P29401 (TKT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transketolase
Short name=TK
EC=2.2.1.1

Gene names

Name:

TKT

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	623 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate.
Cofactor	Binds 1 calcium ion per subunit By similarity. Binds 1 thiamine pyrophosphate per subunit By similarity.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the transketolase family.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	Calcium Metal-binding Thiamine pyrophosphate
Molecular function	Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	energy reserve metabolic process Traceable author statement. Source: Reactome xylulose biosynthetic process Traceable author statement. Source: Reactome
Cellular component	cytosol Traceable author statement. Source: Reactome nucleus Inferred from direct assay. Source: HPA
Molecular function	transketolase activity Inferred from experiment. Source: Reactome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 623

623

Transketolase

PRO_0000191894

Sites

Metal binding

155

1

Calcium By similarity

Metal binding

185

1

Calcium By similarity

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.14 Ref.17

Modified residue

6

1

N6-acetyllysine Ref.17

Modified residue

11

1

N6-acetyllysine Ref.17

Modified residue

144

1

N6-acetyllysine Ref.17

Modified residue

204

1

N6-acetyllysine Ref.17

Modified residue

232

1

N6-acetyllysine Ref.11

Modified residue

241

1

N6-acetyllysine Ref.17

Modified residue

260

1

N6-acetyllysine Ref.17

Modified residue

275

1

Phosphotyrosine Ref.10 Ref.12 Ref.15 Ref.16

Modified residue

287

1

Phosphothreonine Ref.9 Ref.16

Modified residue

295

1

Phosphoserine Ref.13

Modified residue

314

1

N6-acetyllysine Ref.17

Modified residue

597

1

N6-acetyllysine Ref.17

Modified residue

603

1

N6-acetyllysine Ref.17

Natural variations

Natural variant

181

1

I → V.
Corresponds to variant rs17052920 [ dbSNP | Ensembl ].

VAR_052634

Experimental info

Sequence conflict

30 – 31

2

TT → SS in CAA47919. Ref.1

Sequence conflict

46

1

E → V in CAA47919. Ref.1

Sequence conflict

224 – 230

7

LCKAFGQ → AVQGLCE AA sequence Ref.8

Sequence conflict

426

1

P → A in CAA47919. Ref.1

Sequence conflict

585 – 587

3

THL → KTM in AAA61222. Ref.2

Sequence conflict

608 – 623

16

DRDAI…LITKA → TGMPLHKL AA sequence Ref.8

Secondary structure

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623

Helix Strand Turn

Details...

