Full text data of RPS6
RPS6
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
40S ribosomal protein S6 (Phosphoprotein NP33)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
40S ribosomal protein S6 (Phosphoprotein NP33)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00021840
IPI00021840 40S ribosomal protein S6 May play an important role in controlling cell growth and proliferation through the selective translation of particular classes of mRNA, It is dephosphorylated at growth arrest soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
IPI00021840 40S ribosomal protein S6 May play an important role in controlling cell growth and proliferation through the selective translation of particular classes of mRNA, It is dephosphorylated at growth arrest soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
UniProt
P62753
ID RS6_HUMAN Reviewed; 249 AA.
AC P62753; P08227; P10660; Q4VBY7; Q8N6Z7;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-AUG-1988, sequence version 1.
DT 22-JAN-2014, entry version 109.
DE RecName: Full=40S ribosomal protein S6;
DE AltName: Full=Phosphoprotein NP33;
GN Name=RPS6; ORFNames=OK/SW-cl.2;
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=2840355; DOI=10.1016/0378-1119(88)90414-3;
RA Lott J.B., Mackie G.A.;
RT "Isolation and characterization of cloned cDNAs that code for human
RT ribosomal protein S6.";
RL Gene 65:31-39(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3279029;
RA Heinze H., Arnold H.H., Fischer D., Kruppa J.;
RT "The primary structure of the human ribosomal protein S6 derived from
RT a cloned cDNA.";
RL J. Biol. Chem. 263:4139-4144(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1301164; DOI=10.1093/hmg/1.8.565;
RA Antoine M., Fried M.;
RT "The organization of the intron-containing human S6 ribosomal protein
RT (rpS6) gene and determination of its location at chromosome 9p21.";
RL Hum. Mol. Genet. 1:565-570(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1446836; DOI=10.1016/0378-1119(92)90149-J;
RA Pata I., Hoth S., Kruppa J., Metspalu A.;
RT "The human ribosomal protein S6 gene: isolation, primary structure and
RT location in chromosome 9.";
RL Gene 121:387-392(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-
RT reactive CTL generated from TIL of colon cancer patients.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-221.
RC TISSUE=Colon, Muscle, Pancreas, Skin, and Testis;
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 1-15.
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION AT SER-235 AND SER-236.
RX PubMed=17360704; DOI=10.1074/jbc.M700906200;
RA Roux P.P., Shahbazian D., Vu H., Holz M.K., Cohen M.S., Taunton J.,
RA Sonenberg N., Blenis J.;
RT "RAS/ERK signaling promotes site-specific ribosomal protein S6
RT phosphorylation via RSK and stimulates cap-dependent translation.";
RL J. Biol. Chem. 282:14056-14064(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235; SER-236; SER-240;
RP SER-244 AND SER-247, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP PHOSPHORYLATION AT SER-235 AND SER-236 BY DAPK1.
RX PubMed=18974095; DOI=10.1074/jbc.M805165200;
RA Stevens C., Lin Y., Harrison B., Burch L., Ridgway R.A., Sansom O.,
RA Hupp T.;
RT "Peptide combinatorial libraries identify TSC2 as a death-associated
RT protein kinase (DAPK) death domain-binding protein and reveal a
RT stimulatory role for DAPK in mTORC1 signaling.";
RL J. Biol. Chem. 284:334-344(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-211, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
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 [16]
RP PHOSPHORYLATION AT SER-235 AND SER-236, AND MUTAGENESIS OF
RP 235-SER-SER-236.
RX PubMed=21418524; DOI=10.1111/j.1742-4658.2011.08100.x;
RA Schlafli P., Troger J., Eckhardt K., Borter E., Spielmann P.,
RA Wenger R.H.;
RT "Substrate preference and phosphatidylinositol monophosphate
RT inhibition of the catalytic domain of the Per-Arnt-Sim domain kinase
RT PASKIN.";
RL FEBS J. 278:1757-1768(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236; SER-240 AND
RP SER-242, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
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 [19]
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: May play an important role in controlling cell growth
CC and proliferation through the selective translation of particular
CC classes of mRNA.
CC -!- INTERACTION:
CC Q09161:NCBP1; NbExp=3; IntAct=EBI-356625, EBI-464743;
CC Q96RG2:PASK; NbExp=3; IntAct=EBI-356625, EBI-1042651;
CC -!- PTM: Ribosomal protein S6 is the major substrate of protein
CC kinases in eukaryote ribosomes. The phosphorylation is stimulated
CC by growth factors, tumor promoting agents, and mitogens. It is
CC dephosphorylated at growth arrest. Phosphorylated at Ser-235 and
CC Ser-236 by RPS6KA1 and RPS6KA3; phosphorylation at these sites
CC facilitates the assembly of the preinitiation complex.
CC -!- SIMILARITY: Belongs to the ribosomal protein S6e family.
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DR EMBL; M20020; AAA60288.1; -; mRNA.
DR EMBL; J03537; AAA60287.1; -; mRNA.
DR EMBL; X67309; CAA47719.1; -; Genomic_DNA.
DR EMBL; M77232; AAA60289.1; -; Genomic_DNA.
DR EMBL; AB062123; BAB93455.1; -; mRNA.
DR EMBL; BC000524; AAH00524.1; -; mRNA.
DR EMBL; BC009427; AAH09427.2; -; mRNA.
DR EMBL; BC027620; AAH27620.1; -; mRNA.
DR EMBL; BC071907; AAH71907.1; -; mRNA.
DR EMBL; BC071908; AAH71908.1; -; mRNA.
DR EMBL; BC094826; AAH94826.1; -; mRNA.
DR PIR; JC1394; R3HU6.
DR RefSeq; NP_001001.2; NM_001010.2.
DR UniGene; Hs.408073; -.
DR PDB; 3J3A; EM; 5.00 A; G=1-249.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; P62753; -.
DR SMR; P62753; 1-237.
DR DIP; DIP-31507N; -.
DR IntAct; P62753; 40.
DR MINT; MINT-1162101; -.
DR STRING; 9606.ENSP00000369757; -.
DR PhosphoSite; P62753; -.
DR DMDM; 51338632; -.
DR PaxDb; P62753; -.
DR PRIDE; P62753; -.
DR DNASU; 6194; -.
DR Ensembl; ENST00000380394; ENSP00000369757; ENSG00000137154.
DR GeneID; 6194; -.
DR KEGG; hsa:6194; -.
DR UCSC; uc003znv.1; human.
DR CTD; 6194; -.
DR GeneCards; GC09M019366; -.
DR HGNC; HGNC:10429; RPS6.
DR HPA; CAB004027; -.
DR HPA; HPA031153; -.
DR MIM; 180460; gene.
DR neXtProt; NX_P62753; -.
DR PharmGKB; PA34844; -.
DR eggNOG; COG2125; -.
DR HOGENOM; HOG000190952; -.
DR HOVERGEN; HBG011441; -.
DR InParanoid; P62753; -.
DR KO; K02991; -.
DR OMA; CQKLFEV; -.
DR OrthoDB; EOG7Z0JXB; -.
DR PhylomeDB; P62753; -.
DR Reactome; REACT_111102; Signal Transduction.
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 SignaLink; P62753; -.
DR ChiTaRS; RPS6; human.
DR GenomeRNAi; 6194; -.
DR NextBio; 24053; -.
DR PRO; PR:P62753; -.
DR ArrayExpress; P62753; -.
DR Bgee; P62753; -.
DR CleanEx; HS_RPS6; -.
DR Genevestigator; P62753; -.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IEA:Ensembl.
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:0031929; P:TOR signaling cascade; IDA:UniProtKB.
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 InterPro; IPR014401; Ribosomal_S6_euk.
