Full text data of RPS29
RPS29
[Confidence: low (only semi-automatic identification from reviews)]
40S ribosomal protein S29
Note: presumably soluble (membrane word is not in UniProt keywords or features)
40S ribosomal protein S29
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P62273
ID RS29_HUMAN Reviewed; 56 AA.
AC P62273; A8MZ73; P30054;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 96.
DE RecName: Full=40S ribosomal protein S29;
GN Name=RPS29;
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] (ISOFORM 1).
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 [MRNA] (ISOFORM 1).
RC TISSUE=Colon;
RX PubMed=8781548; DOI=10.1016/0167-4889(96)00052-3;
RA Kondoh N., Noda M., Fisher R.J., Schweinfest C.W., Papas T.S.,
RA Kondoh A., Samuel K.P., Oikawa T.;
RT "The S29 ribosomal protein increases tumor suppressor activity of K
RT rev-1 gene on v-K ras-transformed NIH3T3 cells.";
RL Biochim. Biophys. Acta 1313:41-46(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Blood, Bone marrow, and Eye;
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 2-11.
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 PROTEIN SEQUENCE OF 2-12 AND 49-56, CLEAVAGE OF INITIATOR METHIONINE,
RP AND MASS SPECTROMETRY.
RC TISSUE=Colon adenocarcinoma;
RA Bienvenut W.V., Murray L., Brunton V.G., Frame M.C.;
RL Submitted (FEB-2008) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-54.
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-48, 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 [10]
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 [11]
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 -!- COFACTOR: Binds 1 zinc ion per subunit (Potential).
CC -!- INTERACTION:
CC Q9NY93:DDX56; NbExp=1; IntAct=EBI-1054121, EBI-372376;
CC O60739:EIF1B; NbExp=1; IntAct=EBI-1054121, EBI-1043343;
CC Q14240:EIF4A2; NbExp=1; IntAct=EBI-1054121, EBI-73473;
CC Q93063:EXT2; NbExp=1; IntAct=EBI-1054121, EBI-1047761;
CC Q9Y6J8:STYXL1; NbExp=1; IntAct=EBI-1054121, EBI-1044511;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P62273-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P62273-2; Sequence=VSP_042844;
CC -!- SIMILARITY: Belongs to the ribosomal protein S14P 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; U14973; AAA85661.1; -; mRNA.
DR EMBL; L31610; AAB27426.1; -; mRNA.
DR EMBL; AB061847; BAB79485.1; -; Genomic_DNA.
DR EMBL; AL139099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015974; AAH15974.2; -; mRNA.
DR EMBL; BC032813; AAH32813.1; -; mRNA.
DR EMBL; BC035313; AAH35313.1; -; mRNA.
DR EMBL; AB007165; BAA25827.1; -; Genomic_DNA.
DR PIR; S55919; S55919.
DR RefSeq; NP_001023.1; NM_001032.4.
DR RefSeq; NP_001025172.1; NM_001030001.2.
DR UniGene; Hs.156367; -.
DR PDB; 2ZKQ; EM; 8.70 A; n=1-56.
DR PDB; 3J3A; EM; 5.00 A; d=1-56.
DR PDBsum; 2ZKQ; -.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; P62273; -.
DR SMR; P62273; 4-56.
DR IntAct; P62273; 7.
DR MINT; MINT-4133209; -.
DR STRING; 9606.ENSP00000379339; -.
DR PhosphoSite; P62273; -.
DR DMDM; 50403626; -.
DR PaxDb; P62273; -.
DR PRIDE; P62273; -.
DR DNASU; 6235; -.
DR Ensembl; ENST00000245458; ENSP00000245458; ENSG00000213741.
DR Ensembl; ENST00000396020; ENSP00000379339; ENSG00000213741.
DR GeneID; 6235; -.
DR KEGG; hsa:6235; -.
DR UCSC; uc001wwm.4; human.
DR CTD; 6235; -.
DR GeneCards; GC14M050043; -.
DR HGNC; HGNC:10419; RPS29.
DR HPA; HPA004107; -.
DR MIM; 603633; gene.
DR neXtProt; NX_P62273; -.
DR PharmGKB; PA34826; -.
DR eggNOG; COG0199; -.
DR HOVERGEN; HBG004459; -.
DR KO; K02980; -.
DR OMA; CFREKAA; -.
DR OrthoDB; EOG78D7P4; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; RPS29; -.
DR GenomeRNAi; 6235; -.
DR NextBio; 24205; -.
DR PRO; PR:P62273; -.
DR Bgee; P62273; -.
DR CleanEx; HS_RPS29; -.
DR Genevestigator; P62273; -.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; 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 InterPro; IPR001209; Ribosomal_S14.
DR InterPro; IPR018271; Ribosomal_S14_CS.
DR Pfam; PF00253; Ribosomal_S14; 1.
