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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: Phosphoglucomutase, chloroplastic

UniprotKB/SwissProt ID: Q9SCY0 (Q9SCY0)

Gene Name: PGMP

Organism: Arabidopsis thaliana (Mouse-ear cress)

Function: Catalyzes the reversible isomerization of alpha-D-glucose 1-phosphate to alpha-D-glucose 6-phosphate (PubMed:10759515). The mechanism proceeds via the intermediate compound alpha-D-glucose 1,6-bisphosphate (Probable). This enzyme participates in both the breakdown and synthesis of glucose (By similarity). Factor that affects seed oil content (PubMed:10759515). Accumulated starch in young embryos may play an important role in providing carbon resources for seed storage lipid biosynthesis in oilseed plants (Probable). Promotes gravitropic responses, negative in shoots but positive in roots, by facilitating starch granules (statoliths) formation in hypocotyls and roots columella (PubMed:34367195)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Plastid, chloroplast

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR005844 A-D-PHexomutase_a/b/a-I
IPR016055 A-D-PHexomutase_a/b/a-I/II/III
IPR005845 A-D-PHexomutase_a/b/a-II
IPR005846 A-D-PHexomutase_a/b/a-III
IPR036900 A-D-PHexomutase_C_sf
IPR016066 A-D-PHexomutase_CS
IPR005841 Alpha-D-phosphohexomutase_SF
IPR045244 PGM

The S-nitrosylation sites of Q9SCY0

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 431 NLMDAGKLSI C GEESFGTGSD   
2 499 NFFSRYDYEE C ESEGANKMIE