RL32_HUMAN
ID RL32_HUMAN Reviewed; 135 AA.
AC P62910; B2R4Q3; P02433;
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 L32;
DE AltName: Full=Large ribosomal subunit protein eL32 {ECO:0000303|PubMed:24524803};
GN Name=RPL32; ORFNames=PP9932;
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].
RX PubMed=3866218; DOI=10.1093/nar/13.24.8883;
RA Young J.A.T., Trowsdale J.;
RT "A processed pseudogene in an intron of the HLA-DP beta 1 chain gene is a
RT member of the ribosomal protein L32 gene family.";
RL Nucleic Acids Res. 13:8883-8891(1985).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [7]
RP PROTEIN SEQUENCE OF 2-11; 84-93 AND 115-121, CLEAVAGE OF INITIATOR
RP METHIONINE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lung carcinoma;
RA Bienvenut W.V., Vousden K.H., Lukashchuk N.;
RL Submitted (MAR-2008) to UniProtKB.
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-9, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [14]
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 [15] {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 eL32 family.
CC {ECO:0000305}.
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DR EMBL; X03342; CAA27048.1; -; mRNA.
DR EMBL; AB061831; BAB79469.1; -; Genomic_DNA.
DR EMBL; AF370435; AAQ15271.1; -; mRNA.
DR EMBL; AK311909; BAG34850.1; -; mRNA.
DR EMBL; CH471055; EAW64144.1; -; Genomic_DNA.
DR EMBL; BC011514; AAH11514.1; -; mRNA.
DR EMBL; BC070209; AAH70209.1; -; mRNA.
DR CCDS; CCDS2614.1; -.
DR PIR; S11393; R5HU32.
DR RefSeq; NP_000985.1; NM_000994.3.
DR RefSeq; NP_001007074.1; NM_001007073.1.
DR RefSeq; NP_001007075.1; NM_001007074.1.
DR PDB; 4UG0; EM; -; Le=1-135.
DR PDB; 4V6X; EM; 5.00 A; Ce=1-135.
DR PDB; 5AJ0; EM; 3.50 A; Ae=1-135.
DR PDB; 5LKS; EM; 3.60 A; Le=1-135.
DR PDB; 5T2C; EM; 3.60 A; Y=1-135.
DR PDB; 6IP5; EM; 3.90 A; 2Y=1-135.
DR PDB; 6IP6; EM; 4.50 A; 2Y=1-135.
DR PDB; 6IP8; EM; 3.90 A; 2Y=1-135.
DR PDB; 6LQM; EM; 3.09 A; t=1-135.
DR PDB; 6LSR; EM; 3.13 A; t=1-135.
DR PDB; 6LSS; EM; 3.23 A; k=1-135.
DR PDB; 6LU8; EM; 3.13 A; k=1-135.
DR PDB; 6OLE; EM; 3.10 A; f=2-130.
DR PDB; 6OLF; EM; 3.90 A; f=2-130.
DR PDB; 6OLG; EM; 3.40 A; Ae=2-130.
DR PDB; 6OLI; EM; 3.50 A; f=2-130.
DR PDB; 6OLZ; EM; 3.90 A; Ae=2-130.
DR PDB; 6OM0; EM; 3.10 A; f=2-130.
DR PDB; 6OM7; EM; 3.70 A; f=2-130.
DR PDB; 6QZP; EM; 2.90 A; Le=2-129.
DR PDB; 6W6L; EM; 3.84 A; f=1-135.
DR PDB; 6XA1; EM; 2.80 A; Le=2-129.
DR PDB; 6Y0G; EM; 3.20 A; Le=1-135.
DR PDB; 6Y2L; EM; 3.00 A; Le=1-135.
DR PDB; 6Y57; EM; 3.50 A; Le=1-135.
DR PDB; 6Y6X; EM; 2.80 A; Le=2-129.
DR PDB; 6Z6L; EM; 3.00 A; Le=1-135.
DR PDB; 6Z6M; EM; 3.10 A; Le=1-135.
DR PDB; 6Z6N; EM; 2.90 A; Le=1-135.
DR PDB; 6ZM7; EM; 2.70 A; Le=1-135.
DR PDB; 6ZME; EM; 3.00 A; Le=1-135.
DR PDB; 6ZMI; EM; 2.60 A; Le=1-135.
DR PDB; 6ZMO; EM; 3.10 A; Le=1-135.
