ID RL40_LEIMA Reviewed; 128 AA. AC P69201; Q05550; Q05551; Q4Q672; DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 10-AUG-2010, sequence version 2. DT 27-MAR-2024, entry version 79. DE RecName: Full=Ubiquitin-ribosomal protein eL40 fusion protein {ECO:0000305}; DE Contains: DE RecName: Full=Ubiquitin; DE Contains: DE RecName: Full=Large ribosomal subunit protein eL40 {ECO:0000305}; DE AltName: Full=60S ribosomal protein L40; DE AltName: Full=CEP52; DE Flags: Precursor; GN Name=UB-EP52; ORFNames=LmjF31.1900, LmjF_31_1900; GN and GN ORFNames=LmjF31.2030, LmjF_31_2030; OS Leishmania major. OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina; OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania. OX NCBI_TaxID=5664; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (UB-EP52). RC STRAIN=MHOM/IR/83/Lt252; RX PubMed=8396548; DOI=10.1016/0378-1119(93)90687-x; RA Graeff G.R., Steele P.M., Peterson C.L., Bennett M.L., Langer P.J.; RT "Sequence of a Leishmania major gene encoding an ubiquitin fusion RT protein."; RL Gene 131:155-156(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (UB-EP52 AND LMJF31.2030). RC STRAIN=MHOM/IL/81/Friedlin; RX PubMed=16020728; DOI=10.1126/science.1112680; RA Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G., RA Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A., RA Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M., RA Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E., RA Ciarloni L., Clayton C., Coulson R.M.R., Cronin A., Cruz A.K., Davies R.M., RA De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N., RA Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A., RA Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S., RA Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M., RA Masuy D., Matthews K., Michaeli S., Mottram J.C., Mueller-Auer S., RA Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M., RA Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E., RA Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C., RA Rutter S., Saunders D., Schaefer M., Schein J., Schwartz D.C., Seeger K., RA Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V., RA Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J., RA Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D., RA Barrell B.G., Myler P.J.; RT "The genome of the kinetoplastid parasite, Leishmania major."; RL Science 309:436-442(2005). 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 -!- FUNCTION: [Large ribosomal subunit protein eL40]: Component of the 60S CC subunit of the ribosome. {ECO:0000250}. CC -!- SUBUNIT: [Large ribosomal subunit protein eL40]: Part of the 60S CC ribosomal subunit. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: [Large ribosomal subunit protein eL40]: Cytoplasm CC {ECO:0000250}. CC -!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin family. CC {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the eukaryotic CC ribosomal protein eL40 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z14232; CAA78598.1; -; Genomic_DNA. DR EMBL; Z14232; CAA78599.1; -; Genomic_DNA. DR EMBL; FR796427; CAJ08378.1; -; Genomic_DNA. DR EMBL; FR796427; CAJ08391.1; -; Genomic_DNA. DR RefSeq; XP_001685176.1; XM_001685124.1. DR RefSeq; XP_001685189.1; XM_001685137.1. DR AlphaFoldDB; P69201; -. DR SMR; P69201; -. DR STRING; 5664.P69201; -. DR EnsemblProtists; CAJ08378; CAJ08378; LMJF_31_1900. DR EnsemblProtists; CAJ08391; CAJ08391; LMJF_31_2030. DR GeneID; 5654121; -. DR GeneID; 5654134; -. DR KEGG; lma:LMJF_31_1900; -. DR KEGG; lma:LMJF_31_2030; -. DR VEuPathDB; TriTrypDB:LmjF.31.1900; -. DR VEuPathDB; TriTrypDB:LMJFC_310033800; -. DR VEuPathDB; TriTrypDB:LMJLV39_000007200; -. DR VEuPathDB; TriTrypDB:LMJSD75_310027300; -. DR eggNOG; KOG0003; Eukaryota. DR InParanoid; P69201; -. DR OMA; ARKYKCD; -. DR Proteomes; UP000000542; Chromosome 31. 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:0031386; F:protein tag activity; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central. DR GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central. DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central. 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; IPR011332; Ribosomal_zn-bd. 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 SUPFAM; SSF57829; Zn-binding ribosomal proteins; 1. DR PROSITE; PS00299; UBIQUITIN_1; 1. DR PROSITE; PS50053; UBIQUITIN_2; 1. PE 3: Inferred from homology; KW Cytoplasm; Isopeptide bond; Nucleus; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; Ubl conjugation. FT CHAIN 1..76 FT /note="Ubiquitin" FT /id="PRO_0000114825" FT CHAIN 77..128 FT /note="Large ribosomal subunit protein eL40" FT /id="PRO_0000138765" FT DOMAIN 1..76 FT /note="Ubiquitin-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214" 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 128 AA; 14682 MW; 4B46DF6563C3E7FF CRC64; MQIFVKTLTG KTIALEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EEGRTLSDYN IQKESTLHLV LRLRGGVMEP TLVALAKKYN WEKKVCRRCY ARLPVRATNC RKKACGHCSN LRMKKKLR //