Full text data of RPLP1
RPLP1
(RRP1)
[Confidence: low (only semi-automatic identification from reviews)]
60S acidic ribosomal protein P1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
60S acidic ribosomal protein P1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P05386
ID RLA1_HUMAN Reviewed; 114 AA.
AC P05386; A6NIB2;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1988, sequence version 1.
DT 22-JAN-2014, entry version 145.
DE RecName: Full=60S acidic ribosomal protein P1;
GN Name=RPLP1; Synonyms=RRP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3323886;
RA Rich B.E., Steitz J.A.;
RT "Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of
RT cDNA 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
RT analysis of 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.,
RA Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
RA Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
RA Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
RA Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
RA Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
RA Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
RA Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human
RT chromosome 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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 MASS
RP SPECTROMETRY.
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, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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.,
RA Buerckstuemmer T., 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 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 [11]
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
CC protein synthesis.
CC -!- SUBUNIT: Heterodimer with RPLP2 at the lateral ribosomal stalk of
CC the large ribosomal subunit.
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 Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the ribosomal protein L12P family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 PIR; B27125; R6HUP1.
DR RefSeq; NP_000994.1; NM_001003.2.
DR RefSeq; NP_998890.1; NM_213725.1.
DR UniGene; Hs.356502; -.
DR PDB; 2LBF; NMR; -; A=1-69.
DR PDB; 3J3B; EM; 5.00 A; s/t=1-114.
DR PDB; 4BEH; NMR; -; A=1-114.
DR PDBsum; 2LBF; -.
DR PDBsum; 3J3B; -.
DR PDBsum; 4BEH; -.
DR ProteinModelPortal; P05386; -.
DR SMR; P05386; 1-69.
DR IntAct; P05386; 49.
DR MINT; MINT-193188; -.
DR STRING; 9606.ENSP00000346037; -.
DR PhosphoSite; P05386; -.
DR DMDM; 133051; -.
DR PaxDb; P05386; -.
DR PRIDE; P05386; -.
DR DNASU; 6176; -.
DR Ensembl; ENST00000260379; ENSP00000346037; ENSG00000137818.
DR Ensembl; ENST00000357790; ENSP00000350437; ENSG00000137818.
DR GeneID; 6176; -.
DR KEGG; hsa:6176; -.
DR UCSC; uc002ase.1; human.
DR CTD; 6176; -.
DR GeneCards; GC15P069745; -.
DR HGNC; HGNC:10372; RPLP1.
DR HPA; HPA003368; -.
DR MIM; 180520; gene.
DR neXtProt; NX_P05386; -.
DR PharmGKB; PA34775; -.
DR eggNOG; COG2058; -.
DR HOGENOM; HOG000229898; -.
DR HOVERGEN; HBG002291; -.
DR InParanoid; P05386; -.
DR KO; K02942; -.
DR OMA; SSEVACT; -.
DR OrthoDB; EOG7M0NVC; -.
DR PhylomeDB; P05386; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; RpLP1; human.
DR GeneWiki; RPLP1; -.
DR GenomeRNAi; 6176; -.
DR NextBio; 23995; -.
DR PRO; PR:P05386; -.
DR ArrayExpress; P05386; -.
DR Bgee; P05386; -.
DR CleanEx; HS_RPLP1; -.
DR CleanEx; HS_RRP1; -.
DR Genevestigator; P05386; -.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
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:0006414; P:translational elongation; TAS:Reactome.
DR GO; GO:0006413; P:translational initiation; TAS:Reactome.
DR GO; GO:0006415; P:translational termination; TAS:Reactome.
DR GO; GO:0019083; P:viral transcription; TAS:Reactome.
DR HAMAP; MF_01478; Ribosomal_L12_arch; 1; -.
DR InterPro; IPR001813; Ribosomal_L10/L12.
DR InterPro; IPR027534; Ribosomal_L12.
DR Pfam; PF00428; Ribosomal_60s; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 114 60S acidic ribosomal protein P1.
FT /FTId=PRO_0000157686.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 101 101 Phosphoserine.
FT VAR_SEQ 25 49 Missing (in isoform 2).
FT /FTId=VSP_045244.
