P37837 (TALDO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transaldolase
EC=2.2.1.2

Gene names

Name:	TALDO1
Synonyms:	TAL, TALDO, TALDOR

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	337 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Catalytic activity	Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate.
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.
Subcellular location	Cytoplasm Probable.
Involvement in disease	Defects in TALDO1 are the cause of transaldolase 1 deficiency (TALDO1 deficiency) [MIM:606003]. It results in telangiectases of the skin, hepatosplenomegaly, and enlarged clitoris.
Sequence similarities	Belongs to the transaldolase family. Type 1 subfamily.

Ontologies

Keywords
Biological process	Pentose shunt
Cellular component	Cytoplasm
Disease	Disease mutation
Molecular function	Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Molecular function	protein binding Inferred from physical interaction. Source: IntAct transaldolase activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NAA38	O95777	1	EBI-1056712,EBI-347779

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 337

337

Transaldolase

PRO_0000173564

Sites

Active site

142

1

By similarity

Amino acid modifications

Modified residue

4

1

Phosphoserine Ref.7

Modified residue

219

1

N6-acetyllysine Ref.10

Modified residue

237

1

Phosphoserine Ref.9

Modified residue

269

1

N6-acetyllysine Ref.10

Modified residue

286

1

N6-acetyllysine Ref.10

Modified residue

321

1

N6-acetyllysine Ref.10

Natural variations

Natural variant

171

1

Missing in TALDO1 deficiency.

VAR_011511

Secondary structure

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337

Helix Strand Turn

Details...

Helix

14 – 21

8

Beta strand

22 – 27

6

Turn

31 – 34

4

Helix

35 – 37

3

Beta strand

40 – 43

4

Helix

46 – 53

8

Helix

56 – 58

3

Helix

59 – 72

14

Helix

76 – 98

23

Beta strand

103 – 106

4

Helix

109 – 111

3

Helix

115 – 131

17

Helix

136 – 138

3

Beta strand

139 – 144

6

Helix

147 – 160

14

Beta strand

164 – 169

6

Helix

172 – 180

9

Beta strand

184 – 190

7

Helix

191 – 200

10

Helix

208 – 210

3

Helix

212 – 226

15

Beta strand

232 – 236

5

Helix

241 – 245

5

Turn

246 – 249

4

Beta strand

250 – 255

6

Helix

257 – 265

9

Helix

276 – 281

6

Helix

291 – 299

9

Helix

302 – 330

29

Sequences

	Sequence		Length	Mass (Da)
	P37837-1 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 8CB4992AEF364E64	FASTA	337	37,540
	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

References

	« Hide 'large scale' referencesShow '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: 8300619] [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: 9339383] [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: 9524206] [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: 10702296] [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: 14702039] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung and Ovary.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-219; LYS-269; LYS-286 AND LYS-321, MASS SPECTROMETRY.
[11]	"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: 11283793] [Abstract] Cited for: VARIANT TALDO1 DEFICIENCY SER-171 DEL.
+	Additional computationally mapped references.

Web resources

GeneReviews

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.

IPI

IPI00744692.

PIR

A49985.

RefSeq

NP_006746.1.

UniGene

Hs.438678.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F05	X-ray	2.45	A/B	1-337	[»]

ProteinModelPortal

P37837.

ModBase

Search...

Protein-protein interaction databases

IntAct

P37837. 9 interactions.

MINT

MINT-4999914.

STRING

P37837.

PTM databases

PhosphoSite

P37837.

2-D gel databases

OGP

P37837.

REPRODUCTION-2DPAGE

IPI00744692.

Proteomic databases

PeptideAtlas

P37837.

PRIDE

P37837.

Genome annotation databases

Ensembl

ENST00000319006; ENSP00000321259; ENSG00000177156; Homo sapiens. [Genome view]

GeneID

6888.

KEGG

hsa:6888.

UCSC

uc001lqz.1. human.

Organism-specific databases

CTD

6888.

GeneCards

GC11P000737.

H-InvDB

HIX0019993.

HGNC

HGNC:11559. TALDO1.

MIM

602063. gene.
606003. phenotype.

Orphanet

101028. Transaldolase deficiency.

PharmGKB

PA36328.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG06896.

HOGENOM

HBG286747.

HOVERGEN

HBG054014.

InParanoid

P37837.

OMA

DTGDFHA.

OrthoDB

EOG9CJZ3C.

PhylomeDB

P37837.

Enzyme and pathway databases

BRENDA

2.2.1.2. 247.

Reactome

REACT_1505. Integration of energy metabolism.
REACT_474. Metabolism of carbohydrates.

Gene expression databases

ArrayExpress

P37837.

Bgee

P37837.

CleanEx

HS_TALDO1.

Genevestigator

P37837.

GermOnline

ENSG00000177156. Homo sapiens.

Family and domain databases

InterPro

IPR013785. Aldolase_TIM.
IPR001585. Transaldolase.
IPR004730. Transaldolase_AB.
IPR018225. Transaldolase_AS.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

PANTHER

PTHR10683. Transaldolase. 1 hit.
PTHR10683:SF3. Transaldolase_AB. 1 hit.

Pfam

PF00923. Transaldolase. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00874. talAB. 1 hit.

PROSITE

PS01054. TRANSALDOLASE_1. 1 hit.
PS00958. TRANSALDOLASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

26917.

SOURCE

Search...

Entry information

Entry name

TALDO_HUMAN

Accession

Primary (citable) accession number: P37837
Secondary accession number(s): B2R8M2, O00751, Q8WV32

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	May 30, 2000
Last modified:	August 10, 2010
This is version 121 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.