Full text data of TALDO1
TALDO1
(TAL, TALDO, TALDOR)
[Confidence: low (only semi-automatic identification from reviews)]
Transaldolase; 2.2.1.2
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Transaldolase; 2.2.1.2
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P37837
ID TALDO_HUMAN Reviewed; 337 AA.
AC P37837; B2R8M2; O00751; Q8WV32; Q8WZ45;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 30-MAY-2000, sequence version 2.
DT 22-JAN-2014, entry version 152.
DE RecName: Full=Transaldolase;
DE EC=2.2.1.2;
GN Name=TALDO1; Synonyms=TAL, TALDO, TALDOR;
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=8300619;
RA Banki K., Halladay D.L., Perl A.;
RT "Cloning and expression of the human gene for transaldolase. A novel
RT highly repetitive element constitutes an integral part of the coding
RT sequence.";
RL J. Biol. Chem. 269:2847-2851(1994).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=9339383; DOI=10.1006/geno.1997.4932;
RA Banki K., Eddy R.L., Shows T.B., Halladay D.L., Bullrich F.,
RA Croce C.M., Jurecic V., Baldini A., Perl A.;
RT "The human transaldolase gene (TALDO1) is located on chromosome 11 at
RT p15.4-p15.5.";
RL Genomics 45:233-238(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9524206; DOI=10.1016/S0378-1119(97)00639-2;
RA Kusuda J., Hirai M., Toyoda A., Tanuma R., Nomura-Kitabayashi A.,
RA Hashimoto K.;
RT "Cloning and chromosomal localization of a paralog and a mouse homolog
RT of the human transaldolase gene.";
RL Gene 209:13-21(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10702296; DOI=10.1074/jbc.275.10.7261;
RA Perl A., Colombo E., Samoilova E., Butler M.C., Banki K.;
RT "Human transaldolase-associated repetitive elements are transcribed by
RT RNA polymerase III.";
RL J. Biol. Chem. 275:7261-7272(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-110.
RA Perl A.;
RT "Family of active retrotransposons carry two exons of the
RT transaldolase gene and shows evidence of reverse splicing in human
RT DNA.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-219; LYS-269; LYS-286 AND
RP LYS-321, 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 [10]
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 [11]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS), SUBUNIT, AND ACTIVE SITE.
RX PubMed=10869557; DOI=10.1016/S0014-5793(00)01658-6;
RA Thorell S., Gergely P. Jr., Banki K., Perl A., Schneider G.;
RT "The three-dimensional structure of human transaldolase.";
RL FEBS Lett. 475:205-208(2000).
RN [12]
RP VARIANT TALDO1 DEFICIENCY SER-171 DEL.
RX PubMed=11283793; DOI=10.1086/320108;
RA Verhoeven N.M., Huck J.H.J., Roos B., Struys E.A., Salomons G.S.,
RA Douwes A.C., van der Knaap M.S., Jakobs C.;
RT "Transaldolase deficiency: liver cirrhosis associated with a new
RT inborn error in the pentose phosphate pathway.";
RL Am. J. Hum. Genet. 68:1086-1092(2001).
CC -!- FUNCTION: Transaldolase is important for the balance of
CC metabolites in the pentose-phosphate pathway.
CC -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde
CC 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate.
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-
CC ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative
CC stage): step 2/3.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC -!- DISEASE: Transaldolase 1 deficiency (TALDO1 deficiency)
CC [MIM:606003]: Results in telangiectases of the skin,
CC hepatosplenomegaly, and enlarged clitoris. Note=The disease is
CC caused by mutations affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC -!- WEB RESOURCE: Name=GeneReviews;
CC URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/TALDO1";
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; L19437; AAB53943.1; -; mRNA.
DR EMBL; AF010400; AAC52068.1; -; Genomic_DNA.
DR EMBL; AF010398; AAC52068.1; JOINED; Genomic_DNA.
DR EMBL; AF010399; AAC52068.1; JOINED; Genomic_DNA.
DR EMBL; AF058913; AAF40478.1; -; Genomic_DNA.
DR EMBL; AK313427; BAG36219.1; -; mRNA.
DR EMBL; BC010103; AAH10103.1; -; mRNA.
DR EMBL; BC018847; AAH18847.2; -; mRNA.
DR EMBL; L27346; AAL31313.1; -; Genomic_DNA.
DR PIR; A49985; A49985.
DR RefSeq; NP_006746.1; NM_006755.1.
DR UniGene; Hs.438678; -.
DR PDB; 1F05; X-ray; 2.45 A; A/B=1-337.
DR PDBsum; 1F05; -.
DR ProteinModelPortal; P37837; -.
DR SMR; P37837; 11-332.
