UBC10_DROME
ID UBC10_DROME Reviewed; 154 AA.
AC Q7K738;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Ubiquitin-conjugating enzyme E2-18 kDa {ECO:0000305|PubMed:10880484};
DE EC=2.3.2.23 {ECO:0000255|PROSITE-ProRule:PRU00388};
DE AltName: Full=Ubiquitin conjugating enzyme 10 {ECO:0000312|FlyBase:FBgn0026316};
GN Name=Ubc10 {ECO:0000312|FlyBase:FBgn0026316};
GN Synonyms=ubcD10 {ECO:0000303|PubMed:10880484};
GN ORFNames=CG5788 {ECO:0000312|FlyBase:FBgn0026316};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|EMBL:CAB40790.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH ARI-1.
RX PubMed=10880484; DOI=10.1093/genetics/155.3.1231;
RA Aguilera M., Oliveros M., Martinez-Padron M., Barbas J.A., Ferrus A.;
RT "Ariadne-1: a vital Drosophila gene is required in development and defines
RT a new conserved family of ring-finger proteins.";
RL Genetics 155:1231-1244(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [3] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [4] {ECO:0000312|EMBL:AAS93730.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAS93730.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAS93730.1};
RA Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
RA Park S., Wan K., Yu C., Rubin G.M., Celniker S.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000312|EMBL:ANY27213.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Wan K., Booth B., Spirohn K., Hao T., Hu Y., Calderwood M., Hill D.,
RA Mohr S., Vidal M., Celniker S., Perrimon N.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=21900267; DOI=10.1534/genetics.111.132191;
RA Gradilla A.C., Mansilla A., Ferrus A.;
RT "Isoform-specific regulation of a steroid hormone nuclear receptor by an E3
RT ubiquitin ligase in Drosophila melanogaster.";
RL Genetics 189:871-883(2011).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=27702987; DOI=10.15252/embr.201642378;
RA Asaoka T., Almagro J., Ehrhardt C., Tsai I., Schleiffer A., Deszcz L.,
RA Junttila S., Ringrose L., Mechtler K., Kavirayani A., Gyenesei A.,
RA Hofmann K., Duchek P., Rittinger K., Ikeda F.;
RT "Linear ubiquitination by LUBEL has a role in Drosophila heat stress
RT response.";
RL EMBO Rep. 17:1624-1640(2016).
RN [8] {ECO:0000305}
RP FUNCTION, INTERACTION WITH ARI-1, AND DISRUPTION PHENOTYPE.
RX PubMed=29689197; DOI=10.1016/j.devcel.2018.03.020;
RG University of Washington Center for Mendelian Genomics;
RA Tan K.L., Haelterman N.A., Kwartler C.S., Regalado E.S., Lee P.T.,
RA Nagarkar-Jaiswal S., Guo D.C., Duraine L., Wangler M.F., Bamshad M.J.,
RA Nickerson D.A., Lin G., Milewicz D.M., Bellen H.J.;
RT "Ari-1 Regulates Myonuclear Organization Together with Parkin and Is
RT Associated with Aortic Aneurysms.";
RL Dev. Cell 45:226-244(2018).
CC -!- FUNCTION: Ubiquitin-conjugating enzyme E2 that acts with the RBR family
CC ligases LUBEL, ari-1 and possibly parkin (PubMed:27702987,
CC PubMed:29689197, PubMed:21900267). Accepts ubiquitin from the E1
CC complex and catalyzes its covalent attachment to other proteins (By
CC similarity). Appears to be involved in the selective degradation of
CC short-lived and abnormal proteins (PubMed:29689197, PubMed:27702987,
CC PubMed:21900267). Functions with ari-1 to control the subcellular
CC localization and morphology of muscle nuclei (myonuclei) by regulating
CC the protein levels and distribution of the LINC (LInker of
CC Nucleoskeleton and Cytoskeleton) complex (PubMed:29689197). Functions
CC by mediating the monoubiquitination of the LINC complex subunit koi
CC leading to its subsequent proteasomal degradation (PubMed:29689197).
