Full text data of RPE
RPE
[Confidence: low (only semi-automatic identification from reviews)]
Ribulose-phosphate 3-epimerase; 5.1.3.1 (Ribulose-5-phosphate-3-epimerase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ribulose-phosphate 3-epimerase; 5.1.3.1 (Ribulose-5-phosphate-3-epimerase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q96AT9
ID RPE_HUMAN Reviewed; 228 AA.
AC Q96AT9; A8K4S0; O43767; Q53TV9; Q8N215; Q96N34; Q9BSB5;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=Ribulose-phosphate 3-epimerase;
DE EC=5.1.3.1;
DE AltName: Full=Ribulose-5-phosphate-3-epimerase;
GN Name=RPE; ORFNames=HUSSY-17;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow, Placenta, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 55-228 (ISOFORM 1).
RC TISSUE=Spleen;
RX PubMed=11124703;
RX DOI=10.1002/1097-0061(200101)18:1<69::AID-YEA647>3.3.CO;2-8;
RA Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B.,
RA Cannata N., Zimbello R., Lanfranchi G., Valle G.;
RT "Characterization of 16 novel human genes showing high similarity to
RT yeast sequences.";
RL Yeast 18:69-80(2001).
RN [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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 [8]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH IRON ION;
RP D-RIBULOSE 5-PHOSPHATE AND D-XYLULOSE 5-PHOSPHATE, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, AND MUTAGENESIS OF SER-10; LEU-12; HIS-35; ASP-37;
RP MET-39; HIS-70; MET-72; MET-141 AND ASP-175.
RX PubMed=20923965; DOI=10.1096/fj.10-171207;
RA Liang W., Ouyang S., Shaw N., Joachimiak A., Zhang R., Liu Z.J.;
RT "Conversion of D-ribulose 5-phosphate to D-xylulose 5-phosphate: new
RT insights from structural and biochemical studies on human RPE.";
RL FASEB J. 25:497-504(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-224 IN COMPLEX WITH ZINC
RP AND IRON IONS.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of a D-ribulose-5-phosphate-3-epimerase (NP_954699)
RT from Homo sapiens at 2.20 A resolution.";
RL Submitted (MAR-2011) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the reversible epimerization of D-ribulose 5-
CC phosphate to D-xylulose 5-phosphate.
CC -!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = D-xylulose 5-
CC phosphate.
CC -!- COFACTOR: Binds 1 divalent metal cation per subunit. Active with
CC Fe(2+), and probably also with Mn(2+), Zn(2+) and Co(2+).
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC Self; NbExp=2; IntAct=EBI-372480, EBI-372480;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96AT9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96AT9-2; Sequence=VSP_008317, VSP_008318;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q96AT9-3; Sequence=VSP_047117, VSP_008318;
CC Note=Gene prediction based on EST data;
CC -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71076.1; Type=Frameshift; Positions=69;
CC Sequence=BAC04212.1; Type=Frameshift; Positions=42;
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DR EMBL; AK056028; BAB71076.1; ALT_FRAME; mRNA.
DR EMBL; AK093658; BAC04212.1; ALT_FRAME; mRNA.
DR EMBL; AK291035; BAF83724.1; -; mRNA.
DR EMBL; AC007038; AAX93087.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70473.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70474.1; -; Genomic_DNA.
DR EMBL; BC005148; AAH05148.2; -; mRNA.
DR EMBL; BC016764; AAH16764.1; -; mRNA.
DR EMBL; BC072401; AAH72401.1; -; mRNA.
DR EMBL; AJ224326; CAA11895.1; -; mRNA.
DR RefSeq; NP_001265211.1; NM_001278282.1.
DR RefSeq; NP_001265212.1; NM_001278283.1.
DR RefSeq; NP_001265214.1; NM_001278285.1.
DR RefSeq; NP_001265215.1; NM_001278286.1.
DR RefSeq; NP_001265217.1; NM_001278288.1.
DR RefSeq; NP_001265218.1; NM_001278289.1.
DR RefSeq; NP_008847.1; NM_006916.2.
DR RefSeq; NP_954699.1; NM_199229.2.
DR UniGene; Hs.282260; -.
DR UniGene; Hs.591638; -.
DR UniGene; Hs.734255; -.
DR PDB; 3OVP; X-ray; 1.70 A; A/B=1-228.
DR PDB; 3OVQ; X-ray; 2.00 A; A/B=1-228.
DR PDB; 3OVR; X-ray; 1.95 A; A/B=1-228.
DR PDB; 3QC3; X-ray; 2.20 A; A/B=1-224.
DR PDBsum; 3OVP; -.
DR PDBsum; 3OVQ; -.
DR PDBsum; 3OVR; -.
DR PDBsum; 3QC3; -.
DR ProteinModelPortal; Q96AT9; -.
DR SMR; Q96AT9; 4-225.
DR IntAct; Q96AT9; 2.
DR MINT; MINT-1448309; -.
DR STRING; 9606.ENSP00000352401; -.
DR DMDM; 34924986; -.
DR PaxDb; Q96AT9; -.
DR PRIDE; Q96AT9; -.
DR DNASU; 6120; -.
DR Ensembl; ENST00000359429; ENSP00000352401; ENSG00000197713.
DR Ensembl; ENST00000429921; ENSP00000401838; ENSG00000197713.
DR Ensembl; ENST00000436630; ENSP00000403808; ENSG00000197713.
DR Ensembl; ENST00000454822; ENSP00000394455; ENSG00000197713.
DR GeneID; 6120; -.
DR KEGG; hsa:6120; -.
DR UCSC; uc002vdo.4; human.
DR CTD; 6120; -.
DR GeneCards; GC02P210867; -.
DR H-InvDB; HIX0190555; -.
DR HGNC; HGNC:10293; RPE.
DR HPA; HPA036499; -.
DR MIM; 180480; gene.
DR neXtProt; NX_Q96AT9; -.
DR PharmGKB; PA34654; -.
DR eggNOG; COG0036; -.
DR HOGENOM; HOG000259349; -.
DR HOVERGEN; HBG044821; -.
DR InParanoid; Q96AT9; -.
DR KO; K01783; -.
DR OMA; HIDRTLQ; -.
DR OrthoDB; EOG789CC1; -.
DR Reactome; REACT_111217; Metabolism.
DR EvolutionaryTrace; Q96AT9; -.
DR GeneWiki; RPE_(gene); -.
DR GenomeRNAi; 6120; -.
DR NextBio; 23767; -.
DR PRO; PR:Q96AT9; -.
DR ArrayExpress; Q96AT9; -.
DR Bgee; Q96AT9; -.
DR CleanEx; HS_RPE; -.
DR Genevestigator; Q96AT9; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR GO; GO:0048029; F:monosaccharide binding; IEA:Ensembl.
DR GO; GO:0004750; F:ribulose-phosphate 3-epimerase activity; IDA:UniProtKB.
DR GO; GO:0006098; P:pentose-phosphate shunt; IDA:UniProtKB.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IEA:Ensembl.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR026019; Ribul_P_3_epim.
DR InterPro; IPR000056; Ribul_P_3_epim-like.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR11749; PTHR11749; 1.
DR Pfam; PF00834; Ribul_P_3_epim; 1.
DR PIRSF; PIRSF001461; RPE; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR01163; rpe; 1.
DR PROSITE; PS01085; RIBUL_P_3_EPIMER_1; 1.
DR PROSITE; PS01086; RIBUL_P_3_EPIMER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing;
KW Carbohydrate metabolism; Cobalt; Complete proteome; Iron; Isomerase;
KW Manganese; Metal-binding; Reference proteome; Zinc.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 228 Ribulose-phosphate 3-epimerase.
FT /FTId=PRO_0000171587.
FT REGION 146 149 Substrate binding.