DR IntAct; P37837; 4.
DR MINT; MINT-4999914; -.
DR STRING; 9606.ENSP00000321259; -.
DR Allergome; 9551; Hom s Transaldolase.
DR PhosphoSite; P37837; -.
DR DMDM; 6648092; -.
DR OGP; P37837; -.
DR REPRODUCTION-2DPAGE; IPI00744692; -.
DR PaxDb; P37837; -.
DR PeptideAtlas; P37837; -.
DR PRIDE; P37837; -.
DR Ensembl; ENST00000319006; ENSP00000321259; ENSG00000177156.
DR GeneID; 6888; -.
DR KEGG; hsa:6888; -.
DR UCSC; uc001lqz.3; human.
DR CTD; 6888; -.
DR GeneCards; GC11P000737; -.
DR HGNC; HGNC:11559; TALDO1.
DR HPA; HPA040373; -.
DR MIM; 602063; gene.
DR MIM; 606003; phenotype.
DR neXtProt; NX_P37837; -.
DR Orphanet; 101028; Transaldolase deficiency.
DR PharmGKB; PA36328; -.
DR eggNOG; COG0176; -.
DR HOGENOM; HOG000281234; -.
DR HOVERGEN; HBG054014; -.
DR InParanoid; P37837; -.
DR KO; K00616; -.
DR OMA; AQMPAYQ; -.
DR OrthoDB; EOG7MD4QF; -.
DR PhylomeDB; P37837; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00115; UER00414.
DR ChiTaRS; TALDO1; human.
DR EvolutionaryTrace; P37837; -.
DR GenomeRNAi; 6888; -.
DR NextBio; 26917; -.
DR PRO; PR:P37837; -.
DR ArrayExpress; P37837; -.
DR Bgee; P37837; -.
DR CleanEx; HS_TALDO1; -.
DR Genevestigator; P37837; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004801; F:sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity; TAS:ProtInc.
DR GO; GO:0006112; P:energy reserve metabolic process; TAS:Reactome.
DR GO; GO:0006098; P:pentose-phosphate shunt; TAS:Reactome.
DR GO; GO:0005999; P:xylulose biosynthetic process; TAS:Reactome.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001585; Transaldolase.
DR InterPro; IPR004730; Transaldolase_1.
DR InterPro; IPR018225; Transaldolase_AS.
DR PANTHER; PTHR10683; PTHR10683; 1.
DR Pfam; PF00923; Transaldolase; 1.
DR TIGRFAMs; TIGR00874; talAB; 1.
DR PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Disease mutation; Pentose shunt; Reference proteome; Schiff base;
KW Transferase.
FT CHAIN 1 337 Transaldolase.
FT /FTId=PRO_0000173564.
FT ACT_SITE 142 142 Schiff-base intermediate with substrate.
FT MOD_RES 219 219 N6-acetyllysine.
FT MOD_RES 269 269 N6-acetyllysine.
FT MOD_RES 286 286 N6-acetyllysine.
FT MOD_RES 321 321 N6-acetyllysine.
FT VARIANT 171 171 Missing (in TALDO1 deficiency).
FT /FTId=VAR_011511.
FT HELIX 14 21
FT STRAND 22 27
FT TURN 31 34
FT HELIX 35 37
FT STRAND 40 43
FT HELIX 46 53
FT HELIX 56 58
FT HELIX 59 72
FT HELIX 76 98
FT STRAND 103 106
FT HELIX 109 111
FT HELIX 115 131
FT HELIX 136 138
FT STRAND 139 144
FT HELIX 147 160
FT STRAND 164 169
FT HELIX 172 180
FT STRAND 184 190
FT HELIX 191 200
FT HELIX 208 210
FT HELIX 212 226
FT STRAND 232 236
FT HELIX 241 245
FT TURN 246 249
FT STRAND 250 255
FT HELIX 257 265
FT HELIX 276 281
FT HELIX 291 299
FT HELIX 302 330
SQ SEQUENCE 337 AA; 37540 MW; 8CB4992AEF364E64 CRC64;
MSSSPVKRQR MESALDQLKQ FTTVVADTGD FHAIDEYKPQ DATTNPSLIL AAAQMPAYQE
LVEEAIAYGR KLGGSQEDQI KNAIDKLFVL FGAEILKKIP GRVSTEVDAR LSFDKDAMVA
RARRLIELYK EAGISKDRIL IKLSSTWEGI QAGKELEEQH GIHCNMTLLF SFAQAVACAE
AGVTLISPFV GRILDWHVAN TDKKSYEPLE DPGVKSVTKI YNYYKKFSYK TIVMGASFRN
TGEIKALAGC DFLTISPKLL GELLQDNAKL VPVLSAKAAQ ASDLEKIHLD EKSFRWLHNE
DQMAVEKLSD GIRKFAADAV KLERMLTERM FNAENGK
//
ID TALDO_HUMAN Reviewed; 337 AA.
