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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: E3 ubiquitin-protein ligase synoviolin

UniprotKB/SwissProt ID: Q9DBY1 (Q9DBY1)

Gene Name: Syvn1

Organism: Mus musculus (Mouse)

Function: E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC7 E2 ligase and transfers it to substrates, promoting their degradation (PubMed:12975321, PubMed:15611074). Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins (PubMed:12975321, PubMed:15611074). Also promotes the degradation of normal but naturally short-lived proteins such as SGK. Protects cells from ER stress-induced apoptosis. Sequesters p53/TP53 in the cytoplasm and promotes its degradation, thereby negatively regulating its biological function in transcription, cell cycle regulation and apoptosis (PubMed:17170702). Required for embryogenesis (PubMed:15611074). Mediates the ubiquitination and subsequent degradation of cytoplasmic NFE2L1 (PubMed:21911472). During the early stage of B cell development, required for degradation of the pre-B cell receptor (pre-BCR) complex, hence supporting further differentiation into mature B cells (PubMed:29907570)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Endoplasmic reticulum membrane

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR050731 HRD1_E3_ubiq-ligases
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD