Full text data of RPS11
RPS11
[Confidence: low (only semi-automatic identification from reviews)]
40S ribosomal protein S11
Note: presumably soluble (membrane word is not in UniProt keywords or features)
40S ribosomal protein S11
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P62280
ID RS11_HUMAN Reviewed; 158 AA.
AC P62280; B2R4F5; P04643; Q498Y6; Q6IRY0;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 111.
DE RecName: Full=40S ribosomal protein S11;
GN Name=RPS11;
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].
RX PubMed=3267208; DOI=10.1093/nar/16.3.1205;
RA Lott J.B., Mackie G.A.;
RT "Sequence of a cloned cDNA encoding human ribosomal protein S11.";
RL Nucleic Acids Res. 16:1205-1205(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10580157; DOI=10.1016/S0378-1119(99)00429-1;
RA Higa S., Yoshihama M., Tanaka T., Kenmochi N.;
RT "Gene organization and sequence of the region containing the ribosomal
RT protein genes RPL13A and RPS11 in the human genome and conserved
RT features in the mouse genome.";
RL Gene 240:371-377(1999).
RN [3]
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 [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=B-cell, Eye, Lung, and Prostate;
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 2-11, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=T-cell;
RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
RL Submitted (MAY-2006) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 39-45 AND 137-143.
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-158.
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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-38 AND LYS-45, AND MASS
RP 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 [11]
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 [12]
RP MUTAGENESIS OF CYS-60, AND PALMITOYLATION AT CYS-60.
RX PubMed=21044946; DOI=10.1194/jlr.D011106;
RA Forrester M.T., Hess D.T., Thompson J.W., Hultman R., Moseley M.A.,
RA Stamler J.S., Casey P.J.;
RT "Site-specific analysis of protein S-acylation by resin-assisted
RT capture.";
RL J. Lipid Res. 52:393-398(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, 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 [14]
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 -!- INTERACTION:
CC Q9NY93:DDX56; NbExp=1; IntAct=EBI-1047710, EBI-372376;
CC O60739:EIF1B; NbExp=1; IntAct=EBI-1047710, EBI-1043343;
CC O15479:MAGEB2; NbExp=1; IntAct=EBI-1047710, EBI-1057615;
CC Q99608:NDN; NbExp=1; IntAct=EBI-1047710, EBI-718177;
CC Q9Y230:RUVBL2; NbExp=1; IntAct=EBI-1047710, EBI-352939;
CC -!- SIMILARITY: Belongs to the ribosomal protein S17P 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; X06617; CAA29834.1; -; mRNA.
DR EMBL; AB028893; BAA88215.1; -; Genomic_DNA.
DR EMBL; AK311809; BAG34752.1; -; mRNA.
DR EMBL; CH471177; EAW52497.1; -; Genomic_DNA.
DR EMBL; BC007283; AAH07283.1; -; mRNA.
DR EMBL; BC007603; AAH07603.1; -; mRNA.
DR EMBL; BC007945; AAH07945.1; -; mRNA.
DR EMBL; BC010028; AAH10028.1; -; mRNA.
DR EMBL; BC016378; AAH16378.1; -; mRNA.
DR EMBL; BC070224; AAH70224.1; -; mRNA.
DR EMBL; BC100025; AAI00026.1; -; mRNA.
DR EMBL; AB007152; BAA25818.1; -; Genomic_DNA.
DR PIR; S02133; R3HU11.
DR RefSeq; NP_001006.1; NM_001015.4.
DR UniGene; Hs.433529; -.
DR PDB; 3J3A; EM; 5.00 A; L=1-158.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; P62280; -.
DR SMR; P62280; 1-158.
DR IntAct; P62280; 31.
DR MINT; MINT-1154341; -.
DR STRING; 9606.ENSP00000270625; -.
DR PhosphoSite; P62280; -.
DR DMDM; 50403609; -.
DR SWISS-2DPAGE; P62280; -.
DR PaxDb; P62280; -.
DR PeptideAtlas; P62280; -.
DR PRIDE; P62280; -.
DR DNASU; 6205; -.
DR Ensembl; ENST00000270625; ENSP00000270625; ENSG00000142534.
DR GeneID; 6205; -.
DR KEGG; hsa:6205; -.
DR UCSC; uc002pob.2; human.
DR CTD; 6205; -.
DR GeneCards; GC19P049999; -.
DR H-InvDB; HIX0037158; -.
DR HGNC; HGNC:10384; RPS11.
DR HPA; HPA049719; -.
DR MIM; 180471; gene.
DR neXtProt; NX_P62280; -.
DR PharmGKB; PA34782; -.
DR eggNOG; COG0186; -.
DR HOGENOM; HOG000231341; -.
DR HOVERGEN; HBG004670; -.
DR InParanoid; P62280; -.
DR KO; K02949; -.
DR OMA; GAKKQFQ; -.
DR OrthoDB; EOG78H3VQ; -.
DR PhylomeDB; P62280; -.
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; RPS11; human.
DR GeneWiki; RPS11; -.
DR GenomeRNAi; 6205; -.
DR NextBio; 24099; -.
DR PMAP-CutDB; P62280; -.
DR PRO; PR:P62280; -.
DR ArrayExpress; P62280; -.
DR Bgee; P62280; -.
DR CleanEx; HS_RPS11; -.
DR Genevestigator; P62280; -.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
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; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR000266; Ribosomal_S17.
DR InterPro; IPR028333; Ribosomal_S17_arc-typ.
DR InterPro; IPR019979; Ribosomal_S17_CS.
DR PANTHER; PTHR10744; PTHR10744; 1.
DR Pfam; PF00366; Ribosomal_S17; 1.
DR PRINTS; PR00973; RIBOSOMALS17.
DR ProDom; PD001295; Ribosomal_S17; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR03630; arch_S17P; 1.
DR PROSITE; PS00056; RIBOSOMAL_S17; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; Lipoprotein; Palmitate; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 158 40S ribosomal protein S11.
FT /FTId=PRO_0000128509.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 38 38 N6-acetyllysine.
FT MOD_RES 45 45 N6-acetyllysine.
FT LIPID 60 60 S-palmitoyl cysteine (Probable).
FT MUTAGEN 60 60 C->S: Abolishes S-acylation.
SQ SEQUENCE 158 AA; 18431 MW; 9FB75DC1D99614B0 CRC64;
MADIQTERAY QKQPTIFQNK KRVLLGETGK EKLPRYYKNI GLGFKTPKEA IEGTYIDKKC
PFTGNVSIRG RILSGVVTKM KMQRTIVIRR DYLHYIRKYN RFEKRHKNMS VHLSPCFRDV
QIGDIVTVGE CRPLSKTVRF NVLKVTKAAG TKKQFQKF
//
ID RS11_HUMAN Reviewed; 158 AA.
AC P62280; B2R4F5; P04643; Q498Y6; Q6IRY0;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 111.
DE RecName: Full=40S ribosomal protein S11;
GN Name=RPS11;
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].
RX PubMed=3267208; DOI=10.1093/nar/16.3.1205;
RA Lott J.B., Mackie G.A.;
RT "Sequence of a cloned cDNA encoding human ribosomal protein S11.";
RL Nucleic Acids Res. 16:1205-1205(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10580157; DOI=10.1016/S0378-1119(99)00429-1;
RA Higa S., Yoshihama M., Tanaka T., Kenmochi N.;
RT "Gene organization and sequence of the region containing the ribosomal
RT protein genes RPL13A and RPS11 in the human genome and conserved
RT features in the mouse genome.";
RL Gene 240:371-377(1999).
RN [3]
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 [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=B-cell, Eye, Lung, and Prostate;
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 2-11, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=T-cell;
RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
RL Submitted (MAY-2006) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 39-45 AND 137-143.
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-158.
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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-38 AND LYS-45, AND MASS
RP 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 [11]
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 [12]
RP MUTAGENESIS OF CYS-60, AND PALMITOYLATION AT CYS-60.
RX PubMed=21044946; DOI=10.1194/jlr.D011106;
RA Forrester M.T., Hess D.T., Thompson J.W., Hultman R., Moseley M.A.,
RA Stamler J.S., Casey P.J.;
RT "Site-specific analysis of protein S-acylation by resin-assisted
RT capture.";
RL J. Lipid Res. 52:393-398(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, 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 [14]
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 -!- INTERACTION:
CC Q9NY93:DDX56; NbExp=1; IntAct=EBI-1047710, EBI-372376;
CC O60739:EIF1B; NbExp=1; IntAct=EBI-1047710, EBI-1043343;
CC O15479:MAGEB2; NbExp=1; IntAct=EBI-1047710, EBI-1057615;
CC Q99608:NDN; NbExp=1; IntAct=EBI-1047710, EBI-718177;
CC Q9Y230:RUVBL2; NbExp=1; IntAct=EBI-1047710, EBI-352939;
CC -!- SIMILARITY: Belongs to the ribosomal protein S17P 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; X06617; CAA29834.1; -; mRNA.
DR EMBL; AB028893; BAA88215.1; -; Genomic_DNA.
DR EMBL; AK311809; BAG34752.1; -; mRNA.
DR EMBL; CH471177; EAW52497.1; -; Genomic_DNA.
DR EMBL; BC007283; AAH07283.1; -; mRNA.
DR EMBL; BC007603; AAH07603.1; -; mRNA.
DR EMBL; BC007945; AAH07945.1; -; mRNA.
DR EMBL; BC010028; AAH10028.1; -; mRNA.
DR EMBL; BC016378; AAH16378.1; -; mRNA.
DR EMBL; BC070224; AAH70224.1; -; mRNA.
DR EMBL; BC100025; AAI00026.1; -; mRNA.
DR EMBL; AB007152; BAA25818.1; -; Genomic_DNA.
DR PIR; S02133; R3HU11.
DR RefSeq; NP_001006.1; NM_001015.4.
DR UniGene; Hs.433529; -.
DR PDB; 3J3A; EM; 5.00 A; L=1-158.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; P62280; -.
DR SMR; P62280; 1-158.
DR IntAct; P62280; 31.
DR MINT; MINT-1154341; -.
DR STRING; 9606.ENSP00000270625; -.
DR PhosphoSite; P62280; -.
DR DMDM; 50403609; -.
DR SWISS-2DPAGE; P62280; -.
DR PaxDb; P62280; -.
DR PeptideAtlas; P62280; -.
DR PRIDE; P62280; -.
DR DNASU; 6205; -.
DR Ensembl; ENST00000270625; ENSP00000270625; ENSG00000142534.
DR GeneID; 6205; -.
DR KEGG; hsa:6205; -.
DR UCSC; uc002pob.2; human.
DR CTD; 6205; -.
DR GeneCards; GC19P049999; -.
DR H-InvDB; HIX0037158; -.
DR HGNC; HGNC:10384; RPS11.
DR HPA; HPA049719; -.
DR MIM; 180471; gene.
DR neXtProt; NX_P62280; -.
DR PharmGKB; PA34782; -.
DR eggNOG; COG0186; -.
DR HOGENOM; HOG000231341; -.
DR HOVERGEN; HBG004670; -.
DR InParanoid; P62280; -.
DR KO; K02949; -.
DR OMA; GAKKQFQ; -.
DR OrthoDB; EOG78H3VQ; -.
DR PhylomeDB; P62280; -.
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; RPS11; human.
DR GeneWiki; RPS11; -.
DR GenomeRNAi; 6205; -.
DR NextBio; 24099; -.
DR PMAP-CutDB; P62280; -.
DR PRO; PR:P62280; -.
DR ArrayExpress; P62280; -.
DR Bgee; P62280; -.
DR CleanEx; HS_RPS11; -.
DR Genevestigator; P62280; -.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
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; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR000266; Ribosomal_S17.
DR InterPro; IPR028333; Ribosomal_S17_arc-typ.
DR InterPro; IPR019979; Ribosomal_S17_CS.
DR PANTHER; PTHR10744; PTHR10744; 1.
DR Pfam; PF00366; Ribosomal_S17; 1.
DR PRINTS; PR00973; RIBOSOMALS17.
DR ProDom; PD001295; Ribosomal_S17; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR03630; arch_S17P; 1.
DR PROSITE; PS00056; RIBOSOMAL_S17; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; Lipoprotein; Palmitate; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 158 40S ribosomal protein S11.
FT /FTId=PRO_0000128509.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 38 38 N6-acetyllysine.
FT MOD_RES 45 45 N6-acetyllysine.
FT LIPID 60 60 S-palmitoyl cysteine (Probable).
FT MUTAGEN 60 60 C->S: Abolishes S-acylation.
SQ SEQUENCE 158 AA; 18431 MW; 9FB75DC1D99614B0 CRC64;
MADIQTERAY QKQPTIFQNK KRVLLGETGK EKLPRYYKNI GLGFKTPKEA IEGTYIDKKC
PFTGNVSIRG RILSGVVTKM KMQRTIVIRR DYLHYIRKYN RFEKRHKNMS VHLSPCFRDV
QIGDIVTVGE CRPLSKTVRF NVLKVTKAAG TKKQFQKF
//
MIM
180471
*RECORD*
*FIELD* NO
180471
*FIELD* TI
*180471 RIBOSOMAL PROTEIN S11; RPS11
*FIELD* TX
See 180466 for general information about ribosomal proteins.
read more
By screening a human fibroblast cDNA library with a rat ribosomal
protein S11 (Rps11) cDNA, Lott and Mackie (1988) isolated a cDNA
encoding human RPS11. The deduced 158-amino acid human RPS11 protein is
identical to the rat Rps11 protein.
Using a PCR product for the analysis of rodent/human somatic cell
hybrids, Feo et al. (1992) mapped the RPS11 gene to 19cen-qter. By
somatic cell hybrid and radiation hybrid mapping analyses, Kenmochi et
al. (1998) mapped the RPS11 gene to 19q13.3 (GenBank GENBANK AB007152).
*FIELD* RF
1. Feo, S.; Davies, B.; Fried, M.: The mapping of seven intron-containing
ribosomal protein genes shows they are unlinked in the human genome. Genomics 13:
201-207, 1992.
2. 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.
3. Lott, J. B.; Mackie, G. A.: Sequence of a cloned cDNA encoding
human ribosomal protein S11. Nucleic Acids Res. 16: 1205 only, 1988.
*FIELD* CN
Patti M. Sherman - updated: 4/5/1999
*FIELD* CD
Victor A. McKusick: 6/6/1992
*FIELD* ED
carol: 04/16/1999
carol: 6/6/1992
*RECORD*
*FIELD* NO
180471
*FIELD* TI
*180471 RIBOSOMAL PROTEIN S11; RPS11
*FIELD* TX
See 180466 for general information about ribosomal proteins.
read more
By screening a human fibroblast cDNA library with a rat ribosomal
protein S11 (Rps11) cDNA, Lott and Mackie (1988) isolated a cDNA
encoding human RPS11. The deduced 158-amino acid human RPS11 protein is
identical to the rat Rps11 protein.
Using a PCR product for the analysis of rodent/human somatic cell
hybrids, Feo et al. (1992) mapped the RPS11 gene to 19cen-qter. By
somatic cell hybrid and radiation hybrid mapping analyses, Kenmochi et
al. (1998) mapped the RPS11 gene to 19q13.3 (GenBank GENBANK AB007152).
*FIELD* RF
1. Feo, S.; Davies, B.; Fried, M.: The mapping of seven intron-containing
ribosomal protein genes shows they are unlinked in the human genome. Genomics 13:
201-207, 1992.
2. 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.
3. Lott, J. B.; Mackie, G. A.: Sequence of a cloned cDNA encoding
human ribosomal protein S11. Nucleic Acids Res. 16: 1205 only, 1988.
*FIELD* CN
Patti M. Sherman - updated: 4/5/1999
*FIELD* CD
Victor A. McKusick: 6/6/1992
*FIELD* ED
carol: 04/16/1999
carol: 6/6/1992