DR InterPro; IPR001377; Ribosomal_S6e.
DR InterPro; IPR018282; Ribosomal_S6e_CS.
DR PANTHER; PTHR11502; PTHR11502; 1.
DR Pfam; PF01092; Ribosomal_S6e; 1.
DR PIRSF; PIRSF002129; Ribosom_S6_euk; 1.
DR PROSITE; PS00578; RIBOSOMAL_S6E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; Phosphoprotein; Polymorphism;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1 249 40S ribosomal protein S6.
FT /FTId=PRO_0000137312.
FT MOD_RES 211 211 N6-acetyllysine.
FT MOD_RES 235 235 Phosphoserine; by RPS6KA1, RPS6KA3, DAPK1
FT and PASK.
FT MOD_RES 236 236 Phosphoserine; by RPS6KA1, RPS6KA3, DAPK1
FT and PASK.
FT MOD_RES 240 240 Phosphoserine.
FT MOD_RES 242 242 Phosphoserine.
FT MOD_RES 244 244 Phosphoserine.
FT MOD_RES 247 247 Phosphoserine.
FT VARIANT 221 221 K -> R (in dbSNP:rs17852447).
FT /FTId=VAR_025314.
FT MUTAGEN 235 236 SS->AA: Abolishes phosphorylation by
FT PASK.
FT CONFLICT 23 23 K -> T (in Ref. 1; AAA60288).
FT CONFLICT 144 144 L -> R (in Ref. 1; AAA60288).
FT CONFLICT 155 156 QY -> EC (in Ref. 2; AAA60287).
FT CONFLICT 168 168 K -> R (in Ref. 2; AAA60287).
FT CONFLICT 196 196 K -> Q (in Ref. 1; AAA60288).
FT CONFLICT 219 219 E -> Q (in Ref. 2; AAA60287).
SQ SEQUENCE 249 AA; 28681 MW; A61E435884E636AE CRC64;
MKLNISFPAT GCQKLIEVDD ERKLRTFYEK RMATEVAADA LGEEWKGYVV RISGGNDKQG
FPMKQGVLTH GRVRLLLSKG HSCYRPRRTG ERKRKSVRGC IVDANLSVLN LVIVKKGEKD
IPGLTDTTVP RRLGPKRASR IRKLFNLSKE DDVRQYVVRK PLNKEGKKPR TKAPKIQRLV
TPRVLQHKRR RIALKKQRTK KNKEEAAEYA KLLAKRMKEA KEKRQEQIAK RRRLSSLRAS
TSKSESSQK
//
ID RS6_HUMAN Reviewed; 249 AA.
AC P62753; P08227; P10660; Q4VBY7; Q8N6Z7;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-AUG-1988, sequence version 1.
DT 22-JAN-2014, entry version 109.
DE RecName: Full=40S ribosomal protein S6;
DE AltName: Full=Phosphoprotein NP33;
GN Name=RPS6; ORFNames=OK/SW-cl.2;
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=2840355; DOI=10.1016/0378-1119(88)90414-3;
RA Lott J.B., Mackie G.A.;
RT "Isolation and characterization of cloned cDNAs that code for human
RT ribosomal protein S6.";
RL Gene 65:31-39(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3279029;
RA Heinze H., Arnold H.H., Fischer D., Kruppa J.;
RT "The primary structure of the human ribosomal protein S6 derived from
RT a cloned cDNA.";
RL J. Biol. Chem. 263:4139-4144(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1301164; DOI=10.1093/hmg/1.8.565;
RA Antoine M., Fried M.;
RT "The organization of the intron-containing human S6 ribosomal protein
RT (rpS6) gene and determination of its location at chromosome 9p21.";
RL Hum. Mol. Genet. 1:565-570(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1446836; DOI=10.1016/0378-1119(92)90149-J;
RA Pata I., Hoth S., Kruppa J., Metspalu A.;
RT "The human ribosomal protein S6 gene: isolation, primary structure and
RT location in chromosome 9.";
RL Gene 121:387-392(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-
RT reactive CTL generated from TIL of colon cancer patients.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-221.
