Full text data of RPS2
RPS2
(RPS4)
[Confidence: low (only semi-automatic identification from reviews)]
40S ribosomal protein S2 (40S ribosomal protein S4; Protein LLRep3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
40S ribosomal protein S2 (40S ribosomal protein S4; Protein LLRep3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P15880
ID RS2_HUMAN Reviewed; 293 AA.
AC P15880; B2R5G0; D3DU82; Q3MIB1;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 2.
DT 22-JAN-2014, entry version 151.
DE RecName: Full=40S ribosomal protein S2;
DE AltName: Full=40S ribosomal protein S4;
DE AltName: Full=Protein LLRep3;
GN Name=RPS2; Synonyms=RPS4;
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].
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.,
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 [3]
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 [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
RT project: 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.,
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 [6]
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
RT arginine methyltransferase 3).";
RL Biochem. J. 386:85-91(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, 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 [8]
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-263 AND LYS-275, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264 AND SER-281, AND
RP MASS 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 [11]
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 [12]
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
RT array: antagonistic citrullination and methylation of human ribosomal
RT protein S2.";
RL Mol. Biosyst. 7:2286-2295(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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 [14]
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).
CC -!- PTM: Citrullinated by PADI4 in the Arg/Gly-rich region.
CC -!- PTM: Asymmetric arginine dimethylation by PRMT3 occurs at multiple
CC sites in the Arg/Gly-rich region.
CC -!- SIMILARITY: Belongs to the ribosomal protein S5P family.
CC -!- SIMILARITY: Contains 1 S5 DRBM domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA35078.1; Type=Frameshift; Positions=14, 27, 40, 46, 48, 52;
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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 PIR; S08228; S08228.
DR RefSeq; NP_002943.2; NM_002952.3.
DR UniGene; Hs.356366; -.
DR UniGene; Hs.381079; -.
DR UniGene; Hs.498569; -.
DR UniGene; Hs.506997; -.
DR PDB; 3J3A; EM; 5.00 A; C=1-293.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; P15880; -.
DR SMR; P15880; 53-278.
DR IntAct; P15880; 31.
DR MINT; MINT-3008399; -.
DR STRING; 9606.ENSP00000341885; -.
DR PhosphoSite; P15880; -.
DR DMDM; 1710756; -.
DR PaxDb; P15880; -.
DR PRIDE; P15880; -.
DR DNASU; 6187; -.
DR Ensembl; ENST00000343262; ENSP00000341885; ENSG00000140988.
DR GeneID; 6187; -.
DR KEGG; hsa:6187; -.
DR UCSC; uc002cnn.2; human.
DR CTD; 6187; -.
DR GeneCards; GC16M002012; -.
DR H-InvDB; HIX0029256; -.
DR H-InvDB; HIX0039223; -.
DR H-InvDB; HIX0202579; -.
DR HGNC; HGNC:10404; RPS2.
DR HPA; HPA055133; -.
DR MIM; 603624; gene.
DR neXtProt; NX_P15880; -.
DR PharmGKB; PA34806; -.
DR eggNOG; COG0098; -.
DR HOGENOM; HOG000072596; -.
DR HOVERGEN; HBG000437; -.
DR InParanoid; P15880; -.
DR KO; K02981; -.
DR OMA; GIKDVWT; -.
DR OrthoDB; EOG7P5T1Q; -.
DR PhylomeDB; P15880; -.
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; RPS2; -.
DR GenomeRNAi; 6187; -.
DR NextBio; 24025; -.
DR PRO; PR:P15880; -.
DR ArrayExpress; P15880; -.
DR Bgee; P15880; -.
DR CleanEx; HS_RPS2; -.
DR Genevestigator; P15880; -.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0051347; P:positive regulation of transferase activity; IDA:UniProtKB.
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:Reactome.
DR GO; GO:0006415; P:translational termination; TAS:Reactome.
DR GO; GO:0019083; P:viral transcription; TAS:Reactome.
DR Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR014720; dsRNA-bd_dom.
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; rpsE_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; Complete proteome;
KW Direct protein sequencing; Methylation; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 293 40S ribosomal protein S2.
FT /FTId=PRO_0000131673.
FT DOMAIN 102 165 S5 DRBM.
FT COMPBIAS 22 53 Arg/Gly-rich.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 263 263 N6-acetyllysine.
FT MOD_RES 264 264 Phosphoserine.
FT MOD_RES 275 275 N6-acetyllysine.
FT MOD_RES 281 281 Phosphoserine.
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
//
ID RS2_HUMAN Reviewed; 293 AA.
AC P15880; B2R5G0; D3DU82; Q3MIB1;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 2.
DT 22-JAN-2014, entry version 151.
DE RecName: Full=40S ribosomal protein S2;
DE AltName: Full=40S ribosomal protein S4;
DE AltName: Full=Protein LLRep3;
GN Name=RPS2; Synonyms=RPS4;
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].
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.,
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 [3]
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 [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
RT project: 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.,
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 [6]
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
RT arginine methyltransferase 3).";
RL Biochem. J. 386:85-91(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, 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 [8]
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-263 AND LYS-275, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264 AND SER-281, AND
RP MASS 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 [11]
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 [12]
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
RT array: antagonistic citrullination and methylation of human ribosomal
RT protein S2.";
RL Mol. Biosyst. 7:2286-2295(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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 [14]
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).
CC -!- PTM: Citrullinated by PADI4 in the Arg/Gly-rich region.
CC -!- PTM: Asymmetric arginine dimethylation by PRMT3 occurs at multiple
CC sites in the Arg/Gly-rich region.
CC -!- SIMILARITY: Belongs to the ribosomal protein S5P family.
CC -!- SIMILARITY: Contains 1 S5 DRBM domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA35078.1; Type=Frameshift; Positions=14, 27, 40, 46, 48, 52;
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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 PIR; S08228; S08228.
DR RefSeq; NP_002943.2; NM_002952.3.
DR UniGene; Hs.356366; -.
DR UniGene; Hs.381079; -.
DR UniGene; Hs.498569; -.
DR UniGene; Hs.506997; -.
DR PDB; 3J3A; EM; 5.00 A; C=1-293.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; P15880; -.
DR SMR; P15880; 53-278.
DR IntAct; P15880; 31.
DR MINT; MINT-3008399; -.
DR STRING; 9606.ENSP00000341885; -.
DR PhosphoSite; P15880; -.
DR DMDM; 1710756; -.
DR PaxDb; P15880; -.
DR PRIDE; P15880; -.
DR DNASU; 6187; -.
DR Ensembl; ENST00000343262; ENSP00000341885; ENSG00000140988.
DR GeneID; 6187; -.
DR KEGG; hsa:6187; -.
DR UCSC; uc002cnn.2; human.
DR CTD; 6187; -.
DR GeneCards; GC16M002012; -.
DR H-InvDB; HIX0029256; -.
DR H-InvDB; HIX0039223; -.
DR H-InvDB; HIX0202579; -.
DR HGNC; HGNC:10404; RPS2.
DR HPA; HPA055133; -.
DR MIM; 603624; gene.
DR neXtProt; NX_P15880; -.
DR PharmGKB; PA34806; -.
DR eggNOG; COG0098; -.
DR HOGENOM; HOG000072596; -.
DR HOVERGEN; HBG000437; -.
DR InParanoid; P15880; -.
DR KO; K02981; -.
DR OMA; GIKDVWT; -.
DR OrthoDB; EOG7P5T1Q; -.
DR PhylomeDB; P15880; -.
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; RPS2; -.
DR GenomeRNAi; 6187; -.
DR NextBio; 24025; -.
DR PRO; PR:P15880; -.
DR ArrayExpress; P15880; -.
DR Bgee; P15880; -.
DR CleanEx; HS_RPS2; -.
DR Genevestigator; P15880; -.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0051347; P:positive regulation of transferase activity; IDA:UniProtKB.
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:Reactome.
DR GO; GO:0006415; P:translational termination; TAS:Reactome.
DR GO; GO:0019083; P:viral transcription; TAS:Reactome.
DR Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR014720; dsRNA-bd_dom.
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; rpsE_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; Complete proteome;
KW Direct protein sequencing; Methylation; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 293 40S ribosomal protein S2.
FT /FTId=PRO_0000131673.
FT DOMAIN 102 165 S5 DRBM.
FT COMPBIAS 22 53 Arg/Gly-rich.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 263 263 N6-acetyllysine.
FT MOD_RES 264 264 Phosphoserine.
FT MOD_RES 275 275 N6-acetyllysine.
FT MOD_RES 281 281 Phosphoserine.
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
//
MIM
603624
*RECORD*
*FIELD* NO
603624
*FIELD* TI
*603624 RIBOSOMAL PROTEIN S2; RPS2
*FIELD* TX
The mammalian ribosome is composed of 4 RNA species (see 180450) and
read moreapproximately 80 different proteins.
Slynn et al. (1990) isolated a human colon cDNA encoding ribosomal
protein S2 (RPS2). The deduced 293-amino acid RPS2 protein (SWISS-PROT
SWISSPROT P15880) is nearly identical to the mouse LLRep3 protein.
By somatic cell hybrid mapping analysis, Kenmochi et al. (1998) mapped
the RPS2 gene to 16p13.3 (GenBank GENBANK AB007147).
*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. Slynn, G.; Jenner, D.; Potts, W.; Elvin, P.; Morten, J. E. N.;
Markham, A. F.: Human cDNA sequence homologous to the mouse LLRep3
gene family. Nucleic Acids Res. 18: 681 only, 1990.
*FIELD* CD
Patti M. Sherman: 3/10/1999
*FIELD* ED
carol: 03/31/1999
carol: 3/31/1999
*RECORD*
*FIELD* NO
603624
*FIELD* TI
*603624 RIBOSOMAL PROTEIN S2; RPS2
*FIELD* TX
The mammalian ribosome is composed of 4 RNA species (see 180450) and
read moreapproximately 80 different proteins.
Slynn et al. (1990) isolated a human colon cDNA encoding ribosomal
protein S2 (RPS2). The deduced 293-amino acid RPS2 protein (SWISS-PROT
SWISSPROT P15880) is nearly identical to the mouse LLRep3 protein.
By somatic cell hybrid mapping analysis, Kenmochi et al. (1998) mapped
the RPS2 gene to 16p13.3 (GenBank GENBANK AB007147).
*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. Slynn, G.; Jenner, D.; Potts, W.; Elvin, P.; Morten, J. E. N.;
Markham, A. F.: Human cDNA sequence homologous to the mouse LLRep3
gene family. Nucleic Acids Res. 18: 681 only, 1990.
*FIELD* CD
Patti M. Sherman: 3/10/1999
*FIELD* ED
carol: 03/31/1999
carol: 3/31/1999