FT REGION 197 198 Substrate binding.
FT ACT_SITE 37 37 Proton acceptor (Probable).
FT ACT_SITE 175 175 Proton donor (Probable).
FT METAL 35 35 Divalent metal cation.
FT METAL 37 37 Divalent metal cation.
FT METAL 70 70 Divalent metal cation.
FT METAL 175 175 Divalent metal cation.
FT BINDING 10 10 Substrate.
FT BINDING 70 70 Substrate.
FT BINDING 177 177 Substrate; via amide nitrogen.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 1 68 Missing (in isoform 3).
FT /FTId=VSP_047117.
FT VAR_SEQ 43 68 Missing (in isoform 2).
FT /FTId=VSP_008317.
FT VAR_SEQ 114 114 K -> KSCSVTQAEVQWHSQGPLQ (in isoform 2
FT and isoform 3).
FT /FTId=VSP_008318.
FT MUTAGEN 10 10 S->A: Nearly abolishes enzyme activity.
FT MUTAGEN 12 12 L->A: Reduces enzyme activity by half.
FT MUTAGEN 35 35 H->A: Alters protein structure. Nearly
FT abolishes enzyme activity.
FT MUTAGEN 37 37 D->A: Alters protein structure. Nearly
FT abolishes enzyme activity.
FT MUTAGEN 39 39 M->A: Lowers enzyme activity by 10%.
FT MUTAGEN 70 70 H->A: Alters protein structure.
FT MUTAGEN 72 72 M->A: Reduces enzyme activity by half.
FT MUTAGEN 141 141 M->A: No effect on enzyme activity.
FT MUTAGEN 175 175 D->A: Alters protein structure.
FT CONFLICT 180 180 P -> L (in Ref. 1; BAC04212).
FT STRAND 6 10
FT HELIX 16 18
FT HELIX 19 28
FT STRAND 34 45
FT HELIX 51 61
FT STRAND 63 65
FT STRAND 67 72
FT HELIX 76 79
FT HELIX 80 86
FT STRAND 89 94
FT HELIX 95 97
FT HELIX 101 110
FT STRAND 114 119
FT HELIX 125 127
FT HELIX 129 134
FT STRAND 136 143
FT TURN 145 147
FT HELIX 154 156
FT HELIX 157 166
FT STRAND 171 177
FT TURN 180 182
FT HELIX 183 189
FT STRAND 193 197
FT HELIX 198 201
FT HELIX 206 223
SQ SEQUENCE 228 AA; 24928 MW; 447130018AC52331 CRC64;
MASGCKIGPS ILNSDLANLG AECLRMLDSG ADYLHLDVMD GHFVPNITFG HPVVESLRKQ
LGQDPFFDMH MMVSKPEQWV KPMAVAGANQ YTFHLEATEN PGALIKDIRE NGMKVGLAIK
PGTSVEYLAP WANQIDMALV MTVEPGFGGQ KFMEDMMPKV HWLRTQFPSL DIEVDGGVGP
DTVHKCAEAG ANMIVSGSAI MRSEDPRSVI NLLRNVCSEA AQKRSLDR
//
ID RPE_HUMAN Reviewed; 228 AA.
AC Q96AT9; A8K4S0; O43767; Q53TV9; Q8N215; Q96N34; Q9BSB5;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=Ribulose-phosphate 3-epimerase;
DE EC=5.1.3.1;
DE AltName: Full=Ribulose-5-phosphate-3-epimerase;
GN Name=RPE; ORFNames=HUSSY-17;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow, Placenta, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 55-228 (ISOFORM 1).
RC TISSUE=Spleen;
RX PubMed=11124703;
RX DOI=10.1002/1097-0061(200101)18:1<69::AID-YEA647>3.3.CO;2-8;
RA Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B.,
RA Cannata N., Zimbello R., Lanfranchi G., Valle G.;
RT "Characterization of 16 novel human genes showing high similarity to
RT yeast sequences.";
RL Yeast 18:69-80(2001).
