RL7_HUMAN
ID RL7_HUMAN Reviewed; 248 AA.
AC P18124; A8K504; Q15289; Q3KQU0; Q5I0X1; Q6IBM9;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=60S ribosomal protein L7;
DE AltName: Full=Large ribosomal subunit protein uL30 {ECO:0000303|PubMed:24524803};
GN Name=RPL7;
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], AND CHARACTERIZATION.
RX PubMed=8441630; DOI=10.1093/nar/21.2.223;
RA Hemmerich P., von Mikecz A., Neumann F., Soezen O., Wolff-Vorbeck G.,
RA Zoebelein R., Krawinkel U.;
RT "Structural and functional properties of ribosomal protein L7 from humans
RT and rodents.";
RL Nucleic Acids Res. 21:223-231(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fibroblast;
RX PubMed=8360149; DOI=10.1016/s0021-9258(17)46650-6;
RA Seshadri T., Uzman J.A., Oshima J., Campisi J.;
RT "Identification of a transcript that is down-regulated in senescent human
RT fibroblasts. Cloning, sequence analysis, and regulation of the human L7
RT ribosomal protein gene.";
RL J. Biol. Chem. 268:18474-18480(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Schneider R., Herzog H., Hfferer L., Schweiger M.;
RL Submitted (MAY-1990) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, Eye, Lung, Mammary gland, Muscle, and Skin;
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 1-7; 10-20; 48-53; 77-88; 107-113; 128-156; 167-177;
RP 201-212 AND 224-242, ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.;
RL Submitted (JUL-2007) to UniProtKB.
RN [8]
RP CHARACTERIZATION.
RX PubMed=7862521; DOI=10.1093/nar/23.2.195;
RA Neumann F., Hemmerich P., von Mikecz A., Peter H.-H., Krawinkel U.;
RT "Human ribosomal protein L7 inhibits cell-free translation in reticulocyte
RT lysates and affects the expression of nuclear proteins upon stable
RT transfection into Jurkat T-lymphoma cells.";
RL Nucleic Acids Res. 23:195-202(1995).
RN [9]
RP ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND
RP 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 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-139, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-124, 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 [14]
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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-17, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [17]
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 [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP INTERACTION WITH DHX33.
RX PubMed=26100019; DOI=10.1128/mcb.00315-15;
RA Zhang Y., You J., Wang X., Weber J.;
RT "The DHX33 RNA Helicase Promotes mRNA Translation Initiation.";
RL Mol. Cell. Biol. 35:2918-2931(2015).
RN [20]
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 [21]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME, FUNCTION,
RP SUBUNIT, AND 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 [22] {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). Binds to
CC G-rich structures in 28S rRNA and in mRNAs (PubMed:12962325). Plays a
CC regulatory role in the translation apparatus; inhibits cell-free
CC translation of mRNAs (PubMed:12962325). {ECO:0000269|PubMed:23636399,
CC ECO:0000269|PubMed:32669547, ECO:0000305|PubMed:12962325}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (PubMed:12962325,
CC PubMed:23636399, PubMed:32669547). Homodimer (PubMed:12962325).
CC Interacts with DHX33 (PubMed:26100019). {ECO:0000269|PubMed:23636399,
CC ECO:0000269|PubMed:26100019, ECO:0000269|PubMed:32669547,
CC ECO:0000305|PubMed:12962325}.
CC -!- INTERACTION:
CC P18124; O00410: IPO5; NbExp=4; IntAct=EBI-350806, EBI-356424;
CC P18124; Q15843: NEDD8; NbExp=2; IntAct=EBI-350806, EBI-716247;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL30 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA41026.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X57958; CAA41026.1; ALT_INIT; mRNA.
DR EMBL; X57959; CAA41027.1; -; mRNA.
DR EMBL; L16558; AAA03081.1; -; mRNA.
DR EMBL; X52967; CAA37139.1; -; mRNA.
DR EMBL; CR456773; CAG33054.1; -; mRNA.
DR EMBL; AK291119; BAF83808.1; -; mRNA.
DR EMBL; AK313365; BAG36165.1; -; mRNA.
DR EMBL; BC006095; AAH06095.1; -; mRNA.
DR EMBL; BC008850; AAH08850.1; -; mRNA.
DR EMBL; BC009599; AAH09599.1; -; mRNA.
DR EMBL; BC071671; AAH71671.1; -; mRNA.
DR EMBL; BC071894; AAH71894.1; -; mRNA.
DR EMBL; BC071895; AAH71895.1; -; mRNA.
DR EMBL; BC087837; AAH87837.1; -; mRNA.
DR CCDS; CCDS6212.1; -.
DR PIR; S11709; R5HU7.
DR RefSeq; NP_000962.2; NM_000971.3.
DR PDB; 4UG0; EM; -; LF=1-248.
DR PDB; 4V6X; EM; 5.00 A; CF=1-248.
DR PDB; 5AJ0; EM; 3.50 A; AF=1-248.
DR PDB; 5LKS; EM; 3.60 A; LF=1-248.
DR PDB; 5T2C; EM; 3.60 A; m=1-248.
DR PDB; 6IP5; EM; 3.90 A; 2A=1-248.
DR PDB; 6IP6; EM; 4.50 A; 2A=1-248.
DR PDB; 6IP8; EM; 3.90 A; 2A=1-248.
DR PDB; 6LQM; EM; 3.09 A; w=1-248.
DR PDB; 6LSR; EM; 3.13 A; w=1-248.
DR PDB; 6LSS; EM; 3.23 A; p=1-248.
DR PDB; 6LU8; EM; 3.13 A; p=1-248.
DR PDB; 6OLE; EM; 3.10 A; H=24-248.
DR PDB; 6OLF; EM; 3.90 A; H=24-248.
DR PDB; 6OLG; EM; 3.40 A; AF=15-248.
DR PDB; 6OLI; EM; 3.50 A; H=24-248.
DR PDB; 6OLZ; EM; 3.90 A; AF=15-248.
DR PDB; 6OM0; EM; 3.10 A; H=24-248.
DR PDB; 6OM7; EM; 3.70 A; H=24-248.
DR PDB; 6QZP; EM; 2.90 A; LF=24-248.
DR PDB; 6W6L; EM; 3.84 A; H=1-248.
DR PDB; 6XA1; EM; 2.80 A; LF=24-248.
DR PDB; 6Y0G; EM; 3.20 A; LF=1-248.
DR PDB; 6Y2L; EM; 3.00 A; LF=1-248.
DR PDB; 6Y57; EM; 3.50 A; LF=1-248.
DR PDB; 6Y6X; EM; 2.80 A; LF=24-248.
DR PDB; 6Z6L; EM; 3.00 A; LF=1-248.
DR PDB; 6Z6M; EM; 3.10 A; LF=1-248.
DR PDB; 6Z6N; EM; 2.90 A; LF=1-248.
DR PDB; 6ZM7; EM; 2.70 A; LF=1-248.
DR PDB; 6ZME; EM; 3.00 A; LF=1-248.
DR PDB; 6ZMI; EM; 2.60 A; LF=1-248.
DR PDB; 6ZMO; EM; 3.10 A; LF=1-248.
DR PDB; 7BHP; EM; 3.30 A; LF=1-248.
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; P18124; -.
DR SMR; P18124; -.
DR BioGRID; 112049; 387.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; P18124; -.
DR IntAct; P18124; 112.
DR MINT; P18124; -.
DR STRING; 9606.ENSP00000339795; -.
DR GlyGen; P18124; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P18124; -.
DR MetOSite; P18124; -.
DR PhosphoSitePlus; P18124; -.
DR SwissPalm; P18124; -.
DR BioMuta; RPL7; -.
DR DMDM; 133021; -.
DR SWISS-2DPAGE; P18124; -.
DR EPD; P18124; -.
DR jPOST; P18124; -.
DR MassIVE; P18124; -.
DR MaxQB; P18124; -.
DR PaxDb; P18124; -.
DR PeptideAtlas; P18124; -.
DR PRIDE; P18124; -.
DR ProteomicsDB; 53549; -.
DR TopDownProteomics; P18124; -.
DR Antibodypedia; 25169; 259 antibodies from 30 providers.
DR DNASU; 6129; -.
DR Ensembl; ENST00000352983.7; ENSP00000339795.2; ENSG00000147604.14.
DR GeneID; 6129; -.
DR KEGG; hsa:6129; -.
DR MANE-Select; ENST00000352983.7; ENSP00000339795.2; NM_000971.4; NP_000962.2.
DR UCSC; uc003xzg.4; human.
DR CTD; 6129; -.
DR DisGeNET; 6129; -.
DR GeneCards; RPL7; -.
DR HGNC; HGNC:10363; RPL7.
DR HPA; ENSG00000147604; Low tissue specificity.
DR MIM; 604166; gene.
DR neXtProt; NX_P18124; -.
DR OpenTargets; ENSG00000147604; -.
DR PharmGKB; PA34759; -.
DR VEuPathDB; HostDB:ENSG00000147604; -.
DR eggNOG; KOG3184; Eukaryota.
DR GeneTree; ENSGT00950000182878; -.
DR InParanoid; P18124; -.
DR OMA; TKKTNHF; -.
DR OrthoDB; 1544778at2759; -.
DR PhylomeDB; P18124; -.
DR TreeFam; TF300740; -.
DR PathwayCommons; P18124; -.
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; P18124; -.
DR SIGNOR; P18124; -.
DR BioGRID-ORCS; 6129; 801 hits in 1057 CRISPR screens.
DR ChiTaRS; RPL7; human.
DR GeneWiki; RPL7; -.
DR GenomeRNAi; 6129; -.
DR Pharos; P18124; Tbio.
DR PRO; PR:P18124; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P18124; protein.
DR Bgee; ENSG00000147604; Expressed in ganglionic eminence and 157 other tissues.
DR ExpressionAtlas; P18124; baseline and differential.
DR Genevisible; P18124; HS.
DR GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
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:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0003729; F:mRNA binding; IDA:MGI.
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; IC:FlyBase.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR CDD; cd01657; Ribosomal_L7_archeal_euk; 1.
DR Gene3D; 3.30.1390.20; -; 2.
DR InterPro; IPR036919; L30_ferredoxin-like_sf.
DR InterPro; IPR018038; Ribosomal_L30_CS.
DR InterPro; IPR016082; Ribosomal_L30_ferredoxin-like.
DR InterPro; IPR012988; Ribosomal_L30_N.
DR InterPro; IPR039699; Ribosomal_L7/L30.
DR InterPro; IPR005998; Ribosomal_L7_euk.
DR InterPro; IPR035808; Ribosomal_L7_euk_arc.
DR PANTHER; PTHR11524; PTHR11524; 1.
DR Pfam; PF00327; Ribosomal_L30; 1.
DR Pfam; PF08079; Ribosomal_L30_N; 1.
DR SUPFAM; SSF55129; SSF55129; 1.
DR TIGRFAMs; TIGR01310; uL30_euk; 1.
DR PROSITE; PS00634; RIBOSOMAL_L30; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding.
FT CHAIN 1..248
FT /note="60S ribosomal protein L7"
FT /id="PRO_0000104633"
FT REPEAT 7..18
FT /note="1"
FT REPEAT 19..30
FT /note="2"
FT REPEAT 31..42
FT /note="3"
FT REPEAT 43..54
FT /note="4"
FT REGION 7..54
FT /note="4 X 12 AA tandem repeats"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:12962325, ECO:0000269|Ref.7,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378"
FT MOD_RES 17
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 124
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 127
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P14148"
FT MOD_RES 139
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT CONFLICT 48
FT /note="K -> E (in Ref. 4; CAG33054)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="R -> L (in Ref. 1; CAA41026/CAA41027)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="G -> A (in Ref. 1; CAA41026)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="R -> Q (in Ref. 1; CAA41026)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="A -> S (in Ref. 2; AAA03081)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="H -> R (in Ref. 4; CAG33054)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 29226 MW; 070EB4C904E6795A CRC64;
MEGVEEKKKE VPAVPETLKK KRRNFAELKI KRLRKKFAQK MLRKARRKLI YEKAKHYHKE
YRQMYRTEIR MARMARKAGN FYVPAEPKLA FVIRIRGING VSPKVRKVLQ LLRLRQIFNG
TFVKLNKASI NMLRIVEPYI AWGYPNLKSV NELIYKRGYG KINKKRIALT DNALIARSLG
KYGIICMEDL IHEIYTVGKR FKEANNFLWP FKLSSPRGGM KKKTTHFVEG GDAGNREDQI
NRLIRRMN
