A heteromeric complex of flotillin 1, flotillin 2, caveolin 1 and caveolin 2 within the caveolar membrane.

The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of component monomers; protein oligomers may be composed of different or identical monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.

Interacting selectively with a tetratricopeptide repeat (TPR) domain of a protein, the consensus sequence of which is defined by a pattern of small and large hydrophobic amino acids and a structure composed of helices.

A series of molecular signals within the cell that are mediated by a member of the Rac family of proteins switching to a GTP-bound active state.

A heteromeric transcription factor complex that binds to the CCAAT-box upstream of promoters; in Saccharomyces it activates the transcription of genes in response to growth in a nonfermentable carbon source; consists of four known subunits: HAP2, HAP3, HAP4 and HAP5.

Formation of the junction between an axon and the glial cell that forms the myelin sheath. Paranodal junctions form at each paranode, i.e. at the ends of the unmyelinated nodes of Ranvier.

A ribosome contained within a subcellular organelle.

The chemical reactions involving pyrimidine ribonucleoside monophosphate, a glycosamine consisting of a pyrimidine base linked to a ribose sugar esterified with phosphate on its glycose moiety.

Catalysis of the reaction: L-glutaminyl-peptide = 5-oxoprolyl-peptide + NH3.

Located in a membrane such that some covalently attached portion of the gene product spans or is embedded in one or both leaflets of the membrane.

The smaller of the two subunits of an organellar ribosome.

The formation from simpler components of pyrimidine ribonucleoside monophosphate, a glycosamine consisting of a pyrimidine base linked to a ribose sugar esterified with phosphate on its glycose moiety.

Extra-nucleolar nuclear domains usually visualized by confocal microscopy and fluorescent antibodies to specific proteins.