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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. A protein complex required for sister chromatid cohesion in eukaryotes. A structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information. A cohesin complex that mediates sister chromatid cohesion during meiosis; has a subunit composition distinct from that of the mitotic cohesin complex. The core heterodimer of a cohesin complex; a structure required for sister chromatid cohesion in eukaryotes. A cohesin complex required for cohesion between sister chromatids that remain in the nucleus. A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which the constituent parts function together. A cohesin complex that mediates sister chromatid cohesion during mitosis; has a subunit composition distinct from that of the meiotic cohesin complex. A constituent part of an intracellular organelle, an organized structure of distinctive morphology and function, occurring within the cell. Includes constituent parts of the nucleus, mitochondria, plastids, vacuoles, vesicles, ribosomes and the cytoskeleton but excludes the plasma membrane. Any constituent part of a chromosome, a structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information.

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: cohesin complex
Acc: GO:0008278
Aspect: Cellular Component
Desc: A protein complex required for sister chromatid cohesion in eukaryotes.
Synonyms:
  • GO:0008279
  • SMC complex
  • 14S cohesin
Proteins in PDR annotated with:
   This term: 28 [Search]
   Term or descendants: 51 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0008278 - cohesin complex (interactive image map)
YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle