UBE2W_HUMAN
ID UBE2W_HUMAN Reviewed; 151 AA.
AC Q96B02; B4DIV1; Q1XBE0; Q9H823; Q9HAG6; Q9NV07;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 W;
DE EC=2.3.2.23 {ECO:0000269|PubMed:20061386};
DE AltName: Full=E2 ubiquitin-conjugating enzyme W;
DE AltName: Full=N-terminal E2 ubiquitin-conjugating enzyme;
DE EC=2.3.2.25 {ECO:0000269|PubMed:23560854, ECO:0000269|PubMed:23696636};
DE AltName: Full=N-terminus-conjugating E2;
DE AltName: Full=Ubiquitin carrier protein W;
DE AltName: Full=Ubiquitin-conjugating enzyme 16;
DE Short=UBC-16;
DE AltName: Full=Ubiquitin-protein ligase W;
GN Name=UBE2W; Synonyms=UBC16;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF CYS-91.
RX PubMed=16368532; DOI=10.2741/1899;
RA Yin G., Ji C., Wu T., Shen Z., Xu X., Xie Y., Mao Y.;
RT "Cloning, characterization and subcellular localization of a gene encoding
RT a human Ubiquitin-conjugating enzyme (E2) homologous to the Arabidopsis
RT thaliana UBC-16 gene product.";
RL Front. Biosci. 11:1500-1507(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Embryo, Hippocampus, and Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Urinary bladder;
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 [7]
RP FUNCTION, AND INTERACTION WITH FANCL.
RX PubMed=19111657; DOI=10.1016/j.molcel.2008.12.003;
RA Alpi A.F., Pace P.E., Babu M.M., Patel K.J.;
RT "Mechanistic insight into site-restricted monoubiquitination of FANCD2 by
RT Ube2t, FANCL, and FANCI.";
RL Mol. Cell 32:767-777(2008).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20061386; DOI=10.1074/jbc.m109.089003;
RA David Y., Ziv T., Admon A., Navon A.;
RT "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to
RT preferred lysines.";
RL J. Biol. Chem. 285:8595-8604(2010).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 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).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, UBIQUITINATION AT MET-1, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=23560854; DOI=10.1042/bj20130244;
RA Tatham M.H., Plechanovova A., Jaffray E.G., Salmen H., Hay R.T.;
RT "Ube2W conjugates ubiquitin to alpha-amino groups of protein N-termini.";
RL Biochem. J. 453:137-145(2013).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND MUTAGENESIS OF
RP HIS-83.
RX PubMed=23696636; DOI=10.1074/jbc.c113.477596;
RA Scaglione K.M., Basrur V., Ashraf N.S., Konen J.R., Elenitoba-Johnson K.S.,
RA Todi S.V., Paulson H.L.;
RT "The ubiquitin-conjugating enzyme (E2) Ube2w ubiquitinates the N terminus
RT of substrates.";
RL J. Biol. Chem. 288:18784-18788(2013).
RN [12] {ECO:0007744|PDB:2A7L}
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 1-117, AND AUTOUBIQUITINATION.
RX PubMed=22496338; DOI=10.1074/mcp.o111.013706;
RA Sheng Y., Hong J.H., Doherty R., Srikumar T., Shloush J., Avvakumov G.V.,
RA Walker J.R., Xue S., Neculai D., Wan J.W., Kim S.K., Arrowsmith C.H.,
RA Raught B., Dhe-Paganon S.;
RT "A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-
RT function screen.";
RL Mol. Cell. Proteomics 11:329-341(2012).
RN [13] {ECO:0007744|PDB:2MT6}
RP STRUCTURE BY NMR, FUNCTION, AND MUTAGENESIS OF 132-VAL--TRP-145 AND
RP TRP-144.
RX PubMed=25436519; DOI=10.1038/nchembio.1700;
RA Vittal V., Shi L., Wenzel D.M., Scaglione K.M., Duncan E.D., Basrur V.,
RA Elenitoba-Johnson K.S., Baker D., Paulson H.L., Brzovic P.S., Klevit R.E.;
RT "Intrinsic disorder drives N-terminal ubiquitination by Ube2w.";
RL Nat. Chem. Biol. 11:83-89(2015).
CC -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins (PubMed:20061386,
CC PubMed:21229326). Specifically monoubiquitinates the N-terminus of
CC various substrates, including ATXN3, MAPT/TAU, POLR2H/RPB8 and
CC STUB1/CHIP, by recognizing backbone atoms of disordered N-termini
CC (PubMed:23560854, PubMed:23696636, PubMed:25436519). Involved in
CC degradation of misfolded chaperone substrates by mediating
CC monoubiquitination of STUB1/CHIP, leading to recruitment of ATXN3 to
CC monoubiquitinated STUB1/CHIP, and restriction of the length of
CC ubiquitin chain attached to STUB1/CHIP substrates by ATXN3. 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:19111657, 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 (PubMed:25436519).
