Full text data of RPL17
RPL17
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
60S ribosomal protein L17 (60S ribosomal protein L23; PD-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
60S ribosomal protein L17 (60S ribosomal protein L23; PD-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P18621
ID RL17_HUMAN Reviewed; 184 AA.
AC P18621; B2R4H3; B4E3C2; B5ME31; J3QL51; Q3KQW2; Q6NZ54; Q7M4M5;
read moreDT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 145.
DE RecName: 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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT Halobacterium 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
RT analysis of 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
RA Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
RA Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
RA Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
RA Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 2-10, AND MASS SPECTROMETRY.
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.,
RA Karpova G.G.;
RT "Characterization and analysis of posttranslational modifications of
RT the human large cytoplasmic ribosomal subunit proteins by mass
RT spectrometry and 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,
RP CLEAVAGE OF INITIATOR METHIONINE, AND 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;
RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N.,
RA Hudson T.J., Tanaka T., Page D.C.;
RT "A map of 75 human ribosomal protein genes.";
RL Genome Res. 8:509-523(1998).
RN [12]
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
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.,
RA Buerckstuemmer T., 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 [17]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
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).
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
CC duct, gall bladder, kidney and liver. Expressed at high levels in
CC the well differentiated pancreatic tumor cell lines HPAF, COLO 357
CC and Capan-1, the moderately differentiated pancreatic tumor cell
CC lines T3M-4, AsPc-1 and BxPc-3, the poorly differentiated
CC pancreatic tumor cell line MIA PaCa-2, and the pancreatic tumor
CC cell lines of undefined differentiation status such as SW979.
CC Expressed at lower levels in the poorly differentiated pancreatic
CC tumor cell lines HCG-25 and PANC-1.
CC -!- SIMILARITY: Belongs to the ribosomal protein L22P family.
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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 PIR; A61192; A61192.
DR PIR; S11218; R5HU22.
DR RefSeq; NP_000976.1; NM_000985.4.
DR RefSeq; NP_001030178.1; NM_001035006.2.
DR RefSeq; NP_001186269.1; NM_001199340.1.
DR RefSeq; NP_001186270.1; NM_001199341.1.
DR RefSeq; NP_001186271.1; NM_001199342.1.
DR RefSeq; NP_001186272.1; NM_001199343.1.
DR RefSeq; NP_001186273.1; NM_001199344.1.
DR RefSeq; NP_001186274.1; NM_001199345.1.
DR RefSeq; NP_001186284.1; NM_001199355.1.
DR UniGene; Hs.293653; -.
DR UniGene; Hs.374588; -.
DR UniGene; Hs.485081; -.
DR UniGene; Hs.603040; -.
DR PDB; 3J3B; EM; 5.00 A; P=1-184.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; P18621; -.
DR SMR; P18621; 2-179.
DR IntAct; P18621; 29.
DR MINT; MINT-1393841; -.
DR STRING; 9606.ENSP00000389465; -.
DR PhosphoSite; P18621; -.
DR DMDM; 132799; -.
DR PaxDb; P18621; -.
DR PRIDE; P18621; -.
DR DNASU; 6139; -.
DR Ensembl; ENST00000418495; ENSP00000397798; ENSG00000265681.
DR Ensembl; ENST00000579248; ENSP00000462023; ENSG00000265681.
DR Ensembl; ENST00000579408; ENSP00000463842; ENSG00000265681.
DR Ensembl; ENST00000580261; ENSP00000462385; ENSG00000265681.
DR Ensembl; ENST00000581373; ENSP00000462944; ENSG00000265681.
DR GeneID; 100526842; -.
DR GeneID; 6139; -.
DR KEGG; hsa:100526842; -.
DR KEGG; hsa:6139; -.
DR UCSC; uc002ldm.2; human.
DR CTD; 100526842; -.
DR CTD; 6139; -.
DR GeneCards; GC18M047009; -.
DR GeneCards; GC18M047014; -.
DR HGNC; HGNC:10307; RPL17.
DR HPA; HPA043724; -.
DR HPA; HPA046385; -.
DR MIM; 603661; gene.
DR neXtProt; NX_P18621; -.
DR PharmGKB; PA34676; -.
DR eggNOG; COG0091; -.
DR HOGENOM; HOG000205045; -.
DR HOVERGEN; HBG000955; -.
DR InParanoid; P18621; -.
DR KO; K02880; -.
DR OMA; MHIRKAN; -.
DR OrthoDB; EOG70GMHF; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; RPL17; -.
DR GenomeRNAi; 100526842; -.
DR NextBio; 23849; -.
DR PRO; PR:P18621; -.
DR ArrayExpress; P18621; -.
DR Bgee; P18621; -.
DR CleanEx; HS_RPL17; -.
DR Genevestigator; P18621; -.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006414; P:translational elongation; TAS:Reactome.
DR GO; GO:0006413; P:translational initiation; TAS:Reactome.
DR GO; GO:0006415; P:translational termination; TAS:Reactome.
DR GO; GO:0019083; P:viral transcription; TAS:Reactome.
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 PANTHER; PTHR11593; PTHR11593; 1.
DR Pfam; PF00237; Ribosomal_L22; 1.
DR SUPFAM; SSF54843; SSF54843; 1.
DR TIGRFAMs; TIGR01038; L22_arch; 1.
DR PROSITE; PS00464; RIBOSOMAL_L22; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 184 60S ribosomal protein L17.
FT /FTId=PRO_0000125331.
FT MOD_RES 5 5 Phosphoserine.
FT VAR_SEQ 1 38 Missing (in isoform 2).
FT /FTId=VSP_045445.
FT VAR_SEQ 170 184 ISQKKLKKQKLMARE -> LRSSSLGKWCAFLVSSFQFCSG
FT STKNSWSHIYTLWFPPSLVVYGLRKQYKNPMIQTKAK (in
FT isoform 3).
FT /FTId=VSP_046965.
FT CONFLICT 133 133 H -> R (in Ref. 8; AAH66324).
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
//
ID RL17_HUMAN Reviewed; 184 AA.
AC P18621; B2R4H3; B4E3C2; B5ME31; J3QL51; Q3KQW2; Q6NZ54; Q7M4M5;
read moreDT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 145.
DE RecName: 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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT Halobacterium 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
RT analysis of 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
RA Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
RA Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
RA Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
RA Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 2-10, AND MASS SPECTROMETRY.
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.,
RA Karpova G.G.;
RT "Characterization and analysis of posttranslational modifications of
RT the human large cytoplasmic ribosomal subunit proteins by mass
RT spectrometry and 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,
RP CLEAVAGE OF INITIATOR METHIONINE, AND 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;
RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N.,
RA Hudson T.J., Tanaka T., Page D.C.;
RT "A map of 75 human ribosomal protein genes.";
RL Genome Res. 8:509-523(1998).
RN [12]
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
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.,
RA Buerckstuemmer T., 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 [17]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
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).
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
CC duct, gall bladder, kidney and liver. Expressed at high levels in
CC the well differentiated pancreatic tumor cell lines HPAF, COLO 357
CC and Capan-1, the moderately differentiated pancreatic tumor cell
CC lines T3M-4, AsPc-1 and BxPc-3, the poorly differentiated
CC pancreatic tumor cell line MIA PaCa-2, and the pancreatic tumor
CC cell lines of undefined differentiation status such as SW979.
CC Expressed at lower levels in the poorly differentiated pancreatic
CC tumor cell lines HCG-25 and PANC-1.
CC -!- SIMILARITY: Belongs to the ribosomal protein L22P family.
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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 PIR; A61192; A61192.
DR PIR; S11218; R5HU22.
DR RefSeq; NP_000976.1; NM_000985.4.
DR RefSeq; NP_001030178.1; NM_001035006.2.
DR RefSeq; NP_001186269.1; NM_001199340.1.
DR RefSeq; NP_001186270.1; NM_001199341.1.
DR RefSeq; NP_001186271.1; NM_001199342.1.
DR RefSeq; NP_001186272.1; NM_001199343.1.
DR RefSeq; NP_001186273.1; NM_001199344.1.
DR RefSeq; NP_001186274.1; NM_001199345.1.
DR RefSeq; NP_001186284.1; NM_001199355.1.
DR UniGene; Hs.293653; -.
DR UniGene; Hs.374588; -.
DR UniGene; Hs.485081; -.
DR UniGene; Hs.603040; -.
DR PDB; 3J3B; EM; 5.00 A; P=1-184.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; P18621; -.
DR SMR; P18621; 2-179.
DR IntAct; P18621; 29.
DR MINT; MINT-1393841; -.
DR STRING; 9606.ENSP00000389465; -.
DR PhosphoSite; P18621; -.
DR DMDM; 132799; -.
DR PaxDb; P18621; -.
DR PRIDE; P18621; -.
DR DNASU; 6139; -.
DR Ensembl; ENST00000418495; ENSP00000397798; ENSG00000265681.
DR Ensembl; ENST00000579248; ENSP00000462023; ENSG00000265681.
DR Ensembl; ENST00000579408; ENSP00000463842; ENSG00000265681.
DR Ensembl; ENST00000580261; ENSP00000462385; ENSG00000265681.
DR Ensembl; ENST00000581373; ENSP00000462944; ENSG00000265681.
DR GeneID; 100526842; -.
DR GeneID; 6139; -.
DR KEGG; hsa:100526842; -.
DR KEGG; hsa:6139; -.
DR UCSC; uc002ldm.2; human.
DR CTD; 100526842; -.
DR CTD; 6139; -.
DR GeneCards; GC18M047009; -.
DR GeneCards; GC18M047014; -.
DR HGNC; HGNC:10307; RPL17.
DR HPA; HPA043724; -.
DR HPA; HPA046385; -.
DR MIM; 603661; gene.
DR neXtProt; NX_P18621; -.
DR PharmGKB; PA34676; -.
DR eggNOG; COG0091; -.
DR HOGENOM; HOG000205045; -.
DR HOVERGEN; HBG000955; -.
DR InParanoid; P18621; -.
DR KO; K02880; -.
DR OMA; MHIRKAN; -.