RC TISSUE=Colon, Muscle, Pancreas, Skin, and Testis;
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 1-15.
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION AT SER-235 AND SER-236.
RX PubMed=17360704; DOI=10.1074/jbc.M700906200;
RA Roux P.P., Shahbazian D., Vu H., Holz M.K., Cohen M.S., Taunton J.,
RA Sonenberg N., Blenis J.;
RT "RAS/ERK signaling promotes site-specific ribosomal protein S6
RT phosphorylation via RSK and stimulates cap-dependent translation.";
RL J. Biol. Chem. 282:14056-14064(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235; SER-236; SER-240;
RP SER-244 AND SER-247, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP PHOSPHORYLATION AT SER-235 AND SER-236 BY DAPK1.
RX PubMed=18974095; DOI=10.1074/jbc.M805165200;
RA Stevens C., Lin Y., Harrison B., Burch L., Ridgway R.A., Sansom O.,
RA Hupp T.;
RT "Peptide combinatorial libraries identify TSC2 as a death-associated
RT protein kinase (DAPK) death domain-binding protein and reveal a
RT stimulatory role for DAPK in mTORC1 signaling.";
RL J. Biol. Chem. 284:334-344(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-211, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
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 [16]
RP PHOSPHORYLATION AT SER-235 AND SER-236, AND MUTAGENESIS OF
RP 235-SER-SER-236.
RX PubMed=21418524; DOI=10.1111/j.1742-4658.2011.08100.x;
RA Schlafli P., Troger J., Eckhardt K., Borter E., Spielmann P.,
RA Wenger R.H.;
RT "Substrate preference and phosphatidylinositol monophosphate
RT inhibition of the catalytic domain of the Per-Arnt-Sim domain kinase
RT PASKIN.";
RL FEBS J. 278:1757-1768(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236; SER-240 AND
RP SER-242, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
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 [19]
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: May play an important role in controlling cell growth
CC and proliferation through the selective translation of particular
CC classes of mRNA.
CC -!- INTERACTION:
CC Q09161:NCBP1; NbExp=3; IntAct=EBI-356625, EBI-464743;
CC Q96RG2:PASK; NbExp=3; IntAct=EBI-356625, EBI-1042651;
CC -!- PTM: Ribosomal protein S6 is the major substrate of protein
CC kinases in eukaryote ribosomes. The phosphorylation is stimulated
CC by growth factors, tumor promoting agents, and mitogens. It is
CC dephosphorylated at growth arrest. Phosphorylated at Ser-235 and
CC Ser-236 by RPS6KA1 and RPS6KA3; phosphorylation at these sites
CC facilitates the assembly of the preinitiation complex.
CC -!- SIMILARITY: Belongs to the ribosomal protein S6e family.
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DR EMBL; M20020; AAA60288.1; -; mRNA.
DR EMBL; J03537; AAA60287.1; -; mRNA.
DR EMBL; X67309; CAA47719.1; -; Genomic_DNA.
DR EMBL; M77232; AAA60289.1; -; Genomic_DNA.
DR EMBL; AB062123; BAB93455.1; -; mRNA.
DR EMBL; BC000524; AAH00524.1; -; mRNA.
DR EMBL; BC009427; AAH09427.2; -; mRNA.
DR EMBL; BC027620; AAH27620.1; -; mRNA.
DR EMBL; BC071907; AAH71907.1; -; mRNA.
DR EMBL; BC071908; AAH71908.1; -; mRNA.
DR EMBL; BC094826; AAH94826.1; -; mRNA.
DR PIR; JC1394; R3HU6.
DR RefSeq; NP_001001.2; NM_001010.2.
DR UniGene; Hs.408073; -.
