ARMT1 report

I. Expression across cell types

II. Expression across tissues

sc-RNAseq data

Insufficient scRNA-seq data for expression of ARMT1 at tissue level.

III. Associated gene sets

GO_0006974Biological processDNA damage response
GO_0032259Biological processmethylation
GO_0016791Molecular functionphosphatase activity
GO_0019899Molecular functionenzyme binding
GO_0097023Molecular functionfructose 6-phosphate aldolase activity
GO_0008983Molecular functionprotein-glutamate O-methyltransferase activity
GO_0005515Molecular functionprotein binding
GO_0051998Molecular functionprotein carboxyl O-methyltransferase activity
GO_0008757Molecular functionS-adenosylmethionine-dependent methyltransferase activity
GO_0046872Molecular functionmetal ion binding
GO_0103026Molecular functionfructose-1-phosphatase activity

IV. Literature review

[source]
Gene nameARMT1
Protein nameSugar phosphate phosphatase (EC 2.1.1.-) (EC 3.1.3.-)
Damage-control phosphatase ARMT1 (EC 3.1.3.-) (Acidic residue methyltransferase 1) (Protein-glutamate O-methyltransferase) (EC 2.1.1.-) (Sugar phosphate phosphatase ARMT1)
Acidic residue methyltransferase 1
SynonymsC6orf211
DescriptionFUNCTION: Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate (By similarity). Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function in hexose phosphate metabolism (By similarity). Has also been shown to have O-methyltransferase activity that methylates glutamate residues of target proteins to form gamma-glutamyl methyl ester residues . Possibly methylates PCNA, suggesting it is involved in the DNA damage response . .

FUNCTION: Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate. Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function in hexose phosphate metabolism. Has also been shown to have O-methyltransferase activity that methylates glutamate residues of target proteins to form gamma-glutamyl methyl ester residues. Possibly methylates PCNA, suggesting it is involved in the DNA damage response. .

AccessionsENST00000367294.4
F5GZY1
Q9H993
ENST00000494826.1
ENST00000545879.5
F2Z3I8