Full text data of RPS13
RPS13
[Confidence: low (only semi-automatic identification from reviews)]
40S ribosomal protein S13
Note: presumably soluble (membrane word is not in UniProt keywords or features)
40S ribosomal protein S13
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P62277
ID RS13_HUMAN Reviewed; 151 AA.
AC P62277; B2R549; P19116; Q02546; Q29200; Q498Y0;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=40S ribosomal protein S13;
GN Name=RPS13;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8332508; DOI=10.1093/nar/21.12.2945;
RA Chadeneau C., Lemoullac B., Denis M.G.;
RT "Cloning and analysis of the human S13 ribosomal protein cDNA.";
RL Nucleic Acids Res. 21:2945-2945(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RA Filipenko M.L.;
RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8920921; DOI=10.1006/bbrc.1996.1668;
RA Kenmochi N., Higa S., Yoshihama M., Tanaka T.;
RT "U14 snoRNAs are encoded in introns of human ribosomal protein S13
RT gene.";
RL Biochem. Biophys. Res. Commun. 228:371-374(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone, Brain, Muscle, Pancreas, and Placenta;
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 [7]
RP PROTEIN SEQUENCE OF 2-8, AND CLEAVAGE OF INITIATOR METHIONINE.
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-127.
RA Bhat K.S.;
RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-38, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [10]
RP IDENTIFICATION BY 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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-27, AND MASS 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 [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.,
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 [13]
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 -!- INTERACTION:
CC Q53EL6:PDCD4; NbExp=2; IntAct=EBI-351850, EBI-935824;
CC -!- SIMILARITY: Belongs to the ribosomal protein S15P family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L01124; AAA60283.1; -; mRNA.
DR EMBL; X79239; CAA55821.1; -; mRNA.
DR EMBL; D88010; BAA13528.1; -; Genomic_DNA.
DR EMBL; AK312060; BAG34996.1; -; mRNA.
DR EMBL; CH471064; EAW68448.1; -; Genomic_DNA.
DR EMBL; BC000475; AAH00475.1; -; mRNA.
DR EMBL; BC006772; AAH06772.1; -; mRNA.
DR EMBL; BC029732; AAH29732.1; -; mRNA.
DR EMBL; BC066322; AAH66322.1; -; mRNA.
DR EMBL; BC100032; AAI00033.1; -; mRNA.
DR EMBL; L05090; AAC15854.1; -; mRNA.
DR PIR; S34109; S34109.
DR RefSeq; NP_001008.1; NM_001017.2.
DR UniGene; Hs.446588; -.
DR PDB; 3J3A; EM; 5.00 A; N=1-151.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; P62277; -.
DR SMR; P62277; 2-151.
DR IntAct; P62277; 21.
DR MINT; MINT-4999984; -.
DR STRING; 9606.ENSP00000228140; -.
DR PhosphoSite; P62277; -.
DR DMDM; 50403608; -.
DR PaxDb; P62277; -.
DR PeptideAtlas; P62277; -.
DR PRIDE; P62277; -.
DR DNASU; 6207; -.
DR Ensembl; ENST00000525634; ENSP00000435777; ENSG00000110700.
DR GeneID; 6207; -.
DR KEGG; hsa:6207; -.
DR UCSC; uc001mmp.3; human.
DR CTD; 6207; -.
DR GeneCards; GC11M017055; -.
DR HGNC; HGNC:10386; RPS13.
DR HPA; HPA005985; -.
DR MIM; 180476; gene.
DR neXtProt; NX_P62277; -.
DR PharmGKB; PA34785; -.
DR eggNOG; COG0184; -.
DR HOGENOM; HOG000180723; -.
DR HOVERGEN; HBG000938; -.
DR InParanoid; P62277; -.
DR KO; K02953; -.
DR OMA; NWKYESA; -.
DR PhylomeDB; P62277; -.
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 ChiTaRS; RPS13; human.
DR GeneWiki; RPS13; -.
DR GenomeRNAi; 6207; -.
DR NextBio; 24107; -.
DR PRO; PR:P62277; -.
DR ArrayExpress; P62277; -.
DR Bgee; P62277; -.
DR CleanEx; HS_RPS13; -.
DR Genevestigator; P62277; -.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0033119; P:negative regulation of RNA splicing; IDA:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006414; P:translational elongation; TAS:Reactome.
DR GO; GO:0006413; P:translational initiation; TAS:Reactome.
DR GO; GO:0006415; P:translational termination; TAS:Reactome.
DR GO; GO:0019083; P:viral transcription; TAS:Reactome.
DR HAMAP; MF_01343_A; Ribosomal_S15_A; 1; -.
DR InterPro; IPR012606; Ribosomal_S13/S15_N.
DR InterPro; IPR000589; Ribosomal_S15.
DR InterPro; IPR023029; Ribosomal_S15P.
DR InterPro; IPR009068; S15_NS1_RNA-bd.
DR Pfam; PF08069; Ribosomal_S13_N; 1.
DR Pfam; PF00312; Ribosomal_S15; 1.
DR SUPFAM; SSF47060; SSF47060; 1.
DR PROSITE; PS00362; RIBOSOMAL_S15; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 151 40S ribosomal protein S13.
FT /FTId=PRO_0000115661.
FT MOD_RES 27 27 N6-acetyllysine.
FT MOD_RES 38 38 Phosphotyrosine.
FT CONFLICT 82 82 P -> S (in Ref. 8; AAC15854).
SQ SEQUENCE 151 AA; 17222 MW; 23F94D38F87B8D53 CRC64;
MGRMHAPGKG LSQSALPYRR SVPTWLKLTS DDVKEQIYKL AKKGLTPSQI GVILRDSHGV
AQVRFVTGNK ILRILKSKGL APDLPEDLYH LIKKAVAVRK HLERNRKDKD AKFRLILIES
RIHRLARYYK TKRVLPPNWK YESSTASALV A
//
ID RS13_HUMAN Reviewed; 151 AA.
AC P62277; B2R549; P19116; Q02546; Q29200; Q498Y0;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=40S ribosomal protein S13;
GN Name=RPS13;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8332508; DOI=10.1093/nar/21.12.2945;
RA Chadeneau C., Lemoullac B., Denis M.G.;
RT "Cloning and analysis of the human S13 ribosomal protein cDNA.";
RL Nucleic Acids Res. 21:2945-2945(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RA Filipenko M.L.;
RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8920921; DOI=10.1006/bbrc.1996.1668;
RA Kenmochi N., Higa S., Yoshihama M., Tanaka T.;
RT "U14 snoRNAs are encoded in introns of human ribosomal protein S13
RT gene.";
RL Biochem. Biophys. Res. Commun. 228:371-374(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone, Brain, Muscle, Pancreas, and Placenta;
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 [7]
RP PROTEIN SEQUENCE OF 2-8, AND CLEAVAGE OF INITIATOR METHIONINE.
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-127.
RA Bhat K.S.;
RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-38, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [10]
RP IDENTIFICATION BY 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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-27, AND MASS 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 [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.,
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 [13]
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 -!- INTERACTION:
CC Q53EL6:PDCD4; NbExp=2; IntAct=EBI-351850, EBI-935824;
CC -!- SIMILARITY: Belongs to the ribosomal protein S15P family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L01124; AAA60283.1; -; mRNA.
DR EMBL; X79239; CAA55821.1; -; mRNA.
DR EMBL; D88010; BAA13528.1; -; Genomic_DNA.
DR EMBL; AK312060; BAG34996.1; -; mRNA.
DR EMBL; CH471064; EAW68448.1; -; Genomic_DNA.
DR EMBL; BC000475; AAH00475.1; -; mRNA.
DR EMBL; BC006772; AAH06772.1; -; mRNA.
DR EMBL; BC029732; AAH29732.1; -; mRNA.
DR EMBL; BC066322; AAH66322.1; -; mRNA.
DR EMBL; BC100032; AAI00033.1; -; mRNA.
DR EMBL; L05090; AAC15854.1; -; mRNA.
DR PIR; S34109; S34109.
DR RefSeq; NP_001008.1; NM_001017.2.
DR UniGene; Hs.446588; -.
DR PDB; 3J3A; EM; 5.00 A; N=1-151.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; P62277; -.
DR SMR; P62277; 2-151.
DR IntAct; P62277; 21.
DR MINT; MINT-4999984; -.
DR STRING; 9606.ENSP00000228140; -.
DR PhosphoSite; P62277; -.
DR DMDM; 50403608; -.
DR PaxDb; P62277; -.
DR PeptideAtlas; P62277; -.
DR PRIDE; P62277; -.
DR DNASU; 6207; -.
DR Ensembl; ENST00000525634; ENSP00000435777; ENSG00000110700.
DR GeneID; 6207; -.
DR KEGG; hsa:6207; -.
DR UCSC; uc001mmp.3; human.
DR CTD; 6207; -.
DR GeneCards; GC11M017055; -.
DR HGNC; HGNC:10386; RPS13.
DR HPA; HPA005985; -.
DR MIM; 180476; gene.
DR neXtProt; NX_P62277; -.
DR PharmGKB; PA34785; -.
DR eggNOG; COG0184; -.
DR HOGENOM; HOG000180723; -.
DR HOVERGEN; HBG000938; -.
DR InParanoid; P62277; -.
DR KO; K02953; -.
DR OMA; NWKYESA; -.
DR PhylomeDB; P62277; -.
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 ChiTaRS; RPS13; human.
DR GeneWiki; RPS13; -.
DR GenomeRNAi; 6207; -.
DR NextBio; 24107; -.
DR PRO; PR:P62277; -.
DR ArrayExpress; P62277; -.
DR Bgee; P62277; -.
DR CleanEx; HS_RPS13; -.
DR Genevestigator; P62277; -.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0033119; P:negative regulation of RNA splicing; IDA:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006414; P:translational elongation; TAS:Reactome.
DR GO; GO:0006413; P:translational initiation; TAS:Reactome.
DR GO; GO:0006415; P:translational termination; TAS:Reactome.
DR GO; GO:0019083; P:viral transcription; TAS:Reactome.
DR HAMAP; MF_01343_A; Ribosomal_S15_A; 1; -.
DR InterPro; IPR012606; Ribosomal_S13/S15_N.
DR InterPro; IPR000589; Ribosomal_S15.
DR InterPro; IPR023029; Ribosomal_S15P.
DR InterPro; IPR009068; S15_NS1_RNA-bd.
DR Pfam; PF08069; Ribosomal_S13_N; 1.
DR Pfam; PF00312; Ribosomal_S15; 1.
DR SUPFAM; SSF47060; SSF47060; 1.
DR PROSITE; PS00362; RIBOSOMAL_S15; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 151 40S ribosomal protein S13.
FT /FTId=PRO_0000115661.
FT MOD_RES 27 27 N6-acetyllysine.
FT MOD_RES 38 38 Phosphotyrosine.
FT CONFLICT 82 82 P -> S (in Ref. 8; AAC15854).
SQ SEQUENCE 151 AA; 17222 MW; 23F94D38F87B8D53 CRC64;
MGRMHAPGKG LSQSALPYRR SVPTWLKLTS DDVKEQIYKL AKKGLTPSQI GVILRDSHGV
AQVRFVTGNK ILRILKSKGL APDLPEDLYH LIKKAVAVRK HLERNRKDKD AKFRLILIES
RIHRLARYYK TKRVLPPNWK YESSTASALV A
//
MIM
180476
*RECORD*
*FIELD* NO
180476
*FIELD* TI
*180476 RIBOSOMAL PROTEIN S13; RPS13
*FIELD* TX
DESCRIPTION
The mammalian ribosome is a macromolecular assembly of 4 RNA species
read more(see 180450) and approximately 80 different proteins, including RPS13.
CLONING
Chadeneau et al. (1993) cloned a cDNA encoding human RPS13. The deduced
151-amino acid RPS13 protein is identical to rat Rps13.
GENE STRUCTURE
By sequence analysis, Caldwell et al. (2001) determined that the RPS13
gene contains 6 exons and spans approximately 2.7 kb.
MAPPING
By somatic cell hybrid and radiation hybrid mapping analyses, Kenmochi
et al. (1998) mapped the human RPS13 gene to 11p. By sequence analysis,
Caldwell et al. (2001) localized the gene to 11p15.1-p14.
*FIELD* RF
1. Caldwell, G. M.; Eddy, R. L.; Day, C. D.; Haley, L. H.; Cooper,
P. R.; Sait, S. S. J.; Hejtmancik, F.; Smith, R. J. H.; Morton, C.
C.; Higgins, M. J.; Shows, T. B.: Mapping of genes and transcribed
sequences in a gene rich 400-kb region on human chromosome 11p15.1-p14. Cytogenet.
Cell Genet. 92: 103-107, 2001.
2. Chadeneau, C.; LeMoullac, B.; Denis, M. G.: Cloning and analysis
of the human S13 ribosomal protein cDNA. Nucleic Acids Res. 21:
2945 only, 1993.
3. 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.
*FIELD* CN
Carol A. Bocchini - updated: 8/7/2003
Patti M. Sherman - updated: 3/24/1999
*FIELD* CD
Victor A. McKusick: 9/17/1993
*FIELD* ED
tkritzer: 08/08/2003
carol: 8/7/2003
carol: 3/31/1999
carol: 9/17/1993
*RECORD*
*FIELD* NO
180476
*FIELD* TI
*180476 RIBOSOMAL PROTEIN S13; RPS13
*FIELD* TX
DESCRIPTION
The mammalian ribosome is a macromolecular assembly of 4 RNA species
read more(see 180450) and approximately 80 different proteins, including RPS13.
CLONING
Chadeneau et al. (1993) cloned a cDNA encoding human RPS13. The deduced
151-amino acid RPS13 protein is identical to rat Rps13.
GENE STRUCTURE
By sequence analysis, Caldwell et al. (2001) determined that the RPS13
gene contains 6 exons and spans approximately 2.7 kb.
MAPPING
By somatic cell hybrid and radiation hybrid mapping analyses, Kenmochi
et al. (1998) mapped the human RPS13 gene to 11p. By sequence analysis,
Caldwell et al. (2001) localized the gene to 11p15.1-p14.
*FIELD* RF
1. Caldwell, G. M.; Eddy, R. L.; Day, C. D.; Haley, L. H.; Cooper,
P. R.; Sait, S. S. J.; Hejtmancik, F.; Smith, R. J. H.; Morton, C.
C.; Higgins, M. J.; Shows, T. B.: Mapping of genes and transcribed
sequences in a gene rich 400-kb region on human chromosome 11p15.1-p14. Cytogenet.
Cell Genet. 92: 103-107, 2001.
2. Chadeneau, C.; LeMoullac, B.; Denis, M. G.: Cloning and analysis
of the human S13 ribosomal protein cDNA. Nucleic Acids Res. 21:
2945 only, 1993.
3. 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.
*FIELD* CN
Carol A. Bocchini - updated: 8/7/2003
Patti M. Sherman - updated: 3/24/1999
*FIELD* CD
Victor A. McKusick: 9/17/1993
*FIELD* ED
tkritzer: 08/08/2003
carol: 8/7/2003
carol: 3/31/1999
carol: 9/17/1993