Entry euk: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   10-MAY-2017, entry version 149.
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;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; 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;
RA   Oh C.E., McMahon R., Benzer S., Tanouye M.A.;
RT   "Bendless, a Drosophila gene affecting neuronal connectivity, encodes
RT   a 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
RT   in 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.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   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.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   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.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., 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.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic 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.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., 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: S-ubiquitinyl-[E1 ubiquitin-activating
CC       enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
CC       = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2
CC       ubiquitin-conjugating enzyme]-L-cysteine. {ECO:0000255|PROSITE-
CC       ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- DISRUPTION PHENOTYPE: Mutants in this gene exhibit several,
CC       largely neuronal defects including lesions affecting the neuronal
CC       connectivity of the giant fiber with the "jumping muscle", and the
CC       axons of photoreceptor cells R7 and R8 fail to make the proper
CC       right-angle turn 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}.
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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   UniGene; Dm.2088; -.
DR   ProteinModelPortal; P35128; -.
DR   SMR; P35128; -.
DR   BioGrid; 58728; 4.
DR   DIP; DIP-22866N; -.
DR   MINT; MINT-1003000; -.
DR   STRING; 7227.FBpp0073686; -.
DR   PaxDb; P35128; -.
DR   PRIDE; P35128; -.
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   eggNOG; KOG0417; Eukaryota.
DR   eggNOG; COG5078; LUCA.
DR   GeneTree; ENSGT00540000070023; -.
DR   InParanoid; P35128; -.
DR   KO; K10580; -.
DR   OMA; YFDVEIH; -.
DR   OrthoDB; EOG091G0VPD; -.
DR   PhylomeDB; P35128; -.
DR   Reactome; R-DME-446652; Interleukin-1 signaling.
DR   Reactome; R-DME-5696395; Formation of Incision Complex in GG-NER.
DR   Reactome; R-DME-937039; IRAK1 recruits IKK complex.
DR   Reactome; R-DME-975110; TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
DR   Reactome; R-DME-975144; IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
DR   SignaLink; P35128; -.
DR   UniPathway; UPA00143; -.
DR   GenomeRNAi; 32358; -.
DR   PRO; PR:P35128; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0000173; -.
DR   ExpressionAtlas; P35128; differential.
DR   Genevisible; P35128; DM.
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:0031624; F:ubiquitin conjugating enzyme binding; IPI:FlyBase.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:FlyBase.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS: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:1902916; P:positive regulation of protein polyubiquitination; IMP: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 growth 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; UBIQUITIN_CONJUGAT_1; 1.
DR   PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Complete proteome; Nucleotide-binding;
KW   Reference proteome; Transferase; Ubl conjugation pathway.
FT   CHAIN         1    151       Ubiquitin-conjugating enzyme E2 N.
FT                                /FTId=PRO_0000082521.
FT   ACT_SITE     87     87       Glycyl thioester intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00388,
FT                                ECO:0000255|PROSITE-ProRule:PRU10133}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT         7    143       ipfam:UQ_con [T]
FT   MYHIT        76     91       ipat:UBIQUITIN_CONJUGAT_1 [T]
FT   MYHIT         6    138       iprf:UBIQUITIN_CONJUGAT_2 [T]
SQ   SEQUENCE   151 AA;  17236 MW;  1D096E72A7AEA420 CRC64;
     MSSLPRRIIK ETQRLMQEPV PGINAIPDEN NARYFHVIVT GPNDSPFEGG VFKLELFLPE
     DYPMSAPKVR FITKIYHPNI DRLGRICLDV LKDKWSPALQ IRTILLSIQA LLSAPNPDDP
     LANDVAELWK VNEAEAIRNA REWTQKYAVE D
//