DR PDB; 3J3A; EM; 5.00 A; G=1-249.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; P62753; -.
DR SMR; P62753; 1-237.
DR DIP; DIP-31507N; -.
DR IntAct; P62753; 40.
DR MINT; MINT-1162101; -.
DR STRING; 9606.ENSP00000369757; -.
DR PhosphoSite; P62753; -.
DR DMDM; 51338632; -.
DR PaxDb; P62753; -.
DR PRIDE; P62753; -.
DR DNASU; 6194; -.
DR Ensembl; ENST00000380394; ENSP00000369757; ENSG00000137154.
DR GeneID; 6194; -.
DR KEGG; hsa:6194; -.
DR UCSC; uc003znv.1; human.
DR CTD; 6194; -.
DR GeneCards; GC09M019366; -.
DR HGNC; HGNC:10429; RPS6.
DR HPA; CAB004027; -.
DR HPA; HPA031153; -.
DR MIM; 180460; gene.
DR neXtProt; NX_P62753; -.
DR PharmGKB; PA34844; -.
DR eggNOG; COG2125; -.
DR HOGENOM; HOG000190952; -.
DR HOVERGEN; HBG011441; -.
DR InParanoid; P62753; -.
DR KO; K02991; -.
DR OMA; CQKLFEV; -.
DR OrthoDB; EOG7Z0JXB; -.
DR PhylomeDB; P62753; -.
DR Reactome; REACT_111102; Signal Transduction.
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 SignaLink; P62753; -.
DR ChiTaRS; RPS6; human.
DR GenomeRNAi; 6194; -.
DR NextBio; 24053; -.
DR PRO; PR:P62753; -.
DR ArrayExpress; P62753; -.
DR Bgee; P62753; -.
DR CleanEx; HS_RPS6; -.
DR Genevestigator; P62753; -.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IEA:Ensembl.
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:0031929; P:TOR signaling cascade; IDA:UniProtKB.
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 InterPro; IPR014401; Ribosomal_S6_euk.
DR InterPro; IPR001377; Ribosomal_S6e.
DR InterPro; IPR018282; Ribosomal_S6e_CS.
DR PANTHER; PTHR11502; PTHR11502; 1.
DR Pfam; PF01092; Ribosomal_S6e; 1.
DR PIRSF; PIRSF002129; Ribosom_S6_euk; 1.
DR PROSITE; PS00578; RIBOSOMAL_S6E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; Phosphoprotein; Polymorphism;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1 249 40S ribosomal protein S6.
FT /FTId=PRO_0000137312.
FT MOD_RES 211 211 N6-acetyllysine.
FT MOD_RES 235 235 Phosphoserine; by RPS6KA1, RPS6KA3, DAPK1
FT and PASK.
FT MOD_RES 236 236 Phosphoserine; by RPS6KA1, RPS6KA3, DAPK1
FT and PASK.
FT MOD_RES 240 240 Phosphoserine.
FT MOD_RES 242 242 Phosphoserine.
FT MOD_RES 244 244 Phosphoserine.
FT MOD_RES 247 247 Phosphoserine.
FT VARIANT 221 221 K -> R (in dbSNP:rs17852447).
FT /FTId=VAR_025314.
FT MUTAGEN 235 236 SS->AA: Abolishes phosphorylation by
FT PASK.
FT CONFLICT 23 23 K -> T (in Ref. 1; AAA60288).
FT CONFLICT 144 144 L -> R (in Ref. 1; AAA60288).
FT CONFLICT 155 156 QY -> EC (in Ref. 2; AAA60287).
FT CONFLICT 168 168 K -> R (in Ref. 2; AAA60287).
FT CONFLICT 196 196 K -> Q (in Ref. 1; AAA60288).
FT CONFLICT 219 219 E -> Q (in Ref. 2; AAA60287).
