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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 ZNF451

UniprotKB/SwissProt ID: Q9Y4E5 (Q9Y4E5)

Gene Name: ZNF451

Organism: Homo sapiens (Human)

Function: E3 SUMO-protein ligase; has a preference for SUMO2 and SUMO3 and facilitates UBE2I/UBC9-mediated sumoylation of target proteins (PubMed:26524493, PubMed:26524494). Plays a role in protein SUMO2 modification in response to stress caused by DNA damage and by proteasome inhibitors (in vitro). Required for MCM4 sumoylation (By similarity). Has no activity with SUMO1 (PubMed:26524493). Preferentially transfers an additional SUMO2 chain onto the SUMO2 consensus site 'Lys-11' (PubMed:26524493). Negatively regulates transcriptional activation mediated by the SMAD4 complex in response to TGF-beta signaling. Inhibits EP300-mediated acetylation of histone H3 at 'Lys-9' (PubMed:24324267). Plays a role in regulating the transcription of AR targets (PubMed:18656483)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus. Nucleus, PML body. Nucleus, nucleoplasm

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR041192 PIN_11
IPR013087 Znf_C2H2_type

The S-nitrosylation sites of Q9Y4E5

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 150 MPGLKTGTIN C GTKSSFRRGG