ID   RL402_SCHPO             Reviewed;         128 AA.
AC   P0CH07; O13697; O14257; P0C014; P0C015; Q76PD0; Q9HDZ4;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=Ubiquitin-ribosomal protein eL40B fusion protein {ECO:0000305};
DE   Contains:
DE     RecName: Full=Ubiquitin;
DE   Contains:
DE     RecName: Full=Large ribosomal subunit protein eL40B {ECO:0000305};
DE     AltName: Full=60S ribosomal protein L40;
DE     AltName: Full=CEP52;
DE   Flags: Precursor;
GN   Name=uep1; Synonyms=ubi2; ORFNames=SPAC1805.12c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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-6-linked may be involved in DNA repair; Lys-11-linked is involved
CC       in ERAD (endoplasmic reticulum-associated degradation) and in cell-
CC       cycle regulation; Lys-29-linked is involved in lysosomal degradation;
CC       Lys-33-linked is involved in kinase modification; Lys-48-linked is
CC       involved in protein degradation via the proteasome; Lys-63-linked is
CC       involved in endocytosis, and DNA-damage responses. 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 (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: [Large ribosomal subunit protein eL40B]: Component of the
CC       ribosome, a large ribonucleoprotein complex responsible for the
CC       synthesis of proteins in the cell. The small ribosomal subunit (SSU)
CC       binds messenger RNAs (mRNAs) and translates the encoded message by
CC       selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large
CC       subunit (LSU) contains the ribosomal catalytic site termed the peptidyl
CC       transferase center (PTC), which catalyzes the formation of peptide
CC       bonds, thereby polymerizing the amino acids delivered by tRNAs into a
CC       polypeptide chain. The nascent polypeptides leave the ribosome through
CC       a tunnel in the LSU and interact with protein factors that function in
CC       enzymatic processing, targeting, and the membrane insertion of nascent
CC       chains at the exit of the ribosomal tunnel. eL40 is essential for
CC       translation of a subset of cellular transcripts, including stress
CC       response transcripts, such as DDR2. {ECO:0000250|UniProtKB:P0CH09}.
CC   -!- SUBUNIT: [Large ribosomal subunit protein eL40B]: Component of the
CC       small ribosomal subunit (SSU). Mature yeast ribosomes consist of a
CC       small (40S) and a large (60S) subunit. The 40S small subunit contains 1
CC       molecule of ribosomal RNA (18S rRNA) and at least 33 different
CC       proteins. The large 60S subunit contains 3 rRNA molecules (25S, 5.8S
CC       and 5S rRNA) and at least 46 different proteins.
CC       {ECO:0000250|UniProtKB:P0CH09}.
CC   -!- SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Large ribosomal subunit protein eL40B]:
CC       Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}. Nucleus, nucleolus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- MISCELLANEOUS: Ubiquitin is encoded by 5 different genes. Ubi1 and ubi2
CC       are synthesized as a polyprotein with one copy of ubiquitin fused to
CC       ribosomal proteins eL40A and eL40B, respectively. Ubi3 and ubi5 are
CC       polyproteins with one copy of ubiquitin fused to ribosomal proteins
CC       eS31A and eS31B, respectively. Ubi4 is a polyprotein containing 5 exact
CC       head to tail repeats of ubiquitin.
CC   -!- MISCELLANEOUS: There are 2 genes for eL40 in S.pombe.
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; CU329670; CAB55853.1; -; Genomic_DNA.
DR   PIR; T37547; T37547.
DR   RefSeq; NP_593923.1; NM_001019352.2.
DR   RefSeq; NP_594398.1; NM_001019821.2.
DR   PDB; 4II2; X-ray; 2.20 A; B=1-76.
DR   PDB; 4II3; X-ray; 2.90 A; B/D=1-76.
DR   PDB; 6O82; X-ray; 2.60 A; B/D=1-76.
DR   PDB; 6O83; X-ray; 3.15 A; B/D=1-75.
DR   PDBsum; 4II2; -.
DR   PDBsum; 4II3; -.
DR   PDBsum; 6O82; -.
DR   PDBsum; 6O83; -.
DR   AlphaFoldDB; P0CH07; -.
DR   SMR; P0CH07; -.
DR   BioGRID; 278262; 7.
DR   BioGRID; 278890; 14.
DR   STRING; 284812.P0CH07; -.
DR   iPTMnet; P0CH07; -.
DR   EnsemblFungi; SPAC11G7.04.1; SPAC11G7.04.1:pep; SPAC11G7.04.
DR   EnsemblFungi; SPAC1805.12c.1; SPAC1805.12c.1:pep; SPAC1805.12c.
DR   GeneID; 2541768; -.
DR   GeneID; 2542428; -.
DR   KEGG; spo:SPAC11G7.04; -.
DR   KEGG; spo:SPAC1805.12c; -.
DR   PomBase; SPAC1805.12c; uep1.
DR   VEuPathDB; FungiDB:SPAC11G7.04; -.
DR   VEuPathDB; FungiDB:SPAC1805.12c; -.
DR   HOGENOM; CLU_010412_3_4_1; -.
DR   InParanoid; P0CH07; -.
DR   PhylomeDB; P0CH07; -.
DR   PRO; PR:P0CH07; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; ISO:PomBase.
DR   GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0031386; F:protein tag activity; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; ISO:PomBase.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR   GO; GO:0002181; P:cytoplasmic translation; ISO:PomBase.
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:0042254; P:ribosome biogenesis; ISO:PomBase.
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:SF466; SIMILAR TO POLYUBIQUITIN; 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   3D-structure; Cytoplasm; Isopeptide bond; Nucleus; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT   CHAIN           1..76
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396452"
FT   CHAIN           77..128
FT                   /note="Large ribosomal subunit protein eL40B"
FT                   /id="PRO_0000396453"
FT   DOMAIN          1..76
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   CROSSLNK        6
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT   CROSSLNK        11
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT   CROSSLNK        27
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT   CROSSLNK        29
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        33
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT   CROSSLNK        48
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        63
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   STRAND          1..7
FT                   /evidence="ECO:0007829|PDB:4II2"
FT   STRAND          12..18
FT                   /evidence="ECO:0007829|PDB:4II2"
FT   HELIX           23..34
FT                   /evidence="ECO:0007829|PDB:4II2"
FT   HELIX           38..40
FT                   /evidence="ECO:0007829|PDB:4II2"
FT   STRAND          42..45
FT                   /evidence="ECO:0007829|PDB:4II2"
FT   HELIX           56..59
FT                   /evidence="ECO:0007829|PDB:4II2"
FT   STRAND          66..70
FT                   /evidence="ECO:0007829|PDB:4II2"
SQ   SEQUENCE   128 AA;  14595 MW;  A35EA817EFD46D38 CRC64;
     MQIFVKTLTG KTITLEVESS DTIDNVKSKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
     IQKESTLHLV LRLRGGIIEP SLKALASKYN CEKQICRKCY ARLPPRATNC RKKKCGHTNQ
     LRPKKKLK
//