ID UBE2N_DROME Reviewed; 151 AA. AC P35128; A9YHJ7; Q9VY67; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 02-SEP-2026, entry version 196. DE RecName: Full=Ubiquitin-conjugating enzyme E2 N; DE EC=2.3.2.23; DE AltName: Full=E2 ubiquitin-conjugating enzyme N; DE AltName: Full=Protein bendless; DE AltName: Full=Ubiquitin carrier protein N; DE AltName: Full=Ubiquitin-conjugating enzyme E2-17 kDa; DE AltName: Full=Ubiquitin-protein ligase D3; DE AltName: Full=Ubiquitin-protein ligase N; GN Name=ben; Synonyms=UbcD3; ORFNames=CG18319; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida; OC Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota; OC Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND DISRUPTION PHENOTYPE. RX PubMed=8394720; DOI=10.1016/0896-6273(93)90182-q; RA Muralidhar M., Thomas J.B.; RT "The Drosophila bendless gene encodes a neural protein related to RT ubiquitin-conjugating enzymes."; RL Neuron 11:253-266(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8182464; DOI=10.1523/jneurosci.14-05-03166.1994; RA Oh C.E., McMahon R., Benzer S., Tanouye M.A.; RT "Bendless, a Drosophila gene affecting neuronal connectivity, encodes a RT ubiquitin-conjugating enzyme homolog."; RL J. Neurosci. 14:3166-3179(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ZW104, ZW109, ZW122, ZW123, ZW133, ZW136, ZW139, ZW140, ZW141, RC ZW142, ZW143, and ZW144; RX PubMed=17989248; DOI=10.1101/gr.6691007; RA Andolfatto P.; RT "Hitchhiking effects of recurrent beneficial amino acid substitutions in RT the Drosophila melanogaster genome."; RL Genome Res. 17:1755-1762(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., RA Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP GENOME REANNOTATION. RC STRAIN=Berkeley; RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic RT review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Embryo; RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., RA Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other CC proteins. 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, ECO:0000255|PROSITE- CC ProRule:PRU10133}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000255|PROSITE-ProRule:PRU00388}. CC -!- INTERACTION: CC P35128; Q9VRL1: Uev1A; NbExp=4; IntAct=EBI-101550, EBI-192329; CC -!- DISRUPTION PHENOTYPE: Mutants in this gene exhibit several, largely CC neuronal defects including lesions affecting the neuronal connectivity CC of the giant fiber with the 'jumping muscle', and the axons of CC photoreceptor cells R7 and R8 fail to make the proper right-angle turn CC into the medulla (hence the term 'bendless'). CC {ECO:0000269|PubMed:8394720}. CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. CC {ECO:0000255|PROSITE-ProRule:PRU00388}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L20126; AAA28392.1; -; mRNA. DR EMBL; S70118; AAB30753.1; -; mRNA. DR EMBL; EU217226; ABW92183.1; -; Genomic_DNA. DR EMBL; EU217227; ABW92184.1; -; Genomic_DNA. DR EMBL; EU217228; ABW92185.1; -; Genomic_DNA. DR EMBL; EU217229; ABW92186.1; -; Genomic_DNA. DR EMBL; EU217230; ABW92187.1; -; Genomic_DNA. DR EMBL; EU217231; ABW92188.1; -; Genomic_DNA. DR EMBL; EU217232; ABW92189.1; -; Genomic_DNA. DR EMBL; EU217233; ABW92190.1; -; Genomic_DNA. DR EMBL; EU217234; ABW92191.1; -; Genomic_DNA. DR EMBL; EU217235; ABW92192.1; -; Genomic_DNA. DR EMBL; EU217236; ABW92193.1; -; Genomic_DNA. DR EMBL; EU217237; ABW92194.1; -; Genomic_DNA. DR EMBL; AE014298; AAF48338.1; -; Genomic_DNA. DR EMBL; AY069527; AAL39672.1; -; mRNA. DR PIR; S35793; S35793. DR RefSeq; NP_001162752.1; NM_001169281.2. DR RefSeq; NP_001245663.1; NM_001258734.2. DR RefSeq; NP_001259540.1; NM_001272611.2. DR RefSeq; NP_001259541.1; NM_001272612.2. DR RefSeq; NP_511150.1; NM_078595.3. DR AlphaFoldDB; P35128; -. DR SMR; P35128; -. DR BioGRID; 58728; 19. DR DIP; DIP-22866N; -. DR FunCoup; P35128; 2295. DR IntAct; P35128; 17. DR STRING; 7227.FBpp0298297; -. DR PaxDb; 7227-FBpp0298297; -. DR PeptideAtlas; P35128; -. DR DNASU; 32358; -. DR EnsemblMetazoa; FBtr0073855; FBpp0073686; FBgn0000173. DR