RS29_HUMAN
ID RS29_HUMAN Reviewed; 56 AA.
AC P62273; A8MZ73; P30054;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=40S ribosomal protein S29;
DE AltName: Full=Small ribosomal subunit protein uS14 {ECO:0000303|PubMed:24524803};
GN Name=RPS29;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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, S10
RT 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., Kondoh A.,
RA Samuel K.P., Oikawa T.;
RT "The S29 ribosomal protein increases tumor suppressor activity of K rev-1
RT 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 analysis of
RT 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., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., 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., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA 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 project:
RT 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., Egorov T.A.,
RA 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, AND
RP IDENTIFICATION BY 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; DOI=10.1101/gr.8.5.509;
RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J.,
RA 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 IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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., Buerckstuemmer T.,
RA 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
RN [13]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-12, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS), AND SUBUNIT.
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 [16] {ECO:0007744|PDB:5AJ0}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) IN COMPLEX WITH ZINC,
RP SUBCELLULAR LOCATION, SUBUNIT, AND COFACTOR.
RX PubMed=25957688; DOI=10.1016/j.cell.2015.03.052;
RA Behrmann E., Loerke J., Budkevich T.V., Yamamoto K., Schmidt A.,
RA Penczek P.A., Vos M.R., Burger J., Mielke T., Scheerer P., Spahn C.M.;
RT "Structural snapshots of actively translating human ribosomes.";
RL Cell 161:845-857(2015).
RN [17] {ECO:0007744|PDB:4UG0}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS).
RX PubMed=25901680; DOI=10.1038/nature14427;
RA Khatter H., Myasnikov A.G., Natchiar S.K., Klaholz B.P.;
RT "Structure of the human 80S ribosome.";
RL Nature 520:640-645(2015).
RN [18]
RP INVOLVEMENT IN DBA13, VARIANTS DBA13 PHE-31 AND THR-50, AND
RP CHARACTERIZATION OF VARIANTS DBA13 PHE-31 AND THR-50.
RX PubMed=24829207; DOI=10.1182/blood-2013-11-540278;
RA Mirabello L., Macari E.R., Jessop L., Ellis S.R., Myers T., Giri N.,
RA Taylor A.M., McGrath K.E., Humphries J.M., Ballew B.J., Yeager M.,
RA Boland J.F., He J., Hicks B.D., Burdett L., Alter B.P., Zon L.,
RA Savage S.A.;
RT "Whole-exome sequencing and functional studies identify RPS29 as a novel
RT gene mutated in multicase Diamond-Blackfan anemia families.";
RL Blood 124:24-32(2014).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:25957688};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:25957688};
CC -!- SUBUNIT: Component of the 40S small ribosomal subunit.
CC {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:25901680,
CC ECO:0000269|PubMed:25957688}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:25957688}.
CC Cytoplasm {ECO:0000305|PubMed:23636399, ECO:0000305|PubMed:25901680}.
CC Rough endoplasmic reticulum {ECO:0000250|UniProtKB:Q6QAP6}.
CC Note=Detected on cytosolic polysomes (PubMed:25957688). Detected in
CC ribosomes that are associated with the rough endoplasmic reticulum (By
CC similarity). {ECO:0000250|UniProtKB:Q6QAP6,
CC ECO:0000269|PubMed:25957688}.
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 -!- DISEASE: Diamond-Blackfan anemia 13 (DBA13) [MIM:615909]: A form of
CC Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic
CC anemia that usually presents early in infancy. Diamond-Blackfan anemia
CC is characterized by a moderate to severe macrocytic anemia,
CC erythroblastopenia, and an increased risk of malignancy. 30 to 40% of
CC Diamond-Blackfan anemia patients present with short stature and
CC congenital anomalies, the most frequent being craniofacial (Pierre-
CC Robin syndrome and cleft palate), thumb and urogenital anomalies.
CC {ECO:0000269|PubMed:24829207}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS14 family.
CC {ECO:0000305}.
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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 CCDS; CCDS32072.1; -. [P62273-2]
DR CCDS; CCDS9685.1; -. [P62273-1]
DR PIR; S55919; S55919.
