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Database: UniProt
Entry: P05387
LinkDB: P05387
Original site: P05387 
ID   RLA2_HUMAN              Reviewed;         115 AA.
AC   P05387; Q6FG96;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   07-OCT-2020, entry version 220.
DE   RecName: Full=60S acidic ribosomal protein P2;
DE   AltName: Full=Large ribosomal subunit protein P2 {ECO:0000303|PubMed:24524803};
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; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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 [MRNA].
RC   TISSUE=Mammary carcinoma;
RX   PubMed=2153399; DOI=10.1038/bjc.1990.19;
RA   Sharp M.G.F., Adams S.M., Elvin P., Walker R.A., Brammar W.J., Varley J.M.;
RT   "A sequence previously identified as metastasis-related encodes an acidic
RT   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 analysis of
RT   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., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., 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., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   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., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., 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., 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   [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 project:
RT   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-cell
RT   carcinoma.";
RL   Int. J. Cancer 83:456-464(1999).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Lymphoblast;
RX   PubMed=14654843; DOI=10.1038/nature02166;
RA   Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT   "Proteomic characterization of the human centrosome by protein correlation
RT   profiling.";
RL   Nature 426:570-574(2003).
RN   [12]
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   [13]
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., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-79 AND SER-86, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [17]
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., 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   [18]
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   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-79, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [20]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   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   [21]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT SER-17 AND SER-79, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
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., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [22]
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   [23]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [24]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-19 AND SER-86, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [25]
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   [26]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79 AND SER-86, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [27]
RP   IDENTIFICATION BY MASS SPECTROMETRY [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   [28]
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 stalk.";
RL   Nucleic Acids Res. 38:5206-5216(2010).
RN   [29]
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 RPLP1 at the lateral ribosomal stalk of the
CC       large ribosomal subunit. {ECO:0000269|PubMed:20385603}.
CC   -!- INTERACTION:
CC       P05387; P05386: RPLP1; NbExp=2; IntAct=EBI-352813, EBI-354582;
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.
CC       {ECO:0000305}.
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   CCDS; CCDS7717.1; -.
DR   PIR; C27125; R6HUP2.
DR   RefSeq; NP_000995.1; NM_001004.3.
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; 4BEH; NMR; -; B=1-115.
DR   PDB; 4V6X; EM; 5.00 A; Cu/Cv=1-115.
DR   PDB; 5DDZ; X-ray; 1.50 A; B=106-115.
DR   PDB; 5GU4; X-ray; 1.55 A; C/D=107-115.
DR   PDBsum; 1S4J; -.
DR   PDBsum; 2JDL; -.
DR   PDBsum; 2LBF; -.
DR   PDBsum; 2W1O; -.
DR   PDBsum; 4BEH; -.
DR   PDBsum; 4V6X; -.
DR   PDBsum; 5DDZ; -.
DR   PDBsum; 5GU4; -.
DR   BMRB; P05387; -.
DR   SMR; P05387; -.
DR   BioGRID; 112096; 201.
DR   ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR   CORUM; P05387; -.
DR   IntAct; P05387; 71.
DR   MINT; P05387; -.
DR   STRING; 9606.ENSP00000322419; -.
DR   ChEMBL; CHEMBL4295698; -.
DR   Allergome; 1276; Hom s P2.
DR   GlyGen; P05387; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P05387; -.
DR   PhosphoSitePlus; P05387; -.
DR   SwissPalm; P05387; -.
DR   BioMuta; RPLP2; -.
DR   SWISS-2DPAGE; P05387; -.
DR   EPD; P05387; -.
DR   jPOST; P05387; -.
DR   MassIVE; P05387; -.
DR   PaxDb; P05387; -.
DR   PeptideAtlas; P05387; -.
DR   PRIDE; P05387; -.
DR   ProteomicsDB; 51832; -.
DR   TopDownProteomics; P05387; -.
DR   Antibodypedia; 22683; 194 antibodies.