RN [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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 [8]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH IRON ION;
RP D-RIBULOSE 5-PHOSPHATE AND D-XYLULOSE 5-PHOSPHATE, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, AND MUTAGENESIS OF SER-10; LEU-12; HIS-35; ASP-37;
RP MET-39; HIS-70; MET-72; MET-141 AND ASP-175.
RX PubMed=20923965; DOI=10.1096/fj.10-171207;
RA Liang W., Ouyang S., Shaw N., Joachimiak A., Zhang R., Liu Z.J.;
RT "Conversion of D-ribulose 5-phosphate to D-xylulose 5-phosphate: new
RT insights from structural and biochemical studies on human RPE.";
RL FASEB J. 25:497-504(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-224 IN COMPLEX WITH ZINC
RP AND IRON IONS.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of a D-ribulose-5-phosphate-3-epimerase (NP_954699)
RT from Homo sapiens at 2.20 A resolution.";
RL Submitted (MAR-2011) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the reversible epimerization of D-ribulose 5-
CC phosphate to D-xylulose 5-phosphate.
CC -!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = D-xylulose 5-
CC phosphate.
CC -!- COFACTOR: Binds 1 divalent metal cation per subunit. Active with
CC Fe(2+), and probably also with Mn(2+), Zn(2+) and Co(2+).
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC Self; NbExp=2; IntAct=EBI-372480, EBI-372480;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96AT9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96AT9-2; Sequence=VSP_008317, VSP_008318;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q96AT9-3; Sequence=VSP_047117, VSP_008318;
CC Note=Gene prediction based on EST data;
CC -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71076.1; Type=Frameshift; Positions=69;
CC Sequence=BAC04212.1; Type=Frameshift; Positions=42;
CC -----------------------------------------------------------------------
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DR EMBL; AK056028; BAB71076.1; ALT_FRAME; mRNA.
DR EMBL; AK093658; BAC04212.1; ALT_FRAME; mRNA.
DR EMBL; AK291035; BAF83724.1; -; mRNA.
DR EMBL; AC007038; AAX93087.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70473.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70474.1; -; Genomic_DNA.
DR EMBL; BC005148; AAH05148.2; -; mRNA.
DR EMBL; BC016764; AAH16764.1; -; mRNA.
DR EMBL; BC072401; AAH72401.1; -; mRNA.
DR EMBL; AJ224326; CAA11895.1; -; mRNA.
DR RefSeq; NP_001265211.1; NM_001278282.1.
DR RefSeq; NP_001265212.1; NM_001278283.1.
DR RefSeq; NP_001265214.1; NM_001278285.1.
DR RefSeq; NP_001265215.1; NM_001278286.1.
DR RefSeq; NP_001265217.1; NM_001278288.1.
DR RefSeq; NP_001265218.1; NM_001278289.1.
DR RefSeq; NP_008847.1; NM_006916.2.
DR RefSeq; NP_954699.1; NM_199229.2.
DR UniGene; Hs.282260; -.
DR UniGene; Hs.591638; -.
DR UniGene; Hs.734255; -.
DR PDB; 3OVP; X-ray; 1.70 A; A/B=1-228.
DR PDB; 3OVQ; X-ray; 2.00 A; A/B=1-228.
DR PDB; 3OVR; X-ray; 1.95 A; A/B=1-228.
DR PDB; 3QC3; X-ray; 2.20 A; A/B=1-224.
DR PDBsum; 3OVP; -.
DR PDBsum; 3OVQ; -.
DR PDBsum; 3OVR; -.
DR PDBsum; 3QC3; -.
DR ProteinModelPortal; Q96AT9; -.
DR SMR; Q96AT9; 4-225.
DR IntAct; Q96AT9; 2.
DR MINT; MINT-1448309; -.
DR STRING; 9606.ENSP00000352401; -.
DR DMDM; 34924986; -.
