POMK report

I. Expression across cell types

II. Expression across tissues

sc-RNAseq data

Insufficient scRNA-seq data for expression of POMK at tissue level.

III. Associated gene sets

GO_0019233Biological processsensory perception of pain
GO_0007420Biological processbrain development
GO_0046835Biological processcarbohydrate phosphorylation
GO_0050905Biological processneuromuscular process
GO_0006493Biological processprotein O-linked glycosylation
GO_0007611Biological processlearning or memory
GO_0005789Cellular componentendoplasmic reticulum membrane
GO_0019200Molecular functioncarbohydrate kinase activity
GO_0005515Molecular functionprotein binding
GO_0016773Molecular functionphosphotransferase activity, alcohol group as acceptor
GO_0005524Molecular functionATP binding
GO_0004672Molecular functionprotein kinase activity

IV. Literature review

[source]
Gene namePOMK
Protein nameProtein O-mannose kinase
Protein O-mannose kinase (EC 2.7.1.183) (Protein kinase-like protein SgK196) (Sugen kinase 196)
Protein O-mannose kinase (POMK) (EC 2.7.1.183) (Protein kinase-like protein SgK196) (Sugen kinase 196)
SynonymsSGK196
DescriptionFUNCTION: 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. .

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. .

AccessionsQ9H5K3
ENST00000674937.1
A0A6Q8PF73
ENST00000674676.1
ENST00000675675.1
ENST00000675129.1
A0A6Q8PFX5
A0A6Q8PFG8
ENST00000518991.6
A0A6Q8PFH3
ENST00000674646.1
ENST00000675322.1
ENST00000676178.1
ENST00000331373.10
ENST00000676193.1
ENST00000674820.1
ENST00000674782.1
ENST00000614426.2
E5RJD5