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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: Bifunctional purine biosynthesis protein PURH

UniprotKB/SwissProt ID: PUR9_HUMAN (P31939)

Gene Name: ATIC

Synonyms: PURH

Organism: Homo sapiens (Human).

Function: Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis.

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization:

PDB :
( If your security settings prevent Jmol from running, please register http://140.138.144.145/ as a safe location in your Java settings. )

Protein disease:
Disease database Database Entry Disease information
HPRD03434Aica-ribosiduria due to ATIC deficiency
Network with metabolic pathway:
Kegg map ID Pathway Link
map00230Purine metabolism
map00670One carbon pool by folate
Graphical Visualization of S-nitrosylation Sites:
Overview of Protein S-nitrosylation Sites with Functional and Structural Information
InterPro ID Domain
IPR002695
IPR011607
IPR013982

3D Structure Databases:
3D structure databases
EntryMethodResolution (A)ChainPositionsView
1P4R X-ray 2.55 A A/B1-592Link
1PKX X-ray 1.90 A A/B/C/D1-592Link
1PL0 X-ray 2.60 A A/B/C/D1-592Link

The S-nitrosylation sites of PUR9_HUMAN

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site Substrate Motifs PubMed ID Experiment
1434AVKYTQSNSV C YAKNGQVIGI HHHHHCCCEE E EEECCEEEEE 2.47%HC0619483679in vivo