DR PaxDb; Q96AT9; -.
DR PRIDE; Q96AT9; -.
DR DNASU; 6120; -.
DR Ensembl; ENST00000359429; ENSP00000352401; ENSG00000197713.
DR Ensembl; ENST00000429921; ENSP00000401838; ENSG00000197713.
DR Ensembl; ENST00000436630; ENSP00000403808; ENSG00000197713.
DR Ensembl; ENST00000454822; ENSP00000394455; ENSG00000197713.
DR GeneID; 6120; -.
DR KEGG; hsa:6120; -.
DR UCSC; uc002vdo.4; human.
DR CTD; 6120; -.
DR GeneCards; GC02P210867; -.
DR H-InvDB; HIX0190555; -.
DR HGNC; HGNC:10293; RPE.
DR HPA; HPA036499; -.
DR MIM; 180480; gene.
DR neXtProt; NX_Q96AT9; -.
DR PharmGKB; PA34654; -.
DR eggNOG; COG0036; -.
DR HOGENOM; HOG000259349; -.
DR HOVERGEN; HBG044821; -.
DR InParanoid; Q96AT9; -.
DR KO; K01783; -.
DR OMA; HIDRTLQ; -.
DR OrthoDB; EOG789CC1; -.
DR Reactome; REACT_111217; Metabolism.
DR EvolutionaryTrace; Q96AT9; -.
DR GeneWiki; RPE_(gene); -.
DR GenomeRNAi; 6120; -.
DR NextBio; 23767; -.
DR PRO; PR:Q96AT9; -.
DR ArrayExpress; Q96AT9; -.
DR Bgee; Q96AT9; -.
DR CleanEx; HS_RPE; -.
DR Genevestigator; Q96AT9; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR GO; GO:0048029; F:monosaccharide binding; IEA:Ensembl.
DR GO; GO:0004750; F:ribulose-phosphate 3-epimerase activity; IDA:UniProtKB.
DR GO; GO:0006098; P:pentose-phosphate shunt; IDA:UniProtKB.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IEA:Ensembl.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR026019; Ribul_P_3_epim.
DR InterPro; IPR000056; Ribul_P_3_epim-like.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR11749; PTHR11749; 1.
DR Pfam; PF00834; Ribul_P_3_epim; 1.
DR PIRSF; PIRSF001461; RPE; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR01163; rpe; 1.
DR PROSITE; PS01085; RIBUL_P_3_EPIMER_1; 1.
DR PROSITE; PS01086; RIBUL_P_3_EPIMER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing;
KW Carbohydrate metabolism; Cobalt; Complete proteome; Iron; Isomerase;
KW Manganese; Metal-binding; Reference proteome; Zinc.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 228 Ribulose-phosphate 3-epimerase.
FT /FTId=PRO_0000171587.
FT REGION 146 149 Substrate binding.
FT REGION 197 198 Substrate binding.
FT ACT_SITE 37 37 Proton acceptor (Probable).
FT ACT_SITE 175 175 Proton donor (Probable).
FT METAL 35 35 Divalent metal cation.
FT METAL 37 37 Divalent metal cation.
FT METAL 70 70 Divalent metal cation.
FT METAL 175 175 Divalent metal cation.
FT BINDING 10 10 Substrate.
FT BINDING 70 70 Substrate.
FT BINDING 177 177 Substrate; via amide nitrogen.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 1 68 Missing (in isoform 3).
FT /FTId=VSP_047117.
FT VAR_SEQ 43 68 Missing (in isoform 2).
FT /FTId=VSP_008317.
FT VAR_SEQ 114 114 K -> KSCSVTQAEVQWHSQGPLQ (in isoform 2
FT and isoform 3).
FT /FTId=VSP_008318.
FT MUTAGEN 10 10 S->A: Nearly abolishes enzyme activity.
FT MUTAGEN 12 12 L->A: Reduces enzyme activity by half.
