RLA4_SCHPO
ID RLA4_SCHPO Reviewed; 110 AA.
AC P17478;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=60S acidic ribosomal protein P2-beta;
DE AltName: Full=A4;
GN Name=rpp202; Synonyms=rpa4, rpp2-2, rpp2b; ORFNames=SPBC23G7.15c;
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=2325655; DOI=10.1128/mcb.10.5.2341-2348.1990;
RA Beltrame M., Bianchi M.E.;
RT "A gene family for acidic ribosomal proteins in Schizosaccharomyces pombe:
RT two essential and two nonessential genes.";
RL Mol. Cell. Biol. 10:2341-2348(1990).
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-100, 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.
CC -!- SUBUNIT: P1 and P2 exist as dimers at the large ribosomal subunit.
CC -!- MISCELLANEOUS: Yeasts contain 4 individual small ribosomal A proteins
CC (RPA) which can be classified into two couples of similar but not
CC identical sequences. Each couple is distinctly related to one of the
CC two A proteins present in multicellular organisms.
CC -!- MISCELLANEOUS: Rpa3 and rpa4 are essential for cell survival, whereas
CC rpa1 and rpa2 are not.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.
CC {ECO:0000305}.
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DR EMBL; M33142; AAA35337.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA22631.1; -; Genomic_DNA.
DR PIR; D34715; R6BY24.
DR RefSeq; NP_595873.1; NM_001021779.2.
DR AlphaFoldDB; P17478; -.
DR SMR; P17478; -.
DR BioGRID; 277113; 6.
DR IntAct; P17478; 2.
DR MINT; P17478; -.
DR STRING; 4896.SPBC23G7.15c.1; -.
DR iPTMnet; P17478; -.
DR MaxQB; P17478; -.
DR PaxDb; P17478; -.
DR PRIDE; P17478; -.
DR EnsemblFungi; SPBC23G7.15c.1; SPBC23G7.15c.1:pep; SPBC23G7.15c.
DR GeneID; 2540587; -.
DR KEGG; spo:SPBC23G7.15c; -.
DR PomBase; SPBC23G7.15c; rpp202.
DR VEuPathDB; FungiDB:SPBC23G7.15c; -.
DR eggNOG; KOG3449; Eukaryota.
DR HOGENOM; CLU_114656_0_1_1; -.
DR InParanoid; P17478; -.
DR OMA; TCPSAND; -.
DR PhylomeDB; P17478; -.
DR PRO; PR:P17478; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; ISO:PomBase.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:PomBase.
DR GO; GO:0002182; P:cytoplasmic translational elongation; ISO:PomBase.
DR CDD; cd05833; Ribosomal_P2; 1.
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.
DR InterPro; IPR044076; Ribosomal_P2.
DR InterPro; IPR001859; T.cruzi_P2-like.
DR PANTHER; PTHR21141; PTHR21141; 1.
DR PRINTS; PR00456; RIBOSOMALP2.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..110
FT /note="60S acidic ribosomal protein P2-beta"
FT /id="PRO_0000157684"
FT REGION 73..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..110
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 110 AA; 11120 MW; 477D7B04CF3652CF CRC64;
MKYLAAYLLL TVGGKQSPSA SDIESVLSTV GIEAEAERVE SLISELNGKN IEELIAAGNE
KLSTVPSAGA VATPAAGGAA GAEATSAAEE AKEEEAAEES DEDMGFGLFD
