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P37837 (TALDO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transaldolase

EC=2.2.1.2
Gene names
Name:TALDO1
Synonyms:TAL, TALDO, TALDOR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. HAMAP-Rule MF_00492

Catalytic activity

Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. HAMAP-Rule MF_00492

Pathway

Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3. HAMAP-Rule MF_00492

Subunit structure

Homodimer. Ref.11

Subcellular location

Cytoplasm Probable HAMAP-Rule MF_00492.

Involvement in disease

Transaldolase 1 deficiency (TALDO1 deficiency) [MIM:606003]: Results in telangiectases of the skin, hepatosplenomegaly, and enlarged clitoris.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Sequence similarities

Belongs to the transaldolase family. Type 1 subfamily.

Ontologies

Keywords
   Biological processPentose shunt
   Cellular componentCytoplasm
   DiseaseDisease mutation
   LigandSchiff base
   Molecular functionTransferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

energy reserve metabolic process

Traceable author statement. Source: Reactome

fructose 6-phosphate metabolic process

Inferred from electronic annotation. Source: Ensembl

glyceraldehyde-3-phosphate metabolic process

Inferred from electronic annotation. Source: Ensembl

pentose-phosphate shunt

Traceable author statement. Source: Reactome

pentose-phosphate shunt, non-oxidative branch

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

xylulose biosynthetic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Traceable author statement PubMed 16130169. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337PubMed 23376485. Source: UniProt

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

   Molecular_functionmonosaccharide binding

Inferred from electronic annotation. Source: Ensembl

sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity

Traceable author statement Ref.3. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 337337Transaldolase HAMAP-Rule MF_00492
PRO_0000173564

Sites

Active site1421Schiff-base intermediate with substrate Ref.11

Amino acid modifications

Modified residue1151N6-acetyllysine By similarity
Modified residue2191N6-acetyllysine Ref.9
Modified residue2691N6-acetyllysine Ref.9
Modified residue2861N6-acetyllysine Ref.9
Modified residue3211N6-acetyllysine Ref.9

Natural variations

Natural variant1711Missing in TALDO1 deficiency. Ref.12
VAR_011511

Secondary structure

.................................................... 337
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P37837 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 8CB4992AEF364E64

FASTA33737,540
        10         20         30         40         50         60 
MSSSPVKRQR MESALDQLKQ FTTVVADTGD FHAIDEYKPQ DATTNPSLIL AAAQMPAYQE 

        70         80         90        100        110        120 
LVEEAIAYGR KLGGSQEDQI KNAIDKLFVL FGAEILKKIP GRVSTEVDAR LSFDKDAMVA 

       130        140        150        160        170        180 
RARRLIELYK EAGISKDRIL IKLSSTWEGI QAGKELEEQH GIHCNMTLLF SFAQAVACAE 

       190        200        210        220        230        240 
AGVTLISPFV GRILDWHVAN TDKKSYEPLE DPGVKSVTKI YNYYKKFSYK TIVMGASFRN 

       250        260        270        280        290        300 
TGEIKALAGC DFLTISPKLL GELLQDNAKL VPVLSAKAAQ ASDLEKIHLD EKSFRWLHNE 

