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   27-MAR-2024, entry version 228.
DE   RecName: Full=Large ribosomal subunit protein uL22 {ECO:0000303|PubMed:24524803};
DE   AltName: Full=60S ribosomal protein L17;
DE   AltName: Full=60S ribosomal protein L23;
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   PDB; 7F5S; EM; 2.72 A; LP=1-184.
DR   PDB; 7OW7; EM; 2.20 A; J=1-184.
DR   PDB; 7QVP; EM; 3.00 A; LP=1-154, MP=1-184.
DR   PDB; 7XNX; EM; 2.70 A; LP=1-184.
DR   PDB; 7XNY; EM; 2.50 A; LP=1-184.
DR   PDB; 8A3D; EM; 1.67 A; J=1-184.
DR   PDB; 8FKP; EM; 2.85 A; LA=1-184.
DR   PDB; 8FKQ; EM; 2.76 A; LA=1-184.
DR   PDB; 8FKR; EM; 2.89 A; LA=1-184.
DR   PDB; 8FKS; EM; 2.88 A; LA=1-184.
DR   PDB; 8FKT; EM; 2.81 A; LA=1-184.
DR   PDB; 8FKU; EM; 2.82 A; LA=1-184.
DR   PDB; 8FKV; EM; 2.47 A; LA=1-184.
DR   PDB; 8FKW; EM; 2.50 A; LA=1-184.
DR   PDB; 8FKX; EM; 2.59 A; LA=1-184.
DR   PDB; 8FKY; EM; 2.67 A; LA=1-184.
DR   PDB; 8FKZ; EM; 3.04 A; LA=1-184.
DR   PDB; 8FL2; EM; 2.67 A; LA=1-184.
DR   PDB; 8FL3; EM; 2.53 A; LA=1-184.
DR   PDB; 8FL4; EM; 2.89 A; LA=1-184.
DR   PDB; 8FL6; EM; 2.62 A; LA=1-184.
DR   PDB; 8FL7; EM; 2.55 A; LA=1-184.
DR   PDB; 8FL9; EM; 2.75 A; LA=1-184.
DR   PDB; 8FLA; EM; 2.63 A; LA=1-184.
DR   PDB; 8FLB; EM; 2.55 A; LA=1-184.
DR   PDB; 8FLC; EM; 2.76 A; LA=1-184.
DR   PDB; 8FLD; EM; 2.58 A; LA=1-184.
DR   PDB; 8FLE; EM; 2.48 A; LA=1-184.
DR   PDB; 8FLF; EM; 2.65 A; LA=1-184.
DR   PDB; 8G5Y; EM; 2.29 A; LP=1-184.
DR   PDB; 8G5Z; EM; 2.64 A; LP=2-154.
DR   PDB; 8G60; EM; 2.54 A; LP=1-184.
DR   PDB; 8G61; EM; 2.94 A; LP=1-184.
DR   PDB; 8G6J; EM; 2.80 A; LP=1-184.
DR   PDB; 8GLP; EM; 1.67 A; LP=1-184.
DR   PDB; 8IDT; EM; 2.80 A; Y=1-184.
DR   PDB; 8IDY; EM; 3.00 A; Y=1-184.
DR   PDB; 8IE3; EM; 3.30 A; Y=1-184.
DR   PDB; 8INE; EM; 3.20 A; Y=1-184.
DR   PDB; 8INF; EM; 3.00 A; Y=1-184.
DR   PDB; 8INK; EM; 3.20 A; Y=1-184.
DR   PDB; 8IPD; EM; 3.20 A; Y=1-184.
DR   PDB; 8IPX; EM; 4.30 A; Y=1-184.
DR   PDB; 8IPY; EM; 3.20 A; Y=1-184.
DR   PDB; 8IR1; EM; 3.30 A; Y=1-184.
DR   PDB; 8IR3; EM; 3.50 A; Y=1-184.
DR   PDB; 8JDJ; EM; 2.50 A; U=1-184.