AC P37837; B2R8M2; O00751; Q8WV32; Q8WZ45;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 30-MAY-2000, sequence version 2.
DT 22-JAN-2014, entry version 152.
DE RecName: Full=Transaldolase;
DE EC=2.2.1.2;
GN Name=TALDO1; Synonyms=TAL, TALDO, TALDOR;
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=8300619;
RA Banki K., Halladay D.L., Perl A.;
RT "Cloning and expression of the human gene for transaldolase. A novel
RT highly repetitive element constitutes an integral part of the coding
RT sequence.";
RL J. Biol. Chem. 269:2847-2851(1994).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=9339383; DOI=10.1006/geno.1997.4932;
RA Banki K., Eddy R.L., Shows T.B., Halladay D.L., Bullrich F.,
RA Croce C.M., Jurecic V., Baldini A., Perl A.;
RT "The human transaldolase gene (TALDO1) is located on chromosome 11 at
RT p15.4-p15.5.";
RL Genomics 45:233-238(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9524206; DOI=10.1016/S0378-1119(97)00639-2;
RA Kusuda J., Hirai M., Toyoda A., Tanuma R., Nomura-Kitabayashi A.,
RA Hashimoto K.;
RT "Cloning and chromosomal localization of a paralog and a mouse homolog
RT of the human transaldolase gene.";
RL Gene 209:13-21(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10702296; DOI=10.1074/jbc.275.10.7261;
RA Perl A., Colombo E., Samoilova E., Butler M.C., Banki K.;
RT "Human transaldolase-associated repetitive elements are transcribed by
RT RNA polymerase III.";
RL J. Biol. Chem. 275:7261-7272(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-110.
RA Perl A.;
RT "Family of active retrotransposons carry two exons of the
RT transaldolase gene and shows evidence of reverse splicing in human
RT DNA.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-219; LYS-269; LYS-286 AND
RP LYS-321, 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 [10]
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 [11]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS), SUBUNIT, AND ACTIVE SITE.
RX PubMed=10869557; DOI=10.1016/S0014-5793(00)01658-6;
RA Thorell S., Gergely P. Jr., Banki K., Perl A., Schneider G.;
RT "The three-dimensional structure of human transaldolase.";
RL FEBS Lett. 475:205-208(2000).
RN [12]
RP VARIANT TALDO1 DEFICIENCY SER-171 DEL.
RX PubMed=11283793; DOI=10.1086/320108;
RA Verhoeven N.M., Huck J.H.J., Roos B., Struys E.A., Salomons G.S.,
RA Douwes A.C., van der Knaap M.S., Jakobs C.;
RT "Transaldolase deficiency: liver cirrhosis associated with a new
RT inborn error in the pentose phosphate pathway.";
RL Am. J. Hum. Genet. 68:1086-1092(2001).
CC -!- FUNCTION: Transaldolase is important for the balance of
CC metabolites in the pentose-phosphate pathway.
CC -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde
CC 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate.
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-
CC ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative
CC stage): step 2/3.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC -!- DISEASE: Transaldolase 1 deficiency (TALDO1 deficiency)
CC [MIM:606003]: Results in telangiectases of the skin,
CC hepatosplenomegaly, and enlarged clitoris. Note=The disease is
CC caused by mutations affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC -!- WEB RESOURCE: Name=GeneReviews;
CC URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/TALDO1";
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; L19437; AAB53943.1; -; mRNA.
DR EMBL; AF010400; AAC52068.1; -; Genomic_DNA.
DR EMBL; AF010398; AAC52068.1; JOINED; Genomic_DNA.
DR EMBL; AF010399; AAC52068.1; JOINED; Genomic_DNA.
DR EMBL; AF058913; AAF40478.1; -; Genomic_DNA.
DR EMBL; AK313427; BAG36219.1; -; mRNA.
DR EMBL; BC010103; AAH10103.1; -; mRNA.
DR EMBL; BC018847; AAH18847.2; -; mRNA.
DR EMBL; L27346; AAL31313.1; -; Genomic_DNA.
DR PIR; A49985; A49985.
DR RefSeq; NP_006746.1; NM_006755.1.
DR UniGene; Hs.438678; -.
DR PDB; 1F05; X-ray; 2.45 A; A/B=1-337.
DR PDBsum; 1F05; -.
DR ProteinModelPortal; P37837; -.
DR SMR; P37837; 11-332.
DR IntAct; P37837; 4.
DR MINT; MINT-4999914; -.
DR STRING; 9606.ENSP00000321259; -.
DR Allergome; 9551; Hom s Transaldolase.
DR PhosphoSite; P37837; -.
DR DMDM; 6648092; -.
DR OGP; P37837; -.
DR REPRODUCTION-2DPAGE; IPI00744692; -.
DR PaxDb; P37837; -.
DR PeptideAtlas; P37837; -.
DR PRIDE; P37837; -.
DR Ensembl; ENST00000319006; ENSP00000321259; ENSG00000177156.
DR GeneID; 6888; -.
DR KEGG; hsa:6888; -.
DR UCSC; uc001lqz.3; human.
DR CTD; 6888; -.
DR GeneCards; GC11P000737; -.
DR HGNC; HGNC:11559; TALDO1.
DR HPA; HPA040373; -.
DR MIM; 602063; gene.
DR MIM; 606003; phenotype.
DR neXtProt; NX_P37837; -.
DR Orphanet; 101028; Transaldolase deficiency.
DR PharmGKB; PA36328; -.
DR eggNOG; COG0176; -.
DR HOGENOM; HOG000281234; -.
DR HOVERGEN; HBG054014; -.
DR InParanoid; P37837; -.
DR KO; K00616; -.
DR OMA; AQMPAYQ; -.
DR OrthoDB; EOG7MD4QF; -.
DR PhylomeDB; P37837; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00115; UER00414.
DR ChiTaRS; TALDO1; human.
DR EvolutionaryTrace; P37837; -.
DR GenomeRNAi; 6888; -.
DR NextBio; 26917; -.
DR PRO; PR:P37837; -.
DR ArrayExpress; P37837; -.
DR Bgee; P37837; -.
DR CleanEx; HS_TALDO1; -.
DR Genevestigator; P37837; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004801; F:sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity; TAS:ProtInc.
DR GO; GO:0006112; P:energy reserve metabolic process; TAS:Reactome.
DR GO; GO:0006098; P:pentose-phosphate shunt; TAS:Reactome.
DR GO; GO:0005999; P:xylulose biosynthetic process; TAS:Reactome.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001585; Transaldolase.
DR InterPro; IPR004730; Transaldolase_1.
DR InterPro; IPR018225; Transaldolase_AS.
DR PANTHER; PTHR10683; PTHR10683; 1.
DR Pfam; PF00923; Transaldolase; 1.
DR TIGRFAMs; TIGR00874; talAB; 1.
DR PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Disease mutation; Pentose shunt; Reference proteome; Schiff base;
KW Transferase.
FT CHAIN 1 337 Transaldolase.
FT /FTId=PRO_0000173564.
FT ACT_SITE 142 142 Schiff-base intermediate with substrate.
FT MOD_RES 219 219 N6-acetyllysine.
FT MOD_RES 269 269 N6-acetyllysine.
FT MOD_RES 286 286 N6-acetyllysine.
FT MOD_RES 321 321 N6-acetyllysine.
FT VARIANT 171 171 Missing (in TALDO1 deficiency).
FT /FTId=VAR_011511.
FT HELIX 14 21
FT STRAND 22 27
FT TURN 31 34
FT HELIX 35 37
FT STRAND 40 43
FT HELIX 46 53
FT HELIX 56 58
FT HELIX 59 72
FT HELIX 76 98
FT STRAND 103 106
FT HELIX 109 111
FT HELIX 115 131
FT HELIX 136 138
FT STRAND 139 144
FT HELIX 147 160
FT STRAND 164 169
FT HELIX 172 180
FT STRAND 184 190
FT HELIX 191 200
FT HELIX 208 210
FT HELIX 212 226
FT STRAND 232 236
FT HELIX 241 245
FT TURN 246 249
FT STRAND 250 255
FT HELIX 257 265
FT HELIX 276 281
FT HELIX 291 299
FT HELIX 302 330
SQ SEQUENCE 337 AA; 37540 MW; 8CB4992AEF364E64 CRC64;
MSSSPVKRQR MESALDQLKQ FTTVVADTGD FHAIDEYKPQ DATTNPSLIL AAAQMPAYQE
LVEEAIAYGR KLGGSQEDQI KNAIDKLFVL FGAEILKKIP GRVSTEVDAR LSFDKDAMVA
RARRLIELYK EAGISKDRIL IKLSSTWEGI QAGKELEEQH GIHCNMTLLF SFAQAVACAE
AGVTLISPFV GRILDWHVAN TDKKSYEPLE DPGVKSVTKI YNYYKKFSYK TIVMGASFRN
TGEIKALAGC DFLTISPKLL GELLQDNAKL VPVLSAKAAQ ASDLEKIHLD EKSFRWLHNE
DQMAVEKLSD GIRKFAADAV KLERMLTERM FNAENGK
//
MIM
602063
*RECORD*
*FIELD* NO
602063
*FIELD* TI
*602063 TRANSALDOLASE 1; TALDO1
*FIELD* TX
DESCRIPTION
Transaldolase (EC 2.2.1.2) is the key enzyme of the pentose phosphate
read morepathway, which is responsible for generation of reducing equivalents to
protect cellular integrity from reactive oxygen intermediates (Banki et
al., 1997).