CC {ECO:0000269|PubMed:19111657, ECO:0000269|PubMed:20061386,
CC ECO:0000269|PubMed:21229326, ECO:0000269|PubMed:23560854,
CC ECO:0000269|PubMed:23696636, ECO:0000269|PubMed:25436519}.
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:0000255|PROSITE-ProRule:PRU00388,
CC ECO:0000269|PubMed:20061386};
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:0000269|PubMed:23560854,
CC ECO:0000269|PubMed:23696636};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: Homodimer. Interacts with FANCL (PubMed:19111657,
CC PubMed:21229326). Interacts with STUB1/CHIP (By similarity).
CC {ECO:0000250|UniProtKB:Q8VDW4, ECO:0000269|PubMed:19111657,
CC ECO:0000269|PubMed:21229326}.
CC -!- INTERACTION:
CC Q96B02; P48643: CCT5; NbExp=3; IntAct=EBI-716589, EBI-355710;
CC Q96B02; Q9NX47: MARCHF5; NbExp=5; IntAct=EBI-716589, EBI-2341610;
CC Q96B02; O43586: PSTPIP1; NbExp=4; IntAct=EBI-716589, EBI-1050964;
CC Q96B02; Q99942: RNF5; NbExp=4; IntAct=EBI-716589, EBI-348482;
CC Q96B02; Q9HAT0: ROPN1; NbExp=3; IntAct=EBI-716589, EBI-1378139;
CC Q96B02; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-716589, EBI-739895;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16368532,
CC ECO:0000269|PubMed:21229326}. Note=In the nucleus, colocalizes with
CC FANCL. {ECO:0000269|PubMed:21229326}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96B02-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96B02-2; Sequence=VSP_017943;
CC Name=3;
CC IsoId=Q96B02-3; Sequence=VSP_042974;
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest expression in brain,
CC liver, pancreas and heart. {ECO:0000269|PubMed:16368532}.
CC -!- PTM: Autoubiquitinated at Met-1. {ECO:0000269|PubMed:22496338,
CC ECO:0000269|PubMed:23560854}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; AY948289; AAY24555.1; -; mRNA.
DR EMBL; AK001873; BAA91954.1; -; mRNA.
DR EMBL; AK021735; BAB13883.1; -; mRNA.
DR EMBL; AK024050; BAB14800.1; -; mRNA.
DR EMBL; AK295792; BAG58613.1; -; mRNA.
DR EMBL; CR457275; CAG33556.1; -; mRNA.
DR EMBL; CH471068; EAW87009.1; -; Genomic_DNA.
DR EMBL; CH471068; EAW87011.1; -; Genomic_DNA.
DR EMBL; AC022826; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016326; AAH16326.1; -; mRNA.
DR CCDS; CCDS47874.2; -. [Q96B02-1]
DR CCDS; CCDS47875.2; -. [Q96B02-2]
DR RefSeq; NP_001001481.2; NM_001001481.2. [Q96B02-2]
DR RefSeq; NP_001257944.1; NM_001271015.1.
DR RefSeq; NP_060769.4; NM_018299.4. [Q96B02-1]
DR PDB; 2A7L; X-ray; 1.82 A; A/B=1-117.
DR PDB; 2MT6; NMR; -; A=1-151.
DR PDBsum; 2A7L; -.
DR PDBsum; 2MT6; -.
DR AlphaFoldDB; Q96B02; -.
DR SMR; Q96B02; -.
DR BioGRID; 120572; 96.
DR DIP; DIP-52724N; -.
DR IntAct; Q96B02; 73.
DR MINT; Q96B02; -.
DR STRING; 9606.ENSP00000397453; -.
DR MoonDB; Q96B02; Predicted.
DR iPTMnet; Q96B02; -.
DR PhosphoSitePlus; Q96B02; -.
DR BioMuta; UBE2W; -.
DR DMDM; 74751754; -.
DR EPD; Q96B02; -.
DR MassIVE; Q96B02; -.
DR MaxQB; Q96B02; -.
DR PaxDb; Q96B02; -.
DR PeptideAtlas; Q96B02; -.
DR PRIDE; Q96B02; -.
DR ProteomicsDB; 76030; -. [Q96B02-1]
DR ProteomicsDB; 76031; -. [Q96B02-2]
DR ProteomicsDB; 76032; -. [Q96B02-3]
DR Antibodypedia; 25199; 174 antibodies from 26 providers.
DR DNASU; 55284; -.
DR Ensembl; ENST00000517608.5; ENSP00000428813.2; ENSG00000104343.21. [Q96B02-3]
DR Ensembl; ENST00000602593.6; ENSP00000473561.1; ENSG00000104343.21. [Q96B02-1]
DR Ensembl; ENST00000651945.1; ENSP00000499153.1; ENSG00000104343.21. [Q96B02-2]
DR GeneID; 55284; -.
