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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 SUMO-protein ligase PIAS2

UniprotKB/SwissProt ID: PIAS2_MOUSE (Q8C5D8)

Gene Name: Pias2

Synonyms: Miz1, Piasx

Organism: Mus musculus (Mouse).

Function: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. The effects of this transcriptional coregulation, transactivation or silencing may vary depending upon the biological context and PIAS2 isoform studied. However, it seems to be mostly involved in gene silencing. Binds to sumoylated ELK1 and enhances its transcriptional activity by preventing recruitment of HDAC2 by ELK1, thus reversing SUMO-mediated repression of ELK1 transactivation activity. Isoform PIASx-beta, but not isoform PIASx-alpha, promotes MDM2 sumoylation. Isoform PIASx-alpha promotes PARK7 sumoylation. Isoform PIASx-beta promotes NCOA2 sumoylation more efficiently than isoform PIASx- alpha (By similarity). Sumoylates PML at'Lys-65' and 'Lys-160' (By similarity).

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus speckle. Nucleus, PML body. Note=Colocalizes at least partially with promyelocytic leukemia nuclear bodies (PML NBs).

Network with metabolic pathway:
Kegg map ID Pathway Link
map05222Small cell lung cancer
map04630Jak-STAT signaling pathway
map05200Pathways in cancer
map04120Ubiquitin mediated proteolysis
Graphical Visualization of S-nitrosylation Sites:
Overview of Protein S-nitrosylation Sites with Functional and Structural Information
InterPro ID Domain
IPR003034
IPR004181

The S-nitrosylation sites of PIAS2_MOUSE

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site Substrate Motifs PubMed ID Experiment
149MRALHLLKSG C SPAVQIKIRE HHHHHHHHCC C CHHHHHHHHH 5.94%MC0322865876in vivo