Q8VDW4 (UBE2W_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-conjugating enzyme E2 W
EC=6.3.2.19

Alternative name(s):
Ubiquitin carrier protein W
Ubiquitin-protein ligase W

Gene names

Name:

Ube2w

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	151 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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	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.

Ontologies

Keywords
Biological process	DNA damage DNA repair Ubl conjugation pathway
Cellular component	Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW cellular response to misfolded protein Inferred from mutant phenotype Ref.3. Source: UniProtKB misfolded or incompletely synthesized protein catabolic process Inferred from mutant phenotype Ref.3. Source: UniProtKB proteasomal ubiquitin-dependent protein catabolic process Inferred from mutant phenotype Ref.3. Source: UniProtKB protein K11-linked ubiquitination Inferred from sequence or structural similarity. Source: UniProtKB protein monoubiquitination Inferred from direct assay Ref.3. Source: UniProtKB
Cellular_component	nucleus Inferred from direct assay Ref.4. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Inferred from direct assay Ref.4Ref.3. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 151	151	Ubiquitin-conjugating enzyme E2 W		PRO_0000232690
Sites
	Active site	91	1	Glycyl thioester intermediate By similarity
Experimental info
	Mutagenesis	91	1	C → S: Loss of in vitro ubiquitin-conjugating activity. Ref.4
	Sequence conflict	1	1	M → L in BAC37094. Ref.1
	Sequence conflict	36 – 38	3	QWI → HGV in BAB29807. Ref.1
	Sequence conflict	37	1	W → V in BAC37094. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8VDW4 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: FCC840E01F4CEB63	FASTA	151	17,345
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00462217.
RefSeq	NP_080049.2. NM_025773.3.
UniGene	Mm.122430.
3D structure databases
ProteinModelPortal	Q8VDW4.
SMR	Q8VDW4. Positions 1-117.
ModBase	Search...
PTM databases
PhosphoSite	Q8VDW4.
Proteomic databases
PRIDE	Q8VDW4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000117146; ENSMUSP00000112741; ENSMUSG00000025939.
GeneID	66799.
KEGG	mmu:66799.
UCSC	uc007ajt.1. mouse.
Organism-specific databases
CTD	55284.
MGI	MGI:1914049. Ube2w.
Phylogenomic databases
eggNOG	COG5078.
GeneTree	ENSGT00700000104488.
HOGENOM	HOG000233453.
HOVERGEN	HBG063308.
InParanoid	Q8VDW4.
KO	K10688.
OMA	FTGDNIP.
OrthoDB	EOG49CQ8W.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
ArrayExpress	Q8VDW4.
Bgee	Q8VDW4.
CleanEx	MM_UBE2W.
Genevestigator	Q8VDW4.
Family and domain databases
Gene3D	3.10.110.10. 1 hit.
InterPro	IPR000608. UBQ-conjugat_E2. IPR016135. UBQ-conjugating_enzyme/RWD. [Graphical view]
Pfam	PF00179. UQ_con. 1 hit. [Graphical view]
SUPFAM	SSF54495. UBQ-conjugat/RWD-like. 1 hit.
PROSITE	PS00183. UBIQUITIN_CONJUGAT_1. False negative. PS50127. UBIQUITIN_CONJUGAT_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	322681.
SOURCE	Search...

Entry information

Entry name

UBE2W_MOUSE

Accession

Primary (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 3, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program