RS3A_HUMAN
ID RS3A_HUMAN Reviewed; 264 AA.
AC P61247; B2R4D4; D3DP05; P33443; P49241;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=40S ribosomal protein S3a {ECO:0000255|HAMAP-Rule:MF_03122};
DE AltName: Full=Small ribosomal subunit protein eS1 {ECO:0000303|PubMed:24524803};
DE AltName: Full=v-fos transformation effector protein;
DE Short=Fte-1;
GN Name=RPS3A {ECO:0000255|HAMAP-Rule:MF_03122}; Synonyms=FTE1, MFTL;
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=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 structure of
RT 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 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., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., 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., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., 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., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 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., 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (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 project:
RT 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., Egorov T.A.,
RA 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; DOI=10.1101/gr.8.5.509;
RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J.,
RA 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, and its
RT 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 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-256, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION BY
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, 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 [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION BY
RP 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 [20]
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 [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-34 AND LYS-249, AND
RP IDENTIFICATION BY MASS 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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 [23]
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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, 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 [25]
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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236, AND IDENTIFICATION BY
RP 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 [27]
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 [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION BY
RP 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 [29]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-249, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [30]
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 [31]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-34 AND LYS-249, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [32]
RP ADP-RIBOSYLATION AT TYR-155, AND MUTAGENESIS OF TYR-155.
RX PubMed=29954836; DOI=10.15252/embr.201745310;
RA Leslie Pedrioli D.M., Leutert M., Bilan V., Nowak K., Gunasekera K.,
RA Ferrari E., Imhof R., Malmstroem L., Hottiger M.O.;
RT "Comprehensive ADP-ribosylome analysis identifies tyrosine as an ADP-ribose
RT acceptor site.";
RL EMBO Rep. 19:0-0(2018).
RN [33]
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 of
CC transcription factor DDIT3. {ECO:0000255|HAMAP-Rule:MF_03122}.
CC -!- SUBUNIT: Component of the small ribosomal subunit. Mature ribosomes
CC consist of a small (40S) and a large (60S) subunit. The 40S subunit
CC contains about 33 different proteins and 1 molecule of RNA (18S). The
CC 60S subunit contains about 49 different proteins and 3 molecules of RNA
CC (28S, 5.8S and 5S). Identified in a IGF2BP1-dependent mRNP granule
CC complex containing untranslated mRNAs. Binds with high affinity to
CC IPO4. Interacts with DDIT3. {ECO:0000255|HAMAP-Rule:MF_03122,
CC ECO:0000269|PubMed:11823430, ECO:0000269|PubMed:17289661}.
CC -!- INTERACTION:
CC P61247; P07900: HSP90AA1; NbExp=3; IntAct=EBI-352378, EBI-296047;
CC P61247; P62263: RPS14; NbExp=2; IntAct=EBI-352378, EBI-352783;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03122,
CC ECO:0000269|PubMed:17289661}. Nucleus {ECO:0000255|HAMAP-
CC Rule:MF_03122}. Note=Localized in cytoplasmic mRNP granules containing
CC untranslated mRNAs.
CC -!- PTM: ADP-ribosylated at Tyr-155 by PARP1 in presence of HPF1.
CC {ECO:0000269|PubMed:29954836}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS1 family.
CC {ECO:0000255|HAMAP-Rule:MF_03122}.
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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 CCDS; CCDS3775.1; -.
DR PIR; JC4662; JC4662.
DR RefSeq; NP_000997.1; NM_001006.4.
DR PDB; 4UG0; EM; -; SB=1-264.
DR PDB; 4V6X; EM; 5.00 A; AB=1-264.
DR PDB; 5A2Q; EM; 3.90 A; B=1-264.
DR PDB; 5AJ0; EM; 3.50 A; BB=1-264.
DR PDB; 5FLX; EM; 3.90 A; B=1-264.
DR PDB; 5LKS; EM; 3.60 A; SB=1-264.
DR PDB; 5OA3; EM; 4.30 A; B=1-264.
DR PDB; 5T2C; EM; 3.60 A; Ap=1-264.
DR PDB; 5VYC; X-ray; 6.00 A; B1/B2/B3/B4/B5/B6=1-264.
DR PDB; 6FEC; EM; 6.30 A; i=19-233.
DR PDB; 6G18; EM; 3.60 A; B=1-264.
DR PDB; 6G4S; EM; 4.00 A; B=1-264.
DR PDB; 6G4W; EM; 4.50 A; B=1-264.
DR PDB; 6G51; EM; 4.10 A; B=1-264.
DR PDB; 6G53; EM; 4.50 A; B=1-264.
DR PDB; 6G5H; EM; 3.60 A; B=1-264.
DR PDB; 6G5I; EM; 3.50 A; B=1-264.
DR PDB; 6IP5; EM; 3.90 A; 2o=1-264.
DR PDB; 6IP6; EM; 4.50 A; 2o=1-264.
DR PDB; 6IP8; EM; 3.90 A; 2o=1-264.
DR PDB; 6OLE; EM; 3.10 A; SB=21-234.
DR PDB; 6OLF; EM; 3.90 A; SB=21-234.
DR PDB; 6OLG; EM; 3.40 A; BB=22-233.
DR PDB; 6OLI; EM; 3.50 A; SB=21-234.
DR PDB; 6OLZ; EM; 3.90 A; BB=22-233.
DR PDB; 6OM0; EM; 3.10 A; SB=21-234.
DR PDB; 6OM7; EM; 3.70 A; SB=21-234.
DR PDB; 6QZP; EM; 2.90 A; SB=21-234.
DR PDB; 6XA1; EM; 2.80 A; SB=22-232.
DR PDB; 6Y0G; EM; 3.20 A; SB=1-264.
DR PDB; 6Y2L; EM; 3.00 A; SB=1-264.
DR PDB; 6Y57; EM; 3.50 A; SB=1-264.
DR PDB; 6YBD; EM; 3.30 A; O=1-264.
DR PDB; 6YBW; EM; 3.10 A; O=1-264.
DR PDB; 6Z6L; EM; 3.00 A; SB=1-264.
DR PDB; 6Z6M; EM; 3.10 A; SB=1-264.
DR PDB; 6Z6N; EM; 2.90 A; SB=1-264.
DR PDB; 6ZLW; EM; 2.60 A; C=1-264.
DR PDB; 6ZM7; EM; 2.70 A; SB=1-264.
DR PDB; 6ZME; EM; 3.00 A; SB=1-264.
DR PDB; 6ZMI; EM; 2.60 A; SB=1-264.
DR PDB; 6ZMO; EM; 3.10 A; SB=1-264.
DR PDB; 6ZMT; EM; 3.00 A; C=1-264.
DR PDB; 6ZMW; EM; 3.70 A; O=1-264.
DR PDB; 6ZN5; EM; 3.20 A; C=21-233.
DR PDB; 6ZOJ; EM; 2.80 A; B=1-264.
DR PDB; 6ZOK; EM; 2.80 A; B=1-264.
DR PDB; 6ZON; EM; 3.00 A; p=1-264.
DR PDB; 6ZP4; EM; 2.90 A; p=1-264.
DR PDB; 6ZUO; EM; 3.10 A; B=1-264.
DR PDB; 6ZV6; EM; 2.90 A; B=1-264.
DR PDB; 6ZVH; EM; 2.90 A; B=1-264.
DR PDB; 6ZVJ; EM; 3.80 A; p=23-233.
DR PDB; 6ZXD; EM; 3.20 A; B=1-264.
DR PDB; 6ZXE; EM; 3.00 A; B=1-264.
DR PDB; 6ZXF; EM; 3.70 A; B=1-264.
DR PDB; 6ZXG; EM; 2.60 A; B=1-264.
DR PDB; 6ZXH; EM; 2.70 A; B=1-264.
DR PDB; 7A09; EM; 3.50 A; p=1-264.
DR PDB; 7K5I; EM; 2.90 A; B=1-264.
DR PDB; 7MQ8; EM; 3.60 A; NM=1-264.
DR PDB; 7MQ9; EM; 3.87 A; NM=1-264.
DR PDB; 7MQA; EM; 2.70 A; NM=1-264.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5A2Q; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 5FLX; -.
DR PDBsum; 5LKS; -.
DR PDBsum; 5OA3; -.
DR PDBsum; 5T2C; -.
DR PDBsum; 5VYC; -.
DR PDBsum; 6FEC; -.
DR PDBsum; 6G18; -.
DR PDBsum; 6G4S; -.
DR PDBsum; 6G4W; -.
DR PDBsum; 6G51; -.
DR PDBsum; 6G53; -.
DR PDBsum; 6G5H; -.
DR PDBsum; 6G5I; -.
DR PDBsum; 6IP5; -.
DR PDBsum; 6IP6; -.
DR PDBsum; 6IP8; -.
DR PDBsum; 6OLE; -.
DR PDBsum; 6OLF; -.
DR PDBsum; 6OLG; -.
DR PDBsum; 6OLI; -.
DR PDBsum; 6OLZ; -.
DR PDBsum; 6OM0; -.
DR PDBsum; 6OM7; -.
DR PDBsum; 6QZP; -.
DR PDBsum; 6XA1; -.
DR PDBsum; 6Y0G; -.
DR PDBsum; 6Y2L; -.
DR PDBsum; 6Y57; -.
DR PDBsum; 6YBD; -.
DR PDBsum; 6YBW; -.
DR PDBsum; 6Z6L; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR PDBsum; 6ZLW; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 6ZMT; -.
DR PDBsum; 6ZMW; -.
DR PDBsum; 6ZN5; -.
DR PDBsum; 6ZOJ; -.
DR PDBsum; 6ZOK; -.
DR PDBsum; 6ZON; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 6ZUO; -.
DR PDBsum; 6ZV6; -.
