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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: Spastin

UniprotKB/SwissProt ID: Q9UBP0 (Q9UBP0)

Gene Name: SPAST

Organism: Homo sapiens (Human)

Function: ATP-dependent microtubule severing protein that specifically recognizes and cuts microtubules that are polyglutamylated (PubMed:11809724, PubMed:15716377, PubMed:16219033, PubMed:17389232, PubMed:20530212, PubMed:22637577, PubMed:26875866). Preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (PubMed:26875866). Severing activity is not dependent on tubulin acetylation or detyrosination (PubMed:26875866). Microtubule severing promotes reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. It is critical for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. SPAST is involved in abscission step of cytokinesis and nuclear envelope reassembly during anaphase in cooperation with the ESCRT-III complex (PubMed:19000169, PubMed:21310966, PubMed:26040712). Recruited at the midbody, probably by IST1, and participates in membrane fission during abscission together with the ESCRT-III complex (PubMed:21310966). Recruited to the nuclear membrane by IST1 and mediates microtubule severing, promoting nuclear envelope sealing and mitotic spindle disassembly during late anaphase (PubMed:26040712). Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and endosome recycling (PubMed:23897888). Recruited by IST1 to endosomes and regulates early endosomal tubulation and recycling by mediating microtubule severing (PubMed:23897888). Probably plays a role in axon growth and the formation of axonal branches (PubMed:15716377) Involved in lipid metabolism by regulating the size and distribution of lipid droplets

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Membrane. Endoplasmic reticulum. Midbody. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton. Cytoplasm, perinuclear region. Nucleus. Cytoplasm, cytoskeleton, spindle. Cytoplasm. Cell projection, axon. Endoplasmic reticulum membrane. Nucleus membrane. Lipid droplet. Cytoplasm, cytoskeleton. Endosome. Cytoplasm. Endosome. Nucleus membrane. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR003593 AAA+_ATPase
IPR041569 AAA_lid_3
IPR003959 ATPase_AAA_core
IPR003960 ATPase_AAA_CS
IPR007330 MIT_dom
IPR050304 MT-severing_AAA_ATPase
IPR027417 P-loop_NTPase
IPR015415 Spast_Vps4_C
IPR017179 Spastin
IPR035106 Spastin_chordate

The S-nitrosylation sites of Q9UBP0

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 220 DVYNDSTNLA C RNGHLQSESG