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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: Multifunctional protein CAD

UniprotKB/SwissProt ID: B2RQC6 (B2RQC6)

Gene Name: Cad

Organism: Mus musculus (Mouse)

Function: Multifunctional protein that encodes the first 3 enzymatic activities of the de novo pyrimidine pathway: carbamoylphosphate synthetase (CPSase; EC 6.3.5.5), aspartate transcarbamylase (ATCase; EC 2.1.3.2) and dihydroorotase (DHOase; EC 3.5.2.3). The CPSase-function is accomplished in 2 steps, by a glutamine-dependent amidotransferase activity (GATase) that binds and cleaves glutamine to produce ammonia, followed by an ammonium-dependent carbamoyl phosphate synthetase, which reacts with the ammonia, hydrogencarbonate and ATP to form carbamoyl phosphate. The endogenously produced carbamoyl phosphate is sequestered and channeled to the ATCase active site. ATCase then catalyzes the formation of carbamoyl-L-aspartate from L-aspartate and carbamoyl phosphate. In the last step, DHOase catalyzes the cyclization of carbamoyl aspartate to dihydroorotate

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Nucleus

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR006680 Amidohydro-rel
IPR006132 Asp/Orn_carbamoyltranf_P-bd
IPR006130 Asp/Orn_carbamoylTrfase
IPR036901 Asp/Orn_carbamoylTrfase_sf
IPR002082 Asp_carbamoyltransf
IPR006131 Asp_carbamoyltransf_Asp/Orn-bd
IPR011761 ATP-grasp
IPR013815 ATP_grasp_subdomain_1
IPR006275 CarbamoylP_synth_lsu
IPR005480 CarbamoylP_synth_lsu_oligo
IPR036897 CarbamoylP_synth_lsu_oligo_sf
IPR006274 CarbamoylP_synth_ssu
IPR002474 CarbamoylP_synth_ssu_N
IPR036480 CarbP_synth_ssu_N_sf
IPR005479 CbamoylP_synth_lsu-like_ATP-bd
IPR005483 CbamoylP_synth_lsu_CPSase_dom
IPR029062 Class_I_gatase-like
IPR035686 CPSase_GATase1
IPR002195 Dihydroorotase_CS
IPR017926 GATASE
IPR011059 Metal-dep_hydrolase_composite
IPR032466 Metal_Hydrolase
IPR011607 MGS-like_dom
IPR036914 MGS-like_dom_sf
IPR016185 PreATP-grasp_dom_sf

The S-nitrosylation sites of B2RQC6

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 179 VFNAGGAPRI C ALDCGLKYNQ  CCEEEECCCC E ECCCCCCCEE 
2 192 DCGLKYNQIR C LCQLGAEVTV  CCEEEECCCC E ECCCCCCCEE 
3 2092 KHGRTVHSLA C LLTQYRVSLR  CCEEEECCCC E ECCCCCCCEE  20925432
4 280 RYGNRGHNQP C LLVGTGRCFL  CCEEEECCCC E ECCCCCCCEE  20925432
5 897 VRKLRQELGI C PAVKQIDTVA  CCEEEECCCC E ECCCCCCCEE  20925432