ID   RS29_MOUSE              Reviewed;          56 AA.
AC   P62274; P30054;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 152.
DE   RecName: Full=Small ribosomal subunit protein uS14 {ECO:0000305};
DE   AltName: Full=40S ribosomal protein S29;
GN   Name=Rps29;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon, and Mammary gland;
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   [4]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-12, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryo;
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   [5] {ECO:0007744|PDB:7CPU, ECO:0007744|PDB:7CPV}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.03 ANGSTROMS) OF RIBOSOME, FUNCTION,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=36517592; DOI=10.1038/s41586-022-05508-0;
RA   Li H., Huo Y., He X., Yao L., Zhang H., Cui Y., Xiao H., Xie W., Zhang D.,
RA   Wang Y., Zhang S., Tu H., Cheng Y., Guo Y., Cao X., Zhu Y., Jiang T.,
RA   Guo X., Qin Y., Sha J.;
RT   "A male germ-cell-specific ribosome controls male fertility.";
RL   Nature 0:0-0(2022).
CC   -!- FUNCTION: Component of the small ribosomal subunit (PubMed:36517592).
CC       The ribosome is a large ribonucleoprotein complex responsible for the
CC       synthesis of proteins in the cell (PubMed:36517592).
CC       {ECO:0000269|PubMed:36517592}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P62273};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P62273};
CC   -!- SUBUNIT: Component of the 40S small ribosomal subunit.
CC       {ECO:0000269|PubMed:36517592}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P62273}. Cytoplasm
CC       {ECO:0000269|PubMed:36517592}. Rough endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:Q6QAP6}. Note=Detected on cytosolic polysomes
CC       (By similarity). Detected in ribosomes that are associated with the
CC       rough endoplasmic reticulum (By similarity).
CC       {ECO:0000250|UniProtKB:P62273, ECO:0000250|UniProtKB:Q6QAP6}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS14 family.
CC       {ECO:0000305}.
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DR   EMBL; L31609; AAB27429.1; -; mRNA.
DR   EMBL; AK002939; BAB22469.1; -; mRNA.
DR   EMBL; AK012285; BAB28143.1; -; mRNA.
DR   EMBL; BC024393; AAH24393.1; -; mRNA.
DR   EMBL; BC051203; AAH51203.1; -; mRNA.
DR   CCDS; CCDS36461.1; -.
DR   PIR; S71578; S71578.
DR   RefSeq; NP_033119.1; NM_009093.2.
DR   PDB; 7CPU; EM; 2.82 A; Sd=1-56.
DR   PDB; 7CPV; EM; 3.03 A; Sd=1-56.
DR   PDB; 7LS1; EM; 3.30 A; H3=1-56.
DR   PDB; 7LS2; EM; 3.10 A; H3=1-56.
DR   PDBsum; 7CPU; -.
DR   PDBsum; 7CPV; -.
DR   PDBsum; 7LS1; -.
DR   PDBsum; 7LS2; -.
DR   AlphaFoldDB; P62274; -.
DR   EMDB; EMD-23500; -.
DR   EMDB; EMD-23501; -.
DR   EMDB; EMD-30432; -.
DR   EMDB; EMD-30433; -.
DR   SMR; P62274; -.
DR   BioGRID; 203009; 7.
DR   ComplexPortal; CPX-5261; 40S cytosolic small ribosomal subunit.
DR   IntAct; P62274; 2.
DR   STRING; 10090.ENSMUSP00000038352; -.
DR   iPTMnet; P62274; -.
DR   PhosphoSitePlus; P62274; -.
DR   SwissPalm; P62274; -.
DR   EPD; P62274; -.
DR   jPOST; P62274; -.
DR   MaxQB; P62274; -.
DR   PaxDb; 10090-ENSMUSP00000038352; -.
DR   PeptideAtlas; P62274; -.
DR   ProteomicsDB; 260856; -.
DR   Pumba; P62274; -.
DR   DNASU; 20090; -.
DR   Ensembl; ENSMUST00000037023.9; ENSMUSP00000038352.9; ENSMUSG00000034892.9.
DR   GeneID; 20090; -.
DR   KEGG; mmu:20090; -.
DR   UCSC; uc007nrp.2; mouse.
DR   AGR; MGI:107681; -.
DR   CTD; 6235; -.
DR   MGI; MGI:107681; Rps29.
DR   VEuPathDB; HostDB:ENSMUSG00000034892; -.
DR   eggNOG; KOG3506; Eukaryota.
DR   GeneTree; ENSGT00940000154720; -.
DR   HOGENOM; CLU_177289_1_1_1; -.
DR   InParanoid; P62274; -.
DR   OMA; HCFREIA; -.
DR   OrthoDB; 5476442at2759; -.
DR   PhylomeDB; P62274; -.
DR   TreeFam; TF300217; -.
DR   Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-MMU-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR   Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   Reactome; R-MMU-72649; Translation initiation complex formation.
DR   Reactome; R-MMU-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-MMU-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR   Reactome; R-MMU-72702; Ribosomal scanning and start codon recognition.
DR   Reactome; R-MMU-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR   Reactome; R-MMU-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR   Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   BioGRID-ORCS; 20090; 30 hits in 63 CRISPR screens.
DR   ChiTaRS; Rps29; mouse.
DR   PRO; PR:P62274; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; P62274; Protein.
DR   Bgee; ENSMUSG00000034892; Expressed in mesodermal cell in embryo and 64 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; NAS: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:0042788; C:polysomal ribosome; ISO:MGI.
DR   GO; GO:0005840; C:ribosome; ISS:UniProtKB.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0002181; P:cytoplasmic translation; ISS:UniProtKB.
DR   GO; GO:0006412; P:translation; ISO:MGI.
DR   InterPro; IPR001209; Ribosomal_uS14.
DR   InterPro; IPR018271; Ribosomal_uS14_CS.
DR   InterPro; IPR039744; RIbosomal_uS14_euk_arc.
DR   InterPro; IPR043140; Ribosomal_uS14_sf.
DR   PANTHER; PTHR12010; 40S RIBOSOMAL PROTEIN S29; 1.
DR   PANTHER; PTHR12010:SF2; 40S RIBOSOMAL PROTEIN S29; 1.
DR   Pfam; PF00253; Ribosomal_S14; 1.
DR   PROSITE; PS00527; RIBOSOMAL_S14; 1.
DR   Genevisible; P62274; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Endoplasmic reticulum; Metal-binding;
KW   Methylation; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; Zinc.
FT   CHAIN           1..56
FT                   /note="Small ribosomal subunit protein uS14"
FT                   /id="PRO_0000131020"
FT   BINDING         21
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P62273"
FT   BINDING         24
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P62273"
FT   BINDING         39
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P62273"
FT   BINDING         42
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P62273"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62273"
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:0000250|UniProtKB:P62273"
SQ   SEQUENCE   56 AA;  6677 MW;  41325122B493EFF9 CRC64;
     MGHQQLYWSH PRKFGQGSRS CRVCSNRHGL IRKYGLNMCR QCFRQYAKDI GFIKLD
//