CLONING
Banki et al. (1994) cloned the TALDO1 gene. The deduced 336-amino acid
protein has a predicted molecular mass of 38 kD and shows 58% overall
sequence homology with the 37-kD yeast transaldolase.
Kusuda et al. (1998) isolated the cDNA for the mouse homolog of TALDO1
and determined the nucleotide sequence covering the complete coding
region.
GENE STRUCTURE
Banki et al. (1994) determined that, unlike the intronless yeast
transaldolase gene, the human TALDO1 gene contains 5 exons, the second
and third of which are developed by insertion of a retrotransposable
element. Detection of a retrotransposon in the coding sequence of the
human transaldolase gene demonstrated the importance of these repetitive
elements in the evolution of the eukaryotic genome.
MAPPING
By Southern blot analysis of human/mouse somatic cell hybrid DNA, Banki
et al. (1997) mapped TALDO1 to the region 11pter-p13. By fluorescence in
situ hybridization (FISH), they narrowed the assignment to
11p15.5-p15.4. A truncated and mutated segment of exon 5 terminating
with a poly(A) tail was identified in a pseudogene locus (TALDOP1) on
chromosome 1. RT-PCR studies of mouse/human somatic cell hybrids
revealed the presence of the functional gene on chromosome 11 and its
absence on chromosome 1. Mapping of radiation hybrids placed TALDO1
between the markers WI-1421 and D11S922 on 11p15.
By FISH, Kusuda et al. (1997) concluded that the functional TALDO1 gene
is located on 1p34.1-p33. Kusuda et al. (1998) mapped a paralogous gene
to 11p15, where Banki et al. (1997) had mapped the TALDO1 gene. Kusuda
et al. (1998) symbolized the gene on chromosome 11 as TALDOR (TALDO
related). The exon sequence of TALDOR was almost identical to that of
TALDO but its exons corresponding to exons 4 and 5 of TALDO were found
to be split by 4 introns.
By FISH using cDNA as a probe, Kusuda et al. (1998) showed that the
mouse transaldolase gene is localized to bands F3-F4 of chromosome 7 as
a single-copy gene. This chromosomal region is known to be syntenic to
human chromosome 11p15 rather than to 1p34.1-p33, suggesting that TALDOR
is the ancestral form. The existence of TALDOR implied a duplication of
the mammalian transaldolase gene after divergence of rodent and primate.
Hashimoto (1998) concluded that the functional TALDO gene is on human
chromosome 11 and a pseudogene on human chromosome 1.
MOLECULAR GENETICS
Verhoeven et al. (2001) described a patient with transaldolase
deficiency (606003) caused by a homozygous 3-bp deletion (602063.0001)
in the TALDO1 gene, resulting in the absence of serine at position 171
of the transaldolase protein. This amino acid is invariable between
species and is located in a conserved region, indicating its importance
for enzyme activity.
ANIMAL MODEL
Perl et al. (2006) found that Taldo1-null mice developed normally, but
males were sterile due to functional and structural defects of
mitochondria. Reduced motility in Taldo1-null spermatozoa was associated
with diminished mitochondrial reactive oxygen intermediate production,
reduced calcium levels, intracellular acidosis, and compensatory
downregulation of carbonic anhydrase IV (CA4; 114760) and overexpression
of Cd38 (107270) and gamma-glutamyltransferase (GGT1; 612346).
*FIELD* AV
.0001
TRANSALDOLASE DEFICIENCY
TALDO1, SER171DEL
In the first child of healthy, consanguineous Turkish parents, Verhoeven
et al. (2001) demonstrated transaldolase deficiency (606003) caused by a
homozygous 3-bp deletion in the TALDO1 gene that resulted in the loss of
ser171 in the transaldolase protein. Soon after birth, the patient had
undergone surgical correction of aortic coarctation. Within several
months, she developed hepatosplenomegaly. Elevated levels of several
pentoses were found in urine, plasma, and cerebrospinal fluid samples.
At the age of 10, the patient showed many telangiectases of the skin,
hepatosplenomegaly, and enlarged clitoris. She had persistent
thrombocytopenia which was thought to be caused by splenic pooling due
to the hepatosplenomegaly.