DR PROSITE; PS00527; RIBOSOMAL_S14; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Metal-binding; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Zinc.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 56 40S ribosomal protein S29.
FT /FTId=PRO_0000131019.
FT METAL 21 21 Zinc (Potential).
FT METAL 24 24 Zinc (Potential).
FT METAL 39 39 Zinc (Potential).
FT METAL 42 42 Zinc (Potential).
FT MOD_RES 48 48 N6-acetyllysine.
FT VAR_SEQ 54 56 KLD -> KKDLSCLPWHCLWR (in isoform 2).
FT /FTId=VSP_042844.
SQ SEQUENCE 56 AA; 6677 MW; 41325122B493EFF9 CRC64;
MGHQQLYWSH PRKFGQGSRS CRVCSNRHGL IRKYGLNMCR QCFRQYAKDI GFIKLD
//
ID RS29_HUMAN Reviewed; 56 AA.
AC P62273; A8MZ73; P30054;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 96.
DE RecName: Full=40S ribosomal protein S29;
GN Name=RPS29;
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] (ISOFORM 1).
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 [MRNA] (ISOFORM 1).
RC TISSUE=Colon;
RX PubMed=8781548; DOI=10.1016/0167-4889(96)00052-3;
RA Kondoh N., Noda M., Fisher R.J., Schweinfest C.W., Papas T.S.,
RA Kondoh A., Samuel K.P., Oikawa T.;
RT "The S29 ribosomal protein increases tumor suppressor activity of K
RT rev-1 gene on v-K ras-transformed NIH3T3 cells.";
RL Biochim. Biophys. Acta 1313:41-46(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Blood, Bone marrow, and Eye;
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 2-11.
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 PROTEIN SEQUENCE OF 2-12 AND 49-56, CLEAVAGE OF INITIATOR METHIONINE,
RP AND MASS SPECTROMETRY.
RC TISSUE=Colon adenocarcinoma;
RA Bienvenut W.V., Murray L., Brunton V.G., Frame M.C.;
RL Submitted (FEB-2008) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-54.
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-48, 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 [10]
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 [11]
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 -!- COFACTOR: Binds 1 zinc ion per subunit (Potential).
CC -!- INTERACTION:
CC Q9NY93:DDX56; NbExp=1; IntAct=EBI-1054121, EBI-372376;
CC O60739:EIF1B; NbExp=1; IntAct=EBI-1054121, EBI-1043343;
CC Q14240:EIF4A2; NbExp=1; IntAct=EBI-1054121, EBI-73473;
CC Q93063:EXT2; NbExp=1; IntAct=EBI-1054121, EBI-1047761;
CC Q9Y6J8:STYXL1; NbExp=1; IntAct=EBI-1054121, EBI-1044511;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P62273-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P62273-2; Sequence=VSP_042844;
CC -!- SIMILARITY: Belongs to the ribosomal protein S14P 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; U14973; AAA85661.1; -; mRNA.
DR EMBL; L31610; AAB27426.1; -; mRNA.
DR EMBL; AB061847; BAB79485.1; -; Genomic_DNA.
DR EMBL; AL139099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015974; AAH15974.2; -; mRNA.
DR EMBL; BC032813; AAH32813.1; -; mRNA.
DR EMBL; BC035313; AAH35313.1; -; mRNA.
DR EMBL; AB007165; BAA25827.1; -; Genomic_DNA.
DR PIR; S55919; S55919.
DR RefSeq; NP_001023.1; NM_001032.4.
DR RefSeq; NP_001025172.1; NM_001030001.2.
DR UniGene; Hs.156367; -.
DR PDB; 2ZKQ; EM; 8.70 A; n=1-56.
DR PDB; 3J3A; EM; 5.00 A; d=1-56.
DR PDBsum; 2ZKQ; -.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; P62273; -.
DR SMR; P62273; 4-56.
DR IntAct; P62273; 7.
DR MINT; MINT-4133209; -.
DR STRING; 9606.ENSP00000379339; -.
DR PhosphoSite; P62273; -.
DR DMDM; 50403626; -.
DR PaxDb; P62273; -.
DR PRIDE; P62273; -.
DR DNASU; 6235; -.
DR Ensembl; ENST00000245458; ENSP00000245458; ENSG00000213741.
DR Ensembl; ENST00000396020; ENSP00000379339; ENSG00000213741.
DR GeneID; 6235; -.
DR KEGG; hsa:6235; -.
DR UCSC; uc001wwm.4; human.
DR CTD; 6235; -.
DR GeneCards; GC14M050043; -.
DR HGNC; HGNC:10419; RPS29.
DR HPA; HPA004107; -.
DR MIM; 603633; gene.
DR neXtProt; NX_P62273; -.
DR PharmGKB; PA34826; -.
DR eggNOG; COG0199; -.
DR HOVERGEN; HBG004459; -.
DR KO; K02980; -.
DR OMA; CFREKAA; -.
DR OrthoDB; EOG78D7P4; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; RPS29; -.