SQ SEQUENCE 249 AA; 28681 MW; A61E435884E636AE CRC64;
MKLNISFPAT GCQKLIEVDD ERKLRTFYEK RMATEVAADA LGEEWKGYVV RISGGNDKQG
FPMKQGVLTH GRVRLLLSKG HSCYRPRRTG ERKRKSVRGC IVDANLSVLN LVIVKKGEKD
IPGLTDTTVP RRLGPKRASR IRKLFNLSKE DDVRQYVVRK PLNKEGKKPR TKAPKIQRLV
TPRVLQHKRR RIALKKQRTK KNKEEAAEYA KLLAKRMKEA KEKRQEQIAK RRRLSSLRAS
TSKSESSQK
//
MIM
180460
*RECORD*
*FIELD* NO
180460
*FIELD* TI
*180460 RIBOSOMAL PROTEIN S6; RPS6
*FIELD* TX
CLONING
Ribosomal protein S6 is the major substrate of protein kinases (e.g.,
read more300075) in eukaryotic ribosomes. Heinze et al. (1988) used polyclonal
antibodies directed against a synthetic octopeptide of the
phosphorylation site of the ribosomal protein S6 of rat liver to screen
a lambda-gt11 cDNA expression library of human lymphoblasts. In this way
an S6-specific clone was isolated. It consisted of the complete coding
sequence of 747 bases. The sequence of 249 amino acids deduced from the
nucleotide sequence showed a high degree of similarity to that of rat
liver S6. Southern blot analysis of human genomic DNA suggested that
multiple genes exist for the S6 protein. Independently, Lott and Mackie
(1988) cloned human RPS6 cDNAs using oligonucleotides based on the rat
Rps6 and yeast Rps10 amino acid sequences.
By Northern blot analysis using a rat Rps6 probe, Pogue-Geile et al.
(1991) found increased levels of RPS6 mRNA in 3 of 3 human colorectal
tumors and 2 of 4 human colon polyps relative to matched normal colonic
mucosa. RPS6 is expressed as an approximately 820-bp transcript.
GENE STRUCTURE
Antoine and Fried (1992) demonstrated that the RPS6 gene is 3,979 bp
long and comprises 6 exons.
MAPPING
Using a PCR product for the analysis of rodent/human somatic cell
hybrids, Feo et al. (1992) mapped the RPS6 gene to 9pter-p13. By
fluorescence in situ hybridization, Antoine and Fried (1992)
sublocalized the RPS6 gene to 9p21. Kenmochi et al. (1998) confirmed the
mapping assignment reported by Antoine and Fried (1992).
ANIMAL MODEL
Because ribosome biogenesis plays an essential role in cell
proliferation, control mechanisms may have evolved to recognize lesions
in this critical anabolic process. To test this possibility, Volarevic
et al. (2000) conditionally deleted the gene encoding 40S ribosomal
protein S6 in the liver of adult mice. Unexpectedly, livers from fasted
animals deficient in S6 grew in response to nutrients even though
biogenesis of 40S ribosomes was abolished. However, liver cells failed
to proliferate or induce cyclin E expression after partial hepatectomy,
despite formation of active cyclin D-CDK4 complexes. Volarevic et al.
(2000) concluded that their results implied that abrogation of 40S
ribosome biogenesis may induce a checkpoint control that prevents cell
cycle progression.
In order to study the relationship between ribosome biogenesis, cell
growth, and proliferation, Sulic et al. (2005) conditionally deleted 1
or 2 alleles of Rps6 in mouse thymi. Complete Rps6 deletion abrogated
T-cell development. Hemizygous Rps6 expression had no effect on T-cell
maturation in the thymus but inhibited the accumulation of T cells in
the spleen and lymph nodes as a result of their decreased survival in
peripheral lymphoid organs. Stimulation of Rps6-heterozygous T cells
induced a normal increase in size, but cell cycle progression was
impaired in a p53 (TP53; 191170)-dependent manner.