       310        320        330 
DQMAVEKLSD GIRKFAADAV KLERMLTERM FNAENGK 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of the human gene for transaldolase. A novel highly repetitive element constitutes an integral part of the coding sequence."
Banki K., Halladay D.L., Perl A.
J. Biol. Chem. 269:2847-2851(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The human transaldolase gene (TALDO1) is located on chromosome 11 at p15.4-p15.5."
Banki K., Eddy R.L., Shows T.B., Halladay D.L., Bullrich F., Croce C.M., Jurecic V., Baldini A., Perl A.
Genomics 45:233-238(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[3]"Cloning and chromosomal localization of a paralog and a mouse homolog of the human transaldolase gene."
Kusuda J., Hirai M., Toyoda A., Tanuma R., Nomura-Kitabayashi A., Hashimoto K.
Gene 209:13-21(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Human transaldolase-associated repetitive elements are transcribed by RNA polymerase III."
Perl A., Colombo E., Samoilova E., Butler M.C., Banki K.
J. Biol. Chem. 275:7261-7272(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Cerebellum.
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung and Ovary.
[7]"Family of active retrotransposons carry two exons of the transaldolase gene and shows evidence of reverse splicing in human DNA."
Perl A.
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-110.
[8]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-219; LYS-269; LYS-286 AND LYS-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"The three-dimensional structure of human transaldolase."
Thorell S., Gergely P. Jr., Banki K., Perl A., Schneider G.
FEBS Lett. 475:205-208(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS), SUBUNIT, ACTIVE SITE.
[12]"Transaldolase deficiency: liver cirrhosis associated with a new inborn error in the pentose phosphate pathway."
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.
Am. J. Hum. Genet. 68:1086-1092(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TALDO1 DEFICIENCY SER-171 DEL.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L19437 mRNA. Translation: AAB53943.1.
AF010400, AF010398, AF010399 Genomic DNA. Translation: AAC52068.1.
AF058913 Genomic DNA. Translation: AAF40478.1.
AK313427 mRNA. Translation: BAG36219.1.
BC010103 mRNA. Translation: AAH10103.1.
BC018847 mRNA. Translation: AAH18847.2.
L27346 Genomic DNA. Translation: AAL31313.1.
CCDSCCDS7712.1.
PIRA49985.
RefSeqNP_006746.1. NM_006755.1.
UniGeneHs.438678.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F05X-ray2.45A/B1-337[»]
ProteinModelPortalP37837.
SMRP37837. Positions 11-332.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112751. 26 interactions.
IntActP37837. 4 interactions.
MINTMINT-4999914.
STRING9606.ENSP00000321259.

Protein family/group databases

Allergome9551. Hom s Transaldolase.

PTM databases

PhosphoSiteP37837.

Polymorphism databases

DMDM6648092.

2D gel databases

OGPP37837.
REPRODUCTION-2DPAGEIPI00744692.

Proteomic databases

MaxQBP37837.
PaxDbP37837.
PeptideAtlasP37837.
PRIDEP37837.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000319006; ENSP00000321259; ENSG00000177156.
GeneID6888.
KEGGhsa:6888.
UCSCuc001lqz.3. human.

Organism-specific databases

CTD6888.
GeneCardsGC11P000737.
HGNCHGNC:11559. TALDO1.
HPAHPA040373.
HPA048089.
MIM602063. gene.
606003. phenotype.
neXtProtNX_P37837.
Orphanet101028. Transaldolase deficiency.
PharmGKBPA36328.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0176.
HOGENOMHOG000281234.
HOVERGENHBG054014.
InParanoidP37837.
KOK00616.
OMAEAKFRWA.
OrthoDBEOG7MD4QF.
PhylomeDBP37837.
TreeFamTF300757.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
UniPathwayUPA00115; UER00414.

Gene expression databases

ArrayExpressP37837.
BgeeP37837.
CleanExHS_TALDO1.
GenevestigatorP37837.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00492. Transaldolase_1.
InterProIPR013785. Aldolase_TIM.
IPR001585. Transaldolase.
IPR004730. Transaldolase_1.
IPR018225. Transaldolase_AS.
[Graphical view]
PANTHERPTHR10683. PTHR10683. 1 hit.
PfamPF00923. Transaldolase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00874. talAB. 1 hit.
PROSITEPS01054. TRANSALDOLASE_1. 1 hit.
PS00958. TRANSALDOLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTALDO1. human.
EvolutionaryTraceP37837.
GenomeRNAi6888.
NextBio26917.
PROP37837.
SOURCESearch...

Entry information

Entry nameTALDO_HUMAN
AccessionPrimary (citable) accession number: P37837
Secondary accession number(s): B2R8M2 expand/collapse secondary AC list , O00751, Q8WV32, Q8WZ45
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: May 30, 2000
Last modified: July 9, 2014
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM