Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Transketolase

Gene

Tkt

Organism
Mus musculus (Mouse)
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.By similarity

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Mg2+By similarity, Ca2+By similarity, Mn2+By similarity, Co2+By similarityNote: Binds 1 Mg2+ ion per subunit. Can also utilize other divalent metal cations, such as Ca2+, Mn2+ and Co2+.By similarity
  • thiamine diphosphateBy similarityNote: Binds 1 thiamine pyrophosphate per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei37 – 371SubstrateBy similarity
Sitei37 – 371Important for catalytic activityBy similarity
Binding sitei40 – 401Thiamine pyrophosphateBy similarity
Binding sitei77 – 771Thiamine pyrophosphateBy similarity
Metal bindingi155 – 1551MagnesiumBy similarity
Binding sitei156 – 1561Thiamine pyrophosphate; via amide nitrogenBy similarity
Metal bindingi185 – 1851MagnesiumBy similarity
Binding sitei185 – 1851Thiamine pyrophosphateBy similarity
Metal bindingi187 – 1871Magnesium; via carbonyl oxygenBy similarity
Binding sitei244 – 2441Thiamine pyrophosphateBy similarity
Binding sitei258 – 2581SubstrateBy similarity
Binding sitei258 – 2581Thiamine pyrophosphateBy similarity
Sitei258 – 2581Important for catalytic activityBy similarity
Binding sitei318 – 3181SubstrateBy similarity
Binding sitei345 – 3451SubstrateBy similarity
Active sitei366 – 3661Proton donorBy similarity
Binding sitei392 – 3921Thiamine pyrophosphateBy similarity
Binding sitei416 – 4161SubstrateBy similarity
Binding sitei424 – 4241SubstrateBy similarity
Binding sitei428 – 4281Thiamine pyrophosphateBy similarity
Binding sitei474 – 4741SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi123 – 1253Thiamine pyrophosphateBy similarity

GO - Molecular functioni

GO - Biological processi

  • glyceraldehyde-3-phosphate biosynthetic process Source: MGI
  • regulation of growth Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Calcium, Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BRENDAi2.2.1.1. 3474.
ReactomeiR-MMU-163754. Insulin effects increased synthesis of Xylulose-5-Phosphate.
R-MMU-71336. Pentose phosphate pathway (hexose monophosphate shunt).

Names & Taxonomyi

Protein namesi
Recommended name:
Transketolase (EC:2.2.1.1)
Short name:
TK
Alternative name(s):
P68
Gene namesi
Name:Tkt
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:105992. Tkt.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • myelin sheath Source: UniProtKB
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • vesicle Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 623623TransketolasePRO_0000191896Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei6 – 61N6-acetyllysineCombined sources
Modified residuei11 – 111N6-acetyllysineBy similarity
Modified residuei104 – 1041PhosphoserineBy similarity
Modified residuei144 – 1441N6-acetyllysineBy similarity
Modified residuei204 – 2041N6-acetyllysineBy similarity
Modified residuei232 – 2321N6-acetyllysineCombined sources
Modified residuei241 – 2411N6-acetyllysineBy similarity
Modified residuei260 – 2601N6-acetyllysineBy similarity
Modified residuei275 – 2751PhosphotyrosineCombined sources
Modified residuei287 – 2871PhosphothreonineCombined sources
Modified residuei295 – 2951PhosphoserineBy similarity
Modified residuei345 – 3451PhosphoserineBy similarity
Modified residuei538 – 5381N6-acetyllysineCombined sources
Modified residuei603 – 6031N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP40142.
MaxQBiP40142.
PaxDbiP40142.
PeptideAtlasiP40142.
PRIDEiP40142.

2D gel databases

REPRODUCTION-2DPAGEP40142.
SWISS-2DPAGEP40142.

PTM databases

iPTMnetiP40142.
PhosphoSiteiP40142.
SwissPalmiP40142.

Expressioni

Gene expression databases

BgeeiP40142.
CleanExiMM_TKT.
ExpressionAtlasiP40142. baseline and differential.
GenevisibleiP40142. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204213. 1 interaction.
IntActiP40142. 13 interactions.
MINTiMINT-1855010.
STRINGi10090.ENSMUSP00000022529.

Structurei

3D structure databases

ProteinModelPortaliP40142.
SMRiP40142. Positions 4-618.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the transketolase family.Curated

Phylogenomic databases

eggNOGiKOG0523. Eukaryota.
COG0021. LUCA.
GeneTreeiENSGT00390000005240.
HOGENOMiHOG000243868.
HOVERGENiHBG004036.
InParanoidiP40142.
KOiK00615.
OMAiKAFGQAR.
OrthoDBiEOG72RMXF.
PhylomeDBiP40142.
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]

Sequencei

Sequence statusi: Complete.

