Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q0P5K3 (UBE2N_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-conjugating enzyme E2 N

EC=6.3.2.19
Alternative name(s):
Ubiquitin carrier protein N
Ubiquitin-protein ligase N
Gene names
Name:UBE2N
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length152 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

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 By similarity. 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.

Catalytic activity

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.

Enzyme regulation

Activity is inhibited by binding to OTUB1, which prevents 'Lys-63'-linked polyubiquitination By similarity.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Heterodimer with UBE2V2. Interacts (UBE2V2-UBE2N heterodimer) with the E3 ligase STUB1 (via the U-box domain); the complex has a specific 'Lys-63'-linked polyubiquitination activity. Interacts with RNF8 and RNF168. Interacts with RNF11. 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. Interacts with ARIH2 (via RING-type 2). Interacts with OTUB1; leading to inhibit E2-conjugating activity By similarity.

Post-translational modification

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

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Ubl conjugation pathway
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
Isopeptide bond
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA double-strand break processing

Inferred from electronic annotation. Source: Ensembl

T cell receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

double-strand break repair via homologous recombination

Inferred from electronic annotation. Source: Ensembl

histone ubiquitination

Inferred from electronic annotation. Source: Ensembl

positive regulation of DNA repair

Inferred from electronic annotation. Source: Ensembl

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of NF-kappaB transcription factor activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of histone modification

Inferred from electronic annotation. Source: Ensembl

positive regulation of ubiquitin-protein transferase activity

Inferred from electronic annotation. Source: Ensembl

postreplication repair

Inferred from electronic annotation. Source: Ensembl

protein K63-linked ubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of histone ubiquitination

Inferred from electronic annotation. Source: Ensembl

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentUBC13-MMS2 complex

Inferred from electronic annotation. Source: Ensembl

UBC13-UEV1A complex

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: Ensembl

ubiquitin ligase complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin-protein transferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 152152Ubiquitin-conjugating enzyme E2 N
PRO_0000278832

Sites

Active site871Glycyl thioester intermediate

Amino acid modifications

Modified residue821N6-acetyllysine By similarity
Cross-link92Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0P5K3 [UniParc].

Last modified September 19, 2006. Version 1.
Checksum: FACD84D883D77407

FASTA15217,138
        10         20         30         40         50         60 
MAGLPRRIIK ETQRLLAEPV PGIKAEPDES NARYFHVVIA GPQDSPFEGG TFKLELFLPE 

        70         80         90        100        110        120 
EYPMAAPKVR FMTKIYHPNV DKLGRICLDI LKDKWSPALQ IRTVLLSIQA LLSAPNPDDP 

       130        140        150 
LANDVAEQWK TNEAQAIETA RAWTRLYAMN NI 

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal skin.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC119931 mRNA. Translation: AAI19932.1.
RefSeqNP_001069726.1. NM_001076258.1.
UniGeneBt.22061.

3D structure databases

ProteinModelPortalQ0P5K3.
SMRQ0P5K3. Positions 3-152.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ0P5K3.

Proteomic databases

PaxDbQ0P5K3.
PRIDEQ0P5K3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000052393; ENSBTAP00000052296; ENSBTAG00000021767.
GeneID541130.
KEGGbta:541130.

Organism-specific databases

CTD7334.

Phylogenomic databases

eggNOGCOG5078.
GeneTreeENSGT00540000070023.
HOGENOMHOG000233455.
HOVERGENHBG063308.
InParanoidQ0P5K3.
KOK10580.
OMADVAKHYK.
OrthoDBEOG7XWPQB.
TreeFamTF101126.

Enzyme and pathway databases

UniPathwayUPA00143.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20879024.

Entry information

Entry nameUBE2N_BOVIN
AccessionPrimary (citable) accession number: Q0P5K3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: September 19, 2006
Last modified: February 19, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways