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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: Lipid droplet-regulating VLDL assembly factor AUP1

UniprotKB/SwissProt ID: Q9Y679 (Q9Y679)

Gene Name: AUP1

Organism: Homo sapiens (Human)

Function: Plays a role in the translocation of terminally misfolded proteins from the endoplasmic reticulum lumen to the cytoplasm and their degradation by the proteasome (PubMed:18711132, PubMed:21857022). Plays a role in lipid droplet formation (PubMed:21857022). Induces lipid droplet clustering (PubMed:24039768). Recruits ubiquitin-conjugating enzyme UBE2G2 to lipid droplets which facilitates its interaction with ubiquitin ligases AMFR/gp78 and RNF139/TRC8, leading to sterol-induced ubiquitination of HMGCR and its subsequent proteasomal degradation (PubMed:21127063, PubMed:23223569). Also required for the degradation of INSIG1, SREBF1 and SREBF2 (PubMed:23223569). Plays a role in regulating assembly and secretion of very low density lipoprotein particles and stability of apolipoprotein APOB (PubMed:28183703) (Microbial infection) Following Dengue virus infection, required for induction of lipophagy which facilitates production of virus progeny particles

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Endoplasmic reticulum membrane. Lipid droplet. Cytoplasmic vesicle, autophagosome

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR048056 AUP1_CUE
IPR003892 CUE

The S-nitrosylation sites of Q9Y679

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 325 VIQRDLAKTG C VDLTITNLLE   
2 70 VLRRFVVRTM C AVLGLVARQE