Helix

9 – 32

24

Helix

38 – 42

5

Helix

45 – 53

9

Beta strand

70 – 73

4

Helix

79 – 88

10

Helix

94 – 99

6

Beta strand

149 – 153

5

Helix

163 – 172

10

Beta strand

178 – 184

7

Turn

194 – 197

4

Helix

199 – 208

10

Beta strand

212 – 216

5

Helix

221 – 227

7

Beta strand

236 – 241

6

Helix

264 – 276

13

Helix

317 – 320

4

Helix

324 – 327

4

Beta strand

335 – 339

5

Helix

343 – 346

4

Helix

348 – 354

7

Helix

356 – 358

3

Beta strand

359 – 361

3

Helix

366 – 373

8

Helix

378 – 380

3

Beta strand

383 – 388

6

Helix

390 – 396

7

Helix

397 – 405

9

Beta strand

411 – 413

3

Helix

433 – 438

6

Beta strand

444 – 446

3

Helix

453 – 462

10

Beta strand

468 – 470

3

Beta strand

493 – 496

4

Beta strand

499 – 506

8

Helix

511 – 523

13

Turn

524 – 526

3

Beta strand

528 – 533

6

Beta strand

535 – 539

5

Helix

542 – 551

10

Beta strand

556 – 563

8

Helix

571 – 576

6

Beta strand

584 – 589

6

Helix

598 – 604

7

Helix

609 – 616

8

Sequences

	Sequence		Length	Mass (Da)
	P29401 [UniParc]. Last modified October 1, 1996. Version 3. Checksum: 176C89C02FD2712B	FASTA	623	67,878
	10 20 30 40 50 60 MESYHKPDQQ KLQALKDTAN RLRISSIQAT TAAGSGHPTS CCSAAEIMAV LFFHTMRYKS 70 80 90 100 110 120 QDPRNPHNDR FVLSKGHAAP ILYAVWAEAG FLAEAELLNL RKISSDLDGH PVPKQAFTDV 130 140 150 160 170 180 ATGSLGQGLG AACGMAYTGK YFDKASYRVY CLLGDGELSE GSVWEAMAFA SIYKLDNLVA 190 200 210 220 230 240 ILDINRLGQS DPAPLQHQMD IYQKRCEAFG WHAIIVDGHS VEELCKAFGQ AKHQPTAIIA 250 260 270 280 290 300 KTFKGRGITG VEDKESWHGK PLPKNMAEQI IQEIYSQIQS KKKILATPPQ EDAPSVDIAN 310 320 330 340 350 360 IRMPSLPSYK VGDKIATRKA YGQALAKLGH ASDRIIALDG DTKNSTFSEI FKKEHPDRFI 370 380 390 400 410 420 ECYIAEQNMV SIAVGCATRN RTVPFCSTFA AFFTRAFDQI RMAAISESNI NLCGSHCGVS 430 440 450 460 470 480 IGEDGPSQMA LEDLAMFRSV PTSTVFYPSD GVATEKAVEL AANTKGICFI RTSRPENAII 490 500 510 520 530 540 YNNNEDFQVG QAKVVLKSKD DQVTVIGAGV TLHEALAAAE LLKKEKINIR VLDPFTIKPL 550 560 570 580 590 600 DRKLILDSAR ATKGRILTVE DHYYEGGIGE AVSSAVVGEP GITVTHLAVN RVPRSGKPAE 610 620 LLKMFGIDRD AIAQAVRGLI TKA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of human transketolase cDNAs and comparison of the nucleotide sequence of the coding region in Wernicke-Korsakoff and non-Wernicke-Korsakoff individuals." McCool B.A., Plonk S.G., Martin P.R., Singleton C.K. J. Biol. Chem. 268:1397-1404(1993) [PubMed: 8419340] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Molecular cloning, sequence and chromosome localization of human transketolase." Jung E.-H., Sheu K.-F.R.E., Szabo P., Blass J.P. Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[3]	"Molecular evolutionary analysis of the thiamine-diphosphate-dependent enzyme, transketolase." Schenk G., Layfield R., Candy J.M., Duggleby R.G., Nixon P.F. J. Mol. Evol. 44:552-572(1997) [PubMed: 9115179] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[4]	"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].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: Brain, Kidney and Lymph.
[7]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-21. Tissue: Platelet.
[8]	"Nucleotide and predicted amino acid sequence of a cDNA clone encoding part of human transketolase." Abedinia M., Layfield R., Jones S.M., Nixon P.F., Mattick J.S. Biochem. Biophys. Res. Commun. 183:1159-1166(1992) [PubMed: 1567394] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 224-623, PARTIAL PROTEIN SEQUENCE. Tissue: Brain.
[9]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-275, MASS SPECTROMETRY.
[11]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-232, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-275, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[13]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[15]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-275, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[16]	"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 TYR-275 AND THR-287, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"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 MET-1; LYS-6; LYS-11; LYS-144; LYS-204; LYS-241; LYS-260; LYS-314; LYS-597 AND LYS-603, MASS SPECTROMETRY.
[18]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Web resources

Wikipedia

Transketolase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X67688 mRNA. Translation: CAA47919.1.
L12711 mRNA. Translation: AAA61222.1.
U55017 mRNA. Translation: AAA98961.1.
AK289454 mRNA. Translation: BAF82143.1.
CH471055 Genomic DNA. Translation: EAW65281.1.
BC008615 mRNA. Translation: AAH08615.1.
BC009970 mRNA. Translation: AAH09970.1.
BC024026 mRNA. Translation: AAH24026.2.

IPI

IPI00942979.

PIR

A45050.

RefSeq

NP_001055.1. NM_001064.3.
NP_001128527.1. NM_001135055.2.

UniGene

Hs.89643.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3MOS	X-ray	1.75	A	3-618	[»]
3OOY	X-ray	2.05	A/B	10-620	[»]

ProteinModelPortal

P29401.

SMR

P29401. Positions 3-618.

ModBase

Search...

Protein-protein interaction databases

IntAct

P29401. 8 interactions.

MINT

MINT-3011391.

STRING

P29401.

PTM databases

PhosphoSite

P29401.

Polymorphism databases

DMDM

1729976.

2D gel databases

REPRODUCTION-2DPAGE

IPI00643920.

Proteomic databases

PRIDE

P29401.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000423525; ENSP00000405455; ENSG00000163931.
ENST00000462138; ENSP00000417773; ENSG00000163931.

GeneID

7086.

KEGG

hsa:7086.

NMPDR

fig|9606.3.peg.22691.

UCSC

uc003dgo.1. human.

Organism-specific databases

CTD

7086.

GeneCards

GC03M053233.

H-InvDB

HIX0003374.

HGNC

HGNC:11834. TKT.

HPA

HPA029480.
HPA029481.

MIM

606781. gene.

neXtProt

NX_P29401.

PharmGKB

PA36537.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG06936.

HOVERGEN

HBG004036.

InParanoid

P29401.

OrthoDB

EOG4R23TG.

PhylomeDB

P29401.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.
REACT_474. Metabolism of carbohydrates.

Gene expression databases

ArrayExpress

P29401.

Bgee

P29401.

CleanEx

HS_TKT.

Genevestigator

P29401.

GermOnline

ENSG00000163931. Homo sapiens.

Family and domain databases

InterPro

IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR015941. Transketolase-like_C.
IPR005475. Transketolase-like_Pyr-bd.
IPR020826. Transketolase_BS.
IPR005476. Transketolase_C.
IPR005474. Transketolase_N.
[Graphical view]

Gene3D

G3DSA:3.40.50.920. Transketo_C_like. 1 hit.

KO

K00615.

Pfam

PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
PF00456. Transketolase_N. 1 hit.
[Graphical view]

SMART

SM00861. Transket_pyr. 1 hit.
[Graphical view]

SUPFAM

SSF52922. Transketo_C_like. 1 hit.

PROSITE

PS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00152. Thiamine.

NextBio

27715.

SOURCE

Search...

Entry information

Entry name

TKT_HUMAN

Accession

Primary (citable) accession number: P29401
Secondary accession number(s): A8K089, Q8TBA3, Q96HH3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 127 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.