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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 procollagen lysine hydroxylase and glycosyltransferase LH3

UniprotKB/SwissProt ID: Q5U367 (Q5U367)

Gene Name: Plod3

Organism: Rattus norvegicus (Rat)

Function: Multifunctional enzyme that catalyzes a series of post-translational modifications on Lys residues in procollagen. Plays a redundant role in catalyzing the formation of hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens (By similarity). Plays a redundant role in catalyzing the transfer of galactose onto hydroxylysine groups, giving rise to galactosyl 5-hydroxylysine (By similarity). Has an essential role by catalyzing the subsequent transfer of glucose moieties, giving rise to 1,2-glucosylgalactosyl-5-hydroxylysine residues. Catalyzes hydroxylation and glycosylation of Lys residues in the MBL1 collagen-like domain, giving rise to hydroxylysine and 1,2-glucosylgalactosyl-5-hydroxylysine residues. Catalyzes hydroxylation and glycosylation of Lys residues in the ADIPOQ collagen-like domain, giving rise to hydroxylysine and 1,2-glucosylgalactosyl-5-hydroxylysine residues. Essential for normal biosynthesis and secretion of type IV collagens. Essential for normal formation of basement membranes (By similarity)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Rough endoplasmic reticulum. Endoplasmic reticulum lumen. Endoplasmic reticulum membrane. Secreted. Secreted, extracellular space

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR050757 Collagen_mod_GT25
IPR044861 IPNS-like_FE2OG_OXY
IPR029044 Nucleotide-diphossugar_trans
IPR005123 Oxoglu/Fe-dep_dioxygenase_dom
IPR006620 Pro_4_hyd_alph
IPR001006 Procol_lys_dOase

The S-nitrosylation sites of Q5U367

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 694 HKGVDYEGGG C RFLRYDCRVS