A homozygous mutation in the UBE3B gene was found to segregate perfectly with disease in a multiplex ASD family. No homozygotes for this mutation were observed in 1344 control chromosomes. An additional compound heterozygous mutation in the UBE3B gene was identified in one ASD case from the replication cohort that was not observed in 371 controls (Chahrour et al., 2012).
Molecular Function
The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: E1 ubiquitin-activating enzymes, E2 ubiquitin-conjugating enzymes, and E3 ubiquitin-protein ligases. This gene encodes a member of the E3 ubiquitin-conjugating enzyme family which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme and transfers the ubiquitin to the targeted substrates. A HECT (homology to E6-AP C-terminus) domain in the C-terminus of the longer isoform of this protein is the catalytic site of ubiquitin transfer and forms a complex with E2 conjugases.
External Links
References
Type
Title
Type of Disorder
Associated Disorders
Author, Year
Primary
Whole-exome sequencing and homozygosity analysis implicate depolarization-regulated neuronal genes in autism.
Blepharophimosis-ptosis-intellectual disability syndrome: A report of nine Egyptian patients with further expansion of phenotypic and mutational spectrum
Model Type:
Genetic
Model Genotype:
Homozygous
Mutation:
Blastocyst injection of mutant embryonic stem cells obtained from BayGenomics gene trap ESC clone RRJ142.
Allele Type: Targeted (Knock Out)
Strain of Origin: Not specified
Genetic Background: 129P2/Ola x CBA/Ca
ES Cell Line: Not specified
Mutant ES Cell Line: Not Specified
Model Source: Not Specified
Description: Abnormal eye morphology indicated by acute inflammation, calcification, and dilated lymphovascular channels of the cornea
Exp Paradigm: Histopathological examination