DR PDBsum; 6ZVH; -.
DR PDBsum; 6ZVJ; -.
DR PDBsum; 6ZXD; -.
DR PDBsum; 6ZXE; -.
DR PDBsum; 6ZXF; -.
DR PDBsum; 6ZXG; -.
DR PDBsum; 6ZXH; -.
DR PDBsum; 7A09; -.
DR PDBsum; 7K5I; -.
DR PDBsum; 7MQ8; -.
DR PDBsum; 7MQ9; -.
DR PDBsum; 7MQA; -.
DR AlphaFoldDB; P61247; -.
DR SMR; P61247; -.
DR BioGRID; 112103; 481.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P61247; -.
DR DIP; DIP-29408N; -.
DR IntAct; P61247; 138.
DR MINT; P61247; -.
DR STRING; 9606.ENSP00000346050; -.
DR CarbonylDB; P61247; -.
DR GlyGen; P61247; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P61247; -.
DR MetOSite; P61247; -.
DR PhosphoSitePlus; P61247; -.
DR SwissPalm; P61247; -.
DR BioMuta; RPS3A; -.
DR DMDM; 47117764; -.
DR SWISS-2DPAGE; P61247; -.
DR EPD; P61247; -.
DR jPOST; P61247; -.
DR MassIVE; P61247; -.
DR MaxQB; P61247; -.
DR PaxDb; P61247; -.
DR PeptideAtlas; P61247; -.
DR PRIDE; P61247; -.
DR ProteomicsDB; 57286; -.
DR TopDownProteomics; P61247; -.
DR Antibodypedia; 27718; 196 antibodies from 30 providers.
DR DNASU; 6189; -.
DR Ensembl; ENST00000274065.9; ENSP00000346050.3; ENSG00000145425.10.
DR GeneID; 6189; -.
DR KEGG; hsa:6189; -.
DR MANE-Select; ENST00000274065.9; ENSP00000346050.3; NM_001006.5; NP_000997.1.
DR UCSC; uc003ilz.4; human.
DR CTD; 6189; -.
DR DisGeNET; 6189; -.
DR GeneCards; RPS3A; -.
DR HGNC; HGNC:10421; RPS3A.
DR HPA; ENSG00000145425; Low tissue specificity.
DR MIM; 180478; gene.
DR neXtProt; NX_P61247; -.
DR OpenTargets; ENSG00000145425; -.
DR PharmGKB; PA34830; -.
DR VEuPathDB; HostDB:ENSG00000145425; -.
DR eggNOG; KOG1628; Eukaryota.
DR GeneTree; ENSGT00390000018433; -.
DR HOGENOM; CLU_062507_0_1_1; -.
DR InParanoid; P61247; -.
DR OMA; GQNAYTK; -.
DR OrthoDB; 1207239at2759; -.
DR PhylomeDB; P61247; -.
DR TreeFam; TF300037; -.
DR PathwayCommons; P61247; -.
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-72649; Translation initiation complex formation.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
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-9754678; SARS-CoV-2 modulates host translation machinery.
DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P61247; -.
DR SIGNOR; P61247; -.
DR BioGRID-ORCS; 6189; 432 hits in 665 CRISPR screens.
DR ChiTaRS; RPS3A; human.
DR GeneWiki; RPS3A; -.
DR GenomeRNAi; 6189; -.
DR Pharos; P61247; Tbio.
DR PRO; PR:P61247; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P61247; protein.
DR Bgee; ENSG00000145425; Expressed in cortical plate and 97 other tissues.
DR ExpressionAtlas; P61247; baseline and differential.
DR Genevisible; P61247; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:CAFA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0002181; P:cytoplasmic translation; IC:FlyBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0006412; P:translation; IMP:UniProtKB.
DR GO; GO:0006413; P:translational initiation; TAS:UniProtKB.
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 SMART; SM01397; Ribosomal_S3Ae; 1.
DR PROSITE; PS01191; RIBOSOMAL_S3AE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ADP-ribosylation; Cytoplasm; Differentiation;
KW Direct protein sequencing; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03122,
FT ECO:0000269|PubMed:8706699"
FT CHAIN 2..264
FT /note="40S ribosomal protein S3a"
FT /id="PRO_0000153524"
FT REGION 232..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 56
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P97351"
FT MOD_RES 155
FT /note="ADP-ribosyltyrosine"
FT /evidence="ECO:0000269|PubMed:29954836"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97351"
FT MOD_RES 249
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 256
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT CROSSLNK 34
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT MUTAGEN 155
FT /note="Y->F: Decreased ADP-ribosylation."
FT /evidence="ECO:0000269|PubMed:29954836"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 27..34
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 58..62
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 80..91
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 93..105
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:6ZV6"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:6ZV6"
FT STRAND 134..143
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 158..177
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 181..188
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 192..201
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:6ZV6"
FT STRAND 211..219
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 225..232
FT /evidence="ECO:0007829|PDB:6ZLW"
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
