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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 ARIH2

UniprotKB/SwissProt ID: O95376 (O95376)

Gene Name: ARIH2

Organism: Homo sapiens (Human)

Function: E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3 (PubMed:16118314, PubMed:17646546, PubMed:19340006, PubMed:24076655, PubMed:33268465, PubMed:34518685, PubMed:38418882). Acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-5-RING ubiquitin ligase complex (ECS complex, also named CRL5 complex) and initiating ubiquitination of ECS substrates: associates with ECS complex and specifically mediates addition of the first ubiquitin on ECS targets (PubMed:33268465, PubMed:34518685, PubMed:38418882). The initial ubiquitin is then elongated (PubMed:33268465). E3 ubiquitin-protein ligase activity is activated upon binding to neddylated form of the cullin-5 (CUL5) component of the ECS complex (PubMed:24076655). Together with the ECS(ASB9) complex, catalyzes ubiquitination of CKB (PubMed:33268465). Promotes ubiquitination of DCUN1D1 (PubMed:30587576). Mediates 'Lys-6', 'Lys-48'- and 'Lys-63'-linked polyubiquitination (PubMed:16118314, PubMed:17646546, PubMed:19340006). May play a role in myelopoiesis (PubMed:19340006) (Microbial infection) Following infection by HIV-1 virus, acts together with a cullin-5-RING E3 ubiquitin-protein ligase complex (ECS complex) hijacked by the HIV-1 Vif protein, to catalyze ubiquitination and degradation of APOBEC3F and APOBEC3G

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus. Cytoplasm

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR045840 Ariadne
IPR047555 BRcat_RBR_TRIAD1
IPR031127 E3_UB_ligase_RBR
IPR002867 IBR_dom
IPR047556 Rcat_RBR_TRIAD1
IPR044066 TRIAD_supradom
IPR018957 Znf_C3HC4_RING-type
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS

The S-nitrosylation sites of O95376

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 340 WKTHGSEYYE C SRYKENPDIV