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Protein

Ubiquitin-conjugating enzyme E2 W

Gene

Ube2w

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

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. ATP binding Source: UniProtKB-KW
  2. ligase activity Source: UniProtKB-KW
  3. small conjugating protein transferase activity Source: GO_Central
  4. ubiquitin conjugating enzyme activity Source: MGI
  5. ubiquitin protein ligase activity Source: GO_Central
  6. ubiquitin protein ligase binding Source: UniProtKB
  7. 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
  7. protein polyubiquitination Source: GO_Central
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

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: Unplaced

Organism-specific databases

MGIiMGI:1914049. Ube2w.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: GO_Central
  2. nucleus Source: UniProtKB
Complete GO annotation...

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

MaxQBiQ8VDW4.
PRIDEiQ8VDW4.

PTM databases

PhosphoSiteiQ8VDW4.

Expressioni

Gene expression databases

BgeeiQ8VDW4.
CleanExiMM_UBE2W.
ExpressionAtlasiQ8VDW4. baseline and differential.
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.
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

        10         20         30         40         50
MASMQKRLQK ELLALQNDPP PGMTLNEKSV QNSITQWIVD MEGAPGTLYE
60 70 80 90 100
GEKFQLLFKF SSRYPFDSPQ VMFTGENIPI HPHVYSNGHI CLSILTEDWS
110 120 130 140 150
PALSVQSVCL SIISMLSSCK EKRRPPDNSF YVRTCNKNPK KTKWWYHDDT

C
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.Curated

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:
EMBLi
GenBanki
DDBJi
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

GeneIDi66799.
KEGGimmu:66799.
UCSCiuc007ajt.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi211726. 1 interaction.

PTM databases

PhosphoSiteiQ8VDW4.

Proteomic databases

MaxQBiQ8VDW4.
PRIDEiQ8VDW4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi66799.
KEGGimmu:66799.
UCSCiuc007ajt.1. mouse.

Organism-specific databases

CTDi55284.
MGIiMGI:1914049. Ube2w.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

NextBioi322681.
PROiQ8VDW4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VDW4.
CleanExiMM_UBE2W.
ExpressionAtlasiQ8VDW4. baseline and differential.
GenevestigatoriQ8VDW4.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: March 4, 2015
This is version 113 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

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.