Gene Ontology annotation through association of InterPro records with GO terms.
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt.
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara.
Combined Automated Annotation using Multiple IEA Methods.
Identification of a human homolog of the Drosophila rotated abdomen gene (POMT1) encoding a putative protein O-mannosyl-transferase, and assignment to human chromosome 9q34.1.
Demonstration of mammalian protein O-mannosyltransferase activity: coexpression of POMT1 and POMT2 required for enzymatic activity.
Physical and functional association of human protein O-mannosyltransferases 1 and 2.
Mammalian O-mannosylation of cadherins and plexins is independent of protein O-mannosyltransferases 1 and 2.
Defective POMT2 does not transfer Man from Dol-P-Man to DAG1
Defective POMT1 does not transfer Man from Dol-P-Man to DAG1
POMT1:POMT2 transfers Man from Dol-P-Man to DAG1(30-653)
Deep research on POMT1 function
Deep research on POMT1 (falcon, Edison Scientific Literature, 2026-05-29)
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POMT1 is a multi-pass ER membrane glycosyltransferase that functions with POMT2 as the canonical protein O-mannosyltransferase initiating O-mannosylation on selected substrates, most notably alpha-dystroglycan; POMT/Pmt enzymes are classified as GT-C fold enzymes in CAZy GT39 and contain a conserved luminal DD/DE acidic motif essential for activity.
"human POMT1 (Q9Y6A1) is a multi-pass ER membrane glycosyltransferase that functions with **POMT2** as the canonical **protein O-mannosyltransferase** initiating O-mannosylation on selected substrates, most notably **α-dystroglycan (α-DG)**"
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The donor is Dol-P-Man (GDP-mannose is not used) and mannose transferred is sensitive to alpha-mannosidase consistent with Man-alpha-Ser/Thr linkages.
"The donor was **Dol-P-Man**; **GDP-mannose was not used** as a donor (manya2004demonstrationofmammalian pages 3-4, manya2004demonstrationofmammalian pages 4-5)."
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Mammalian POMT1/2 have narrow substrate specificity; substrates include alpha-DG, KIAA1549 and SUCO, distinct from cadherins/plexins which are served by TMTC1-4 and TMEM260 pathways.
"The study supports that mammalian POMT1/2 have a relatively **narrow substrate specificity**, with examples including α-DG and additional targets such as **KIAA1549** and **SUCO**"
Global View of Domain-Specific O-Linked Mannose Glycosylation in Glycoengineered Cells.
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POMT1/POMT2 is one of three nonredundant enzyme families (with TMTC1-4 and TMEM260) that selectively initiate O-Man glycosylation; POMT1/POMT2 are distinguished by narrow substrate specificity targeting KIAA1549, SUCO and alpha-dystroglycan.
"The mammalian orthologs POMT1 and POMT2, which are absent in plants, are distinguished from yeast PMTs by their narrow substrate specificities and dedicated functions for O-Man initiation on only a few human proteins, including KIAA1549, SUCO, and α-dystroglycan (α-DG)"
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O-Man biosynthesis is initiated in the ER lumen by integral transmembrane GT-CA enzymes that use dolichol phosphate mannose as donor substrate.
"Biosynthesis of O-Man is initiated in the endoplasmic reticulum (ER) lumen by integral transmembrane GT-CA enzymes (5, 6, 7) that utilize lipid-linked dolichol phosphate mannose as donor substrate"
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Functional O-Man glycosylation of alpha-DG (matriglycan) is required for interactions with ECM components laminin, agrin and perlecan within the dystrophin-associated glycoprotein complex.
"Functional O-Man glycosylation of α-DG is required for interactions with extracellular matrix (ECM) components, including laminin, agrin, and perlecan, which are anchored to the dystrophin-associated glycoprotein complex and the actin cytoskeleton through a complex O-Man polysaccharide known as matriglycan"
Removal of pomt1 in zebrafish leads to loss of alpha-dystroglycan glycosylation and dystroglycanopathy phenotypes.
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POMT1 catalyzes the addition of an O-linked mannose to alpha-DG, starting the assembly of the functional glycan as the protein is translated in the ER; loss of pomt1 in zebrafish abolishes alpha-DG glycosylation and recapitulates dystroglycanopathy phenotypes affecting muscle, eye and brain.
"Protein O-mannosyltransferase 1 (POMT1, OMIM:607423) catalyzes the addition of an O-linked mannose to α-DG starting the assembly of the functional glycan as the protein is translated in the ER"
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Global Pomt1 knockout in mouse causes early embryonic lethality due to the role of dystroglycan in Reichert's membrane formation, requiring conditional approaches in mammals.
"Global knock-out (KO) of Pomt1 in the mouse leads to early embryonic lethality similarly to Dag1 mutants. This is due to the critical role of dystroglycan in Reichert's membrane, a specialized basement membrane in rodent embryos"
Protein O-mannosylation: one sugar, several pathways, many functions.
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Protein O-mannosylation plays a crucial role in the nervous system in animals, and POMT defects cause severe neurological abnormalities and congenital muscular dystrophies.
"In animals, protein O-mannosylation plays a crucial role in the nervous system, whereas protein O-mannosylation defects cause severe neurological abnormalities and congenital muscular dystrophies."
Cardiomyopathy in patients with POMT1-related congenital and limb-girdle muscular dystrophy.
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POMT1 is a glycosyltransferase involved in alpha-dystroglycan glycosylation; POMT1 mutations cause a clinical spectrum from CMD with brain abnormalities to LGMD, and can include cardiomyopathy with reduced alpha-DG immunolabeling in muscle biopsies.
"Protein-o-mannosyl transferase 1 (POMT1) is a glycosyltransferase involved in α-dystroglycan (α-DG) glycosylation. Clinical phenotype in POMT1-mutated patients ranges from congenital muscular dystrophy (CMD) with structural brain abnormalities, to limb-girdle muscular dystrophy (LGMD) with microcephaly and mental retardation, to mild LGMD."