RL30_MOUSE
ID RL30_MOUSE Reviewed; 115 AA.
AC P62889; P04645;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=60S ribosomal protein L30;
GN Name=Rpl30;
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.
RX PubMed=6513928; DOI=10.1128/mcb.4.11.2518-2528.1984;
RA Wiedemann L.M., Perry R.P.;
RT "Characterization of the expressed gene and several processed pseudogenes
RT for the mouse ribosomal protein L30 gene family.";
RL Mol. Cell. Biol. 4:2518-2528(1984).
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 STRAIN=FVB/N; TISSUE=Kidney, and Mammary tumor;
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 IDENTIFICATION BY 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:P62888}.
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000250|UniProtKB:P62888}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62888}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL30 family.
CC {ECO:0000305}.
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DR EMBL; K02928; AAA03645.1; -; Unassigned_DNA.
DR EMBL; AK002988; BAB22500.1; -; mRNA.
DR EMBL; BC002060; AAH02060.1; -; mRNA.
DR EMBL; BC086890; AAH86890.1; -; mRNA.
DR CCDS; CCDS37057.1; -.
DR PIR; S11622; R6MS30.
DR RefSeq; NP_001156957.1; NM_001163485.1.
DR RefSeq; NP_033109.1; NM_009083.4.
DR PDB; 6SWA; EM; 3.10 A; a=1-115.
DR PDB; 7CPU; EM; 2.82 A; Lc=1-115.
DR PDB; 7CPV; EM; 3.03 A; Lc=1-115.
DR PDB; 7LS1; EM; 3.30 A; W2=1-115.
DR PDB; 7LS2; EM; 3.10 A; W2=1-115.
DR PDBsum; 6SWA; -.
DR PDBsum; 7CPU; -.
DR PDBsum; 7CPV; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P62889; -.
DR SMR; P62889; -.
DR BioGRID; 202978; 89.
DR ComplexPortal; CPX-5262; 60S cytosolic large ribosomal subunit.
DR IntAct; P62889; 7.
DR MINT; P62889; -.
DR STRING; 10090.ENSMUSP00000106014; -.
DR iPTMnet; P62889; -.
DR PhosphoSitePlus; P62889; -.
DR SwissPalm; P62889; -.
DR EPD; P62889; -.
DR jPOST; P62889; -.
DR PaxDb; P62889; -.
DR PeptideAtlas; P62889; -.
DR PRIDE; P62889; -.
DR ProteomicsDB; 253307; -.
DR Antibodypedia; 1242; 270 antibodies from 31 providers.
DR DNASU; 19946; -.
DR Ensembl; ENSMUST00000009039; ENSMUSP00000009039; ENSMUSG00000058600.
DR Ensembl; ENSMUST00000079735; ENSMUSP00000106014; ENSMUSG00000058600.
DR GeneID; 19946; -.
DR KEGG; mmu:19946; -.
DR UCSC; uc007vlq.2; mouse.
DR CTD; 6156; -.
DR MGI; MGI:98037; Rpl30.
DR VEuPathDB; HostDB:ENSMUSG00000058600; -.
DR eggNOG; KOG2988; Eukaryota.
DR GeneTree; ENSGT00390000012138; -.
DR HOGENOM; CLU_130502_0_1_1; -.
DR InParanoid; P62889; -.
DR OMA; RPHKIMA; -.
DR OrthoDB; 1503991at2759; -.
DR PhylomeDB; P62889; -.
DR TreeFam; TF300252; -.
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; 19946; 20 hits in 59 CRISPR screens.
DR ChiTaRS; Rpl30; mouse.
DR PRO; PR:P62889; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P62889; protein.
DR Bgee; ENSMUSG00000058600; Expressed in ectoplacental cone and 198 other tissues.
DR ExpressionAtlas; P62889; baseline and differential.
DR Genevisible; P62889; MM.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IPI:ComplexPortal.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0042788; C:polysomal ribosome; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0005840; C:ribosome; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0035368; F:selenocysteine insertion sequence binding; ISO:MGI.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; ISO:MGI.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISO:MGI.
DR GO; GO:0031640; P:killing of cells of another organism; ISO:MGI.
DR Gene3D; 3.30.1330.30; -; 1.
DR HAMAP; MF_00481; Ribosomal_L30e; 1.
DR InterPro; IPR039109; L30/L30e/YlxQ.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR000231; Ribosomal_L30e.
DR InterPro; IPR022991; Ribosomal_L30e_CS.
DR InterPro; IPR004038; Ribosomal_L7Ae/L30e/S12e/Gad45.
DR PANTHER; PTHR11449; PTHR11449; 1.
DR PANTHER; PTHR11449:SF12; PTHR11449:SF12; 1.
DR Pfam; PF01248; Ribosomal_L7Ae; 1.
DR SUPFAM; SSF55315; SSF55315; 1.
DR PROSITE; PS00709; RIBOSOMAL_L30E_1; 1.
DR PROSITE; PS00993; RIBOSOMAL_L30E_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT CHAIN 1..115
FT /note="60S ribosomal protein L30"
FT /id="PRO_0000146122"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62888"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62888"
FT MOD_RES 26
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62888"
FT CROSSLNK 26
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62888"
SQ SEQUENCE 115 AA; 12784 MW; 95186B081E39748C CRC64;
MVAAKKTKKS LESINSRLQL VMKSGKYVLG YKQTLKMIRQ GKAKLVILAN NCPALRKSEI
EYYAMLAKTG VHHYSGNNIE LGTACGKYYR VCTLAIIDPG DSDIIRSMPE QTGEK
