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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 RNF34

UniprotKB/SwissProt ID: Q969K3 (Q969K3)

Gene Name: RNF34

Organism: Homo sapiens (Human)

Function: E3 ubiquitin-protein ligase that regulates several biological processes through the ubiquitin-mediated proteasomal degradation of various target proteins. Ubiquitinates the caspases CASP8 and CASP10, promoting their proteasomal degradation, to negatively regulate cell death downstream of death domain receptors in the extrinsic pathway of apoptosis (PubMed:15069192). May mediate 'Lys-48'-linked polyubiquitination of RIPK1 and its subsequent proteasomal degradation thereby indirectly regulating the tumor necrosis factor-mediated signaling pathway (Ref.13). Negatively regulates p53/TP53 through its direct ubiquitination and targeting to proteasomal degradation (PubMed:17121812). Indirectly, may also negatively regulate p53/TP53 through ubiquitination and degradation of SFN (PubMed:18382127). Mediates PPARGC1A proteasomal degradation probably through ubiquitination thereby indirectly regulating the metabolism of brown fat cells (PubMed:22064484). Possibly involved in innate immunity, through 'Lys-48'-linked polyubiquitination of NOD1 and its subsequent proteasomal degradation (PubMed:25012219)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cell membrane. Endomembrane system. Nucleus. Nucleus speckle. Cytoplasm, cytosol

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR049320 CARP1_2_FYVE
IPR049323 CARP1_FYVE
IPR051728 RING-FYVE_E3_ubiquitin-ligase
IPR055111 RNF34L-like_HeH
IPR036361 SAP_dom_sf
IPR011011 Znf_FYVE_PHD
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD

The S-nitrosylation sites of Q969K3

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 137 LILRNIPIDT C REKEDLVDLV