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   27-MAR-2024, entry version 161.
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; 2.
DR   STRING; 10090.ENSMUSP00000157633; -.
DR   PhosphoSitePlus; Q8VDW4; -.
DR   MaxQB; Q8VDW4; -.
DR   PaxDb; 10090-ENSMUSP00000112741; -.
DR   PeptideAtlas; Q8VDW4; -.
DR   ProteomicsDB; 298404; -.
DR   Pumba; Q8VDW4; -.
DR   Ensembl; ENSMUST00000117146.9; ENSMUSP00000112741.4; ENSMUSG00000025939.20.
DR   GeneID; 66799; -.
DR   KEGG; mmu:66799; -.
DR   AGR; MGI:1914049; -.
DR   CTD; 55284; -.
DR   MGI; MGI:1914049; Ube2w.
DR   VEuPathDB; HostDB:ENSMUSG00000025939; -.
DR   eggNOG; KOG0427; Eukaryota.
DR   GeneTree; ENSGT00940000156908; -.
DR   InParanoid; Q8VDW4; -.
DR   OMA; HNVESVC; -.
DR   OrthoDB; 452at2759; -.
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 114 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 258 other cell types or 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:0140374; P:antiviral innate immune response; ISO:MGI.
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:1904262; P:negative regulation of TORC1 signaling; ISO:MGI.
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; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   PANTHER; PTHR24067:SF373; UBIQUITIN-CONJUGATING ENZYME E2 W; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 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
//