FT MUTAGEN 35 35 H->A: Alters protein structure. Nearly
FT abolishes enzyme activity.
FT MUTAGEN 37 37 D->A: Alters protein structure. Nearly
FT abolishes enzyme activity.
FT MUTAGEN 39 39 M->A: Lowers enzyme activity by 10%.
FT MUTAGEN 70 70 H->A: Alters protein structure.
FT MUTAGEN 72 72 M->A: Reduces enzyme activity by half.
FT MUTAGEN 141 141 M->A: No effect on enzyme activity.
FT MUTAGEN 175 175 D->A: Alters protein structure.
FT CONFLICT 180 180 P -> L (in Ref. 1; BAC04212).
FT STRAND 6 10
FT HELIX 16 18
FT HELIX 19 28
FT STRAND 34 45
FT HELIX 51 61
FT STRAND 63 65
FT STRAND 67 72
FT HELIX 76 79
FT HELIX 80 86
FT STRAND 89 94
FT HELIX 95 97
FT HELIX 101 110
FT STRAND 114 119
FT HELIX 125 127
FT HELIX 129 134
FT STRAND 136 143
FT TURN 145 147
FT HELIX 154 156
FT HELIX 157 166
FT STRAND 171 177
FT TURN 180 182
FT HELIX 183 189
FT STRAND 193 197
FT HELIX 198 201
FT HELIX 206 223
SQ SEQUENCE 228 AA; 24928 MW; 447130018AC52331 CRC64;
MASGCKIGPS ILNSDLANLG AECLRMLDSG ADYLHLDVMD GHFVPNITFG HPVVESLRKQ
LGQDPFFDMH MMVSKPEQWV KPMAVAGANQ YTFHLEATEN PGALIKDIRE NGMKVGLAIK
PGTSVEYLAP WANQIDMALV MTVEPGFGGQ KFMEDMMPKV HWLRTQFPSL DIEVDGGVGP
DTVHKCAEAG ANMIVSGSAI MRSEDPRSVI NLLRNVCSEA AQKRSLDR
//
MIM
180480
*RECORD*
*FIELD* NO
180480
*FIELD* TI
*180480 RIBULOSE 5-PHOSPHATE 3-EPIMERASE; RPE
*FIELD* TX
Spencer and Hopkinson (1980) found this enzyme (EC 5.1.3.1) of the
read morepentose phosphate cycle in all human tissues. No evidence was found for
more than one structural locus. No allelic variation was found in over
200 unrelated persons. The authors did find an electrophoretic
difference between human and mouse RPE and suggested that gene mapping
might be possible. Donald et al. (1982) assigned RPE to chromosome 2 by
study of human-Chinese hamster hybrid cells. Gross et al. (1982)
assigned RPE to the 2q32-2qter segment. By studies of dosage effect in a
new case of interstitial deletion of 2q, Dallapiccola et al. (1988)
reported that the RPE locus is situated in the subregion 2q32-q33.3.
Miyazaki et al. (1988) corroborated the assignment of RPE to 2q32.1-q34
by demonstration of half-normal activity of the enzyme in a child with
interstitial deletion of that segment.
*FIELD* SA
Donald et al. (1982)
*FIELD* RF
1. Dallapiccola, B.; Novelli, G.; Giannotti, A.: Deletion 2q31.3-2q33.3:
gene dosage effect of ribulose 5-phosphate 3-epimerase. Hum. Genet. 79:
92 only, 1988.
2. Donald, L. J.; Wang, H. S.; Hamerton, J. L.: Assignment of the
gene for ribulose-5-phosphate 3-epimerase (RPE) to human chromosome
2. (Abstract) Cytogenet. Cell Genet. 32: 268 only, 1982.
3. Donald, L. J.; Wang, H. S.; Hamerton, J. L.: A ribulose-5-phosphate-3-epimerase
(RPE) locus is on human chromosome 2. Cytogenet. Cell Genet. 33:
261-263, 1982.
