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Q8VDW4

- UBE2W_MOUSE

UniProt

Q8VDW4 - UBE2W_MOUSE

Protein

Ubiquitin-conjugating enzyme E2 W

Gene

Ube2w

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

    Transfers ubiquitin in complex with RING/U-box type E3s that do not have active site cysteine residues to form thioester bonds with ubiquitin, and preferentially ubiquitinates the N-terminus of substrates, such as ATXN3, STUB1 and SUMO2 By similarity. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes monoubiquitination. Involved in degradation of misfolded chaperone substrates by mediating monoubiquitination of STUB1/CHIP, leading to recruitment of ATXN3 to monoubiquitinated STUB1/CHIP, and restriction of the length of ubiquitin chain attached to STUB1/CHIP substrates by ATXN3. After UV irradiation, but not after mitomycin-C (MMC) treatment, acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway. In vitro catalyzes 'Lys-11'-linked polyubiquitination.By similarity2 Publications

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei91 – 911Glycyl thioester intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. acid-amino acid ligase activity Source: InterPro
    2. ATP binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. ubiquitin protein ligase binding Source: UniProtKB
    5. ubiquitin-protein transferase activity Source: UniProtKB

    GO - Biological processi

    1. cellular response to misfolded protein Source: UniProtKB
    2. DNA repair Source: UniProtKB-KW
    3. misfolded or incompletely synthesized protein catabolic process Source: UniProtKB
    4. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    5. protein K11-linked ubiquitination Source: UniProtKB
    6. protein monoubiquitination Source: UniProtKB

    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 W (EC:6.3.2.19)
    Alternative name(s):
    N-terminus-conjugating E2
    Ubiquitin carrier protein W
    Ubiquitin-protein ligase W
    Gene namesi
    Name:Ube2w
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1914049. Ube2w.

    Subcellular locationi

    Nucleus 1 Publication
    Note: In the nucleus, colocalizes with FANCL.

    GO - Cellular componenti

    1. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi91 – 911C → S: Loss of in vitro ubiquitin-conjugating activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 151151Ubiquitin-conjugating enzyme E2 WPRO_0000232690Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki1 – 1Peptide (Met-Gly) (interchain with G-Cter in ubiquitin)By similarity

    Post-translational modificationi

    Autoubiquitinated at Met-1 By similarity. Ubiquitinated in vitro in the presence of FANCL.By similarity

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    PRIDEiQ8VDW4.

    PTM databases

    PhosphoSiteiQ8VDW4.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8VDW4.
    BgeeiQ8VDW4.
    CleanExiMM_UBE2W.
    GenevestigatoriQ8VDW4.

    Interactioni

    Subunit structurei

    Homodimer By similarity. Interacts with FANCL. Interacts with STUB1/CHIP.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi211726. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8VDW4.
    SMRiQ8VDW4. Positions 1-117.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5078.
    GeneTreeiENSGT00730000110854.
    HOGENOMiHOG000233453.
    HOVERGENiHBG063308.
    InParanoidiQ8VDW4.
    KOiK10688.
    OrthoDBiEOG7CG71H.
    PhylomeDBiQ8VDW4.
    TreeFamiTF314582.

    Family and domain databases

    Gene3Di3.10.110.10. 1 hit.
    InterProiIPR000608. UBQ-conjugat_E2.
    IPR016135. UBQ-conjugating_enzyme/RWD.
    [Graphical view]
    PfamiPF00179. UQ_con. 1 hit.
    [Graphical view]
    SUPFAMiSSF54495. SSF54495. 1 hit.
    PROSITEiPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8VDW4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASMQKRLQK ELLALQNDPP PGMTLNEKSV QNSITQWIVD MEGAPGTLYE    50
    GEKFQLLFKF SSRYPFDSPQ VMFTGENIPI HPHVYSNGHI CLSILTEDWS 100
    PALSVQSVCL SIISMLSSCK EKRRPPDNSF YVRTCNKNPK KTKWWYHDDT 150
    C 151
    Length:151
    Mass (Da):17,345
    Last modified:March 1, 2002 - v1
    Checksum:iFCC840E01F4CEB63
    GO

