RL5A_SCHPO
ID RL5A_SCHPO Reviewed; 294 AA.
AC P52822; O14153;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=60S ribosomal protein L5-A;
GN Name=rpl501; Synonyms=rpl5a; ORFNames=SPAC3H5.12c;
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 [GENOMIC DNA].
RX PubMed=8626719; DOI=10.1074/jbc.271.19.11571;
RA Michael W.M., Dreyfuss G.;
RT "Distinct domains in ribosomal protein L5 mediate 5 S rRNA binding and
RT nucleolar localization.";
RL J. Biol. Chem. 271:11571-11574(1996).
RN [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; TYR-12 AND SER-81, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell. The small
CC ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC molecules. The large subunit (LSU) contains the ribosomal catalytic
CC site termed the peptidyl transferase center (PTC), which catalyzes the
CC formation of peptide bonds, thereby polymerizing the amino acids
CC delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC leave the ribosome through a tunnel in the LSU and interact with
CC protein factors that function in enzymatic processing, targeting, and
CC the membrane insertion of nascent chains at the exit of the ribosomal
CC tunnel. {ECO:0000250|UniProtKB:P26321}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (LSU).
CC {ECO:0000250|UniProtKB:P26321}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P26321}. Nucleus
CC {ECO:0000250|UniProtKB:P26321}.
CC -!- MISCELLANEOUS: There are two genes for L5 in S.pombe.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL18 family.
CC {ECO:0000305}.
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DR EMBL; U48270; AAB05674.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB16596.1; -; Genomic_DNA.
DR PIR; T38758; T38758.
DR RefSeq; NP_594180.1; NM_001019604.2.
DR AlphaFoldDB; P52822; -.
DR SMR; P52822; -.
DR BioGRID; 280056; 3.
DR IntAct; P52822; 1.
DR MINT; P52822; -.
DR STRING; 4896.SPAC3H5.12c.1; -.
DR iPTMnet; P52822; -.
DR MaxQB; P52822; -.
DR PaxDb; P52822; -.
DR PRIDE; P52822; -.
DR EnsemblFungi; SPAC3H5.12c.1; SPAC3H5.12c.1:pep; SPAC3H5.12c.
DR GeneID; 2543642; -.
DR KEGG; spo:SPAC3H5.12c; -.
DR PomBase; SPAC3H5.12c; rpl501.
DR VEuPathDB; FungiDB:SPAC3H5.12c; -.
DR eggNOG; KOG0875; Eukaryota.
DR HOGENOM; CLU_056222_1_0_1; -.
DR InParanoid; P52822; -.
DR OMA; MAHGPRY; -.
DR PhylomeDB; P52822; -.
DR Reactome; R-SPO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SPO-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-SPO-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-SPO-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-SPO-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-SPO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:P52822; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008097; F:5S rRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:PomBase.
DR GO; GO:0002181; P:cytoplasmic translation; ISO:PomBase.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR HAMAP; MF_01337_A; Ribosomal_L18_A; 1.
DR InterPro; IPR005485; Rbsml_L5_euk/L18_arc.
DR InterPro; IPR025607; Rbsml_L5e_C.
DR PANTHER; PTHR23410; PTHR23410; 1.
DR Pfam; PF14204; Ribosomal_L18_c; 1.
DR Pfam; PF17144; Ribosomal_L5e; 1.
DR PRINTS; PR00058; RIBOSOMALL5.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..294
FT /note="60S ribosomal protein L5-A"
FT /id="PRO_0000131452"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 12
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 24
FT /note="Missing (in Ref. 1; AAB05674)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="T -> I (in Ref. 1; AAB05674)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="F -> S (in Ref. 1; AAB05674)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 294 AA; 33460 MW; CA72FE578EB3E35F CRC64;
MPFIKAVKSS PYFSRYQTKY RRRREGKTDY YARKRLIAQA KNKYNAPKYR LVVRFSNRFV
TCQIVSSRVN GDYVLAHAHS SELPRYGIKW GLANWTAAYA TGLLVARRAL AKVGLADKYE
GVTEPEGEFE LTEAIEDGPR PFKVFLDVGL KRTSTGSRVF GAMKGASDGG LFIPHSPNRF
PGFDIETEEL DDETLRKYIY GGHVAEYMEM LIDDDEERYQ KQFSGLIADG IESDQLEDIY
AEAYAKIRED PSFQKSGKDA AAFKAESLKH TQRKLTAEER KERFNAKVIE AGRA
