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Protein

Transaldolase

Gene

TALDO1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Pathwayi: pentose phosphate pathway

This protein is involved in step 2 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage).
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Transaldolase (TALDO1), Transaldolase (TALDO1)
  3. no protein annotated in this organism
This subpathway is part of the pathway pentose phosphate pathway, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage), the pathway pentose phosphate pathway and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei142 – 1421Schiff-base intermediate with substrate1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Pentose shunt

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

ReactomeiR-HSA-163754. Insulin effects increased synthesis of Xylulose-5-Phosphate.
R-HSA-6791055. TALDO1 deficiency: failed conversion of SH7P, GA3P to Fru(6)P, E4P.
R-HSA-6791462. TALDO1 deficiency: failed conversion of Fru(6)P, E4P to SH7P, GA3P.
R-HSA-71336. Pentose phosphate pathway (hexose monophosphate shunt).
UniPathwayiUPA00115; UER00414.

Names & Taxonomyi

Protein namesi
Recommended name:
Transaldolase (EC:2.2.1.2)
Gene namesi
Name:TALDO1
Synonyms:TAL, TALDO, TALDOR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:11559. TALDO1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Transaldolase deficiency (TALDOD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn inborn error of the pentose phosphate pathway resulting in early-onset multisystem disease. Clinical features include growth retardation, dysmorphic features, cutis laxa, congenital heart disease, hepatosplenomegaly, telangiectases of the skin, pancytopenia, and bleeding tendency.
See also OMIM:606003
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti171 – 1711Missing in TALDOD. 1 Publication
VAR_011511

Keywords - Diseasei

Disease mutation

Organism-specific databases

MalaCardsiTALDO1.
MIMi606003. phenotype.
Orphaneti101028. Transaldolase deficiency.
PharmGKBiPA36328.

Protein family/group databases

Allergomei9551. Hom s Transaldolase.

Polymorphism and mutation databases

BioMutaiTALDO1.
DMDMi6648092.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 337337TransaldolasePRO_0000173564Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei115 – 1151N6-acetyllysineBy similarity
Modified residuei219 – 2191N6-acetyllysineCombined sources
Modified residuei237 – 2371PhosphoserineCombined sources
Modified residuei269 – 2691N6-acetyllysineCombined sources
Modified residuei286 – 2861N6-acetyllysineCombined sources
Modified residuei321 – 3211N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP37837.
MaxQBiP37837.
PaxDbiP37837.
PeptideAtlasiP37837.
PRIDEiP37837.
TopDownProteomicsiP37837.

2D gel databases

OGPiP37837.
REPRODUCTION-2DPAGEIPI00744692.

PTM databases

iPTMnetiP37837.
PhosphoSiteiP37837.
SwissPalmiP37837.

Expressioni

Gene expression databases

BgeeiP37837.
CleanExiHS_TALDO1.
ExpressionAtlasiP37837. baseline and differential.
GenevisibleiP37837. HS.

Organism-specific databases

HPAiHPA040373.
HPA048089.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
TERF2IPQ9NYB02EBI-1056712,EBI-750109

Protein-protein interaction databases

BioGridi112751. 73 interactions.
IntActiP37837. 10 interactions.
MINTiMINT-4999914.
STRINGi9606.ENSP00000321259.

Structurei

Secondary structure

1
337
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 218Combined sources
Beta strandi22 – 276Combined sources
Turni31 – 344Combined sources
Helixi35 – 373Combined sources
Beta strandi40 – 434Combined sources
Helixi46 – 538Combined sources
Helixi56 – 583Combined sources
Helixi59 – 7214Combined sources
Helixi76 – 9823Combined sources
Beta strandi103 – 1064Combined sources
Helixi109 – 1113Combined sources
Helixi115 – 13117Combined sources
Helixi136 – 1383Combined sources
Beta strandi139 – 1446Combined sources
Helixi147 – 16014Combined sources
Beta strandi164 – 1696Combined sources
Helixi172 – 1809Combined sources
Beta strandi184 – 1907Combined sources
Helixi191 – 20010Combined sources
Helixi208 – 2103Combined sources
Helixi212 – 22615Combined sources
Beta strandi232 – 2365Combined sources
Helixi241 – 2455Combined sources
Turni246 – 2494Combined sources
Beta strandi250 – 2556Combined sources
Helixi257 – 2659Combined sources
Helixi276 – 2816Combined sources
Helixi291 – 2999Combined sources
Helixi302 – 33029Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F05X-ray2.45A/B1-337[»]
ProteinModelPortaliP37837.
SMRiP37837. Positions 11-332.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37837.

