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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: Ubiquitin-conjugating enzyme E2 N

UniprotKB/SwissProt ID: UBE2N_HUMAN (P61088)

Gene Name: UBE2N

Synonyms: BLU

Organism: Homo sapiens (Human).

Function: The UBE2V1-UBE2N and UBE2V2-UBE2N heterodimers catalyze the synthesis of non-canonical 'Lys-63'-linked polyubiquitin chains. This type of polyubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Acts together with the E3 ligases, HLTF and SHPRH, in the 'Lys-63'-linked poly-ubiquitination of PCNA upon genotoxic stress, which is required for DNA repair. Appears to act together with E3 ligase RNF5 in the 'Lys-63'-linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD. Promotes TRIM5 capsid-specific restriction activity and the UBE2V1-UBE2N heterodimer acts in concert with TRIM5 to generate 'Lys-63'-linked polyubiquitin chains which activate the MAP3K7/TAK1 complex which in turn results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes (By similarity).

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus. Cytoplasm.

PDB :
( If your security settings prevent Jmol from running, please register http://140.138.144.145/ as a safe location in your Java settings. )

Network with metabolic pathway:
Kegg map ID Pathway Link
map04120Ubiquitin mediated proteolysis
Graphical Visualization of S-nitrosylation Sites:
Overview of Protein S-nitrosylation Sites with Functional and Structural Information
InterPro ID Domain
IPR000608

3D Structure Databases:
3D structure databases
EntryMethodResolution (A)ChainPositionsView
1J7D X-ray 1.85 A B1-152Link
2C2V X-ray 2.90 A B/E/H/K2-152Link
3HCT X-ray 2.10 A B1-152Link
3HCU X-ray 2.60 A B/D1-152Link
3VON X-ray 3.15 A C/E/G/J/L/N/Q/S/U/X/Z/b/e/g/i/l/n/p3-150Link
3W31 X-ray 2.96 A B1-152Link
4DHI X-ray 1.80 A D1-152Link
4DHJ X-ray 2.35 A C/G/K/N1-152Link
4DHZ X-ray 3.11 A F1-152Link
4IP3 X-ray 2.30 A B1-152Link
4ORH X-ray 4.80 A B/F/J1-150Link

The S-nitrosylation sites of UBE2N_HUMAN

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site Substrate Motifs PubMed ID Experiment
187HPNVDKLGRI C LDILKDKWSP CCCCCCCCCE E EEECCCCCCC 2.42%HC0322178444-
287HPNVDKLGRI C LDILKDKWSP CCCCCCCCCE E EEECCCCCCC 2.42%HC0319483679in vivo