RS29_MOUSE
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 03-AUG-2022, entry version 143.
DE RecName: 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).
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:0000250|UniProtKB:Q6QAP6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P62273}. Cytoplasm
CC {ECO:0000250|UniProtKB:P62273}. 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 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; P62274; -.
DR PeptideAtlas; P62274; -.
DR PRIDE; P62274; -.
DR ProteomicsDB; 260856; -.
DR DNASU; 20090; -.
DR Ensembl; ENSMUST00000037023; ENSMUSP00000038352; ENSMUSG00000034892.
DR GeneID; 20090; -.
DR KEGG; mmu:20090; -.
DR UCSC; uc007nrp.2; mouse.
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; 1635465at2759; -.
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 62 CRISPR screens.
DR ChiTaRS; Rps29; mouse.
DR PRO; PR:P62274; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P62274; protein.
DR Bgee; ENSMUSG00000034892; Expressed in ectoplacental cone and 61 other tissues.
DR Genevisible; P62274; MM.
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; ISS:UniProtKB.
DR GO; GO:0042788; C:polysomal ribosome; ISS:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0002181; P:cytoplasmic translation; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0006412; P:translation; ISO:MGI.
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; Cytoplasm; Endoplasmic reticulum; Metal-binding;
KW Methylation; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Zinc.
FT CHAIN 1..56
FT /note="40S ribosomal protein S29"
FT /id="PRO_0000131020"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
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
