UBE2C_DROME
ID UBE2C_DROME Reviewed; 178 AA.
AC Q9VTY6;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 C;
DE EC=2.3.2.23;
DE AltName: Full=(E3-independent) E2 ubiquitin-conjugating enzyme C;
DE EC=2.3.2.24;
DE AltName: Full=E2 ubiquitin-conjugating enzyme C;
DE AltName: Full=Ubiquitin carrier protein C;
DE AltName: Full=Ubiquitin carrier protein vihar;
DE AltName: Full=Ubiquitin-protein ligase C;
GN Name=vih; Synonyms=Ubch10; ORFNames=CG10682;
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], FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=15458643; DOI=10.1016/j.cub.2004.09.023;
RA Mathe E., Kraft C., Giet R., Deak P., Peters J.-M., Glover D.M.;
RT "The E2-C vihar is required for the correct spatiotemporal proteolysis of
RT cyclin B and itself undergoes cyclical degradation.";
RL Curr. Biol. 14:1723-1733(2004).
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;
RA Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
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 initiating polyubiquitin
CC chains on APC/C substrates, leading to the degradation of APC/C
CC substrates by the proteasome and promoting mitotic exit.
CC {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:15458643,
CC 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:0000250|UniProtKB:O00762, ECO:0000255|PROSITE-
CC ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-
CC cysteine + N(6)-monoubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.24; Evidence={ECO:0000250|UniProtKB:O00762};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: Component of the APC/C complex.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15458643}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:15458643}. Note=Localizes in the cytoplasm of
CC mitotic cells but also associates with centrosomes, and its own
CC degradation is initiated at the metaphase-anaphase transition.
CC -!- PTM: Ubiquitinated by the APC/C complex, leading to its degradation at
CC the metaphase-anaphase transition. {ECO:0000269|PubMed:15458643}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality. Both homozygous and
CC hemizygous females show maternal effect lethality and produce syncytial
CC embryos that fail to develop as a result of mitotic defects.
CC {ECO:0000269|PubMed:15458643}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; AF410850; AAL02117.1; -; mRNA.
DR EMBL; AE014296; AAF49909.1; -; Genomic_DNA.
DR EMBL; BT028772; ABI34153.1; -; mRNA.
DR RefSeq; NP_648582.1; NM_140325.3.
DR AlphaFoldDB; Q9VTY6; -.
DR SMR; Q9VTY6; -.
DR BioGRID; 68841; 9.
DR IntAct; Q9VTY6; 1.
DR STRING; 7227.FBpp0075690; -.
DR SwissPalm; Q9VTY6; -.
DR PaxDb; Q9VTY6; -.
DR PRIDE; Q9VTY6; -.
DR DNASU; 44118; -.
DR EnsemblMetazoa; FBtr0075958; FBpp0075690; FBgn0264848.
DR GeneID; 44118; -.
DR KEGG; dme:Dmel_CG10682; -.
DR UCSC; CG10682-RA; d. melanogaster.
DR CTD; 44118; -.
DR FlyBase; FBgn0264848; vih.
DR VEuPathDB; VectorBase:FBgn0264848; -.
DR eggNOG; KOG0421; Eukaryota.
DR GeneTree; ENSGT00930000150941; -.
DR HOGENOM; CLU_030988_9_3_1; -.
DR InParanoid; Q9VTY6; -.
DR OMA; HPNVDMS; -.
DR OrthoDB; 1444506at2759; -.
DR PhylomeDB; Q9VTY6; -.
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; 44118; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 44118; -.
DR PRO; PR:Q9VTY6; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0264848; Expressed in secondary oocyte and 22 other tissues.
DR Genevisible; Q9VTY6; DM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0000151; C:ubiquitin ligase 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:0031145; P:anaphase-promoting complex-dependent catabolic process; IDA:FlyBase.
DR GO; GO:0010458; P:exit from mitosis; IMP:UniProtKB.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IMP:FlyBase.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:FlyBase.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; 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; Cytoplasm; Cytoskeleton; Nucleotide-binding;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..178
FT /note="Ubiquitin-conjugating enzyme E2 C"
FT /id="PRO_0000390471"
FT DOMAIN 32..177
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 116
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
SQ SEQUENCE 178 AA; 19832 MW; 7EF04EE68FEDC7AB CRC64;
MAQNISPEQS GGAGGGGSKH SDDSMPVKDN HAVSKRLHKE LMNLMMANER GISAFPDGEN
IFKWVGTIAG PRNTVYSGQT YRLSLDFPNS YPYAAPVVKF LTSCFHPNVD LQGAICLDIL
KDKWSALYDV RTILLSIQSL LGEPNNESPL NAQAAMMWND QKEYKKYLDA FYEKHKDT
