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Q9EQX9

- UBE2N_RAT

UniProt

Q9EQX9 - UBE2N_RAT

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Protein
Ubiquitin-conjugating enzyme E2 N
Gene
Ube2n
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein 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. ATP binding Source: UniProtKB-KW
  2. acid-amino acid ligase activity Source: InterPro
  3. ubiquitin-protein transferase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. DNA repair Source: UniProtKB-KW
  2. protein K63-linked ubiquitination Source: UniProtKB
  3. protein ubiquitination Source: RGD
  4. ubiquitin-dependent protein catabolic process Source: RGD
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

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 N (EC:6.3.2.19)
Alternative name(s):
Bendless-like ubiquitin-conjugating enzyme
Ubiquitin carrier protein N
Ubiquitin-protein ligase N
Gene namesi
Name:Ube2n
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi621096. Ube2n.

Subcellular locationi

GO - Cellular componenti

  1. UBC13-UEV1A complex Source: UniProtKB
  2. ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 152152Ubiquitin-conjugating enzyme E2 N
PRO_0000082506Add
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

PaxDbiQ9EQX9.
PRIDEiQ9EQX9.

PTM databases

PhosphoSiteiQ9EQX9.

Expressioni

Gene expression databases

GenevestigatoriQ9EQX9.

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.

Protein-protein interaction databases

BioGridi250592. 1 interaction.
IntActiQ9EQX9. 1 interaction.
MINTiMINT-1775821.
STRINGi10116.ENSRNOP00000055805.

Structurei

3D structure databases

ProteinModelPortaliQ9EQX9.
SMRiQ9EQX9. Positions 2-150.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5078.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
KOiK10580.
PhylomeDBiQ9EQX9.
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.

Q9EQX9-1 [UniParc]FASTAAdd to Basket

« Hide

MAGLPRRIIK ETQRLLAEPV PGIKAEPDES NARYFHVVIA GPQDSPFEGG    50
TFKLELFLPE EYPMAAPKVR FMTKIYHPNV DKLGRICLDI LKDKWSPALQ 100
IRTVLLSIQA LLSAPNPDDP LANDVAEQWK SNEAQAIETA RAWTRLYAMN 150
NI 152
Length:152
Mass (Da):17,124
Last modified:March 1, 2001 - v1
Checksum:iFACD84D883D27457
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB032739 mRNA. Translation: BAB20414.1.
BC090072 mRNA. Translation: AAH90072.1.
RefSeqiNP_446380.1. NM_053928.2.
UniGeneiRn.230134.

Genome annotation databases

GeneIDi116725.
KEGGirno:116725.
UCSCiRGD:621096. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB032739 mRNA. Translation: BAB20414.1 .
BC090072 mRNA. Translation: AAH90072.1 .
RefSeqi NP_446380.1. NM_053928.2.
UniGenei Rn.230134.

3D structure databases

ProteinModelPortali Q9EQX9.
SMRi Q9EQX9. Positions 2-150.
ModBasei Search...

Protein-protein interaction databases

BioGridi 250592. 1 interaction.
IntActi Q9EQX9. 1 interaction.
MINTi MINT-1775821.
STRINGi 10116.ENSRNOP00000055805.

PTM databases

PhosphoSitei Q9EQX9.

Proteomic databases

PaxDbi Q9EQX9.
PRIDEi Q9EQX9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 116725.
KEGGi rno:116725.
UCSCi RGD:621096. rat.

Organism-specific databases

CTDi 7334.
RGDi 621096. Ube2n.

Phylogenomic databases

eggNOGi COG5078.
HOGENOMi HOG000233455.
HOVERGENi HBG063308.
KOi K10580.
PhylomeDBi Q9EQX9.
TreeFami TF101126.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

NextBioi 619648.
PROi Q9EQX9.

Gene expression databases

Genevestigatori Q9EQX9.

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

« Hide 'large scale' publications
  1. "Expression of rat Bendless gene in the developing brain."
    Takahashi H., Yamamoto M., Saito Y.
    Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  3. Lubec G., Afjehi-Sadat L., Diao W.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 34-68, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus and Spinal cord.
  4. Maurya D.K., Bhargava P.
    Submitted (DEC-2008) to UniProtKB
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiUBE2N_RAT
AccessioniPrimary (citable) accession number: Q9EQX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: March 1, 2001
Last modified: September 3, 2014
This is version 109 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, Direct protein sequencing, 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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