RS2_HUMAN
ID RS2_HUMAN Reviewed; 293 AA.
AC P15880; B2R5G0; D3DU82; Q3MIB1;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=40S ribosomal protein S2;
DE AltName: Full=40S ribosomal protein S4;
DE AltName: Full=Protein LLRep3;
DE AltName: Full=Small ribosomal subunit protein uS5 {ECO:0000303|PubMed:24524803};
GN Name=RPS2; Synonyms=RPS4;
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].
RC TISSUE=Colon;
RX PubMed=2308862; DOI=10.1093/nar/18.3.681;
RA Slynn G., Jenner D., Potts W., Elvin P., Morten J.E.N., Markham A.F.;
RT "Human cDNA sequence homologous to the mouse LLRep3 gene family.";
RL Nucleic Acids Res. 18:681-681(1990).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Cervix, Colon, Eye, Kidney, Lung, Mammary gland, Muscle,
RC Placenta, Skin, Testis, 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 [5]
RP PROTEIN SEQUENCE OF 276-291.
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 [6]
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 [7]
RP METHYLATION BY PRMT3.
RX PubMed=15473865; DOI=10.1042/bj20041466;
RA Swiercz R., Person M.D., Bedford M.T.;
RT "Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine
RT methyltransferase 3).";
RL Biochem. J. 386:85-91(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-263 AND LYS-275, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264 AND SER-281, AND
RP IDENTIFICATION BY 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 [12]
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 [13]
RP CITRULLINATION.
RX PubMed=21584310; DOI=10.1039/c1mb05089c;
RA Guo Q., Bedford M.T., Fast W.;
RT "Discovery of peptidylarginine deiminase-4 substrates by protein array:
RT antagonistic citrullination and methylation of human ribosomal protein
RT S2.";
RL Mol. Biosyst. 7:2286-2295(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-252; SER-264 AND THR-270, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
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 [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-275, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [19]
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 [20]
RP UBIQUITINATION AT LYS-58 AND LYS-275, AND MUTAGENESIS OF LYS-58 AND
RP LYS-275.
RX PubMed=28132843; DOI=10.1016/j.molcel.2016.12.026;
RA Sundaramoorthy E., Leonard M., Mak R., Liao J., Fulzele A., Bennett E.J.;
RT "ZNF598 and RACK1 regulate mammalian ribosome-associated quality control
RT function by mediating regulatory 40S ribosomal ubiquitylation.";
RL Mol. Cell 65:751-760(2017).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-275, AND IDENTIFICATION BY MASS
RP 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 [22]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
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).
RN [23]
RP INTERACTION WITH ZNF277.
RX PubMed=30530495; DOI=10.1074/jbc.ra118.004928;
RA Dionne K.L., Bergeron D., Landry-Voyer A.M., Bachand F.;
RT "The 40S ribosomal protein uS5 (RPS2) assembles into an extraribosomal
RT complex with human ZNF277 that competes with the PRMT3-uS5 interaction.";
RL J. Biol. Chem. 294:1944-1955(2019).
CC -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell. The small
CC ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC molecules. The large subunit (LSU) contains the ribosomal catalytic
CC site termed the peptidyl transferase center (PTC), which catalyzes the
CC formation of peptide bonds, thereby polymerizing the amino acids
CC delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC leave the ribosome through a tunnel in the LSU and interact with
CC protein factors that function in enzymatic processing, targeting, and
CC the membrane insertion of nascent chains at the exit of the ribosomal
CC tunnel. Plays a role in the assembly and function of the 40S ribosomal
CC subunit. Mutations in this protein affects the control of translational
CC fidelity. Involved in nucleolar processing of pre-18S ribosomal RNA and
CC ribosome assembly. {ECO:0000250|UniProtKB:P25443}.
CC -!- SUBUNIT: Interacts with zinc finger protein ZNF277 (via zinc-finger
CC domains); the interaction is direct; the interaction is extra-ribosomal
CC (PubMed:30530495). Interacts with arginine methyltransferase PRMT3
CC (PubMed:30530495). Interaction with ZNF277 competes with the binding of
CC RPS2 to protein arginine methyltransferase PRMT3 (PubMed:30530495).