4. Gross, M.-S.; Weil, D.; Van Cong, N.; Finaz, C.; Foubert, C.; Cochet,
C.; Parisi, I.; de Grouchy, J.; Frezal, J.: Localisation du gene
de la ribulose-5-phosphate-3-epimerase (RPE) sur le segment 2q32-2qter
par hybridation cellulaire interspecifique. Ann. Genet. 25: 87-91,
1982.
5. Miyazaki, K.; Yamanaka, T.; Ogasawara, N.: Interstitial deletion
2q32.1-q34 in a child with half normal activity of ribulose 5-phosphate
3-epimerase (RPE). J. Med. Genet. 25: 850-851, 1988.
6. Spencer, N.; Hopkinson, D. A.: Biochemical genetics of the pentose
phosphate cycle: human ribose 5-phosphate isomerase (RPI) and ribulose
5-phosphate 3-epimerase (RPE). Ann. Hum. Genet. 43: 335-342, 1980.
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
root: 12/19/1988
root: 6/20/1988
marie: 3/25/1988
*RECORD*
*FIELD* NO
180480
*FIELD* TI
*180480 RIBULOSE 5-PHOSPHATE 3-EPIMERASE; RPE
*FIELD* TX
Spencer and Hopkinson (1980) found this enzyme (EC 5.1.3.1) of the
read morepentose phosphate cycle in all human tissues. No evidence was found for
more than one structural locus. No allelic variation was found in over
200 unrelated persons. The authors did find an electrophoretic
difference between human and mouse RPE and suggested that gene mapping
might be possible. Donald et al. (1982) assigned RPE to chromosome 2 by
study of human-Chinese hamster hybrid cells. Gross et al. (1982)
assigned RPE to the 2q32-2qter segment. By studies of dosage effect in a
new case of interstitial deletion of 2q, Dallapiccola et al. (1988)
reported that the RPE locus is situated in the subregion 2q32-q33.3.
Miyazaki et al. (1988) corroborated the assignment of RPE to 2q32.1-q34
by demonstration of half-normal activity of the enzyme in a child with
interstitial deletion of that segment.
*FIELD* SA
Donald et al. (1982)
*FIELD* RF
1. Dallapiccola, B.; Novelli, G.; Giannotti, A.: Deletion 2q31.3-2q33.3:
gene dosage effect of ribulose 5-phosphate 3-epimerase. Hum. Genet. 79:
92 only, 1988.
2. Donald, L. J.; Wang, H. S.; Hamerton, J. L.: Assignment of the
gene for ribulose-5-phosphate 3-epimerase (RPE) to human chromosome
2. (Abstract) Cytogenet. Cell Genet. 32: 268 only, 1982.
3. Donald, L. J.; Wang, H. S.; Hamerton, J. L.: A ribulose-5-phosphate-3-epimerase
(RPE) locus is on human chromosome 2. Cytogenet. Cell Genet. 33:
261-263, 1982.
4. Gross, M.-S.; Weil, D.; Van Cong, N.; Finaz, C.; Foubert, C.; Cochet,
C.; Parisi, I.; de Grouchy, J.; Frezal, J.: Localisation du gene
de la ribulose-5-phosphate-3-epimerase (RPE) sur le segment 2q32-2qter
par hybridation cellulaire interspecifique. Ann. Genet. 25: 87-91,
1982.
5. Miyazaki, K.; Yamanaka, T.; Ogasawara, N.: Interstitial deletion
2q32.1-q34 in a child with half normal activity of ribulose 5-phosphate
3-epimerase (RPE). J. Med. Genet. 25: 850-851, 1988.
6. Spencer, N.; Hopkinson, D. A.: Biochemical genetics of the pentose
phosphate cycle: human ribose 5-phosphate isomerase (RPI) and ribulose
5-phosphate 3-epimerase (RPE). Ann. Hum. Genet. 43: 335-342, 1980.
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
root: 12/19/1988
root: 6/20/1988
marie: 3/25/1988