UBE2N

The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. Studies in mouse suggest that this protein plays a role in DNA postreplication repair. [provided by RefSeq, Jul 2008]

Full Name

Ubiquitin Conjugating Enzyme E2 N

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. Together with RNF135 and UB2V1, catalyzes the viral RNA-dependent 'Lys-63'-linked polyubiquitination of RIGI to activate the downstream signaling pathway that leads to interferon beta production (PubMed:28469175, PubMed:31006531).
UBE2V1-UBE2N together with TRAF3IP2 E3 ubiquitin ligase mediate 'Lys-63'-linked polyubiquitination of TRAF6, a component of IL17A-mediated signaling pathway.

Biological Process

Biological Process DNA double-strand break processing Source:HGNC-UCL1 Publication
Biological Process double-strand break repair via homologous recombination Source:HGNC-UCL1 Publication
Biological Process histone ubiquitination Source:HGNC-UCL1 Publication
Biological Process positive regulation of DNA repair Source:HGNC-UCL1 Publication
Biological Process positive regulation of double-strand break repair Source:ComplexPortal1 Publication
Biological Process positive regulation of histone modification Source:HGNC-UCL1 Publication
Biological Process positive regulation of I-kappaB kinase/NF-kappaB signaling Source:HGNC-UCL1 Publication
Biological Process positive regulation of intracellular signal transduction Source:ComplexPortal1 Publication
Biological Process positive regulation of NF-kappaB transcription factor activity Source:UniProtKB1 Publication
Biological Process positive regulation of protein K63-linked ubiquitination Source:ComplexPortal2 Publications
Biological Process positive regulation of ubiquitin-protein transferase activity Source:HGNC-UCL1 Publication
Biological Process postreplication repair Source:HGNC-UCL1 Publication
Biological Process protein K63-linked ubiquitination Source:UniProtKB4 Publications
Biological Process protein polyubiquitination Source:GO_Central1 Publication
Biological Process protein ubiquitination Source:HGNC-UCL1 Publication
Biological Process regulation of DNA repair Source:ProtInc1 Publication
Biological Process regulation of histone ubiquitination Source:HGNC-UCL1 Publication
Biological Process T cell receptor signaling pathway Source:UniProtKB1 Publication

Cellular Location

Nucleus
Cytoplasm

PTM

Conjugation to ISG15 impairs formation of the thioester bond with ubiquitin but not interaction with UBE2V2.