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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Phosphoethanolamine N-methyltransferase 1

UniprotKB/SwissProt ID: Q9FR44 (Q9FR44)

Gene Name: NMT1

Organism: Arabidopsis thaliana (Mouse-ear cress)

Function: Involved in phosphocholine biosynthesis (PubMed:11115895, PubMed:15295103, PubMed:30218542). Catalyzes the N-methylation of phosphoethanolamine, phosphomonomethylethanolamine and phosphodimethylethanolamine, the three methylation steps required to convert phosphoethanolamine to phosphocholine (PC) (PubMed:11115895). Required for root system development and epidermal cell integrity through its role in choline and phospholipid metabolism (PubMed:15295103). In association with NMT3, regulates PC homeostasis, phase transition at the shoot apex, coordinated organ development, and fertility (PubMed:29777000). In association with NMT3, involved in phosphatidylcholine biosynthesis and vascular development (PubMed:30218542). In association with NMT2, involved in the production of phosphatidylcholine in roots, essential for root development (PubMed:30518673). In association with NMT2 produce phosphocholine mainly for leaf growth maintenance (PubMed:35560207). Contributes to the regulation of overall root zonation dynamics through reactive oxygen species (ROS) and auxin-regulated cell differentiation (PubMed:31246280). Participates in root development of primary root elongation under salt stress conditions by balancing reactive oxygen species (ROS) production and distribution through abscisic acid (ABA) signaling (PubMed:35789105)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR025714 Methyltranfer_dom
IPR041698 Methyltransf_25
IPR025771 Phosphoethanolamine_N-MeTrfase
IPR029063 SAM-dependent_MTases_sf

The S-nitrosylation sites of Q9FR44

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 105 NGHYKNVKFM C ADVTSPDLKI   
2 160 VGGYIFFRES C FHQSGDSKRK