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Database: UniProt
Entry: P05386
LinkDB: P05386
Original site: P05386 
ID   RLA1_HUMAN              Reviewed;         114 AA.
AC   P05386; A6NIB2;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   07-OCT-2020, entry version 212.
DE   RecName: Full=60S acidic ribosomal protein P1;
DE   AltName: Full=Large ribosomal subunit protein P1 {ECO:0000303|PubMed:24524803};
GN   Name=RPLP1; Synonyms=RRP1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=3323886; DOI=10.1128/mcb.7.11.4065;
RA   Rich B.E., Steitz J.A.;
RT   "Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of cDNA
RT   clones, in vitro synthesis, and assembly.";
RL   Mol. Cell. Biol. 7:4065-4074(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11875025; DOI=10.1101/gr.214202;
RA   Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S.,
RA   Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
RT   "The human ribosomal protein genes: sequencing and comparative analysis of
RT   73 genes.";
RL   Genome Res. 12:379-390(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA   Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA   Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   15.";
RL   Nature 440:671-675(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Eye, Placenta, and Trophoblast;
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   [6]
RP   PHOSPHORYLATION AT SER-101.
RC   TISSUE=Pituitary;
RX   PubMed=14997482; DOI=10.1002/pmic.200300584;
RA   Giorgianni F., Beranova-Giorgianni S., Desiderio D.M.;
RT   "Identification and characterization of phosphorylated proteins in the
RT   human pituitary.";
RL   Proteomics 4:587-598(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Pituitary;
RX   PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
RA   Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
RT   "Phosphoproteomic analysis of the human pituitary.";
RL   Pituitary 9:109-120(2006).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [11]
RP   NOMENCLATURE.
RX   PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA   Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA   Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA   Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA   Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA   Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT   "A new system for naming ribosomal proteins.";
RL   Curr. Opin. Struct. Biol. 24:165-169(2014).
RN   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [13]
RP   STRUCTURE BY NMR OF 1-69, AND SUBUNIT.
RX   PubMed=22135285; DOI=10.1093/nar/gkr1143;
RA   Lee K.M., Yu C.W., Chiu T.Y., Sze K.H., Shaw P.C., Wong K.B.;
RT   "Solution structure of the dimerization domain of the eukaryotic stalk
RT   P1/P2 complex reveals the structural organization of eukaryotic stalk
RT   complex.";
RL   Nucleic Acids Res. 40:3172-3182(2012).
RN   [14]
RP   STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.
RX   PubMed=23636399; DOI=10.1038/nature12104;
RA   Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA   Wilson D.N., Beckmann R.;
RT   "Structures of the human and Drosophila 80S ribosome.";
RL   Nature 497:80-85(2013).
CC   -!- FUNCTION: Plays an important role in the elongation step of protein
CC       synthesis.
CC   -!- SUBUNIT: Heterodimer with RPLP2 at the lateral ribosomal stalk of the
CC       large ribosomal subunit. {ECO:0000269|PubMed:22135285}.
CC   -!- INTERACTION:
CC       P05386; P05387: RPLP2; NbExp=2; IntAct=EBI-354582, EBI-352813;
CC       P05386; P51687: SUOX; NbExp=3; IntAct=EBI-354582, EBI-3921347;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P05386-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P05386-2; Sequence=VSP_045244;
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.
CC       {ECO:0000305}.
DR   EMBL; M17886; AAA36471.1; -; mRNA.
DR   EMBL; AB061836; BAB79474.1; -; Genomic_DNA.
DR   EMBL; AC027237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471082; EAW77845.1; -; Genomic_DNA.
DR   EMBL; BC003369; AAH03369.1; -; mRNA.
DR   EMBL; BC007590; AAH07590.1; -; mRNA.
DR   EMBL; CD388103; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS10233.1; -. [P05386-1]
DR   CCDS; CCDS10234.1; -. [P05386-2]
DR   PIR; B27125; R6HUP1.
DR   RefSeq; NP_000994.1; NM_001003.2. [P05386-1]
DR   RefSeq; NP_998890.1; NM_213725.1. [P05386-2]
DR   PDB; 2LBF; NMR; -; A=1-69.
DR   PDB; 4BEH; NMR; -; A=1-114.
DR   PDB; 4V6X; EM; 5.00 A; Cs/Ct=1-114.
DR   PDBsum; 2LBF; -.
DR   PDBsum; 4BEH; -.
DR   PDBsum; 4V6X; -.
DR   BMRB; P05386; -.
DR   SMR; P05386; -.
DR   BioGRID; 112095; 180.
DR   ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR   CORUM; P05386; -.
DR   IntAct; P05386; 85.
DR   MINT; P05386; -.
DR   STRING; 9606.ENSP00000346037; -.
DR   iPTMnet; P05386; -.
DR   MetOSite; P05386; -.
DR   PhosphoSitePlus; P05386; -.
DR   SwissPalm; P05386; -.