DR   DNASU; 6181; -.
DR   Ensembl; ENST00000321153; ENSP00000322419; ENSG00000177600.
DR   Ensembl; ENST00000530797; ENSP00000431240; ENSG00000177600.
DR   GeneID; 6181; -.
DR   KEGG; hsa:6181; -.
DR   UCSC; uc001lrq.2; human.
DR   CTD; 6181; -.
DR   DisGeNET; 6181; -.
DR   EuPathDB; HostDB:ENSG00000177600.8; -.
DR   GeneCards; RPLP2; -.
DR   HGNC; HGNC:10377; RPLP2.
DR   HPA; ENSG00000177600; Low tissue specificity.
DR   MIM; 180530; gene.
DR   neXtProt; NX_P05387; -.
DR   OpenTargets; ENSG00000177600; -.
DR   PharmGKB; PA34776; -.
DR   eggNOG; KOG3449; Eukaryota.
DR   GeneTree; ENSGT00550000074828; -.
DR   HOGENOM; CLU_114656_0_2_1; -.
DR   InParanoid; P05387; -.
DR   KO; K02943; -.
DR   OMA; SLNGKCY; -.
DR   OrthoDB; 1626327at2759; -.
DR   PhylomeDB; P05387; -.
DR   TreeFam; TF320650; -.
DR   PathwayCommons; P05387; -.
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   SIGNOR; P05387; -.
DR   BioGRID-ORCS; 6181; 740 hits in 873 CRISPR screens.
DR   ChiTaRS; RPLP2; human.
DR   EvolutionaryTrace; P05387; -.
DR   GeneWiki; RPLP2; -.
DR   GenomeRNAi; 6181; -.
DR   Pharos; P05387; Tbio.
DR   PRO; PR:P05387; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; P05387; protein.
DR   Bgee; ENSG00000177600; Expressed in adipose tissue of abdominal region and 251 other tissues.
DR   ExpressionAtlas; P05387; baseline and differential.
DR   Genevisible; P05387; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:GO_Central.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA: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; DP00793; -.
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; Direct protein sequencing; Phosphoprotein;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT   CHAIN           1..115
FT                   /note="60S acidic ribosomal protein P2"
FT                   /id="PRO_0000157640"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000244|PubMed:20068231"
FT   MOD_RES         17
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:16964243,
FT                   ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:19690332,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         19
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         21
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000244|PubMed:19608861"
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:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:18691976, ECO:0000244|PubMed:19690332,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:24275569"
FT   MOD_RES         86
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569"
FT   MOD_RES         102
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:14997482"
FT   MOD_RES         105
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P99027"
FT   STRAND          1..3
FT                   /evidence="ECO:0000244|PDB:4BEH"
FT   HELIX           4..13
FT                   /evidence="ECO:0000244|PDB:2LBF"
FT   HELIX           20..28
FT                   /evidence="ECO:0000244|PDB:2LBF"
FT   TURN            29..31
FT                   /evidence="ECO:0000244|PDB:2LBF"
FT   HELIX           38..46
FT                   /evidence="ECO:0000244|PDB:2LBF"
FT   HELIX           51..55
FT                   /evidence="ECO:0000244|PDB:2LBF"
FT   STRAND          59..61
FT                   /evidence="ECO:0000244|PDB:2LBF"
FT   STRAND          63..66
FT                   /evidence="ECO:0000244|PDB:4BEH"
FT   TURN            91..94
FT                   /evidence="ECO:0000244|PDB:4BEH"
FT   HELIX           112..114
FT                   /evidence="ECO:0000244|PDB:5DDZ"
SQ   SEQUENCE   115 AA;  11665 MW;  B5ECFE2510A756BF CRC64;
     MRYVASYLLA ALGGNSSPSA KDIKKILDSV GIEADDDRLN KVISELNGKN IEDVIAQGIG
     KLASVPAGGA VAVSAAPGSA APAAGSAPAA AEEKKDEKKE ESEESDDDMG FGLFD
//
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