RL17_HUMAN
ID RL17_HUMAN Reviewed; 184 AA.
AC P18621; B2R4H3; B4E3C2; B5ME31; J3QL51; Q3KQW2; Q6NZ54; Q7M4M5;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=60S ribosomal protein L17;
DE AltName: Full=60S ribosomal protein L23;
DE AltName: Full=Large ribosomal subunit protein uL22 {ECO:0000303|PubMed:24524803};
DE AltName: Full=PD-1;
GN Name=RPL17;
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] (ISOFORM 1).
RC TISSUE=Blood;
RX PubMed=2402465; DOI=10.1093/nar/18.17.5301;
RA Mager D.L., Freeman J.D.;
RT "A human gene related to the ribosomal protein L23 gene of Halobacterium
RT marismortui.";
RL Nucleic Acids Res. 18:5301-5301(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Pancreatic tumor;
RX PubMed=1793733;
RA Batra S.K., Metzgar R.S., Hollingsworth M.A.;
RT "Isolation and characterization of a complementary DNA (PD-1)
RT differentially expressed by human pancreatic ductal cell tumors.";
RL Cell Growth Differ. 2:385-390(1991).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Uterus;
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 MRNA] (ISOFORM 3).
RC TISSUE=Neuroblastoma;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hypothalamus, Lung, Prostate, and Testis;
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 [9]
RP PROTEIN SEQUENCE OF 2-10, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP AND SUBUNIT.
RX PubMed=12962325; DOI=10.1023/a:1025068419698;
RA Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R.,
RA Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B., Karpova G.G.;
RT "Characterization and analysis of posttranslational modifications of the
RT human large cytoplasmic ribosomal subunit proteins by mass spectrometry and
RT Edman sequencing.";
RL J. Protein Chem. 22:249-258(2003).
RN [10]
RP PROTEIN SEQUENCE OF 2-13; 31-42; 47-55; 75-82; 86-96 AND 106-124, CLEAVAGE
RP OF INITIATOR METHIONINE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Calvo F., Kolch W.;
RL Submitted (FEB-2008) to UniProtKB.
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 170-183.
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 [12]
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 [13]
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 [14] {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:12962325,
CC PubMed:23636399, PubMed:32669547). The ribosome is a large
CC ribonucleoprotein complex responsible for the synthesis of proteins in
CC the cell (PubMed:12962325, PubMed:23636399, PubMed:32669547).
CC {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547,
CC ECO:0000305|PubMed:12962325}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (PubMed:12962325,
CC PubMed:23636399, PubMed:32669547). {ECO:0000269|PubMed:23636399,
CC ECO:0000269|PubMed:32669547, ECO:0000305|PubMed:12962325}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P18621-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P18621-2; Sequence=VSP_045445;
CC Name=3;
CC IsoId=P18621-3; Sequence=VSP_046965;
CC -!- TISSUE SPECIFICITY: Expressed in pancreas, lung, colon, cystic duct,
CC gall bladder, kidney and liver. Expressed at high levels in the well
CC differentiated pancreatic tumor cell lines HPAF, COLO 357 and Capan-1,
CC the moderately differentiated pancreatic tumor cell lines T3M-4, AsPc-1
CC and BxPc-3, the poorly differentiated pancreatic tumor cell line MIA
CC PaCa-2, and the pancreatic tumor cell lines of undefined
CC differentiation status such as SW979. Expressed at lower levels in the
CC poorly differentiated pancreatic tumor cell lines HCG-25 and PANC-1.
CC {ECO:0000269|PubMed:1793733}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL22 family.
CC {ECO:0000305}.
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DR EMBL; X53777; CAA37793.1; -; mRNA.
DR EMBL; AB061824; BAB79462.1; -; Genomic_DNA.
DR EMBL; AC100778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK304659; BAG65434.1; -; mRNA.
DR EMBL; AK311828; BAG34770.1; -; mRNA.
DR EMBL; BX393840; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CH471096; EAW62940.1; -; Genomic_DNA.
DR EMBL; BC000502; AAH00502.1; -; mRNA.
DR EMBL; BC017831; AAH17831.1; -; mRNA.
DR EMBL; BC066323; AAH66323.1; -; mRNA.
DR EMBL; BC066324; AAH66324.1; -; mRNA.
DR EMBL; BC106031; AAI06032.1; -; mRNA.
DR EMBL; AB007174; BAA25834.1; -; Genomic_DNA.
DR CCDS; CCDS45865.1; -. [P18621-1]
DR CCDS; CCDS56070.1; -. [P18621-2]
DR PIR; A61192; A61192.
DR PIR; S11218; R5HU22.
DR RefSeq; NP_000976.1; NM_000985.4. [P18621-1]
DR RefSeq; NP_001030178.1; NM_001035006.2. [P18621-1]
DR RefSeq; NP_001186269.1; NM_001199340.1. [P18621-1]
DR RefSeq; NP_001186270.1; NM_001199341.1. [P18621-1]
DR RefSeq; NP_001186271.1; NM_001199342.1. [P18621-1]
DR RefSeq; NP_001186272.1; NM_001199343.1. [P18621-1]
DR RefSeq; NP_001186273.1; NM_001199344.1. [P18621-1]
DR RefSeq; NP_001186274.1; NM_001199345.1. [P18621-2]
DR PDB; 4UG0; EM; -; LP=1-184.
DR PDB; 4V6X; EM; 5.00 A; CP=1-184.
DR PDB; 5A8L; EM; 3.80 A; D=1-184.
DR PDB; 5AJ0; EM; 3.50 A; AP=1-184.
DR PDB; 5LKS; EM; 3.60 A; LP=1-184.
DR PDB; 5T2C; EM; 3.60 A; J=1-160.
DR PDB; 6IP5; EM; 3.90 A; 2J=1-184.
DR PDB; 6IP6; EM; 4.50 A; 2J=1-184.
DR PDB; 6IP8; EM; 3.90 A; 2J=1-184.
DR PDB; 6LQM; EM; 3.09 A; Y=1-184.
DR PDB; 6LSR; EM; 3.13 A; Y=1-184.
DR PDB; 6LSS; EM; 3.23 A; Y=1-184.
DR PDB; 6LU8; EM; 3.13 A; Y=1-184.
DR PDB; 6OLE; EM; 3.10 A; Q=2-154.
DR PDB; 6OLF; EM; 3.90 A; Q=2-154.
DR PDB; 6OLG; EM; 3.40 A; AP=2-154.
DR PDB; 6OLI; EM; 3.50 A; Q=2-154.
DR PDB; 6OLZ; EM; 3.90 A; AP=2-154.
DR PDB; 6OM0; EM; 3.10 A; Q=2-154.
DR PDB; 6OM7; EM; 3.70 A; Q=2-154.
DR PDB; 6QZP; EM; 2.90 A; LP=2-154.
DR PDB; 6W6L; EM; 3.84 A; Q=1-184.
DR PDB; 6XA1; EM; 2.80 A; LP=2-154.
DR PDB; 6Y0G; EM; 3.20 A; LP=1-184.
DR PDB; 6Y2L; EM; 3.00 A; LP=1-184.
DR PDB; 6Y57; EM; 3.50 A; LP=1-184.
DR PDB; 6Y6X; EM; 2.80 A; LP=2-154.
DR PDB; 6Z6L; EM; 3.00 A; LP=1-184.
DR PDB; 6Z6M; EM; 3.10 A; LP=1-184.
DR PDB; 6Z6N; EM; 2.90 A; LP=1-184.
DR PDB; 6ZM7; EM; 2.70 A; LP=1-184.
DR PDB; 6ZME; EM; 3.00 A; LP=1-184.
DR PDB; 6ZMI; EM; 2.60 A; LP=1-184.
DR PDB; 6ZMO; EM; 3.10 A; LP=1-184.
DR PDB; 7BHP; EM; 3.30 A; LP=1-184.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5A8L; -.
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; P18621; -.
DR SMR; P18621; -.
DR BioGRID; 112059; 498.
DR BioGRID; 1529331; 5.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; P18621; -.
DR IntAct; P18621; 75.
DR MINT; P18621; -.
DR STRING; 9606.ENSP00000397798; -.
DR GlyGen; P18621; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P18621; -.
DR MetOSite; P18621; -.
DR PhosphoSitePlus; P18621; -.
DR SwissPalm; P18621; -.
DR BioMuta; RPL17; -.
DR DMDM; 132799; -.
DR EPD; P18621; -.
DR jPOST; P18621; -.
DR MassIVE; P18621; -.
DR MaxQB; P18621; -.
DR PaxDb; P18621; -.
DR PeptideAtlas; P18621; -.
DR PRIDE; P18621; -.
DR ProteomicsDB; 53603; -. [P18621-1]
DR ProteomicsDB; 5890; -.
DR TopDownProteomics; P18621-1; -. [P18621-1]
DR TopDownProteomics; P18621-2; -. [P18621-2]
DR Antibodypedia; 65728; 321 antibodies from 29 providers.
DR DNASU; 6139; -.
DR Ensembl; ENST00000579248.5; ENSP00000462023.1; ENSG00000265681.8. [P18621-1]
DR Ensembl; ENST00000579408.5; ENSP00000463842.1; ENSG00000265681.8. [P18621-1]
DR Ensembl; ENST00000580261.6; ENSP00000462385.1; ENSG00000265681.8. [P18621-1]
DR Ensembl; ENST00000581373.5; ENSP00000462944.1; ENSG00000265681.8. [P18621-2]
DR Ensembl; ENST00000618613.5; ENSP00000480555.1; ENSG00000265681.8. [P18621-1]
DR Ensembl; ENST00000618619.4; ENSP00000482577.1; ENSG00000265681.8. [P18621-1]
DR GeneID; 6139; -.
DR KEGG; hsa:6139; -.
DR MANE-Select; ENST00000580261.6; ENSP00000462385.1; NM_001035006.5; NP_001030178.1.
DR UCSC; uc002ldp.4; human. [P18621-1]
DR CTD; 6139; -.
DR DisGeNET; 6139; -.
DR GeneCards; RPL17; -.
DR HGNC; HGNC:10307; RPL17.
DR HPA; ENSG00000265681; Low tissue specificity.
DR MIM; 603661; gene.
DR neXtProt; NX_P18621; -.
DR OpenTargets; ENSG00000265681; -.
DR PharmGKB; PA34676; -.
DR VEuPathDB; HostDB:ENSG00000265681; -.
DR eggNOG; KOG3353; Eukaryota.
DR GeneTree; ENSGT00950000183010; -.
DR InParanoid; P18621; -.
DR OMA; ANAEYKG; -.
DR PhylomeDB; P18621; -.
DR TreeFam; TF300042; -.
DR PathwayCommons; P18621; -.
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; P18621; -.
DR SIGNOR; P18621; -.
DR BioGRID-ORCS; 6139; 767 hits in 995 CRISPR screens.
DR ChiTaRS; RPL17; human.
DR GeneWiki; RPL17; -.
DR GenomeRNAi; 6139; -.
DR Pharos; P18621; Tbio.
DR PRO; PR:P18621; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; P18621; protein.
DR Bgee; ENSG00000265681; Expressed in left ovary and 94 other tissues.
DR ExpressionAtlas; P18621; baseline and differential.
DR Genevisible; P18621; 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:0005634; C:nucleus; HDA: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; IBA:GO_Central.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR CDD; cd00336; Ribosomal_L22; 1.
DR Gene3D; 3.90.470.10; -; 1.
DR HAMAP; MF_01331_A; Ribosomal_L22_A; 1.
DR InterPro; IPR001063; Ribosomal_L22.
DR InterPro; IPR018260; Ribosomal_L22/L17_CS.
DR InterPro; IPR005721; Ribosomal_L22/L17_euk/arc.
DR InterPro; IPR036394; Ribosomal_L22/L17_sf.
DR PANTHER; PTHR11593; PTHR11593; 1.
DR Pfam; PF00237; Ribosomal_L22; 1.
DR SUPFAM; SSF54843; SSF54843; 1.
DR TIGRFAMs; TIGR01038; uL22_arch_euk; 1.
DR PROSITE; PS00464; RIBOSOMAL_L22; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12962325, ECO:0000269|Ref.10"
FT CHAIN 2..184
FT /note="60S ribosomal protein L17"
FT /id="PRO_0000125331"
FT REGION 160..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..184
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..38
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045445"
FT VAR_SEQ 170..184
FT /note="ISQKKLKKQKLMARE -> LRSSSLGKWCAFLVSSFQFCSGSTKNSWSHIYT
FT LWFPPSLVVYGLRKQYKNPMIQTKAK (in isoform 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_046965"
FT CONFLICT 133
FT /note="H -> R (in Ref. 8; AAH66324)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 184 AA; 21397 MW; 2FC595DD74ED1CA0 CRC64;
MVRYSLDPEN PTKSCKSRGS NLRVHFKNTR ETAQAIKGMH IRKATKYLKD VTLQKQCVPF
RRYNGGVGRC AQAKQWGWTQ GRWPKKSAEF LLHMLKNAES NAELKGLDVD SLVIEHIQVN
KAPKMRRRTY RAHGRINPYM SSPCHIEMIL TEKEQIVPKP EEEVAQKKKI SQKKLKKQKL
MARE
