A transcription factor which in humans consists of a complex of six protein subunits. Involved in transcription by RNA polymerase II and in nucleotide excision repair.

Any protein complex that mediates changes in chromatin structure that result in transcriptional silencing.

Any protein complex that acts in the formation of nucleosomes or higher order chromatin structure.

Catalysis of the hydrolysis of the imidazole ring of GTP, releasing formate. Two C-N bonds are hydrolyzed and the pentase unit is isomerized.

Catalysis of the reaction: GTP + 2 H2O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate.

A multiprotein complex that forms the critical link between the cytoskeleton and extracellular matrix; typical of, but not confined, to muscle cells. The constituents of the complex are somewhat tissue specific. The rod-like dystrophin forms a link between the actin cytoskeleton and the plasma membrane; links between dystrophin and the extracellular matrix are provided by the sarcoglycan complex.

Catalysis of the reaction: inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH + H+.

Includes alpha- and beta-dystroglycan; alternative products of the same gene; the laminin-binding component of the dystrophin-associated glycoprotein complex, providing a link between the subsarcolemmal cytoskeleton (in muscle cells) and the extracellular matrix. alpha-dystroglycan is an extracellular protein binding to alpha-laminin and to beta-dystroglycan; beta-dystroglycan is a transmembrane protein which binds alpha-dystroglycan and dystrophin.

Catalysis of the reaction: L-iditol + NAD+ = L-sorbose + NADH + H+.

Formed of five N-glycosylated sarcoglycans: alpha-, beta-, gamma-, delta-, and epsilon sarcoglycan, single-pass transmembrane proteins that form a complex which is fixed to the dystrophin axis by a lateral association with the dystroglycan complex.

That fraction of cells, prepared by disruptive biochemical methods, that includes the plasma and other membranes.