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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: Ubiquitin-conjugating enzyme E2 S

UniprotKB/SwissProt ID: Q16763 (Q16763)

Gene Name: UBE2S

Organism: Homo sapiens (Human)

Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins (PubMed:19820702, PubMed:19822757, PubMed:22496338, PubMed:27259151). Catalyzes 'Lys-11'-linked polyubiquitination. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis (PubMed:19820702, PubMed:19822757, PubMed:27259151, PubMed:27910872). Acts by specifically elongating 'Lys-11'-linked polyubiquitin chains initiated by the E2 enzyme UBE2C/UBCH10 on APC/C substrates, enhancing the degradation of APC/C substrates by the proteasome and promoting mitotic exit (PubMed:19820702, PubMed:19822757, PubMed:27259151). Also acts by elongating ubiquitin chains initiated by the E2 enzyme UBE2D1/UBCH5 in vitro; it is however unclear whether UBE2D1/UBCH5 acts as an E2 enzyme for the APC/C in vivo. Also involved in ubiquitination and subsequent degradation of VHL, resulting in an accumulation of HIF1A (PubMed:16819549). In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, except 'Lys-48'-linked polyubiquitination (PubMed:20061386, PubMed:20622874)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization:

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR050113 Ub_conjugating_enzyme
IPR000608 UBQ-conjugat_E2_core
IPR023313 UBQ-conjugating_AS
IPR016135 UBQ-conjugating_enzyme/RWD

The S-nitrosylation sites of Q16763

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 118 GIRHVLLTIK C LLIHPNPESA   
2 95 HPNVGANGEI C VNVLKRDWTA