DR   BioMuta; RPLP1; -.
DR   EPD; P05386; -.
DR   jPOST; P05386; -.
DR   MassIVE; P05386; -.
DR   MaxQB; P05386; -.
DR   PaxDb; P05386; -.
DR   PeptideAtlas; P05386; -.
DR   PRIDE; P05386; -.
DR   ProteomicsDB; 1259; -.
DR   ProteomicsDB; 51831; -. [P05386-1]
DR   TopDownProteomics; P05386-1; -. [P05386-1]
DR   TopDownProteomics; P05386-2; -. [P05386-2]
DR   Antibodypedia; 1247; 144 antibodies.
DR   DNASU; 6176; -.
DR   Ensembl; ENST00000260379; ENSP00000346037; ENSG00000137818. [P05386-1]
DR   Ensembl; ENST00000357790; ENSP00000350437; ENSG00000137818. [P05386-2]
DR   GeneID; 6176; -.
DR   KEGG; hsa:6176; -.
DR   UCSC; uc002asd.2; human. [P05386-1]
DR   CTD; 6176; -.
DR   DisGeNET; 6176; -.
DR   EuPathDB; HostDB:ENSG00000137818.11; -.
DR   GeneCards; RPLP1; -.
DR   HGNC; HGNC:10372; RPLP1.
DR   HPA; ENSG00000137818; Tissue enhanced (lymphoid).
DR   MIM; 180520; gene.
DR   neXtProt; NX_P05386; -.
DR   OpenTargets; ENSG00000137818; -.
DR   PharmGKB; PA34775; -.
DR   eggNOG; KOG1762; Eukaryota.
DR   GeneTree; ENSGT00550000074698; -.
DR   HOGENOM; CLU_114656_1_2_1; -.
DR   InParanoid; P05386; -.
DR   KO; K02942; -.
DR   OMA; SQETACV; -.
DR   PhylomeDB; P05386; -.
DR   TreeFam; TF312932; -.
DR   PathwayCommons; P05386; -.
DR   Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-HSA-156902; Peptide chain elongation.
DR   Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR   Reactome; R-HSA-192823; Viral mRNA Translation.
DR   Reactome; R-HSA-2408557; Selenocysteine synthesis.
DR   Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR   Reactome; R-HSA-72764; Eukaryotic Translation Termination.
DR   Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR   Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency.
DR   Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR   Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   BioGRID-ORCS; 6176; 751 hits in 881 CRISPR screens.
DR   ChiTaRS; RPLP1; human.
DR   GeneWiki; RPLP1; -.
DR   GenomeRNAi; 6176; -.
DR   Pharos; P05386; Tbio.
DR   PRO; PR:P05386; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; P05386; protein.
DR   Bgee; ENSG00000137818; Expressed in uterus and 134 other tissues.
DR   ExpressionAtlas; P05386; baseline and differential.
DR   Genevisible; P05386; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:GO_Central.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
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; IDA:GO_Central.
DR   GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR   GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR   GO; GO:0006412; P:translation; NAS:UniProtKB.
DR   GO; GO:0006414; P:translational elongation; IEA:InterPro.
DR   GO; GO:0006413; P:translational initiation; TAS:Reactome.
DR   GO; GO:0019083; P:viral transcription; TAS:Reactome.
DR   DisProt; DP01253; -.
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.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Phosphoprotein;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000244|PubMed:19413330,
FT                   ECO:0000244|PubMed:22223895, ECO:0000244|PubMed:25944712"
FT   CHAIN           2..114
FT                   /note="60S acidic ribosomal protein P1"
FT                   /id="PRO_0000157686"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000244|PubMed:19413330,
FT                   ECO:0000244|PubMed:22223895, ECO:0000244|PubMed:25944712"
FT   MOD_RES         101
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:16807684,
FT                   ECO:0000269|PubMed:14997482"
FT   VAR_SEQ         25..49
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_045244"
FT   HELIX           4..19
FT                   /evidence="ECO:0000244|PDB:2LBF"
FT   HELIX           25..35
FT                   /evidence="ECO:0000244|PDB:2LBF"
FT   HELIX           42..50
FT                   /evidence="ECO:0000244|PDB:2LBF"
FT   TURN            51..53
FT                   /evidence="ECO:0000244|PDB:2LBF"
FT   HELIX           56..60
FT                   /evidence="ECO:0000244|PDB:2LBF"
FT   TURN            61..64
FT                   /evidence="ECO:0000244|PDB:2LBF"
SQ   SEQUENCE   114 AA;  11514 MW;  4C282AB8DCA079C8 CRC64;
     MASVSELACI YSALILHDDE VTVTEDKINA LIKAAGVNVE PFWPGLFAKA LANVNIGSLI
     CNVGAGGPAP AAGAAPAGGP APSTAAAPAE EKKVEAKKEE SEESDDDMGF GLFD
//
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