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P37837

- TALDO_HUMAN

UniProt

P37837 - TALDO_HUMAN

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Protein
Transaldolase
Gene
TALDO1, TAL, TALDO, TALDOR
Organism
Homo sapiens (Human)
Status
Reviewed - 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.UniRule annotation

Catalytic activityi

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

Pathwayi

Sites

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

GO - Molecular functioni

  1. monosaccharide binding Source: Ensembl
  2. sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity Source: ProtInc

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. energy reserve metabolic process Source: Reactome
  3. fructose 6-phosphate metabolic process Source: Ensembl
  4. glyceraldehyde-3-phosphate metabolic process Source: Ensembl
  5. pentose-phosphate shunt Source: Reactome
  6. pentose-phosphate shunt, non-oxidative branch Source: Ensembl
  7. small molecule metabolic process Source: Reactome
  8. xylulose biosynthetic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Pentose shunt

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

ReactomeiREACT_1859. Pentose phosphate pathway (hexose monophosphate shunt).
REACT_939. Insulin effects increased synthesis of Xylulose-5-Phosphate.
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
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:11559. TALDO1.

Subcellular locationi

Cytoplasm Inferred UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
  4. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

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.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti171 – 1711Missing in TALDO1 deficiency. 1 Publication
VAR_011511

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi606003. phenotype.
Orphaneti101028. Transaldolase deficiency.
PharmGKBiPA36328.

Protein family/group databases

Allergomei9551. Hom s Transaldolase.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 337337TransaldolaseUniRule annotation
PRO_0000173564Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei115 – 1151N6-acetyllysine By similarity
Modified residuei219 – 2191N6-acetyllysine1 Publication
Modified residuei269 – 2691N6-acetyllysine1 Publication
Modified residuei286 – 2861N6-acetyllysine1 Publication
Modified residuei321 – 3211N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP37837.
PaxDbiP37837.
PeptideAtlasiP37837.
PRIDEiP37837.

2D gel databases

OGPiP37837.
REPRODUCTION-2DPAGEIPI00744692.

PTM databases

PhosphoSiteiP37837.

Expressioni

Gene expression databases

ArrayExpressiP37837.
BgeeiP37837.
CleanExiHS_TALDO1.
GenevestigatoriP37837.

Organism-specific databases

HPAiHPA040373.
HPA048089.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi112751. 27 interactions.
IntActiP37837. 4 interactions.
MINTiMINT-4999914.
STRINGi9606.ENSP00000321259.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F05X-ray2.45A/B1-337[»]
ProteinModelPortaliP37837.
SMRiP37837. Positions 11-332.

Miscellaneous databases

EvolutionaryTraceiP37837.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0176.
HOGENOMiHOG000281234.
HOVERGENiHBG054014.
InParanoidiP37837.
KOiK00616.
OMAiEAKFRWA.
OrthoDBiEOG7MD4QF.
PhylomeDBiP37837.
TreeFamiTF300757.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00492. Transaldolase_1.
InterProiIPR013785. Aldolase_TIM.
IPR001585. Transaldolase.
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

MSSSPVKRQR MESALDQLKQ FTTVVADTGD FHAIDEYKPQ DATTNPSLIL    50
AAAQMPAYQE LVEEAIAYGR KLGGSQEDQI KNAIDKLFVL FGAEILKKIP 100
GRVSTEVDAR LSFDKDAMVA RARRLIELYK EAGISKDRIL IKLSSTWEGI 150
QAGKELEEQH GIHCNMTLLF SFAQAVACAE AGVTLISPFV GRILDWHVAN 200
TDKKSYEPLE DPGVKSVTKI YNYYKKFSYK TIVMGASFRN TGEIKALAGC 250
DFLTISPKLL GELLQDNAKL VPVLSAKAAQ ASDLEKIHLD EKSFRWLHNE 300
DQMAVEKLSD GIRKFAADAV KLERMLTERM FNAENGK 337
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 TALDO1 deficiency. 1 Publication
VAR_011511

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.3. human.

Polymorphism databases

DMDMi6648092.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS7712.1.
PIRi A49985.
RefSeqi NP_006746.1. NM_006755.1.
UniGenei Hs.438678.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1F05 X-ray 2.45 A/B 1-337 [» ]
ProteinModelPortali P37837.
SMRi P37837. Positions 11-332.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112751. 27 interactions.
IntActi P37837. 4 interactions.
MINTi MINT-4999914.
STRINGi 9606.ENSP00000321259.

Protein family/group databases

Allergomei 9551. Hom s Transaldolase.

PTM databases

PhosphoSitei P37837.

Polymorphism databases

DMDMi 6648092.

2D gel databases

OGPi P37837.
REPRODUCTION-2DPAGE IPI00744692.

Proteomic databases

MaxQBi P37837.
PaxDbi P37837.
PeptideAtlasi P37837.
PRIDEi P37837.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000319006 ; ENSP00000321259 ; ENSG00000177156 .
GeneIDi 6888.
KEGGi hsa:6888.
UCSCi uc001lqz.3. human.

Organism-specific databases

CTDi 6888.
GeneCardsi GC11P000737.
HGNCi HGNC:11559. TALDO1.
HPAi HPA040373.
HPA048089.
MIMi 602063. gene.
606003. phenotype.
neXtProti NX_P37837.
Orphaneti 101028. Transaldolase deficiency.
PharmGKBi PA36328.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0176.
HOGENOMi HOG000281234.
HOVERGENi HBG054014.
InParanoidi P37837.
KOi K00616.
OMAi EAKFRWA.
OrthoDBi EOG7MD4QF.
PhylomeDBi P37837.
TreeFami TF300757.

Enzyme and pathway databases

UniPathwayi UPA00115 ; UER00414 .
Reactomei REACT_1859. Pentose phosphate pathway (hexose monophosphate shunt).
REACT_939. Insulin effects increased synthesis of Xylulose-5-Phosphate.

Miscellaneous databases

ChiTaRSi TALDO1. human.
EvolutionaryTracei P37837.
GenomeRNAii 6888.
NextBioi 26917.
PROi P37837.
SOURCEi Search...

Gene expression databases

ArrayExpressi P37837.
Bgeei P37837.
CleanExi HS_TALDO1.
Genevestigatori P37837.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_00492. Transaldolase_1.
InterProi IPR013785. Aldolase_TIM.
IPR001585. Transaldolase.
IPR004730. Transaldolase_1.
IPR018225. Transaldolase_AS.
[Graphical view ]
PANTHERi PTHR10683. PTHR10683. 1 hit.
Pfami PF00923. Transaldolase. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00874. talAB. 1 hit.
PROSITEi PS01054. TRANSALDOLASE_1. 1 hit.
PS00958. TRANSALDOLASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "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. 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.

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: September 3, 2014
This is version 159 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

External Data

Dasty 3

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