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Protein

Transketolase

Gene

TKT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate.

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei37SubstrateBy similarity1
Sitei37Important for catalytic activityBy similarity1
Binding sitei40Thiamine pyrophosphate1
Binding sitei77Thiamine pyrophosphate1
Metal bindingi155Magnesium1
Binding sitei156Thiamine pyrophosphate; via amide nitrogen1
Metal bindingi185Magnesium1
Binding sitei185Thiamine pyrophosphate1
Metal bindingi187Magnesium; via carbonyl oxygen1
Binding sitei244Thiamine pyrophosphate1
Binding sitei258SubstrateBy similarity1
Binding sitei258Thiamine pyrophosphate1
Sitei258Important for catalytic activityBy similarity1
Binding sitei318SubstrateBy similarity1
Binding sitei345SubstrateBy similarity1
Active sitei366Proton donorBy similarity1
Binding sitei392Thiamine pyrophosphate1
Binding sitei416SubstrateBy similarity1
Binding sitei424SubstrateBy similarity1
Binding sitei428Thiamine pyrophosphate1
Binding sitei474SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi123 – 125Thiamine pyrophosphate3

GO - Molecular functioni

  • cofactor binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • protein homodimerization activity Source: UniProtKB
  • transketolase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Calcium, Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciZFISH:HS08968-MONOMER.
BRENDAi2.2.1.1. 2681.
ReactomeiR-HSA-163754. Insulin effects increased synthesis of Xylulose-5-Phosphate.
R-HSA-71336. Pentose phosphate pathway (hexose monophosphate shunt).
SABIO-RKP29401.

Names & Taxonomyi

Protein namesi
Recommended name:
Transketolase (EC:2.2.1.1)
Short name:
TK
Gene namesi
Name:TKT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:11834. TKT.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • myelin sheath Source: Ensembl
  • nucleoplasm Source: HPA
  • nucleus Source: HPA
  • peroxisome Source: UniProtKB
  • vesicle Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

DisGeNETi7086.
MalaCardsiTKT.
OpenTargetsiENSG00000163931.
PharmGKBiPA36537.

Chemistry databases

ChEMBLiCHEMBL4983.

Polymorphism and mutation databases

BioMutaiTKT.
DMDMi1729976.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001918941 – 623TransketolaseAdd BLAST623

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei3PhosphoserineCombined sources1
Modified residuei6N6-acetyllysineCombined sources1
Modified residuei11N6-acetyllysineCombined sources1
Modified residuei104PhosphoserineCombined sources1
Modified residuei144N6-acetyllysineCombined sources1
Modified residuei204N6-acetyllysineCombined sources1
Modified residuei232N6-acetyllysineBy similarity1
Modified residuei241N6-acetyllysineCombined sources1
Modified residuei260N6-acetyllysineCombined sources1
Modified residuei275PhosphotyrosineCombined sources1
Modified residuei287PhosphothreonineCombined sources1
Modified residuei295PhosphoserineCombined sources1
Modified residuei345PhosphoserineBy similarity1
Modified residuei538N6-acetyllysineBy similarity1
Modified residuei603N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP29401.
PaxDbiP29401.
PeptideAtlasiP29401.
PRIDEiP29401.
TopDownProteomicsiP29401-1. [P29401-1]

2D gel databases

REPRODUCTION-2DPAGEIPI00643920.

PTM databases

iPTMnetiP29401.
PhosphoSitePlusiP29401.
SwissPalmiP29401.

Expressioni

Gene expression databases

BgeeiENSG00000163931.
CleanExiHS_TKT.
ExpressionAtlasiP29401. baseline and differential.
GenevisibleiP29401. HS.

Organism-specific databases

HPAiHPA029480.
HPA029481.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
TERF1P542742EBI-1050560,EBI-710997

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi112941. 164 interactors.
IntActiP29401. 17 interactors.
MINTiMINT-3011391.
STRINGi9606.ENSP00000405455.

Chemistry databases

BindingDBiP29401.

