Full text data of RPS9
RPS9
[Confidence: high (present in two of the MS resources)]
40S ribosomal protein S9
Note: presumably soluble (membrane word is not in UniProt keywords or features)
40S ribosomal protein S9
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P46781
ID RS9_HUMAN Reviewed; 194 AA.
AC P46781; A9C4C1; Q4QRK7; Q9BVZ0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 141.
DE RecName: Full=40S ribosomal protein S9;
GN Name=RPS9;
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=7772601; DOI=10.1016/0167-4781(95)00045-I;
RA Frigerio J.-M., Dagorn J.-C., Iovanna J.L.;
RT "Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9,
RT S10 and S29 human ribosomal protein mRNAs.";
RL Biochim. Biophys. Acta 1262:64-68(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11875025; DOI=10.1101/gr.214202;
RA Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S.,
RA Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
RT "The human ribosomal protein genes: sequencing and comparative
RT analysis of 73 genes.";
RL Genome Res. 12:379-390(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Muscle, 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 [6]
RP PROTEIN SEQUENCE OF 2-19.
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-73.
RX PubMed=9582194;
RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N.,
RA Hudson T.J., Tanaka T., Page D.C.;
RT "A map of 75 human ribosomal protein genes.";
RL Genome Res. 8:509-523(1998).
RN [8]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [9]
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-155, 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 [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 STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
RN [13]
RP VARIANT [LARGE SCALE ANALYSIS] PHE-137.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs.
CC -!- INTERACTION:
CC P40763:STAT3; NbExp=2; IntAct=EBI-351206, EBI-518675;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Localized in cytoplasmic
CC mRNP granules containing untranslated mRNAs.
CC -!- SIMILARITY: Belongs to the ribosomal protein S4P family.
CC -!- SIMILARITY: Contains 1 S4 RNA-binding domain.
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DR EMBL; U14971; AAA85659.1; -; mRNA.
DR EMBL; AB061839; BAB79477.1; -; Genomic_DNA.
DR EMBL; CU457734; CAP19125.1; -; Genomic_DNA.
DR EMBL; CU151838; CAQ09597.1; -; Genomic_DNA.
DR EMBL; CH471135; EAW72209.1; -; Genomic_DNA.
DR EMBL; BC000802; AAH00802.1; -; mRNA.
DR EMBL; BC007410; AAH07410.1; -; mRNA.
DR EMBL; BC007434; AAH07434.1; -; mRNA.
DR EMBL; BC007857; AAH07857.1; -; mRNA.
DR EMBL; BC068055; AAH68055.1; -; mRNA.
DR EMBL; BC071940; AAH71940.1; -; mRNA.
DR EMBL; BC096756; AAH96756.1; -; mRNA.
DR EMBL; AB007150; BAA25816.1; -; Genomic_DNA.
DR PIR; S55917; S55917.
DR RefSeq; NP_001004.2; NM_001013.3.
DR RefSeq; XP_005259192.1; XM_005259135.1.
DR RefSeq; XP_005259193.1; XM_005259136.1.
DR RefSeq; XP_005277141.1; XM_005277084.1.
DR RefSeq; XP_005277142.1; XM_005277085.1.
DR RefSeq; XP_005277179.1; XM_005277122.1.
DR RefSeq; XP_005277180.1; XM_005277123.1.
DR RefSeq; XP_005277204.1; XM_005277147.1.
DR RefSeq; XP_005277205.1; XM_005277148.1.
DR RefSeq; XP_005277226.1; XM_005277169.1.
DR RefSeq; XP_005277227.1; XM_005277170.1.
DR RefSeq; XP_005277249.1; XM_005277192.1.
DR RefSeq; XP_005277250.1; XM_005277193.1.
DR RefSeq; XP_005277272.1; XM_005277215.1.
DR RefSeq; XP_005277273.1; XM_005277216.1.
DR RefSeq; XP_005277331.1; XM_005277274.1.
DR RefSeq; XP_005277372.1; XM_005277315.1.
DR RefSeq; XP_005277373.1; XM_005277316.1.
DR RefSeq; XP_005278344.1; XM_005278287.1.
DR RefSeq; XP_005278345.1; XM_005278288.1.
DR UniGene; Hs.467284; -.
DR UniGene; Hs.546288; -.
DR PDB; 3J3A; EM; 5.00 A; J=1-194.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; P46781; -.
DR SMR; P46781; 7-177.
