RLA5_SCHPO
ID RLA5_SCHPO Reviewed; 109 AA.
AC Q9UU78; O14316;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=60S acidic ribosomal protein P1-alpha 5;
GN Name=rpp103; Synonyms=rpa5, rpap1-5, rpp1-3; ORFNames=SPCP1E11.09c;
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 [MRNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=10701132; DOI=10.1139/g99-102;
RA Bonnet C., Perret E., Bonnin O., Picard A., Caput D., Lenaers G.;
RT "Identification of rpaP1-5 and rpaP2-6 genes encoding two additional
RT variants of the 60S acidic ribosomal proteins of Schizosaccharomyces
RT pombe.";
RL Genome 43:205-207(2000).
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-99, AND IDENTIFICATION BY
RP 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: Plays an important role in the elongation step of protein
CC synthesis. {ECO:0000250}.
CC -!- SUBUNIT: P1 and P2 exist as dimers at the large ribosomal subunit.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.
CC {ECO:0000305}.
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DR EMBL; AJ002733; CAA05695.1; -; mRNA.
DR EMBL; CU329672; CAB54868.1; -; Genomic_DNA.
DR PIR; T41688; T41688.
DR RefSeq; NP_588562.1; NM_001023549.2.
DR AlphaFoldDB; Q9UU78; -.
DR SMR; Q9UU78; -.
DR BioGRID; 276156; 1.
DR STRING; 4896.SPCP1E11.09c.1; -.
DR iPTMnet; Q9UU78; -.
DR MaxQB; Q9UU78; -.
DR PaxDb; Q9UU78; -.
DR PRIDE; Q9UU78; -.
DR EnsemblFungi; SPCP1E11.09c.1; SPCP1E11.09c.1:pep; SPCP1E11.09c.
DR GeneID; 2539598; -.
DR KEGG; spo:SPCP1E11.09c; -.
DR PomBase; SPCP1E11.09c; rpp103.
DR VEuPathDB; FungiDB:SPCP1E11.09c; -.
DR eggNOG; KOG1762; Eukaryota.
DR HOGENOM; CLU_114656_1_0_1; -.
DR InParanoid; Q9UU78; -.
DR OMA; IEGIWAD; -.
DR PhylomeDB; Q9UU78; -.
DR PRO; PR:Q9UU78; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; ISO:PomBase.
DR GO; GO:0030295; F:protein kinase activator activity; IBA:GO_Central.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:PomBase.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0002182; P:cytoplasmic translational elongation; ISO:PomBase.
DR Gene3D; 1.10.10.1410; -; 1.
DR HAMAP; MF_01478; Ribosomal_L12_arch; 1.
DR InterPro; IPR038716; P1/P2_N_sf.
DR InterPro; IPR027534; Ribosomal_L12/P1/P2.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..109
FT /note="60S acidic ribosomal protein P1-alpha 5"
FT /id="PRO_0000157709"
FT REGION 68..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..109
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 11
FT /note="A -> T (in Ref. 1; CAA05695)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="A -> T (in Ref. 1; CAA05695)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 109 AA; 11216 MW; E090154420413966 CRC64;
MSASELATSY AALILADEGI EITSDKLLSL TKAGNVEVEP IWATIFAKAL EGKDLKELLL
NIGSAGAASA PTAAGAGAAA PAEAAEEEKK EEAKEEEESD EDMGFGLFD
