ID   RL8_MOUSE               Reviewed;         257 AA.
AC   P62918; P25120; Q3V288;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Large ribosomal subunit protein uL2 {ECO:0000305};
DE   AltName: Full=60S ribosomal protein L8;
GN   Name=Rpl8;
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/6J;
RA   Rocha D., Carrier A., Victorero G., Mattei M.-G., Szatanik M.,
RA   Guenet J.-L., Jordan B.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Liver, 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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   INTERACTION WITH CRY1.
RX   PubMed=19129230; DOI=10.1093/nar/gkn1013;
RA   Hara Y., Onishi Y., Oishi K., Miyazaki K., Fukamizu A., Ishida N.;
RT   "Molecular characterization of Mybbp1a as a co-repressor on the Period2
RT   promoter.";
RL   Nucleic Acids Res. 37:1115-1126(2009).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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).
RN   [6] {ECO:0007744|PDB:7CPU, ECO:0007744|PDB:7CPV}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.03 ANGSTROMS) OF RIBOSOME, FUNCTION,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=36517592; DOI=10.1038/s41586-022-05508-0;
RA   Li H., Huo Y., He X., Yao L., Zhang H., Cui Y., Xiao H., Xie W., Zhang D.,
RA   Wang Y., Zhang S., Tu H., Cheng Y., Guo Y., Cao X., Zhu Y., Jiang T.,
RA   Guo X., Qin Y., Sha J.;
RT   "A male germ-cell-specific ribosome controls male fertility.";
RL   Nature 0:0-0(2022).
CC   -!- FUNCTION: Component of the large ribosomal subunit (PubMed:36517592).
CC       The ribosome is a large ribonucleoprotein complex responsible for the
CC       synthesis of proteins in the cell (PubMed:36517592).
CC       {ECO:0000269|PubMed:36517592}.
CC   -!- SUBUNIT: Component of the large ribosomal subunit (PubMed:36517592).
CC       Interacts with CRY1 (PubMed:19129230). {ECO:0000269|PubMed:19129230,
CC       ECO:0000269|PubMed:36517592}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:36517592}.
CC   -!- PTM: Hydroxylated on His-216 by RIOX1. The modification is impaired by
CC       hypoxia. {ECO:0000250|UniProtKB:P62917}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC       {ECO:0000305}.
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DR   EMBL; U67771; AAC35587.1; -; mRNA.
DR   EMBL; AK088263; BAC40244.1; -; mRNA.
DR   EMBL; AK131970; BAE20910.1; -; mRNA.
DR   EMBL; AK145498; BAE26472.1; -; mRNA.
DR   EMBL; AK167775; BAE39807.1; -; mRNA.
DR   EMBL; AK168769; BAE40605.1; -; mRNA.
DR   EMBL; BC043017; AAH43017.1; -; mRNA.
DR   CCDS; CCDS27595.1; -.
DR   RefSeq; NP_036183.1; NM_012053.2.
DR   PDB; 6SWA; EM; 3.10 A; A=1-257.
DR   PDB; 7CPU; EM; 2.82 A; LA=1-257.
DR   PDB; 7CPV; EM; 3.03 A; LA=1-257.
DR   PDB; 7LS1; EM; 3.30 A; D2=1-257.
DR   PDB; 7LS2; EM; 3.10 A; D2=1-257.
DR   PDBsum; 6SWA; -.
DR   PDBsum; 7CPU; -.
DR   PDBsum; 7CPV; -.
DR   PDBsum; 7LS1; -.
DR   PDBsum; 7LS2; -.
DR   AlphaFoldDB; P62918; -.
DR   EMDB; EMD-10321; -.
DR   EMDB; EMD-23500; -.
DR   EMDB; EMD-23501; -.
DR   EMDB; EMD-30432; -.
DR   EMDB; EMD-30433; -.
DR   SMR; P62918; -.
DR   BioGRID; 205087; 96.
DR   ComplexPortal; CPX-5262; 60S cytosolic large ribosomal subunit.
DR   ComplexPortal; CPX-7662; 60S cytosolic large ribosomal subunit, testis-specific variant.
DR   ComplexPortal; CPX-7663; 60S cytosolic large ribosomal subunit, striated muscle variant.
DR   CORUM; P62918; -.
DR   IntAct; P62918; 8.
DR   MINT; P62918; -.
DR   STRING; 10090.ENSMUSP00000155657; -.
DR   GlyGen; P62918; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P62918; -.
DR   MetOSite; P62918; -.
DR   PhosphoSitePlus; P62918; -.
DR   SwissPalm; P62918; -.
DR   EPD; P62918; -.
DR   jPOST; P62918; -.
DR   MaxQB; P62918; -.
DR   PaxDb; 10090-ENSMUSP00000004072; -.
DR   PeptideAtlas; P62918; -.
DR   ProteomicsDB; 299825; -.
DR   Pumba; P62918; -.
DR   TopDownProteomics; P62918; -.
