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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: Nucleoside diphosphate kinase 3

UniprotKB/SwissProt ID: Q13232 (Q13232)

Gene Name: NME3

Organism: Homo sapiens (Human)

Function: Catalyzes the phosphorylation of ribonucleosides and deoxyribonucleoside diphosphates, other than ATP, into the corresponding triphosphates with ATP as the major phosphate donor (PubMed:11277919, PubMed:30587587). The ATP gamma phosphate is transferred to the nucleoside diphosphate beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Through the catalyzed exchange of gamma-phosphate between di- and triphosphonucleosides participates in regulation of intracellular nucleotide homeostasis (PubMed:11277919, PubMed:30587587). Inhibits granulocyte differentiation (PubMed:7638209). May be required for ciliary function during renal development (By similarity) Independently of its kinase activity, facilitates mitochondrial tethering prior to membrane fusion through its direct membrane-binding and hexamerization (PubMed:30587587, PubMed:37584589). Implicated in repair of both single- and double-stranded breaks in DNA through its association with the ribonucleotide reductase complex (RNR complex) via its interaction with the histone acetyltransferase KAT5, this interaction enables recruitment of NME3 at DNA damage sites where it plays a role in the repair of DNA, independently of its kinase activity (PubMed:37584589)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Mitochondrion outer membrane. Cytoplasm. Cytoplasm, cytoskeleton, cilium basal body

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR034907 NDK-like_dom
IPR036850 NDK-like_dom_sf
IPR001564 Nucleoside_diP_kinase
IPR023005 Nucleoside_diP_kinase_AS

The S-nitrosylation sites of Q13232

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 126 APPGTIRGDF C IEVGKNLIHG   
2 158 ALWFRADELL C WEDSAGHWLY