UBE2N_DROME
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 03-AUG-2022, entry version 179.
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; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; 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; 12.
DR DIP; DIP-22866N; -.
DR IntAct; P35128; 6.
DR STRING; 7227.FBpp0073686; -.
DR PaxDb; P35128; -.
DR PRIDE; 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 CTD; 32358; -.
DR FlyBase; FBgn0000173; ben.
DR VEuPathDB; VectorBase:FBgn0000173; -.
DR eggNOG; KOG0417; Eukaryota.
DR GeneTree; ENSGT00540000070023; -.
DR HOGENOM; CLU_030988_13_2_1; -.
DR InParanoid; P35128; -.
DR OMA; PDDYPME; -.
DR OrthoDB; 1345547at2759; -.
DR PhylomeDB; P35128; -.
DR Reactome; R-DME-209447; Activation of the IkappaB kinase complex, KEY:IRD5 dimer:KEY.
DR Reactome; R-DME-9020702; Interleukin-1 signaling.
DR Reactome; R-DME-9646399; Aggrephagy.
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 ChiTaRS; ben; fly.
DR GenomeRNAi; 32358; -.
DR PRO; PR:P35128; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0000173; Expressed in wing disc and 49 other tissues.
DR ExpressionAtlas; P35128; baseline and differential.
DR Genevisible; P35128; DM.
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:0035370; C:UBC13-UEV1A complex; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0010942; P:positive regulation of cell death; IGI: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:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; IGI:FlyBase.
DR GO; GO:0006301; P:postreplication repair; IBA:GO_Central.
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; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Nucleotide-binding; Reference proteome; Transferase;
KW 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
