Full text data of RPS3A
RPS3A
(FTE1, MFTL)
[Confidence: low (only semi-automatic identification from reviews)]
40S ribosomal protein S3a (v-fos transformation effector protein; Fte-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
40S ribosomal protein S3a (v-fos transformation effector protein; Fte-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P61247
ID RS3A_HUMAN Reviewed; 264 AA.
AC P61247; B2R4D4; D3DP05; P33443; P49241;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=40S ribosomal protein S3a;
DE AltName: Full=v-fos transformation effector protein;
DE Short=Fte-1;
GN Name=RPS3A; Synonyms=FTE1, MFTL;
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=1398113; DOI=10.1016/0378-1119(92)90289-2;
RA Metspalu A., Rebane A., Hoth S., Pooga M., Stahl J., Kruppa J.;
RT "Human ribosomal protein S3a: cloning of the cDNA and primary
RT structure of the protein.";
RL Gene 119:313-316(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1549582; DOI=10.1073/pnas.89.6.2200;
RA Kho C.J., Zarbl H.;
RT "Fte-1, a v-fos transformation effector gene, encodes the mammalian
RT homologue of a yeast gene involved in protein import into
RT mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:2200-2204(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Bonaldo M., Soares M.B.;
RL Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8647443; DOI=10.1016/0378-1119(95)00708-3;
RA Nolte D., Taimor G., Kalff-Suske M., Seifart K.H.;
RT "The human S3a ribosomal protein: sequence, location and cell-free
RT transcription of the functional gene.";
RL Gene 169:179-185(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell, Eye, Muscle, Ovary, Skin, and Uterus;
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 2-13.
RC TISSUE=Placenta;
RX PubMed=8706699; DOI=10.1111/j.1432-1033.1996.0144u.x;
RA Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K.,
RA Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.;
RT "Characterization of the human small-ribosomal-subunit proteins by N-
RT terminal and internal sequencing, and mass spectrometry.";
RL Eur. J. Biochem. 239:144-149(1996).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 206-262.
RX PubMed=9582194;
RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N.,
RA Hudson T.J., Tanaka T., Page D.C.;
RT "A map of 75 human ribosomal protein genes.";
RL Genome Res. 8:509-523(1998).
RN [11]
RP GENE NOMENCLATURE.
RX PubMed=9074506; DOI=10.1016/S0378-1119(96)00719-6;
RA Lecomte F., Szpirer J., Szpirer C.;
RT "The S3a ribosomal protein gene is identical to the Fte-1 (v-fos
RT transformation effector) gene and the TNF-alpha-induced TU-11 gene,
RT and its transcript level is altered in transformed and tumor cells.";
RL Gene 186:271-277(1997).
RN [12]
RP INTERACTION WITH IPO4.
RX PubMed=11823430; DOI=10.1093/emboj/21.3.377;
RA Jaekel S., Mingot J.-M., Schwarzmaier P., Hartmann E., Goerlich D.;
RT "Importins fulfill a dual function as nuclear import receptors and
RT cytoplasmic chaperones for exposed basic domains.";
RL EMBO J. 21:377-386(2002).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-256, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND MASS
RP SPECTROMETRY.
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, 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 [16]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND MASS
RP 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 [19]
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 [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-34 AND LYS-249, AND MASS
RP 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND MASS
RP 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 [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.,
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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, 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 [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [25]
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: May play a role during erythropoiesis through regulation
CC of transcription factor DDIT3 (By similarity).
CC -!- SUBUNIT: Component of the small ribosomal subunit. Mature
CC ribosomes consist of a small (40S) and a large (60S) subunit. The
CC 40S subunit contains about 33 different proteins and 1 molecule of
CC RNA (18S). The 60S subunit contains about 49 different proteins
CC and 3 molecules of RNA (28S, 5.8S and 5S). Identified in a
CC IGF2BP1-dependent mRNP granule complex containing untranslated
CC mRNAs. Binds with high affinity to IPO4. Interacts with DDIT3.
CC -!- INTERACTION:
CC P07900:HSP90AA1; NbExp=2; IntAct=EBI-352378, EBI-296047;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus (By similarity).
CC Note=Localized in cytoplasmic mRNP granules containing
CC untranslated mRNAs.
CC -!- SIMILARITY: Belongs to the ribosomal protein S3Ae family.
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DR EMBL; M77234; AAA60290.1; -; mRNA.
DR EMBL; M84711; AAA58487.1; -; mRNA.