EnsemblMetazoa; FBtr0300566; FBpp0289793; FBgn0000173. DR EnsemblMetazoa; FBtr0307296; FBpp0298297; FBgn0000173. DR EnsemblMetazoa; FBtr0332843; FBpp0305066; FBgn0000173. DR EnsemblMetazoa; FBtr0332844; FBpp0305067; FBgn0000173. DR GeneID; 32358; -. DR KEGG; dme:Dmel_CG18319; -. DR UCSC; CG18319-RA; d. melanogaster. DR AGR; FB:FBgn0000173; -. DR CTD; 32358; -. DR FlyBase; FBgn0000173; ben. DR VEuPathDB; VectorBase:FBgn0000173; -. DR eggNOG; KOG0417; Eukaryota. DR HOGENOM; CLU_030988_13_2_1; -. DR InParanoid; P35128; -. DR OMA; AEPHEDN; -. DR OrthoDB; 7851174at2759; -. DR PhylomeDB; P35128; -. DR Reactome; R-DME-209447; Activation of the IkappaB kinase complex, KEY:IRD5 dimer:KEY. DR Reactome; R-DME-445989; TAK1-dependent IKK and NF-kappa-B activation. DR Reactome; R-DME-5205685; PINK1-PRKN Mediated Mitophagy. DR Reactome; R-DME-9020702; Interleukin-1 signaling. DR Reactome; R-DME-937039; IRAK1 recruits IKK complex. DR Reactome; R-DME-9646399; Aggrephagy. DR Reactome; R-DME-975144; IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation. DR Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; P35128; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 32358; 0 hits in 3 CRISPR screens. DR GenomeRNAi; 32358; -. DR PRO; PR:P35128; -. DR Proteomes; UP000000803; Chromosome X. DR Bgee; FBgn0000173; Expressed in wing disc and 300 other cell types or tissues. DR ExpressionAtlas; P35128; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:FlyBase. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:FlyBase. DR GO; GO:0031372; C:UBC13-MMS2 complex; IDA:FlyBase. DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:FlyBase. DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IPI:FlyBase. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:FlyBase. DR GO; GO:0007412; P:axon target recognition; IMP:FlyBase. DR GO; GO:0007409; P:axonogenesis; IMP:FlyBase. DR GO; GO:0007629; P:flight behavior; IMP:FlyBase. DR GO; GO:0007625; P:grooming behavior; IMP:FlyBase. DR GO; GO:0007630; P:jump response; IMP:FlyBase. DR GO; GO:0061057; P:peptidoglycan recognition protein signaling pathway; IMP:FlyBase. DR GO; GO:0008594; P:photoreceptor cell morphogenesis; IMP:FlyBase. DR GO; GO:0046330; P:positive regulation of JNK cascade; IGI:FlyBase. DR GO; GO:0045977; P:positive regulation of mitotic cell cycle, embryonic; IMP:FlyBase. DR GO; GO:0043068; P:positive regulation of programmed cell death; IGI:FlyBase. DR GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; IGI:FlyBase. DR GO; GO:0070534; P:protein K63-linked ubiquitination; IBA:GO_Central. DR GO; GO:0000209; P:protein polyubiquitination; IDA:FlyBase. DR GO; GO:0072347; P:response to anesthetic; IMP:FlyBase. DR GO; GO:0006979; P:response to oxidative stress; IMP:FlyBase. DR GO; GO:0060074; P:synapse maturation; IMP:FlyBase. DR GO; GO:0051124; P:synaptic assembly at neuromuscular junction; IMP:FlyBase. DR CDD; cd23813; UBCc_UBE2N; 1. DR FunFam; 3.10.110.10:FF:000015; Ubiquitin-conjugating enzyme E2 N; 1. DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1. DR InterPro; IPR000608; UBC. DR InterPro; IPR023313; UBQ-conjugating_AS. DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD. DR PANTHER; PTHR24068; UBIQUITIN-CONJUGATING ENZYME E2; 1. DR Pfam; PF00179; UQ_con; 1. DR SMART; SM00212; UBCc; 1. DR SUPFAM; SSF54495; UBC-like; 1. DR PROSITE; PS00183; UBC_1; 1. DR PROSITE; PS50127; UBC_2; 1. PE 1: Evidence at protein level; KW Reference proteome; Transferase; Ubl conjugation pathway. FT CHAIN 1..151 FT /note="Ubiquitin-conjugating enzyme E2 N" FT /id="PRO_0000082521" FT DOMAIN 3..149 FT /note="UBC core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388" FT ACT_SITE 87 FT /note="Glycyl thioester intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388, FT ECO:0000255|PROSITE-ProRule:PRU10133" SQ SEQUENCE 151 AA; 17236 MW; 1D096E72A7AEA420 CRC64; MSSLPRRIIK ETQRLMQEPV PGINAIPDEN NARYFHVIVT GPNDSPFEGG VFKLELFLPE DYPMSAPKVR FITKIYHPNI DRLGRICLDV LKDKWSPALQ IRTILLSIQA LLSAPNPDDP LANDVAELWK VNEAEAIRNA REWTQKYAVE D //