RL10_MOUSE
ID RL10_MOUSE Reviewed; 214 AA.
AC Q6ZWV3; P45634; Q569M8; Q5M9K8;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=60S ribosomal protein L10 {ECO:0000305};
DE AltName: Full=Protein QM homolog;
DE AltName: Full=Ribosomal protein L10 {ECO:0000312|MGI:MGI:105943};
GN Name=Rpl10 {ECO:0000312|MGI:MGI:105943}; Synonyms=Qm;
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 TISSUE=Adipocyte;
RX PubMed=8250879; DOI=10.1006/bbrc.1993.2383;
RA Eisinger D.P., Jiang H.P., Serrero G.;
RT "A novel mouse gene highly conserved throughout evolution: regulation in
RT adipocyte differentiation and in tumorigenic cell lines.";
RL Biochem. Biophys. Res. Commun. 196:1227-1232(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RA Raj N.B.K., Su Y., Au W.C., Pitha P.M.;
RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, DBA/2J, and NOD;
RC TISSUE=Blastula, Bone marrow macrophage, Embryo, Embryonic head,
RC Embryonic heart, Embryonic liver, Lung, Morula, and Thymus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, FVB/N, and FVB/N-3;
RC TISSUE=Brain, Colon, Liver, Mammary tumor, and Thyroid;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC and Spleen;
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).
RN [7]
RP CITRULLINATION AT ARG-32.
RX PubMed=24463520; DOI=10.1038/nature12942;
RA Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S.,
RA Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C.,
RA Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.;
RT "Citrullination regulates pluripotency and histone H1 binding to
RT chromatin.";
RL Nature 507:104-108(2014).
RN [8]
RP UFMYLATION.
RX PubMed=28575669; DOI=10.1016/j.cell.2017.05.022;
RA Simsek D., Tiu G.C., Flynn R.A., Byeon G.W., Leppek K., Xu A.F.,
RA Chang H.Y., Barna M.;
RT "The mammalian ribo-interactome reveals ribosome functional diversity and
RT heterogeneity.";
RL Cell 169:1051-1065(2017).
CC -!- FUNCTION: Component of the large ribosomal subunit. Plays a role in the
CC formation of actively translating ribosomes. May play a role in the
CC embryonic brain development. {ECO:0000250|UniProtKB:P27635}.
CC -!- SUBUNIT: Component of the large ribosomal subunit. Mature ribosomes
CC consist of a small (40S) and a large (60S) subunit. The 40S subunit
CC contains about 33 different proteins and 1 molecule of RNA (18S). The
CC 60S subunit contains about 49 different proteins and 3 molecules of RNA
CC (28S, 5.8S and 5S). {ECO:0000250|UniProtKB:P27635}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
CC -!- PTM: Ufmylated by UFL1. {ECO:0000269|PubMed:28575669}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL16 family.
CC {ECO:0000305}.
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DR EMBL; M93980; AAA16894.1; -; mRNA.
DR EMBL; X75312; CAA53061.1; -; mRNA.
DR EMBL; AK011022; BAB27339.1; -; mRNA.
DR EMBL; AK012561; BAB28316.1; -; mRNA.
DR EMBL; AK014054; BAB29134.1; -; mRNA.
DR EMBL; AK088777; BAC40566.1; -; mRNA.
DR EMBL; AK144831; BAE26087.1; -; mRNA.
DR EMBL; AK146217; BAE26985.1; -; mRNA.
DR EMBL; AK151416; BAE30381.1; -; mRNA.
DR EMBL; AK151655; BAE30584.1; -; mRNA.
DR EMBL; AK151736; BAE30650.1; -; mRNA.
DR EMBL; AK152123; BAE30965.1; -; mRNA.
DR EMBL; AK152854; BAE31547.1; -; mRNA.
DR EMBL; AK153345; BAE31921.1; -; mRNA.
DR EMBL; AK160618; BAE35918.1; -; mRNA.
DR EMBL; AK166610; BAE38892.1; -; mRNA.
DR EMBL; AK167239; BAE39361.1; -; mRNA.
DR EMBL; AK167966; BAE39963.1; -; mRNA.
DR EMBL; AK168854; BAE40675.1; -; mRNA.
DR EMBL; CH466519; EDL27744.1; -; Genomic_DNA.
DR EMBL; CH466650; EDL29836.1; -; Genomic_DNA.
DR EMBL; BC024901; AAH24901.1; -; mRNA.
DR EMBL; BC048872; AAH48872.1; -; mRNA.
DR EMBL; BC082293; AAH82293.1; -; mRNA.
DR EMBL; BC083327; AAH83327.1; -; mRNA.
DR EMBL; BC086917; AAH86917.1; -; mRNA.
DR EMBL; BC092383; AAH92383.1; -; mRNA.
DR EMBL; BC098204; AAH98204.1; -; mRNA.
DR EMBL; BC099437; AAH99437.1; -; mRNA.
DR CCDS; CCDS41019.1; -.
DR PIR; JC2013; JC2013.
DR RefSeq; NP_443067.1; NM_052835.3.
DR PDB; 6SWA; EM; 3.10 A; I=1-214.
DR PDB; 7CPU; EM; 2.82 A; LI=1-214.
DR PDBsum; 6SWA; -.
DR PDBsum; 7CPU; -.
DR AlphaFoldDB; Q6ZWV3; -.
DR SMR; Q6ZWV3; -.
DR BioGRID; 226050; 46.
DR IntAct; Q6ZWV3; 3.
DR MINT; Q6ZWV3; -.
DR STRING; 10090.ENSMUSP00000008826; -.
DR iPTMnet; Q6ZWV3; -.
DR PhosphoSitePlus; Q6ZWV3; -.
DR SwissPalm; Q6ZWV3; -.
DR EPD; Q6ZWV3; -.
DR jPOST; Q6ZWV3; -.
DR MaxQB; Q6ZWV3; -.
DR PaxDb; Q6ZWV3; -.
DR PeptideAtlas; Q6ZWV3; -.
DR PRIDE; Q6ZWV3; -.
DR ProteomicsDB; 253296; -.
DR TopDownProteomics; Q6ZWV3; -.
DR DNASU; 110954; -.
DR Ensembl; ENSMUST00000008826; ENSMUSP00000008826; ENSMUSG00000008682.
DR Ensembl; ENSMUST00000074085; ENSMUSP00000082055; ENSMUSG00000008682.
DR Ensembl; ENSMUST00000076364; ENSMUSP00000125806; ENSMUSG00000058443.
DR GeneID; 110954; -.
DR KEGG; mmu:110954; -.
DR UCSC; uc009toc.2; mouse.
DR CTD; 6134; -.
DR MGI; MGI:105943; Rpl10.
DR VEuPathDB; HostDB:ENSMUSG00000008682; -.
DR VEuPathDB; HostDB:ENSMUSG00000058443; -.
DR eggNOG; KOG0857; Eukaryota.
DR GeneTree; ENSGT00390000003897; -.
DR HOGENOM; CLU_084051_0_0_1; -.
DR InParanoid; Q6ZWV3; -.
DR OMA; NGQHAQE; -.
DR OrthoDB; 1215841at2759; -.
DR PhylomeDB; Q6ZWV3; -.
DR TreeFam; TF300082; -.
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; 110954; 23 hits in 73 CRISPR screens.
DR ChiTaRS; Rpl10; mouse.
DR PRO; PR:Q6ZWV3; -.
DR Proteomes; UP000000589; Chromosome 9.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q6ZWV3; protein.
DR Bgee; ENSMUSG00000008682; Expressed in epiblast (generic) and 79 other tissues.
DR ExpressionAtlas; Q6ZWV3; baseline and differential.
DR Genevisible; Q6ZWV3; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; ISS:UniProtKB.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0003735; F:structural constituent of ribosome; ISS:UniProtKB.
DR GO; GO:0045182; F:translation regulator activity; ISS:UniProtKB.
DR GO; GO:1990403; P:embryonic brain development; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR GO; GO:0006412; P:translation; ISO:MGI.
DR CDD; cd01433; Ribosomal_L16_L10e; 1.
DR Gene3D; 3.90.1170.10; -; 1.
DR InterPro; IPR001197; Ribosomal_L10e.
DR InterPro; IPR016180; Ribosomal_L10e/L16.
DR InterPro; IPR036920; Ribosomal_L10e/L16_sf.
DR InterPro; IPR018255; Ribosomal_L10e_CS.
DR PANTHER; PTHR11726; PTHR11726; 1.
DR Pfam; PF00252; Ribosomal_L16; 1.
DR PIRSF; PIRSF005590; Ribosomal_L10; 1.
DR SUPFAM; SSF54686; SSF54686; 1.
DR TIGRFAMs; TIGR00279; uL16_euk_arch; 1.
DR PROSITE; PS01257; RIBOSOMAL_L10E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Citrullination; Developmental protein; Isopeptide bond;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Translation regulation; Ubl conjugation.
FT CHAIN 1..214
FT /note="60S ribosomal protein L10"
FT /id="PRO_0000147107"
FT MOD_RES 32
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:24463520"
FT CROSSLNK 175
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P27635"
FT CROSSLNK 188
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P27635"
FT CONFLICT 150
FT /note="E -> G (in Ref. 5; AAH86917)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 214 AA; 24604 MW; 0860CECC91DF74FE CRC64;
MGRRPARCYR YCKNKPYPKS RFCRGVPDAK IRIFDLGRKK AKVDEFPLCG HMVSDEYEQL
SSEALEAARI CANKYMVKSC GKDGFHIRVR LHPFHVIRIN KMLSCAGADR LQTGMRGAFG
KPQGTVARVH IGQVIMSIRT KLQNKEHVIE ALRRAKFKFP GRQKIHISKK WGFTKFNADE
FEDMVAEKRL IPDGCGVKYI PNRGPLDKWR ALHS
