UBE2S_DROME
ID UBE2S_DROME Reviewed; 209 AA.
AC Q9VX25;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 S;
DE EC=2.3.2.23 {ECO:0000269|PubMed:19822757};
DE AltName: Full=E2 ubiquitin-conjugating enzyme S;
DE AltName: Full=Ubiquitin carrier protein S;
DE AltName: Full=Ubiquitin-protein ligase S;
GN ORFNames=CG8188;
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].
RA Murphy T.D.;
RT "Full length sequences of assorted Drosophila melanogaster cDNAs.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=19822757; DOI=10.1073/pnas.0907887106;
RA Williamson A., Wickliffe K.E., Mellone B.G., Song L., Karpen G.H., Rape M.;
RT "Identification of a physiological E2 module for the human anaphase-
RT promoting complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:18213-18218(2009).
CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC proteins. Acts as an essential factor of the anaphase promoting
CC complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that
CC controls progression through mitosis. Acts by specifically elongating
CC polyubiquitin chains initiated by the E2 enzyme vih/UbcH10 on APC/C
CC substrates, enhancing the degradation of APC/C substrates by the
CC proteasome and promoting mitotic exit. {ECO:0000255|PROSITE-
CC ProRule:PRU00388, ECO:0000269|PubMed:19822757}.
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, ECO:0000269|PubMed:19822757};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:19822757}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; DQ151896; AAZ57341.1; -; mRNA.
DR EMBL; DQ151897; AAZ57342.1; -; mRNA.
DR EMBL; AE014298; ABC67190.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF48756.2; -; Genomic_DNA.
DR EMBL; BT031269; ABY20510.1; -; mRNA.
DR RefSeq; NP_001033852.1; NM_001038763.2.
DR RefSeq; NP_001285383.1; NM_001298454.1.
DR RefSeq; NP_001285384.1; NM_001298455.1.
DR RefSeq; NP_573237.2; NM_133009.3.
DR AlphaFoldDB; Q9VX25; -.
DR SMR; Q9VX25; -.
DR BioGRID; 59074; 9.
DR IntAct; Q9VX25; 5.
DR STRING; 7227.FBpp0099891; -.
DR PaxDb; Q9VX25; -.
DR PRIDE; Q9VX25; -.
DR DNASU; 32751; -.
DR EnsemblMetazoa; FBtr0074476; FBpp0074250; FBgn0030863.
DR EnsemblMetazoa; FBtr0100463; FBpp0099891; FBgn0030863.
DR EnsemblMetazoa; FBtr0340633; FBpp0309497; FBgn0030863.
DR EnsemblMetazoa; FBtr0346186; FBpp0312005; FBgn0030863.
DR GeneID; 32751; -.
DR KEGG; dme:Dmel_CG8188; -.
DR UCSC; CG8188-RA; d. melanogaster.
DR FlyBase; FBgn0030863; CG8188.
DR VEuPathDB; VectorBase:FBgn0030863; -.
DR eggNOG; KOG0423; Eukaryota.
DR HOGENOM; CLU_030988_5_3_1; -.
DR InParanoid; Q9VX25; -.
DR OMA; QPAKCGA; -.
DR OrthoDB; 1412570at2759; -.
DR PhylomeDB; Q9VX25; -.
DR Reactome; R-DME-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR Reactome; R-DME-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR Reactome; R-DME-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-DME-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-DME-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-DME-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-DME-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR Reactome; R-DME-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-DME-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR Reactome; R-DME-176412; Phosphorylation of the APC/C.
DR Reactome; R-DME-179409; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; R-DME-2467813; Separation of Sister Chromatids.
DR Reactome; R-DME-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-DME-68867; Assembly of the pre-replicative complex.
DR Reactome; R-DME-69017; CDK-mediated phosphorylation and removal of Cdc6.
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 UniPathway; UPA00143; -.
DR BioGRID-ORCS; 32751; 0 hits in 1 CRISPR screen.
DR ChiTaRS; CG8188; fly.
DR GenomeRNAi; 32751; -.
DR PRO; PR:Q9VX25; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030863; Expressed in brain and 32 other tissues.
DR ExpressionAtlas; Q9VX25; baseline and differential.
DR Genevisible; Q9VX25; DM.
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:0004842; F:ubiquitin-protein transferase activity; ISS:FlyBase.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IMP:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0010458; P:exit from mitosis; IMP:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; ISS: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; Cell cycle; Cell division; Nucleotide-binding;
KW Reference proteome; Transferase; Ubl conjugation pathway.
FT CHAIN 1..209
FT /note="Ubiquitin-conjugating enzyme E2 S"
FT /id="PRO_0000390440"
FT DOMAIN 14..160
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 168..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 98
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
SQ SEQUENCE 209 AA; 23337 MW; 65A528912E50A477 CRC64;
MSSQYSNVEN LSPQTIRQVM RELQEMETTP PEGIKVLINE SDVTDIQALI DGPAGTPYAA
GIFRVKLTLN KDFPLTPPKA YFLTKIFHPN VAANGEICVN TLKKDWKPDL GIKHILLTIK
CLLIVPNPES ALNEEAGKML LERYDDYSQR ARMMTEIHAQ PAKCGVGAVG DAKDDGGPST
KKHAGLDKKL QDKKKEKLLK EKKRMLKRL
