Full text data of RPL7
RPL7
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
60S ribosomal protein L7
Note: presumably soluble (membrane word is not in UniProt keywords or features)
60S ribosomal protein L7
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P18124
ID RL7_HUMAN Reviewed; 248 AA.
AC P18124; A8K504; Q15289; Q3KQU0; Q5I0X1; Q6IBM9;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1990, sequence version 1.
DT 22-JAN-2014, entry version 148.
DE RecName: Full=60S ribosomal protein L7;
GN Name=RPL7;
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], 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
RT humans and rodents.";
RL Nucleic Acids Res. 21:223-231(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fibroblast;
RX PubMed=8360149;
RA Seshadri T., Uzman J.A., Oshima J., Campisi J.;
RT "Identification of a transcript that is down-regulated in senescent
RT human fibroblasts. Cloning, sequence analysis, and regulation of the
RT human L7 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.,
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 [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
RT project: 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;
RP 167-177; 201-212 AND 224-242, ACETYLATION AT MET-1, AND 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
RT reticulocyte lysates and affects the expression of nuclear proteins
RT upon stable transfection into Jurkat T-lymphoma cells.";
RL Nucleic Acids Res. 23:195-202(1995).
RN [9]
RP MASS SPECTROMETRY, AND PROBABLE ACETYLATION AT MET-1.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-139, AND MASS
RP SPECTROMETRY.
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
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-124, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [13]
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.
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 -!- FUNCTION: Binds to G-rich structures in 28S rRNA and in mRNAs.
CC Plays a regulatory role in the translation apparatus; inhibits
CC cell-free translation of mRNAs.
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC O00410:IPO5; NbExp=4; IntAct=EBI-350806, EBI-356424;
CC Q15843:NEDD8; NbExp=2; IntAct=EBI-350806, EBI-716247;
CC -!- SIMILARITY: Belongs to the ribosomal protein L30P family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA41026.1; Type=Erroneous initiation;
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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 PIR; S11709; R5HU7.
DR RefSeq; NP_000962.2; NM_000971.3.
DR UniGene; Hs.421257; -.
DR UniGene; Hs.571841; -.
DR PDB; 3J3B; EM; 5.00 A; F=1-248.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; P18124; -.
DR SMR; P18124; 20-248.
DR IntAct; P18124; 28.
DR MINT; MINT-1152474; -.
DR STRING; 9606.ENSP00000339795; -.
DR PhosphoSite; P18124; -.
DR DMDM; 133021; -.
DR SWISS-2DPAGE; P18124; -.
DR PaxDb; P18124; -.
DR PRIDE; P18124; -.
DR DNASU; 6129; -.
DR Ensembl; ENST00000352983; ENSP00000339795; ENSG00000147604.
DR GeneID; 6129; -.
DR KEGG; hsa:6129; -.
DR UCSC; uc003xzg.3; human.
DR CTD; 6129; -.
DR GeneCards; GC08M074202; -.
DR H-InvDB; HIX0058339; -.
DR HGNC; HGNC:10363; RPL7.
DR MIM; 604166; gene.
DR neXtProt; NX_P18124; -.
DR PharmGKB; PA34759; -.
DR eggNOG; COG1841; -.
DR HOGENOM; HOG000170917; -.
DR HOVERGEN; HBG003280; -.
DR KO; K02937; -.
DR OMA; KATQQML; -.
DR OrthoDB; EOG7K9K3X; -.
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 ChiTaRS; RPL7; human.
DR GeneWiki; RPL7; -.
DR GenomeRNAi; 6129; -.
DR NextBio; 23805; -.
DR PRO; PR:P18124; -.
DR ArrayExpress; P18124; -.
DR Bgee; P18124; -.
DR CleanEx; HS_RPL7; -.
DR Genevestigator; P18124; -.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003729; F:mRNA binding; IDA:MGI.
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:0042273; P:ribosomal large subunit biogenesis; IMP:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
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; 3.30.1390.20; -; 2.
DR InterPro; IPR018038; Ribosomal_L30_CS.