DR   Antibodypedia; 14991; 327 antibodies from 33 providers.
DR   DNASU; 26961; -.
DR   Ensembl; ENSMUST00000004072.10; ENSMUSP00000004072.9; ENSMUSG00000003970.10.
DR   Ensembl; ENSMUST00000229183.2; ENSMUSP00000155657.2; ENSMUSG00000003970.10.
DR   GeneID; 26961; -.
DR   KEGG; mmu:26961; -.
DR   UCSC; uc007wmt.2; mouse.
DR   AGR; MGI:1350927; -.
DR   CTD; 6132; -.
DR   MGI; MGI:1350927; Rpl8.
DR   VEuPathDB; HostDB:ENSMUSG00000003970; -.
DR   eggNOG; KOG2309; Eukaryota.
DR   GeneTree; ENSGT00940000153244; -.
DR   HOGENOM; CLU_036235_0_3_1; -.
DR   InParanoid; P62918; -.
DR   OMA; GGRHPCT; -.
DR   OrthoDB; 1086454at2759; -.
DR   PhylomeDB; P62918; -.
DR   TreeFam; TF300748; -.
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-9629569; Protein hydroxylation.
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; 26961; 28 hits in 65 CRISPR screens.
DR   ChiTaRS; Rpl8; mouse.
DR   PRO; PR:P62918; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; P62918; Protein.
DR   Bgee; ENSMUSG00000003970; Expressed in pharyngeal arch 1 and 271 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR   GO; GO:0022626; C:cytosolic ribosome; ISO:MGI.
DR   GO; GO:0042788; C:polysomal ribosome; ISO:MGI.
DR   GO; GO:0098794; C:postsynapse; ISO:MGI.
DR   GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR   GO; GO:0098793; C:presynapse; NAS:SynGO.
DR   GO; GO:0005840; C:ribosome; NAS:SynGO.
DR   GO; GO:0045202; C:synapse; IDA:SynGO.
DR   GO; GO:1990932; F:5.8S rRNA binding; ISO:MGI.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
DR   GO; GO:0002181; P:cytoplasmic translation; ISO:MGI.
DR   GO; GO:0140242; P:translation at postsynapse; NAS:SynGO.
DR   GO; GO:0140236; P:translation at presynapse; NAS:SynGO.
DR   Gene3D; 2.30.30.30; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 4.10.950.10; Ribosomal protein L2, domain 3; 1.
DR   HAMAP; MF_01320_A; Ribosomal_uL2_A; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014722; Rib_uL2_dom2.
DR   InterPro; IPR002171; Ribosomal_uL2.
DR   InterPro; IPR023672; Ribosomal_uL2_arc.
DR   InterPro; IPR022669; Ribosomal_uL2_C.
DR   InterPro; IPR022671; Ribosomal_uL2_CS.
DR   InterPro; IPR014726; Ribosomal_uL2_dom3.
DR   InterPro; IPR022666; Ribosomal_uL2_RNA-bd_dom.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR13691:SF16; 60S RIBOSOMAL PROTEIN L8; 1.
DR   PANTHER; PTHR13691; RIBOSOMAL PROTEIN L2; 1.
DR   Pfam; PF00181; Ribosomal_L2; 1.
DR   Pfam; PF03947; Ribosomal_L2_C; 1.
DR   PIRSF; PIRSF002158; Ribosomal_L2; 1.
DR   SMART; SM01383; Ribosomal_L2; 1.
DR   SMART; SM01382; Ribosomal_L2_C; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
DR   PROSITE; PS00467; RIBOSOMAL_L2; 1.
DR   Genevisible; P62918; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Hydroxylation; Isopeptide bond;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding; Ubl conjugation.
FT   CHAIN           1..257
FT                   /note="Large ribosomal subunit protein uL2"
FT                   /id="PRO_0000129744"
FT   REGION          207..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         216
FT                   /note="(3S)-3-hydroxyhistidine"
FT                   /evidence="ECO:0000250|UniProtKB:P62917"
FT   CROSSLNK        42
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P62917"
FT   CROSSLNK        149
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P62917"
FT   CROSSLNK        234
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P62917"
FT   CROSSLNK        250
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P62917"
SQ   SEQUENCE   257 AA;  28025 MW;  CE1610449749318B CRC64;
     MGRVIRGQRK GAGSVFRAHV KHRKGAARLR AVDFAERHGY IKGIVKDIIH DPGRGAPLAK
     VVFRDPYRFK KRTELFIAAE GIHTGQFVYC GKKAQLNIGN VLPVGTMPEG TIVCCLEEKP
     GDRGKLARAS GNYATVISHN PETKKTRVKL PSGSKKVISS ANRAVVGVVA GGGRIDKPIL
     KAGRAYHKYK AKRNCWPRVR GVAMNPVEHP FGGGNHQHIG KPSTIRRDAP AGRKVGLIAA
     RRTGRLRGTK TVQEKEN
//