RL37_HUMAN
ID RL37_HUMAN Reviewed; 97 AA.
AC P61927; B2R4H2; P02403; Q6IBB4; Q99883;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=60S ribosomal protein L37;
DE AltName: Full=G1.16;
DE AltName: Full=Large ribosomal subunit protein eL37 {ECO:0000303|PubMed:24524803};
GN Name=RPL37;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lymphoma;
RA Kato S.;
RT "Cloning of human ribosomal protein L37 cDNA.";
RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon;
RX PubMed=7545944; DOI=10.1016/0167-4781(94)90197-x;
RA Barnard G.F., Staniunas R.J., Puder M., Steele G.D. Jr., Chen L.B.;
RT "Human ribosomal protein L37 has motifs predicting serine/threonine
RT phosphorylation and a zinc-finger domain.";
RL Biochim. Biophys. Acta 1218:425-428(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7588717; DOI=10.1111/j.1432-1033.1995.tb20874.x;
RA Su S., Bird R.C.;
RT "Cell cycle, differentiation and tissue-independent expression of ribosomal
RT protein L37.";
RL Eur. J. Biochem. 232:789-797(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11875025; DOI=10.1101/gr.214202;
RA Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S.,
RA Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
RT "The human ribosomal protein genes: sequencing and comparative analysis of
RT 73 genes.";
RL Genome Res. 12:379-390(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Ovary;
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-74 AND 76-97.
RX PubMed=9582194; DOI=10.1101/gr.8.5.509;
RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J.,
RA Tanaka T., Page D.C.;
RT "A map of 75 human ribosomal protein genes.";
RL Genome Res. 8:509-523(1998).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-10, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND SER-97, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
RN [17]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
RN [18] {ECO:0007744|PDB:6LQM, ECO:0007744|PDB:6LSR, ECO:0007744|PDB:6LSS, ECO:0007744|PDB:6LU8}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.09 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=32669547; DOI=10.1038/s41467-020-17237-x;
RA Liang X., Zuo M.Q., Zhang Y., Li N., Ma C., Dong M.Q., Gao N.;
RT "Structural snapshots of human pre-60S ribosomal particles before and after
RT nuclear export.";
RL Nat. Commun. 11:3542-3542(2020).
CC -!- FUNCTION: Component of the large ribosomal subunit (PubMed:23636399,
CC PubMed:32669547). The ribosome is a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell (PubMed:23636399,
CC PubMed:32669547). {ECO:0000269|PubMed:23636399,
CC ECO:0000269|PubMed:32669547}.
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL37 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D23661; BAA04888.1; -; mRNA.
DR EMBL; L11567; AAA62148.1; -; mRNA.
DR EMBL; S79979; AAB47039.2; -; mRNA.
DR EMBL; AB061834; BAB79472.1; -; Genomic_DNA.
DR EMBL; CR456890; CAG33171.1; -; mRNA.
DR EMBL; AK311827; BAG34769.1; -; mRNA.
DR EMBL; BC079477; AAH79477.1; -; mRNA.
DR EMBL; BC084576; AAH84576.1; -; mRNA.
DR EMBL; AB007184; BAA25843.1; -; Genomic_DNA.
DR EMBL; AB007183; BAA25842.1; -; Genomic_DNA.
DR CCDS; CCDS3934.1; -.
DR PIR; S47646; S47646.
DR RefSeq; NP_000988.1; NM_000997.4.
DR PDB; 4UG0; EM; -; Lj=1-97.
DR PDB; 4V6X; EM; 5.00 A; Cj=1-97.
DR PDB; 5AJ0; EM; 3.50 A; Aj=1-97.
DR PDB; 5LKS; EM; 3.60 A; Lj=1-97.
DR PDB; 5T2C; EM; 3.60 A; d=1-97.
DR PDB; 6IP5; EM; 3.90 A; 2d=1-97.
DR PDB; 6IP6; EM; 4.50 A; 2d=1-97.
DR PDB; 6IP8; EM; 3.90 A; 2d=1-97.
DR PDB; 6LQM; EM; 3.09 A; M=1-97.
DR PDB; 6LSR; EM; 3.13 A; M=1-97.
DR PDB; 6LSS; EM; 3.23 A; M=1-97.
DR PDB; 6LU8; EM; 3.13 A; M=1-97.
DR PDB; 6OLE; EM; 3.10 A; k=2-85.
DR PDB; 6OLF; EM; 3.90 A; k=2-85.
DR PDB; 6OLG; EM; 3.40 A; Aj=2-85.
DR PDB; 6OLI; EM; 3.50 A; k=2-85.
DR PDB; 6OLZ; EM; 3.90 A; Aj=2-85.
DR PDB; 6OM0; EM; 3.10 A; k=2-85.
DR PDB; 6OM7; EM; 3.70 A; k=2-85.
DR PDB; 6QZP; EM; 2.90 A; Lj=2-87.
DR PDB; 6W6L; EM; 3.84 A; k=1-97.
DR PDB; 6XA1; EM; 2.80 A; Lj=2-87.
DR PDB; 6Y0G; EM; 3.20 A; Lj=1-97.
DR PDB; 6Y2L; EM; 3.00 A; Lj=1-97.
DR PDB; 6Y57; EM; 3.50 A; Lj=1-97.
DR PDB; 6Y6X; EM; 2.80 A; Lj=2-87.
DR PDB; 6Z6L; EM; 3.00 A; Lj=1-97.
DR PDB; 6Z6M; EM; 3.10 A; Lj=1-97.
DR PDB; 6Z6N; EM; 2.90 A; Lj=1-97.