DR IntAct; P46781; 46.
DR MINT; MINT-5001013; -.
DR STRING; 9606.ENSP00000302896; -.
DR PhosphoSite; P46781; -.
DR DMDM; 20178311; -.
DR PaxDb; P46781; -.
DR PeptideAtlas; P46781; -.
DR PRIDE; P46781; -.
DR DNASU; 6203; -.
DR Ensembl; ENST00000302907; ENSP00000302896; ENSG00000170889.
DR Ensembl; ENST00000391752; ENSP00000375632; ENSG00000170889.
DR Ensembl; ENST00000391753; ENSP00000375633; ENSG00000170889.
DR Ensembl; ENST00000573353; ENSP00000461356; ENSG00000263332.
DR Ensembl; ENST00000573511; ENSP00000461393; ENSG00000263076.
DR Ensembl; ENST00000574910; ENSP00000458947; ENSG00000263332.
DR Ensembl; ENST00000575726; ENSP00000460241; ENSG00000263076.
DR Ensembl; ENST00000575746; ENSP00000461170; ENSG00000263332.
DR Ensembl; ENST00000576887; ENSP00000459239; ENSG00000263076.
DR Ensembl; ENST00000604018; ENSP00000474572; ENSG00000271572.
DR Ensembl; ENST00000604119; ENSP00000474184; ENSG00000271572.
DR Ensembl; ENST00000604611; ENSP00000473696; ENSG00000271572.
DR GeneID; 6203; -.
DR KEGG; hsa:6203; -.
DR UCSC; uc002qdx.3; human.
DR CTD; 6203; -.
DR GeneCards; GC19P054851; -.
DR HGNC; HGNC:10442; RPS9.
DR HPA; HPA048746; -.
DR MIM; 603631; gene.
DR neXtProt; NX_P46781; -.
DR PharmGKB; PA34857; -.
DR eggNOG; COG0522; -.
DR HOGENOM; HOG000194525; -.
DR HOVERGEN; HBG001135; -.
DR InParanoid; P46781; -.
DR KO; K02997; -.
DR OMA; KHIDFAV; -.
DR PhylomeDB; P46781; -.
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; RPS9; human.
DR GeneWiki; RPS9; -.
DR GenomeRNAi; 6203; -.
DR NextBio; 24091; -.
DR PRO; PR:P46781; -.
DR ArrayExpress; P46781; -.
DR Bgee; P46781; -.
DR CleanEx; HS_RPS9; -.
DR Genevestigator; P46781; -.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0045182; F:translation regulator activity; IMP:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0008284; P:positive regulation of cell proliferation; 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; 3.10.290.10; -; 1.
DR InterPro; IPR022801; Ribosomal_S4/S9.
DR InterPro; IPR005710; Ribosomal_S4/S9_euk/arc.
DR InterPro; IPR001912; Ribosomal_S4/S9_N.
DR InterPro; IPR018079; Ribosomal_S4_CS.
DR InterPro; IPR002942; S4_RNA-bd.
DR PANTHER; PTHR11831; PTHR11831; 1.
DR Pfam; PF00163; Ribosomal_S4; 1.
DR Pfam; PF01479; S4; 1.
DR SMART; SM00363; S4; 1.
DR TIGRFAMs; TIGR01018; rpsD_arch; 1.
DR PROSITE; PS00632; RIBOSOMAL_S4; 1.
DR PROSITE; PS50889; S4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Polymorphism; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 194 40S ribosomal protein S9.
FT /FTId=PRO_0000132689.
FT DOMAIN 108 182 S4 RNA-binding.
FT MOD_RES 155 155 N6-acetyllysine.
FT VARIANT 25 25 L -> F (in dbSNP:rs41423149).
FT /FTId=VAR_052069.
FT VARIANT 137 137 V -> F (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_036543.
FT CONFLICT 84 84 I -> L (in Ref. 1; AAA85659).
FT CONFLICT 165 167 YGG -> TGV (in Ref. 1; AAA85659).
SQ SEQUENCE 194 AA; 22591 MW; E9CE3CBD59524F81 CRC64;
MPVARSWVCR KTYVTPRRPF EKSRLDQELK LIGEYGLRNK REVWRVKFTL AKIRKAAREL
LTLDEKDPRR LFEGNALLRR LVRIGVLDEG KMKLDYILGL KIEDFLERRL QTQVFKLGLA
KSIHHARVLI RQRHIRVRKQ VVNIPSFIVR LDSQKHIDFS LRSPYGGGRP GRVKRKNAKK
GQGGAGAGDD EEED
//
ID RS9_HUMAN Reviewed; 194 AA.
