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40S ribosomal protein S3a (Small ribosomal subunit protein eS1) (v-fos transformation effector protein) (Fte-1)

 RS3A_HUMAN              Reviewed;         264 AA.
P61247; B2R4D4; D3DP05; P33443; P49241;
10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-APR-2018, entry version 152.
RecName: Full=40S ribosomal protein S3a {ECO:0000255|HAMAP-Rule:MF_03122};
AltName: Full=Small ribosomal subunit protein eS1 {ECO:0000303|PubMed:24524803};
AltName: Full=v-fos transformation effector protein;
Short=Fte-1;
Name=RPS3A {ECO:0000255|HAMAP-Rule:MF_03122}; Synonyms=FTE1, MFTL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1398113; DOI=10.1016/0378-1119(92)90289-2;
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1549582; DOI=10.1073/pnas.89.6.2200;
Kho C.J., Zarbl H.;
"Fte-1, a v-fos transformation effector gene, encodes the mammalian
homologue of a yeast gene involved in protein import into
mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 89:2200-2204(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
Bonaldo M., Soares M.B.;
Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8647443; DOI=10.1016/0378-1119(95)00708-3;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=B-cell, Eye, Muscle, Ovary, Skin, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 2-13.
TISSUE=Placenta;
PubMed=8706699; DOI=10.1111/j.1432-1033.1996.0144u.x;
Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K.,
Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.;
"Characterization of the human small-ribosomal-subunit proteins by N-
terminal and internal sequencing, and mass spectrometry.";
Eur. J. Biochem. 239:144-149(1996).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 206-262.
PubMed=9582194;
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).
[11]
GENE NOMENCLATURE.
PubMed=9074506; DOI=10.1016/S0378-1119(96)00719-6;
Lecomte F., Szpirer J., Szpirer C.;
"The S3a ribosomal protein gene is identical to the Fte-1 (v-fos
transformation effector) gene and the TNF-alpha-induced TU-11 gene,
and its transcript level is altered in transformed and tumor cells.";
Gene 186:271-277(1997).
[12]
INTERACTION WITH IPO4.
PubMed=11823430; DOI=10.1093/emboj/21.3.377;
Jaekel S., Mingot J.-M., Schwarzmaier P., Hartmann E., Goerlich D.;
"Importins fulfill a dual function as nuclear import receptors and
cytoplasmic chaperones for exposed basic domains.";
EMBO J. 21:377-386(2002).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-256, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[16]
IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
Johnsen A.H., Christiansen J., Nielsen F.C.;
"Molecular composition of IMP1 ribonucleoprotein granules.";
Mol. Cell. Proteomics 6:798-811(2007).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-34 AND LYS-249, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[26]
NOMENCLATURE.
PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
Williamson J.R., Wilson D., Yonath A., Yusupov M.;
"A new system for naming ribosomal proteins.";
Curr. Opin. Struct. Biol. 24:165-169(2014).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[28]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-249, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[30]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-34 AND LYS-249, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[31]
STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.
PubMed=23636399; DOI=10.1038/nature12104;
Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
Wilson D.N., Beckmann R.;
"Structures of the human and Drosophila 80S ribosome.";
Nature 497:80-85(2013).
-!- FUNCTION: May play a role during erythropoiesis through regulation
of transcription factor DDIT3. {ECO:0000255|HAMAP-Rule:MF_03122}.
-!- SUBUNIT: Component of the small ribosomal subunit. Mature
ribosomes consist of a small (40S) and a large (60S) subunit. The
40S subunit contains about 33 different proteins and 1 molecule of
RNA (18S). The 60S subunit contains about 49 different proteins
and 3 molecules of RNA (28S, 5.8S and 5S). Identified in a
IGF2BP1-dependent mRNP granule complex containing untranslated
mRNAs. Binds with high affinity to IPO4. Interacts with DDIT3.
{ECO:0000255|HAMAP-Rule:MF_03122, ECO:0000269|PubMed:11823430,
ECO:0000269|PubMed:17289661}.
-!- INTERACTION:
P07900:HSP90AA1; NbExp=3; IntAct=EBI-352378, EBI-296047;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03122,
ECO:0000269|PubMed:17289661}. Nucleus {ECO:0000255|HAMAP-
Rule:MF_03122}. Note=Localized in cytoplasmic mRNP granules
containing untranslated mRNAs.
-!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS1
family. {ECO:0000255|HAMAP-Rule:MF_03122}.
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EMBL; M77234; AAA60290.1; -; mRNA.
EMBL; M84711; AAA58487.1; -; mRNA.
EMBL; L13802; AAA35682.1; -; mRNA.
EMBL; X87373; CAA60827.1; -; Genomic_DNA.
EMBL; AC095055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK311788; BAG34731.1; -; mRNA.
EMBL; CH471056; EAX04991.1; -; Genomic_DNA.
EMBL; CH471056; EAX04995.1; -; Genomic_DNA.
EMBL; BC000204; AAH00204.1; -; mRNA.
EMBL; BC001708; AAH01708.1; -; mRNA.
EMBL; BC004981; AAH04981.1; -; mRNA.
EMBL; BC006298; AAH06298.1; -; mRNA.
EMBL; BC009219; AAH09219.1; -; mRNA.
EMBL; BC009404; AAH09404.1; -; mRNA.
EMBL; BC017123; AAH17123.1; -; mRNA.
EMBL; BC019072; AAH19072.1; -; mRNA.
EMBL; BC030161; AAH30161.1; -; mRNA.
EMBL; BC070211; AAH70211.1; -; mRNA.
EMBL; BC071916; AAH71916.1; -; mRNA.
