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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 ATIC

UniprotKB/SwissProt ID: Q9CWJ9 (Q9CWJ9)

Gene Name: Atic

Organism: Mus musculus (Mouse)

Function: Bifunctional enzyme that catalyzes the last two steps of purine biosynthesis (PubMed:29072452). Acts as a transformylase that incorporates a formyl group to the AMP analog AICAR (5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide) to produce the intermediate formyl-AICAR (FAICAR) (PubMed:29072452). Also displays cyclohydrolase activity involving the cyclization of FAICAR to inosine monophosphate (IMP). Can use both 10-formyldihydrofolate and 10-formyltetrahydrofolate as the formyl donor in this reaction. Also catalyzes the cyclization of FAICAR to IMP. Promotes insulin receptor/INSR autophosphorylation and is involved in INSR internalization (By similarity)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm, cytosol

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR024051 AICAR_Tfase_dup_dom_sf
IPR024050 AICAR_Tfase_insert_dom_sf
IPR016193 Cytidine_deaminase-like
IPR011607 MGS-like_dom
IPR036914 MGS-like_dom_sf
IPR002695 PurH-like

The S-nitrosylation sites of Q9CWJ9

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 101 LDFNLVRVVV C NLYPFVKTVA  CCCCCEEEEE C CCCCCHHHHH  1.64% 21278135
2 325 FGDFVALSDI C DVPTAKIISR  CCCCCEEEEE C CCCCCHHHHH  5.32% 21278135
3 363 ILSKKKNGNY C VLQMDQSYKP  CCCCCEEEEE C CCCCCHHHHH  2.6% 20925432
4 434 AVKYTQSNSV C YAKDGQVIGI  CCCCCEEEEE C CCCCCHHHHH  2.47% 21278135