Annotation inferences using phylogenetic trees
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
Towards a proteome-scale map of the human protein-protein interaction network.
Functional analysis of disease-causing mutations in human UDP-galactose 4-epimerase.
-
Human GALE (EC 5.1.3.2) catalyses the interconversion of UDP-glucose and UDP-galactose; disease-causing mutations reduce catalytic efficiency and increase proteolytic susceptibility, causing type III galactosemia.
"UDP-galactose 4-epimerase (GALE, EC 5.1.3.2) catalyses the interconversion of UDP-glucose and UDP-galactose."
-
GALE forms a homodimer; disease mutations do not impair homodimer formation.
"Protein-protein crosslinking suggests that none of the mutants are impaired in homodimer formation."
A proteome-scale map of the human interactome network.
A massively parallel pipeline to clone DNA variants and examine molecular phenotypes of human disease mutations.
Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.
A reference map of the human binary protein interactome.
Defective GALE does not epimerise UDP-Gal to UDP-Glc
GALE:NAD+ dimer reversibly epimerises UDP-Gal to UDP-Glc
-
Cytosolic GALE catalyses the interconversion of UDP-D-galactose and UDP-D-glucose; the active enzyme is a homodimer with one molecule of bound NAD+ per monomer.
"The active form of the enzyme is a homodimer with one molecule of bound NAD+ per monomer"
Crystallographic evidence for Tyr 157 functioning as the active site base in human UDP-galactose 4-epimerase.