RL40_CAEEL
ID RL40_CAEEL Reviewed; 128 AA.
AC P49632; P14792; Q9U1P3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Ubiquitin-60S ribosomal protein L40;
DE AltName: Full=CEP52;
DE Contains:
DE RecName: Full=Ubiquitin;
DE Contains:
DE RecName: Full=60S ribosomal protein L40;
DE Flags: Precursor;
GN Name=ubq-2; Synonyms=ubib; ORFNames=ZK1010.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7556908; DOI=10.1006/dbio.1995.1260;
RA Jones D., Stringham E.G., Graham R.W., Candido E.P.M.;
RT "A portable regulatory element directs specific expression of the
RT Caenorhabditis elegans ubiquitin gene ubq-2 in the somatic gonad.";
RL Dev. Biol. 171:60-72(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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: [60S ribosomal protein L40]: Component of the 60S subunit of
CC the ribosome. {ECO:0000250}.
CC -!- SUBUNIT: Ribosomal protein L40 is part of the 60S ribosomal subunit.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [60S ribosomal protein L40]: Cytoplasm
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: In C.elegans ubiquitin is encoded by 2 different genes.
CC ubq-2 gene codes for a single copy of ubiquitin fused to the ribosomal
CC proteins L40. ubq-1 gene codes for a polyubiquitin precursor with exact
CC head to tail repeats.
CC -!- MISCELLANEOUS: For a better understanding, features related to
CC ubiquitin are only indicated for the first chain.
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}.
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DR EMBL; L31492; AAC37252.1; -; Genomic_DNA.
DR EMBL; Z82083; CAB04967.1; -; Genomic_DNA.
DR PIR; T27638; T27638.
DR RefSeq; NP_499695.1; NM_067294.3.
DR AlphaFoldDB; P49632; -.
DR SMR; P49632; -.
DR BioGRID; 41891; 96.
DR STRING; 6239.ZK1010.1; -.
DR EPD; P49632; -.
DR PaxDb; P49632; -.
DR PeptideAtlas; P49632; -.
DR EnsemblMetazoa; ZK1010.1.1; ZK1010.1.1; WBGene00006728.
DR GeneID; 176718; -.
DR KEGG; cel:CELE_ZK1010.1; -.
DR UCSC; ZK1010.1.1; c. elegans.
DR CTD; 176718; -.
DR WormBase; ZK1010.1; CE15495; WBGene00006728; ubq-2.
DR eggNOG; KOG0003; Eukaryota.
DR GeneTree; ENSGT00940000153593; -.
DR HOGENOM; CLU_010412_3_4_1; -.
DR InParanoid; P49632; -.
DR OMA; FTIIRTH; -.
DR OrthoDB; 1536766at2759; -.
DR PhylomeDB; P49632; -.
DR PRO; PR:P49632; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006728; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031386; F:protein tag; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
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:0009949; P:polarity specification of anterior/posterior axis; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 4.10.1060.50; -; 1.
DR InterPro; IPR038587; L40e_sf.
DR InterPro; IPR001975; Ribosomal_L40e.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR019956; Ubiquitin_dom.
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; SSF54236; 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_0000396444"
FT CHAIN 77..128
FT /note="60S ribosomal protein L40"
FT /id="PRO_0000396445"
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; 14651 MW; 00CF9072777F017B CRC64;
MQIFVKTLTG KTITLEVEAS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
IQKESTLHLV LRLRGGIIEP SLRQLAQKYN CDKQICRKCY ARLPPRASNC RKKKCGHSSE
LRIKKKLK