*FIELD* RF
1. Banki, K.; Eddy, R. L.; Shows, T. B.; Halladay, D. L.; Bullrich,
F.; Croce, C. M.; Jurecic, V.; Baldini, A.; Perl, A.: The human transaldolase
gene (TALDO1) is located on chromosome 11 at p15.4-p15.5. Genomics 45:
233-238, 1997.
2. Banki, K.; Halladay, D.; Perl, A.: Cloning and expression of the
human gene for transaldolase: a novel highly repetitive element constitutes
an integral part of the coding sequence. J. Biol. Chem. 269: 2847-2851,
1994.
3. Hashimoto, K.: Personal Communication. Tokyo, Japan 7/16/1998.
4. Kusuda, J.; Hirai, M.; Toyoda, A.; Hashimoto, K.: Localization
of the human transaldolase gene (TALDO) to chromosome 1p33-p34.1 by
fluorescence in situ hybridization and PCR analysis of somatic cell
hybrids. Genomics 40: 378-381, 1997.
5. Kusuda, J.; Hirai, M.; Toyoda, A.; Tanuma, R.; Nomura-Kitabayashi,
A.; Hashimoto, K.: Cloning and chromosomal localization of a paralog
and a mouse homolog of the human transaldolase gene. Gene 209: 13-21,
1998.
6. Perl, A.; Qian, Y.; Chohan, K. R.; Shirley, C. R.; Amidon, W.;
Banerjee, S.; Middleton, F. A.; Conkrite, K. L.; Barcza, M.; Gonchoroff,
N.; Suarez, S. S.; Banki, K.: Transaldolase is essential for maintenance
of the mitochondrial transmembrane potential and fertility of spermatozoa. Proc.
Nat. Acad. Sci. 103: 14813-14818, 2006.
7. Verhoeven, N. M.; Huck, J. H. J.; Roos, B.; Struys, E. A.; Salomons,
G. S.; Douwes, A. C.; van der Knaap, M. S.; Jakobs, C.: Transaldolase
deficiency: liver cirrhosis associated with a new inborn error in
the pentose phosphate pathway. Am. J. Hum. Genet. 68: 1086-1092,
2001.
*FIELD* CN
Patricia A. Hartz - updated: 1/25/2007
Victor A. McKusick - updated: 6/5/2001
Victor A. McKusick - updated: 10/1/1998
Victor A. McKusick - updated: 7/1/1998
*FIELD* CD
Victor A. McKusick: 10/16/1997
*FIELD* ED
mgross: 10/07/2008
mgross: 1/25/2007
carol: 6/12/2001
cwells: 6/7/2001
terry: 6/5/2001
dkim: 12/15/1998
carol: 10/5/1998
terry: 10/1/1998
carol: 7/14/1998
dholmes: 7/13/1998
terry: 7/1/1998
mark: 10/22/1997
*RECORD*
*FIELD* NO
602063
*FIELD* TI
*602063 TRANSALDOLASE 1; TALDO1
*FIELD* TX
DESCRIPTION
Transaldolase (EC 2.2.1.2) is the key enzyme of the pentose phosphate
read morepathway, which is responsible for generation of reducing equivalents to
protect cellular integrity from reactive oxygen intermediates (Banki et
al., 1997).
CLONING
Banki et al. (1994) cloned the TALDO1 gene. The deduced 336-amino acid
protein has a predicted molecular mass of 38 kD and shows 58% overall
sequence homology with the 37-kD yeast transaldolase.
Kusuda et al. (1998) isolated the cDNA for the mouse homolog of TALDO1
and determined the nucleotide sequence covering the complete coding
region.
GENE STRUCTURE
Banki et al. (1994) determined that, unlike the intronless yeast
transaldolase gene, the human TALDO1 gene contains 5 exons, the second
and third of which are developed by insertion of a retrotransposable
element. Detection of a retrotransposon in the coding sequence of the
human transaldolase gene demonstrated the importance of these repetitive
elements in the evolution of the eukaryotic genome.
MAPPING
By Southern blot analysis of human/mouse somatic cell hybrid DNA, Banki
et al. (1997) mapped TALDO1 to the region 11pter-p13. By fluorescence in
situ hybridization (FISH), they narrowed the assignment to
11p15.5-p15.4. A truncated and mutated segment of exon 5 terminating
with a poly(A) tail was identified in a pseudogene locus (TALDOP1) on
chromosome 1. RT-PCR studies of mouse/human somatic cell hybrids
revealed the presence of the functional gene on chromosome 11 and its
absence on chromosome 1. Mapping of radiation hybrids placed TALDO1
between the markers WI-1421 and D11S922 on 11p15.
