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 27-MAR-2024, entry version 229.
DE RecName: Full=Large ribosomal subunit protein P1 {ECO:0000303|PubMed:24524803};
DE AltName: Full=60S acidic ribosomal protein P1;
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.7.11.4065-4074.1987;
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 UBIQUITINATION AT LYS-92 AND LYS-93.
RX PubMed=36638793; DOI=10.1016/j.cell.2022.12.025;
RA Oltion K., Carelli J.D., Yang T., See S.K., Wang H.Y., Kampmann M.,
RA Taunton J.;
RT "An E3 ligase network engages GCN1 to promote the degradation of
RT translation factors on stalled ribosomes.";
RL Cell 0:0-0(2023).
RN [14]
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 [15]
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 -!- PTM: Ubiquitinated at Lys-92 and Lys-93 by RNF14 and RNF25 in response
CC to ribosome collisions (ribosome stalling).
CC {ECO:0000269|PubMed:36638793}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.
CC {ECO:0000305}.
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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 AlphaFoldDB; P05386; -.
DR BMRB; P05386; -.
DR SMR; P05386; -.
DR BioGRID; 112095; 301.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR ComplexPortal; CPX-7664; 60S cytosolic large ribosomal subunit, testis-specific variant.
DR ComplexPortal; CPX-7665; 60S cytosolic large ribosomal subunit, striated muscle variant.
DR CORUM; P05386; -.
DR IntAct; P05386; 100.
DR MINT; P05386; -.
DR STRING; 9606.ENSP00000346037; -.
DR GlyGen; P05386; 1 site, 1 O-linked glycan (1 site).
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; 9606-ENSP00000346037; -.
DR PeptideAtlas; P05386; -.
DR PRIDE; P05386; -.
DR ProteomicsDB; 1259; -.
DR ProteomicsDB; 51831; -. [P05386-1]
DR Pumba; P05386; -.
DR TopDownProteomics; P05386-1; -. [P05386-1]
DR TopDownProteomics; P05386-2; -. [P05386-2]
DR Antibodypedia; 1247; 178 antibodies from 28 providers.
DR DNASU; 6176; -.
DR Ensembl; ENST00000260379.11; ENSP00000346037.5; ENSG00000137818.12. [P05386-1]
DR Ensembl; ENST00000357790.5; ENSP00000350437.5; ENSG00000137818.12. [P05386-2]
DR GeneID; 6176; -.
DR KEGG; hsa:6176; -.
DR MANE-Select; ENST00000260379.11; ENSP00000346037.5; NM_001003.3; NP_000994.1.
DR UCSC; uc002asd.2; human. [P05386-1]
DR AGR; HGNC:10372; -.
DR CTD; 6176; -.
DR DisGeNET; 6176; -.
DR GeneCards; RPLP1; -.
DR HGNC; HGNC:10372; RPLP1.
DR HPA; ENSG00000137818; Low tissue specificity.
DR MIM; 180520; gene.
DR neXtProt; NX_P05386; -.
DR OpenTargets; ENSG00000137818; -.
DR PharmGKB; PA34775; -.
DR VEuPathDB; HostDB:ENSG00000137818; -.
DR eggNOG; KOG1762; Eukaryota.
DR GeneTree; ENSGT00550000074698; -.
DR HOGENOM; CLU_114656_1_2_1; -.
DR InParanoid; P05386; -.
DR OMA; REELMCV; -.
DR OrthoDB; 26483at2759; -.
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 SignaLink; P05386; -.
DR SIGNOR; P05386; -.
DR BioGRID-ORCS; 6176; 826 hits in 1137 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 epithelium of bronchus and 114 other cell types or tissues.
DR ExpressionAtlas; P05386; baseline and differential.
DR Genevisible; P05386; HS.
DR GO; GO:0005737; C:cytoplasm; NAS:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:GO_Central.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
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:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR GO; GO:0006414; P:translational elongation; IEA:InterPro.
DR CDD; cd05831; Ribosomal_P1; 1.
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_P1/P2.
DR PANTHER; PTHR45696; 60S ACIDIC RIBOSOMAL PROTEIN P1; 1.
DR PANTHER; PTHR45696:SF10; 60S ACIDIC RIBOSOMAL PROTEIN P1-RELATED; 1.
DR Pfam; PF00428; Ribosomal_60s; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712"
FT CHAIN 2..114
FT /note="Large ribosomal subunit protein P1"
FT /id="PRO_0000157686"
FT REGION 69..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14997482,
FT ECO:0007744|PubMed:16807684"
FT CROSSLNK 92
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:36638793"
FT CROSSLNK 93
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:36638793"
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:0007829|PDB:2LBF"
FT HELIX 25..35
FT /evidence="ECO:0007829|PDB:2LBF"
FT HELIX 42..50
FT /evidence="ECO:0007829|PDB:2LBF"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:2LBF"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:2LBF"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:2LBF"
SQ SEQUENCE 114 AA; 11514 MW; 4C282AB8DCA079C8 CRC64;
MASVSELACI YSALILHDDE VTVTEDKINA LIKAAGVNVE PFWPGLFAKA LANVNIGSLI
CNVGAGGPAP AAGAAPAGGP APSTAAAPAE EKKVEAKKEE SEESDDDMGF GLFD
//