AC P46781; A9C4C1; Q4QRK7; Q9BVZ0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 141.
DE RecName: Full=40S ribosomal protein S9;
GN Name=RPS9;
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=7772601; DOI=10.1016/0167-4781(95)00045-I;
RA Frigerio J.-M., Dagorn J.-C., Iovanna J.L.;
RT "Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9,
RT S10 and S29 human ribosomal protein mRNAs.";
RL Biochim. Biophys. Acta 1262:64-68(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11875025; DOI=10.1101/gr.214202;
RA Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S.,
RA Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
RT "The human ribosomal protein genes: sequencing and comparative
RT analysis of 73 genes.";
RL Genome Res. 12:379-390(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Muscle, 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 [6]
RP PROTEIN SEQUENCE OF 2-19.
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-73.
RX PubMed=9582194;
RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N.,
RA Hudson T.J., Tanaka T., Page D.C.;
RT "A map of 75 human ribosomal protein genes.";
RL Genome Res. 8:509-523(1998).
RN [8]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [9]
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-155, 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 [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 STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
RN [13]
RP VARIANT [LARGE SCALE ANALYSIS] PHE-137.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs.
CC -!- INTERACTION:
CC P40763:STAT3; NbExp=2; IntAct=EBI-351206, EBI-518675;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Localized in cytoplasmic
CC mRNP granules containing untranslated mRNAs.
CC -!- SIMILARITY: Belongs to the ribosomal protein S4P family.
CC -!- SIMILARITY: Contains 1 S4 RNA-binding domain.
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DR EMBL; U14971; AAA85659.1; -; mRNA.
DR EMBL; AB061839; BAB79477.1; -; Genomic_DNA.
DR EMBL; CU457734; CAP19125.1; -; Genomic_DNA.
DR EMBL; CU151838; CAQ09597.1; -; Genomic_DNA.
DR EMBL; CH471135; EAW72209.1; -; Genomic_DNA.
DR EMBL; BC000802; AAH00802.1; -; mRNA.
DR EMBL; BC007410; AAH07410.1; -; mRNA.
DR EMBL; BC007434; AAH07434.1; -; mRNA.
DR EMBL; BC007857; AAH07857.1; -; mRNA.
DR EMBL; BC068055; AAH68055.1; -; mRNA.
DR EMBL; BC071940; AAH71940.1; -; mRNA.
DR EMBL; BC096756; AAH96756.1; -; mRNA.
DR EMBL; AB007150; BAA25816.1; -; Genomic_DNA.
DR PIR; S55917; S55917.
DR RefSeq; NP_001004.2; NM_001013.3.
DR RefSeq; XP_005259192.1; XM_005259135.1.
DR RefSeq; XP_005259193.1; XM_005259136.1.
DR RefSeq; XP_005277141.1; XM_005277084.1.
DR RefSeq; XP_005277142.1; XM_005277085.1.
DR RefSeq; XP_005277179.1; XM_005277122.1.
DR RefSeq; XP_005277180.1; XM_005277123.1.
DR RefSeq; XP_005277204.1; XM_005277147.1.
DR RefSeq; XP_005277205.1; XM_005277148.1.
DR RefSeq; XP_005277226.1; XM_005277169.1.
DR RefSeq; XP_005277227.1; XM_005277170.1.
DR RefSeq; XP_005277249.1; XM_005277192.1.
DR RefSeq; XP_005277250.1; XM_005277193.1.
DR RefSeq; XP_005277272.1; XM_005277215.1.
DR RefSeq; XP_005277273.1; XM_005277216.1.
DR RefSeq; XP_005277331.1; XM_005277274.1.
DR RefSeq; XP_005277372.1; XM_005277315.1.
DR RefSeq; XP_005277373.1; XM_005277316.1.
DR RefSeq; XP_005278344.1; XM_005278287.1.
DR RefSeq; XP_005278345.1; XM_005278288.1.
DR UniGene; Hs.467284; -.
DR UniGene; Hs.546288; -.
DR PDB; 3J3A; EM; 5.00 A; J=1-194.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; P46781; -.
DR SMR; P46781; 7-177.
DR IntAct; P46781; 46.
DR MINT; MINT-5001013; -.