DR RefSeq; NP_001023.1; NM_001032.4. [P62273-1]
DR RefSeq; NP_001025172.1; NM_001030001.2. [P62273-2]
DR PDB; 4UG0; EM; -; Sd=1-56.
DR PDB; 4V6X; EM; 5.00 A; Ad=1-56.
DR PDB; 5A2Q; EM; 3.90 A; d=2-56.
DR PDB; 5AJ0; EM; 3.50 A; Bd=1-56.
DR PDB; 5FLX; EM; 3.90 A; d=1-56.
DR PDB; 5LKS; EM; 3.60 A; Sd=1-56.
DR PDB; 5OA3; EM; 4.30 A; d=2-56.
DR PDB; 5T2C; EM; 3.60 A; AG=1-56.
DR PDB; 5VYC; X-ray; 6.00 A; d1/d2/d3/d4/d5/d6=1-56.
DR PDB; 6FEC; EM; 6.30 A; J=4-56.
DR PDB; 6G51; EM; 4.10 A; d=1-56.
DR PDB; 6G53; EM; 4.50 A; d=1-56.
DR PDB; 6G5H; EM; 3.60 A; d=1-56.
DR PDB; 6G5I; EM; 3.50 A; d=1-56.
DR PDB; 6IP5; EM; 3.90 A; 3E=1-56.
DR PDB; 6IP6; EM; 4.50 A; 3E=1-56.
DR PDB; 6IP8; EM; 3.90 A; 3E=1-56.
DR PDB; 6OLE; EM; 3.10 A; Sd=2-56.
DR PDB; 6OLF; EM; 3.90 A; Sd=2-56.
DR PDB; 6OLG; EM; 3.40 A; Bd=5-55.
DR PDB; 6OLI; EM; 3.50 A; Sd=2-56.
DR PDB; 6OLZ; EM; 3.90 A; Bd=5-55.
DR PDB; 6OM0; EM; 3.10 A; Sd=2-56.
DR PDB; 6OM7; EM; 3.70 A; Sd=2-56.
DR PDB; 6QZP; EM; 2.90 A; Sd=2-56.
DR PDB; 6XA1; EM; 2.80 A; Sd=2-56.
DR PDB; 6Y0G; EM; 3.20 A; Sd=1-56.
DR PDB; 6Y2L; EM; 3.00 A; Sd=1-56.
DR PDB; 6Y57; EM; 3.50 A; Sd=1-56.
DR PDB; 6YBS; EM; 3.10 A; i=1-56.
DR PDB; 6Z6L; EM; 3.00 A; Sd=1-56.
DR PDB; 6Z6M; EM; 3.10 A; Sd=1-56.
DR PDB; 6Z6N; EM; 2.90 A; Sd=1-56.
DR PDB; 6ZLW; EM; 2.60 A; f=1-56.
DR PDB; 6ZM7; EM; 2.70 A; Sd=1-56.
DR PDB; 6ZME; EM; 3.00 A; Sd=1-56.
DR PDB; 6ZMI; EM; 2.60 A; Sd=1-56.
DR PDB; 6ZMO; EM; 3.10 A; Sd=1-56.
DR PDB; 6ZMT; EM; 3.00 A; f=1-56.
DR PDB; 6ZMW; EM; 3.70 A; i=1-56.
DR PDB; 6ZN5; EM; 3.20 A; f=3-56.
DR PDB; 6ZOJ; EM; 2.80 A; d=2-56.
DR PDB; 6ZOL; EM; 2.80 A; d=2-56.
DR PDB; 6ZON; EM; 3.00 A; l=1-56.
DR PDB; 6ZP4; EM; 2.90 A; l=1-56.
DR PDB; 6ZUO; EM; 3.10 A; d=1-56.
DR PDB; 6ZV6; EM; 2.90 A; d=1-56.
DR PDB; 6ZVH; EM; 2.90 A; d=2-56.
DR PDB; 6ZVJ; EM; 3.80 A; l=2-55.
DR PDB; 6ZXD; EM; 3.20 A; d=1-56.
DR PDB; 6ZXE; EM; 3.00 A; d=1-56.
DR PDB; 6ZXF; EM; 3.70 A; d=1-56.
DR PDB; 6ZXG; EM; 2.60 A; d=1-56.
DR PDB; 6ZXH; EM; 2.70 A; d=1-56.
