Rabbit anti-Human POMK Polyclonal Antibody

Uniprot Id

Q9H5K3

Target Species

Human

Target Name

POMK

Target Full Name

Protein O-mannose kinase

Target Function

Protein O-mannose kinase that specifically mediates phosphorylation at the 6-position of an O-mannose of the trisaccharide (N-acetylgalactosamine (GalNAc)-beta-1,3-N-acetylglucosamine (GlcNAc)-beta-1,4-mannose) to generate phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-1,3-N-acetylglucosamine-beta-1,4-(phosphate-6-)mannose). Phosphorylated O-mannosyl trisaccharide is a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity. Only shows kinase activity when the GalNAc-beta-3-GlcNAc-beta-terminus is linked to the 4-position of O-mannose, suggesting that this disaccharide serves as the substrate recognition motif.

Target Involvement

Muscular dystrophy-dystroglycanopathy congenital with brain and eye anomalies A12 (MDDGA12); Muscular dystrophy-dystroglycanopathy limb-girdle C12 (MDDGC12)

Target Subcellular Location

Endoplasmic reticulum membrane; Single-pass type II membrane protein.

Target Protein Families

Protein kinase superfamily, Ser/Thr protein kinase family, STKL subfamily

Target Tissue Specificity

Highest expression is observed in brain, skeletal muscle, kidney and heart in fetal and adult tissues.

Target Synonyms

FLJ23356; MDDGA12; POMK; Probable inactive protein kinase-like protein SgK196; Protein kinase like protein SgK196; Protein kinase-like protein SgK196; Protein O-mannose kinase; SG196_HUMAN; SGK196; Sugen kinase 196

Target Background

This gene encodes a protein that may be involved in the presentation of the laminin-binding O-linked carbohydrate chain of alpha-dystroglycan (a-DG), which forms transmembrane linkages between the extracellular matrix and the exoskeleton. Some pathogens use this O-linked carbohydrate unit for host entry. Loss of function compound heterozygous mutations in this gene were found in a human patient affected by the Walker-Warburg syndrome (WWS) phenotype. Mice lacking this gene contain misplaced neurons (heterotopia) in some regions of the brain, possibly from defects in neuronal migration. Alternative splicing of this gene results in multiple transcript variants.