ID   RL40_BRARP              Reviewed;         128 AA.
AC   P51423; O82079; P03993; P69311;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 2.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Ubiquitin-60S ribosomal protein L40;
DE   Contains:
DE     RecName: Full=Ubiquitin;
DE   Contains:
DE     RecName: Full=60S ribosomal protein L40;
DE     AltName: Full=CEP52;
DE   Flags: Precursor;
OS   Brassica rapa subsp. pekinensis (Chinese cabbage) (Brassica pekinensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=51351;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Jangwon; TISSUE=Shoot;
RA   Song S., Choi Y.;
RL   Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases.
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.
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: Ubiquitin is generally synthesized as a polyubiquitin
CC       precursor with tandem head to tail repeats. Often, there is one to
CC       three additional amino acids after the last repeat, removed in the
CC       mature protein. Alternatively, ubiquitin extension protein is
CC       synthesized as a single copy of ubiquitin fused to a ribosomal protein
CC       (either L40 or S27A) or to an ubiquitin-related protein (either RUB1 or
CC       RUB2). Following translation, extension protein is cleaved from
CC       ubiquitin.
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; Z24738; CAA80863.1; -; mRNA.
DR   EMBL; L21898; AAA33014.1; -; mRNA.
DR   PIR; S34662; S34662.
DR   AlphaFoldDB; P51423; -.
DR   SMR; P51423; -.
DR   STRING; 51351.P51423; -.
DR   eggNOG; KOG0001; Eukaryota.
DR   Proteomes; UP000011750; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; IEA:UniProt.
DR   GO; GO:0031386; F:protein tag; 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   Gene3D; 4.10.1060.50; -; 1.
DR   InterPro; IPR038587; L40e_sf.
DR   InterPro; IPR001975; Ribosomal_L40e.
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   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   SUPFAM; SSF57829; SSF57829; 1.
DR   PROSITE; PS00299; UBIQUITIN_1; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Isopeptide bond; Nucleus; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein.
FT   CHAIN           1..76
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000114836"
FT   CHAIN           77..128
FT                   /note="60S ribosomal protein L40"
FT                   /id="PRO_0000138759"
FT   DOMAIN          1..76
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
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;  14629 MW;  2E4EB17A286E9E07 CRC64;
     MQIFVKTLTG KTITLEVESS DTIDNVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLADYN
     IQKESTLHLV LRLRGGIIEP SLMALARKYN QAKMICRKCY ARLHPRAVNC RKKKCGHSNQ
     LRPKKKIK