DR PDB; 7A09; EM; 3.50 A; l=1-56.
DR PDB; 7K5I; EM; 2.90 A; d=1-56.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5A2Q; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 5FLX; -.
DR PDBsum; 5LKS; -.
DR PDBsum; 5OA3; -.
DR PDBsum; 5T2C; -.
DR PDBsum; 5VYC; -.
DR PDBsum; 6FEC; -.
DR PDBsum; 6G51; -.
DR PDBsum; 6G53; -.
DR PDBsum; 6G5H; -.
DR PDBsum; 6G5I; -.
DR PDBsum; 6IP5; -.
DR PDBsum; 6IP6; -.
DR PDBsum; 6IP8; -.
DR PDBsum; 6OLE; -.
DR PDBsum; 6OLF; -.
DR PDBsum; 6OLG; -.
DR PDBsum; 6OLI; -.
DR PDBsum; 6OLZ; -.
DR PDBsum; 6OM0; -.
DR PDBsum; 6OM7; -.
DR PDBsum; 6QZP; -.
DR PDBsum; 6XA1; -.
DR PDBsum; 6Y0G; -.
DR PDBsum; 6Y2L; -.
DR PDBsum; 6Y57; -.
DR PDBsum; 6YBS; -.
DR PDBsum; 6Z6L; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR PDBsum; 6ZLW; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 6ZMT; -.
DR PDBsum; 6ZMW; -.
DR PDBsum; 6ZN5; -.
DR PDBsum; 6ZOJ; -.
DR PDBsum; 6ZOL; -.
DR PDBsum; 6ZON; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 6ZUO; -.
DR PDBsum; 6ZV6; -.
DR PDBsum; 6ZVH; -.
DR PDBsum; 6ZVJ; -.
DR PDBsum; 6ZXD; -.
DR PDBsum; 6ZXE; -.
DR PDBsum; 6ZXF; -.
DR PDBsum; 6ZXG; -.
DR PDBsum; 6ZXH; -.
DR PDBsum; 7A09; -.
DR PDBsum; 7K5I; -.
DR AlphaFoldDB; P62273; -.
DR SMR; P62273; -.
DR BioGRID; 112149; 138.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P62273; -.
DR IntAct; P62273; 39.
DR MINT; P62273; -.
DR STRING; 9606.ENSP00000379339; -.
DR iPTMnet; P62273; -.
DR PhosphoSitePlus; P62273; -.
DR SwissPalm; P62273; -.
DR BioMuta; RPS29; -.
DR DMDM; 50403626; -.
DR EPD; P62273; -.
DR jPOST; P62273; -.
DR MassIVE; P62273; -.
DR MaxQB; P62273; -.
DR PaxDb; P62273; -.
DR PeptideAtlas; P62273; -.
DR PRIDE; P62273; -.
DR ProteomicsDB; 57382; -. [P62273-1]
DR ProteomicsDB; 57383; -. [P62273-2]
DR TopDownProteomics; P62273-1; -. [P62273-1]
DR TopDownProteomics; P62273-2; -. [P62273-2]
DR Antibodypedia; 179; 87 antibodies from 22 providers.
DR DNASU; 6235; -.
DR Ensembl; ENST00000245458.11; ENSP00000245458.7; ENSG00000213741.11. [P62273-1]
DR Ensembl; ENST00000396020.7; ENSP00000379339.3; ENSG00000213741.11. [P62273-2]
DR Ensembl; ENST00000556230.2; ENSP00000495033.1; ENSG00000213741.11. [P62273-1]
DR GeneID; 6235; -.
DR KEGG; hsa:6235; -.
DR MANE-Select; ENST00000245458.11; ENSP00000245458.7; NM_001032.5; NP_001023.1.
DR UCSC; uc001wwl.5; human. [P62273-1]
DR CTD; 6235; -.
DR DisGeNET; 6235; -.
DR GeneCards; RPS29; -.
DR GeneReviews; RPS29; -.
DR HGNC; HGNC:10419; RPS29.
DR HPA; ENSG00000213741; Low tissue specificity.
DR MalaCards; RPS29; -.
DR MIM; 603633; gene.
DR MIM; 615909; phenotype.