By FISH, Kusuda et al. (1997) concluded that the functional TALDO1 gene
is located on 1p34.1-p33. Kusuda et al. (1998) mapped a paralogous gene
to 11p15, where Banki et al. (1997) had mapped the TALDO1 gene. Kusuda
et al. (1998) symbolized the gene on chromosome 11 as TALDOR (TALDO
related). The exon sequence of TALDOR was almost identical to that of
TALDO but its exons corresponding to exons 4 and 5 of TALDO were found
to be split by 4 introns.
By FISH using cDNA as a probe, Kusuda et al. (1998) showed that the
mouse transaldolase gene is localized to bands F3-F4 of chromosome 7 as
a single-copy gene. This chromosomal region is known to be syntenic to
human chromosome 11p15 rather than to 1p34.1-p33, suggesting that TALDOR
is the ancestral form. The existence of TALDOR implied a duplication of
the mammalian transaldolase gene after divergence of rodent and primate.
Hashimoto (1998) concluded that the functional TALDO gene is on human
chromosome 11 and a pseudogene on human chromosome 1.
MOLECULAR GENETICS
Verhoeven et al. (2001) described a patient with transaldolase
deficiency (606003) caused by a homozygous 3-bp deletion (602063.0001)
in the TALDO1 gene, resulting in the absence of serine at position 171
of the transaldolase protein. This amino acid is invariable between
species and is located in a conserved region, indicating its importance
for enzyme activity.
ANIMAL MODEL
Perl et al. (2006) found that Taldo1-null mice developed normally, but
males were sterile due to functional and structural defects of
mitochondria. Reduced motility in Taldo1-null spermatozoa was associated
with diminished mitochondrial reactive oxygen intermediate production,
reduced calcium levels, intracellular acidosis, and compensatory
downregulation of carbonic anhydrase IV (CA4; 114760) and overexpression
of Cd38 (107270) and gamma-glutamyltransferase (GGT1; 612346).
*FIELD* AV
.0001
TRANSALDOLASE DEFICIENCY
TALDO1, SER171DEL
In the first child of healthy, consanguineous Turkish parents, Verhoeven
et al. (2001) demonstrated transaldolase deficiency (606003) caused by a
homozygous 3-bp deletion in the TALDO1 gene that resulted in the loss of
ser171 in the transaldolase protein. Soon after birth, the patient had
undergone surgical correction of aortic coarctation. Within several
months, she developed hepatosplenomegaly. Elevated levels of several
pentoses were found in urine, plasma, and cerebrospinal fluid samples.
At the age of 10, the patient showed many telangiectases of the skin,
hepatosplenomegaly, and enlarged clitoris. She had persistent
thrombocytopenia which was thought to be caused by splenic pooling due
to the hepatosplenomegaly.
*FIELD* RF
1. Banki, K.; Eddy, R. L.; Shows, T. B.; Halladay, D. L.; Bullrich,
F.; Croce, C. M.; Jurecic, V.; Baldini, A.; Perl, A.: The human transaldolase
gene (TALDO1) is located on chromosome 11 at p15.4-p15.5. Genomics 45:
233-238, 1997.
2. Banki, K.; Halladay, D.; Perl, A.: Cloning and expression of the
human gene for transaldolase: a novel highly repetitive element constitutes
an integral part of the coding sequence. J. Biol. Chem. 269: 2847-2851,
1994.
3. Hashimoto, K.: Personal Communication. Tokyo, Japan 7/16/1998.
4. Kusuda, J.; Hirai, M.; Toyoda, A.; Hashimoto, K.: Localization
of the human transaldolase gene (TALDO) to chromosome 1p33-p34.1 by
fluorescence in situ hybridization and PCR analysis of somatic cell
hybrids. Genomics 40: 378-381, 1997.
5. Kusuda, J.; Hirai, M.; Toyoda, A.; Tanuma, R.; Nomura-Kitabayashi,
A.; Hashimoto, K.: Cloning and chromosomal localization of a paralog
and a mouse homolog of the human transaldolase gene. Gene 209: 13-21,
1998.
6. Perl, A.; Qian, Y.; Chohan, K. R.; Shirley, C. R.; Amidon, W.;
Banerjee, S.; Middleton, F. A.; Conkrite, K. L.; Barcza, M.; Gonchoroff,
N.; Suarez, S. S.; Banki, K.: Transaldolase is essential for maintenance
of the mitochondrial transmembrane potential and fertility of spermatozoa. Proc.
Nat. Acad. Sci. 103: 14813-14818, 2006.
7. Verhoeven, N. M.; Huck, J. H. J.; Roos, B.; Struys, E. A.; Salomons,
G. S.; Douwes, A. C.; van der Knaap, M. S.; Jakobs, C.: Transaldolase
deficiency: liver cirrhosis associated with a new inborn error in
the pentose phosphate pathway. Am. J. Hum. Genet. 68: 1086-1092,
2001.
