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P29401 (TKT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transketolase

Short name=TK
EC=2.2.1.1
Gene names
Name:TKT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length623 AA.
Sequence statusComplete.
Protein existenceEvidence 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 diversityAlternative splicing
Polymorphism
   LigandCalcium
Magnesium
Metal-binding
Thiamine pyrophosphate
   Molecular functionTransferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

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

Traceable author statement. Source: Reactome

pentose-phosphate shunt, non-oxidative branch

Non-traceable author statement PubMed 9357955. Source: UniProtKB

regulation of growth

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

xylulose biosynthetic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337PubMed 23376485. Source: UniProt

nucleus

Inferred from direct assay. Source: HPA

peroxisome

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioncofactor binding

Inferred from direct assay Ref.18PubMed 9611778. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein homodimerization activity

Inferred from direct assay Ref.18PubMed 9357955. Source: UniProtKB

transketolase activity

Inferred from direct assay Ref.18Ref.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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 623623Transketolase
PRO_0000191894

Regions

Nucleotide binding123 – 1253Thiamine pyrophosphate

Sites

Active site3661Proton donor By similarity
Metal binding1551Magnesium
Metal binding1851Magnesium
Metal binding1871Magnesium; via carbonyl oxygen
Binding site371Substrate By similarity
Binding site401Thiamine pyrophosphate
Binding site771Thiamine pyrophosphate
Binding site1561Thiamine pyrophosphate; via amide nitrogen
Binding site1851Thiamine pyrophosphate
Binding site2441Thiamine pyrophosphate
Binding site2581Substrate By similarity
Binding site2581Thiamine pyrophosphate
Binding site3181Substrate By similarity
Binding site3451Substrate By similarity
Binding site3921Thiamine pyrophosphate
Binding site4161Substrate By similarity
Binding site4241Substrate By similarity
Binding site4281Thiamine pyrophosphate
Binding site4741Substrate By similarity
Site371Important for catalytic activity By similarity
Site2581Important for catalytic activity By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.14 Ref.17
Modified residue61N6-acetyllysine Ref.14
Modified residue111N6-acetyllysine Ref.14
Modified residue1441N6-acetyllysine Ref.14
Modified residue2041N6-acetyllysine Ref.14
Modified residue2321N6-acetyllysine By similarity
Modified residue2411N6-acetyllysine Ref.14
Modified residue2601N6-acetyllysine Ref.14
Modified residue2751Phosphotyrosine Ref.13 Ref.15
Modified residue2871Phosphothreonine Ref.13 Ref.15
Modified residue2951Phosphoserine Ref.12 Ref.15
Modified residue5381N6-acetyllysine By similarity
Modified residue6031N6-acetyllysine Ref.14

Natural variations

Alternative sequence1461S → SLPSSWDYS in isoform 2.
VSP_045566
Natural variant1811I → V.
Corresponds to variant rs17052920 [ dbSNP | Ensembl ].
VAR_052634

Experimental info

Sequence conflict30 – 312TT → SS in CAA47919. Ref.1
Sequence conflict461E → V in CAA47919. Ref.1
Sequence conflict224 – 2307LCKAFGQ → AVQGLCE AA sequence Ref.9
Sequence conflict3661E → G in BAG56942. Ref.4
Sequence conflict4261P → A in CAA47919. Ref.1
Sequence conflict585 – 5873THL → KTM in AAA61222. Ref.2
Sequence conflict608 – 62316DRDAI…LITKA → TGMPLHKL AA sequence Ref.9

Secondary structure

.................................................................................................. 623
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1996. Version 3.
Checksum: 176C89C02FD2712B

FASTA62367,878
        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 

« Hide

Isoform 2 [UniParc].

Checksum: E64388EFD41AB530
Show »

FASTA63168,814

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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.
CCDSCCDS2871.1. [P29401-1]
CCDS58834.1. [P29401-2]
PIRA45050.
RefSeqNP_001055.1. NM_001064.3. [P29401-1]
NP_001128527.1. NM_001135055.2. [P29401-1]
NP_001244957.1. NM_001258028.1. [P29401-2]
UniGeneHs.89643.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3MOSX-ray1.75A3-618[»]
3OOYX-ray2.05A/B10-620[»]
4KXUX-ray0.98A1-623[»]
4KXVX-ray0.97A1-623[»]
4KXWX-ray0.97A1-623[»]
4KXXX-ray1.03A1-623[»]
4KXYX-ray1.26A/B1-623[»]
ProteinModelPortalP29401.
SMRP29401. Positions 2-622.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112941. 31 interactions.
IntActP29401. 11 interactions.
MINTMINT-3011391.
STRING9606.ENSP00000405455.

Chemistry

BindingDBP29401.
ChEMBLCHEMBL4983.
DrugBankDB00152. Thiamine.

PTM databases

PhosphoSiteP29401.

Polymorphism databases

DMDM1729976.

2D gel databases

REPRODUCTION-2DPAGEIPI00643920.

Proteomic databases

MaxQBP29401.
PaxDbP29401.
PRIDEP29401.

Protocols and materials databases

DNASU7086.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000423516; ENSP00000391481; ENSG00000163931. [P29401-2]
ENST00000423525; ENSP00000405455; ENSG00000163931. [P29401-1]
ENST00000462138; ENSP00000417773; ENSG00000163931. [P29401-1]
ENST00000608398; ENSP00000476754; ENSG00000272687. [P29401-1]
ENST00000609357; ENSP00000476696; ENSG00000272687. [P29401-2]
ENST00000609496; ENSP00000476998; ENSG00000272687. [P29401-1]
GeneID7086.
KEGGhsa:7086.
UCSCuc003dgo.3. human. [P29401-1]

Organism-specific databases

CTD7086.
GeneCardsGC03M053258.
HGNCHGNC:11834. TKT.
HPAHPA029480.
HPA029481.
MIM606781. gene.
neXtProtNX_P29401.
PharmGKBPA36537.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0021.
HOGENOMHOG000243868.
HOVERGENHBG004036.
InParanoidP29401.
KOK00615.
OMAPPNYKVG.
OrthoDBEOG72RMXF.
PhylomeDBP29401.
TreeFamTF313097.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKP29401.

Gene expression databases

ArrayExpressP29401.
BgeeP29401.
CleanExHS_TKT.
GenevestigatorP29401.

Family and domain databases

Gene3D3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
InterProIPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR020826. Transketolase_BS.
IPR005476. Transketolase_C.
IPR005474. Transketolase_N.
[Graphical view]
PfamPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
PF00456. Transketolase_N. 1 hit.
[Graphical view]
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMSSF52518. SSF52518. 2 hits.
SSF52922. SSF52922. 1 hit.
PROSITEPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTKT. human.
EvolutionaryTraceP29401.
GenomeRNAi7086.
NextBio27715.
PROP29401.
SOURCESearch...

Entry information

Entry nameTKT_HUMAN
AccessionPrimary (citable) accession number: P29401
Secondary accession number(s): A8K089 expand/collapse secondary AC list , B4DE31, E7EPA7, Q8TBA3, Q96HH3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 155 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM