RS14_MOUSE
ID RS14_MOUSE Reviewed; 151 AA.
AC P62264; P06366; Q544W4;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=40S ribosomal protein S14;
GN Name=Rps14;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Kidney, and Pancreas;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N-3; TISSUE=Brain, 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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS11 family.
CC {ECO:0000305}.
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DR EMBL; AK003148; BAB22604.1; -; mRNA.
DR EMBL; AK011213; BAB27472.1; -; mRNA.
DR EMBL; AK012425; BAB28230.1; -; mRNA.
DR EMBL; AK012584; BAB28334.1; -; mRNA.
DR EMBL; AK019233; BAB31615.1; -; mRNA.
DR EMBL; AK028106; BAC25751.1; -; mRNA.
DR EMBL; AK146976; BAE27580.1; -; mRNA.
DR EMBL; AK168237; BAE40187.1; -; mRNA.
DR EMBL; BC042940; AAH42940.1; -; mRNA.
DR EMBL; BC081449; AAH81449.1; -; mRNA.
DR EMBL; BC062874; AAH62874.1; -; mRNA.
DR CCDS; CCDS29274.1; -.
DR RefSeq; NP_065625.2; NM_020600.4.
DR PDB; 7CPU; EM; 2.82 A; SO=1-151.
DR PDB; 7CPV; EM; 3.03 A; SO=1-151.
DR PDB; 7LS1; EM; 3.30 A; O3=1-151.
DR PDB; 7LS2; EM; 3.10 A; O3=1-151.
DR PDBsum; 7CPU; -.
DR PDBsum; 7CPV; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P62264; -.
DR SMR; P62264; -.
DR BioGRID; 203002; 122.
DR ComplexPortal; CPX-5261; 40S cytosolic small ribosomal subunit.
DR IntAct; P62264; 5.
DR MINT; P62264; -.
DR STRING; 10090.ENSMUSP00000025511; -.
DR iPTMnet; P62264; -.
DR PhosphoSitePlus; P62264; -.
DR SwissPalm; P62264; -.
DR EPD; P62264; -.
DR jPOST; P62264; -.
DR MaxQB; P62264; -.
DR PaxDb; P62264; -.
DR PRIDE; P62264; -.
DR ProteomicsDB; 260845; -.
DR TopDownProteomics; P62264; -.
DR Antibodypedia; 1243; 266 antibodies from 29 providers.
DR DNASU; 20044; -.
DR Ensembl; ENSMUST00000025511; ENSMUSP00000025511; ENSMUSG00000024608.
DR Ensembl; ENSMUST00000118551; ENSMUSP00000113081; ENSMUSG00000024608.
DR Ensembl; ENSMUST00000122279; ENSMUSP00000113504; ENSMUSG00000024608.
DR Ensembl; ENSMUST00000235603; ENSMUSP00000157948; ENSMUSG00000024608.
DR Ensembl; ENSMUST00000235966; ENSMUSP00000158138; ENSMUSG00000024608.
DR GeneID; 20044; -.
DR KEGG; mmu:20044; -.
DR UCSC; uc008fay.2; mouse.
DR CTD; 6208; -.
DR MGI; MGI:98107; Rps14.
DR VEuPathDB; HostDB:ENSMUSG00000024608; -.
DR eggNOG; KOG0407; Eukaryota.
DR GeneTree; ENSGT00390000000703; -.
DR HOGENOM; CLU_072439_6_0_1; -.
DR InParanoid; P62264; -.
DR OMA; KWGVAHI; -.
DR OrthoDB; 1408000at2759; -.
DR PhylomeDB; P62264; -.
DR TreeFam; TF300125; -.
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; 20044; 25 hits in 67 CRISPR screens.
DR ChiTaRS; Rps14; mouse.
DR PRO; PR:P62264; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; P62264; protein.
DR Bgee; ENSMUSG00000024608; Expressed in medial ganglionic eminence and 249 other tissues.
DR ExpressionAtlas; P62264; baseline and differential.
DR Genevisible; P62264; MM.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:MGI.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:0045182; F:translation regulator activity; ISO:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0030218; P:erythrocyte differentiation; ISO:MGI.
DR GO; GO:0030490; P:maturation of SSU-rRNA; ISS:UniProtKB.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0000028; P:ribosomal small subunit assembly; ISS:UniProtKB.
DR GO; GO:0006412; P:translation; ISO:MGI.
DR Gene3D; 3.30.420.80; -; 1.
DR HAMAP; MF_01310; Ribosomal_S11; 1.
DR InterPro; IPR001971; Ribosomal_S11.
DR InterPro; IPR018102; Ribosomal_S11_CS.
DR InterPro; IPR036967; Ribosomal_S11_sf.
DR PANTHER; PTHR11759; PTHR11759; 1.
DR Pfam; PF00411; Ribosomal_S11; 1.
DR PIRSF; PIRSF002131; Ribosomal_S11; 1.
DR PROSITE; PS00054; RIBOSOMAL_S11; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isopeptide bond; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT CHAIN 1..151
FT /note="40S ribosomal protein S14"
FT /id="PRO_0000123338"
FT REGION 131..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62263"
FT MOD_RES 133
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P62263"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 61
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P62263"
FT CROSSLNK 63
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P62263"
FT CROSSLNK 106
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P62263"
SQ SEQUENCE 151 AA; 16273 MW; 4F4387F9FADAC278 CRC64;
MAPRKGKEKK EEQVISLGPQ VAEGENVFGV CHIFASFNDT FVHVTDLSGK ETICRVTGGM
KVKADRDESS PYAAMLAAQD VAQRCKELGI TALHIKLRAT GGNRTKTPGP GAQSALRALA
RSGMKIGRIE DVTPIPSDST RRKGGRRGRR L