Structurei

Secondary structure

1623
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 33Combined sources25
Helixi38 – 42Combined sources5
Helixi45 – 53Combined sources9
Beta strandi70 – 75Combined sources6
Helixi76 – 78Combined sources3
Helixi79 – 88Combined sources10
Helixi94 – 99Combined sources6
Helixi128 – 141Combined sources14
Beta strandi149 – 155Combined sources7
Helixi156 – 159Combined sources4
Helixi161 – 172Combined sources12
Beta strandi178 – 184Combined sources7
Beta strandi189 – 192Combined sources4
Turni194 – 197Combined sources4
Helixi199 – 208Combined sources10
Beta strandi212 – 217Combined sources6
Helixi221 – 229Combined sources9
Beta strandi236 – 241Combined sources6
Turni244 – 247Combined sources4
Turni249 – 253Combined sources5
Helixi264 – 275Combined sources12
Beta strandi314 – 316Combined sources3
Helixi317 – 331Combined sources15
Beta strandi335 – 341Combined sources7
Helixi343 – 346Combined sources4
Helixi349 – 354Combined sources6
Helixi356 – 358Combined sources3
Beta strandi359 – 361Combined sources3
Helixi366 – 377Combined sources12
Helixi378 – 380Combined sources3
Beta strandi383 – 389Combined sources7
Helixi390 – 396Combined sources7
Helixi397 – 405Combined sources9
Beta strandi410 – 418Combined sources9
Helixi419 – 421Combined sources3
Helixi426 – 428Combined sources3
Beta strandi430 – 432Combined sources3
Helixi433 – 438Combined sources6
Beta strandi443 – 446Combined sources4
Helixi451 – 462Combined sources12
Beta strandi466 – 471Combined sources6
Beta strandi474 – 478Combined sources5
Beta strandi493 – 496Combined sources4
Beta strandi501 – 506Combined sources6
Helixi510 – 523Combined sources14
Turni524 – 526Combined sources3
Beta strandi528 – 533Combined sources6
Beta strandi535 – 539Combined sources5
Helixi542 – 551Combined sources10
Turni552 – 554Combined sources3
Beta strandi555 – 564Combined sources10
Helixi568 – 576Combined sources9
Beta strandi583 – 589Combined sources7
Helixi598 – 604Combined sources7
Helixi609 – 620Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP29401.
SMRiP29401.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29401.

Family & Domainsi

Sequence similaritiesi

Belongs to the transketolase family.Curated

Phylogenomic databases

eggNOGiKOG0523. Eukaryota.
COG0021. LUCA.
GeneTreeiENSGT00390000005240.
HOGENOMiHOG000243868.
HOVERGENiHBG004036.
InParanoidiP29401.
KOiK00615.
OMAiKAFGQAR.
OrthoDBiEOG091G03M5.
PhylomeDBiP29401.
TreeFamiTF313097.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR029061. THDP-binding.
IPR009014. Transketo_C/PFOR_II.
IPR005475. Transketolase-like_Pyr-bd.
IPR020826. Transketolase_BS.
IPR033248. Transketolase_C.
IPR033247. Transketolase_fam.
IPR005474. Transketolase_N.
[Graphical view]
PANTHERiPTHR11624. PTHR11624. 1 hit.
PfamiPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
PF00456. Transketolase_N. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
SSF52922. SSF52922. 1 hit.
PROSITEiPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P29401-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MESYHKPDQQ KLQALKDTAN RLRISSIQAT TAAGSGHPTS CCSAAEIMAV
60 70 80 90 100
LFFHTMRYKS QDPRNPHNDR FVLSKGHAAP ILYAVWAEAG FLAEAELLNL
110 120 130 140 150
RKISSDLDGH PVPKQAFTDV ATGSLGQGLG AACGMAYTGK YFDKASYRVY
160 170 180 190 200
CLLGDGELSE GSVWEAMAFA SIYKLDNLVA ILDINRLGQS DPAPLQHQMD
210 220 230 240 250
IYQKRCEAFG WHAIIVDGHS VEELCKAFGQ AKHQPTAIIA KTFKGRGITG
260 270 280 290 300
VEDKESWHGK PLPKNMAEQI IQEIYSQIQS KKKILATPPQ EDAPSVDIAN
310 320 330 340 350
IRMPSLPSYK VGDKIATRKA YGQALAKLGH ASDRIIALDG DTKNSTFSEI
360 370 380 390 400
FKKEHPDRFI ECYIAEQNMV SIAVGCATRN RTVPFCSTFA AFFTRAFDQI
410 420 430 440 450
RMAAISESNI NLCGSHCGVS IGEDGPSQMA LEDLAMFRSV PTSTVFYPSD
460 470 480 490 500
GVATEKAVEL AANTKGICFI RTSRPENAII YNNNEDFQVG QAKVVLKSKD
510 520 530 540 550
DQVTVIGAGV TLHEALAAAE LLKKEKINIR VLDPFTIKPL DRKLILDSAR
560 570 580 590 600
ATKGRILTVE DHYYEGGIGE AVSSAVVGEP GITVTHLAVN RVPRSGKPAE
610 620
LLKMFGIDRD AIAQAVRGLI TKA
Length:623
Mass (Da):67,878
Last modified:October 1, 1996 - v3
Checksum:i176C89C02FD2712B
GO
Isoform 2 (identifier: P29401-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:631
Mass (Da):68,814
Checksum:iE64388EFD41AB530
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti30 – 31TT → SS in CAA47919 (PubMed:8419340).Curated2
Sequence conflicti46E → V in CAA47919 (PubMed:8419340).Curated1
Sequence conflicti224 – 230LCKAFGQ → AVQGLCE AA sequence (PubMed:1567394).Curated7
Sequence conflicti366E → G in BAG56942 (PubMed:14702039).Curated1
Sequence conflicti426P → A in CAA47919 (PubMed:8419340).Curated1
Sequence conflicti585 – 587THL → KTM in AAA61222 (Ref. 2) Curated3
Sequence conflicti608 – 623DRDAI…LITKA → TGMPLHKL AA sequence (PubMed:1567394).CuratedAdd BLAST16

