Full text data of RPS16
RPS16
[Confidence: low (only semi-automatic identification from reviews)]
40S ribosomal protein S16
Note: presumably soluble (membrane word is not in UniProt keywords or features)
40S ribosomal protein S16
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P62249
ID RS16_HUMAN Reviewed; 146 AA.
AC P62249; B2RDD5; P17008;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 93.
DE RecName: Full=40S ribosomal protein S16;
GN Name=RPS16;
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=2016298;
RA Batra S.K., Metzgar R.S., Hollingsworth M.A.;
RT "Molecular cloning and sequence analysis of the human ribosomal
RT protein S16.";
RL J. Biol. Chem. 266:6830-6833(1991).
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=Brain, and Kidney;
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.
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 [7]
RP PROTEIN SEQUENCE OF 2-15 AND 51-62, CLEAVAGE OF INITIATOR METHIONINE,
RP LACK OF N-TERMINAL ACETYLATION, AND MASS SPECTROMETRY.
RC TISSUE=Mammary carcinoma;
RA Bienvenut W.V., Lourenco F., Olson M.F.;
RL Submitted (DEC-2009) to UniProtKB.
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60, 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 [9]
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 [10]
RP IDENTIFICATION BY MASS 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.,
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 [11]
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 S9P 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; M60854; AAA60583.1; -; mRNA.
DR EMBL; AB061841; BAB79479.1; -; Genomic_DNA.
DR EMBL; AK315498; BAG37882.1; -; mRNA.
DR EMBL; CH471126; EAW56894.1; -; Genomic_DNA.
DR EMBL; BC004324; AAH04324.1; -; mRNA.
DR EMBL; BC007977; AAH07977.1; -; mRNA.
DR PIR; A39760; R3HU16.
DR RefSeq; NP_001011.1; NM_001020.4.
DR UniGene; Hs.397609; -.
DR PDB; 3J3A; EM; 5.00 A; Q=1-146.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; P62249; -.
DR SMR; P62249; 6-146.
DR IntAct; P62249; 23.
DR MINT; MINT-5001167; -.
DR STRING; 9606.ENSP00000251453; -.
DR PhosphoSite; P62249; -.
DR DMDM; 50403607; -.
DR PaxDb; P62249; -.
DR PeptideAtlas; P62249; -.
DR PRIDE; P62249; -.
DR DNASU; 6217; -.
DR Ensembl; ENST00000251453; ENSP00000251453; ENSG00000105193.
DR GeneID; 6217; -.
DR KEGG; hsa:6217; -.
DR UCSC; uc002olk.3; human.
DR CTD; 6217; -.
DR GeneCards; GC19M039923; -.
DR H-InvDB; HIX0212796; -.
DR HGNC; HGNC:10396; RPS16.
DR MIM; 603675; gene.
DR neXtProt; NX_P62249; -.
DR PharmGKB; PA34796; -.
DR eggNOG; COG0103; -.
DR HOGENOM; HOG000019803; -.
DR HOVERGEN; HBG055171; -.
DR KO; K02960; -.
DR OMA; NRRCEPK; -.
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; RPS16; human.
DR GeneWiki; RPS16; -.
DR GenomeRNAi; 6217; -.
DR NextBio; 24141; -.
DR PRO; PR:P62249; -.
DR ArrayExpress; P62249; -.
DR Bgee; P62249; -.
DR CleanEx; HS_RPS16; -.
DR Genevestigator; P62249; -.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
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:0042274; P:ribosomal small 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; 3.30.230.10; -; 1.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR000754; Ribosomal_S9.
DR InterPro; IPR020574; Ribosomal_S9_CS.
DR PANTHER; PTHR21569; PTHR21569; 1.
DR Pfam; PF00380; Ribosomal_S9; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR PROSITE; PS00360; RIBOSOMAL_S9; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 146 40S ribosomal protein S16.
FT /FTId=PRO_0000111479.
FT SITE 2 2 Not acetylated.
FT MOD_RES 60 60 N6-acetyllysine.
SQ SEQUENCE 146 AA; 16445 MW; 519BCFB91BB68A15 CRC64;
MPSKGPLQSV QVFGRKKTAT AVAHCKRGNG LIKVNGRPLE MIEPRTLQYK LLEPVLLLGK
ERFAGVDIRV RVKGGGHVAQ IYAIRQSISK ALVAYYQKYV DEASKKEIKD ILIQYDRTLL
VADPRRCESK KFGGPGARAR YQKSYR
//
ID RS16_HUMAN Reviewed; 146 AA.
AC P62249; B2RDD5; P17008;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 93.
DE RecName: Full=40S ribosomal protein S16;
GN Name=RPS16;
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=2016298;
RA Batra S.K., Metzgar R.S., Hollingsworth M.A.;
RT "Molecular cloning and sequence analysis of the human ribosomal
RT protein S16.";
RL J. Biol. Chem. 266:6830-6833(1991).
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=Brain, and Kidney;
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.
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 [7]
RP PROTEIN SEQUENCE OF 2-15 AND 51-62, CLEAVAGE OF INITIATOR METHIONINE,
RP LACK OF N-TERMINAL ACETYLATION, AND MASS SPECTROMETRY.
RC TISSUE=Mammary carcinoma;
RA Bienvenut W.V., Lourenco F., Olson M.F.;
RL Submitted (DEC-2009) to UniProtKB.
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60, 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 [9]
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 [10]
RP IDENTIFICATION BY MASS 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.,
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 [11]
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 S9P 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; M60854; AAA60583.1; -; mRNA.
DR EMBL; AB061841; BAB79479.1; -; Genomic_DNA.
DR EMBL; AK315498; BAG37882.1; -; mRNA.
DR EMBL; CH471126; EAW56894.1; -; Genomic_DNA.
DR EMBL; BC004324; AAH04324.1; -; mRNA.
DR EMBL; BC007977; AAH07977.1; -; mRNA.
DR PIR; A39760; R3HU16.
DR RefSeq; NP_001011.1; NM_001020.4.
DR UniGene; Hs.397609; -.
DR PDB; 3J3A; EM; 5.00 A; Q=1-146.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; P62249; -.
DR SMR; P62249; 6-146.
DR IntAct; P62249; 23.
DR MINT; MINT-5001167; -.
DR STRING; 9606.ENSP00000251453; -.
DR PhosphoSite; P62249; -.
DR DMDM; 50403607; -.
DR PaxDb; P62249; -.
DR PeptideAtlas; P62249; -.
DR PRIDE; P62249; -.
DR DNASU; 6217; -.
DR Ensembl; ENST00000251453; ENSP00000251453; ENSG00000105193.
DR GeneID; 6217; -.
DR KEGG; hsa:6217; -.
DR UCSC; uc002olk.3; human.
DR CTD; 6217; -.
DR GeneCards; GC19M039923; -.
DR H-InvDB; HIX0212796; -.
DR HGNC; HGNC:10396; RPS16.
DR MIM; 603675; gene.
DR neXtProt; NX_P62249; -.
DR PharmGKB; PA34796; -.
DR eggNOG; COG0103; -.
DR HOGENOM; HOG000019803; -.
DR HOVERGEN; HBG055171; -.
DR KO; K02960; -.
DR OMA; NRRCEPK; -.
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; RPS16; human.
DR GeneWiki; RPS16; -.
DR GenomeRNAi; 6217; -.
DR NextBio; 24141; -.
DR PRO; PR:P62249; -.
DR ArrayExpress; P62249; -.
DR Bgee; P62249; -.
DR CleanEx; HS_RPS16; -.
DR Genevestigator; P62249; -.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
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:0042274; P:ribosomal small 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; 3.30.230.10; -; 1.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR000754; Ribosomal_S9.
DR InterPro; IPR020574; Ribosomal_S9_CS.
DR PANTHER; PTHR21569; PTHR21569; 1.
DR Pfam; PF00380; Ribosomal_S9; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR PROSITE; PS00360; RIBOSOMAL_S9; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 146 40S ribosomal protein S16.