FT HELIX 4 19
FT HELIX 25 35
FT HELIX 42 50
FT TURN 51 53
FT HELIX 56 60
FT TURN 61 64
SQ SEQUENCE 114 AA; 11514 MW; 4C282AB8DCA079C8 CRC64;
MASVSELACI YSALILHDDE VTVTEDKINA LIKAAGVNVE PFWPGLFAKA LANVNIGSLI
CNVGAGGPAP AAGAAPAGGP APSTAAAPAE EKKVEAKKEE SEESDDDMGF GLFD
//
ID RLA1_HUMAN Reviewed; 114 AA.
AC P05386; A6NIB2;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1988, sequence version 1.
DT 22-JAN-2014, entry version 145.
DE RecName: Full=60S acidic ribosomal protein P1;
GN Name=RPLP1; Synonyms=RRP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3323886;
RA Rich B.E., Steitz J.A.;
RT "Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of
RT cDNA 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
RT analysis of 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.,
RA Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
RA Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
RA Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
RA Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
RA Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
RA Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
RA Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human
RT chromosome 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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 MASS
RP SPECTROMETRY.
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, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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.,
RA Buerckstuemmer T., 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 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 [11]
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
CC protein synthesis.
CC -!- SUBUNIT: Heterodimer with RPLP2 at the lateral ribosomal stalk of
CC the large ribosomal subunit.
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 Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the ribosomal protein L12P family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 PIR; B27125; R6HUP1.
DR RefSeq; NP_000994.1; NM_001003.2.
DR RefSeq; NP_998890.1; NM_213725.1.
DR UniGene; Hs.356502; -.
DR PDB; 2LBF; NMR; -; A=1-69.
DR PDB; 3J3B; EM; 5.00 A; s/t=1-114.
DR PDB; 4BEH; NMR; -; A=1-114.
DR PDBsum; 2LBF; -.
DR PDBsum; 3J3B; -.
DR PDBsum; 4BEH; -.
DR ProteinModelPortal; P05386; -.
DR SMR; P05386; 1-69.
DR IntAct; P05386; 49.
DR MINT; MINT-193188; -.
DR STRING; 9606.ENSP00000346037; -.
DR PhosphoSite; P05386; -.
DR DMDM; 133051; -.
DR PaxDb; P05386; -.
DR PRIDE; P05386; -.
DR DNASU; 6176; -.
DR Ensembl; ENST00000260379; ENSP00000346037; ENSG00000137818.
DR Ensembl; ENST00000357790; ENSP00000350437; ENSG00000137818.
DR GeneID; 6176; -.
DR KEGG; hsa:6176; -.
DR UCSC; uc002ase.1; human.
DR CTD; 6176; -.
DR GeneCards; GC15P069745; -.
DR HGNC; HGNC:10372; RPLP1.
DR HPA; HPA003368; -.
DR MIM; 180520; gene.
DR neXtProt; NX_P05386; -.
DR PharmGKB; PA34775; -.
DR eggNOG; COG2058; -.
DR HOGENOM; HOG000229898; -.
DR HOVERGEN; HBG002291; -.
DR InParanoid; P05386; -.
DR KO; K02942; -.
DR OMA; SSEVACT; -.
DR OrthoDB; EOG7M0NVC; -.
DR PhylomeDB; P05386; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; RpLP1; human.
DR GeneWiki; RPLP1; -.
DR GenomeRNAi; 6176; -.
DR NextBio; 23995; -.
DR PRO; PR:P05386; -.
DR ArrayExpress; P05386; -.
DR Bgee; P05386; -.
DR CleanEx; HS_RPLP1; -.
DR CleanEx; HS_RRP1; -.
DR Genevestigator; P05386; -.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
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:0006414; P:translational elongation; TAS:Reactome.
DR GO; GO:0006413; P:translational initiation; TAS:Reactome.
DR GO; GO:0006415; P:translational termination; TAS:Reactome.
DR GO; GO:0019083; P:viral transcription; TAS:Reactome.
DR HAMAP; MF_01478; Ribosomal_L12_arch; 1; -.
DR InterPro; IPR001813; Ribosomal_L10/L12.
DR InterPro; IPR027534; Ribosomal_L12.
DR Pfam; PF00428; Ribosomal_60s; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 114 60S acidic ribosomal protein P1.
FT /FTId=PRO_0000157686.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 101 101 Phosphoserine.
FT VAR_SEQ 25 49 Missing (in isoform 2).
FT /FTId=VSP_045244.
FT HELIX 4 19
FT HELIX 25 35
FT HELIX 42 50
FT TURN 51 53
FT HELIX 56 60
FT TURN 61 64
SQ SEQUENCE 114 AA; 11514 MW; 4C282AB8DCA079C8 CRC64;
MASVSELACI YSALILHDDE VTVTEDKINA LIKAAGVNVE PFWPGLFAKA LANVNIGSLI
CNVGAGGPAP AAGAAPAGGP APSTAAAPAE EKKVEAKKEE SEESDDDMGF GLFD
//
MIM
180520
*RECORD*
*FIELD* NO
180520
*FIELD* TI
*180520 RIBOSOMAL PHOSPHOPROTEIN, LARGE, P1; RPLP1
;;RIBOSOMAL PHOSPHOPROTEIN, ACIDIC, P1
read more*FIELD* TX
DESCRIPTION
Acidic ribosomal proteins, called A-proteins or P-proteins, are
generally present in multiple copies on the ribosome and have
isoelectric points in the range of pH 3 to 5, in contrast to most
ribosomal proteins, which are single copy and basic. A-proteins have
hydrophobic amino acid compositions, notably about 20% alanine.
CLONING
Rich and Steitz (1987) described the isolation and analysis of 3 cDNA
molecules that encode the human P-proteins, P2 (180530), P1, and P0
(180510). The human P1 and P2 cDNA nucleotide sequences and deduced
amino acid sequences of the proteins are very similar to the sequences
that have been determined for the corresponding rat, shrimp, and yeast
proteins and cDNAs. P0 sequences had not previously been described. To
demonstrate that the coding sequences are full length, Rich and Steitz
(1987) transcribed the P0, P1, and P2 cDNAs in vitro. The P0, P1, and P2
proteins produced were serologically and electrophoretically identical
to P-proteins extracted from HeLa cells. The deduced P1 protein contains
114 amino acids. Northern blot analysis revealed expression of a 0.65-kb
transcript in HeLa cells.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the RPLP1
gene to chromosome 15 (TMAP D15S1202).
*FIELD* RF
1. Rich, B. E.; Steitz, J. A.: Human acidic ribosomal phosphoproteins
P0, P1, and P2: analysis of cDNA clones, in vitro synthesis, and assembly. Mole
c. Cell. Biol. 7: 4065-4074, 1987.
*FIELD* CN
Paul J. Converse - updated: 04/12/2002
*FIELD* CD
Victor A. McKusick: 12/3/1987
*FIELD* ED
mgross: 04/12/2002
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
marie: 3/25/1988
root: 12/3/1987
*RECORD*
*FIELD* NO
180520
*FIELD* TI
*180520 RIBOSOMAL PHOSPHOPROTEIN, LARGE, P1; RPLP1
;;RIBOSOMAL PHOSPHOPROTEIN, ACIDIC, P1
read more*FIELD* TX
DESCRIPTION
Acidic ribosomal proteins, called A-proteins or P-proteins, are
generally present in multiple copies on the ribosome and have
isoelectric points in the range of pH 3 to 5, in contrast to most
ribosomal proteins, which are single copy and basic. A-proteins have
hydrophobic amino acid compositions, notably about 20% alanine.
CLONING
Rich and Steitz (1987) described the isolation and analysis of 3 cDNA
molecules that encode the human P-proteins, P2 (180530), P1, and P0
(180510). The human P1 and P2 cDNA nucleotide sequences and deduced
amino acid sequences of the proteins are very similar to the sequences
that have been determined for the corresponding rat, shrimp, and yeast
proteins and cDNAs. P0 sequences had not previously been described. To
demonstrate that the coding sequences are full length, Rich and Steitz
(1987) transcribed the P0, P1, and P2 cDNAs in vitro. The P0, P1, and P2
proteins produced were serologically and electrophoretically identical
to P-proteins extracted from HeLa cells. The deduced P1 protein contains
114 amino acids. Northern blot analysis revealed expression of a 0.65-kb
transcript in HeLa cells.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the RPLP1
gene to chromosome 15 (TMAP D15S1202).
*FIELD* RF
1. Rich, B. E.; Steitz, J. A.: Human acidic ribosomal phosphoproteins
P0, P1, and P2: analysis of cDNA clones, in vitro synthesis, and assembly. Mole
c. Cell. Biol. 7: 4065-4074, 1987.
*FIELD* CN
Paul J. Converse - updated: 04/12/2002
*FIELD* CD
Victor A. McKusick: 12/3/1987
*FIELD* ED
mgross: 04/12/2002
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
marie: 3/25/1988
root: 12/3/1987