DR   PDB; 8JDK; EM; 2.26 A; U=1-184.
DR   PDB; 8JDL; EM; 2.42 A; U=1-184.
DR   PDB; 8JDM; EM; 2.67 A; U=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   PDBsum; 7F5S; -.
DR   PDBsum; 7OW7; -.
DR   PDBsum; 7QVP; -.
DR   PDBsum; 7XNX; -.
DR   PDBsum; 7XNY; -.
DR   PDBsum; 8A3D; -.
DR   PDBsum; 8FKP; -.
DR   PDBsum; 8FKQ; -.
DR   PDBsum; 8FKR; -.
DR   PDBsum; 8FKS; -.
DR   PDBsum; 8FKT; -.
DR   PDBsum; 8FKU; -.
DR   PDBsum; 8FKV; -.
DR   PDBsum; 8FKW; -.
DR   PDBsum; 8FKX; -.
DR   PDBsum; 8FKY; -.
DR   PDBsum; 8FKZ; -.
DR   PDBsum; 8FL2; -.
DR   PDBsum; 8FL3; -.
DR   PDBsum; 8FL4; -.
DR   PDBsum; 8FL6; -.
DR   PDBsum; 8FL7; -.
DR   PDBsum; 8FL9; -.
DR   PDBsum; 8FLA; -.
DR   PDBsum; 8FLB; -.
DR   PDBsum; 8FLC; -.
DR   PDBsum; 8FLD; -.
DR   PDBsum; 8FLE; -.
DR   PDBsum; 8FLF; -.
DR   PDBsum; 8G5Y; -.
DR   PDBsum; 8G5Z; -.
DR   PDBsum; 8G60; -.
DR   PDBsum; 8G61; -.
DR   PDBsum; 8G6J; -.
DR   PDBsum; 8GLP; -.
DR   PDBsum; 8IDT; -.
DR   PDBsum; 8IDY; -.
DR   PDBsum; 8IE3; -.
DR   PDBsum; 8INE; -.
DR   PDBsum; 8INF; -.
DR   PDBsum; 8INK; -.
DR   PDBsum; 8IPD; -.
DR   PDBsum; 8IPX; -.
DR   PDBsum; 8IPY; -.
DR   PDBsum; 8IR1; -.
DR   PDBsum; 8IR3; -.
DR   PDBsum; 8JDJ; -.
DR   PDBsum; 8JDK; -.
DR   PDBsum; 8JDL; -.
DR   PDBsum; 8JDM; -.
DR   AlphaFoldDB; P18621; -.
DR   EMDB; EMD-0948; -.
DR   EMDB; EMD-0963; -.
DR   EMDB; EMD-0964; -.
DR   EMDB; EMD-0978; -.
DR   EMDB; EMD-10668; -.
DR   EMDB; EMD-10674; -.
DR   EMDB; EMD-10690; -.
DR   EMDB; EMD-10709; -.
DR   EMDB; EMD-11098; -.
DR   EMDB; EMD-11099; -.
DR   EMDB; EMD-11100; -.
DR   EMDB; EMD-11288; -.
DR   EMDB; EMD-11289; -.
DR   EMDB; EMD-11292; -.
DR   EMDB; EMD-11299; -.
DR   EMDB; EMD-12189; -.
DR   EMDB; EMD-13094; -.
DR   EMDB; EMD-14181; -.
DR   EMDB; EMD-15113; -.
DR   EMDB; EMD-29252; -.
DR   EMDB; EMD-29253; -.
DR   EMDB; EMD-29254; -.
DR   EMDB; EMD-29255; -.
DR   EMDB; EMD-29256; -.
DR   EMDB; EMD-29257; -.
DR   EMDB; EMD-29258; -.
DR   EMDB; EMD-29259; -.
DR   EMDB; EMD-29260; -.
DR   EMDB; EMD-29261; -.
DR   EMDB; EMD-29262; -.
