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The protein encoded by POMT2 is an O-mannosyltransferase that requires interaction with the product of the POMT1 gene for enzymatic function. Additionally we are shipping POMT2 Antibodies (42) and many more products for this protein.
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Drosophila POMT1 (show POMT1 Proteins) and POMT2 function as a protein O-mannosyltransferase in association with each other to generate and maintain normal muscle development.
establish a central role for Dystroglycan (Dg) in maintaining integrity in Drosophila larval muscles and demonstrate the importance of glycosylation to Dg function in Drosophila
POMT2 missense mutation is associated with Cystic kidneys in fetal Walker-Warburg syndrome.
O-mannosylation of cadherins and protocadherins does not require POMT1 (show POMT1 Proteins) and/or POMT2 in contrast to alpha-dystroglycan, and moreover, the O-Man glycans on cadherins are not elongated.
Our report is the first to document an association between POMT2 mutations and aortopathy with concomitant depressed left ventricular systolic function.
the effects of replacing Arg(64), Glu (show DCTN1 Proteins)(78) and Arg(138)residues in human POMT1 (show POMT1 Proteins) and POMT2 with Ala on complex formation and enzymatic activity were studied.
the function of the gene products is only known for POMT1 (show POMT1 Proteins), POMT2, and POMGnT1 (show POMGNT1 Proteins), all responsible for the O-mannosylglycan biosynthesis
the N-glycosylation of POMT1 (show POMT1 Proteins) and POMT2 is required for maintaining the conformation as well as the activity of the POMT1 (show POMT1 Proteins)-POMT2 complex.
active enzyme complex of POMT1 (show POMT1 Proteins) and POMT2 suggests that the regulation of protein O-mannosylation is complex and appears to be required for normal structure and function of alpha-dystroglycan in muscle and brain
POMT2 mutations cause alpha-dystroglycan hypoglycosylation and Walker-Warburg syndrome [case reports]
Several mutations were found in the Protein O-Mannosyltransferase 1 (show POMT1 Proteins) and 2 (POMT1 (show POMT1 Proteins) and POMT2) genes, and one mutation was found in each of the fukutin (show FKTN Proteins) and fukutin-related protein (FKRP (show FKRP Proteins)) genes.
Our results broaden the clinical spectrum associated with POMT2 mutations, which should be considered in patients with CMD (show ACAN Proteins) associated with microcephaly, and severe mental retardation with or without ocular involvement.
Data show that POMT2 deletion in the meninges did not disrupt the development of the neocortex, and suggest that normal brain development requires protein O-mannosylation activity in neural tissue but not the meninges.
testis POMT2 is highly conserved among mammals, including humans, suggesting a crucial function that is distinct from somatic POMT2
The protein encoded by this gene is an O-mannosyltransferase that requires interaction with the product of the POMT1 gene for enzymatic function. The encoded protein is found in the membrane of the endoplasmic reticulum. Defects in this gene are a cause of Walker-Warburg syndrome (WWS).
, protein O-mannosyltransferase 2
, putative protein O-mannosyltransferase
, protein-O-mannosyltransferase 2
, protein O-mannosyl-transferase 2
, protein O-mannosyl-transferase 2-like
, dolichyl-phosphate-mannose--protein mannosyltransferase 2