*FIELD* RF
1. Antoine, M.; Fried, M.: The organization of the intron-containing
human S6 ribosomal protein (rpS6) gene and determination of its location
at chromosome 9p21. Hum. Molec. Genet. 1: 565-570, 1992.
2. 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.
3. Heinze, H.; Arnold, H. H.; Fischer, D.; Kruppa, J.: The primary
structure of the human ribosomal protein S6 derived from a cloned
cDNA. J. Biol. Chem. 263: 4139-4144, 1988.
4. 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.
5. Lott, J. B.; Mackie, G. A.: Isolation and characterization of
cloned cDNAs that code for human ribosomal protein S6. Gene 65:
31-39, 1988.
6. Pogue-Geile, K.; Geiser, J. R.; Shu, M.; Miller, C.; Wool, I. G.;
Meisler, A. I.; Pipas, J. M.: Ribosomal protein genes are overexpressed
in colorectal cancer: isolation of a cDNA clone encoding the human
S3 ribosomal protein. Molec. Cell. Biol. 11: 3842-3849, 1991.
7. Sulic, S.; Panic, L.; Barkic, M.; Mercep, M.; Uzelac, M.; Volarevic,
S.: Inactivation of S6 ribosomal protein gene in T lymphocytes activates
a p53-dependent checkpoint response. Genes Dev. 19: 3070-3082, 2005.
8. Volarevic, S.; Stewart, M. J.; Ledermann, B.; Zilberman, F.; Terracciano,
L.; Montini, E.; Grompe, M.; Kozma, S. C.; Thomas, G.: Proliferation,
but not growth, blocked by conditional deletion of 40S ribosomal protein
S6. Science 288: 2045-2047, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 1/24/2006
Ada Hamosh - updated: 6/13/2000
Patti M. Sherman - updated: 3/18/1999
*FIELD* CD
Victor A. McKusick: 10/16/1986
*FIELD* ED
wwang: 03/02/2006
wwang: 2/10/2006
terry: 1/24/2006
alopez: 6/15/2000
terry: 6/13/2000
carol: 3/18/1999
dholmes: 4/8/1998
carol: 4/7/1993
carol: 11/30/1992
carol: 6/5/1992
supermim: 3/16/1992
carol: 3/6/1992
supermim: 3/20/1990
*RECORD*
*FIELD* NO
180460
*FIELD* TI
*180460 RIBOSOMAL PROTEIN S6; RPS6
*FIELD* TX
CLONING
Ribosomal protein S6 is the major substrate of protein kinases (e.g.,
read more300075) in eukaryotic ribosomes. Heinze et al. (1988) used polyclonal
antibodies directed against a synthetic octopeptide of the
phosphorylation site of the ribosomal protein S6 of rat liver to screen
a lambda-gt11 cDNA expression library of human lymphoblasts. In this way
an S6-specific clone was isolated. It consisted of the complete coding
sequence of 747 bases. The sequence of 249 amino acids deduced from the
nucleotide sequence showed a high degree of similarity to that of rat
liver S6. Southern blot analysis of human genomic DNA suggested that
multiple genes exist for the S6 protein. Independently, Lott and Mackie
(1988) cloned human RPS6 cDNAs using oligonucleotides based on the rat
Rps6 and yeast Rps10 amino acid sequences.
By Northern blot analysis using a rat Rps6 probe, Pogue-Geile et al.
(1991) found increased levels of RPS6 mRNA in 3 of 3 human colorectal
tumors and 2 of 4 human colon polyps relative to matched normal colonic
mucosa. RPS6 is expressed as an approximately 820-bp transcript.
GENE STRUCTURE
Antoine and Fried (1992) demonstrated that the RPS6 gene is 3,979 bp
long and comprises 6 exons.