DR   EMDB; EMD-29265; -.
DR   EMDB; EMD-29266; -.
DR   EMDB; EMD-29267; -.
DR   EMDB; EMD-29268; -.
DR   EMDB; EMD-29269; -.
DR   EMDB; EMD-29271; -.
DR   EMDB; EMD-29272; -.
DR   EMDB; EMD-29273; -.
DR   EMDB; EMD-29274; -.
DR   EMDB; EMD-29275; -.
DR   EMDB; EMD-29276; -.
DR   EMDB; EMD-29277; -.
DR   EMDB; EMD-29757; -.
DR   EMDB; EMD-29758; -.
DR   EMDB; EMD-29759; -.
DR   EMDB; EMD-29760; -.
DR   EMDB; EMD-29771; -.
DR   EMDB; EMD-31465; -.
DR   EMDB; EMD-33329; -.
DR   EMDB; EMD-33330; -.
DR   EMDB; EMD-35370; -.
DR   EMDB; EMD-35371; -.
DR   EMDB; EMD-35375; -.
DR   EMDB; EMD-35596; -.
DR   EMDB; EMD-35597; -.
DR   EMDB; EMD-35599; -.
DR   EMDB; EMD-35639; -.
DR   EMDB; EMD-35649; -.
DR   EMDB; EMD-35651; -.
DR   EMDB; EMD-35672; -.
DR   EMDB; EMD-35673; -.
DR   EMDB; EMD-3883; -.
DR   EMDB; EMD-40205; -.
DR   EMDB; EMD-4070; -.
DR   EMDB; EMD-9701; -.
DR   EMDB; EMD-9702; -.
DR   EMDB; EMD-9703; -.
DR   SMR; P18621; -.
DR   BioGRID; 112059; 560.
DR   BioGRID; 1529331; 12.
DR   ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR   ComplexPortal; CPX-7664; 60S cytosolic large ribosomal subunit, testis-specific variant.
DR   ComplexPortal; CPX-7665; 60S cytosolic large ribosomal subunit, striated muscle variant.
DR   CORUM; P18621; -.
DR   IntAct; P18621; 81.
DR   MINT; P18621; -.
DR   STRING; 9606.ENSP00000463842; -.
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; 9606-ENSP00000397798; -.
DR   PeptideAtlas; P18621; -.
DR   ProteomicsDB; 53603; -. [P18621-1]
DR   ProteomicsDB; 5890; -.
DR   Pumba; P18621; -.
DR   TopDownProteomics; P18621-1; -. [P18621-1]
DR   TopDownProteomics; P18621-2; -. [P18621-2]
DR   Antibodypedia; 65728; 345 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   AGR; HGNC:10307; -.
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   OrthoDB; 5479326at2759; -.
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; 787 hits in 1061 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 96 other cell types or tissues.
DR   ExpressionAtlas; P18621; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; NAS: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:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
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; Ribosomal protein L22/L17; 1.
DR   HAMAP; MF_01331_A; Ribosomal_uL22_A; 1.
DR   InterPro; IPR001063; Ribosomal_uL22.
DR   InterPro; IPR018260; Ribosomal_uL22_CS.
DR   InterPro; IPR005721; Ribosomal_uL22_euk/arc.
DR   InterPro; IPR036394; Ribosomal_uL22_sf.
DR   NCBIfam; TIGR01038; uL22_arch_euk; 1.
DR   PANTHER; PTHR11593; 60S RIBOSOMAL PROTEIN L17; 1.
DR   PANTHER; PTHR11593:SF10; 60S RIBOSOMAL PROTEIN L17; 1.
DR   Pfam; PF00237; Ribosomal_L22; 1.
DR   SUPFAM; SSF54843; Ribosomal protein L22; 1.
DR   PROSITE; PS00464; RIBOSOMAL_L22; 1.
DR   Genevisible; P18621; HS.
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="Large ribosomal subunit protein uL22"
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
//