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Any constituent part of the cytoplasm, all of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. Any macromolecular complex composed of two or more polypeptide subunits, which may or may not be identical. Protein complexes may have other associated non-protein prosthetic groups, such as nucleotides, metal ions or other small molecules. All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. A heterodimeric enzyme complex, which in mammals is composed of an alpha and a beta subunit, and which associates with an accessory protein Rep (Rab escort protein). Catalyzes of the transfer of a geranyl-geranyl moiety from geranylgeranyl pyrophosphate to a Rab protein. A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which the constituent parts function together. Any constituent part of the living contents of a cell; the matter contained within (but not including) the plasma membrane, usually taken to exclude large vacuoles and masses of secretory or ingested material. In eukaryotes it includes the nucleus and cytoplasm.

View Gene Ontology (GO) Term

GO TERM SUMMARY

Name: Rab-protein geranylgeranyltransferase complex
Acc: GO:0005968
Aspect: Cellular Component
Desc: A heterodimeric enzyme complex, which in mammals is composed of an alpha and a beta subunit, and which associates with an accessory protein Rep (Rab escort protein). Catalyzes of the transfer of a geranyl-geranyl moiety from geranylgeranyl pyrophosphate to a Rab protein.
Synonyms:
  • RabGGTase complex
  • RAB-protein geranylgeranyltransferase complex
  • Rab geranylgeranyltransferase complex
  • GGTase-II complex
Proteins in PDR annotated with:
   This term: 16 [Search]
   Term or descendants: 16 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0005968 - Rab-protein geranylgeranyltransferase complex (interactive image map)

YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle