Full text data of RPLP2
RPLP2
(D11S2243E, RPP2)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
60S acidic ribosomal protein P2 (Renal carcinoma antigen NY-REN-44)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
60S acidic ribosomal protein P2 (Renal carcinoma antigen NY-REN-44)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P05387
ID RLA2_HUMAN Reviewed; 115 AA.
AC P05387; Q6FG96;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1988, sequence version 1.
DT 22-JAN-2014, entry version 155.
DE RecName: Full=60S acidic ribosomal protein P2;
DE AltName: Full=Renal carcinoma antigen NY-REN-44;
GN Name=RPLP2; Synonyms=D11S2243E, RPP2;
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].
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 [MRNA].
RC TISSUE=Mammary carcinoma;
RX PubMed=2153399;
RA Sharp M.G.F., Adams S.M., Elvin P., Walker R.A., Brammar W.J.,
RA Varley J.M.;
RT "A sequence previously identified as metastasis-related encodes an
RT acidic ribosomal phosphoprotein, P2.";
RL Br. J. Cancer 61:83-88(1990).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, Ovary, Prostate, and Skin;
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 [9]
RP PROTEIN SEQUENCE OF 1-10.
RC TISSUE=Liver;
RX PubMed=1286669; DOI=10.1002/elps.11501301201;
RA Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
RA Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
RA Appel R.D., Hughes G.J.;
RT "Human liver protein map: a reference database established by
RT microsequencing and gel comparison.";
RL Electrophoresis 13:992-1001(1992).
RN [10]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-
RT cell carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [11]
RP PHOSPHORYLATION AT SER-102.
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-79 AND SER-86,
RP AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-79, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-17 AND SER-79, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [21]
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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [23]
RP STRUCTURE BY NMR OF 1-69, AND SUBUNIT.
RX PubMed=20385603; DOI=10.1093/nar/gkq231;
RA Lee K.M., Yu C.W., Chan D.S., Chiu T.Y., Zhu G., Sze K.H., Shaw P.C.,
RA Wong K.B.;
RT "Solution structure of the dimerization domain of ribosomal protein P2
RT provides insights for the structural organization of eukaryotic
RT stalk.";
RL Nucleic Acids Res. 38:5206-5216(2010).
RN [24]
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 RPLP1 at the lateral ribosomal stalk of
CC the large ribosomal subunit.
CC -!- SIMILARITY: Belongs to the ribosomal protein L12P family.
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DR EMBL; M17887; AAA36472.1; -; mRNA.
DR EMBL; AB061837; BAB79475.1; -; Genomic_DNA.
DR EMBL; AK311954; BAG34894.1; -; mRNA.
DR EMBL; CR542212; CAG47008.1; -; mRNA.
DR EMBL; CR542248; CAG47044.1; -; mRNA.
DR EMBL; AP006621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471158; EAX02393.1; -; Genomic_DNA.
DR EMBL; BC005354; AAH05354.1; -; mRNA.
DR EMBL; BC005920; AAH05920.1; -; mRNA.
DR EMBL; BC007573; AAH07573.1; -; mRNA.
DR EMBL; BC062314; AAH62314.1; -; mRNA.
DR PIR; C27125; R6HUP2.
DR RefSeq; NP_000995.1; NM_001004.3.
DR UniGene; Hs.437594; -.
DR PDB; 1S4J; NMR; -; A=103-115.
DR PDB; 2JDL; X-ray; 2.20 A; C/D=105-115.
DR PDB; 2LBF; NMR; -; B=1-69.
DR PDB; 2W1O; NMR; -; A/B=1-69.
DR PDB; 3J3B; EM; 5.00 A; u/v=1-115.
DR PDB; 4BEH; NMR; -; B=1-115.
DR PDBsum; 1S4J; -.
DR PDBsum; 2JDL; -.
DR PDBsum; 2LBF; -.
DR PDBsum; 2W1O; -.
DR PDBsum; 3J3B; -.
DR PDBsum; 4BEH; -.
DR ProteinModelPortal; P05387; -.
DR SMR; P05387; 1-69.
DR IntAct; P05387; 19.
DR MINT; MINT-4999550; -.
DR STRING; 9606.ENSP00000322419; -.
DR Allergome; 1276; Hom s P2.
DR PhosphoSite; P05387; -.
DR DMDM; 133061; -.
DR SWISS-2DPAGE; P05387; -.
DR PaxDb; P05387; -.
DR PeptideAtlas; P05387; -.
DR PRIDE; P05387; -.
DR DNASU; 6181; -.
DR Ensembl; ENST00000321153; ENSP00000322419; ENSG00000177600.
DR Ensembl; ENST00000530797; ENSP00000431240; ENSG00000177600.
DR GeneID; 6181; -.
DR KEGG; hsa:6181; -.
DR UCSC; uc001lrq.1; human.
DR CTD; 6181; -.
DR GeneCards; GC11P000799; -.
DR HGNC; HGNC:10377; RPLP2.
DR MIM; 180530; gene.
DR neXtProt; NX_P05387; -.
DR PharmGKB; PA34776; -.
DR eggNOG; COG2058; -.
DR HOGENOM; HOG000229897; -.
DR HOVERGEN; HBG014761; -.
DR InParanoid; P05387; -.
DR KO; K02943; -.
DR OMA; VISELHG; -.
DR OrthoDB; EOG7JMGHH; -.
DR PhylomeDB; P05387; -.
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; RPLP2; human.
DR EvolutionaryTrace; P05387; -.
DR GeneWiki; RPLP2; -.
DR GenomeRNAi; 6181; -.
DR NextBio; 24001; -.
DR PRO; PR:P05387; -.
DR Bgee; P05387; -.
DR CleanEx; HS_RPLP2; -.
DR Genevestigator; P05387; -.
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; Complete proteome;
KW Direct protein sequencing; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1 115 60S acidic ribosomal protein P2.
FT /FTId=PRO_0000157640.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 17 17 Phosphoserine.
FT MOD_RES 21 21 N6-acetyllysine.
FT MOD_RES 79 79 Phosphoserine.
FT MOD_RES 86 86 Phosphoserine.
FT MOD_RES 102 102 Phosphoserine.
FT MOD_RES 105 105 Phosphoserine (By similarity).
FT STRAND 1 3
FT HELIX 4 13
FT HELIX 20 28
FT TURN 29 31
FT HELIX 38 46
FT HELIX 51 55
FT STRAND 59 61
FT STRAND 63 66
FT TURN 91 94
FT STRAND 106 113
SQ SEQUENCE 115 AA; 11665 MW; B5ECFE2510A756BF CRC64;
MRYVASYLLA ALGGNSSPSA KDIKKILDSV GIEADDDRLN KVISELNGKN IEDVIAQGIG
KLASVPAGGA VAVSAAPGSA APAAGSAPAA AEEKKDEKKE ESEESDDDMG FGLFD
//
ID RLA2_HUMAN Reviewed; 115 AA.
AC P05387; Q6FG96;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1988, sequence version 1.
DT 22-JAN-2014, entry version 155.
DE RecName: Full=60S acidic ribosomal protein P2;
DE AltName: Full=Renal carcinoma antigen NY-REN-44;
GN Name=RPLP2; Synonyms=D11S2243E, RPP2;
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].
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 [MRNA].
RC TISSUE=Mammary carcinoma;
RX PubMed=2153399;
RA Sharp M.G.F., Adams S.M., Elvin P., Walker R.A., Brammar W.J.,
RA Varley J.M.;
RT "A sequence previously identified as metastasis-related encodes an
RT acidic ribosomal phosphoprotein, P2.";
RL Br. J. Cancer 61:83-88(1990).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, Ovary, Prostate, and Skin;
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 [9]
RP PROTEIN SEQUENCE OF 1-10.
RC TISSUE=Liver;
RX PubMed=1286669; DOI=10.1002/elps.11501301201;
RA Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
RA Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
RA Appel R.D., Hughes G.J.;
RT "Human liver protein map: a reference database established by
RT microsequencing and gel comparison.";
RL Electrophoresis 13:992-1001(1992).
RN [10]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-
RT cell carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [11]
RP PHOSPHORYLATION AT SER-102.
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-79 AND SER-86,
RP AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-79, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-17 AND SER-79, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [21]
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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [23]
RP STRUCTURE BY NMR OF 1-69, AND SUBUNIT.
RX PubMed=20385603; DOI=10.1093/nar/gkq231;
RA Lee K.M., Yu C.W., Chan D.S., Chiu T.Y., Zhu G., Sze K.H., Shaw P.C.,
RA Wong K.B.;
RT "Solution structure of the dimerization domain of ribosomal protein P2
RT provides insights for the structural organization of eukaryotic
RT stalk.";
RL Nucleic Acids Res. 38:5206-5216(2010).
RN [24]
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 RPLP1 at the lateral ribosomal stalk of
CC the large ribosomal subunit.
CC -!- SIMILARITY: Belongs to the ribosomal protein L12P family.
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DR EMBL; M17887; AAA36472.1; -; mRNA.
DR EMBL; AB061837; BAB79475.1; -; Genomic_DNA.
DR EMBL; AK311954; BAG34894.1; -; mRNA.
DR EMBL; CR542212; CAG47008.1; -; mRNA.
DR EMBL; CR542248; CAG47044.1; -; mRNA.
DR EMBL; AP006621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471158; EAX02393.1; -; Genomic_DNA.
DR EMBL; BC005354; AAH05354.1; -; mRNA.
DR EMBL; BC005920; AAH05920.1; -; mRNA.
DR EMBL; BC007573; AAH07573.1; -; mRNA.
DR EMBL; BC062314; AAH62314.1; -; mRNA.
DR PIR; C27125; R6HUP2.
DR RefSeq; NP_000995.1; NM_001004.3.
DR UniGene; Hs.437594; -.
DR PDB; 1S4J; NMR; -; A=103-115.
DR PDB; 2JDL; X-ray; 2.20 A; C/D=105-115.
DR PDB; 2LBF; NMR; -; B=1-69.
DR PDB; 2W1O; NMR; -; A/B=1-69.
DR PDB; 3J3B; EM; 5.00 A; u/v=1-115.
DR PDB; 4BEH; NMR; -; B=1-115.
DR PDBsum; 1S4J; -.
DR PDBsum; 2JDL; -.
DR PDBsum; 2LBF; -.
DR PDBsum; 2W1O; -.
DR PDBsum; 3J3B; -.
DR PDBsum; 4BEH; -.
DR ProteinModelPortal; P05387; -.
DR SMR; P05387; 1-69.
DR IntAct; P05387; 19.
DR MINT; MINT-4999550; -.
DR STRING; 9606.ENSP00000322419; -.
DR Allergome; 1276; Hom s P2.
DR PhosphoSite; P05387; -.
DR DMDM; 133061; -.
DR SWISS-2DPAGE; P05387; -.
DR PaxDb; P05387; -.
DR PeptideAtlas; P05387; -.
DR PRIDE; P05387; -.
DR DNASU; 6181; -.
DR Ensembl; ENST00000321153; ENSP00000322419; ENSG00000177600.
DR Ensembl; ENST00000530797; ENSP00000431240; ENSG00000177600.
DR GeneID; 6181; -.
DR KEGG; hsa:6181; -.
DR UCSC; uc001lrq.1; human.
DR CTD; 6181; -.
DR GeneCards; GC11P000799; -.
DR HGNC; HGNC:10377; RPLP2.
DR MIM; 180530; gene.
DR neXtProt; NX_P05387; -.
DR PharmGKB; PA34776; -.
DR eggNOG; COG2058; -.
DR HOGENOM; HOG000229897; -.
DR HOVERGEN; HBG014761; -.
DR InParanoid; P05387; -.
DR KO; K02943; -.
DR OMA; VISELHG; -.
DR OrthoDB; EOG7JMGHH; -.
DR PhylomeDB; P05387; -.
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; RPLP2; human.
DR EvolutionaryTrace; P05387; -.
DR GeneWiki; RPLP2; -.
DR GenomeRNAi; 6181; -.
DR NextBio; 24001; -.
DR PRO; PR:P05387; -.
DR Bgee; P05387; -.
DR CleanEx; HS_RPLP2; -.
DR Genevestigator; P05387; -.
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; Complete proteome;
KW Direct protein sequencing; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1 115 60S acidic ribosomal protein P2.
FT /FTId=PRO_0000157640.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 17 17 Phosphoserine.
FT MOD_RES 21 21 N6-acetyllysine.
FT MOD_RES 79 79 Phosphoserine.
FT MOD_RES 86 86 Phosphoserine.
FT MOD_RES 102 102 Phosphoserine.
FT MOD_RES 105 105 Phosphoserine (By similarity).
FT STRAND 1 3
FT HELIX 4 13
FT HELIX 20 28
FT TURN 29 31
FT HELIX 38 46
FT HELIX 51 55
FT STRAND 59 61
FT STRAND 63 66
FT TURN 91 94
FT STRAND 106 113
SQ SEQUENCE 115 AA; 11665 MW; B5ECFE2510A756BF CRC64;
MRYVASYLLA ALGGNSSPSA KDIKKILDSV GIEADDDRLN KVISELNGKN IEDVIAQGIG
KLASVPAGGA VAVSAAPGSA APAAGSAPAA AEEKKDEKKE ESEESDDDMG FGLFD
//
MIM
180530
*RECORD*
*FIELD* NO
180530
*FIELD* TI
*180530 RIBOSOMAL PHOSPHOPROTEIN, LARGE, P2; RPLP2
;;RIBOSOMAL PHOSPHOPROTEIN, ACIDIC, P2
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, P1 (180520), 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 P2 protein contains
115 amino acids. Northern blot analysis revealed expression of a 0.60-kb
transcript in HeLa cells.
*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
180530
*FIELD* TI
*180530 RIBOSOMAL PHOSPHOPROTEIN, LARGE, P2; RPLP2
;;RIBOSOMAL PHOSPHOPROTEIN, ACIDIC, P2
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, P1 (180520), 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 P2 protein contains
115 amino acids. Northern blot analysis revealed expression of a 0.60-kb
transcript in HeLa cells.
*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