequency, rate or extent of the chemical reactions involving nucleotides.

The chemical reactions involving purine bases, one of the two classes of nitrogen-containing ring compounds found in DNA and RNA, which include adenine and guanine.

The breakdown into simpler components of purine bases, one of the two classes of nitrogen-containing ring compounds found in DNA and RNA, which include adenine and guanine.

The breakdown into simpler components of adenine, 6-aminopurine, one of the 5 main bases found in nucleic acids and a component of numerous important derivatives of its corresponding ribonucleoside, adenosine.

Interacting selectively with Ral protein, any member of the Ral subfamily of the Ras superfamily of monomeric GTPases.

Interacting selectively with an aryl hydrocarbon receptor.

negative regulator of basal transcription activity

Catalysis of the hydrolysis of dipeptides Asp-Xaa; does not act on peptides with N-terminal Glu, Asn or Gln, nor does it cleave isoaspartyl peptides.

Interacting selectively with vinculin, a protein found in muscle, fibroblasts, and epithelial cells that binds actin and appears to mediate attachment of actin filaments to integral proteins of the plasma membrane.

Catalysis of the reaction: ATP + 5-oxo-L-proline + 2 H2O = ADP + phosphate + L-glutamate.

Catalysis of the reaction: CDP + alcohol = CMP + phosphatidyl alcohol.

Interacting selectively with the enzyme DEAD/H-box RNA helicase.

Catalysis of the reaction: dicarboxylate(out) + Na+(out) = dicarboxylate(in) + Na+(in).

The release of intracellular molecules (e.g. hormones, matrix proteins) contained within a membrane-bounded vesicle by fusion of the vesicle with the plasma membrane of a cell, requiring the presence of calcium ions.

Any process that modulates the frequency, rate or extent of exocytosis.

regulation of calcium ion-dependent exocytosis

Any process that modulates the frequency, rate or extent of calcium ion-dependent exocytosis.

The chemical reactions involving peptidyl-diphthamide, a modified histidine residue.