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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: Dynamin-2

UniprotKB/SwissProt ID: P39054 (P39054)

Gene Name: Dnm2

Organism: Mus musculus (Mouse)

Function: Catalyzes the hydrolysis of GTP and utilizes this energy to mediate vesicle scission at plasma membrane during endocytosis and filament remodeling at many actin structures during organization of the actin cytoskeleton (By similarity). Plays an important role in vesicular trafficking processes, namely clathrin-mediated endocytosis (CME), exocytic and clathrin-coated vesicle from the trans-Golgi network, and PDGF stimulated macropinocytosis (PubMed:18923138). During vesicular trafficking process, associates to the membrane, through lipid binding, and self-assembles into ring-like structure through oligomerization to form a helical polymer around the vesicle membrane and leading to vesicle scission (By similarity). Plays a role in organization of the actin cytoskeleton by mediating arrangement of stress fibers and actin bundles in podocytes (By similarity). During organization of the actin cytoskeleton, self-assembles into ring-like structure that directly bundles actin filaments to form typical membrane tubules decorated with dynamin spiral polymers (PubMed:33113375). Self-assembly increases GTPase activity and the GTP hydrolysis causes the rapid depolymerization of dynamin spiral polymers, and results in dispersion of actin bundles (By similarity). Remodels, through its interaction with CTTN, bundled actin filaments in a GTPase-dependent manner and plays a role in orchestrating the global actomyosin cytoskeleton (By similarity). The interaction with CTTN stabilizes the interaction of DNM2 and actin filaments and stimulates the intrinsic GTPase activity that results in actin filament-barbed ends and increases the sensitivity of filaments in bundles to the actin depolymerizing factor, CFL1 (By similarity). Plays a role in the autophagy process, by participating in the formation of ATG9A vesicles destined for the autophagosomes through its interaction with SNX18, by mediating recycling endosome scission leading to autophagosome release through MAP1LC3B interaction (By similarity). Also regulates maturation of apoptotic cell corpse-containing phagosomes by recruiting PIK3C3 to the phagosome membrane (PubMed:18425118). Also plays a role in cytokinesis (PubMed:18923138). May participate in centrosome cohesion through its interaction with TUBG1 (By similarity). Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones (By similarity). Involved in membrane tubulation (By similarity)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm, cytoskeleton. Cytoplasmic vesicle, clathrin-coated vesicle. Cell projection, uropodium. Endosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Recycling endosome. Cell projection, phagocytic cup. Cytoplasmic vesicle, phagosome membrane. Cell projection, podosome. Cytoplasm. Cell junction. Postsynaptic density. Synapse, synaptosome. Midbody. Membrane, clathrin-coated pit

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR022812 Dynamin
IPR001401 Dynamin_GTPase
IPR019762 Dynamin_GTPase_CS
IPR045063 Dynamin_N
IPR000375 Dynamin_stalk
IPR030381 G_DYNAMIN_dom
IPR003130 GED
IPR020850 GED_dom
IPR027417 P-loop_NTPase
IPR011993 PH-like_dom_sf
IPR001849 PH_domain

The S-nitrosylation sites of P39054

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 27 QDAFSSIGQS C HLDLPQIAVV   
2 607 YKDLRQIELA C DSQEDVDSWK