Transaldolase 1

Protein-coding gene in the species Homo sapiens
TALDO1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1F05

Identifiers
AliasesTALDO1, TAL, TAL-H, TALDOR, TALH, transaldolase 1
External IDsOMIM: 602063; MGI: 1274789; HomoloGene: 4916; GeneCards: TALDO1; OMA:TALDO1 - orthologs
Gene location (Human)
Chromosome 11 (human)
Chr.Chromosome 11 (human)[1]
Chromosome 11 (human)
Genomic location for TALDO1
Genomic location for TALDO1
Band11p15.5Start747,415 bp[1]
End765,012 bp[1]
Gene location (Mouse)
Chromosome 7 (mouse)
Chr.Chromosome 7 (mouse)[2]
Chromosome 7 (mouse)
Genomic location for TALDO1
Genomic location for TALDO1
Band7|7 F5Start140,972,112 bp[2]
End140,982,881 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • trabecular bone

  • blood

  • gingival epithelium

  • oocyte

  • monocyte

  • bone marrow

  • oral cavity

  • palpebral conjunctiva

  • secondary oocyte

  • granulocyte
Top expressed in
  • granulocyte

  • lacrimal gland

  • blood

  • brown adipose tissue

  • endothelial cell of lymphatic vessel

  • conjunctival fornix

  • retinal pigment epithelium

  • tunica adventitia of aorta

  • fetal liver hematopoietic progenitor cell

  • parotid gland
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • transferase activity
  • transaldolase activity
  • catalytic activity
  • protein binding
  • monosaccharide binding
  • carbohydrate binding
Cellular component
  • cytoplasm
  • cytosol
  • extracellular exosome
  • intracellular membrane-bounded organelle
  • nucleus
  • nucleoplasm
Biological process
  • fructose 6-phosphate metabolic process
  • pentose-phosphate shunt
  • pentose-phosphate shunt, non-oxidative branch
  • xylulose biosynthetic process
  • glyceraldehyde-3-phosphate metabolic process
  • interleukin-12-mediated signaling pathway
  • carbohydrate metabolic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

6888

21351

Ensembl

ENSG00000177156

ENSMUSG00000025503

UniProt

P37837

Q93092

RefSeq (mRNA)

NM_006755

NM_011528

RefSeq (protein)

NP_006746

NP_035658

Location (UCSC)Chr 11: 0.75 – 0.77 MbChr 7: 140.97 – 140.98 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Transaldolase 1 is a protein that in humans is encoded by the TALDO1 gene. [5]

Function

Transaldolase 1 is a key enzyme of the nonoxidative pentose phosphate pathway providing ribose-5-phosphate for nucleic acid synthesis and NADPH for lipid biosynthesis. This pathway can also maintain glutathione at a reduced state and thus protect sulfhydryl groups and cellular integrity from oxygen radicals. The functional gene of transaldolase 1 is located on chromosome 11 and a pseudogene is identified on chromosome 1 but there are conflicting map locations. The second and third exon of this gene were developed by insertion of a retrotransposable element. This gene is thought to be involved in multiple sclerosis. [provided by RefSeq, Jul 2008].

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000177156 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000025503 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ "Entrez Gene: Transaldolase 1". Retrieved 2017-10-19.

Further reading

  • Grossman CE, Qian Y, Banki K, Perl A (2004). "ZNF143 mediates basal and tissue-specific expression of human transaldolase". J. Biol. Chem. 279 (13): 12190–205. doi:10.1074/jbc.M307039200. PMID 14702349.
  • Huang JB, Espinoza J, Romero R, Petty HR (2005). "Transaldolase is part of a supramolecular complex containing glucose-6-phosphate dehydrogenase in human neutrophils that undergoes retrograde trafficking during pregnancy". Metab. Clin. Exp. 54 (8): 1027–33. doi:10.1016/j.metabol.2005.03.005. PMID 16092052.
  • Valayannopoulos V, Verhoeven NM, Mention K, Salomons GS, Sommelet D, Gonzales M, Touati G, de Lonlay P, Jakobs C, Saudubray JM (2006). "Transaldolase deficiency: a new cause of hydrops fetalis and neonatal multi-organ disease". J. Pediatr. 149 (5): 713–7. doi:10.1016/j.jpeds.2006.08.016. PMID 17095351.
  • Silberstein M, Landon MR, Wang YE, Perl A, Vajda S (2006). "Computational methods for functional site identification suggest a substrate access channel in transaldolase". Genome Inform. 17 (1): 13–22. PMID 17503352.
  • Wamelink MM, Smith DE, Jansen EE, Verhoeven NM, Struys EA, Jakobs C (2007). "Detection of transaldolase deficiency by quantification of novel seven-carbon chain carbohydrate biomarkers in urine". J. Inherit. Metab. Dis. 30 (5): 735–42. doi:10.1007/s10545-007-0590-2. PMID 17603756. S2CID 22549126.
  • Wamelink MM, Struys EA, Salomons GS, Fowler D, Jakobs C, Clayton PT (2008). "Transaldolase deficiency in a two-year-old boy with cirrhosis". Mol. Genet. Metab. 94 (2): 255–8. doi:10.1016/j.ymgme.2008.01.011. PMID 18331807.
  • Qian Y, Banerjee S, Grossman CE, Amidon W, Nagy G, Barcza M, Niland B, Karp DR, Middleton FA, Banki K, Perl A (2008). "Transaldolase deficiency influences the pentose phosphate pathway, mitochondrial homoeostasis and apoptosis signal processing". Biochem. J. 415 (1): 123–34. doi:10.1042/BJ20080722. PMID 18498245.
  • Schneider S, Sandalova T, Schneider G, Sprenger GA, Samland AK (2008). "Replacement of a phenylalanine by a tyrosine in the active site confers fructose-6-phosphate aldolase activity to the transaldolase of Escherichia coli and human origin". J. Biol. Chem. 283 (44): 30064–72. doi:10.1074/jbc.M803184200. PMC 2662071. PMID 18687684.
  • Basta PV, Bensen JT, Tse CK, Perou CM, Sullivan PF, Olshan AF (2008). "Genetic variation in Transaldolase 1 and risk of squamous cell carcinoma of the head and neck". Cancer Detect. Prev. 32 (3): 200–8. doi:10.1016/j.cdp.2008.08.008. PMC 2614275. PMID 18805652.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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