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Q5R7J6 (UBE2N_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 152152Ubiquitin-conjugating enzyme E2 N
PRO_0000082505

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
Q5R7J6 [UniParc].

Last modified December 21, 2004. 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]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR860119 mRNA. Translation: CAH92264.1.
RefSeqNP_001127530.1. NM_001134058.1.

3D structure databases

ProteinModelPortalQ5R7J6.
SMRQ5R7J6. Positions 3-152.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ5R7J6.

Proteomic databases

PRIDEQ5R7J6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSPPYT00000005723; ENSPPYP00000005510; ENSPPYG00000004832.
GeneID100174607.
KEGGpon:100174607.

Organism-specific databases

CTD7334.

Phylogenomic databases

GeneTreeENSGT00540000070023.
HOVERGENHBG063308.
InParanoidQ5R7J6.
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...

Entry information

Entry nameUBE2N_PONAB
AccessionPrimary (citable) accession number: Q5R7J6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: December 21, 2004
Last modified: February 19, 2014
This is version 73 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