UBIQP_DROME
ID UBIQP_DROME Reviewed; 763 AA.
AC P0CG69; P68198; Q0E8I1; Q9VKW6; Q9VQX7; Q9VZL4;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Polyubiquitin;
DE Contains:
DE RecName: Full=Ubiquitin;
DE Flags: Precursor;
GN Name=Ubi-p63E; Synonyms=Ubi-m; ORFNames=CG11624;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-76.
RA Arribas C., Sampedro J., Izquierdo M.;
RT "The ubiquitin genes in D. melanogaster: transcription and polymorphism.";
RL Biochim. Biophys. Acta 868:119-127(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 533-763.
RX PubMed=2463465; DOI=10.1128/mcb.8.11.4727-4735.1988;
RA Lee H., Simon J.A., Lis J.T.;
RT "Structure and expression of ubiquitin genes of Drosophila melanogaster.";
RL Mol. Cell. Biol. 8:4727-4735(1988).
RN [4]
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: Ubiquitin exists either covalently attached to another
CC protein, or free (unanchored). When covalently bound, it is conjugated
CC to target proteins via an isopeptide bond either as a monomer
CC (monoubiquitin), a polymer linked via different Lys residues of the
CC ubiquitin (polyubiquitin chains) or a linear polymer linked via the
CC initiator Met of the ubiquitin (linear polyubiquitin chains).
CC Polyubiquitin chains, when attached to a target protein, have different
CC functions depending on the Lys residue of the ubiquitin that is linked:
CC Lys-48-linked is involved in protein degradation via the proteasome.
CC Linear polymer chains formed via attachment by the initiator Met lead
CC to cell signaling. Ubiquitin is usually conjugated to Lys residues of
CC target proteins, however, in rare cases, conjugation to Cys or Ser
CC residues has been observed. When polyubiquitin is free (unanchored-
CC polyubiquitin), it also has distinct roles, such as in activation of
CC protein kinases, and in signaling (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: In Drosophila ubiquitin is encoded by 3 different genes.
CC RpL40 and RpS27A genes code for a single copy of ubiquitin fused to the
CC ribosomal proteins L40 and S27a, respectively. Ubi-p63E gene codes for
CC a polyubiquitin precursor with 10 exact head to tail repeats.
CC -!- MISCELLANEOUS: For the sake of clarity sequence features are annotated
CC only for the first chain, and are not repeated for each of the
CC following chains.
CC -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
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DR EMBL; AE014296; AAF47806.3; -; Genomic_DNA.
DR EMBL; M33013; AAA28999.1; -; Genomic_DNA.
DR EMBL; M33015; AAA29001.1; -; Genomic_DNA.
DR EMBL; M33122; AAA29007.1; -; Genomic_DNA.
DR EMBL; M22428; AAA28997.1; -; Genomic_DNA.
DR PIR; A26087; A26087.
DR RefSeq; NP_001261383.1; NM_001274454.1.
DR RefSeq; NP_523909.2; NM_079185.4.
DR RefSeq; NP_728908.1; NM_168043.3.
DR RefSeq; NP_995994.1; NM_206272.1.
DR AlphaFoldDB; P0CG69; -.
DR BMRB; P0CG69; -.
DR SMR; P0CG69; -.
DR BioGRID; 63944; 39.
DR STRING; 7227.FBpp0073035; -.
DR PaxDb; P0CG69; -.
DR PRIDE; P0CG69; -.
DR EnsemblMetazoa; FBtr0073177; FBpp0073034; FBgn0003943.
DR EnsemblMetazoa; FBtr0073178; FBpp0073035; FBgn0003943.
DR EnsemblMetazoa; FBtr0073179; FBpp0089269; FBgn0003943.
DR EnsemblMetazoa; FBtr0333142; FBpp0305348; FBgn0003943.
DR GeneID; 38456; -.
DR KEGG; dme:Dmel_CG11624; -.
DR CTD; 38456; -.
DR FlyBase; FBgn0003943; Ubi-p63E.
DR VEuPathDB; VectorBase:FBgn0003943; -.
DR eggNOG; KOG0001; Eukaryota.
DR GeneTree; ENSGT00940000163900; -.
DR HOGENOM; CLU_010412_1_0_1; -.
DR InParanoid; P0CG69; -.
DR OMA; HLTMQIF; -.
DR OrthoDB; 1536766at2759; -.
DR PhylomeDB; P0CG69; -.