DR OrthoDB; EOG70GMHF; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; RPL17; -.
DR GenomeRNAi; 100526842; -.
DR NextBio; 23849; -.
DR PRO; PR:P18621; -.
DR ArrayExpress; P18621; -.
DR Bgee; P18621; -.
DR CleanEx; HS_RPL17; -.
DR Genevestigator; P18621; -.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006414; P:translational elongation; TAS:Reactome.
DR GO; GO:0006413; P:translational initiation; TAS:Reactome.
DR GO; GO:0006415; P:translational termination; TAS:Reactome.
DR GO; GO:0019083; P:viral transcription; TAS:Reactome.
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 PANTHER; PTHR11593; PTHR11593; 1.
DR Pfam; PF00237; Ribosomal_L22; 1.
DR SUPFAM; SSF54843; SSF54843; 1.
DR TIGRFAMs; TIGR01038; L22_arch; 1.
DR PROSITE; PS00464; RIBOSOMAL_L22; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 184 60S ribosomal protein L17.
FT /FTId=PRO_0000125331.
FT MOD_RES 5 5 Phosphoserine.
FT VAR_SEQ 1 38 Missing (in isoform 2).
FT /FTId=VSP_045445.
FT VAR_SEQ 170 184 ISQKKLKKQKLMARE -> LRSSSLGKWCAFLVSSFQFCSG
FT STKNSWSHIYTLWFPPSLVVYGLRKQYKNPMIQTKAK (in
FT isoform 3).
FT /FTId=VSP_046965.
FT CONFLICT 133 133 H -> R (in Ref. 8; AAH66324).
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
//
MIM
603661
*RECORD*
*FIELD* NO
603661
*FIELD* TI
*603661 RIBOSOMAL PROTEIN L17; RPL17
*FIELD* TX
The mammalian ribosome is composed of 4 RNA species (see 180450) and
read moreapproximately 80 different proteins.
Mager and Freeman (1990) isolated human peripheral blood cDNAs encoding
ribosomal protein L17 (RPL17), which they called humrprel or the
ribosomal protein L23 gene (GenBank GENBANK X53777). The deduced
184-amino acid RPL17 protein is 33% identical to the ribosomal protein
L23 from Halobacterium marismortui. RPL17 was expressed as an
approximately 750-bp transcript in all cell types tested. Southern blot
analysis indicated that the human genome contains multiple copies of the
RPL17 gene.
Using somatic cell hybrid and radiation hybrid mapping analyses,
Kenmochi et al. (1998) mapped the RPL17 gene to 18q.
Nomenclature: The gene referred to as the ribosomal protein L23 gene by
Mager and Freeman (1990) in their GenBank submission (GENBANK X53777)
has been given the gene symbol RPL17 by the HUGO Nomenclature Committee.
*FIELD* RF
1. Kenmochi, N.; Kawaguchi, T.; Rozen, S.; Davis, E.; Goodman, N.;
Hudson, T. J.; Tanaka, T.; Page, D. C.: A map of 75 human ribosomal
protein genes. Genome Res. 8: 509-523, 1998.
2. Mager, D. L.; Freeman, J. D.: A human gene related to the ribosomal
protein L23 gene of Halobacterium marismortui. Nucleic Acids Res. 18:
5301 only, 1990.
*FIELD* CD
Patti M. Sherman: 3/19/1999
*FIELD* ED
carol: 04/07/1999
*RECORD*
*FIELD* NO
603661
*FIELD* TI
*603661 RIBOSOMAL PROTEIN L17; RPL17
*FIELD* TX
The mammalian ribosome is composed of 4 RNA species (see 180450) and
read moreapproximately 80 different proteins.
Mager and Freeman (1990) isolated human peripheral blood cDNAs encoding
ribosomal protein L17 (RPL17), which they called humrprel or the
ribosomal protein L23 gene (GenBank GENBANK X53777). The deduced
184-amino acid RPL17 protein is 33% identical to the ribosomal protein
L23 from Halobacterium marismortui. RPL17 was expressed as an
approximately 750-bp transcript in all cell types tested. Southern blot
analysis indicated that the human genome contains multiple copies of the
RPL17 gene.
Using somatic cell hybrid and radiation hybrid mapping analyses,
Kenmochi et al. (1998) mapped the RPL17 gene to 18q.
Nomenclature: The gene referred to as the ribosomal protein L23 gene by
Mager and Freeman (1990) in their GenBank submission (GENBANK X53777)
has been given the gene symbol RPL17 by the HUGO Nomenclature Committee.
*FIELD* RF
1. Kenmochi, N.; Kawaguchi, T.; Rozen, S.; Davis, E.; Goodman, N.;
Hudson, T. J.; Tanaka, T.; Page, D. C.: A map of 75 human ribosomal
protein genes. Genome Res. 8: 509-523, 1998.
2. Mager, D. L.; Freeman, J. D.: A human gene related to the ribosomal
protein L23 gene of Halobacterium marismortui. Nucleic Acids Res. 18:
5301 only, 1990.
*FIELD* CD
Patti M. Sherman: 3/19/1999
*FIELD* ED
carol: 04/07/1999