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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: Farnesyl pyrophosphate synthase

UniprotKB/SwissProt ID: FPPS_MOUSE (Q920E5)

Gene Name: Fdps

Organism: Mus musculus (Mouse).

Function: Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FPP also serves as substrate for protein farnesylation and geranylgeranylation. Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (By similarity).

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm (By similarity).

Network with metabolic pathway:
Kegg map ID Pathway Link
map00900Terpenoid backbone biosynthesis
map05164Influenza A
map05166HTLV-I infection
Graphical Visualization of S-nitrosylation Sites:
Overview of Protein S-nitrosylation Sites with Functional and Structural Information
InterPro ID Domain
IPR000092
IPR008949

The S-nitrosylation sites of FPPS_MOUSE

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site Substrate Motifs PubMed ID Experiment
1332YNRLKSLIEQ C SAPLPPSIFM HHHHHHHHHH C CCCCHHHHHH 2.13%MC1322178444-
2332YNRLKSLIEQ C SAPLPPSIFM HHHHHHHHHH C CCCCHHHHHH 2.13%MC1319483679in vivo