DR Reactome; R-DME-209360; Ubiquitination and proteolysis of phosphorylated CI.
DR Reactome; R-DME-209447; Activation of the IkappaB kinase complex, KEY:IRD5 dimer:KEY.
DR Reactome; R-DME-209461; Ubiquitination and degradation of phosphorylated ARM.
DR Reactome; R-DME-216167; Nuclear CI is degraded.
DR Reactome; R-DME-432395; Degradation of TIM.
DR Reactome; R-DME-432524; Degradation of PER.
DR Reactome; R-DME-538864; Degradation of CRY.
DR BioGRID-ORCS; 38456; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 38456; -.
DR PRO; PR:P0CG69; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0003943; Expressed in adult Malpighian tubule (Drosophila) and 25 other tissues.
DR ExpressionAtlas; P0CG69; baseline and differential.
DR Genevisible; P0CG69; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031386; F:protein tag; ISS:FlyBase.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IMP:FlyBase.
DR GO; GO:0035096; P:larval midgut cell programmed cell death; IMP:FlyBase.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; ISS:FlyBase.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR019956; Ubiquitin_dom.
DR Pfam; PF00240; ubiquitin; 10.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 10.
DR SUPFAM; SSF54236; SSF54236; 10.
DR PROSITE; PS00299; UBIQUITIN_1; 10.
DR PROSITE; PS50053; UBIQUITIN_2; 10.
PE 3: Inferred from homology;
KW Cytoplasm; Isopeptide bond; Nucleus; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..76
FT /note="Ubiquitin"
FT /id="PRO_0000114813"
FT CHAIN 77..152
FT /note="Ubiquitin"
FT /id="PRO_0000396260"
FT CHAIN 153..228
FT /note="Ubiquitin"
FT /id="PRO_0000396261"
FT CHAIN 229..304
FT /note="Ubiquitin"
FT /id="PRO_0000396262"
FT CHAIN 305..380
FT /note="Ubiquitin"
FT /id="PRO_0000396263"
FT CHAIN 381..456
FT /note="Ubiquitin"
FT /id="PRO_0000396264"
FT CHAIN 457..532
FT /note="Ubiquitin"
FT /id="PRO_0000396265"
FT CHAIN 533..608
FT /note="Ubiquitin"
FT /id="PRO_0000396266"
FT CHAIN 609..684
FT /note="Ubiquitin"
FT /id="PRO_0000396267"
FT CHAIN 685..760
FT /note="Ubiquitin"
FT /id="PRO_0000396268"
FT PROPEP 761..763
FT /id="PRO_0000396269"
FT DOMAIN 1..76
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 77..152
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 153..228
FT /note="Ubiquitin-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 229..304
FT /note="Ubiquitin-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 305..380
FT /note="Ubiquitin-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 381..456
FT /note="Ubiquitin-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 457..532
FT /note="Ubiquitin-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 533..608
FT /note="Ubiquitin-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 609..684
FT /note="Ubiquitin-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 685..760
FT /note="Ubiquitin-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT SITE 54
FT /note="Interacts with activating enzyme"
FT SITE 68
FT /note="Essential for function"
FT SITE 72
FT /note="Interacts with activating enzyme"
FT CROSSLNK 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
FT CROSSLNK 76
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
SQ SEQUENCE 763 AA; 85799 MW; 5693123AE7B186A7 CRC64;
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE NVKAKIQDKE GIPPDQQRLI
FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLEVE PSDTIENVKA
KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT
ITLEVEPSDT IENVKAKIQD KEGIPPDQQR LIFAGKQLED GRTLSDYNIQ KESTLHLVLR
LRGGMQIFVK TLTGKTITLE VEPSDTIENV KAKIQDKEGI PPDQQRLIFA GKQLEDGRTL
SDYNIQKEST LHLVLRLRGG MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ
QRLIFAGKQL EDGRTLSDYN IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE
NVKAKIQDKE GIPPDQQRLI FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL
TGKTITLEVE PSDTIENVKA KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH
LVLRLRGGMQ IFVKTLTGKT ITLEVEPSDT IENVKAKIQD KEGIPPDQQR LIFAGKQLED
GRTLSDYNIQ KESTLHLVLR LRGGMQIFVK TLTGKTITLE VEPSDTIENV KAKIQDKEGI
PPDQQRLIFA GKQLEDGRTL SDYNIQKEST LHLVLRLRGG IQA