DR KEGG; hsa:55284; -.
DR MANE-Select; ENST00000602593.6; ENSP00000473561.1; NM_018299.6; NP_060769.5.
DR UCSC; uc003xzv.4; human. [Q96B02-1]
DR CTD; 55284; -.
DR DisGeNET; 55284; -.
DR GeneCards; UBE2W; -.
DR HGNC; HGNC:25616; UBE2W.
DR HPA; ENSG00000104343; Low tissue specificity.
DR MIM; 614277; gene.
DR neXtProt; NX_Q96B02; -.
DR OpenTargets; ENSG00000104343; -.
DR PharmGKB; PA142670657; -.
DR VEuPathDB; HostDB:ENSG00000104343; -.
DR eggNOG; KOG0427; Eukaryota.
DR GeneTree; ENSGT00940000156908; -.
DR HOGENOM; CLU_030988_15_1_1; -.
DR InParanoid; Q96B02; -.
DR OMA; YNTQRPR; -.
DR OrthoDB; 1522577at2759; -.
DR PhylomeDB; Q96B02; -.
DR TreeFam; TF314582; -.
DR BioCyc; MetaCyc:HS11901-MON; -.
DR BRENDA; 2.3.2.24; 2681.
DR BRENDA; 2.3.2.25; 2681.
DR PathwayCommons; Q96B02; -.
DR Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q96B02; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 55284; 27 hits in 1054 CRISPR screens.
DR ChiTaRS; UBE2W; human.
DR EvolutionaryTrace; Q96B02; -.
DR GenomeRNAi; 55284; -.
DR Pharos; Q96B02; Tbio.
DR PRO; PR:Q96B02; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q96B02; protein.
DR Bgee; ENSG00000104343; Expressed in oocyte and 186 other tissues.
DR ExpressionAtlas; Q96B02; baseline and differential.
DR Genevisible; Q96B02; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; IDA: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; ISS:UniProtKB.
DR CDD; cd00195; UBCc; 1.
DR DisProt; DP01337; -.
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 3D-structure; Alternative splicing; ATP-binding; DNA damage; DNA repair;
KW Nucleotide-binding; Nucleus; Reference proteome; Transferase;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..151
FT /note="Ubiquitin-conjugating enzyme E2 W"
FT /id="PRO_0000232689"
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:0000269|PubMed:23560854"
FT VAR_SEQ 1
FT /note="M -> MLSPRGVTRARQLLPLRLWPRRSWGDGSIM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042974"
FT VAR_SEQ 5
FT /note="Q -> QTTGRRVEVWFP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:16368532"
FT /id="VSP_017943"
FT MUTAGEN 83
FT /note="H->N: Impaired substrate ubiquitination of both Tau
FT and ATXN3."
FT /evidence="ECO:0000269|PubMed:23696636"
FT MUTAGEN 91
FT /note="C->A: Loss of predominant nuclear localization."
FT /evidence="ECO:0000269|PubMed:16368532"
FT MUTAGEN 91
FT /note="C->S: Loss of ubiquitin conjugating activity."
FT /evidence="ECO:0000269|PubMed:21229326"
FT MUTAGEN 132..145
FT /note="Missing: Loss of ubiquitination activity."
FT /evidence="ECO:0000269|PubMed:25436519"
FT MUTAGEN 144
FT /note="W->E: Loss of ubiquitination activity toward various
FT substrates, including POLR2H, ATXN3, STUB1 and MAPT."
FT /evidence="ECO:0000269|PubMed:25436519"
FT CONFLICT 26
FT /note="N -> S (in Ref. 2; BAB13883)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="P -> S (in Ref. 2; BAA91954)"
FT /evidence="ECO:0000305"
FT HELIX 6..17
FT /evidence="ECO:0007829|PDB:2A7L"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:2MT6"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:2A7L"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:2A7L"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:2A7L"
FT TURN 62..66
FT /evidence="ECO:0007829|PDB:2A7L"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:2A7L"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:2MT6"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:2A7L"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:2A7L"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:2A7L"
FT HELIX 128..133
FT /evidence="ECO:0007829|PDB:2MT6"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:2MT6"
SQ SEQUENCE 151 AA; 17331 MW; 276B585BBC4CEB71 CRC64;
MASMQKRLQK ELLALQNDPP PGMTLNEKSV QNSITQWIVD MEGAPGTLYE GEKFQLLFKF
SSRYPFDSPQ VMFTGENIPV HPHVYSNGHI CLSILTEDWS PALSVQSVCL SIISMLSSCK
EKRRPPDNSF YVRTCNKNPK KTKWWYHDDT C