DR PDB; 6ZM7; EM; 2.70 A; Lj=1-97.
DR PDB; 6ZME; EM; 3.00 A; Lj=1-97.
DR PDB; 6ZMI; EM; 2.60 A; Lj=1-97.
DR PDB; 6ZMO; EM; 3.10 A; Lj=1-97.
DR PDB; 7BHP; EM; 3.30 A; Lj=1-97.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 5LKS; -.
DR PDBsum; 5T2C; -.
DR PDBsum; 6IP5; -.
DR PDBsum; 6IP6; -.
DR PDBsum; 6IP8; -.
DR PDBsum; 6LQM; -.
DR PDBsum; 6LSR; -.
DR PDBsum; 6LSS; -.
DR PDBsum; 6LU8; -.
DR PDBsum; 6OLE; -.
DR PDBsum; 6OLF; -.
DR PDBsum; 6OLG; -.
DR PDBsum; 6OLI; -.
DR PDBsum; 6OLZ; -.
DR PDBsum; 6OM0; -.
DR PDBsum; 6OM7; -.
DR PDBsum; 6QZP; -.
DR PDBsum; 6W6L; -.
DR PDBsum; 6XA1; -.
DR PDBsum; 6Y0G; -.
DR PDBsum; 6Y2L; -.
DR PDBsum; 6Y57; -.
DR PDBsum; 6Y6X; -.
DR PDBsum; 6Z6L; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 7BHP; -.
DR AlphaFoldDB; P61927; -.
DR SMR; P61927; -.
DR BioGRID; 112086; 273.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; P61927; -.
DR IntAct; P61927; 26.
DR MINT; P61927; -.
DR STRING; 9606.ENSP00000274242; -.
DR DrugBank; DB02494; (S)-3-phenyllactic acid.
DR DrugBank; DB07374; Anisomycin.
DR DrugBank; DB08437; Puromycin.
DR DrugBank; DB04602; PUROMYCIN AMINONUCLEOSIDE-5'-MONOPHOSPHATE.
DR DrugBank; DB04805; Virginiamycin S1.
DR GlyGen; P61927; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P61927; -.
DR PhosphoSitePlus; P61927; -.
DR BioMuta; RPL37; -.
DR DMDM; 48429090; -.
DR EPD; P61927; -.
DR jPOST; P61927; -.
DR MassIVE; P61927; -.
DR MaxQB; P61927; -.
DR PaxDb; P61927; -.
DR PeptideAtlas; P61927; -.
DR PRIDE; P61927; -.
DR ProteomicsDB; 57340; -.
DR TopDownProteomics; P61927; -.
DR Antibodypedia; 23151; 138 antibodies from 23 providers.
DR DNASU; 6167; -.
DR Ensembl; ENST00000274242.10; ENSP00000274242.5; ENSG00000145592.14.
DR GeneID; 6167; -.
DR KEGG; hsa:6167; -.
DR MANE-Select; ENST00000274242.10; ENSP00000274242.5; NM_000997.5; NP_000988.1.
DR UCSC; uc021xxr.2; human.
DR CTD; 6167; -.
DR DisGeNET; 6167; -.
DR GeneCards; RPL37; -.
DR HGNC; HGNC:10347; RPL37.
DR HPA; ENSG00000145592; Low tissue specificity.
DR MIM; 604181; gene.
DR neXtProt; NX_P61927; -.
DR OpenTargets; ENSG00000145592; -.
DR PharmGKB; PA34736; -.
DR VEuPathDB; HostDB:ENSG00000145592; -.
DR eggNOG; KOG3475; Eukaryota.
DR GeneTree; ENSGT00390000005254; -.
DR HOGENOM; CLU_150908_0_0_1; -.
DR InParanoid; P61927; -.
DR OrthoDB; 1560654at2759; -.
DR PhylomeDB; P61927; -.
DR TreeFam; TF300260; -.
DR PathwayCommons; P61927; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-156902; Peptide chain elongation.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-192823; Viral mRNA Translation.
DR Reactome; R-HSA-2408557; Selenocysteine synthesis.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-HSA-72764; Eukaryotic Translation Termination.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency.
DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P61927; -.
DR SIGNOR; P61927; -.
DR BioGRID-ORCS; 6167; 632 hits in 1046 CRISPR screens.
DR ChiTaRS; RPL37; human.
DR GeneWiki; RPL37; -.
DR GenomeRNAi; 6167; -.
DR Pharos; P61927; Tbio.
DR PRO; PR:P61927; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P61927; protein.
DR Bgee; ENSG00000145592; Expressed in germinal epithelium of ovary and 211 other tissues.
DR ExpressionAtlas; P61927; baseline and differential.
DR Genevisible; P61927; HS.
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; IDA:FlyBase.
DR GO; GO:0097371; F:MDM2/MDM4 family protein binding; IPI:FlyBase.
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; IDA:FlyBase.
DR GO; GO:1990948; F:ubiquitin ligase inhibitor activity; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; IC:FlyBase.
DR GO; GO:1901798; P:positive regulation of signal transduction by p53 class mediator; IDA:FlyBase.
DR GO; GO:0006412; P:translation; TAS:UniProtKB.
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_0000139705"
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:0007744|PubMed:19608861"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT CONFLICT 65
FT /note="R -> S (in Ref. 3; AAB47039)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 97 AA; 11078 MW; F565A11E983027C9 CRC64;
MTKGTSSFGK RRNKTHTLCR RCGSKAYHLQ KSTCGKCGYP AKRKRKYNWS AKAKRRNTTG
TGRMRHLKIV YRRFRHGFRE GTTPKPKRAA VAASSSS
