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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

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

General annotation (Comments)

Function	Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
Catalytic activity	Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate.
Cofactor	Binds 1 magnesium ion per subunit. Can also utilize other divalent metal cations, such as Ca2+, Mn2+ and Co2+. Ref.10 Binds 1 thiamine pyrophosphate per subunit. Ref.10
Subunit structure	Homodimer.
Sequence similarities	Belongs to the transketolase family.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Calcium Magnesium 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 glyceraldehyde-3-phosphate biosynthetic process Inferred from direct assay PubMed 9611778. Source: UniProtKB pentose-phosphate shunt, non-oxidative branch Non-traceable author statement PubMed 9357955. Source: UniProtKB regulation of growth Inferred from electronic annotation. Source: Compara xylulose biosynthetic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleus Inferred from direct assay. Source: HPA peroxisome Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	cofactor binding Inferred from direct assay Ref.17PubMed 9611778. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein homodimerization activity Inferred from direct assay Ref.17PubMed 9357955. Source: UniProtKB transketolase activity Inferred from direct assay Ref.17Ref.1PubMed 9357955PubMed 9611778. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P29401-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P29401-2)

The sequence of this isoform differs from the canonical sequence as follows:
     146-146: S → SLPSSWDYS

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 623

623

Transketolase

PRO_0000191894

Regions

Nucleotide binding

123 – 125

3

Thiamine pyrophosphate

Sites

Active site

366

1

Proton donor By similarity

Metal binding

155

1

Magnesium

Metal binding

185

1

Magnesium

Metal binding

187

1

Magnesium; via carbonyl oxygen

Binding site

37

1

Substrate By similarity

Binding site

40

1

Thiamine pyrophosphate

Binding site

77

1

Thiamine pyrophosphate

Binding site

156

1

Thiamine pyrophosphate; via amide nitrogen

Binding site

185

1

Thiamine pyrophosphate

Binding site

244

1

Thiamine pyrophosphate

Binding site

258

1

Substrate By similarity

Binding site

258

1

Thiamine pyrophosphate

Binding site

318

1

Substrate By similarity

Binding site

345

1

Substrate By similarity

Binding site

392

1

Thiamine pyrophosphate

Binding site

416

1

Substrate By similarity

Binding site

424

1

Substrate By similarity

Binding site

428

1

Thiamine pyrophosphate

Binding site

474

1

Substrate By similarity

Site

37

1

Important for catalytic activity By similarity

Site

258

1

Important for catalytic activity By similarity

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.14

Modified residue

6

1

N6-acetyllysine Ref.14

Modified residue

11

1

N6-acetyllysine Ref.14

Modified residue

144

1

N6-acetyllysine Ref.14

Modified residue

204

1

N6-acetyllysine Ref.14

Modified residue

241

1

N6-acetyllysine Ref.14

Modified residue

260

1

N6-acetyllysine Ref.14

Modified residue

275

1

Phosphotyrosine Ref.13 Ref.15

Modified residue

287

1

Phosphothreonine Ref.13 Ref.15

Modified residue

295

1

Phosphoserine Ref.12 Ref.15

Modified residue

603

1

N6-acetyllysine Ref.14

Natural variations

Alternative sequence

146

1

S → SLPSSWDYS in isoform 2.

VSP_045566

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.9

Sequence conflict

366

1

E → G in BAG56942. Ref.4

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.9

Secondary structure

1

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623

Helix Strand Turn

Details...

