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Database: UniProt
Entry: Q7JYK1_DROME
LinkDB: Q7JYK1_DROME
Original site: Q7JYK1_DROME 
ID   Q7JYK1_DROME            Unreviewed;       128 AA.
AC   Q7JYK1;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 138.
DE   RecName: Full=Ubiquitin-ribosomal protein eL40 fusion protein {ECO:0000256|ARBA:ARBA00035298};
GN   Name=RpL40 {ECO:0000313|EMBL:AGB92554.1,
GN   ECO:0000313|FlyBase:FBgn0003941};
GN   Synonyms=BcDNA:RE10554 {ECO:0000313|EMBL:AGB92554.1}, CEP52
GN   {ECO:0000313|EMBL:AGB92554.1}, Dmel\CG2960
GN   {ECO:0000313|EMBL:AGB92554.1}, DUb52 {ECO:0000313|EMBL:AGB92554.1},
GN   Dub52 {ECO:0000313|EMBL:AGB92554.1}, L40
GN   {ECO:0000313|EMBL:AGB92554.1}, L40e {ECO:0000313|EMBL:AGB92554.1},
GN   RPL40 {ECO:0000313|EMBL:AGB92554.1}, Rpl40
GN   {ECO:0000313|EMBL:AGB92554.1}, Ub52 {ECO:0000313|EMBL:AGB92554.1},
GN   Ubi-f {ECO:0000313|EMBL:AGB92554.1}, Ubi-f52
GN   {ECO:0000313|EMBL:AGB92554.1}, Ubiq {ECO:0000313|EMBL:AGB92554.1};
GN   ORFNames=CG2960 {ECO:0000313|EMBL:AGB92554.1,
GN   ECO:0000313|FlyBase:FBgn0003941}, Dmel_CG2960
GN   {ECO:0000313|EMBL:AGB92554.1};
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 {ECO:0000313|EMBL:AAL68264.1};
RN   [1] {ECO:0000313|EMBL:AGB92554.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J., 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., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA   Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA   Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA   Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA   Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA   Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA   Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2] {ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537568;
RA   Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA   Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA   George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA   Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA   Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA   Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT   "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT   euchromatic genome sequence.";
RL   Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN   [3] {ECO:0000313|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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] {ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537573;
RA   Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA   Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA   Celniker S.E.;
RT   "The transposable elements of the Drosophila melanogaster euchromatin: a
RT   genomics perspective.";
RL   Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN   [5] {ECO:0000313|EMBL:AGB92554.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537574;
RA   Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA   Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA   Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA   Karpen G.H.;
RT   "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL   Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN   [6] {ECO:0000313|EMBL:AAL68264.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Berkeley {ECO:0000313|EMBL:AAL68264.1};
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA   Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA   Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA   Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|EMBL:AGB92554.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA   Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA   Ashburner M., Anxolabehere D.;
RT   "Combined evidence annotation of transposable elements in genome
RT   sequences.";
RL   PLoS Comput. Biol. 1:166-175(2005).
RN   [8] {ECO:0000313|EMBL:AGB92554.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S.,
RA   Svirskas R., Rubin G.;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [9] {ECO:0000313|EMBL:AGB92554.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569856; DOI=10.1126/science.1139815;
RA   Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT   "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL   Science 316:1586-1591(2007).
RN   [10] {ECO:0000313|EMBL:AGB92554.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569867; DOI=10.1126/science.1139816;
RA   Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA   Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA   Dimitri P., Karpen G.H., Celniker S.E.;
RT   "Sequence finishing and mapping of Drosophila melanogaster
RT   heterochromatin.";
RL   Science 316:1625-1628(2007).
RN   [11] {ECO:0000313|EMBL:AGB92554.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26109357; DOI=.1534/g3.115.018929;
RG   FlyBase Consortium;
RA   Matthews B.B., Dos Santos G., Crosby M.A., Emmert D.B., St Pierre S.E.,
RA   Gramates L.S., Zhou P., Schroeder A.J., Falls K., Strelets V., Russo S.M.,
RA   Gelbart W.M., null;
RT   "Gene Model Annotations for Drosophila melanogaster: Impact of High-
RT   Throughput Data.";
RL   G3 (Bethesda) 5:1721-1736(2015).
RN   [12] {ECO:0000313|EMBL:AGB92554.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26109356; DOI=.1534/g3.115.018937;
RG   FlyBase Consortium;
RA   Crosby M.A., Gramates L.S., Dos Santos G., Matthews B.B., St Pierre S.E.,
RA   Zhou P., Schroeder A.J., Falls K., Emmert D.B., Russo S.M., Gelbart W.M.,
RA   null;
RT   "Gene Model Annotations for Drosophila melanogaster: The Rule-Benders.";
RL   G3 (Bethesda) 5:1737-1749(2015).