    Sequence cautioni

    The sequence BAC37094.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 11M → L in BAC37094. (PubMed:16141072)Curated
    Sequence conflicti36 – 383QWI → HGV in BAB29807. (PubMed:16141072)Curated
    Sequence conflicti37 – 371W → V in BAC37094. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK015348 mRNA. Translation: BAB29807.1.
    AK044463 mRNA. Translation: BAC31935.1.
    AK046086 mRNA. Translation: BAC32599.1.
    AK050679 mRNA. Translation: BAC34377.1.
    AK077997 mRNA. Translation: BAC37094.1. Different initiation.
    AK082233 mRNA. Translation: BAC38443.1.
    BC020124 mRNA. Translation: AAH20124.1.
    RefSeqiNP_080049.2. NM_025773.3.
    UniGeneiMm.122430.

    Genome annotation databases

    EnsembliENSMUST00000182984; ENSMUSP00000138299; ENSMUSG00000025939.
    GeneIDi66799.
    KEGGimmu:66799.
    UCSCiuc007ajt.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK015348 mRNA. Translation: BAB29807.1 .
    AK044463 mRNA. Translation: BAC31935.1 .
    AK046086 mRNA. Translation: BAC32599.1 .
    AK050679 mRNA. Translation: BAC34377.1 .
    AK077997 mRNA. Translation: BAC37094.1 . Different initiation.
    AK082233 mRNA. Translation: BAC38443.1 .
    BC020124 mRNA. Translation: AAH20124.1 .
    RefSeqi NP_080049.2. NM_025773.3.
    UniGenei Mm.122430.

    3D structure databases

    ProteinModelPortali Q8VDW4.
    SMRi Q8VDW4. Positions 1-117.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 211726. 1 interaction.

    PTM databases

    PhosphoSitei Q8VDW4.

    Proteomic databases

    PRIDEi Q8VDW4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000182984 ; ENSMUSP00000138299 ; ENSMUSG00000025939 .
    GeneIDi 66799.
    KEGGi mmu:66799.
    UCSCi uc007ajt.1. mouse.

    Organism-specific databases

    CTDi 55284.
    MGIi MGI:1914049. Ube2w.

    Phylogenomic databases

    eggNOGi COG5078.
    GeneTreei ENSGT00730000110854.
    HOGENOMi HOG000233453.
    HOVERGENi HBG063308.
    InParanoidi Q8VDW4.
    KOi K10688.
    OrthoDBi EOG7CG71H.
    PhylomeDBi Q8VDW4.
    TreeFami TF314582.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    NextBioi 322681.
    PROi Q8VDW4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8VDW4.
    Bgeei Q8VDW4.
    CleanExi MM_UBE2W.
    Genevestigatori Q8VDW4.

    Family and domain databases

    Gene3Di 3.10.110.10. 1 hit.
    InterProi IPR000608. UBQ-conjugat_E2.
    IPR016135. UBQ-conjugating_enzyme/RWD.
    [Graphical view ]
    Pfami PF00179. UQ_con. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54495. SSF54495. 1 hit.
    PROSITEi PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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, Corpora quadrigemina, Embryo, Retina and Thymus.
    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].
      Strain: Czech II.
      Tissue: Mammary tumor.
    3. Cited for: FUNCTION, INTERACTION WITH STUB1.
    4. "UBE2W interacts with FANCL and regulates the monoubiquitination of Fanconi anemia protein FANCD2."
      Zhang Y., Zhou X., Zhao L., Li C., Zhu H., Xu L., Shan L., Liao X., Guo Z., Huang P.
      Mol. Cells 31:113-122(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FANCL, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-91.

    Entry informationi

    Entry nameiUBE2W_MOUSE
    AccessioniPrimary (citable) accession number: Q8VDW4
    Secondary accession number(s): Q8BVJ8, Q9D5H3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 18, 2006
    Last sequence update: March 1, 2002
    Last modified: October 1, 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, 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