DR GenomeRNAi; 6235; -.
DR NextBio; 24205; -.
DR PRO; PR:P62273; -.
DR Bgee; P62273; -.
DR CleanEx; HS_RPS29; -.
DR Genevestigator; P62273; -.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; 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 InterPro; IPR001209; Ribosomal_S14.
DR InterPro; IPR018271; Ribosomal_S14_CS.
DR Pfam; PF00253; Ribosomal_S14; 1.
DR PROSITE; PS00527; RIBOSOMAL_S14; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Metal-binding; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Zinc.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 56 40S ribosomal protein S29.
FT /FTId=PRO_0000131019.
FT METAL 21 21 Zinc (Potential).
FT METAL 24 24 Zinc (Potential).
FT METAL 39 39 Zinc (Potential).
FT METAL 42 42 Zinc (Potential).
FT MOD_RES 48 48 N6-acetyllysine.
FT VAR_SEQ 54 56 KLD -> KKDLSCLPWHCLWR (in isoform 2).
FT /FTId=VSP_042844.
SQ SEQUENCE 56 AA; 6677 MW; 41325122B493EFF9 CRC64;
MGHQQLYWSH PRKFGQGSRS CRVCSNRHGL IRKYGLNMCR QCFRQYAKDI GFIKLD
//
MIM
603633
*RECORD*
*FIELD* NO
603633
*FIELD* TI
*603633 RIBOSOMAL PROTEIN S29; RPS29
*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; 603631), S10 (RPS10; 603632), S29 (RPS29), 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 56-amino acid human RPS29 is
identical to rat Rps29. Northern blot analysis suggested variable
expression of RPS29 in colorectal cancers compared to adjacent normal
tissues, although no correlation between the level of expression and the
severity of the disease was found.
Kondoh et al. (1996) isolated RPS29 cDNAs by differential hybridization
screening of a human colon carcinoma cDNA library with probes derived
from a colon carcinoma cell line (HT29) and a differentiated subclone (C
III). Northern blot analysis detected higher levels of the 0.3-kb RPS29
transcript in the undifferentiated HT29 cells compared to the
differentiated C III cells, and in growth-arrested HT29 cells compared
to rapidly proliferating HT29 cells. RPS29 has a zinc finger-like domain
that can bind zinc. The authors demonstrated that RPS29 can enhance the
tumor suppressor activity of KREV1 (179520).
By somatic cell hybrid and radiation hybrid mapping analyses, Kenmochi
et al. (1998) mapped the human RPS29 gene to 14q.
*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.
4. Kondoh, N.; Noda, M.; Fisher, R. J.; Schweinfest, C. W.; Papas,
T. S.; Kondoh, A.; Samuel, K. P.; Oikawa, T.: The S29 ribosomal protein
increases tumor suppressor activity of Krev-1 gene on v-Kras-transformed
NIH3T3 cells. Biochim. Biophys. Acta 1313: 41-46, 1996.
*FIELD* CD
Patti M. Sherman: 3/12/1999
*FIELD* ED
carol: 03/19/1999
carol: 3/19/1999
psherman: 3/16/1999
*RECORD*
*FIELD* NO
603633
*FIELD* TI
*603633 RIBOSOMAL PROTEIN S29; RPS29
*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; 603631), S10 (RPS10; 603632), S29 (RPS29), 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 56-amino acid human RPS29 is
identical to rat Rps29. Northern blot analysis suggested variable
expression of RPS29 in colorectal cancers compared to adjacent normal
tissues, although no correlation between the level of expression and the
severity of the disease was found.
Kondoh et al. (1996) isolated RPS29 cDNAs by differential hybridization
screening of a human colon carcinoma cDNA library with probes derived
from a colon carcinoma cell line (HT29) and a differentiated subclone (C
III). Northern blot analysis detected higher levels of the 0.3-kb RPS29
transcript in the undifferentiated HT29 cells compared to the
differentiated C III cells, and in growth-arrested HT29 cells compared
to rapidly proliferating HT29 cells. RPS29 has a zinc finger-like domain
that can bind zinc. The authors demonstrated that RPS29 can enhance the
tumor suppressor activity of KREV1 (179520).
By somatic cell hybrid and radiation hybrid mapping analyses, Kenmochi
et al. (1998) mapped the human RPS29 gene to 14q.
*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.
4. Kondoh, N.; Noda, M.; Fisher, R. J.; Schweinfest, C. W.; Papas,
T. S.; Kondoh, A.; Samuel, K. P.; Oikawa, T.: The S29 ribosomal protein
increases tumor suppressor activity of Krev-1 gene on v-Kras-transformed
NIH3T3 cells. Biochim. Biophys. Acta 1313: 41-46, 1996.
*FIELD* CD
Patti M. Sherman: 3/12/1999
*FIELD* ED
carol: 03/19/1999
carol: 3/19/1999
psherman: 3/16/1999