DR neXtProt; NX_P62273; -.
DR OpenTargets; ENSG00000213741; -.
DR Orphanet; 124; Blackfan-Diamond anemia.
DR PharmGKB; PA34826; -.
DR VEuPathDB; HostDB:ENSG00000213741; -.
DR eggNOG; KOG3506; Eukaryota.
DR GeneTree; ENSGT00940000154720; -.
DR HOGENOM; CLU_177289_1_0_1; -.
DR InParanoid; P62273; -.
DR OMA; HCFREIA; -.
DR OrthoDB; 1635465at2759; -.
DR PhylomeDB; P62273; -.
DR TreeFam; TF300217; -.
DR PathwayCommons; P62273; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-156902; Peptide chain elongation.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-192823; Viral mRNA Translation.
DR Reactome; R-HSA-2408557; Selenocysteine synthesis.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-HSA-72649; Translation initiation complex formation.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-HSA-72764; Eukaryotic Translation Termination.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency.
DR Reactome; R-HSA-9754678; SARS-CoV-2 modulates host translation machinery.
DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P62273; -.
DR SIGNOR; P62273; -.
DR BioGRID-ORCS; 6235; 688 hits in 1044 CRISPR screens.
DR ChiTaRS; RPS29; human.
DR GeneWiki; RPS29; -.
DR GenomeRNAi; 6235; -.
DR Pharos; P62273; Tbio.
DR PRO; PR:P62273; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P62273; protein.
DR Bgee; ENSG00000213741; Expressed in caput epididymis and 203 other tissues.
DR ExpressionAtlas; P62273; baseline and differential.
DR Genevisible; P62273; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0098556; C:cytoplasmic side of rough endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0042788; C:polysomal ribosome; IDA:UniProtKB.
DR GO; GO:0015935; C:small ribosomal subunit; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0002181; P:cytoplasmic translation; IDA:UniProtKB.
DR GO; GO:0006412; P:translation; IC:UniProtKB.
DR Gene3D; 4.10.830.10; -; 1.
DR InterPro; IPR039744; 40S_S29/30S_S14z.
DR InterPro; IPR001209; Ribosomal_S14.
DR InterPro; IPR043140; Ribosomal_S14/S29.
DR InterPro; IPR018271; Ribosomal_S14_CS.
DR PANTHER; PTHR12010; PTHR12010; 1.
DR Pfam; PF00253; Ribosomal_S14; 1.
DR PROSITE; PS00527; RIBOSOMAL_S14; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Diamond-Blackfan anemia; Direct protein sequencing; Disease variant;
KW Endoplasmic reticulum; Metal-binding; Methylation; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8706699, ECO:0000269|Ref.7"
FT CHAIN 2..56
FT /note="40S ribosomal protein S29"
FT /id="PRO_0000131019"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:5A2Q, ECO:0007744|PDB:5AJ0"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:5A2Q, ECO:0007744|PDB:5AJ0,
FT ECO:0007744|PDB:5FLX, ECO:0007744|PDB:5LKS"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:5A2Q, ECO:0007744|PDB:5AJ0,
FT ECO:0007744|PDB:5FLX, ECO:0007744|PDB:5LKS"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:5A2Q, ECO:0007744|PDB:5AJ0,
FT ECO:0007744|PDB:5LKS"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 12
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 48
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 54..56
FT /note="KLD -> KKDLSCLPWHCLWR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042844"
FT VARIANT 31
FT /note="I -> F (in DBA13; results in reduced protein
FT expression; results in pre-rRNA processing defect;
FT dbSNP:rs587777568)"
FT /evidence="ECO:0000269|PubMed:24829207"
FT /id="VAR_071328"
FT VARIANT 50
FT /note="I -> T (in DBA13; results in reduced protein
FT expression; results in pre-rRNA processing defect;
FT dbSNP:rs587777569)"
FT /evidence="ECO:0000269|PubMed:24829207"
FT /id="VAR_071329"
FT TURN 4..6
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:6ZOJ"
SQ SEQUENCE 56 AA; 6677 MW; 41325122B493EFF9 CRC64;
MGHQQLYWSH PRKFGQGSRS CRVCSNRHGL IRKYGLNMCR QCFRQYAKDI GFIKLD
