TBCE Antibody – Rabbit Polyclonal

Cofactor E is one of four proteins (cofactors A, D, E, and C) involved in the pathway leading to correctly folded beta-tubulin from folding intermediates. Cofactors A and D are believed to play a role in capturing and stabilizing beta-tubulin intermediates in a quasi-native confirmation. Cofactor E binds to the cofactor D/beta-tubulin complex; interaction with cofactor C then causes the release of beta-tubulin polypeptides that are committed to the native state. Two transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008]

Function: Tubulin-folding protein; involved in the second step of the tubulin folding pathway. Seems to be implicated in the maintenance of the neuronal microtubule network. Involved in regulation of tubulin heterodimer dissociation. Ref.5

Subunit structure: Supercomplex made of cofactors A to E. Cofactors A and D function by capturing and stabilizing tubulin in a quasi-native conformation. Cofactor E binds to the cofactor D-tubulin complex; interaction with cofactor C then causes the release of tubulin polypeptides that are committed to the native state. Cofactors B and E can form a heterodimer which binds to alpha-tubulin and enhances their ability to dissociate tubulin heterodimers.

Subcellular location: Cytoplasm

By similarity. Cytoplasm › cytoskeleton

By similarity.

Involvement in disease: Hypoparathyroidism-retardation-dysmorphism syndrome (HRD) [MIM:241410]: Autosomal recessive disorder reported almost exclusively in Middle Eastern populations.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10Kenny-Caffey syndrome 1 (KCS1) [MIM:244460]: An autosomal recessive form of Kenny-Caffey syndrome, a disorder characterized by impaired skeletal development with small and dense bones, short stature, and primary hypoparathyroidism with hypocalcemia. Clinical features include cortical thickening and medullary stenosis of the tubular bones, delayed closure of fontanels, defective dentition, small eyes with hypermetropia, and frontal bossing with a triangular face.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10

Sequence similarities: Belongs to the TBCE family.Contains 1 CAP-Gly domain.Contains 7 LRR (leucine-rich) repeats.Contains 1 LRRCT domain.