FT /FTId=PRO_0000111479.
FT SITE 2 2 Not acetylated.
FT MOD_RES 60 60 N6-acetyllysine.
SQ SEQUENCE 146 AA; 16445 MW; 519BCFB91BB68A15 CRC64;
MPSKGPLQSV QVFGRKKTAT AVAHCKRGNG LIKVNGRPLE MIEPRTLQYK LLEPVLLLGK
ERFAGVDIRV RVKGGGHVAQ IYAIRQSISK ALVAYYQKYV DEASKKEIKD ILIQYDRTLL
VADPRRCESK KFGGPGARAR YQKSYR
//
MIM
603675
*RECORD*
*FIELD* NO
603675
*FIELD* TI
*603675 RIBOSOMAL PROTEIN S16; RPS16
*FIELD* TX
The mammalian ribosome is composed of 4 RNA species (see 180450) and
read moreapproximately 80 different proteins.
To identify genes that are differentially expressed in a poorly
differentiated human pancreatic tumor cell line (Panc-1) compared to a
well-differentiated pancreatic tumor cell line (CD11), Batra et al.
(1991) screened a Panc-1 cDNA library by differential hybridization
using Panc-1 and CD11 cDNAs. They isolated a cDNA encoding ribosomal
protein S16 (RPS16). On Northern blots, the RPS16 cDNA hybridized to a
650-bp transcript showing 30-fold higher expression in Panc-1 cells than
in CD11 cells. The RPS16 transcript was not overexpressed in the other
13 pancreatic tumor cell lines examined or in 2 breast cancer cell
lines, 2 colon cancer cell lines, or normal tissues. Southern blot
analysis showed a 20-fold amplification of the RPS16 gene only in the
Panc-1 cell line. The deduced 146-amino acid RPS16 protein is identical
to rat Rps16.
By somatic cell hybrid and radiation hybrid mapping analyses, Kenmochi
et al. (1998) mapped the human RPS16 gene to 19q.
*FIELD* RF
1. Batra, S. K.; Metzgar, R. S.; Hollingsworth, M. A.: Molecular
cloning and sequence analysis of the human ribosomal protein S16. J.
Biol. Chem. 266: 6830-6833, 1991.
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.
*FIELD* CD
Patti M. Sherman: 3/25/1999
*FIELD* ED
carol: 04/07/1999
carol: 4/1/1999
*RECORD*
*FIELD* NO
603675
*FIELD* TI
*603675 RIBOSOMAL PROTEIN S16; RPS16
*FIELD* TX
The mammalian ribosome is composed of 4 RNA species (see 180450) and
read moreapproximately 80 different proteins.
To identify genes that are differentially expressed in a poorly
differentiated human pancreatic tumor cell line (Panc-1) compared to a
well-differentiated pancreatic tumor cell line (CD11), Batra et al.
(1991) screened a Panc-1 cDNA library by differential hybridization
using Panc-1 and CD11 cDNAs. They isolated a cDNA encoding ribosomal
protein S16 (RPS16). On Northern blots, the RPS16 cDNA hybridized to a
650-bp transcript showing 30-fold higher expression in Panc-1 cells than
in CD11 cells. The RPS16 transcript was not overexpressed in the other
13 pancreatic tumor cell lines examined or in 2 breast cancer cell
lines, 2 colon cancer cell lines, or normal tissues. Southern blot
analysis showed a 20-fold amplification of the RPS16 gene only in the
Panc-1 cell line. The deduced 146-amino acid RPS16 protein is identical
to rat Rps16.
By somatic cell hybrid and radiation hybrid mapping analyses, Kenmochi
et al. (1998) mapped the human RPS16 gene to 19q.
*FIELD* RF
1. Batra, S. K.; Metzgar, R. S.; Hollingsworth, M. A.: Molecular
cloning and sequence analysis of the human ribosomal protein S16. J.
Biol. Chem. 266: 6830-6833, 1991.
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.
*FIELD* CD
Patti M. Sherman: 3/25/1999
*FIELD* ED
carol: 04/07/1999
carol: 4/1/1999