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P61089

- UBE2N_MOUSE

UniProt

P61089 - UBE2N_MOUSE

Protein

Ubiquitin-conjugating enzyme E2 N

Gene

Ube2n

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

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

    GO - Biological processi

    1. DNA double-strand break processing Source: HGNC
    2. double-strand break repair via homologous recombination Source: HGNC
    3. histone ubiquitination Source: HGNC
    4. positive regulation of DNA repair Source: HGNC
    5. positive regulation of histone modification 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 ubiquitin-protein transferase activity Source: HGNC
    9. postreplication repair Source: HGNC
    10. protein K63-linked ubiquitination Source: UniProtKB
    11. protein ubiquitination Source: HGNC
    12. regulation of histone ubiquitination Source: HGNC
    13. T cell receptor signaling pathway Source: HGNC
    14. ubiquitin-dependent protein catabolic process Source: MGI

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

    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.
    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.By similarity

    Protein-protein interaction databases

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

    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.
    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.

    Experimental Info

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

    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 123 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