MAPPING
Using a PCR product for the analysis of rodent/human somatic cell
hybrids, Feo et al. (1992) mapped the RPS6 gene to 9pter-p13. By
fluorescence in situ hybridization, Antoine and Fried (1992)
sublocalized the RPS6 gene to 9p21. Kenmochi et al. (1998) confirmed the
mapping assignment reported by Antoine and Fried (1992).
ANIMAL MODEL
Because ribosome biogenesis plays an essential role in cell
proliferation, control mechanisms may have evolved to recognize lesions
in this critical anabolic process. To test this possibility, Volarevic
et al. (2000) conditionally deleted the gene encoding 40S ribosomal
protein S6 in the liver of adult mice. Unexpectedly, livers from fasted
animals deficient in S6 grew in response to nutrients even though
biogenesis of 40S ribosomes was abolished. However, liver cells failed
to proliferate or induce cyclin E expression after partial hepatectomy,
despite formation of active cyclin D-CDK4 complexes. Volarevic et al.
(2000) concluded that their results implied that abrogation of 40S
ribosome biogenesis may induce a checkpoint control that prevents cell
cycle progression.
In order to study the relationship between ribosome biogenesis, cell
growth, and proliferation, Sulic et al. (2005) conditionally deleted 1
or 2 alleles of Rps6 in mouse thymi. Complete Rps6 deletion abrogated
T-cell development. Hemizygous Rps6 expression had no effect on T-cell
maturation in the thymus but inhibited the accumulation of T cells in
the spleen and lymph nodes as a result of their decreased survival in
peripheral lymphoid organs. Stimulation of Rps6-heterozygous T cells
induced a normal increase in size, but cell cycle progression was
impaired in a p53 (TP53; 191170)-dependent manner.
*FIELD* RF
1. Antoine, M.; Fried, M.: The organization of the intron-containing
human S6 ribosomal protein (rpS6) gene and determination of its location
at chromosome 9p21. Hum. Molec. Genet. 1: 565-570, 1992.
2. 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.
3. Heinze, H.; Arnold, H. H.; Fischer, D.; Kruppa, J.: The primary
structure of the human ribosomal protein S6 derived from a cloned
cDNA. J. Biol. Chem. 263: 4139-4144, 1988.
4. 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.
5. Lott, J. B.; Mackie, G. A.: Isolation and characterization of
cloned cDNAs that code for human ribosomal protein S6. Gene 65:
31-39, 1988.
6. Pogue-Geile, K.; Geiser, J. R.; Shu, M.; Miller, C.; Wool, I. G.;
Meisler, A. I.; Pipas, J. M.: Ribosomal protein genes are overexpressed
in colorectal cancer: isolation of a cDNA clone encoding the human
S3 ribosomal protein. Molec. Cell. Biol. 11: 3842-3849, 1991.
7. Sulic, S.; Panic, L.; Barkic, M.; Mercep, M.; Uzelac, M.; Volarevic,
S.: Inactivation of S6 ribosomal protein gene in T lymphocytes activates
a p53-dependent checkpoint response. Genes Dev. 19: 3070-3082, 2005.
8. Volarevic, S.; Stewart, M. J.; Ledermann, B.; Zilberman, F.; Terracciano,
L.; Montini, E.; Grompe, M.; Kozma, S. C.; Thomas, G.: Proliferation,
but not growth, blocked by conditional deletion of 40S ribosomal protein
S6. Science 288: 2045-2047, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 1/24/2006
Ada Hamosh - updated: 6/13/2000
Patti M. Sherman - updated: 3/18/1999
*FIELD* CD
Victor A. McKusick: 10/16/1986
*FIELD* ED
wwang: 03/02/2006
wwang: 2/10/2006
terry: 1/24/2006
alopez: 6/15/2000
terry: 6/13/2000
carol: 3/18/1999
dholmes: 4/8/1998
carol: 4/7/1993
carol: 11/30/1992
carol: 6/5/1992
supermim: 3/16/1992
carol: 3/6/1992
supermim: 3/20/1990