CC Likely to function with ari-1 to control metamorphosis by regulating
CC the proteins levels of EcR isoform A (ECR-A) and it's heterodimeric
CC partner usp, via the ubiquitination and subsequent degradation of ECR-A
CC (PubMed:21900267). Able to function with LUBEL to mediate 'Lys-63'- and
CC linear 'Met-1'-linked polyubiquitin involved in the heat stress
CC response (PubMed:27702987). {ECO:0000255|PROSITE-ProRule:PRU00388,
CC ECO:0000269|PubMed:21900267, ECO:0000269|PubMed:27702987,
CC ECO:0000269|PubMed:29689197}.
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:0000305|PubMed:21900267, ECO:0000305|PubMed:27702987};
CC -!- SUBUNIT: Interacts with the E3 ubiquitin ligase ari-1 (via RING-type 1
CC zinc finger). {ECO:0000269|PubMed:10880484,
CC ECO:0000269|PubMed:29689197}.
CC -!- DOMAIN: In contrast to other ubiquitin-conjugating enzymes E2, residues
CC essential for lysine reactivity are absent: Pro and a His residues are
CC present instead of an Asp and an Asp residues in positions 88 and 119,
CC respectively. {ECO:0000250|UniProtKB:P68036}.
CC -!- DISRUPTION PHENOTYPE: Nuclei in larval muscles (myonuclear), are
CC mislocalized and often clustered, likely due to mislocalization of the
CC LINC complex, demonstrated by the aberrant localization of the complex
CC member Msp300. {ECO:0000269|PubMed:29689197}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000305}.
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DR EMBL; AJ238007; CAB40790.1; -; mRNA.
DR EMBL; AE013599; AAF57787.1; -; Genomic_DNA.
DR EMBL; AL035311; CAA22948.1; -; Genomic_DNA.
DR EMBL; BT012459; AAS93730.1; -; mRNA.
DR EMBL; KX531403; ANY27213.1; -; mRNA.
DR PIR; T13578; T13578.
DR RefSeq; NP_477414.1; NM_058066.4.
DR AlphaFoldDB; Q7K738; -.
DR SMR; Q7K738; -.
DR IntAct; Q7K738; 2.
DR STRING; 7227.FBpp0088522; -.
DR PaxDb; Q7K738; -.
DR PRIDE; Q7K738; -.
DR DNASU; 37035; -.
DR EnsemblMetazoa; FBtr0089553; FBpp0088522; FBgn0026316.
DR GeneID; 37035; -.
DR KEGG; dme:Dmel_CG5788; -.
DR CTD; 37035; -.
DR FlyBase; FBgn0026316; Ubc10.
DR VEuPathDB; VectorBase:FBgn0026316; -.
DR eggNOG; KOG0422; Eukaryota.
DR GeneTree; ENSGT00940000165322; -.
DR HOGENOM; CLU_030988_13_3_1; -.
DR InParanoid; Q7K738; -.
DR OMA; HPNITND; -.
DR OrthoDB; 1420213at2759; -.
DR PhylomeDB; Q7K738; -.
DR Reactome; R-DME-1169408; ISG15 antiviral mechanism.
DR Reactome; R-DME-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 37035; 0 hits in 1 CRISPR screen.
DR ChiTaRS; CG8188; fly.
DR GenomeRNAi; 37035; -.
DR PRO; PR:Q7K738; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0026316; Expressed in thoracico-abdominal ganglion (Drosophila) and 26 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:FlyBase.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:FlyBase.
DR GO; GO:0097039; P:protein linear polyubiquitination; IDA:FlyBase.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IDA:FlyBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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; Ligase; Nucleotide-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..154
FT /note="Ubiquitin-conjugating enzyme E2-18 kDa"
FT /id="PRO_0000448741"
FT DOMAIN 2..149
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 86
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
SQ SEQUENCE 154 AA; 17907 MW; 3C71B5ADD007C4FB CRC64;
MTAPRRLRKE LSDLQGNALK SFRDIKADDD NLLRWTGLIV PDNPPYNKGA FRIEINFPAE
YPFKPPKINF KTRIYHPNID EKGQVCLPII STENWKPATR TDQVVQALVD LINDPEPEHP
LRAELAEEFL KDRKKFVKNA EDYTKKHSEK RPAD
