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Q8VDW4 (UBE2W_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Ube2w
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length151 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.4

Catalytic activity

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

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Homodimer By similarity. Interacts with FANCL. Interacts with STUB1/CHIP. Ref.3 Ref.4

Subcellular location

Nucleus. Note: In the nucleus, colocalizes with FANCL. Ref.4

Post-translational modification

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

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 151151Ubiquitin-conjugating enzyme E2 W
PRO_0000232690

Sites

Active site911Glycyl thioester intermediate By similarity

Amino acid modifications

Cross-link1Peptide (Met-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Mutagenesis911C → S: Loss of in vitro ubiquitin-conjugating activity. Ref.4
Sequence conflict11M → L in BAC37094. Ref.1
Sequence conflict36 – 383QWI → HGV in BAB29807. Ref.1
Sequence conflict371W → V in BAC37094. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8VDW4 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: FCC840E01F4CEB63

FASTA15117,345
        10         20         30         40         50         60 
MASMQKRLQK ELLALQNDPP PGMTLNEKSV QNSITQWIVD MEGAPGTLYE GEKFQLLFKF 

        70         80         90        100        110        120 
SSRYPFDSPQ VMFTGENIPI HPHVYSNGHI CLSILTEDWS PALSVQSVCL SIISMLSSCK 

       130        140        150 
EKRRPPDNSF YVRTCNKNPK KTKWWYHDDT C 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Ube2w and ataxin-3 coordinately regulate the ubiquitin ligase CHIP."
Scaglione K.M., Zavodszky E., Todi S.V., Patury S., Xu P., Rodriguez-Lebron E., Fischer S., Konen J., Djarmati A., Peng J., Gestwicki J.E., Paulson H.L.
Mol. Cell 43:599-612(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_080049.2. NM_025773.3.
UniGeneMm.122430.

3D structure databases

ProteinModelPortalQ8VDW4.
SMRQ8VDW4. Positions 1-117.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid211726. 1 interaction.

PTM databases

PhosphoSiteQ8VDW4.

Proteomic databases

PRIDEQ8VDW4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000182984; ENSMUSP00000138299; ENSMUSG00000025939.
GeneID66799.
KEGGmmu:66799.
UCSCuc007ajt.1. mouse.

Organism-specific databases

CTD55284.
MGIMGI:1914049. Ube2w.

Phylogenomic databases

eggNOGCOG5078.
GeneTreeENSGT00730000110854.
HOGENOMHOG000233453.
HOVERGENHBG063308.
InParanoidQ8VDW4.
KOK10688.
OMAFTGDNIP.
OrthoDBEOG7CG71H.
PhylomeDBQ8VDW4.
TreeFamTF314582.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ8VDW4.
BgeeQ8VDW4.
CleanExMM_UBE2W.
GenevestigatorQ8VDW4.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio322681.
PROQ8VDW4.
SOURCESearch...

Entry information

Entry nameUBE2W_MOUSE
AccessionPrimary (citable) accession number: Q8VDW4
Secondary accession number(s): Q8BVJ8, Q9D5H3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: March 1, 2002
Last modified: April 16, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot