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P61089 (UBE2N_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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):
Bendless-like ubiquitin-conjugating enzyme
Ubc13
Ubiquitin carrier protein N
Ubiquitin-protein ligase N
Gene names
Name:Ube2n
Synonyms:Blu
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length152 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. Ref.6

Subcellular location

Nucleus By similarity. Cytoplasm 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 caution

The sequence BAE36659.1 differs from that shown. Reason: Frameshift at position 105.

Ontologies

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

Inferred from sequence or structural similarity. Source: HGNC

T cell receptor signaling pathway

Inferred from sequence or structural similarity PubMed 15125833. Source: HGNC

double-strand break repair via homologous recombination

Inferred from sequence or structural similarity. Source: HGNC

histone ubiquitination

Inferred from sequence or structural similarity. Source: HGNC

positive regulation of DNA repair

Inferred from sequence or structural similarity. Source: HGNC

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

Inferred from sequence or structural similarity. Source: HGNC

positive regulation of NF-kappaB transcription factor activity

Inferred from sequence or structural similarity PubMed 14695475. Source: HGNC

positive regulation of histone modification

Inferred from sequence or structural similarity. Source: HGNC

positive regulation of ubiquitin-protein transferase activity

Inferred from sequence or structural similarity. Source: HGNC

postreplication repair

Inferred from sequence or structural similarity. Source: HGNC

protein K63-linked ubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein ubiquitination

Inferred from sequence or structural similarity. Source: HGNC

regulation of histone ubiquitination

Inferred from sequence or structural similarity. Source: HGNC

ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.2. Source: MGI

   Cellular_componentUBC13-MMS2 complex

Inferred from sequence or structural similarity. Source: HGNC

UBC13-UEV1A complex

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

protein complex

Inferred from sequence orthology PubMed 22797923. Source: MGI

ubiquitin ligase complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 23776175. Source: MGI

ubiquitin binding

Inferred from sequence or structural similarity. Source: HGNC

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_0000082504

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

Experimental info

Sequence conflict1141A → D in BAB24239. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P61089 [UniParc].

Last modified April 26, 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

« Hide 'large scale' references
[1]Rugarli E.I., Valsecchi V., Ballabio A.
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ICR X Swiss Webster.
[2]"Roles of mouse UBC13 in DNA postreplication repair and Lys63-linked ubiquitination."
Ashley C., Pastushok L., McKenna S., Ellison M.J., Xiao W.
Gene 285:183-191(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: B-cell.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cerebellum, Olfactory bulb and Testis.
[4]"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].
Strain: C57BL/6.
Tissue: Eye and Mammary gland.
[5]Lubec G., Klug S., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 15-24; 34-68; 95-102 AND 131-141, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[6]"Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex."
Zhang M., Windheim M., Roe S.M., Peggie M., Cohen P., Prodromou C., Pearl L.H.
Mol. Cell 20:525-538(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH STUB1 AND UBE2V1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y09873 mRNA. Translation: CAA71001.1.
AY039837 mRNA. Translation: AAK74128.1.
AK005302 mRNA. Translation: BAB23941.1.
AK005788 mRNA. Translation: BAB24239.1.
AK161968 mRNA. Translation: BAE36659.1. Frameshift.
BC034898 mRNA. Translation: AAH34898.3.
BC067069 mRNA. Translation: AAH67069.1.
CCDSCCDS48677.1.
RefSeqNP_542127.1. NM_080560.3.
UniGeneMm.371667.
Mm.440187.
Mm.486592.

3D structure databases

ProteinModelPortalP61089.
SMRP61089. Positions 3-152.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid220301. 17 interactions.
IntActP61089. 7 interactions.
MINTMINT-1869813.

Chemistry

BindingDBP61089.

PTM databases

PhosphoSiteP61089.

2D gel databases

REPRODUCTION-2DPAGEIPI00165854.
P61089.

Proteomic databases

MaxQBP61089.
PaxDbP61089.
PRIDEP61089.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000099329; ENSMUSP00000096932; ENSMUSG00000074781.
GeneID93765.
KEGGmmu:93765.
UCSCuc007gwm.1. mouse.

Organism-specific databases

CTD7334.
MGIMGI:1934835. Ube2n.

Phylogenomic databases

eggNOGCOG5078.
GeneTreeENSGT00540000070023.
HOGENOMHOG000233455.
HOVERGENHBG063308.
InParanoidP61089.
KOK10580.
OMAIDIAGEW.
OrthoDBEOG7XWPQB.
PhylomeDBP61089.
TreeFamTF101126.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

BgeeP61089.
CleanExMM_UBE2N.
GenevestigatorP61089.

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

NextBio28704.
PROP61089.
SOURCESearch...

Entry information

Entry nameUBE2N_MOUSE
AccessionPrimary (citable) accession number: P61089
Secondary accession number(s): Q16781 expand/collapse secondary AC list , Q3TSL6, Q6ZWZ0, Q9DAJ6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: July 9, 2014
This is version 121 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot