RLA2_RAT
ID RLA2_RAT Reviewed; 115 AA.
AC P02401; Q499W9;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=60S acidic ribosomal protein P2;
GN Name=Rplp2; Synonyms=Rp2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=1742361; DOI=10.1016/0300-9084(91)90127-m;
RA Wool I.G., Chan Y.-L., Glueck A., Suzuki K.;
RT "The primary structure of rat ribosomal proteins P0, P1, and P2 and a
RT proposal for a uniform nomenclature for mammalian and yeast ribosomal
RT proteins.";
RL Biochimie 73:861-870(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=1923757; DOI=10.1093/nar/19.18.4895;
RA Chan Y.-L., Wool I.G.;
RT "The structure of a gene containing introns and encoding rat ribosomal
RT protein P2.";
RL Nucleic Acids Res. 19:4895-4900(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PRELIMINARY PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=7096359; DOI=10.1016/s0021-9258(18)34259-5;
RA Lin A., Wittmann-Liebold B., McNally J., Wool I.G.;
RT "The primary structure of the acidic phosphoprotein P2 from rat liver 60 S
RT ribosomal subunits. Comparison with ribosomal 'A' proteins from other
RT species.";
RL J. Biol. Chem. 257:9189-9197(1982).
RN [5]
RP PROTEIN SEQUENCE OF 3-21, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-105, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-105, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Plays an important role in the elongation step of protein
CC synthesis.
CC -!- SUBUNIT: Heterodimer with RPLP1 at the lateral ribosomal stalk of the
CC large ribosomal subunit. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.
CC {ECO:0000305}.
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DR EMBL; X15098; CAA33201.1; -; mRNA.
DR EMBL; X55153; CAA38953.1; -; Genomic_DNA.
DR EMBL; BC099697; AAH99697.1; -; mRNA.
DR PIR; S22320; R6RTP2.
DR RefSeq; NP_001025192.1; NM_001030021.1.
DR RefSeq; XP_003749061.1; XM_003749013.2.
DR RefSeq; XP_008772967.1; XM_008774745.1.
DR AlphaFoldDB; P02401; -.
DR SMR; P02401; -.
DR BioGRID; 250823; 5.
DR IntAct; P02401; 6.
DR STRING; 10116.ENSRNOP00000038214; -.
DR iPTMnet; P02401; -.
DR PhosphoSitePlus; P02401; -.
DR jPOST; P02401; -.
DR PaxDb; P02401; -.
DR PRIDE; P02401; -.
DR Ensembl; ENSRNOT00000109157; ENSRNOP00000097047; ENSRNOG00000068445.
DR GeneID; 140662; -.
DR KEGG; rno:140662; -.
DR UCSC; RGD:621775; rat.
DR CTD; 6181; -.
DR RGD; 621775; Rplp2.
DR eggNOG; KOG3449; Eukaryota.
DR GeneTree; ENSGT00550000074828; -.
DR HOGENOM; CLU_114656_0_2_1; -.
DR InParanoid; P02401; -.
DR OMA; AYLMNVL; -.
DR OrthoDB; 1626327at2759; -.
DR PhylomeDB; P02401; -.
DR TreeFam; TF320650; -.
DR Reactome; R-RNO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-RNO-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-RNO-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-RNO-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-RNO-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-RNO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:P02401; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000002116; Expressed in ovary and 19 other tissues.
DR Genevisible; P02401; RN.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0005506; F:iron ion binding; IDA:RGD.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IPI:RGD.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:RGD.
DR GO; GO:0071320; P:cellular response to cAMP; IEP:RGD.
DR GO; GO:1904401; P:cellular response to Thyroid stimulating hormone; IEP:RGD.
DR GO; GO:0002182; P:cytoplasmic translational elongation; IEA:InterPro.
DR GO; GO:0045727; P:positive regulation of translation; IDA:RGD.
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 PANTHER; PTHR21141; PTHR21141; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..115
FT /note="60S acidic ribosomal protein P2"
FT /id="PRO_0000157644"
FT REGION 76..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P05387"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05387"
FT MOD_RES 21
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05387"
FT MOD_RES 21
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P99027"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05387"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05387"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
SQ SEQUENCE 115 AA; 11692 MW; 503B346F9F49591B CRC64;
MRYVASYLLA ALGGNSNPSA KDIKKILDSV GIEADDERLN KVISELNGKN IEDVIAQGVG
KLASVPAGGA VAVSAAPGSA APAAGSAPAA AEEKKDEKKE ESEESDDDMG FGLFD
