RL18_MOUSE
ID RL18_MOUSE Reviewed; 188 AA.
AC P35980; Q9CQF1; Q9D987;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=60S ribosomal protein L18;
GN Name=Rpl18;
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=C57BL/6 X CBA; TISSUE=Lung;
RX PubMed=8359697; DOI=10.1016/0378-1119(93)90433-4;
RA Hou E.W., Li S.S.L.;
RT "Sequence analysis of mouse cDNAs encoding ribosomal proteins L12 and
RT L18.";
RL Gene 130:287-290(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Testis, and Tongue;
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 STRAIN=FVB/N-3; TISSUE=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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, 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 -!- FUNCTION: Component of the large ribosomal subunit. The ribosome is a
CC large ribonucleoprotein complex responsible for the synthesis of
CC proteins in the cell. {ECO:0000250|UniProtKB:Q07020}.
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000250|UniProtKB:Q07020}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q07020}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q07020}. Rough endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q95342}. 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:Q07020, ECO:0000250|UniProtKB:Q95342}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL18 family.
CC {ECO:0000305}.
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DR EMBL; L04128; AAA40067.1; -; mRNA.
DR EMBL; AK007263; BAB24923.1; -; mRNA.
DR EMBL; AK009044; BAB26043.1; -; mRNA.
DR EMBL; AK010510; BAB26993.1; -; mRNA.
DR EMBL; AK012580; BAB28332.1; -; mRNA.
DR EMBL; BC082290; AAH82290.1; -; mRNA.
DR CCDS; CCDS39958.1; -.
DR PIR; JN0779; JN0779.
DR RefSeq; NP_033103.2; NM_009077.2.
DR PDB; 6SWA; EM; 3.10 A; P=1-188.
DR PDB; 7CPU; EM; 2.82 A; LQ=1-188.
DR PDB; 7CPV; EM; 3.03 A; LQ=1-188.
DR PDB; 7LS1; EM; 3.30 A; K2=1-188.
DR PDB; 7LS2; EM; 3.10 A; K2=1-188.
DR PDBsum; 6SWA; -.
DR PDBsum; 7CPU; -.
DR PDBsum; 7CPV; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P35980; -.
DR SMR; P35980; -.
DR BioGRID; 202968; 86.
DR ComplexPortal; CPX-5262; 60S cytosolic large ribosomal subunit.
DR CORUM; P35980; -.
DR IntAct; P35980; 4.
DR MINT; P35980; -.
DR STRING; 10090.ENSMUSP00000103365; -.
DR iPTMnet; P35980; -.
DR PhosphoSitePlus; P35980; -.
DR SwissPalm; P35980; -.
DR EPD; P35980; -.
DR jPOST; P35980; -.
DR PaxDb; P35980; -.
DR PeptideAtlas; P35980; -.
DR PRIDE; P35980; -.
DR ProteomicsDB; 254890; -.
DR DNASU; 19899; -.
DR Ensembl; ENSMUST00000072503; ENSMUSP00000072320; ENSMUSG00000059070.
DR Ensembl; ENSMUST00000210640; ENSMUSP00000147816; ENSMUSG00000059070.
DR GeneID; 19899; -.
DR KEGG; mmu:19899; -.
DR UCSC; uc009gww.1; mouse.
DR CTD; 6141; -.
DR MGI; MGI:98003; Rpl18.
DR VEuPathDB; HostDB:ENSMUSG00000059070; -.
DR eggNOG; KOG1714; Eukaryota.
DR GeneTree; ENSGT00390000012976; -.
DR HOGENOM; CLU_080024_0_0_1; -.
DR InParanoid; P35980; -.
DR OMA; MSKIHRP; -.
DR OrthoDB; 1303996at2759; -.
DR PhylomeDB; P35980; -.
DR TreeFam; TF300202; -.
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-72689; Formation of a pool of free 40S subunits.
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; 19899; 26 hits in 51 CRISPR screens.
DR ChiTaRS; Rpl18; mouse.
DR PRO; PR:P35980; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P35980; protein.
DR Bgee; ENSMUSG00000059070; Expressed in epiblast (generic) and 64 other tissues.
DR ExpressionAtlas; P35980; baseline and differential.
DR Genevisible; P35980; MM.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IPI:ComplexPortal.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0042788; C:polysomal ribosome; ISS:UniProtKB.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; ISS:UniProtKB.
DR InterPro; IPR036227; L18e/L15P_sf.
DR InterPro; IPR021132; Ribosomal_L18/L18-A/B/e_CS.
DR InterPro; IPR000039; Ribosomal_L18e.
DR InterPro; IPR021131; Ribosomal_L18e/L15P.
DR PANTHER; PTHR10934; PTHR10934; 1.
DR Pfam; PF17135; Ribosomal_L18; 1.
DR SUPFAM; SSF52080; SSF52080; 1.
DR PROSITE; PS01106; RIBOSOMAL_L18E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endoplasmic reticulum; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT CHAIN 1..188
FT /note="60S ribosomal protein L18"
FT /id="PRO_0000132770"
FT REGION 150..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..188
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 158
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07020"
FT CROSSLNK 119
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q07020"
FT CROSSLNK 164
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q07020"
FT CONFLICT 59
FT /note="P -> S (in Ref. 1; AAA40067)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="A -> V (in Ref. 1; AAA40067)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="K -> R (in Ref. 2; BAB24923)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="A -> G (in Ref. 1; AAA40067)"
FT /evidence="ECO:0000305"
FT CONFLICT 147..150
FT /note="EVYR -> DVFP (in Ref. 1; AAA40067)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="A -> V (in Ref. 1; AAA40067)"
FT /evidence="ECO:0000305"
FT CONFLICT 160..162
FT /note="HSH -> YSQ (in Ref. 1; AAA40067)"
FT /evidence="ECO:0000305"
FT CONFLICT 173..174
FT /note="KF -> RL (in Ref. 1; AAA40067)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 188 AA; 21645 MW; 9489EFE201ABF7A1 CRC64;
MGVDIRHNKD RKVRRKEPKS QDIYLRLLVK LYRFLARRTN STFNQVVLKR LFMSRTNRPP
LSLSRMIRKM KLPGRENKTA VVVGTVTDDV RILEVPKLKV CALRVSSRAR SRILKAGGKI
LTFDQLALES PKGRGTVLLS GPRKGREVYR HFGKAPGTPH SHTKPYVRSK GRKFERARGR
RASRGYKN
