ID   UBCD2_DROME             Reviewed;         232 AA.
AC   P52485; Q9VKQ4;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 167.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2-24 kDa;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme 2;
DE   AltName: Full=Ubiquitin carrier protein;
DE   AltName: Full=Ubiquitin-protein ligase;
GN   Name=Ubc2 {ECO:0000312|FlyBase:FBgn0015320}; Synonyms=UbcD2;
GN   ORFNames=CG6720 {ECO:0000312|FlyBase:FBgn0015320};
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].
RC   STRAIN=DP CN BW;
RX   PubMed=8576256; DOI=10.1074/jbc.271.5.2789;
RA   Matuschewski K., Hauser H.P., Treier M., Jentsch S.;
RT   "Identification of a novel family of ubiquitin-conjugating enzymes with
RT   distinct amino-terminal extensions.";
RL   J. Biol. Chem. 271:2789-2794(1996).
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).
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   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; X92663; CAA63351.1; -; mRNA.
DR   EMBL; AE014134; AAF53008.1; -; Genomic_DNA.
DR   RefSeq; NP_001260362.1; NM_001273433.1.
DR   RefSeq; NP_001285814.1; NM_001298885.1.
DR   RefSeq; NP_477137.1; NM_057789.4.
DR   RefSeq; NP_723616.1; NM_164943.2.
DR   AlphaFoldDB; P52485; -.
DR   SMR; P52485; -.
DR   BioGRID; 60561; 17.
DR   DIP; DIP-17329N; -.
DR   IntAct; P52485; 15.
DR   STRING; 7227.FBpp0305676; -.
DR   SwissPalm; P52485; -.
DR   PaxDb; 7227-FBpp0305676; -.
DR   DNASU; 34487; -.
DR   EnsemblMetazoa; FBtr0080115; FBpp0079704; FBgn0015320.
DR   EnsemblMetazoa; FBtr0080116; FBpp0079705; FBgn0015320.
DR   EnsemblMetazoa; FBtr0333492; FBpp0305676; FBgn0015320.
DR   EnsemblMetazoa; FBtr0345437; FBpp0311562; FBgn0015320.
DR   GeneID; 34487; -.
DR   KEGG; dme:Dmel_CG6720; -.
DR   AGR; FB:FBgn0015320; -.
DR   CTD; 34487; -.
DR   FlyBase; FBgn0015320; Ubc2.
DR   VEuPathDB; VectorBase:FBgn0015320; -.
DR   eggNOG; KOG0417; Eukaryota.
DR   HOGENOM; CLU_030988_14_0_1; -.
DR   InParanoid; P52485; -.
DR   OMA; GDRAKHD; -.
DR   OrthoDB; 5478564at2759; -.
DR   PhylomeDB; P52485; -.
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   SignaLink; P52485; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 34487; 1 hit in 3 CRISPR screens.
DR   ChiTaRS; Ubc2; fly.
DR   GenomeRNAi; 34487; -.
DR   PRO; PR:P52485; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0015320; Expressed in wing disc and 37 other cell types or tissues.
DR   ExpressionAtlas; P52485; baseline and differential.
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; IGI:FlyBase.
DR   GO; GO:0019915; P:lipid storage; IDA:FlyBase.
DR   GO; GO:0000209; P:protein polyubiquitination; ISS:FlyBase.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24068; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   PANTHER; PTHR24068:SF41; UBIQUITIN-CONJUGATING ENZYME E2-24 KDA; 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.
DR   Genevisible; P52485; DM.
PE   2: Evidence at transcript level;
KW   ATP-binding; Nucleotide-binding; Reference proteome; Transferase;
KW   Ubl conjugation pathway.
FT   CHAIN           1..232
FT                   /note="Ubiquitin-conjugating enzyme E2-24 kDa"
FT                   /id="PRO_0000082520"
FT   DOMAIN          86..232
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   REGION          1..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        170
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
SQ   SEQUENCE   232 AA;  24435 MW;  DE71AFD8EB618C86 CRC64;
     MSSTPAAGSA AEVATSSATS NAPSAPSTTA SNVSNTSQPT TAGTPQARGG RGSNANGGAS
     GSNAGGGDEP RKEAKTTPRI SRALGTSAKR IQKELAEITL DPPPNCSAGP KGDNLYEWVS
     TILGPPGSVY EGGVFFLDIH FSPEYPFKPP KVTFRTRIYH CNINSQGVIC LDILKDNWSP
     ALTISKVLLS ICSLLTDCNP ADPLVGSIAT QYLQNREEHD RIARLWTKRY AT
//