Full text data of RPS14
RPS14
[Confidence: low (only semi-automatic identification from reviews)]
40S ribosomal protein S14
Note: presumably soluble (membrane word is not in UniProt keywords or features)
40S ribosomal protein S14
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P62263
ID RS14_HUMAN Reviewed; 151 AA.
AC P62263; B2R5G5; D3DQG5; P06366; Q5BJI0;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=40S ribosomal protein S14;
GN Name=RPS14; ORFNames=PRO2640;
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 [GENOMIC DNA].
RX PubMed=3529092; DOI=10.1073/pnas.83.18.6907;
RA Chen I.-T., Dixit A., Rhoads D.D., Roufa D.J.;
RT "Homologous ribosomal proteins in bacteria, yeast, and humans.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:6907-6911(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3785212;
RA Rhoads D.D., Dixit A., Roufa D.J.;
RT "Primary structure of human ribosomal protein S14 and the gene that
RT encodes it.";
RL Mol. Cell. Biol. 6:2774-2783(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J.,
RA Liu M., He F.;
RT "Functional prediction of the coding sequences of 121 new genes
RT deduced by analysis of cDNA clones from human fetal liver.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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=Ovary, Placenta, and Skin;
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 2-15.
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 MUTAGENESIS.
RX PubMed=1549121;
RA Diaz J.-J., Roufa D.J.;
RT "Fine-structure map of the human ribosomal protein gene RPS14.";
RL Mol. Cell. Biol. 12:1680-1686(1992).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-133, AND MASS
RP SPECTROMETRY.
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 IDENTIFICATION BY 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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [13]
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
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 O15479:MAGEB2; NbExp=1; IntAct=EBI-352783, EBI-1057615;
CC O43353:RIPK2; NbExp=1; IntAct=EBI-352783, EBI-358522;
CC Q15654:TRIP6; NbExp=1; IntAct=EBI-352783, EBI-742327;
CC -!- SIMILARITY: Belongs to the ribosomal protein S11P 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; M13934; AAB59505.1; -; Genomic_DNA.
DR EMBL; AF116710; AAF71130.1; -; mRNA.
DR EMBL; AK312179; BAG35112.1; -; mRNA.
DR EMBL; CH471062; EAW61723.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61724.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61725.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61726.1; -; Genomic_DNA.
DR EMBL; BC001126; AAH01126.1; -; mRNA.
DR EMBL; BC003401; AAH03401.1; -; mRNA.
DR EMBL; BC006784; AAH06784.1; -; mRNA.
DR EMBL; BC020515; AAH20515.1; -; mRNA.
DR EMBL; BC091474; AAH91474.1; -; mRNA.
DR PIR; A25220; A25220.
DR RefSeq; NP_001020241.1; NM_001025070.1.
DR RefSeq; NP_001020242.1; NM_001025071.1.
DR RefSeq; NP_005608.1; NM_005617.3.
DR UniGene; Hs.744846; -.
DR PDB; 3J3A; EM; 5.00 A; O=1-151.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; P62263; -.
DR SMR; P62263; 16-140.
DR IntAct; P62263; 24.
DR MINT; MINT-4999998; -.
DR STRING; 9606.ENSP00000311028; -.
DR PhosphoSite; P62263; -.
DR DMDM; 50403752; -.
DR SWISS-2DPAGE; P62263; -.
DR PaxDb; P62263; -.
DR PeptideAtlas; P62263; -.
DR PRIDE; P62263; -.
DR DNASU; 6208; -.
DR Ensembl; ENST00000312037; ENSP00000311028; ENSG00000164587.
DR Ensembl; ENST00000401695; ENSP00000385958; ENSG00000164587.
DR Ensembl; ENST00000407193; ENSP00000385425; ENSG00000164587.
DR Ensembl; ENST00000521466; ENSP00000428509; ENSG00000164587.
DR GeneID; 6208; -.
DR KEGG; hsa:6208; -.
DR UCSC; uc003lsh.3; human.
DR CTD; 6208; -.
DR GeneCards; GC05M149803; -.
DR HGNC; HGNC:10387; RPS14.
DR HPA; HPA018504; -.
DR MIM; 130620; gene.
DR neXtProt; NX_P62263; -.
DR Orphanet; 86841; Myelodysplastic syndrome associated with isolated del(5q) chromosome abnormality.
DR PharmGKB; PA34786; -.
DR eggNOG; COG0100; -.
DR HOGENOM; HOG000111598; -.
DR HOVERGEN; HBG053098; -.
DR InParanoid; P62263; -.
DR KO; K02955; -.
DR OMA; LHVKIRA; -.
DR OrthoDB; EOG77DJ81; -.
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; RPS14; human.
DR GeneWiki; RPS14; -.
DR GenomeRNAi; 6208; -.
DR NextBio; 24111; -.
DR PRO; PR:P62263; -.
DR ArrayExpress; P62263; -.
DR Bgee; P62263; -.
DR CleanEx; HS_RPS14; -.
DR Genevestigator; P62263; -.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0045182; F:translation regulator activity; IMP:UniProtKB.
DR GO; GO:0030218; P:erythrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0030490; P:maturation of SSU-rRNA; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IMP: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; 3.30.420.80; -; 1.
DR HAMAP; MF_01310; Ribosomal_S11; 1; -.
DR InterPro; IPR001971; Ribosomal_S11.
DR InterPro; IPR018102; Ribosomal_S11_CS.
DR PANTHER; PTHR11759; PTHR11759; 1.
DR Pfam; PF00411; Ribosomal_S11; 1.
DR PIRSF; PIRSF002131; Ribosomal_S11; 1.
DR PROSITE; PS00054; RIBOSOMAL_S11; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Direct protein sequencing;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 151 40S ribosomal protein S14.
FT /FTId=PRO_0000123337.
FT MOD_RES 133 133 Phosphothreonine.
SQ SEQUENCE 151 AA; 16273 MW; 4F4387F9FADAC278 CRC64;
MAPRKGKEKK EEQVISLGPQ VAEGENVFGV CHIFASFNDT FVHVTDLSGK ETICRVTGGM
KVKADRDESS PYAAMLAAQD VAQRCKELGI TALHIKLRAT GGNRTKTPGP GAQSALRALA
RSGMKIGRIE DVTPIPSDST RRKGGRRGRR L
//
ID RS14_HUMAN Reviewed; 151 AA.
AC P62263; B2R5G5; D3DQG5; P06366; Q5BJI0;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=40S ribosomal protein S14;
GN Name=RPS14; ORFNames=PRO2640;
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 [GENOMIC DNA].
RX PubMed=3529092; DOI=10.1073/pnas.83.18.6907;
RA Chen I.-T., Dixit A., Rhoads D.D., Roufa D.J.;
RT "Homologous ribosomal proteins in bacteria, yeast, and humans.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:6907-6911(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3785212;
RA Rhoads D.D., Dixit A., Roufa D.J.;
RT "Primary structure of human ribosomal protein S14 and the gene that
RT encodes it.";
RL Mol. Cell. Biol. 6:2774-2783(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J.,
RA Liu M., He F.;
RT "Functional prediction of the coding sequences of 121 new genes
RT deduced by analysis of cDNA clones from human fetal liver.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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=Ovary, Placenta, and Skin;
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 2-15.
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 MUTAGENESIS.
RX PubMed=1549121;
RA Diaz J.-J., Roufa D.J.;
RT "Fine-structure map of the human ribosomal protein gene RPS14.";
RL Mol. Cell. Biol. 12:1680-1686(1992).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-133, AND MASS
RP SPECTROMETRY.
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 IDENTIFICATION BY 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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [13]
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
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 O15479:MAGEB2; NbExp=1; IntAct=EBI-352783, EBI-1057615;
CC O43353:RIPK2; NbExp=1; IntAct=EBI-352783, EBI-358522;
CC Q15654:TRIP6; NbExp=1; IntAct=EBI-352783, EBI-742327;
CC -!- SIMILARITY: Belongs to the ribosomal protein S11P 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; M13934; AAB59505.1; -; Genomic_DNA.
DR EMBL; AF116710; AAF71130.1; -; mRNA.
DR EMBL; AK312179; BAG35112.1; -; mRNA.
DR EMBL; CH471062; EAW61723.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61724.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61725.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61726.1; -; Genomic_DNA.
DR EMBL; BC001126; AAH01126.1; -; mRNA.
DR EMBL; BC003401; AAH03401.1; -; mRNA.
DR EMBL; BC006784; AAH06784.1; -; mRNA.
DR EMBL; BC020515; AAH20515.1; -; mRNA.
DR EMBL; BC091474; AAH91474.1; -; mRNA.
DR PIR; A25220; A25220.
DR RefSeq; NP_001020241.1; NM_001025070.1.
DR RefSeq; NP_001020242.1; NM_001025071.1.
DR RefSeq; NP_005608.1; NM_005617.3.
DR UniGene; Hs.744846; -.
DR PDB; 3J3A; EM; 5.00 A; O=1-151.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; P62263; -.
DR SMR; P62263; 16-140.
DR IntAct; P62263; 24.
DR MINT; MINT-4999998; -.
DR STRING; 9606.ENSP00000311028; -.
DR PhosphoSite; P62263; -.
DR DMDM; 50403752; -.
DR SWISS-2DPAGE; P62263; -.
DR PaxDb; P62263; -.
DR PeptideAtlas; P62263; -.
DR PRIDE; P62263; -.
DR DNASU; 6208; -.
DR Ensembl; ENST00000312037; ENSP00000311028; ENSG00000164587.
DR Ensembl; ENST00000401695; ENSP00000385958; ENSG00000164587.
DR Ensembl; ENST00000407193; ENSP00000385425; ENSG00000164587.
DR Ensembl; ENST00000521466; ENSP00000428509; ENSG00000164587.
DR GeneID; 6208; -.
DR KEGG; hsa:6208; -.
DR UCSC; uc003lsh.3; human.
DR CTD; 6208; -.
DR GeneCards; GC05M149803; -.
DR HGNC; HGNC:10387; RPS14.
DR HPA; HPA018504; -.
DR MIM; 130620; gene.
DR neXtProt; NX_P62263; -.
DR Orphanet; 86841; Myelodysplastic syndrome associated with isolated del(5q) chromosome abnormality.
DR PharmGKB; PA34786; -.
DR eggNOG; COG0100; -.
DR HOGENOM; HOG000111598; -.
DR HOVERGEN; HBG053098; -.
DR InParanoid; P62263; -.
DR KO; K02955; -.
DR OMA; LHVKIRA; -.
DR OrthoDB; EOG77DJ81; -.
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; RPS14; human.
DR GeneWiki; RPS14; -.
DR GenomeRNAi; 6208; -.
DR NextBio; 24111; -.
DR PRO; PR:P62263; -.
DR ArrayExpress; P62263; -.
DR Bgee; P62263; -.
DR CleanEx; HS_RPS14; -.
DR Genevestigator; P62263; -.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0045182; F:translation regulator activity; IMP:UniProtKB.
DR GO; GO:0030218; P:erythrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0030490; P:maturation of SSU-rRNA; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IMP: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; 3.30.420.80; -; 1.
DR HAMAP; MF_01310; Ribosomal_S11; 1; -.
DR InterPro; IPR001971; Ribosomal_S11.
DR InterPro; IPR018102; Ribosomal_S11_CS.
DR PANTHER; PTHR11759; PTHR11759; 1.
DR Pfam; PF00411; Ribosomal_S11; 1.
DR PIRSF; PIRSF002131; Ribosomal_S11; 1.
DR PROSITE; PS00054; RIBOSOMAL_S11; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Direct protein sequencing;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 151 40S ribosomal protein S14.
FT /FTId=PRO_0000123337.
FT MOD_RES 133 133 Phosphothreonine.
SQ SEQUENCE 151 AA; 16273 MW; 4F4387F9FADAC278 CRC64;
MAPRKGKEKK EEQVISLGPQ VAEGENVFGV CHIFASFNDT FVHVTDLSGK ETICRVTGGM
KVKADRDESS PYAAMLAAQD VAQRCKELGI TALHIKLRAT GGNRTKTPGP GAQSALRALA
RSGMKIGRIE DVTPIPSDST RRKGGRRGRR L
//
MIM
130620
*RECORD*
*FIELD* NO
130620
*FIELD* TI
*130620 RIBOSOMAL PROTEIN S14; RPS14
;;EMETINE RESISTANCE GENE; EMTB
*FIELD* TX
CLONING
read more
The mammalian ribosome consists of 4 RNA species (see 180450) and
approximately 80 different proteins. The ribosomal proteins are encoded
by complex gene families that include at least 1 active
intron-containing gene and multiple processed pseudogenes.
Dana and Wasmuth (1982) isolated interspecific hybrids between normal
human leukocytes and a Chinese hamster ovary (CHO) cell line that had a
mutation in the EMTB locus, leading to alteration of the 40S ribosomal
protein S14 and, as a result, resistance to the protein synthesis
inhibitor emetine. The cell line was also chromate-resistant due to a
mutation in the CHR gene (118840) and temperature-sensitive because of a
mutation in the leucyl-tRNA synthetase gene (LEUS; 151350). All 3
mutations were recessive in CHO cells. Therefore, human-CHO cell hybrids
were emetine-sensitive, chromate-sensitive, and temperature-resistant.
By screening cDNAs derived from HeLa cell 10S to 12S mRNAs with a CHO
Rps14 cDNA, Rhoads et al. (1986) isolated cDNAs encoding human RPS14.
The deduced 151-amino acid human RPS14 protein is identical to CHO
Rps14. The authors isolated human RPS14 genomic clones using human and
CHO RPS14 cDNAs.
Chen et al. (1986) reported that the RPS14 gene appears to have been
stringently conserved during evolution. They found high similarity
between the C termini of mammalian RPS14 and yeast ribosomal protein 59;
this region includes nucleotides that are mutated in emetine-resistant
CHO cells (Rhoads and Roufa, 1985).
GENE STRUCTURE
Rhoads et al. (1986) determined that the human RPS14 gene contains 5
exons and spans 5.9 kb.
MAPPING
All 3 genes related to emetine resistance isolated by Dana and Wasmuth
(1982) appeared to be linked to the long arm of chromosome 2 in the
Chinese hamster. Dana and Wasmuth (1982) showed that the genes for these
3 characteristics are carried by human chromosome 5. The results showed
that synteny of the 3 genes has been long maintained in evolution. The
EMTB locus, 1 of 3 genes that can be altered to give rise to the
emetine-resistance phenotype, encodes ribosomal protein S14 (Madjar et
al., 1982, Dana et al., 1985). Dana and Wasmuth (1982) subjected Chinese
hamster-human interspecific hybrid cells, which contained human
chromosome 5 and expressed the 4 syntenic genes LEUS, HEXB (606873),
EMTB, and CHR, to selective conditions requiring them to retain the LEUS
gene but lose either the EMTB or CHR gene. Using cytogenetic and
biochemical analyses of spontaneous segregants, which arose primarily by
terminal deletions of various portions of 5q, Dana and Wasmuth (1982)
concluded that the order and specific locations of the linked genes are:
LEUS, 5pter-5q1; HEXB, 5q13; EMTB, 5q23-5q35; and CHR, 5q35. Other
ribosomal protein genes were mapped to chromosomes 8 and 17 by Nakamichi
et al. (1986), using cDNA probes and hamster-human hybrid cells. The
region of chromosome 8 carrying ribosomal protein genes was 8pter-q21.1.
The ribosomal protein genes on chromosome 17 were on the long arm.
Nakamichi et al. (1986) placed the RPS14 gene on the segment 5q23-q33.
Rhoads et al. (1986) mapped a DNA fragment derived from an intron of the
RPS14 gene to 5q23-q33 using somatic cell hybrid DNAs, indicating that
the functional RPS14 gene is located at this locus. Kenmochi et al.
(1998) confirmed the mapping assignment reported by Rhoads et al.
(1986).
MOLECULAR GENETICS
- Somatic RPS14 Haploinsufficiency Causes 5q Deletion Syndrome
The 5q- syndrome (153550) is a myelodysplastic syndrome subtype
characterized by a defect in erythroid differentiation caused by
recurring somatic deletion of a 1.5-Mb region on chromosome 5q
containing 40 genes. While somatic chromosomal deletions in cancer have
been thought to indicate the location of tumor suppressor genes whose
biallelic inactivation results in cancer, no such biallelic inactivation
had been found in patients with 5q- syndrome. Using an RNA-mediated
interference-based approach, Ebert et al. (2008) found that partial loss
of function of the ribosomal subunit protein RPS14 phenocopied the
disease in normal hematopoietic progenitor cells. Forced expression of
RPS14 rescued the disease phenotype in patient-derived bone marrow
cells. In addition, the authors identified a block in the processing of
preribosomal RNA in RPS14-deficient cells that is functionally
equivalent to the defect in Diamond-Blackfan anemia (105650), linking
the molecular pathophysiology of the 5q- syndrome (the somatic deletion
of one allele of RPS14) to a congenital syndrome causing bone marrow
failure. Ebert et al. (2008) concluded that the 5q- syndrome is caused
by defects in ribosomal protein function and suggested that RNA
interference screening is an effective strategy for identifying causal
haploinsufficiency disease genes.
*FIELD* RF
1. Chen, I.-T.; Dixit, A.; Rhoads, D. D.; Roufa, D. J.: Homologous
ribosomal proteins in bacteria, yeast, and humans. Proc. Nat. Acad.
Sci. 83: 6907-6911, 1986.
2. Dana, S.; Wasmuth, J. J.: Linkage of the leuS, emtB, and chr genes
on chromosome 5 in humans and expression of human genes encoding protein
synthetic components in human-Chinese hamster hybrids. Somat. Cell
Genet. 8: 245-264, 1982.
3. Dana, S.; Wasmuth, J. J.: Selective linkage disruption in human-Chinese
hamster cell hybrids: deletion mapping of the leuS, hexB, emtB, and
chr genes on human chromosome 5. Molec. Cell. Biol. 2: 1220-1228,
1982.
4. Dana, S. L.; Chang, S.; Wasmuth, J. J.: Synthesis and incorporation
of human ribosomal protein S14 into functional ribosomes in human-Chinese
hamster cell hybrids containing human chromosome 5: human RPS14 gene
is the structural gene for ribosomal protein S14. Somat. Cell Molec.
Genet. 11: 625-631, 1985.
5. Ebert, B. L.; Pretz, J.; Bosco, J.; Chang, C. Y.; Tamayo, P.; Galili,
N.; Raza, A.; Root, D. E.; Attar, E.; Ellis, S. R.; Golub, T. R.:
Identification of RPS14 as a 5q- syndrome gene by RNA interference
screen. Nature 451: 335-339, 2008.
6. 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.
7. Madjar, J. J.; Nielsen-Smith, K.; Frahm, M.; Roufa, D.: Emetine
resistance in Chinese hamster ovary cells is associated with an altered
ribosomal protein S14 mRNA. Proc. Nat. Acad. Sci. 79: 1003-1007,
1982.
8. Nakamichi, N. N.; Kao, F.-T.; Wasmuth, J.; Roufa, D. J.: Ribosomal
protein gene sequences map to human chromosomes 5, 8, and 17. Somat.
Cell Molec. Genet. 12: 225-236, 1986.
9. Rhoads, D. D.; Dixit, A.; Roufa, D. J.: Primary structure of human
ribosomal protein S14 and the gene that encodes it. Molec. Cell.
Biol. 6: 2774-2783, 1986.
10. Rhoads, D. D.; Roufa, D. J.: Emetine resistance of Chinese hamster
cells: structures of wild-type and mutant ribosomal protein S14 mRNAs. Molec.
Cell. Biol. 5: 1655-1659, 1985.
*FIELD* CN
Ada Hamosh - updated: 2/21/2008
Patti M. Sherman - updated: 3/26/1999
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
alopez: 03/19/2008
terry: 2/21/2008
ckniffin: 5/7/2002
psherman: 4/5/1999
carol: 4/1/1999
psherman: 3/24/1999
psherman: 2/2/1999
carol: 7/22/1993
carol: 6/5/1992
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/26/1989
marie: 3/25/1988
*RECORD*
*FIELD* NO
130620
*FIELD* TI
*130620 RIBOSOMAL PROTEIN S14; RPS14
;;EMETINE RESISTANCE GENE; EMTB
*FIELD* TX
CLONING
read more
The mammalian ribosome consists of 4 RNA species (see 180450) and
approximately 80 different proteins. The ribosomal proteins are encoded
by complex gene families that include at least 1 active
intron-containing gene and multiple processed pseudogenes.
Dana and Wasmuth (1982) isolated interspecific hybrids between normal
human leukocytes and a Chinese hamster ovary (CHO) cell line that had a
mutation in the EMTB locus, leading to alteration of the 40S ribosomal
protein S14 and, as a result, resistance to the protein synthesis
inhibitor emetine. The cell line was also chromate-resistant due to a
mutation in the CHR gene (118840) and temperature-sensitive because of a
mutation in the leucyl-tRNA synthetase gene (LEUS; 151350). All 3
mutations were recessive in CHO cells. Therefore, human-CHO cell hybrids
were emetine-sensitive, chromate-sensitive, and temperature-resistant.
By screening cDNAs derived from HeLa cell 10S to 12S mRNAs with a CHO
Rps14 cDNA, Rhoads et al. (1986) isolated cDNAs encoding human RPS14.
The deduced 151-amino acid human RPS14 protein is identical to CHO
Rps14. The authors isolated human RPS14 genomic clones using human and
CHO RPS14 cDNAs.
Chen et al. (1986) reported that the RPS14 gene appears to have been
stringently conserved during evolution. They found high similarity
between the C termini of mammalian RPS14 and yeast ribosomal protein 59;
this region includes nucleotides that are mutated in emetine-resistant
CHO cells (Rhoads and Roufa, 1985).
GENE STRUCTURE
Rhoads et al. (1986) determined that the human RPS14 gene contains 5
exons and spans 5.9 kb.
MAPPING
All 3 genes related to emetine resistance isolated by Dana and Wasmuth
(1982) appeared to be linked to the long arm of chromosome 2 in the
Chinese hamster. Dana and Wasmuth (1982) showed that the genes for these
3 characteristics are carried by human chromosome 5. The results showed
that synteny of the 3 genes has been long maintained in evolution. The
EMTB locus, 1 of 3 genes that can be altered to give rise to the
emetine-resistance phenotype, encodes ribosomal protein S14 (Madjar et
al., 1982, Dana et al., 1985). Dana and Wasmuth (1982) subjected Chinese
hamster-human interspecific hybrid cells, which contained human
chromosome 5 and expressed the 4 syntenic genes LEUS, HEXB (606873),
EMTB, and CHR, to selective conditions requiring them to retain the LEUS
gene but lose either the EMTB or CHR gene. Using cytogenetic and
biochemical analyses of spontaneous segregants, which arose primarily by
terminal deletions of various portions of 5q, Dana and Wasmuth (1982)
concluded that the order and specific locations of the linked genes are:
LEUS, 5pter-5q1; HEXB, 5q13; EMTB, 5q23-5q35; and CHR, 5q35. Other
ribosomal protein genes were mapped to chromosomes 8 and 17 by Nakamichi
et al. (1986), using cDNA probes and hamster-human hybrid cells. The
region of chromosome 8 carrying ribosomal protein genes was 8pter-q21.1.
The ribosomal protein genes on chromosome 17 were on the long arm.
Nakamichi et al. (1986) placed the RPS14 gene on the segment 5q23-q33.
Rhoads et al. (1986) mapped a DNA fragment derived from an intron of the
RPS14 gene to 5q23-q33 using somatic cell hybrid DNAs, indicating that
the functional RPS14 gene is located at this locus. Kenmochi et al.
(1998) confirmed the mapping assignment reported by Rhoads et al.
(1986).
MOLECULAR GENETICS
- Somatic RPS14 Haploinsufficiency Causes 5q Deletion Syndrome
The 5q- syndrome (153550) is a myelodysplastic syndrome subtype
characterized by a defect in erythroid differentiation caused by
recurring somatic deletion of a 1.5-Mb region on chromosome 5q
containing 40 genes. While somatic chromosomal deletions in cancer have
been thought to indicate the location of tumor suppressor genes whose
biallelic inactivation results in cancer, no such biallelic inactivation
had been found in patients with 5q- syndrome. Using an RNA-mediated
interference-based approach, Ebert et al. (2008) found that partial loss
of function of the ribosomal subunit protein RPS14 phenocopied the
disease in normal hematopoietic progenitor cells. Forced expression of
RPS14 rescued the disease phenotype in patient-derived bone marrow
cells. In addition, the authors identified a block in the processing of
preribosomal RNA in RPS14-deficient cells that is functionally
equivalent to the defect in Diamond-Blackfan anemia (105650), linking
the molecular pathophysiology of the 5q- syndrome (the somatic deletion
of one allele of RPS14) to a congenital syndrome causing bone marrow
failure. Ebert et al. (2008) concluded that the 5q- syndrome is caused
by defects in ribosomal protein function and suggested that RNA
interference screening is an effective strategy for identifying causal
haploinsufficiency disease genes.
*FIELD* RF
1. Chen, I.-T.; Dixit, A.; Rhoads, D. D.; Roufa, D. J.: Homologous
ribosomal proteins in bacteria, yeast, and humans. Proc. Nat. Acad.
Sci. 83: 6907-6911, 1986.
2. Dana, S.; Wasmuth, J. J.: Linkage of the leuS, emtB, and chr genes
on chromosome 5 in humans and expression of human genes encoding protein
synthetic components in human-Chinese hamster hybrids. Somat. Cell
Genet. 8: 245-264, 1982.
3. Dana, S.; Wasmuth, J. J.: Selective linkage disruption in human-Chinese
hamster cell hybrids: deletion mapping of the leuS, hexB, emtB, and
chr genes on human chromosome 5. Molec. Cell. Biol. 2: 1220-1228,
1982.
4. Dana, S. L.; Chang, S.; Wasmuth, J. J.: Synthesis and incorporation
of human ribosomal protein S14 into functional ribosomes in human-Chinese
hamster cell hybrids containing human chromosome 5: human RPS14 gene
is the structural gene for ribosomal protein S14. Somat. Cell Molec.
Genet. 11: 625-631, 1985.
5. Ebert, B. L.; Pretz, J.; Bosco, J.; Chang, C. Y.; Tamayo, P.; Galili,
N.; Raza, A.; Root, D. E.; Attar, E.; Ellis, S. R.; Golub, T. R.:
Identification of RPS14 as a 5q- syndrome gene by RNA interference
screen. Nature 451: 335-339, 2008.
6. 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.
7. Madjar, J. J.; Nielsen-Smith, K.; Frahm, M.; Roufa, D.: Emetine
resistance in Chinese hamster ovary cells is associated with an altered
ribosomal protein S14 mRNA. Proc. Nat. Acad. Sci. 79: 1003-1007,
1982.
8. Nakamichi, N. N.; Kao, F.-T.; Wasmuth, J.; Roufa, D. J.: Ribosomal
protein gene sequences map to human chromosomes 5, 8, and 17. Somat.
Cell Molec. Genet. 12: 225-236, 1986.
9. Rhoads, D. D.; Dixit, A.; Roufa, D. J.: Primary structure of human
ribosomal protein S14 and the gene that encodes it. Molec. Cell.
Biol. 6: 2774-2783, 1986.
10. Rhoads, D. D.; Roufa, D. J.: Emetine resistance of Chinese hamster
cells: structures of wild-type and mutant ribosomal protein S14 mRNAs. Molec.
Cell. Biol. 5: 1655-1659, 1985.
*FIELD* CN
Ada Hamosh - updated: 2/21/2008
Patti M. Sherman - updated: 3/26/1999
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
alopez: 03/19/2008
terry: 2/21/2008
ckniffin: 5/7/2002
psherman: 4/5/1999
carol: 4/1/1999
psherman: 3/24/1999
psherman: 2/2/1999
carol: 7/22/1993
carol: 6/5/1992
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/26/1989
marie: 3/25/1988