UBCD6_DROME
ID UBCD6_DROME Reviewed; 151 AA.
AC P25153; Q9VN70;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Ubiquitin-conjugating enzyme E2-17 kDa;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 6;
DE AltName: Full=Ubiquitin carrier protein;
DE AltName: Full=Ubiquitin-protein ligase;
GN Name=Ubc6 {ECO:0000312|FlyBase:FBgn0004436};
GN Synonyms=Dhr6, UbcD6 {ECO:0000312|FlyBase:FBgn0004436};
GN ORFNames=CG2013 {ECO:0000312|FlyBase:FBgn0004436};
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 [GENOMIC DNA / MRNA], AND FUNCTION.
RX PubMed=1902572; DOI=10.1073/pnas.88.9.3832;
RA Koken M.H.M., Reynolds P., Bootsma D., Hoeijmakers J.H.J., Prakash S.,
RA Prakash L.;
RT "Dhr6, a Drosophila homolog of the yeast DNA-repair gene RAD6.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:3832-3836(1991).
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=Head;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=27552662; DOI=10.1371/journal.pbio.1002539;
RA Ashton-Beaucage D., Lemieux C., Udell C.M., Sahmi M., Rochette S.,
RA Therrien M.;
RT "The Deubiquitinase USP47 Stabilizes MAPK by Counteracting the Function of
RT the N-end Rule ligase POE/UBR4 in Drosophila.";
RL PLoS Biol. 14:E1002539-E1002539(2016).
CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC proteins. Required for postreplication repair of UV-damaged DNA
CC (PubMed:1902572). Involved in the negative regulation of the Ras/MAPK
CC signaling pathway in the wing by acting with the putative E3 ligases
CC poe, Kcmf1 and Ufd4 to mediate the ubiquitination and proteasomal
CC degradation of rl/MAPK (PubMed:27552662). {ECO:0000269|PubMed:1902572,
CC ECO:0000269|PubMed:27552662}.
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 -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; M63792; AAA28308.1; -; mRNA.
DR EMBL; M64435; AAA28309.1; -; Genomic_DNA.
DR EMBL; M63791; AAA28309.1; JOINED; Genomic_DNA.
DR EMBL; AE014297; AAF52079.1; -; Genomic_DNA.
DR EMBL; BT003481; AAO39484.1; -; mRNA.
DR PIR; A39392; A39392.
DR RefSeq; NP_001246916.1; NM_001259987.3.
DR RefSeq; NP_524230.2; NM_079506.4.
DR AlphaFoldDB; P25153; -.
DR SMR; P25153; -.
DR BioGRID; 65824; 2.
DR STRING; 7227.FBpp0078490; -.
DR PaxDb; P25153; -.
DR DNASU; 40610; -.
DR EnsemblMetazoa; FBtr0078849; FBpp0078490; FBgn0004436.
DR EnsemblMetazoa; FBtr0306106; FBpp0297243; FBgn0004436.
DR GeneID; 40610; -.
DR KEGG; dme:Dmel_CG2013; -.
DR CTD; 40610; -.
DR FlyBase; FBgn0004436; Ubc6.
DR VEuPathDB; VectorBase:FBgn0004436; -.
DR eggNOG; KOG0419; Eukaryota.
DR GeneTree; ENSGT00940000156580; -.
DR HOGENOM; CLU_030988_10_2_1; -.
DR InParanoid; P25153; -.
DR OMA; DHKSQYI; -.
DR OrthoDB; 1292821at2759; -.
DR PhylomeDB; P25153; -.
DR Reactome; R-DME-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-DME-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 40610; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 40610; -.
DR PRO; PR:P25153; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0004436; Expressed in brain and 22 other tissues.
DR ExpressionAtlas; P25153; baseline and differential.
DR Genevisible; P25153; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0033503; C:HULC complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0002039; F:p53 binding; IPI:BHF-UCL.
DR GO; GO:0019904; F:protein domain specific binding; IPI:BHF-UCL.
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:0000422; P:autophagy of mitochondrion; IMP:FlyBase.
DR GO; GO:0007098; P:centrosome cycle; IMP:FlyBase.
DR GO; GO:0051299; P:centrosome separation; IMP:FlyBase.
DR GO; GO:0006281; P:DNA repair; IGI:FlyBase.
DR GO; GO:0032456; P:endocytic recycling; IMP:FlyBase.
DR GO; GO:0007507; P:heart development; IMP:FlyBase.
DR GO; GO:0016574; P:histone ubiquitination; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:FlyBase.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IMP:BHF-UCL.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IGI:FlyBase.
DR GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:BHF-UCL.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:BHF-UCL.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:BHF-UCL.
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 2: Evidence at transcript level;
KW ATP-binding; DNA damage; DNA repair; Nucleotide-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway.
FT CHAIN 1..151
FT /note="Ubiquitin-conjugating enzyme E2-17 kDa"
FT /id="PRO_0000082523"
FT DOMAIN 4..150
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 88
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT CONFLICT 99
FT /note="T -> R (in Ref. 1; AAA28308/AAA28309)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 151 AA; 17152 MW; CC4B35992E4A9220 CRC64;
MSTPARRRLM RDFKRLQEDP PTGVSGAPTD NNIMIWNAVI FGPHDTPFED GTFKLTIEFT
EEYPNKPPTV RFVSKVFHPN VYADGGICLD ILQNRWSPTY DVSAILTSIQ SLLSDPNPNS
PANSTAAQLY KENRREYEKR VKACVEQSFI D
