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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: Porphobilinogen deaminase

UniprotKB/SwissProt ID: P08397 (P08397)

Gene Name: HMBS

Organism: Homo sapiens (Human)

Function: As part of the heme biosynthetic pathway, catalyzes the sequential polymerization of four molecules of porphobilinogen to form hydroxymethylbilane, also known as preuroporphyrinogen (PubMed:18004775, PubMed:18936296, PubMed:19138865, PubMed:23815679). Catalysis begins with the assembly of the dipyrromethane cofactor by the apoenzyme from two molecules of porphobilinogen or from preuroporphyrinogen. The covalently linked cofactor acts as a primer, around which the tetrapyrrole product is assembled (PubMed:18936296). In the last step of catalysis, the product, preuroporphyrinogen, is released, leaving the cofactor bound to the holodeaminase intact (PubMed:18936296)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm, cytosol

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR000860 HemC
IPR022419 Porphobilin_deaminase_cofac_BS
IPR022417 Porphobilin_deaminase_N
IPR022418 Porphobilinogen_deaminase_C
IPR036803 Porphobilinogen_deaminase_C_sf

The S-nitrosylation sites of P08397

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 114 LPPGFTIGAI C KRENPHDAVV  CCCCCCCCCC C CCCCCCEEEE  3.18% 19483679
2 211 RVGQILHPEE C MYAVGQGALG  CCCCCCCCCC C CCCCCCEEEE  2.11%
3 261 RAFLRHLEGG C SVPVAVHTAM  CCCCCCCCCC C CCCCCCEEEE  5.65% 2212679