Family & Domainsi

Sequence similaritiesi

Belongs to the transaldolase family. Type 1 subfamily.Curated

Phylogenomic databases

eggNOGiKOG2772. Eukaryota.
COG0176. LUCA.
GeneTreeiENSGT00390000017361.
HOGENOMiHOG000281234.
HOVERGENiHBG054014.
InParanoidiP37837.
KOiK00616.
OMAiNAIDEYK.
OrthoDBiEOG7MD4QF.
PhylomeDBiP37837.
TreeFamiTF300757.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00492. Transaldolase_1.
InterProiIPR013785. Aldolase_TIM.
IPR001585. TAL/FSA.
IPR004730. Transaldolase_1.
IPR018225. Transaldolase_AS.
[Graphical view]
PANTHERiPTHR10683. PTHR10683. 1 hit.
PfamiPF00923. Transaldolase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00874. talAB. 1 hit.
PROSITEiPS01054. TRANSALDOLASE_1. 1 hit.
PS00958. TRANSALDOLASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P37837-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSPVKRQR MESALDQLKQ FTTVVADTGD FHAIDEYKPQ DATTNPSLIL
60 70 80 90 100
AAAQMPAYQE LVEEAIAYGR KLGGSQEDQI KNAIDKLFVL FGAEILKKIP
110 120 130 140 150
GRVSTEVDAR LSFDKDAMVA RARRLIELYK EAGISKDRIL IKLSSTWEGI
160 170 180 190 200
QAGKELEEQH GIHCNMTLLF SFAQAVACAE AGVTLISPFV GRILDWHVAN
210 220 230 240 250
TDKKSYEPLE DPGVKSVTKI YNYYKKFSYK TIVMGASFRN TGEIKALAGC
260 270 280 290 300
DFLTISPKLL GELLQDNAKL VPVLSAKAAQ ASDLEKIHLD EKSFRWLHNE
310 320 330
DQMAVEKLSD GIRKFAADAV KLERMLTERM FNAENGK
Length:337
Mass (Da):37,540
Last modified:May 30, 2000 - v2
Checksum:i8CB4992AEF364E64
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti171 – 1711Missing in TALDOD. 1 Publication
VAR_011511

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS7712.1.
PIRiA49985.
RefSeqiNP_006746.1. NM_006755.1.
UniGeneiHs.438678.

Genome annotation databases

EnsembliENST00000319006; ENSP00000321259; ENSG00000177156.
GeneIDi6888.
KEGGihsa:6888.
UCSCiuc001lqz.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS7712.1.
PIRiA49985.
RefSeqiNP_006746.1. NM_006755.1.
UniGeneiHs.438678.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F05X-ray2.45A/B1-337[»]
ProteinModelPortaliP37837.
SMRiP37837. Positions 11-332.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112751. 73 interactions.
IntActiP37837. 10 interactions.
MINTiMINT-4999914.
STRINGi9606.ENSP00000321259.

Protein family/group databases

Allergomei9551. Hom s Transaldolase.

PTM databases

iPTMnetiP37837.
PhosphoSiteiP37837.
SwissPalmiP37837.

Polymorphism and mutation databases

BioMutaiTALDO1.
DMDMi6648092.

2D gel databases

OGPiP37837.
REPRODUCTION-2DPAGEIPI00744692.

Proteomic databases

EPDiP37837.
MaxQBiP37837.
PaxDbiP37837.
PeptideAtlasiP37837.
PRIDEiP37837.
TopDownProteomicsiP37837.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000319006; ENSP00000321259; ENSG00000177156.
GeneIDi6888.
KEGGihsa:6888.
UCSCiuc001lqz.4. human.

Organism-specific databases

CTDi6888.
GeneCardsiTALDO1.
HGNCiHGNC:11559. TALDO1.
HPAiHPA040373.
HPA048089.
MalaCardsiTALDO1.
MIMi602063. gene.
606003. phenotype.
neXtProtiNX_P37837.
Orphaneti101028. Transaldolase deficiency.
PharmGKBiPA36328.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2772. Eukaryota.
COG0176. LUCA.
GeneTreeiENSGT00390000017361.
HOGENOMiHOG000281234.
HOVERGENiHBG054014.
InParanoidiP37837.
KOiK00616.
OMAiNAIDEYK.
OrthoDBiEOG7MD4QF.
PhylomeDBiP37837.
TreeFamiTF300757.

Enzyme and pathway databases

UniPathwayiUPA00115; UER00414.
ReactomeiR-HSA-163754. Insulin effects increased synthesis of Xylulose-5-Phosphate.
R-HSA-6791055. TALDO1 deficiency: failed conversion of SH7P, GA3P to Fru(6)P, E4P.
R-HSA-6791462. TALDO1 deficiency: failed conversion of Fru(6)P, E4P to SH7P, GA3P.
R-HSA-71336. Pentose phosphate pathway (hexose monophosphate shunt).

Miscellaneous databases

ChiTaRSiTALDO1. human.
EvolutionaryTraceiP37837.
GenomeRNAii6888.
NextBioi26917.
PROiP37837.
SOURCEiSearch...

Gene expression databases

BgeeiP37837.
CleanExiHS_TALDO1.
ExpressionAtlasiP37837. baseline and differential.
GenevisibleiP37837. HS.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00492. Transaldolase_1.
InterProiIPR013785. Aldolase_TIM.
IPR001585. TAL/FSA.
IPR004730. Transaldolase_1.
IPR018225. Transaldolase_AS.
[Graphical view]
PANTHERiPTHR10683. PTHR10683. 1 hit.
PfamiPF00923. Transaldolase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00874. talAB. 1 hit.
PROSITEiPS01054. TRANSALDOLASE_1. 1 hit.
PS00958. TRANSALDOLASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. "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].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  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 TALDOD SER-171 DEL.

Entry informationi

Entry nameiTALDO_HUMAN
AccessioniPrimary (citable) accession number: P37837
Secondary accession number(s): B2R8M2
, O00751, Q8WV32, Q8WZ45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: May 30, 2000
Last modified: May 11, 2016
This is version 178 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.