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_052634181I → V.Corresponds to variant rs17052920dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_045566146S → SLPSSWDYS in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2871.1. [P29401-1]
CCDS58834.1. [P29401-2]
PIRiA45050.
RefSeqiNP_001055.1. NM_001064.3. [P29401-1]
NP_001128527.1. NM_001135055.2. [P29401-1]
NP_001244957.1. NM_001258028.1. [P29401-2]
XP_011532356.1. XM_011534054.1. [P29401-2]
UniGeneiHs.89643.

Genome annotation databases

EnsembliENST00000423516; ENSP00000391481; ENSG00000163931. [P29401-2]
ENST00000423525; ENSP00000405455; ENSG00000163931. [P29401-1]
ENST00000462138; ENSP00000417773; ENSG00000163931. [P29401-1]
GeneIDi7086.
KEGGihsa:7086.
UCSCiuc011beq.4. human. [P29401-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Transketolase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2871.1. [P29401-1]
CCDS58834.1. [P29401-2]
PIRiA45050.
RefSeqiNP_001055.1. NM_001064.3. [P29401-1]
NP_001128527.1. NM_001135055.2. [P29401-1]
NP_001244957.1. NM_001258028.1. [P29401-2]
XP_011532356.1. XM_011534054.1. [P29401-2]
UniGeneiHs.89643.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP29401.
SMRiP29401.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112941. 164 interactors.
IntActiP29401. 17 interactors.
MINTiMINT-3011391.
STRINGi9606.ENSP00000405455.

Chemistry databases

BindingDBiP29401.
ChEMBLiCHEMBL4983.

PTM databases

iPTMnetiP29401.
PhosphoSitePlusiP29401.
SwissPalmiP29401.

Polymorphism and mutation databases

BioMutaiTKT.
DMDMi1729976.

2D gel databases

REPRODUCTION-2DPAGEIPI00643920.

Proteomic databases

EPDiP29401.
PaxDbiP29401.
PeptideAtlasiP29401.
PRIDEiP29401.
TopDownProteomicsiP29401-1. [P29401-1]

Protocols and materials databases

DNASUi7086.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000423516; ENSP00000391481; ENSG00000163931. [P29401-2]
ENST00000423525; ENSP00000405455; ENSG00000163931. [P29401-1]
ENST00000462138; ENSP00000417773; ENSG00000163931. [P29401-1]
GeneIDi7086.
KEGGihsa:7086.
UCSCiuc011beq.4. human. [P29401-1]

Organism-specific databases

CTDi7086.
DisGeNETi7086.
GeneCardsiTKT.
HGNCiHGNC:11834. TKT.
HPAiHPA029480.
HPA029481.
MalaCardsiTKT.
MIMi606781. gene.
neXtProtiNX_P29401.
OpenTargetsiENSG00000163931.
PharmGKBiPA36537.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0523. Eukaryota.
COG0021. LUCA.
GeneTreeiENSGT00390000005240.
HOGENOMiHOG000243868.
HOVERGENiHBG004036.
InParanoidiP29401.
KOiK00615.
OMAiKAFGQAR.
OrthoDBiEOG091G03M5.
PhylomeDBiP29401.
TreeFamiTF313097.

Enzyme and pathway databases

BioCyciZFISH:HS08968-MONOMER.
BRENDAi2.2.1.1. 2681.
ReactomeiR-HSA-163754. Insulin effects increased synthesis of Xylulose-5-Phosphate.
R-HSA-71336. Pentose phosphate pathway (hexose monophosphate shunt).
SABIO-RKP29401.

Miscellaneous databases

ChiTaRSiTKT. human.
EvolutionaryTraceiP29401.
GenomeRNAii7086.
PROiP29401.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000163931.
CleanExiHS_TKT.
ExpressionAtlasiP29401. baseline and differential.
GenevisibleiP29401. HS.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR029061. THDP-binding.
IPR009014. Transketo_C/PFOR_II.
IPR005475. Transketolase-like_Pyr-bd.
IPR020826. Transketolase_BS.
IPR033248. Transketolase_C.
IPR033247. Transketolase_fam.
IPR005474. Transketolase_N.
[Graphical view]
PANTHERiPTHR11624. PTHR11624. 1 hit.
PfamiPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
PF00456. Transketolase_N. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
SSF52922. SSF52922. 1 hit.
PROSITEiPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTKT_HUMAN
AccessioniPrimary (citable) accession number: P29401
Secondary accession number(s): A8K089
, B4DE31, E7EPA7, Q8TBA3, Q96HH3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 180 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.