DR STRING; 9606.ENSP00000302896; -.
DR PhosphoSite; P46781; -.
DR DMDM; 20178311; -.
DR PaxDb; P46781; -.
DR PeptideAtlas; P46781; -.
DR PRIDE; P46781; -.
DR DNASU; 6203; -.
DR Ensembl; ENST00000302907; ENSP00000302896; ENSG00000170889.
DR Ensembl; ENST00000391752; ENSP00000375632; ENSG00000170889.
DR Ensembl; ENST00000391753; ENSP00000375633; ENSG00000170889.
DR Ensembl; ENST00000573353; ENSP00000461356; ENSG00000263332.
DR Ensembl; ENST00000573511; ENSP00000461393; ENSG00000263076.
DR Ensembl; ENST00000574910; ENSP00000458947; ENSG00000263332.
DR Ensembl; ENST00000575726; ENSP00000460241; ENSG00000263076.
DR Ensembl; ENST00000575746; ENSP00000461170; ENSG00000263332.
DR Ensembl; ENST00000576887; ENSP00000459239; ENSG00000263076.
DR Ensembl; ENST00000604018; ENSP00000474572; ENSG00000271572.
DR Ensembl; ENST00000604119; ENSP00000474184; ENSG00000271572.
DR Ensembl; ENST00000604611; ENSP00000473696; ENSG00000271572.
DR GeneID; 6203; -.
DR KEGG; hsa:6203; -.
DR UCSC; uc002qdx.3; human.
DR CTD; 6203; -.
DR GeneCards; GC19P054851; -.
DR HGNC; HGNC:10442; RPS9.
DR HPA; HPA048746; -.
DR MIM; 603631; gene.
DR neXtProt; NX_P46781; -.
DR PharmGKB; PA34857; -.
DR eggNOG; COG0522; -.
DR HOGENOM; HOG000194525; -.
DR HOVERGEN; HBG001135; -.
DR InParanoid; P46781; -.
DR KO; K02997; -.
DR OMA; KHIDFAV; -.
DR PhylomeDB; P46781; -.
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; RPS9; human.
DR GeneWiki; RPS9; -.
DR GenomeRNAi; 6203; -.
DR NextBio; 24091; -.
DR PRO; PR:P46781; -.
DR ArrayExpress; P46781; -.
DR Bgee; P46781; -.
DR CleanEx; HS_RPS9; -.
DR Genevestigator; P46781; -.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0045182; F:translation regulator activity; IMP:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0008284; P:positive regulation of cell proliferation; 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; 3.10.290.10; -; 1.
DR InterPro; IPR022801; Ribosomal_S4/S9.
DR InterPro; IPR005710; Ribosomal_S4/S9_euk/arc.
DR InterPro; IPR001912; Ribosomal_S4/S9_N.
DR InterPro; IPR018079; Ribosomal_S4_CS.
DR InterPro; IPR002942; S4_RNA-bd.
DR PANTHER; PTHR11831; PTHR11831; 1.
DR Pfam; PF00163; Ribosomal_S4; 1.
DR Pfam; PF01479; S4; 1.
DR SMART; SM00363; S4; 1.
DR TIGRFAMs; TIGR01018; rpsD_arch; 1.
DR PROSITE; PS00632; RIBOSOMAL_S4; 1.
DR PROSITE; PS50889; S4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Polymorphism; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 194 40S ribosomal protein S9.
FT /FTId=PRO_0000132689.
FT DOMAIN 108 182 S4 RNA-binding.
FT MOD_RES 155 155 N6-acetyllysine.
FT VARIANT 25 25 L -> F (in dbSNP:rs41423149).
FT /FTId=VAR_052069.
FT VARIANT 137 137 V -> F (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_036543.
FT CONFLICT 84 84 I -> L (in Ref. 1; AAA85659).
FT CONFLICT 165 167 YGG -> TGV (in Ref. 1; AAA85659).
SQ SEQUENCE 194 AA; 22591 MW; E9CE3CBD59524F81 CRC64;
MPVARSWVCR KTYVTPRRPF EKSRLDQELK LIGEYGLRNK REVWRVKFTL AKIRKAAREL
LTLDEKDPRR LFEGNALLRR LVRIGVLDEG KMKLDYILGL KIEDFLERRL QTQVFKLGLA
KSIHHARVLI RQRHIRVRKQ VVNIPSFIVR LDSQKHIDFS LRSPYGGGRP GRVKRKNAKK
GQGGAGAGDD EEED
//
MIM
603631
*RECORD*
*FIELD* NO
603631
*FIELD* TI
*603631 RIBOSOMAL PROTEIN S9; RPS9
*FIELD* TX
The mammalian ribosome is a macromolecular assembly of 4 RNA species
read more(see 180450) and approximately 80 different proteins.
By searching sequence databases with the partial sequences of randomly
selected cDNAs from a human colorectal cDNA library, Frigerio et al.
(1995) identified cDNAs encoding homologs of rat ribosomal proteins S5
(RPS5; 603630), S9 (RPS9), S10 (RPS10; 603632), S29 (RPS29; 603633), L5
(RPL5; 603634), L21 (RPL21; 603636), L27a (RPL27A; 603637), and L28
(RPL28; 603638). Frigerio et al. (1995) completed the cDNA sequences of
these human ribosomal proteins. The deduced 194-amino acid human RPS9
differs from rat Rps9 by 5 amino acids. Northern blot analysis suggested
variable expression of RPS9 in colorectal cancers compared to adjacent
normal tissues, although no correlation between the level of expression
and the severity of the disease was found.
By somatic cell hybrid and radiation hybrid mapping analyses, Kenmochi
et al. (1998) mapped the human RPS9 gene to 19q13.4 (GenBank GENBANK
AB007150).
*FIELD* RF
1. Frigerio, J.-M.; Berthezene, P.; Garrido, P.; Ortiz, E.; Barthellemy,
S.; Vasseur, S.; Sastre, B.; Seleznieff, I.; Dagorn, J. C.; Iovanna,
J. L.: Analysis of 2166 clones from a human colorectal cancer cDNA
library by partial sequencing. Hum. Molec. Genet. 4: 37-43, 1995.
2. Frigerio, J.-M.; Dagorn, J.-C.; Iovanna, J. L.: Cloning, sequencing
and expression of the L5, L21, L27a, L28, S5, S9, S10 and S29 human
ribosomal protein mRNAs. Biochim. Biophys. Acta 1262: 64-68, 1995.
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* CD
Patti M. Sherman: 3/12/1999
*FIELD* ED
psherman: 03/22/1999
carol: 3/19/1999
*RECORD*
*FIELD* NO
603631
*FIELD* TI
*603631 RIBOSOMAL PROTEIN S9; RPS9
*FIELD* TX
The mammalian ribosome is a macromolecular assembly of 4 RNA species
read more(see 180450) and approximately 80 different proteins.
By searching sequence databases with the partial sequences of randomly
selected cDNAs from a human colorectal cDNA library, Frigerio et al.
(1995) identified cDNAs encoding homologs of rat ribosomal proteins S5
(RPS5; 603630), S9 (RPS9), S10 (RPS10; 603632), S29 (RPS29; 603633), L5
(RPL5; 603634), L21 (RPL21; 603636), L27a (RPL27A; 603637), and L28
(RPL28; 603638). Frigerio et al. (1995) completed the cDNA sequences of
these human ribosomal proteins. The deduced 194-amino acid human RPS9
differs from rat Rps9 by 5 amino acids. Northern blot analysis suggested
variable expression of RPS9 in colorectal cancers compared to adjacent
normal tissues, although no correlation between the level of expression
and the severity of the disease was found.
By somatic cell hybrid and radiation hybrid mapping analyses, Kenmochi
et al. (1998) mapped the human RPS9 gene to 19q13.4 (GenBank GENBANK
AB007150).
*FIELD* RF
1. Frigerio, J.-M.; Berthezene, P.; Garrido, P.; Ortiz, E.; Barthellemy,
S.; Vasseur, S.; Sastre, B.; Seleznieff, I.; Dagorn, J. C.; Iovanna,
J. L.: Analysis of 2166 clones from a human colorectal cancer cDNA
library by partial sequencing. Hum. Molec. Genet. 4: 37-43, 1995.
2. Frigerio, J.-M.; Dagorn, J.-C.; Iovanna, J. L.: Cloning, sequencing
and expression of the L5, L21, L27a, L28, S5, S9, S10 and S29 human
ribosomal protein mRNAs. Biochim. Biophys. Acta 1262: 64-68, 1995.
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* CD
Patti M. Sherman: 3/12/1999
*FIELD* ED
psherman: 03/22/1999
carol: 3/19/1999