DR EMBL; L13802; AAA35682.1; -; mRNA.
DR EMBL; X87373; CAA60827.1; -; Genomic_DNA.
DR EMBL; AC095055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK311788; BAG34731.1; -; mRNA.
DR EMBL; CH471056; EAX04991.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04995.1; -; Genomic_DNA.
DR EMBL; BC000204; AAH00204.1; -; mRNA.
DR EMBL; BC001708; AAH01708.1; -; mRNA.
DR EMBL; BC004981; AAH04981.1; -; mRNA.
DR EMBL; BC006298; AAH06298.1; -; mRNA.
DR EMBL; BC009219; AAH09219.1; -; mRNA.
DR EMBL; BC009404; AAH09404.1; -; mRNA.
DR EMBL; BC017123; AAH17123.1; -; mRNA.
DR EMBL; BC019072; AAH19072.1; -; mRNA.
DR EMBL; BC030161; AAH30161.1; -; mRNA.
DR EMBL; BC070211; AAH70211.1; -; mRNA.
DR EMBL; BC071916; AAH71916.1; -; mRNA.
DR EMBL; AB007148; BAA25814.1; -; Genomic_DNA.
DR PIR; JC4662; JC4662.
DR RefSeq; NP_000997.1; NM_001006.4.
DR UniGene; Hs.356572; -.
DR PDB; 3J3A; EM; 5.00 A; B=1-264.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; P61247; -.
DR SMR; P61247; 19-233.
DR DIP; DIP-29408N; -.
DR IntAct; P61247; 27.
DR MINT; MINT-1160853; -.
DR STRING; 9606.ENSP00000346050; -.
DR PhosphoSite; P61247; -.
DR DMDM; 47117764; -.
DR SWISS-2DPAGE; P61247; -.
DR PaxDb; P61247; -.
DR PRIDE; P61247; -.
DR DNASU; 6189; -.
DR Ensembl; ENST00000274065; ENSP00000346050; ENSG00000145425.
DR GeneID; 6189; -.
DR KEGG; hsa:6189; -.
DR UCSC; uc003ilz.4; human.
DR CTD; 6189; -.
DR GeneCards; GC04P152020; -.
DR HGNC; HGNC:10421; RPS3A.
DR HPA; HPA047100; -.
DR MIM; 180478; gene.
DR neXtProt; NX_P61247; -.
DR PharmGKB; PA34830; -.
DR eggNOG; COG1890; -.
DR HOGENOM; HOG000105220; -.
DR HOVERGEN; HBG000783; -.
DR InParanoid; P61247; -.
DR KO; K02984; -.
DR OMA; GQNAYTK; -.
DR OrthoDB; EOG7Q5HDW; -.
DR PhylomeDB; P61247; -.
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 GeneWiki; RPS3A; -.
DR GenomeRNAi; 6189; -.
DR NextBio; 24033; -.
DR PMAP-CutDB; P61247; -.
DR PRO; PR:P61247; -.
DR ArrayExpress; P61247; -.
DR Bgee; P61247; -.
DR CleanEx; HS_RPS3A; -.
DR Genevestigator; P61247; -.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; NAS:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:RefGenome.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:RefGenome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP: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:UniProtKB.
DR GO; GO:0006415; P:translational termination; TAS:Reactome.
DR GO; GO:0019083; P:viral transcription; TAS:Reactome.
DR HAMAP; MF_03122; Ribosomal_S3Ae_euk; 1; -.
DR InterPro; IPR027500; Ribosomal_S1/3_euk.
DR InterPro; IPR001593; Ribosomal_S3Ae.
DR InterPro; IPR018281; Ribosomal_S3Ae_CS.
DR Pfam; PF01015; Ribosomal_S3Ae; 1.
DR PROSITE; PS01191; RIBOSOMAL_S3AE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Differentiation; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 264 40S ribosomal protein S3a.
FT /FTId=PRO_0000153524.
FT MOD_RES 34 34 N6-acetyllysine.
FT MOD_RES 249 249 N6-acetyllysine.
FT MOD_RES 256 256 Phosphotyrosine.
FT MOD_RES 263 263 Phosphoserine.
