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Q0P5K3

- UBE2N_BOVIN

UniProt

Q0P5K3 - UBE2N_BOVIN

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Protein

Ubiquitin-conjugating enzyme E2 N

Gene
UBE2N
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

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 activityi

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

Enzyme regulationi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei87 – 871Glycyl thioester intermediate

GO - Molecular functioni

  1. acid-amino acid ligase activity Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  1. DNA double-strand break processing Source: Ensembl
  2. double-strand break repair via homologous recombination Source: Ensembl
  3. histone ubiquitination Source: Ensembl
  4. positive regulation of DNA repair Source: Ensembl
  5. positive regulation of histone modification Source: Ensembl
  6. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  7. positive regulation of NF-kappaB transcription factor activity Source: Ensembl
  8. positive regulation of ubiquitin-protein transferase activity Source: Ensembl
  9. postreplication repair Source: Ensembl
  10. protein K63-linked ubiquitination Source: UniProtKB
  11. regulation of histone ubiquitination Source: Ensembl
  12. T cell receptor signaling pathway Source: Ensembl
  13. ubiquitin-dependent protein catabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_215264. ISG15 antiviral mechanism.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 N (EC:6.3.2.19)
Alternative name(s):
Ubiquitin carrier protein N
Ubiquitin-protein ligase N
Gene namesi
Name:UBE2N
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 5

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: Ensembl
  2. UBC13-MMS2 complex Source: Ensembl
  3. UBC13-UEV1A complex Source: UniProtKB
  4. ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 152152Ubiquitin-conjugating enzyme E2 NPRO_0000278832Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei82 – 821N6-acetyllysine By similarity
Cross-linki92 – 92Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15) By similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiQ0P5K3.
PRIDEiQ0P5K3.

Interactioni

Subunit structurei

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.

Structurei

3D structure databases

ProteinModelPortaliQ0P5K3.
SMRiQ0P5K3. Positions 3-152.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00540000070023.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiQ0P5K3.
KOiK10580.
OMAiDVAKHYK.
OrthoDBiEOG7XWPQB.
TreeFamiTF101126.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q0P5K3-1 [UniParc]FASTAAdd to Basket

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MAGLPRRIIK ETQRLLAEPV PGIKAEPDES NARYFHVVIA GPQDSPFEGG    50
TFKLELFLPE EYPMAAPKVR FMTKIYHPNV DKLGRICLDI LKDKWSPALQ 100
IRTVLLSIQA LLSAPNPDDP LANDVAEQWK TNEAQAIETA RAWTRLYAMN 150
NI 152
Length:152
Mass (Da):17,138
Last modified:September 19, 2006 - v1
Checksum:iFACD84D883D77407
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC119931 mRNA. Translation: AAI19932.1.
RefSeqiNP_001069726.1. NM_001076258.1.
UniGeneiBt.22061.

Genome annotation databases

EnsembliENSBTAT00000052393; ENSBTAP00000052296; ENSBTAG00000021767.
GeneIDi541130.
KEGGibta:541130.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC119931 mRNA. Translation: AAI19932.1 .
RefSeqi NP_001069726.1. NM_001076258.1.
UniGenei Bt.22061.

3D structure databases

ProteinModelPortali Q0P5K3.
SMRi Q0P5K3. Positions 3-152.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi Q0P5K3.

Proteomic databases

PaxDbi Q0P5K3.
PRIDEi Q0P5K3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000052393 ; ENSBTAP00000052296 ; ENSBTAG00000021767 .
GeneIDi 541130.
KEGGi bta:541130.

Organism-specific databases

CTDi 7334.

Phylogenomic databases

eggNOGi COG5078.
GeneTreei ENSGT00540000070023.
HOGENOMi HOG000233455.
HOVERGENi HBG063308.
InParanoidi Q0P5K3.
KOi K10580.
OMAi DVAKHYK.
OrthoDBi EOG7XWPQB.
TreeFami TF101126.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_215264. ISG15 antiviral mechanism.

Miscellaneous databases

NextBioi 20879024.

Family and domain databases

Gene3Di 3.10.110.10. 1 hit.
InterProi IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view ]
Pfami PF00179. UQ_con. 1 hit.
[Graphical view ]
SUPFAMi SSF54495. SSF54495. 1 hit.
PROSITEi PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiUBE2N_BOVIN
AccessioniPrimary (citable) accession number: Q0P5K3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: September 19, 2006
Last modified: September 3, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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