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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: E3 ubiquitin-protein ligase RNF169

UniprotKB/SwissProt ID: Q8NCN4 (Q8NCN4)

Gene Name: RNF169

Organism: Homo sapiens (Human)

Function: Probable E3 ubiquitin-protein ligase that acts as a regulator of double-strand breaks (DSBs) repair following DNA damage. Functions in a non-canonical fashion to harness RNF168-mediated protein recruitment to DSB-containing chromatin, thereby contributing to regulation of DSB repair pathway utilization (PubMed:22492721, PubMed:30773093). Once recruited to DSB repair sites by recognizing and binding ubiquitin catalyzed by RNF168, competes with TP53BP1 and BRCA1 for association with RNF168-modified chromatin, thereby favouring homologous recombination repair (HRR) and single-strand annealing (SSA) instead of non-homologous end joining (NHEJ) mediated by TP53BP1 (PubMed:30104380, PubMed:30773093). E3 ubiquitin-protein ligase activity is not required for regulation of DSBs repair

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Chromosome. Nucleus, nucleoplasm

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR051657 RNF168/RNF169_E3_ubiq-ligase
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS

The S-nitrosylation sites of Q8NCN4

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 132 GQADSEVLGE C ARRSQPERCR   
2 529 KSSTEIPLET C CSSELKGGGS   
3 530 SSTEIPLETC C SSELKGGGSG