Full text data of RPS5
RPS5
[Confidence: low (only semi-automatic identification from reviews)]
40S ribosomal protein S5; 40S ribosomal protein S5, N-terminally processed
Note: presumably soluble (membrane word is not in UniProt keywords or features)
40S ribosomal protein S5; 40S ribosomal protein S5, N-terminally processed
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P46782
ID RS5_HUMAN Reviewed; 204 AA.
AC P46782; B2R4T2; Q96BN0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 137.
DE RecName: Full=40S ribosomal protein S5;
DE Contains:
DE RecName: Full=40S ribosomal protein S5, N-terminally processed;
GN Name=RPS5;
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].
RC TISSUE=Colon;
RX PubMed=7772601; DOI=10.1016/0167-4781(95)00045-I;
RA Frigerio J.-M., Dagorn J.-C., Iovanna J.L.;
RT "Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9,
RT S10 and S29 human ribosomal protein mRNAs.";
RL Biochim. Biophys. Acta 1262:64-68(1995).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone, and Ovary;
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 [6]
RP PROTEIN SEQUENCE OF 2-18; 23-42; 48-55; 137-145 AND 168-182, CLEAVAGE
RP OF INITIATOR METHIONINE, ACETYLATION AT THR-2, AND MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 1-18; 23-42; 137-159 AND 168-182, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT MET-1 AND THR-2, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 150-204.
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 [9]
RP PROTEIN SEQUENCE OF 192-197.
RC TISSUE=Placenta;
RX PubMed=8706699; DOI=10.1111/j.1432-1033.1996.0144u.x;
RA Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K.,
RA Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.;
RT "Characterization of the human small-ribosomal-subunit proteins by N-
RT terminal and internal sequencing, and mass spectrometry.";
RL Eur. J. Biochem. 239:144-149(1996).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, AND MASS
RP 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-47, 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 [12]
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 [13]
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 -!- SIMILARITY: Belongs to the ribosomal protein S7P family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U14970; AAA85658.1; -; mRNA.
DR EMBL; AB061853; BAB79493.1; -; Genomic_DNA.
DR EMBL; AK311938; BAG34879.1; -; mRNA.
DR EMBL; CH471135; EAW72581.1; -; Genomic_DNA.
DR EMBL; BC015405; AAH15405.1; -; mRNA.
DR EMBL; BC018151; AAH18151.1; -; mRNA.
DR EMBL; AB007149; BAA25815.1; -; Genomic_DNA.
DR PIR; S55916; S55916.
DR RefSeq; NP_001000.2; NM_001009.3.
DR UniGene; Hs.378103; -.
DR PDB; 3J3A; EM; 5.00 A; F=1-204.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; P46782; -.
DR SMR; P46782; 14-204.
DR IntAct; P46782; 14.
DR MINT; MINT-1142463; -.
DR STRING; 9606.ENSP00000196551; -.
DR PhosphoSite; P46782; -.
DR DMDM; 22002064; -.
DR SWISS-2DPAGE; P46782; -.
DR PaxDb; P46782; -.
DR PeptideAtlas; P46782; -.
DR PRIDE; P46782; -.
DR DNASU; 6193; -.
DR Ensembl; ENST00000196551; ENSP00000196551; ENSG00000083845.
DR Ensembl; ENST00000596046; ENSP00000472985; ENSG00000083845.
DR Ensembl; ENST00000601521; ENSP00000470114; ENSG00000083845.
DR GeneID; 6193; -.
DR KEGG; hsa:6193; -.
DR UCSC; uc002qsn.3; human.
DR CTD; 6193; -.
DR GeneCards; GC19P059246; -.
DR H-InvDB; HIX0020415; -.
DR HGNC; HGNC:10426; RPS5.
DR HPA; HPA055878; -.
DR MIM; 603630; gene.
DR neXtProt; NX_P46782; -.
DR PharmGKB; PA34841; -.
DR eggNOG; COG0049; -.
DR HOGENOM; HOG000039066; -.
DR HOVERGEN; HBG028547; -.
DR InParanoid; P46782; -.
DR KO; K02989; -.
DR OrthoDB; EOG7PZRZS; -.
DR PhylomeDB; P46782; -.
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; RPS5; human.
DR GeneWiki; RPS5; -.
DR GenomeRNAi; 6193; -.
DR NextBio; 24049; -.
DR PRO; PR:P46782; -.
DR ArrayExpress; P46782; -.
DR Bgee; P46782; -.
DR CleanEx; HS_RPS5; -.
DR Genevestigator; P46782; -.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0006450; P:regulation of translational fidelity; IGI: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; IC:UniProtKB.
DR GO; GO:0006415; P:translational termination; TAS:Reactome.
DR GO; GO:0019083; P:viral transcription; TAS:Reactome.
DR Gene3D; 1.10.455.10; -; 1.
DR InterPro; IPR000235; Ribosomal_S5/S7.
DR InterPro; IPR005716; Ribosomal_S5/S7_euk/arc.
DR InterPro; IPR020606; Ribosomal_S7_CS.
DR InterPro; IPR023798; Ribosomal_S7_dom.
DR PANTHER; PTHR11205; PTHR11205; 1.
DR Pfam; PF00177; Ribosomal_S7; 1.
DR PIRSF; PIRSF002122; RPS7p_RPS7a_RPS5e_RPS7o; 1.
DR SUPFAM; SSF47973; SSF47973; 1.
DR TIGRFAMs; TIGR01028; S7_S5_E_A; 1.
DR PROSITE; PS00052; RIBOSOMAL_S7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT CHAIN 1 204 40S ribosomal protein S5.
FT /FTId=PRO_0000370369.
FT INIT_MET 1 1 Removed; alternate.
FT CHAIN 2 204 40S ribosomal protein S5, N-terminally
FT processed.
FT /FTId=PRO_0000124526.
FT MOD_RES 1 1 N-acetylmethionine; in 40S ribosomal
FT protein S5; alternate.
FT MOD_RES 2 2 N-acetylthreonine; in 40S ribosomal
FT protein S5, N-terminally processed.
FT MOD_RES 47 47 N6-acetyllysine.
FT CONFLICT 59 60 KR -> NA (in Ref. 1; AAA85658).
SQ SEQUENCE 204 AA; 22876 MW; DFE2FD5AAFCFD894 CRC64;
MTEWETAAPA VAETPDIKLF GKWSTDDVQI NDISLQDYIA VKEKYAKYLP HSAGRYAAKR
FRKAQCPIVE RLTNSMMMHG RNNGKKLMTV RIVKHAFEII HLLTGENPLQ VLVNAIINSG
PREDSTRIGR AGTVRRQAVD VSPLRRVNQA IWLLCTGARE AAFRNIKTIA ECLADELINA
AKGSSNSYAI KKKDELERVA KSNR
//
ID RS5_HUMAN Reviewed; 204 AA.
AC P46782; B2R4T2; Q96BN0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 137.
DE RecName: Full=40S ribosomal protein S5;
DE Contains:
DE RecName: Full=40S ribosomal protein S5, N-terminally processed;
GN Name=RPS5;
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].
RC TISSUE=Colon;
RX PubMed=7772601; DOI=10.1016/0167-4781(95)00045-I;
RA Frigerio J.-M., Dagorn J.-C., Iovanna J.L.;
RT "Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9,
RT S10 and S29 human ribosomal protein mRNAs.";
RL Biochim. Biophys. Acta 1262:64-68(1995).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone, and Ovary;
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 [6]
RP PROTEIN SEQUENCE OF 2-18; 23-42; 48-55; 137-145 AND 168-182, CLEAVAGE
RP OF INITIATOR METHIONINE, ACETYLATION AT THR-2, AND MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 1-18; 23-42; 137-159 AND 168-182, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT MET-1 AND THR-2, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 150-204.
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 [9]
RP PROTEIN SEQUENCE OF 192-197.
RC TISSUE=Placenta;
RX PubMed=8706699; DOI=10.1111/j.1432-1033.1996.0144u.x;
RA Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K.,
RA Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.;
RT "Characterization of the human small-ribosomal-subunit proteins by N-
RT terminal and internal sequencing, and mass spectrometry.";
RL Eur. J. Biochem. 239:144-149(1996).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, AND MASS
RP 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-47, 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 [12]
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 [13]
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 -!- SIMILARITY: Belongs to the ribosomal protein S7P family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U14970; AAA85658.1; -; mRNA.
DR EMBL; AB061853; BAB79493.1; -; Genomic_DNA.
DR EMBL; AK311938; BAG34879.1; -; mRNA.
DR EMBL; CH471135; EAW72581.1; -; Genomic_DNA.
DR EMBL; BC015405; AAH15405.1; -; mRNA.
DR EMBL; BC018151; AAH18151.1; -; mRNA.
DR EMBL; AB007149; BAA25815.1; -; Genomic_DNA.
DR PIR; S55916; S55916.
DR RefSeq; NP_001000.2; NM_001009.3.
DR UniGene; Hs.378103; -.
DR PDB; 3J3A; EM; 5.00 A; F=1-204.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; P46782; -.
DR SMR; P46782; 14-204.
DR IntAct; P46782; 14.
DR MINT; MINT-1142463; -.
DR STRING; 9606.ENSP00000196551; -.
DR PhosphoSite; P46782; -.
DR DMDM; 22002064; -.
DR SWISS-2DPAGE; P46782; -.
DR PaxDb; P46782; -.
DR PeptideAtlas; P46782; -.
DR PRIDE; P46782; -.
DR DNASU; 6193; -.
DR Ensembl; ENST00000196551; ENSP00000196551; ENSG00000083845.
DR Ensembl; ENST00000596046; ENSP00000472985; ENSG00000083845.
DR Ensembl; ENST00000601521; ENSP00000470114; ENSG00000083845.
DR GeneID; 6193; -.
DR KEGG; hsa:6193; -.
DR UCSC; uc002qsn.3; human.
DR CTD; 6193; -.
DR GeneCards; GC19P059246; -.
DR H-InvDB; HIX0020415; -.
DR HGNC; HGNC:10426; RPS5.
DR HPA; HPA055878; -.
DR MIM; 603630; gene.
DR neXtProt; NX_P46782; -.
DR PharmGKB; PA34841; -.
DR eggNOG; COG0049; -.
DR HOGENOM; HOG000039066; -.
DR HOVERGEN; HBG028547; -.
DR InParanoid; P46782; -.
DR KO; K02989; -.
DR OrthoDB; EOG7PZRZS; -.
DR PhylomeDB; P46782; -.
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; RPS5; human.
DR GeneWiki; RPS5; -.
DR GenomeRNAi; 6193; -.
DR NextBio; 24049; -.
DR PRO; PR:P46782; -.
DR ArrayExpress; P46782; -.
DR Bgee; P46782; -.
DR CleanEx; HS_RPS5; -.
DR Genevestigator; P46782; -.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0006450; P:regulation of translational fidelity; IGI: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; IC:UniProtKB.
DR GO; GO:0006415; P:translational termination; TAS:Reactome.
DR GO; GO:0019083; P:viral transcription; TAS:Reactome.
DR Gene3D; 1.10.455.10; -; 1.
DR InterPro; IPR000235; Ribosomal_S5/S7.
DR InterPro; IPR005716; Ribosomal_S5/S7_euk/arc.
DR InterPro; IPR020606; Ribosomal_S7_CS.
DR InterPro; IPR023798; Ribosomal_S7_dom.
DR PANTHER; PTHR11205; PTHR11205; 1.
DR Pfam; PF00177; Ribosomal_S7; 1.
DR PIRSF; PIRSF002122; RPS7p_RPS7a_RPS5e_RPS7o; 1.
DR SUPFAM; SSF47973; SSF47973; 1.
DR TIGRFAMs; TIGR01028; S7_S5_E_A; 1.
DR PROSITE; PS00052; RIBOSOMAL_S7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT CHAIN 1 204 40S ribosomal protein S5.
FT /FTId=PRO_0000370369.
FT INIT_MET 1 1 Removed; alternate.
FT CHAIN 2 204 40S ribosomal protein S5, N-terminally
FT processed.
FT /FTId=PRO_0000124526.
FT MOD_RES 1 1 N-acetylmethionine; in 40S ribosomal
FT protein S5; alternate.
FT MOD_RES 2 2 N-acetylthreonine; in 40S ribosomal
FT protein S5, N-terminally processed.
FT MOD_RES 47 47 N6-acetyllysine.
FT CONFLICT 59 60 KR -> NA (in Ref. 1; AAA85658).
SQ SEQUENCE 204 AA; 22876 MW; DFE2FD5AAFCFD894 CRC64;
MTEWETAAPA VAETPDIKLF GKWSTDDVQI NDISLQDYIA VKEKYAKYLP HSAGRYAAKR
FRKAQCPIVE RLTNSMMMHG RNNGKKLMTV RIVKHAFEII HLLTGENPLQ VLVNAIINSG
PREDSTRIGR AGTVRRQAVD VSPLRRVNQA IWLLCTGARE AAFRNIKTIA ECLADELINA
AKGSSNSYAI KKKDELERVA KSNR
//
MIM
603630
*RECORD*
*FIELD* NO
603630
*FIELD* TI
*603630 RIBOSOMAL PROTEIN S5; RPS5
*FIELD* TX
The mammalian ribosome is a macromolecular assembly of 4 RNA species
read more(see 180450) and approximately 80 different proteins.