CC {ECO:0000269|PubMed:30530495}.
CC -!- INTERACTION:
CC P15880; Q5S007: LRRK2; NbExp=4; IntAct=EBI-443446, EBI-5323863;
CC P15880; Q9H0A0: NAT10; NbExp=2; IntAct=EBI-443446, EBI-876527;
CC P15880; O60678: PRMT3; NbExp=5; IntAct=EBI-443446, EBI-2809009;
CC -!- PTM: Citrullinated by PADI4 in the Arg/Gly-rich region.
CC {ECO:0000269|PubMed:21584310}.
CC -!- PTM: Asymmetric arginine dimethylation by PRMT3 occurs at multiple
CC sites in the Arg/Gly-rich region.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA35078.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X17206; CAA35078.1; ALT_FRAME; mRNA.
DR EMBL; AK312173; BAG35107.1; -; mRNA.
DR EMBL; CH471112; EAW85592.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85595.1; -; Genomic_DNA.
DR EMBL; BC001795; AAH01795.1; -; mRNA.
DR EMBL; BC006559; AAH06559.1; -; mRNA.
DR EMBL; BC008862; AAH08862.1; -; mRNA.
DR EMBL; BC010165; AAH10165.1; -; mRNA.
DR EMBL; BC012354; AAH12354.1; -; mRNA.
DR EMBL; BC016178; AAH16178.1; -; mRNA.
DR EMBL; BC016951; AAH16951.1; -; mRNA.
DR EMBL; BC018993; AAH18993.1; -; mRNA.
DR EMBL; BC021545; AAH21545.1; -; mRNA.
DR EMBL; BC023541; AAH23541.1; -; mRNA.
DR EMBL; BC025677; AAH25677.1; -; mRNA.
DR EMBL; BC066321; AAH66321.1; -; mRNA.
DR EMBL; BC068051; AAH68051.1; -; mRNA.
DR EMBL; BC071922; AAH71922.1; -; mRNA.
DR EMBL; BC071923; AAH71923.1; -; mRNA.
DR EMBL; BC071924; AAH71924.1; -; mRNA.
DR EMBL; BC073966; AAH73966.1; -; mRNA.
DR EMBL; BC075830; AAH75830.1; -; mRNA.
DR EMBL; BC103756; AAI03757.1; -; mRNA.
DR EMBL; BC105985; AAI05986.1; -; mRNA.
DR CCDS; CCDS10452.1; -.
DR PIR; S08228; S08228.
DR RefSeq; NP_002943.2; NM_002952.3.
DR PDB; 4UG0; EM; -; SC=1-293.
DR PDB; 4V6X; EM; 5.00 A; AC=1-293.
DR PDB; 5A2Q; EM; 3.90 A; C=1-293.
DR PDB; 5AJ0; EM; 3.50 A; BC=1-293.
DR PDB; 5FLX; EM; 3.90 A; C=1-293.
DR PDB; 5LKS; EM; 3.60 A; SC=1-293.
DR PDB; 5OA3; EM; 4.30 A; C=1-293.
DR PDB; 5T2C; EM; 3.60 A; AJ=1-293.
DR PDB; 5VYC; X-ray; 6.00 A; C1/C2/C3/C4/C5/C6=1-293.
DR PDB; 6G18; EM; 3.60 A; C=1-293.
DR PDB; 6G4S; EM; 4.00 A; C=1-293.
DR PDB; 6G51; EM; 4.10 A; C=1-293.
DR PDB; 6G53; EM; 4.50 A; C=1-293.
DR PDB; 6G5H; EM; 3.60 A; C=1-293.
DR PDB; 6G5I; EM; 3.50 A; C=1-293.
DR PDB; 6IP5; EM; 3.90 A; 3G=1-293.
DR PDB; 6IP6; EM; 4.50 A; 3G=1-293.
DR PDB; 6IP8; EM; 3.90 A; 3G=1-293.
DR PDB; 6OLE; EM; 3.10 A; SC=59-278.
DR PDB; 6OLF; EM; 3.90 A; SC=59-278.
DR PDB; 6OLG; EM; 3.40 A; BC=57-278.
DR PDB; 6OLI; EM; 3.50 A; SC=59-278.
DR PDB; 6OLZ; EM; 3.90 A; BC=57-278.
DR PDB; 6OM0; EM; 3.10 A; SC=59-278.
DR PDB; 6OM7; EM; 3.70 A; SC=59-278.
DR PDB; 6QZP; EM; 2.90 A; SC=59-280.
DR PDB; 6XA1; EM; 2.80 A; SC=59-278.
DR PDB; 6Y0G; EM; 3.20 A; SC=1-293.
DR PDB; 6Y2L; EM; 3.00 A; SC=1-293.
DR PDB; 6Y57; EM; 3.50 A; SC=1-293.
DR PDB; 6YBD; EM; 3.30 A; L=1-293.
DR PDB; 6YBW; EM; 3.10 A; L=1-293.
DR PDB; 6Z6L; EM; 3.00 A; SC=1-293.
DR PDB; 6Z6M; EM; 3.10 A; SC=1-293.
DR PDB; 6Z6N; EM; 2.90 A; SC=1-293.
DR PDB; 6ZLW; EM; 2.60 A; D=1-293.
DR PDB; 6ZM7; EM; 2.70 A; SC=1-293.
DR PDB; 6ZME; EM; 3.00 A; SC=1-293.
DR PDB; 6ZMI; EM; 2.60 A; SC=1-293.
DR PDB; 6ZMO; EM; 3.10 A; SC=1-293.
DR PDB; 6ZMT; EM; 3.00 A; D=1-293.
DR PDB; 6ZMW; EM; 3.70 A; L=1-293.
DR PDB; 6ZN5; EM; 3.20 A; D=59-276.
DR PDB; 6ZOJ; EM; 2.80 A; C=1-293.
DR PDB; 6ZOK; EM; 2.80 A; C=1-293.
DR PDB; 6ZON; EM; 3.00 A; d=1-293.
DR PDB; 6ZP4; EM; 2.90 A; d=1-293.
DR PDB; 6ZUO; EM; 3.10 A; C=1-293.
DR PDB; 6ZV6; EM; 2.90 A; C=1-293.
DR PDB; 6ZVH; EM; 2.90 A; C=59-280.
DR PDB; 6ZVJ; EM; 3.80 A; d=60-275.
DR PDB; 6ZXD; EM; 3.20 A; C=1-293.
DR PDB; 6ZXE; EM; 3.00 A; C=1-293.
DR PDB; 6ZXF; EM; 3.70 A; C=1-293.
DR PDB; 6ZXG; EM; 2.60 A; C=1-293.
DR PDB; 6ZXH; EM; 2.70 A; C=1-293.
DR PDB; 7A09; EM; 3.50 A; d=1-293.
DR PDB; 7JQB; EM; 2.70 A; D=1-293.
DR PDB; 7JQC; EM; 3.30 A; D=1-293.
DR PDB; 7K5I; EM; 2.90 A; C=1-293.
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; 6G18; -.
DR PDBsum; 6G4S; -.
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; 7JQB; -.
DR PDBsum; 7JQC; -.
DR PDBsum; 7K5I; -.
DR AlphaFoldDB; P15880; -.
DR SMR; P15880; -.
DR BioGRID; 112101; 557.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P15880; -.
DR IntAct; P15880; 159.
DR MINT; P15880; -.
DR STRING; 9606.ENSP00000341885; -.
DR DrugBank; DB09130; Copper.
DR GlyGen; P15880; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P15880; -.
DR MetOSite; P15880; -.
DR PhosphoSitePlus; P15880; -.
DR SwissPalm; P15880; -.
DR BioMuta; RPS2; -.
DR DMDM; 1710756; -.
DR EPD; P15880; -.
DR jPOST; P15880; -.
DR MassIVE; P15880; -.
DR MaxQB; P15880; -.
DR PaxDb; P15880; -.
DR PeptideAtlas; P15880; -.
DR PRIDE; P15880; -.
DR ProteomicsDB; 53233; -.
DR Antibodypedia; 23349; 209 antibodies from 30 providers.
DR DNASU; 6187; -.
DR Ensembl; ENST00000343262.9; ENSP00000341885.4; ENSG00000140988.16.
DR GeneID; 6187; -.
DR KEGG; hsa:6187; -.
DR MANE-Select; ENST00000343262.9; ENSP00000341885.4; NM_002952.4; NP_002943.2.
DR UCSC; uc002cno.3; human.
DR CTD; 6187; -.
DR DisGeNET; 6187; -.
DR GeneCards; RPS2; -.
DR HGNC; HGNC:10404; RPS2.
DR HPA; ENSG00000140988; Low tissue specificity.
DR MIM; 603624; gene.
DR neXtProt; NX_P15880; -.
DR OpenTargets; ENSG00000140988; -.
DR PharmGKB; PA34806; -.
DR VEuPathDB; HostDB:ENSG00000140988; -.
DR eggNOG; KOG0877; Eukaryota.
DR GeneTree; ENSGT00940000153095; -.
DR InParanoid; P15880; -.
DR OMA; DLKNWVP; -.
DR OrthoDB; 1197354at2759; -.
DR PhylomeDB; P15880; -.
DR TreeFam; TF300806; -.
DR PathwayCommons; P15880; -.
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-3214858; RMTs methylate histone arginines.
DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
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-8876725; Protein methylation.
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; P15880; -.
DR SIGNOR; P15880; -.
DR BioGRID-ORCS; 6187; 722 hits in 1085 CRISPR screens.
DR ChiTaRS; RPS2; human.
DR GeneWiki; RPS2; -.
DR GenomeRNAi; 6187; -.
DR Pharos; P15880; Tbio.
DR PRO; PR:P15880; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P15880; protein.
DR Bgee; ENSG00000140988; Expressed in stromal cell of endometrium and 95 other tissues.
DR ExpressionAtlas; P15880; baseline and differential.
DR Genevisible; P15880; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0017134; F:fibroblast growth factor binding; IPI:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; IC:FlyBase.
DR GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR000851; Ribosomal_S5.
DR InterPro; IPR005324; Ribosomal_S5_C.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005711; Ribosomal_S5_euk/arc.
DR InterPro; IPR013810; Ribosomal_S5_N.
DR InterPro; IPR018192; Ribosomal_S5_N_CS.
DR PANTHER; PTHR13718; PTHR13718; 1.
DR Pfam; PF00333; Ribosomal_S5; 1.
DR Pfam; PF03719; Ribosomal_S5_C; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR01020; uS5_euk_arch; 1.
DR PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR PROSITE; PS50881; S5_DSRBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Citrullination; Direct protein sequencing;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Repeat;
KW Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..293
FT /note="40S ribosomal protein S2"
FT /id="PRO_0000131673"
FT DOMAIN 102..165
FT /note="S5 DRBM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00268"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 252
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 263
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 270
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 275
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 58
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:28132843"
FT CROSSLNK 275
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 275
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 275
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:28132843"
FT MUTAGEN 58
FT /note="K->R: Does not affect readthrough on the poly(A)-
FT stall sequences; when associated with R-275."
FT /evidence="ECO:0000269|PubMed:28132843"
FT MUTAGEN 275
FT /note="K->R: Does not affect readthrough on the poly(A)-
FT stall sequences; when associated with R-58."
FT /evidence="ECO:0000269|PubMed:28132843"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:6ZXE"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 92..97
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 103..115
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 117..132
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 136..146
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 147..160
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:6ZOJ"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 208..216
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 222..228
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 233..245
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 246..249
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:7JQB"
SQ SEQUENCE 293 AA; 31324 MW; 66C0DB7ED393B036 CRC64;
MADDAGAAGG PGGPGGPGMG NRGGFRGGFG SGIRGRGRGR GRGRGRGRGA RGGKAEDKEW
MPVTKLGRLV KDMKIKSLEE IYLFSLPIKE SEIIDFFLGA SLKDEVLKIM PVQKQTRAGQ
RTRFKAFVAI GDYNGHVGLG VKCSKEVATA IRGAIILAKL SIVPVRRGYW GNKIGKPHTV
PCKVTGRCGS VLVRLIPAPR GTGIVSAPVP KKLLMMAGID DCYTSARGCT ATLGNFAKAT
FDAISKTYSY LTPDLWKETV FTKSPYQEFT DHLVKTHTRV SVQRTQAPAV ATT
