Q5R7J6 · UBE2N_PONAB

Function

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 (By similarity).
UBE2V1-UBE2N together with TRAF3IP2 E3 ubiquitin ligase mediate 'Lys-63'-linked polyubiquitination of TRAF6, a component of IL17A-mediated signaling pathway

Catalytic activity

  • S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.
    EC:2.3.2.23 (UniProtKB | ENZYME | Rhea)

Activity regulation

Activity is inhibited by binding to OTUB1, which prevents 'Lys-63'-linked polyubiquitination (By similarity).
Activity is inhibited by GPS2, leading to prevent 'Lys-63'-linked polyubiquitination (By similarity).

Pathway

Protein modification; protein ubiquitination.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site87Glycyl thioester intermediate

GO annotations

AspectTerm
Cellular Componentnucleus
Cellular ComponentUBC13-MMS2 complex
Cellular Componentubiquitin ligase complex
Molecular FunctionATP binding
Molecular Functionubiquitin conjugating enzyme activity
Molecular Functionubiquitin-protein transferase activity
Biological Processpostreplication repair
Biological Processprotein K63-linked ubiquitination

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ubiquitin-conjugating enzyme E2 N
  • EC number
  • Alternative names
    • E2 ubiquitin-conjugating enzyme N
    • Ubiquitin carrier protein N
    • Ubiquitin-protein ligase N

Gene names

    • Name
      UBE2N

Organism names

Accessions

  • Primary accession
    Q5R7J6

Proteomes

PTM/Processing

Features

Showing features for chain, modified residue, cross-link.

TypeIDPosition(s)Description
ChainPRO_00000825051-152Ubiquitin-conjugating enzyme E2 N
Modified residue82N6-acetyllysine
Cross-link92Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)

Post-translational modification

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

Keywords

Interaction

Subunit

Heterodimer with UBE2V2 (By similarity).
Interacts (UBE2V2-UBE2N heterodimer) with the E3 ligase STUB1 (via the U-box domain); the complex has a specific 'Lys-63'-linked polyubiquitination activity (By similarity).
Interacts with RNF8 and RNF168 (By similarity).
Interacts with RNF11 (By similarity).
Interacts with the E3 ligases, HLTF and SHPRH; the interactions promote the 'Lys-63'-linked polyubiquitination of PCNA upon genotoxic stress and lead to DNA repair (By similarity).
Interacts with ARIH2 (via RING-type 2) (By similarity).
Interacts with OTUB1; leading to inhibit E2-conjugating activity (By similarity).
Interacts with GPS2; leading to inhibit E2-conjugating activity (By similarity).
Interacts with RIGI and RNF135; involved in RIGI ubiquitination and activation (By similarity).

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain3-149UBC core

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    152
  • Mass (Da)
    17,138
  • Last updated
    2004-12-21 v1
  • Checksum
    FACD84D883D77407
MAGLPRRIIKETQRLLAEPVPGIKAEPDESNARYFHVVIAGPQDSPFEGGTFKLELFLPEEYPMAAPKVRFMTKIYHPNVDKLGRICLDILKDKWSPALQIRTVLLSIQALLSAPNPDDPLANDVAEQWKTNEAQAIETARAWTRLYAMNNI

Computationally mapped potential isoform sequences

There are 5 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8I5U8A0A0A8I5U8A0_PONABUBE2N149
A0A2J8XN72A0A2J8XN72_PONABUBE2N105
A0A8I5YLG9A0A8I5YLG9_PONABUBE2N200
A0A8I5YST4A0A8I5YST4_PONABUBE2N193
A0A8I5YSZ1A0A8I5YSZ1_PONABUBE2N168

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CR860119
EMBL· GenBank· DDBJ
CAH92264.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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