DR PDB; 7BHP; EM; 3.30 A; Le=1-135.
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; P62910; -.
DR SMR; P62910; -.
DR BioGRID; 112080; 256.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; P62910; -.
DR IntAct; P62910; 69.
DR MINT; P62910; -.
DR STRING; 9606.ENSP00000416429; -.
DR CarbonylDB; P62910; -.
DR GlyGen; P62910; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62910; -.
DR MetOSite; P62910; -.
DR PhosphoSitePlus; P62910; -.
DR SwissPalm; P62910; -.
DR BioMuta; RPL32; -.
DR DMDM; 51702809; -.
DR EPD; P62910; -.
DR jPOST; P62910; -.
DR MassIVE; P62910; -.
DR MaxQB; P62910; -.
DR PaxDb; P62910; -.
DR PeptideAtlas; P62910; -.
DR PRIDE; P62910; -.
DR ProteomicsDB; 57451; -.
DR TopDownProteomics; P62910; -.
DR Antibodypedia; 10834; 100 antibodies from 24 providers.
DR DNASU; 6161; -.
DR Ensembl; ENST00000396953.6; ENSP00000380156.2; ENSG00000144713.13.
DR Ensembl; ENST00000396957.5; ENSP00000380158.1; ENSG00000144713.13.
DR Ensembl; ENST00000429711.7; ENSP00000416429.2; ENSG00000144713.13.
DR Ensembl; ENST00000435983.5; ENSP00000388674.1; ENSG00000144713.13.
DR GeneID; 6161; -.
DR KEGG; hsa:6161; -.
DR MANE-Select; ENST00000429711.7; ENSP00000416429.2; NM_000994.4; NP_000985.1.
DR UCSC; uc003bxl.4; human.
DR CTD; 6161; -.
DR DisGeNET; 6161; -.
DR GeneCards; RPL32; -.
DR HGNC; HGNC:10336; RPL32.
DR HPA; ENSG00000144713; Low tissue specificity.
DR neXtProt; NX_P62910; -.
DR OpenTargets; ENSG00000144713; -.
DR PharmGKB; PA34719; -.
DR VEuPathDB; HostDB:ENSG00000144713; -.
DR eggNOG; KOG0878; Eukaryota.
DR GeneTree; ENSGT00940000153973; -.
DR InParanoid; P62910; -.
DR OMA; HPSGYEE; -.
DR OrthoDB; 1460684at2759; -.
DR PhylomeDB; P62910; -.
DR TreeFam; TF314947; -.
DR PathwayCommons; P62910; -.
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; P62910; -.
DR SIGNOR; P62910; -.
DR BioGRID-ORCS; 6161; 784 hits in 1020 CRISPR screens.
DR ChiTaRS; RPL32; human.
DR GeneWiki; RPL32; -.
DR GenomeRNAi; 6161; -.
DR Pharos; P62910; Tbio.
DR PRO; PR:P62910; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P62910; protein.
DR Bgee; ENSG00000144713; Expressed in cortical plate and 105 other tissues.
DR ExpressionAtlas; P62910; baseline and differential.
DR Genevisible; P62910; 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; IDA:UniProtKB.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0042788; C:polysomal ribosome; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; IDA:UniProtKB.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR CDD; cd00513; Ribosomal_L32_L32e; 1.
DR InterPro; IPR001515; Ribosomal_L32e.
DR InterPro; IPR018263; Ribosomal_L32e_CS.
DR InterPro; IPR036351; Ribosomal_L32e_sf.
DR PANTHER; PTHR23413; PTHR23413; 1.
DR Pfam; PF01655; Ribosomal_L32e; 1.
DR SMART; SM01393; Ribosomal_L32e; 1.
DR SUPFAM; SSF52042; SSF52042; 1.
DR PROSITE; PS00580; RIBOSOMAL_L32E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.7"
FT CHAIN 2..135
FT /note="60S ribosomal protein L32"
FT /id="PRO_0000131113"
FT MOD_RES 50
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62911"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 9
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
SQ SEQUENCE 135 AA; 15860 MW; EDEE48446483966E CRC64;
MAALRPLVKP KIVKKRTKKF IRHQSDRYVK IKRNWRKPRG IDNRVRRRFK GQILMPNIGY
GSNKKTKHML PSGFRKFLVH NVKELEVLLM CNKSYCAEIA HNVSSKNRKA IVERAAQLAI
RVTNPNARLR SEENE
