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P61089

- UBE2N_MOUSE

UniProt

P61089 - UBE2N_MOUSE

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Protein
Ubiquitin-conjugating enzyme E2 N
Gene
Ube2n, Blu
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

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. protein binding Source: MGI
  4. ubiquitin binding Source: HGNC
  5. ubiquitin-protein transferase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. DNA double-strand break processing Source: HGNC
  2. T cell receptor signaling pathway Source: HGNC
  3. double-strand break repair via homologous recombination Source: HGNC
  4. histone ubiquitination Source: HGNC
  5. positive regulation of DNA repair Source: HGNC
  6. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: HGNC
  7. positive regulation of NF-kappaB transcription factor activity Source: HGNC
  8. positive regulation of histone modification Source: HGNC
  9. positive regulation of ubiquitin-protein transferase activity Source: HGNC
  10. postreplication repair Source: HGNC
  11. protein K63-linked ubiquitination Source: UniProtKB
  12. protein ubiquitination Source: HGNC
  13. regulation of histone ubiquitination Source: HGNC
  14. ubiquitin-dependent protein catabolic process Source: MGI
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_198527. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
REACT_198533. ISG15 antiviral mechanism.
REACT_198543. IRAK1 recruits IKK complex.
REACT_198546. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
REACT_205561. FCERI mediated NF-kB activation.
REACT_211125. NOD1/2 Signaling Pathway.
REACT_224208. Interleukin-1 signaling.
REACT_225145. Downstream TCR 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: Chromosome 10

Organism-specific databases

MGIiMGI:1934835. Ube2n.

Subcellular locationi

Nucleus By similarity. Cytoplasm By similarity

GO - Cellular componenti

  1. UBC13-MMS2 complex Source: HGNC
  2. UBC13-UEV1A complex Source: UniProtKB
  3. cytoplasm Source: UniProtKB
  4. nucleus Source: UniProtKB
  5. protein complex Source: MGI
  6. ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 152152Ubiquitin-conjugating enzyme E2 N
PRO_0000082504Add
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

MaxQBiP61089.
PaxDbiP61089.
PRIDEiP61089.

2D gel databases

REPRODUCTION-2DPAGEIPI00165854.
P61089.

PTM databases

PhosphoSiteiP61089.

Expressioni

Gene expression databases

BgeeiP61089.
CleanExiMM_UBE2N.
GenevestigatoriP61089.

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.1 Publication

Protein-protein interaction databases

BioGridi220301. 17 interactions.
IntActiP61089. 7 interactions.
MINTiMINT-1869813.

Structurei

3D structure databases

ProteinModelPortaliP61089.
SMRiP61089. Positions 3-152.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00540000070023.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiP61089.
KOiK10580.
OMAiIDIAGEW.
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

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:April 26, 2004 - v1
Checksum:iFACD84D883D77407
GO

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti114 – 1141A → D in BAB24239. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS48677.1.
RefSeqi NP_542127.1. NM_080560.3.
UniGenei Mm.371667.
Mm.440187.
Mm.486592.

3D structure databases

ProteinModelPortali P61089.
SMRi P61089. Positions 3-152.
ModBasei Search...

Protein-protein interaction databases

BioGridi 220301. 17 interactions.
IntActi P61089. 7 interactions.
MINTi MINT-1869813.

Chemistry

BindingDBi P61089.

PTM databases

PhosphoSitei P61089.

2D gel databases

REPRODUCTION-2DPAGE IPI00165854.
P61089.

Proteomic databases

MaxQBi P61089.
PaxDbi P61089.
PRIDEi P61089.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000099329 ; ENSMUSP00000096932 ; ENSMUSG00000074781 .
GeneIDi 93765.
KEGGi mmu:93765.
UCSCi uc007gwm.1. mouse.

Organism-specific databases

CTDi 7334.
MGIi MGI:1934835. Ube2n.

Phylogenomic databases

eggNOGi COG5078.
GeneTreei ENSGT00540000070023.
HOGENOMi HOG000233455.
HOVERGENi HBG063308.
InParanoidi P61089.
KOi K10580.
OMAi IDIAGEW.
OrthoDBi EOG7XWPQB.
PhylomeDBi P61089.
TreeFami TF101126.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_198527. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
REACT_198533. ISG15 antiviral mechanism.
REACT_198543. IRAK1 recruits IKK complex.
REACT_198546. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
REACT_205561. FCERI mediated NF-kB activation.
REACT_211125. NOD1/2 Signaling Pathway.
REACT_224208. Interleukin-1 signaling.
REACT_225145. Downstream TCR signaling.

Miscellaneous databases

NextBioi 28704.
PROi P61089.
SOURCEi Search...

Gene expression databases

Bgeei P61089.
CleanExi MM_UBE2N.
Genevestigatori P61089.

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. 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: September 3, 2014
This is version 122 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

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