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Protein

Ubiquitin-conjugating enzyme E2 N

Gene

Ube2n

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 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).By similarity

Catalytic activityi

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

Enzyme regulationi

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

Pathway: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.PROSITE-ProRule annotation
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

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

GO - Molecular functioni

GO - Biological processi

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_275622. IRAK1 recruits IKK complex.
REACT_278165. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
REACT_280649. Downstream TCR signaling.
REACT_289225. ISG15 antiviral mechanism.
REACT_297122. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
REACT_301153. NOD1/2 Signaling Pathway.
REACT_315145. FCERI mediated NF-kB activation.
REACT_337033. Interleukin-1 signaling.
REACT_360804. CLEC7A (Dectin-1) signaling.
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
Ubc13
Ubiquitin carrier protein N
Ubiquitin-protein ligase N
Gene namesi
Name:Ube2n
Synonyms:Blu
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1934835. Ube2n.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 152152Ubiquitin-conjugating enzyme E2 NPRO_0000082504Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei82 – 821N6-acetyllysineBy 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

MaxQBiP61089.
PaxDbiP61089.
PRIDEiP61089.

2D gel databases

REPRODUCTION-2DPAGEIPI00165854.
P61089.

PTM databases

PhosphoSiteiP61089.

Expressioni

Gene expression databases

BgeeiP61089.
CleanExiMM_UBE2N.
ExpressionAtlasiP61089. baseline and differential.
GenevisibleiP61089. MM.

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).By similarity

Protein-protein interaction databases

BioGridi220301. 16 interactions.
IntActiP61089. 7 interactions.
MINTiMINT-1869813.
STRINGi10090.ENSMUSP00000096932.

Structurei

3D structure databases

ProteinModelPortaliP61089.
SMRiP61089. Positions 3-152.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00540000070023.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiP61089.
KOiK10580.
OMAiYFDVEIH.
OrthoDBiEOG7XWPQB.
PhylomeDBiP61089.
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.

P61089-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGLPRRIIK ETQRLLAEPV PGIKAEPDES NARYFHVVIA GPQDSPFEGG
60 70 80 90 100
TFKLELFLPE EYPMAAPKVR FMTKIYHPNV DKLGRICLDI LKDKWSPALQ
110 120 130 140 150
IRTVLLSIQA LLSAPNPDDP LANDVAEQWK TNEAQAIETA RAWTRLYAMN

NI
Length:152
Mass (Da):17,138
Last modified:April 26, 2004 - v1
Checksum:iFACD84D883D77407
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti114 – 1141A → D in BAB24239 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS48677.1.
RefSeqiNP_542127.1. NM_080560.3.
UniGeneiMm.371667.
Mm.440187.
Mm.486592.

Genome annotation databases

EnsembliENSMUST00000099329; ENSMUSP00000096932; ENSMUSG00000074781.
GeneIDi93765.
KEGGimmu:93765.
UCSCiuc007gwm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS48677.1.
RefSeqiNP_542127.1. NM_080560.3.
UniGeneiMm.371667.
Mm.440187.
Mm.486592.

3D structure databases

ProteinModelPortaliP61089.
SMRiP61089. Positions 3-152.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi220301. 16 interactions.
IntActiP61089. 7 interactions.
MINTiMINT-1869813.
STRINGi10090.ENSMUSP00000096932.

Chemistry

BindingDBiP61089.

PTM databases

PhosphoSiteiP61089.

2D gel databases

REPRODUCTION-2DPAGEIPI00165854.
P61089.

Proteomic databases

MaxQBiP61089.
PaxDbiP61089.
PRIDEiP61089.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000099329; ENSMUSP00000096932; ENSMUSG00000074781.
GeneIDi93765.
KEGGimmu:93765.
UCSCiuc007gwm.1. mouse.

Organism-specific databases

CTDi7334.
MGIiMGI:1934835. Ube2n.

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00540000070023.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiP61089.
KOiK10580.
OMAiYFDVEIH.
OrthoDBiEOG7XWPQB.
PhylomeDBiP61089.
TreeFamiTF101126.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_275622. IRAK1 recruits IKK complex.
REACT_278165. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
REACT_280649. Downstream TCR signaling.
REACT_289225. ISG15 antiviral mechanism.
REACT_297122. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
REACT_301153. NOD1/2 Signaling Pathway.
REACT_315145. FCERI mediated NF-kB activation.
REACT_337033. Interleukin-1 signaling.
REACT_360804. CLEC7A (Dectin-1) signaling.

Miscellaneous databases

NextBioi351655.
PROiP61089.
SOURCEiSearch...

Gene expression databases

BgeeiP61089.
CleanExiMM_UBE2N.
ExpressionAtlasiP61089. baseline and differential.
GenevisibleiP61089. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiUBE2N_MOUSE
AccessioniPrimary (citable) accession number: P61089
Secondary accession number(s): Q16781
, Q3TSL6, Q6ZWZ0, Q9DAJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: June 24, 2015
This is version 131 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.