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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: Non-structural maintenance of chromosomes element 1 homolog

UniprotKB/SwissProt ID: Q8WV22 (Q8WV22)

Gene Name: NSMCE1

Organism: Homo sapiens (Human)

Function: RING-type zinc finger-containing E3 ubiquitin ligase that assembles with melanoma antigen protein (MAGE) to catalyze the direct transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a specific substrate. Within MAGE-RING ubiquitin ligase complex, MAGE stimulates and specifies ubiquitin ligase activity likely through recruitment and/or stabilization of the E2 ubiquitin-conjugating enzyme at the E3:substrate complex. Involved in maintenance of genome integrity, DNA damage response and DNA repair (PubMed:20864041, PubMed:29225034). NSMCE3/MAGEG1 and NSMCE1 ubiquitin ligase are components of SMC5-SMC6 complex and may positively regulate homologous recombination-mediated DNA repair (PubMed:18086888). MAGEF1-NSMCE1 ubiquitin ligase promotes proteasomal degradation of MMS19, a key component of the cytosolic iron-sulfur protein assembly (CIA) machinery. Down-regulation of MMS19 impairs the activity of several DNA repair and metabolism enzymes such as ERCC2/XPD, FANCJ, RTEL1 and POLD1 that require iron-sulfur clusters as cofactors (PubMed:29225034)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus. Chromosome, telomere

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR011513 Nse1
IPR014857 Nse1_RING_C4HC3-type
IPR002219 PE/DAG-bd
IPR036388 WH-like_DNA-bd_sf
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD

The S-nitrosylation sites of Q8WV22

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 194 YPDAVKICNI C HSLLIQGQSC