RN   [13] {ECO:0000313|EMBL:AGB92554.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25589440;
RA   Hoskins R.A., Carlson J.W., Wan K.H., Park S., Mendez I., Galle S.E.,
RA   Booth B.W., Pfeiffer B.D., George R.A., Svirskas R., Krzywinski M.,
RA   Schein J., Accardo M.C., Damia E., Messina G., Mendez-Lago M.,
RA   de Pablos B., Demakova O.V., Andreyeva E.N., Boldyreva L.V., Marra M.,
RA   Carvalho A.B., Dimitri P., Villasante A., Zhimulev I.F., Rubin G.M.,
RA   Karpen G.H., Celniker S.E.;
RT   "The Release 6 reference sequence of the Drosophila melanogaster genome.";
RL   Genome Res. 25:445-458(2015).
RN   [14] {ECO:0000313|EMBL:AGB92554.1}
RP   NUCLEOTIDE SEQUENCE.
RG   Berkeley Drosophila Genome Project;
RA   Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R.,
RA   Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E., Yu C.,
RA   Rubin G.;
RT   "Drosophila melanogaster release 4 sequence.";
RL   Submitted (NOV-2022) to the EMBL/GenBank/DDBJ databases.
RN   [15] {ECO:0000313|EMBL:AGB92554.1}
RP   NUCLEOTIDE SEQUENCE.
RG   FlyBase;
RL   Submitted (NOV-2022) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Exists either covalently attached to another protein, or free
CC       (unanchored). When covalently bound, it is conjugated to target
CC       proteins via an isopeptide bond either as a monomer (monoubiquitin), a
CC       polymer linked via different Lys residues of the ubiquitin
CC       (polyubiquitin chains) or a linear polymer linked via the initiator Met
CC       of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains,
CC       when attached to a target protein, have different functions depending
CC       on the Lys residue of the ubiquitin that is linked: Lys-48-linked is
CC       involved in protein degradation via the proteasome. Linear polymer
CC       chains formed via attachment by the initiator Met lead to cell
CC       signaling. Ubiquitin is usually conjugated to Lys residues of target
CC       proteins, however, in rare cases, conjugation to Cys or Ser residues
CC       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. {ECO:0000256|ARBA:ARBA00029384}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the eukaryotic
CC       ribosomal protein eL40 family. {ECO:0000256|ARBA:ARBA00010570}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin family.
CC       {ECO:0000256|ARBA:ARBA00008373}.
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DR   EMBL; AY075451; AAL68264.1; -; mRNA.
DR   EMBL; AE014134; AGB92554.1; -; Genomic_DNA.
DR   RefSeq; NP_001260018.1; NM_001273089.2.
DR   RefSeq; NP_476776.1; NM_057428.4.
DR   AlphaFoldDB; Q7JYK1; -.
DR   SMR; Q7JYK1; -.
DR   DNASU; 33629; -.
DR   EnsemblMetazoa; FBtr0077470; FBpp0077159; FBgn0003941.
DR   EnsemblMetazoa; FBtr0334787; FBpp0306837; FBgn0003941.
DR   GeneID; 33629; -.
DR   KEGG; dme:Dmel_CG2960; -.
DR   AGR; FB:FBgn0003941; -.
DR   CTD; 33629; -.
DR   FlyBase; FBgn0003941; RpL40.
DR   VEuPathDB; VectorBase:FBgn0003941; -.
DR   GeneTree; ENSGT00940000153593; -.
DR   HOGENOM; CLU_010412_3_4_1; -.
DR   OMA; ARKYKCD; -.
DR   OrthoDB; 312211at2759; -.
DR   BioGRID-ORCS; 33629; 1 hit in 1 CRISPR screen.
DR   ChiTaRS; RpL40; fly.
DR   GenomeRNAi; 33629; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0003941; Expressed in mouthpart and 25 other cell types or tissues.
DR   ExpressionAtlas; Q7JYK1; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0015934; C:large ribosomal subunit; IEA:UniProt.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   CDD; cd01803; Ubl_ubiquitin; 1.
DR   Gene3D; 4.10.1060.50; -; 1.
DR   InterPro; IPR001975; Ribosomal_eL40_dom.
DR   InterPro; IPR038587; Ribosomal_eL40_sf.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019956; Ubiquitin_dom.
DR   PANTHER; PTHR10666:SF515; POLYUBIQUITIN-B; 1.
DR   PANTHER; PTHR10666; UBIQUITIN; 1.
DR   Pfam; PF01020; Ribosomal_L40e; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM01377; Ribosomal_L40e; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS00299; UBIQUITIN_1; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:Q7JYK1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW   ECO:0000313|EMBL:AGB92554.1}.
FT   DOMAIN          1..76
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
SQ   SEQUENCE   128 AA;  14729 MW;  7BDE802AA2D249D2 CRC64;
     MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
     IQKESTLHLV LRLRGGIIEP SLRILAQKYN CDKMICRKCY ARLHPRATNC RKKKCGHTNN
     LRPKKKLK
//
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