*FIELD* CN
Patricia A. Hartz - updated: 1/25/2007
Victor A. McKusick - updated: 6/5/2001
Victor A. McKusick - updated: 10/1/1998
Victor A. McKusick - updated: 7/1/1998
*FIELD* CD
Victor A. McKusick: 10/16/1997
*FIELD* ED
mgross: 10/07/2008
mgross: 1/25/2007
carol: 6/12/2001
cwells: 6/7/2001
terry: 6/5/2001
dkim: 12/15/1998
carol: 10/5/1998
terry: 10/1/1998
carol: 7/14/1998
dholmes: 7/13/1998
terry: 7/1/1998
mark: 10/22/1997
MIM
606003
*RECORD*
*FIELD* NO
606003
*FIELD* TI
#606003 TRANSALDOLASE DEFICIENCY
*FIELD* TX
A number sign (#) is used with this entry because transaldolase
read moredeficiency is caused by homozygous mutation in the TALDO1 gene (602063).
CLINICAL FEATURES
Verhoeven et al. (2001) described deficiency of transaldolase in the
first child of healthy, consanguineous Turkish parents. Soon after
birth, the patient had undergone surgical correction of aortic
coarctation. Within several months, she developed hepatosplenomegaly.
Elevated concentrations of ribitol, D-arabitol, and erythritol were
found in urine and plasma. At the age of 10 years, the patient showed
many telangiectases of the skin, hepatosplenomegaly, and enlarged
clitoris. She had persistent thrombocytopenia which was thought to be
caused by splenic pooling due to the hepatosplenomegaly. A deficiency of
transaldolase was discovered by incubating the patient's lymphoblasts
and erythrocytes with ribose-5-phosphate and subsequently analyzing
phosphate sugar metabolites.
MOLECULAR GENETICS
By sequence analysis of the TALDO1 gene in a patient with transaldolase
deficiency, Verhoeven et al. (2001) identified a homozygous 3-bp
deletion, resulting in the absence of serine at position 171 of the
transaldolase protein (602063.0001).
*FIELD* RF
1. Verhoeven, N. M.; Huck, J. H. J.; Roos, B.; Struys, E. A.; Salomons,
G. S.; Douwes, A. C.; van der Knaap, M. S.; Jakobs, C.: Transaldolase
deficiency: liver cirrhosis associated with a new inborn error in
the pentose phosphate pathway. Am. J. Hum. Genet. 68: 1086-1092,
2001.
*FIELD* CD
Victor A. McKusick: 6/12/2001
*FIELD* ED
carol: 07/12/2010
terry: 2/19/2004
carol: 6/12/2001
*RECORD*
*FIELD* NO
606003
*FIELD* TI
#606003 TRANSALDOLASE DEFICIENCY
*FIELD* TX
A number sign (#) is used with this entry because transaldolase
read moredeficiency is caused by homozygous mutation in the TALDO1 gene (602063).
CLINICAL FEATURES
Verhoeven et al. (2001) described deficiency of transaldolase in the
first child of healthy, consanguineous Turkish parents. Soon after
birth, the patient had undergone surgical correction of aortic
coarctation. Within several months, she developed hepatosplenomegaly.
Elevated concentrations of ribitol, D-arabitol, and erythritol were
found in urine and plasma. At the age of 10 years, the patient showed
many telangiectases of the skin, hepatosplenomegaly, and enlarged
clitoris. She had persistent thrombocytopenia which was thought to be
caused by splenic pooling due to the hepatosplenomegaly. A deficiency of
transaldolase was discovered by incubating the patient's lymphoblasts
and erythrocytes with ribose-5-phosphate and subsequently analyzing
phosphate sugar metabolites.
MOLECULAR GENETICS
By sequence analysis of the TALDO1 gene in a patient with transaldolase
deficiency, Verhoeven et al. (2001) identified a homozygous 3-bp
deletion, resulting in the absence of serine at position 171 of the
transaldolase protein (602063.0001).
*FIELD* RF
1. Verhoeven, N. M.; Huck, J. H. J.; Roos, B.; Struys, E. A.; Salomons,
G. S.; Douwes, A. C.; van der Knaap, M. S.; Jakobs, C.: Transaldolase
deficiency: liver cirrhosis associated with a new inborn error in
the pentose phosphate pathway. Am. J. Hum. Genet. 68: 1086-1092,
2001.
*FIELD* CD
Victor A. McKusick: 6/12/2001
*FIELD* ED
carol: 07/12/2010
terry: 2/19/2004
carol: 6/12/2001