Helix

9 – 33

25

Helix

38 – 42

5

Helix

45 – 53

9

Beta strand

70 – 75

6

Helix

76 – 78

3

Helix

79 – 88

10

Helix

94 – 99

6

Helix

128 – 141

14

Beta strand

149 – 154

6

Helix

156 – 159

4

Helix

161 – 172

12

Beta strand

178 – 184

7

Beta strand

189 – 192

4

Turn

194 – 197

4

Helix

199 – 208

10

Beta strand

212 – 217

6

Helix

221 – 229

9

Beta strand

236 – 241

6

Turn

244 – 247

4

Turn

249 – 253

5

Helix

264 – 276

13

Beta strand

314 – 316

3

Helix

317 – 331

15

Beta strand

335 – 341

7

Helix

343 – 346

4

Helix

348 – 354

7

Helix

356 – 358

3

Beta strand

359 – 361

3

Helix

366 – 377

12

Helix

378 – 380

3

Beta strand

383 – 389

7

Helix

390 – 396

7

Helix

397 – 405

9

Beta strand

410 – 418

9

Helix

419 – 421

3

Helix

426 – 428

3

Beta strand

430 – 432

3

Helix

433 – 438

6

Beta strand

443 – 446

4

Helix

451 – 462

12

Beta strand

466 – 471

6

Beta strand

474 – 478

5

Beta strand

493 – 496

4

Beta strand

499 – 506

8

Helix

510 – 523

14

Turn

524 – 526

3

Beta strand

528 – 533

6

Beta strand

535 – 539

5

Helix

542 – 551

10

Turn

552 – 554

3

Beta strand

555 – 564

10

Helix

568 – 576

9

Beta strand

583 – 589

7

Helix

598 – 604

7

Helix

609 – 616

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [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
	Isoform 2 [UniParc]. Checksum: E64388EFD41AB530	FASTA	631	68,814
	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 YFDKASLPSS WDYSYRVYCL LGDGELSEGS VWEAMAFASI 190 200 210 220 230 240 YKLDNLVAIL DINRLGQSDP APLQHQMDIY QKRCEAFGWH AIIVDGHSVE ELCKAFGQAK 250 260 270 280 290 300 HQPTAIIAKT FKGRGITGVE DKESWHGKPL PKNMAEQIIQ EIYSQIQSKK KILATPPQED 310 320 330 340 350 360 APSVDIANIR MPSLPSYKVG DKIATRKAYG QALAKLGHAS DRIIALDGDT KNSTFSEIFK 370 380 390 400 410 420 KEHPDRFIEC YIAEQNMVSI AVGCATRNRT VPFCSTFAAF FTRAFDQIRM AAISESNINL 430 440 450 460 470 480 CGSHCGVSIG EDGPSQMALE DLAMFRSVPT STVFYPSDGV ATEKAVELAA NTKGICFIRT 490 500 510 520 530 540 SRPENAIIYN NNEDFQVGQA KVVLKSKDDQ VTVIGAGVTL HEALAAAELL KKEKINIRVL 550 560 570 580 590 600 DPFTIKPLDR KLILDSARAT KGRILTVEDH YYEGGIGEAV SSAVVGEPGI TVTHLAVNRV 610 620 630 PRSGKPAELL KMFGIDRDAI AQAVRGLITK A

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). 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] (ISOFORM 1). 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
[5]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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].
[7]	"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] (ISOFORM 1). Tissue: Brain, Kidney and Lymph.
[8]	"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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-21. Tissue: Platelet.
[9]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 224-623 (ISOFORM 1), PARTIAL PROTEIN SEQUENCE. Tissue: Brain.
[10]	"Studies on the nature of thiamine pyrophosphate binding and dependency on divalent cations of transketolase from human erythrocytes." Jung E.H., Takeuchi T., Nishino K., Itokawa Y. Int. J. Biochem. 20:1255-1259(1988) [PubMed] [Europe PMC] [Abstract] Cited for: COFACTOR.
[11]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-275 AND THR-287, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"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 MET-1; LYS-6; LYS-11; LYS-144; LYS-204; LYS-241; LYS-260 AND LYS-603, MASS SPECTROMETRY.
[15]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-275; THR-287 AND SER-295, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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].
[17]	"The crystal structure of human transketolase and new insights into its mode of action." Mitschke L., Parthier C., Schroder-Tittmann K., Coy J., Ludtke S., Tittmann K. J. Biol. Chem. 285:31559-31570(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 3-620 IN COMPLEXES WITH CALCIUM AND THIAMINE PYROPHOSPHATE.
+	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.
AK293438 mRNA. Translation: BAG56942.1.
AC097015 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW65281.1.
BC008615 mRNA. Translation: AAH08615.1.
BC009970 mRNA. Translation: AAH09970.1.
BC024026 mRNA. Translation: AAH24026.2.

IPI

IPI00643920.
IPI00942979.

PIR

A45050.

RefSeq

NP_001055.1. NM_001064.3.
NP_001128527.1. NM_001135055.2.
NP_001244957.1. NM_001258028.1.

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.

ModBase

Search...

Protein-protein interaction databases

IntAct

P29401. 10 interactions.

MINT

MINT-3011391.

STRING

9606.ENSP00000405455.

PTM databases

PhosphoSite

P29401.

Polymorphism databases

DMDM

1729976.

2D gel databases

REPRODUCTION-2DPAGE

IPI00643920.

Proteomic databases

PaxDb

P29401.

PRIDE

P29401.

Protocols and materials databases

DNASU

7086.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000423516; ENSP00000391481; ENSG00000163931.
ENST00000423525; ENSP00000405455; ENSG00000163931.
ENST00000462138; ENSP00000417773; ENSG00000163931.

GeneID

7086.

KEGG

hsa:7086.

UCSC

uc003dgo.3. human.

Organism-specific databases

CTD

7086.

GeneCards

GC03M053233.

HGNC

HGNC:11834. TKT.

HPA

HPA029480.
HPA029481.

MIM

606781. gene.

neXtProt

NX_P29401.

PharmGKB

PA36537.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0021.

HOGENOM

HOG000243868.

HOVERGEN

HBG004036.

InParanoid

P29401.

KO

K00615.

OrthoDB

EOG4R23TG.

PhylomeDB

P29401.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

SABIO-RK

P29401.

Gene expression databases

ArrayExpress

P29401.

Bgee

P29401.

CleanEx

HS_TKT.

Genevestigator

P29401.

GermOnline

ENSG00000163931. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.920. 1 hit.

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]

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

BindingDB

P29401.

ChEMBL

CHEMBL4983.

ChiTaRS

TKT. human.

DrugBank

DB00152. Thiamine.

EvolutionaryTrace

P29401.

GenomeRNAi

7086.

NextBio

27715.

SOURCE

Search...

Entry information

Entry name

TKT_HUMAN

Accession

Primary (citable) accession number: P29401
Secondary accession number(s): A8K089 , B4DE31, E7EPA7, Q8TBA3, Q96HH3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 141 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.