SQ SEQUENCE 264 AA; 29945 MW; 000037AE195F7A9D CRC64;
MAVGKNKRLT KGGKKGAKKK VVDPFSKKDW YDVKAPAMFN IRNIGKTLVT RTQGTKIASD
GLKGRVFEVS LADLQNDEVA FRKFKLITED VQGKNCLTNF HGMDLTRDKM CSMVKKWQTM
IEAHVDVKTT DGYLLRLFCV GFTKKRNNQI RKTSYAQHQQ VRQIRKKMME IMTREVQTND
LKEVVNKLIP DSIGKDIEKA CQSIYPLHDV FVRKVKMLKK PKFELGKLME LHGEGSSSGK
ATGDETGAKV ERADGYEPPV QESV
//
ID RS3A_HUMAN Reviewed; 264 AA.
AC P61247; B2R4D4; D3DP05; P33443; P49241;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=40S ribosomal protein S3a;
DE AltName: Full=v-fos transformation effector protein;
DE Short=Fte-1;
GN Name=RPS3A; Synonyms=FTE1, MFTL;
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=1398113; DOI=10.1016/0378-1119(92)90289-2;
RA Metspalu A., Rebane A., Hoth S., Pooga M., Stahl J., Kruppa J.;
RT "Human ribosomal protein S3a: cloning of the cDNA and primary
RT structure of the protein.";
RL Gene 119:313-316(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1549582; DOI=10.1073/pnas.89.6.2200;
RA Kho C.J., Zarbl H.;
RT "Fte-1, a v-fos transformation effector gene, encodes the mammalian
RT homologue of a yeast gene involved in protein import into
RT mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:2200-2204(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Bonaldo M., Soares M.B.;
RL Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8647443; DOI=10.1016/0378-1119(95)00708-3;
RA Nolte D., Taimor G., Kalff-Suske M., Seifart K.H.;
RT "The human S3a ribosomal protein: sequence, location and cell-free
RT transcription of the functional gene.";
RL Gene 169:179-185(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell, Eye, Muscle, Ovary, Skin, and Uterus;
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 2-13.
RC TISSUE=Placenta;
RX PubMed=8706699; DOI=10.1111/j.1432-1033.1996.0144u.x;
RA Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K.,
RA Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.;
RT "Characterization of the human small-ribosomal-subunit proteins by N-
RT terminal and internal sequencing, and mass spectrometry.";
RL Eur. J. Biochem. 239:144-149(1996).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 206-262.
RX PubMed=9582194;
RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N.,
RA Hudson T.J., Tanaka T., Page D.C.;
RT "A map of 75 human ribosomal protein genes.";
RL Genome Res. 8:509-523(1998).
RN [11]
RP GENE NOMENCLATURE.
RX PubMed=9074506; DOI=10.1016/S0378-1119(96)00719-6;
RA Lecomte F., Szpirer J., Szpirer C.;
RT "The S3a ribosomal protein gene is identical to the Fte-1 (v-fos
RT transformation effector) gene and the TNF-alpha-induced TU-11 gene,
RT and its transcript level is altered in transformed and tumor cells.";
RL Gene 186:271-277(1997).
RN [12]
RP INTERACTION WITH IPO4.
RX PubMed=11823430; DOI=10.1093/emboj/21.3.377;
RA Jaekel S., Mingot J.-M., Schwarzmaier P., Hartmann E., Goerlich D.;
RT "Importins fulfill a dual function as nuclear import receptors and
RT cytoplasmic chaperones for exposed basic domains.";
RL EMBO J. 21:377-386(2002).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-256, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND MASS
RP SPECTROMETRY.
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, 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 [16]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND MASS
RP 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 [19]
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 [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-34 AND LYS-249, AND MASS
RP 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND MASS
RP 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 [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.,
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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, 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 [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [25]
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: May play a role during erythropoiesis through regulation
CC of transcription factor DDIT3 (By similarity).
CC -!- SUBUNIT: Component of the small ribosomal subunit. Mature
CC ribosomes consist of a small (40S) and a large (60S) subunit. The
CC 40S subunit contains about 33 different proteins and 1 molecule of
CC RNA (18S). The 60S subunit contains about 49 different proteins
CC and 3 molecules of RNA (28S, 5.8S and 5S). Identified in a
CC IGF2BP1-dependent mRNP granule complex containing untranslated
CC mRNAs. Binds with high affinity to IPO4. Interacts with DDIT3.
CC -!- INTERACTION:
CC P07900:HSP90AA1; NbExp=2; IntAct=EBI-352378, EBI-296047;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus (By similarity).
CC Note=Localized in cytoplasmic mRNP granules containing
CC untranslated mRNAs.
CC -!- SIMILARITY: Belongs to the ribosomal protein S3Ae family.
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DR EMBL; M77234; AAA60290.1; -; mRNA.
DR EMBL; M84711; AAA58487.1; -; mRNA.
DR EMBL; L13802; AAA35682.1; -; mRNA.
DR EMBL; X87373; CAA60827.1; -; Genomic_DNA.
DR EMBL; AC095055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK311788; BAG34731.1; -; mRNA.
DR EMBL; CH471056; EAX04991.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04995.1; -; Genomic_DNA.
DR EMBL; BC000204; AAH00204.1; -; mRNA.
DR EMBL; BC001708; AAH01708.1; -; mRNA.
DR EMBL; BC004981; AAH04981.1; -; mRNA.
DR EMBL; BC006298; AAH06298.1; -; mRNA.
DR EMBL; BC009219; AAH09219.1; -; mRNA.
DR EMBL; BC009404; AAH09404.1; -; mRNA.
DR EMBL; BC017123; AAH17123.1; -; mRNA.
DR EMBL; BC019072; AAH19072.1; -; mRNA.
DR EMBL; BC030161; AAH30161.1; -; mRNA.
DR EMBL; BC070211; AAH70211.1; -; mRNA.
DR EMBL; BC071916; AAH71916.1; -; mRNA.
DR EMBL; AB007148; BAA25814.1; -; Genomic_DNA.
DR PIR; JC4662; JC4662.
DR RefSeq; NP_000997.1; NM_001006.4.
DR UniGene; Hs.356572; -.
DR PDB; 3J3A; EM; 5.00 A; B=1-264.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; P61247; -.
DR SMR; P61247; 19-233.
DR DIP; DIP-29408N; -.
DR IntAct; P61247; 27.
DR MINT; MINT-1160853; -.
DR STRING; 9606.ENSP00000346050; -.
DR PhosphoSite; P61247; -.
DR DMDM; 47117764; -.
DR SWISS-2DPAGE; P61247; -.
DR PaxDb; P61247; -.
DR PRIDE; P61247; -.
DR DNASU; 6189; -.
DR Ensembl; ENST00000274065; ENSP00000346050; ENSG00000145425.
DR GeneID; 6189; -.
DR KEGG; hsa:6189; -.
DR UCSC; uc003ilz.4; human.
DR CTD; 6189; -.
DR GeneCards; GC04P152020; -.
DR HGNC; HGNC:10421; RPS3A.
DR HPA; HPA047100; -.
DR MIM; 180478; gene.
DR neXtProt; NX_P61247; -.
DR PharmGKB; PA34830; -.
DR eggNOG; COG1890; -.
DR HOGENOM; HOG000105220; -.
DR HOVERGEN; HBG000783; -.
DR InParanoid; P61247; -.
DR KO; K02984; -.
DR OMA; GQNAYTK; -.
DR OrthoDB; EOG7Q5HDW; -.
DR PhylomeDB; P61247; -.
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 GeneWiki; RPS3A; -.
DR GenomeRNAi; 6189; -.
DR NextBio; 24033; -.
DR PMAP-CutDB; P61247; -.
DR PRO; PR:P61247; -.
DR ArrayExpress; P61247; -.
DR Bgee; P61247; -.
DR CleanEx; HS_RPS3A; -.
DR Genevestigator; P61247; -.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; NAS:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:RefGenome.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:RefGenome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP: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:UniProtKB.
DR GO; GO:0006415; P:translational termination; TAS:Reactome.
DR GO; GO:0019083; P:viral transcription; TAS:Reactome.
DR HAMAP; MF_03122; Ribosomal_S3Ae_euk; 1; -.
DR InterPro; IPR027500; Ribosomal_S1/3_euk.
DR InterPro; IPR001593; Ribosomal_S3Ae.
DR InterPro; IPR018281; Ribosomal_S3Ae_CS.
DR Pfam; PF01015; Ribosomal_S3Ae; 1.
DR PROSITE; PS01191; RIBOSOMAL_S3AE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Differentiation; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 264 40S ribosomal protein S3a.
FT /FTId=PRO_0000153524.
FT MOD_RES 34 34 N6-acetyllysine.
FT MOD_RES 249 249 N6-acetyllysine.
FT MOD_RES 256 256 Phosphotyrosine.
FT MOD_RES 263 263 Phosphoserine.
SQ SEQUENCE 264 AA; 29945 MW; 000037AE195F7A9D CRC64;
MAVGKNKRLT KGGKKGAKKK VVDPFSKKDW YDVKAPAMFN IRNIGKTLVT RTQGTKIASD
GLKGRVFEVS LADLQNDEVA FRKFKLITED VQGKNCLTNF HGMDLTRDKM CSMVKKWQTM
IEAHVDVKTT DGYLLRLFCV GFTKKRNNQI RKTSYAQHQQ VRQIRKKMME IMTREVQTND
LKEVVNKLIP DSIGKDIEKA CQSIYPLHDV FVRKVKMLKK PKFELGKLME LHGEGSSSGK
ATGDETGAKV ERADGYEPPV QESV
//
MIM
180478
*RECORD*
*FIELD* NO
180478
*FIELD* TI
*180478 RIBOSOMAL PROTEIN S3a; RPS3A
*FIELD* TX
Meyuhas and Perry (1980) pioneered the cloning of mammalian ribosomal
read moreproteins. Metspalu et al. (1992) cloned the cDNA corresponding to
ribosomal protein S3a, one of the approximately 85 different ribosomal
proteins constituting the human ribosome. The amino acid sequence of
RPS3a was deduced partially from the nucleotide sequence of cDNA and
confirmed by direct amino acid sequencing. The RPS3a protein has 263
amino acids.
Nolte et al. (1996) found that the coding region of the RPS3A gene spans
5,013 bp and consists of 6 exons. They noted that the cDNA sequence
reported by Metspalu et al. (1992) lacks the 5-prime untranslated region
as well as the 6 bp encoding the first 2 amino acids. Southern blot
analysis indicated that there are at least 6 processed RPS3A pseudogenes
in the human genome. Rebane et al. (1998) reported that the mouse and
human RPS3A genes share an identical exon/intron structure. The
predicted proteins differ in only 2 positions.
Kho et al. (1996) showed that monoallelic disruption of the rat S3a, or
fte1 (v-fos (164810) transformation effector), gene in v-fos-transformed
fibroblasts resulted in loss of the transformed phenotype and in a
decreased rate of protein synthesis. They concluded that the
accumulation of ribosomal subunits and the rate of protein synthesis are
important modulators of neoplastic transformation and cell growth.
Some small nucleolar RNA (snoRNA) genes are located within the introns
of protein-encoding genes. There is a preference for ribosome-related
genes as parent genes for the snoRNAs, perhaps to coordinate the
production of protein and RNA components of the ribosome. Rebane et al.
(1998) reported that introns 3 and 4 of human and mouse RPS3A encode a
novel snoRNA designated U73 (603568). Although both variants of U73 are
expressed in mouse, only the variant specified by intron 4 is expressed
in human cell lines.
By analysis of somatic cell hybrids, Nolte et al. (1996) mapped the
RPS3A gene to chromosome 4. Kenmochi et al. (1998) mapped the RPS3A gene
to 4q by use of somatic cell hybrid and radiation hybrid mapping panels.
By fluorescence in situ hybridization, Rebane et al. (1998) refined the
map position to 4q31.2-q31.3.
*FIELD* RF
1. Kenmochi, N.; Kawaguchi, T.; Rozen, S.; Davis, E.; Goodman, N.;
Hudson, T. J.; Tanaka, T.; Page, D. C.: A map of 75 human ribosomal
protein genes. Genome Res. 8: 509-523, 1998.
2. Kho, C. J.; Wang, Y.; Zarbl, H.: Effect of decreased fte-1 gene
expression on protein synthesis, cell growth, and transformation. Cell
Growth Differ. 7: 1157-1166, 1996.
3. Metspalu, A.; Rebane, A.; Hoth, S.; Pooga, M.; Stahl, J.; Kruppa,
J.: Human ribosomal protein S3a: cloning of the cDNA and primary
structure of the protein. Gene 119: 313-316, 1992.
4. Meyuhas, O.; Perry, R. P.: Construction and identification of
cDNA clones for mouse ribosomal proteins: application for the study
of r-protein gene expression. Gene 10: 113-129, 1980.
5. Nolte, D.; Taimor, G.; Kalff-Suske, M.; Seifart, K. H.: The human
S3a ribosomal protein: sequence, location and cell-free transcription
of the functional gene. Gene 169: 179-185, 1996.
6. Rebane, A.; Tamme, R.; Laan, M.; Pata, I.; Metspalu, A.: A novel
snoRNA (U73) is encoded within the introns of the human and mouse
ribosomal protein S3a genes. Gene 210: 255-263, 1998.
