RL37_MOUSE
ID RL37_MOUSE Reviewed; 97 AA.
AC Q9D823; Q6ZWV1;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=60S ribosomal protein L37;
GN Name=Rpl37;
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;
RC TISSUE=Head, Heart, Kidney, Liver, Pancreas, Small intestine, and Stomach;
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; TISSUE=Brain, and Colon;
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).
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:P61927}.
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000250|UniProtKB:P61927}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P61927}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL37 family.
CC {ECO:0000305}.
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DR EMBL; AK002592; BAB22213.1; -; mRNA.
DR EMBL; AK008563; BAB25746.1; -; mRNA.
DR EMBL; AK011101; BAB27398.1; -; mRNA.
DR EMBL; AK012544; BAB28307.1; -; mRNA.
DR EMBL; AK014003; BAB29108.1; -; mRNA.
DR EMBL; AK019020; BAB31512.1; -; mRNA.
DR EMBL; AK019294; BAB31652.1; -; mRNA.
DR EMBL; AK028138; BAC25766.1; -; mRNA.
DR EMBL; AK168550; BAE40425.1; -; mRNA.
DR EMBL; BC054388; AAH54388.1; -; mRNA.
DR EMBL; BC081438; AAH81438.1; -; mRNA.
DR CCDS; CCDS37027.1; -.
DR RefSeq; NP_001258519.1; NM_001271590.1.
DR RefSeq; NP_001258520.1; NM_001271591.1.
DR RefSeq; NP_080345.1; NM_026069.3.
DR PDB; 6SWA; EM; 3.10 A; h=1-97.
DR PDB; 7LS1; EM; 3.30 A; d2=1-97.
DR PDB; 7LS2; EM; 3.10 A; d2=1-97.
DR PDBsum; 6SWA; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; Q9D823; -.
DR SMR; Q9D823; -.
DR BioGRID; 1639134; 2.
DR BioGRID; 212070; 4.
DR ComplexPortal; CPX-5262; 60S cytosolic large ribosomal subunit.
DR STRING; 10090.ENSMUSP00000046506; -.
DR iPTMnet; Q9D823; -.
DR PhosphoSitePlus; Q9D823; -.
DR SwissPalm; Q9D823; -.
DR EPD; Q9D823; -.
DR MaxQB; Q9D823; -.
DR PaxDb; Q9D823; -.
DR PeptideAtlas; Q9D823; -.
DR PRIDE; Q9D823; -.
DR ProteomicsDB; 300488; -.
DR TopDownProteomics; Q9D823; -.
DR Antibodypedia; 23151; 138 antibodies from 23 providers.
DR DNASU; 67281; -.
DR Ensembl; ENSMUST00000045356; ENSMUSP00000046506; ENSMUSG00000041841.
DR GeneID; 100502825; -.
DR GeneID; 67281; -.
DR KEGG; mmu:100502825; -.
DR KEGG; mmu:67281; -.
DR UCSC; uc007vcs.2; mouse.
DR CTD; 100502825; -.
DR CTD; 6167; -.
DR MGI; MGI:1914531; Rpl37.
DR VEuPathDB; HostDB:ENSMUSG00000041841; -.
DR eggNOG; KOG3475; Eukaryota.
DR GeneTree; ENSGT00390000005254; -.
DR HOGENOM; CLU_150908_0_0_1; -.
DR InParanoid; Q9D823; -.
DR OMA; RMAYLKH; -.
DR OrthoDB; 1560654at2759; -.
DR PhylomeDB; Q9D823; -.
DR TreeFam; TF300260; -.
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; 100502825; 4 hits in 10 CRISPR screens.
DR BioGRID-ORCS; 67281; 28 hits in 71 CRISPR screens.
DR ChiTaRS; Rpl37; mouse.
DR PRO; PR:Q9D823; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9D823; protein.
DR Bgee; ENSMUSG00000041841; Expressed in ectoplacental cone and 151 other tissues.
DR Genevisible; Q9D823; 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:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0097371; F:MDM2/MDM4 family protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:1990948; F:ubiquitin ligase inhibitor activity; ISO:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:1901798; P:positive regulation of signal transduction by p53 class mediator; ISO:MGI.
DR Gene3D; 2.20.25.30; -; 1.
DR HAMAP; MF_00547; Ribosomal_L37e; 1.
DR InterPro; IPR011331; Ribosomal_L37ae/L37e.
DR InterPro; IPR001569; Ribosomal_L37e.
DR InterPro; IPR018267; Ribosomal_L37e_CS.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR Pfam; PF01907; Ribosomal_L37e; 1.
DR SUPFAM; SSF57829; SSF57829; 1.
DR PROSITE; PS01077; RIBOSOMAL_L37E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Metal-binding; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..97
FT /note="60S ribosomal protein L37"
FT /id="PRO_0000139706"
FT ZN_FING 19..37
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P49166"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P49166"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P49166"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P49166"
FT MOD_RES 10
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P61927"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61927"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61927"
FT CONFLICT 17
FT /note="T -> R (in Ref. 1; BAB25746)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 97 AA; 11078 MW; F565A11E983027C9 CRC64;
MTKGTSSFGK RRNKTHTLCR RCGSKAYHLQ KSTCGKCGYP AKRKRKYNWS AKAKRRNTTG
TGRMRHLKIV YRRFRHGFRE GTTPKPKRAA VAASSSS