By searching sequence databases with the partial sequences of randomly
selected cDNAs from a human colorectal cDNA library, Frigerio et al.
(1995) identified cDNAs encoding homologs of rat ribosomal proteins S5
(RPS5), S9 (RPS9; 603631), S10 (RPS10; 603632), S29 (RPS29; 603633), L5
(RPL5; 603634), L21 (RPL21; 603636), L27a (RPL27A; 603637), and L28
(RPL28; 603638). Frigerio et al. (1995) completed the cDNA sequences of
these human ribosomal proteins. The deduced 204-amino acid human RPS5
differs from rat Rps5 by 3 amino acids. Northern blot analysis suggested
variable expression of RPS5 in colorectal cancers compared to adjacent
normal tissues, although no correlation between the level of expression
and the severity of the disease was found.
By somatic cell hybrid and radiation hybrid mapping analyses, Kenmochi
et al. (1998) mapped the human RPS5 gene to 19q13.4 (GenBank GENBANK
AB007149).
*FIELD* RF
1. Frigerio, J.-M.; Berthezene, P.; Garrido, P.; Ortiz, E.; Barthellemy,
S.; Vasseur, S.; Sastre, B.; Seleznieff, I.; Dagorn, J. C.; Iovanna,
J. L.: Analysis of 2166 clones from a human colorectal cancer cDNA
library by partial sequencing. Hum. Molec. Genet. 4: 37-43, 1995.
2. Frigerio, J.-M.; Dagorn, J.-C.; Iovanna, J. L.: Cloning, sequencing
and expression of the L5, L21, L27a, L28, S5, S9, S10 and S29 human
ribosomal protein mRNAs. Biochim. Biophys. Acta 1262: 64-68, 1995.
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.
*FIELD* CD
Patti M. Sherman: 3/12/1999
*FIELD* ED
psherman: 03/22/1999
carol: 3/19/1999
psherman: 3/16/1999
*RECORD*
*FIELD* NO
603630
*FIELD* TI
*603630 RIBOSOMAL PROTEIN S5; RPS5
*FIELD* TX
The mammalian ribosome is a macromolecular assembly of 4 RNA species
read more(see 180450) and approximately 80 different proteins.
By searching sequence databases with the partial sequences of randomly
selected cDNAs from a human colorectal cDNA library, Frigerio et al.
(1995) identified cDNAs encoding homologs of rat ribosomal proteins S5
(RPS5), S9 (RPS9; 603631), S10 (RPS10; 603632), S29 (RPS29; 603633), L5
(RPL5; 603634), L21 (RPL21; 603636), L27a (RPL27A; 603637), and L28
(RPL28; 603638). Frigerio et al. (1995) completed the cDNA sequences of
these human ribosomal proteins. The deduced 204-amino acid human RPS5
differs from rat Rps5 by 3 amino acids. Northern blot analysis suggested
variable expression of RPS5 in colorectal cancers compared to adjacent
normal tissues, although no correlation between the level of expression
and the severity of the disease was found.
By somatic cell hybrid and radiation hybrid mapping analyses, Kenmochi
et al. (1998) mapped the human RPS5 gene to 19q13.4 (GenBank GENBANK
AB007149).
*FIELD* RF
1. Frigerio, J.-M.; Berthezene, P.; Garrido, P.; Ortiz, E.; Barthellemy,
S.; Vasseur, S.; Sastre, B.; Seleznieff, I.; Dagorn, J. C.; Iovanna,
J. L.: Analysis of 2166 clones from a human colorectal cancer cDNA
library by partial sequencing. Hum. Molec. Genet. 4: 37-43, 1995.
2. Frigerio, J.-M.; Dagorn, J.-C.; Iovanna, J. L.: Cloning, sequencing
and expression of the L5, L21, L27a, L28, S5, S9, S10 and S29 human
ribosomal protein mRNAs. Biochim. Biophys. Acta 1262: 64-68, 1995.
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.
*FIELD* CD
Patti M. Sherman: 3/12/1999
*FIELD* ED
psherman: 03/22/1999
carol: 3/19/1999
psherman: 3/16/1999