ID RL40_TRYBB Reviewed; 128 AA. AC P21899; P15174; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 10-AUG-2010, sequence version 2. DT 27-MAR-2024, entry version 81. 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; OS Trypanosoma brucei brucei. OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina; OC Trypanosomatida; Trypanosomatidae; Trypanosoma. OX NCBI_TaxID=5702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=427; RX PubMed=2175891; DOI=10.1093/nar/18.23.7181; RA Wong S., Morales T.H., Campbell D.A.; RT "Ubiquitin-EP52 fusion protein homologs from Trypanosoma brucei."; RL Nucleic Acids Res. 18:7181-7181(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=427; RX PubMed=8380221; DOI=10.1128/mcb.13.1.207-216.1993; RA Wong S., Morales T.H., Neigel J.E., Campbell D.A.; RT "Genomic and transcriptional linkage of the genes for calmodulin, EF-hand 5 RT protein, and ubiquitin extension protein 52 in Trypanosoma brucei."; RL Mol. Cell. Biol. 13:207-216(1993). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77. RX PubMed=2559328; DOI=10.1016/0166-6851(89)90111-4; RA Wong S., Campbell D.A.; RT "A polyubiquitin gene from Trypanosoma brucei."; RL Mol. Biochem. Parasitol. 37:147-150(1989). 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; X54641; CAA38453.1; -; mRNA. DR EMBL; X54642; CAA38454.1; -; mRNA. DR EMBL; X56511; CAA39863.1; -; Genomic_DNA. DR EMBL; X56511; CAA39864.1; -; Genomic_DNA. DR EMBL; X14554; CAA32691.1; -; Genomic_DNA. DR PIR; A44981; UQUT. DR PIR; C48111; C48111. DR PDB; 4V8M; EM; 5.57 A; Bs=1-128. DR PDB; 8OVA; EM; 2.47 A; Bs=1-128. DR PDB; 8OVE; EM; 2.60 A; Bs=1-128. DR PDBsum; 4V8M; -. DR PDBsum; 8OVA; -. DR PDBsum; 8OVE; -. DR AlphaFoldDB; P21899; -. DR EMDB; EMD-17208; -. DR EMDB; EMD-17212; -. DR SMR; P21899; -. DR IntAct; P21899; 1. DR SwissPalm; P21899; -. 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; 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; 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 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Isopeptide bond; Nucleus; Ribonucleoprotein; KW Ribosomal protein; Ubl conjugation. FT CHAIN 1..76 FT /note="Ubiquitin" FT /id="PRO_0000114828" FT CHAIN 77..128 FT /note="Large ribosomal subunit protein eL40" FT /id="PRO_0000138770" 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" FT CONFLICT 77 FT /note="V -> L (in Ref. 3; CAA32691)" FT /evidence="ECO:0000305" SQ SEQUENCE 128 AA; 14656 MW; 3F617F6F62B156B6 CRC64; MQIFVKTLTG KTIALEVEAS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EEGRTLADYN IQKESTLHLV LRLRGGVMEP TLEALAKKYN WEKKVCRRCY ARLPVRATNC RKKGCGHCSN LRMKKKLR //