Any macromolecular complex involved in cleavage or polyadenylation of mRNA molecules.

Catalysis of the transfer of an acetyl group to a nitrogen atom on the acceptor molecule.

A ribosome found in the cytosol; this term can also be used to refer to ribosomes associated with the endoplasmic reticulum in eukaryotic cells. As in, but not restricted to, the eukaryotes (Eukaryota, ncbi_taxonomy_id:2759).

Catalysis of the reaction: ATP + biotin + protein = AMP + diphosphate + biotin-protein.

Catalysis of the hydrolysis of a phosphodiester to give a phosphomonoester and a free hydroxyl group.

The function that stimulates a cell to grow or proliferate. Most growth factors have other actions besides the induction of cell growth or proliferation.

An iron-containing, oxygen carrying complex. In vertebrates it is made up of two pairs of associated globin polypeptide chains, each chain carrying a noncovalently bound heme prosthetic group.

Any of a family of heterotrimeric GTP-binding and hydrolyzing proteins; they belong to a superfamily of GTPases that includes monomeric proteins such as EF-Tu and RAS. Heterotrimeric G-proteins consist of three subunits; the alpha subunit contains the guanine nucleotide binding site and possesses GTPase activity; the beta and gamma subunits are tightly associated and function as a beta-gamma heterodimer; extrinsic plasma membrane proteins (cytoplasmic face) that function as a complex to transduce signals from G-protein coupled receptors to an effector protein.

The directed movement of organelles along microtubules in nerve cell axons.

proteasome regulatory particle (sensu Eukaryota)

A multisubunit complex, which caps one or both ends of the proteasome core complex. This complex recognizes, unfolds ubiquitinated proteins and translocates them to the proteasome core complex. As in, but not restricted to, the eukaryotes (Eukaryota, ncbi_taxonomy_id:2759).

protein amino acid N-linked glycosylation via asparagine

The posttranslational 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 also occurs; 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.