*FIELD* CN
Patti M. Sherman - updated: 3/11/1999
Rebekah S. Rasooly - updated: 2/22/1999
*FIELD* CD
Victor A. McKusick: 1/26/1994
*FIELD* ED
carol: 03/18/1999
alopez: 2/22/1999
carol: 1/26/1994
*RECORD*
*FIELD* NO
180478
*FIELD* TI
*180478 RIBOSOMAL PROTEIN S3a; RPS3A
*FIELD* TX
Meyuhas and Perry (1980) pioneered the cloning of mammalian ribosomal
read moreproteins. Metspalu et al. (1992) cloned the cDNA corresponding to
ribosomal protein S3a, one of the approximately 85 different ribosomal
proteins constituting the human ribosome. The amino acid sequence of
RPS3a was deduced partially from the nucleotide sequence of cDNA and
confirmed by direct amino acid sequencing. The RPS3a protein has 263
amino acids.
Nolte et al. (1996) found that the coding region of the RPS3A gene spans
5,013 bp and consists of 6 exons. They noted that the cDNA sequence
reported by Metspalu et al. (1992) lacks the 5-prime untranslated region
as well as the 6 bp encoding the first 2 amino acids. Southern blot
analysis indicated that there are at least 6 processed RPS3A pseudogenes
in the human genome. Rebane et al. (1998) reported that the mouse and
human RPS3A genes share an identical exon/intron structure. The
predicted proteins differ in only 2 positions.
Kho et al. (1996) showed that monoallelic disruption of the rat S3a, or
fte1 (v-fos (164810) transformation effector), gene in v-fos-transformed
fibroblasts resulted in loss of the transformed phenotype and in a
decreased rate of protein synthesis. They concluded that the
accumulation of ribosomal subunits and the rate of protein synthesis are
important modulators of neoplastic transformation and cell growth.
Some small nucleolar RNA (snoRNA) genes are located within the introns
of protein-encoding genes. There is a preference for ribosome-related
genes as parent genes for the snoRNAs, perhaps to coordinate the
production of protein and RNA components of the ribosome. Rebane et al.
(1998) reported that introns 3 and 4 of human and mouse RPS3A encode a
novel snoRNA designated U73 (603568). Although both variants of U73 are
expressed in mouse, only the variant specified by intron 4 is expressed
in human cell lines.
By analysis of somatic cell hybrids, Nolte et al. (1996) mapped the
RPS3A gene to chromosome 4. Kenmochi et al. (1998) mapped the RPS3A gene
to 4q by use of somatic cell hybrid and radiation hybrid mapping panels.
By fluorescence in situ hybridization, Rebane et al. (1998) refined the
map position to 4q31.2-q31.3.
*FIELD* RF
1. Kenmochi, N.; Kawaguchi, T.; Rozen, S.; Davis, E.; Goodman, N.;
Hudson, T. J.; Tanaka, T.; Page, D. C.: A map of 75 human ribosomal
protein genes. Genome Res. 8: 509-523, 1998.
2. Kho, C. J.; Wang, Y.; Zarbl, H.: Effect of decreased fte-1 gene
expression on protein synthesis, cell growth, and transformation. Cell
Growth Differ. 7: 1157-1166, 1996.
3. Metspalu, A.; Rebane, A.; Hoth, S.; Pooga, M.; Stahl, J.; Kruppa,
J.: Human ribosomal protein S3a: cloning of the cDNA and primary
structure of the protein. Gene 119: 313-316, 1992.
4. Meyuhas, O.; Perry, R. P.: Construction and identification of
cDNA clones for mouse ribosomal proteins: application for the study
of r-protein gene expression. Gene 10: 113-129, 1980.
5. Nolte, D.; Taimor, G.; Kalff-Suske, M.; Seifart, K. H.: The human
S3a ribosomal protein: sequence, location and cell-free transcription
of the functional gene. Gene 169: 179-185, 1996.
6. Rebane, A.; Tamme, R.; Laan, M.; Pata, I.; Metspalu, A.: A novel
snoRNA (U73) is encoded within the introns of the human and mouse
ribosomal protein S3a genes. Gene 210: 255-263, 1998.
*FIELD* CN
Patti M. Sherman - updated: 3/11/1999
Rebekah S. Rasooly - updated: 2/22/1999
*FIELD* CD
Victor A. McKusick: 1/26/1994
*FIELD* ED
carol: 03/18/1999
alopez: 2/22/1999
carol: 1/26/1994