UBE2W_MOUSE
ID UBE2W_MOUSE Reviewed; 151 AA.
AC Q8VDW4; Q8BVJ8; Q9D5H3;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 W;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme W;
DE AltName: Full=N-terminal E2 ubiquitin-conjugating enzyme;
DE EC=2.3.2.25;
DE AltName: Full=N-terminus-conjugating E2;
DE AltName: Full=Ubiquitin carrier protein W;
DE AltName: Full=Ubiquitin-protein ligase W;
GN Name=Ube2w;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Cerebellum, Corpora quadrigemina, Embryo, Retina, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, AND INTERACTION WITH STUB1.
RX PubMed=21855799; DOI=10.1016/j.molcel.2011.05.036;
RA Scaglione K.M., Zavodszky E., Todi S.V., Patury S., Xu P.,
RA Rodriguez-Lebron E., Fischer S., Konen J., Djarmati A., Peng J.,
RA Gestwicki J.E., Paulson H.L.;
RT "Ube2w and ataxin-3 coordinately regulate the ubiquitin ligase CHIP.";
RL Mol. Cell 43:599-612(2011).
RN [4]
RP FUNCTION, INTERACTION WITH FANCL, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP CYS-91.
RX PubMed=21229326; DOI=10.1007/s10059-011-0015-9;
RA Zhang Y., Zhou X., Zhao L., Li C., Zhu H., Xu L., Shan L., Liao X., Guo Z.,
RA Huang P.;
RT "UBE2W interacts with FANCL and regulates the monoubiquitination of Fanconi
RT anemia protein FANCD2.";
RL Mol. Cells 31:113-122(2011).
CC -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. Specifically monoubiquitinates
CC the N-terminus of various substrates, including ATXN3, MAPT/TAU,
CC POLR2H/RPB8 and STUB1/CHIP, by recognizing backbone atoms of disordered
CC N-termini (PubMed:21855799, PubMed:21229326). Involved in degradation
CC of misfolded chaperone substrates by mediating monoubiquitination of
CC STUB1/CHIP, leading to recruitment of ATXN3 to monoubiquitinated
CC STUB1/CHIP, and restriction of the length of ubiquitin chain attached
CC to STUB1/CHIP substrates by ATXN3 (PubMed:21855799). After UV
CC irradiation, but not after mitomycin-C (MMC) treatment, acts as a
CC specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex
CC by associating with E3 ubiquitin-protein ligase FANCL and catalyzing
CC monoubiquitination of FANCD2, a key step in the DNA damage pathway
CC (PubMed:21229326). In vitro catalyzes 'Lys-11'-linked
CC polyubiquitination. UBE2W-catalyzed ubiquitination occurs also in the
CC presence of inactive RING/U-box type E3s, i.e. lacking the active site
CC cysteine residues to form thioester bonds with ubiquitin, or even in
CC the absence of E3, albeit at a slower rate (By similarity).
CC {ECO:0000250|UniProtKB:Q96B02, ECO:0000269|PubMed:21229326,
CC ECO:0000269|PubMed:21855799}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC Evidence={ECO:0000250|UniProtKB:Q96B02, ECO:0000255|PROSITE-
CC ProRule:PRU00388};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [acceptor protein]-N-terminal-amino acid = [E1 ubiquitin-activating
CC enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein].;
CC EC=2.3.2.25; Evidence={ECO:0000250|UniProtKB:Q96B02};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with FANCL. Interacts
CC with STUB1/CHIP. {ECO:0000250|UniProtKB:Q96B02,
CC ECO:0000269|PubMed:21229326, ECO:0000269|PubMed:21855799}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21229326}. Note=In
CC the nucleus, colocalizes with FANCL.
CC -!- PTM: Autoubiquitinated at Met-1. {ECO:0000250|UniProtKB:Q96B02}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC37094.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK015348; BAB29807.1; -; mRNA.
DR EMBL; AK044463; BAC31935.1; -; mRNA.
DR EMBL; AK046086; BAC32599.1; -; mRNA.
DR EMBL; AK050679; BAC34377.1; -; mRNA.
DR EMBL; AK077997; BAC37094.1; ALT_INIT; mRNA.
DR EMBL; AK082233; BAC38443.1; -; mRNA.
DR EMBL; BC020124; AAH20124.1; -; mRNA.
DR CCDS; CCDS48224.3; -.
DR RefSeq; NP_080049.2; NM_025773.3.
DR AlphaFoldDB; Q8VDW4; -.
DR SMR; Q8VDW4; -.
DR BioGRID; 211726; 1.
DR STRING; 10090.ENSMUSP00000112741; -.
DR PhosphoSitePlus; Q8VDW4; -.
DR MaxQB; Q8VDW4; -.
DR PaxDb; Q8VDW4; -.
DR PeptideAtlas; Q8VDW4; -.
DR PRIDE; Q8VDW4; -.
DR ProteomicsDB; 298404; -.
DR Ensembl; ENSMUST00000117146; ENSMUSP00000112741; ENSMUSG00000025939.
DR GeneID; 66799; -.
DR KEGG; mmu:66799; -.
DR CTD; 55284; -.
DR MGI; MGI:1914049; Ube2w.
DR VEuPathDB; HostDB:ENSMUSG00000025939; -.
DR eggNOG; KOG0427; Eukaryota.
DR GeneTree; ENSGT00940000156908; -.
DR InParanoid; Q8VDW4; -.
DR OMA; YNTQRPR; -.
DR PhylomeDB; Q8VDW4; -.
DR TreeFam; TF314582; -.
DR BRENDA; 2.3.2.25; 3474.
DR Reactome; R-MMU-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 66799; 5 hits in 109 CRISPR screens.
DR ChiTaRS; Ube2w; mouse.
DR PRO; PR:Q8VDW4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8VDW4; protein.
DR Bgee; ENSMUSG00000025939; Expressed in cumulus cell and 255 other tissues.
DR ExpressionAtlas; Q8VDW4; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0071218; P:cellular response to misfolded protein; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IMP:UniProtKB.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA repair; Nucleotide-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..151
FT /note="Ubiquitin-conjugating enzyme E2 W"
FT /id="PRO_0000232690"
FT DOMAIN 3..151
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 91
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT CROSSLNK 1
FT /note="Peptide (Met-Gly) (interchain with G-Cter in
FT ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q96B02"
FT MUTAGEN 91
FT /note="C->S: Loss of in vitro ubiquitin-conjugating
FT activity."
FT /evidence="ECO:0000269|PubMed:21229326"
FT CONFLICT 1
FT /note="M -> L (in Ref. 1; BAC37094)"
FT /evidence="ECO:0000305"
FT CONFLICT 36..38
FT /note="QWI -> HGV (in Ref. 1; BAB29807)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="W -> V (in Ref. 1; BAC37094)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 151 AA; 17345 MW; FCC840E01F4CEB63 CRC64;
MASMQKRLQK ELLALQNDPP PGMTLNEKSV QNSITQWIVD MEGAPGTLYE GEKFQLLFKF
SSRYPFDSPQ VMFTGENIPI HPHVYSNGHI CLSILTEDWS PALSVQSVCL SIISMLSSCK
EKRRPPDNSF YVRTCNKNPK KTKWWYHDDT C