EMBL; AB007148; BAA25814.1; -; Genomic_DNA.
CCDS; CCDS3775.1; -.
PIR; JC4662; JC4662.
RefSeq; NP_000997.1; NM_001006.4.
UniGene; Hs.356572; -.
PDB; 4UG0; EM; -; SB=1-264.
PDB; 4V6X; EM; 5.00 A; AB=1-264.
PDB; 5A2Q; EM; 3.90 A; B=1-264.
PDB; 5AJ0; EM; 3.50 A; BB=1-264.
PDB; 5FLX; EM; 3.90 A; B=1-264.
PDB; 5LKS; EM; 3.60 A; SB=1-264.
PDB; 5OA3; EM; 4.30 A; B=1-264.
PDB; 5T2C; EM; 3.60 A; Ap=1-264.
PDB; 5VYC; X-ray; 6.00 A; B1/B2/B3/B4/B5/B6=1-264.
PDB; 6EK0; EM; 2.90 A; SB=1-264.
PDB; 6FEC; EM; 6.30 A; i=19-233.
PDBsum; 4UG0; -.
PDBsum; 4V6X; -.
PDBsum; 5A2Q; -.
PDBsum; 5AJ0; -.
PDBsum; 5FLX; -.
PDBsum; 5LKS; -.
PDBsum; 5OA3; -.
PDBsum; 5T2C; -.
PDBsum; 5VYC; -.
PDBsum; 6EK0; -.
PDBsum; 6FEC; -.
ProteinModelPortal; P61247; -.
SMR; P61247; -.
BioGrid; 112103; 253.
CORUM; P61247; -.
DIP; DIP-29408N; -.
IntAct; P61247; 69.
MINT; P61247; -.
STRING; 9606.ENSP00000346050; -.
CarbonylDB; P61247; -.
iPTMnet; P61247; -.
PhosphoSitePlus; P61247; -.
SwissPalm; P61247; -.
BioMuta; RPS3A; -.
DMDM; 47117764; -.
SWISS-2DPAGE; P61247; -.
EPD; P61247; -.
MaxQB; P61247; -.
PaxDb; P61247; -.
PeptideAtlas; P61247; -.
PRIDE; P61247; -.
TopDownProteomics; P61247; -.
DNASU; 6189; -.
Ensembl; ENST00000274065; ENSP00000346050; ENSG00000145425.
GeneID; 6189; -.
KEGG; hsa:6189; -.
UCSC; uc003ilz.4; human.
CTD; 6189; -.
DisGeNET; 6189; -.
EuPathDB; HostDB:ENSG00000145425.9; -.
GeneCards; RPS3A; -.
HGNC; HGNC:10421; RPS3A.
HPA; HPA047100; -.
HPA; HPA053454; -.
MIM; 180478; gene.
neXtProt; NX_P61247; -.
OpenTargets; ENSG00000145425; -.
PharmGKB; PA34830; -.
eggNOG; KOG1628; Eukaryota.
eggNOG; COG1890; LUCA.
GeneTree; ENSGT00390000018433; -.
HOGENOM; HOG000105220; -.
HOVERGEN; HBG000783; -.
InParanoid; P61247; -.
KO; K02984; -.
OMA; MFEIMTR; -.
OrthoDB; EOG091G0HTU; -.
PhylomeDB; P61247; -.
TreeFam; TF300037; -.
Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-HSA-156902; Peptide chain elongation.
Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
Reactome; R-HSA-192823; Viral mRNA Translation.
Reactome; R-HSA-2408557; Selenocysteine synthesis.
Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
Reactome; R-HSA-72649; Translation initiation complex formation.
Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
Reactome; R-HSA-72764; Eukaryotic Translation Termination.
Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
ChiTaRS; RPS3A; human.
GeneWiki; RPS3A; -.
GenomeRNAi; 6189; -.
PMAP-CutDB; P61247; -.
PRO; PR:P61247; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000145425; -.
CleanEx; HS_RPS3A; -.
ExpressionAtlas; P61247; baseline and differential.
Genevisible; P61247; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; HDA:UniProtKB.
GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:CAFA.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
GO; GO:0006364; P:rRNA processing; TAS:Reactome.
GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
GO; GO:0006412; P:translation; IMP:UniProtKB.
GO; GO:0006413; P:translational initiation; TAS:UniProtKB.
GO; GO:0019083; P:viral transcription; TAS:Reactome.
HAMAP; MF_03122; Ribosomal_S3Ae_euk; 1.
InterPro; IPR027500; Ribosomal_S1/3_euk.
InterPro; IPR001593; Ribosomal_S3Ae.
InterPro; IPR018281; Ribosomal_S3Ae_CS.
Pfam; PF01015; Ribosomal_S3Ae; 1.
SMART; SM01397; Ribosomal_S3Ae; 1.
PROSITE; PS01191; RIBOSOMAL_S3AE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Differentiation; Direct protein sequencing; Isopeptide bond; Nucleus;
Phosphoprotein; Reference proteome; Ribonucleoprotein;
Ribosomal protein; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000255|HAMAP-
Rule:MF_03122,
ECO:0000269|PubMed:8706699}.
CHAIN 2 264 40S ribosomal protein S3a.
/FTId=PRO_0000153524.
MOD_RES 34 34 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 56 56 N6-acetyllysine.
{ECO:0000250|UniProtKB:P97351}.
MOD_RES 236 236 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 237 237 Phosphoserine.
{ECO:0000250|UniProtKB:P97351}.
MOD_RES 249 249 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 256 256 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 263 263 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
CROSSLNK 34 34 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 249 249 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
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


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