DR InterPro; IPR016082; Ribosomal_L30_ferredoxin-like.
DR InterPro; IPR012988; Ribosomal_L30_N.
DR InterPro; IPR005998; Ribosomal_L7_euk.
DR Pfam; PF00327; Ribosomal_L30; 1.
DR Pfam; PF08079; Ribosomal_L30_N; 1.
DR SUPFAM; SSF55129; SSF55129; 1.
DR TIGRFAMs; TIGR01310; L7; 1.
DR PROSITE; PS00634; RIBOSOMAL_L30; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; Phosphoprotein; Reference proteome; Repeat;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding.
FT CHAIN 1 248 60S ribosomal protein L7.
FT /FTId=PRO_0000104633.
FT REPEAT 7 18 1.
FT REPEAT 19 30 2.
FT REPEAT 31 42 3.
FT REPEAT 43 54 4.
FT REGION 7 54 4 X 12 AA tandem repeats.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 124 124 N6-acetyllysine.
FT MOD_RES 139 139 Phosphotyrosine.
FT CONFLICT 48 48 K -> E (in Ref. 4; CAG33054).
FT CONFLICT 157 157 R -> L (in Ref. 1; CAA41026/CAA41027).
FT CONFLICT 160 160 G -> A (in Ref. 1; CAA41026).
FT CONFLICT 166 166 R -> Q (in Ref. 1; CAA41026).
FT CONFLICT 173 173 A -> S (in Ref. 2; AAA03081).
FT CONFLICT 192 192 H -> R (in Ref. 4; CAG33054).
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
//
ID RL7_HUMAN Reviewed; 248 AA.
AC P18124; A8K504; Q15289; Q3KQU0; Q5I0X1; Q6IBM9;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1990, sequence version 1.
DT 22-JAN-2014, entry version 148.
DE RecName: Full=60S ribosomal protein L7;
GN Name=RPL7;
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], 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
RT humans and rodents.";
RL Nucleic Acids Res. 21:223-231(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fibroblast;
RX PubMed=8360149;
RA Seshadri T., Uzman J.A., Oshima J., Campisi J.;
RT "Identification of a transcript that is down-regulated in senescent
RT human fibroblasts. Cloning, sequence analysis, and regulation of the
RT human L7 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.,
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 [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
RT project: 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;
RP 167-177; 201-212 AND 224-242, ACETYLATION AT MET-1, AND 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
RT reticulocyte lysates and affects the expression of nuclear proteins
RT upon stable transfection into Jurkat T-lymphoma cells.";
RL Nucleic Acids Res. 23:195-202(1995).
RN [9]
RP MASS SPECTROMETRY, AND PROBABLE ACETYLATION AT MET-1.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-139, AND MASS
RP SPECTROMETRY.
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
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-124, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [13]
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.
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 -!- FUNCTION: Binds to G-rich structures in 28S rRNA and in mRNAs.
CC Plays a regulatory role in the translation apparatus; inhibits
CC cell-free translation of mRNAs.
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC O00410:IPO5; NbExp=4; IntAct=EBI-350806, EBI-356424;
CC Q15843:NEDD8; NbExp=2; IntAct=EBI-350806, EBI-716247;
CC -!- SIMILARITY: Belongs to the ribosomal protein L30P family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA41026.1; Type=Erroneous initiation;
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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 PIR; S11709; R5HU7.
DR RefSeq; NP_000962.2; NM_000971.3.
DR UniGene; Hs.421257; -.
DR UniGene; Hs.571841; -.
DR PDB; 3J3B; EM; 5.00 A; F=1-248.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; P18124; -.
DR SMR; P18124; 20-248.
DR IntAct; P18124; 28.
DR MINT; MINT-1152474; -.
DR STRING; 9606.ENSP00000339795; -.
DR PhosphoSite; P18124; -.
DR DMDM; 133021; -.
DR SWISS-2DPAGE; P18124; -.
DR PaxDb; P18124; -.
DR PRIDE; P18124; -.
DR DNASU; 6129; -.
DR Ensembl; ENST00000352983; ENSP00000339795; ENSG00000147604.
DR GeneID; 6129; -.
DR KEGG; hsa:6129; -.
DR UCSC; uc003xzg.3; human.
DR CTD; 6129; -.
DR GeneCards; GC08M074202; -.
DR H-InvDB; HIX0058339; -.
DR HGNC; HGNC:10363; RPL7.
DR MIM; 604166; gene.
DR neXtProt; NX_P18124; -.
DR PharmGKB; PA34759; -.
DR eggNOG; COG1841; -.
DR HOGENOM; HOG000170917; -.
DR HOVERGEN; HBG003280; -.
DR KO; K02937; -.
DR OMA; KATQQML; -.
DR OrthoDB; EOG7K9K3X; -.
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 ChiTaRS; RPL7; human.
DR GeneWiki; RPL7; -.
DR GenomeRNAi; 6129; -.
DR NextBio; 23805; -.
DR PRO; PR:P18124; -.
DR ArrayExpress; P18124; -.
DR Bgee; P18124; -.
DR CleanEx; HS_RPL7; -.
DR Genevestigator; P18124; -.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003729; F:mRNA binding; IDA:MGI.
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:0042273; P:ribosomal large subunit biogenesis; IMP:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
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; 3.30.1390.20; -; 2.
DR InterPro; IPR018038; Ribosomal_L30_CS.
DR InterPro; IPR016082; Ribosomal_L30_ferredoxin-like.
DR InterPro; IPR012988; Ribosomal_L30_N.
DR InterPro; IPR005998; Ribosomal_L7_euk.
DR Pfam; PF00327; Ribosomal_L30; 1.
DR Pfam; PF08079; Ribosomal_L30_N; 1.
DR SUPFAM; SSF55129; SSF55129; 1.
DR TIGRFAMs; TIGR01310; L7; 1.
DR PROSITE; PS00634; RIBOSOMAL_L30; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; Phosphoprotein; Reference proteome; Repeat;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding.
FT CHAIN 1 248 60S ribosomal protein L7.
FT /FTId=PRO_0000104633.
FT REPEAT 7 18 1.
FT REPEAT 19 30 2.
FT REPEAT 31 42 3.
FT REPEAT 43 54 4.
FT REGION 7 54 4 X 12 AA tandem repeats.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 124 124 N6-acetyllysine.
FT MOD_RES 139 139 Phosphotyrosine.
FT CONFLICT 48 48 K -> E (in Ref. 4; CAG33054).
FT CONFLICT 157 157 R -> L (in Ref. 1; CAA41026/CAA41027).
FT CONFLICT 160 160 G -> A (in Ref. 1; CAA41026).
FT CONFLICT 166 166 R -> Q (in Ref. 1; CAA41026).
FT CONFLICT 173 173 A -> S (in Ref. 2; AAA03081).
FT CONFLICT 192 192 H -> R (in Ref. 4; CAG33054).
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
//
MIM
604166
*RECORD*
*FIELD* NO
604166
*FIELD* TI
*604166 RIBOSOMAL PROTEIN L7; RPL7
*FIELD* TX
The mammalian ribosome is composed of 4 RNA species (see 180450) and
read moreapproximately 80 different proteins (see 180466).
Meyuhas and Klein (1990) identified a transcriptionally active mouse
Rpl7 gene. The 3.1-kb Rpl7 gene contains 7 exons and encodes an mRNA
that is 897 nucleotides long.
Seshadri et al. (1993) partially sequenced the human RPL7 gene and found
that it shares many features with those of mouse Rpl7, including the
position of the first intron and the polypyrimidine translation control
element in the 5-prime noncoding region.
By screening cDNA libraries derived from activated human T-lymphocyte
cell lines with a mouse Rpl7 cDNA, Hemmerich et al. (1993) isolated
human RPL7 cDNAs. The predicted 248-amino acid human RPL7 protein has an
N-terminal basic leucine zipper (bZIP)-like domain and the RNP consensus
submotif RNP2. The authors demonstrated that the N-terminal region of
mammalian RPL7 proteins mediates RPL7 homodimerization and stable
binding of RPL7 to DNA and RNA in vitro. They found that RPL7
preferentially binds to 28S rRNA and mRNA. Hemmerich et al. (1993)
showed that mouse Rpl7 mRNA is induced upon activation of resting B and
T lymphocytes.
The RPL7 protein has been shown to be an autoantigen in patients with
systemic lupus erythematosus (152700) and other systemic autoimmune
diseases (Absi et al., 1989; von Mikecz et al., 1994; Neu et al., 1995;
von Mikecz et al., 1995).
Sapi et al. (1994) identified a processed pseudogene for ribosomal
protein L7 (RPL7P) within intron 1 of the FMS gene (164770). This
pseudogene was not actively transcribed.
By somatic cell hybrid and radiation hybrid mapping analyses, Kenmochi
et al. (1998) mapped the human RPL7 gene to 8q.
*FIELD* RF
1. Absi, M.; La Vergne, J. P.; Marzouki, A.; Giraud, F.; Rigal, D.;
Reboud, A. M.; Reboud, J. P.; Monier, J. C.: Heterogeneity of ribosomal
autoantibodies from human, murine and canine connective tissue diseases. Immun.
Lett. 23: 35-41, 1989.
2. Hemmerich, P.; von Mikecz, A.; Neumann, F.; Sozeri, O.; Wolff-Vorbeck,
G.; Zoebelein, R.; Krawinkel, U.: Structural and functional properties
of ribosomal protein L7 from humans and rodents. Nucleic Acids Res. 21:
223-231, 1993.
3. 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.
4. Meyuhas, O.; Klein, A.: The mouse ribosomal protein L7 gene: its
primary structure and functional analysis of the promoter region. J.
Biol. Chem. 265: 11465-11473, 1990.
5. Neu, E.; von Mikecz, A. H.; Hemmerich, P. H.; Peter, H. H.; Fricke,
M.; Deicher, H.; Genth, E.; Krawinkel, U.: Autoantibodies against
eukaryotic protein L7 in patients suffering from systemic lupus erythematosus
and progressive systemic sclerosis: frequency and correlation with
clinical, serological and genetic parameters. The SLE Study Group. Clin.
Exp. Immun. 100: 198-204, 1995.
6. Sapi, E.; Flick, M. B.; Kacinski, B. M.: The first intron of human
c-fms proto-oncogene contains a processed pseudogene (RPL7P) for ribosomal
protein L7. Genomics 22: 641-645, 1994.
7. Seshadri, T.; Uzman, J. A.; Oshima, J.; Campisi, J.: Identification
of a transcript that is down-regulated in senescent human fibroblasts. J.
Biol. Chem. 268: 18474-18480, 1993.
8. von Mikecz, A.; Hemmerich, P.; Peter, H. H.; Krawinkel, U.: Characterization
of eukaryotic protein L7 as a novel autoantigen which frequently elicits
an immune response in patients suffering from systemic autoimmune
disease. Immunobiology 192: 137-154, 1994.
9. von Mikecz, A. H.; Hemmerich, P. H.; Peter, H. H.; Krawinkel, U.
: Autoantigenic epitopes on eukaryotic L7. Clin. Exp. Immun. 100:
205-213, 1995.
*FIELD* CD
Patti M. Sherman: 9/10/1999
*FIELD* ED
terry: 08/16/2004
carol: 8/5/2004
joanna: 11/2/2001
mgross: 9/20/1999
psherman: 9/13/1999
*RECORD*
*FIELD* NO
604166
*FIELD* TI
*604166 RIBOSOMAL PROTEIN L7; RPL7
*FIELD* TX
The mammalian ribosome is composed of 4 RNA species (see 180450) and
read moreapproximately 80 different proteins (see 180466).
Meyuhas and Klein (1990) identified a transcriptionally active mouse
Rpl7 gene. The 3.1-kb Rpl7 gene contains 7 exons and encodes an mRNA
that is 897 nucleotides long.
Seshadri et al. (1993) partially sequenced the human RPL7 gene and found
that it shares many features with those of mouse Rpl7, including the
position of the first intron and the polypyrimidine translation control
element in the 5-prime noncoding region.
By screening cDNA libraries derived from activated human T-lymphocyte
cell lines with a mouse Rpl7 cDNA, Hemmerich et al. (1993) isolated
human RPL7 cDNAs. The predicted 248-amino acid human RPL7 protein has an
N-terminal basic leucine zipper (bZIP)-like domain and the RNP consensus
submotif RNP2. The authors demonstrated that the N-terminal region of
mammalian RPL7 proteins mediates RPL7 homodimerization and stable
binding of RPL7 to DNA and RNA in vitro. They found that RPL7
preferentially binds to 28S rRNA and mRNA. Hemmerich et al. (1993)
showed that mouse Rpl7 mRNA is induced upon activation of resting B and
T lymphocytes.
The RPL7 protein has been shown to be an autoantigen in patients with
systemic lupus erythematosus (152700) and other systemic autoimmune
diseases (Absi et al., 1989; von Mikecz et al., 1994; Neu et al., 1995;
von Mikecz et al., 1995).
Sapi et al. (1994) identified a processed pseudogene for ribosomal
protein L7 (RPL7P) within intron 1 of the FMS gene (164770). This
pseudogene was not actively transcribed.
By somatic cell hybrid and radiation hybrid mapping analyses, Kenmochi
et al. (1998) mapped the human RPL7 gene to 8q.
*FIELD* RF
1. Absi, M.; La Vergne, J. P.; Marzouki, A.; Giraud, F.; Rigal, D.;
Reboud, A. M.; Reboud, J. P.; Monier, J. C.: Heterogeneity of ribosomal
autoantibodies from human, murine and canine connective tissue diseases. Immun.
Lett. 23: 35-41, 1989.
2. Hemmerich, P.; von Mikecz, A.; Neumann, F.; Sozeri, O.; Wolff-Vorbeck,
G.; Zoebelein, R.; Krawinkel, U.: Structural and functional properties
of ribosomal protein L7 from humans and rodents. Nucleic Acids Res. 21:
223-231, 1993.
3. 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.
4. Meyuhas, O.; Klein, A.: The mouse ribosomal protein L7 gene: its
primary structure and functional analysis of the promoter region. J.
Biol. Chem. 265: 11465-11473, 1990.
5. Neu, E.; von Mikecz, A. H.; Hemmerich, P. H.; Peter, H. H.; Fricke,
M.; Deicher, H.; Genth, E.; Krawinkel, U.: Autoantibodies against
eukaryotic protein L7 in patients suffering from systemic lupus erythematosus
and progressive systemic sclerosis: frequency and correlation with
clinical, serological and genetic parameters. The SLE Study Group. Clin.
Exp. Immun. 100: 198-204, 1995.
6. Sapi, E.; Flick, M. B.; Kacinski, B. M.: The first intron of human
c-fms proto-oncogene contains a processed pseudogene (RPL7P) for ribosomal
protein L7. Genomics 22: 641-645, 1994.
7. Seshadri, T.; Uzman, J. A.; Oshima, J.; Campisi, J.: Identification
of a transcript that is down-regulated in senescent human fibroblasts. J.
Biol. Chem. 268: 18474-18480, 1993.
8. von Mikecz, A.; Hemmerich, P.; Peter, H. H.; Krawinkel, U.: Characterization
of eukaryotic protein L7 as a novel autoantigen which frequently elicits
an immune response in patients suffering from systemic autoimmune
disease. Immunobiology 192: 137-154, 1994.
9. von Mikecz, A. H.; Hemmerich, P. H.; Peter, H. H.; Krawinkel, U.
: Autoantigenic epitopes on eukaryotic L7. Clin. Exp. Immun. 100:
205-213, 1995.
*FIELD* CD
Patti M. Sherman: 9/10/1999
*FIELD* ED
terry: 08/16/2004
carol: 8/5/2004
joanna: 11/2/2001
mgross: 9/20/1999
psherman: 9/13/1999