P40142-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGYHKPDQQ KLQALKDTAN RLRISSIQAT TAAGSGHPTS CCSAAEIMAV
60 70 80 90 100
LFFHTMRYKA LDPRNPHNDR FVLSKGHAAP ILYAVWAEAG FLPEAELLNL
110 120 130 140 150
RKISSDLDGH PVPKQAFTDV ATGSLGQGLG AACGMAYTGK YFDKASYRVY
160 170 180 190 200
CMLGDGEVSE GSVWEAMAFA GIYKLDNLVA IFDINRLGQS DPAPLQHQVD
210 220 230 240 250
IYQKRCEAFG WHTIIVDGHS VEELCKAFGQ AKHQPTAIIA KTFKGRGITG
260 270 280 290 300
IEDKEAWHGK PLPKNMAEQI IQEIYSQVQS KKKILATPPQ EDAPSVDIAN
310 320 330 340 350
IRMPTPPSYK VGDKIATRKA YGLALAKLGH ASDRIIALDG DTKNSTFSEL
360 370 380 390 400
FKKEHPDRFI ECYIAEQNMV SIAVGCATRD RTVPFCSTFA AFFTRAFDQI
410 420 430 440 450
RMAAISESNI NLCGSHCGVS IGEDGPSQMA LEDLAMFRSV PMSTVFYPSD
460 470 480 490 500
GVATEKAVEL AANTKGICFI RTSRPENAII YSNNEDFQVG QAKVVLKSKD
510 520 530 540 550
DQVTVIGAGV TLHEALAAAE SLKKDKISIR VLDPFTIKPL DRKLILDSAR
560 570 580 590 600
ATKGRILTVE DHYYEGGIGE AVSAAVVGEP GVTVTRLAVS QVPRSGKPAE
610 620
LLKMFGIDKD AIVQAVKGLV TKG
Length:623
Mass (Da):67,630
Last modified:February 1, 1995 - v1
Checksum:i870045AD5C58FA09
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti555 – 5551R → G in BAE26940 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U05809 mRNA. Translation: AAC52443.1.
AK002627 mRNA. Translation: BAB22242.1.
AK012794 mRNA. Translation: BAB28474.1.
AK030446 mRNA. Translation: BAC26968.1.
AK140965 mRNA. Translation: BAE24531.1.
AK144146 mRNA. Translation: BAE25728.1.
AK146157 mRNA. Translation: BAE26940.1.
AK150139 mRNA. Translation: BAE29335.1.
AK150769 mRNA. Translation: BAE29835.1.
AK150844 mRNA. Translation: BAE29902.1.
AK150856 mRNA. Translation: BAE29911.1.
AK152460 mRNA. Translation: BAE31238.1.
AK159922 mRNA. Translation: BAE35484.1.
AK167084 mRNA. Translation: BAE39242.1.
BC055336 mRNA. Translation: AAH55336.1.
U90889 Genomic DNA. Translation: AAC53570.1.
AF195533 mRNA. Translation: AAG28459.1.
CCDSiCCDS26894.1.
RefSeqiNP_033414.1. NM_009388.6.
UniGeneiMm.290692.

Genome annotation databases

EnsembliENSMUST00000022529; ENSMUSP00000022529; ENSMUSG00000021957.
GeneIDi21881.
KEGGimmu:21881.
UCSCiuc007svc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U05809 mRNA. Translation: AAC52443.1.
AK002627 mRNA. Translation: BAB22242.1.
AK012794 mRNA. Translation: BAB28474.1.
AK030446 mRNA. Translation: BAC26968.1.
AK140965 mRNA. Translation: BAE24531.1.
AK144146 mRNA. Translation: BAE25728.1.
AK146157 mRNA. Translation: BAE26940.1.
AK150139 mRNA. Translation: BAE29335.1.
AK150769 mRNA. Translation: BAE29835.1.
AK150844 mRNA. Translation: BAE29902.1.
AK150856 mRNA. Translation: BAE29911.1.
AK152460 mRNA. Translation: BAE31238.1.
AK159922 mRNA. Translation: BAE35484.1.
AK167084 mRNA. Translation: BAE39242.1.
BC055336 mRNA. Translation: AAH55336.1.
U90889 Genomic DNA. Translation: AAC53570.1.
AF195533 mRNA. Translation: AAG28459.1.
CCDSiCCDS26894.1.
RefSeqiNP_033414.1. NM_009388.6.
UniGeneiMm.290692.

3D structure databases

ProteinModelPortaliP40142.
SMRiP40142. Positions 4-618.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204213. 1 interaction.
IntActiP40142. 13 interactions.
MINTiMINT-1855010.
STRINGi10090.ENSMUSP00000022529.

PTM databases

iPTMnetiP40142.
PhosphoSiteiP40142.
SwissPalmiP40142.

2D gel databases

REPRODUCTION-2DPAGEP40142.
SWISS-2DPAGEP40142.

Proteomic databases

EPDiP40142.
MaxQBiP40142.
PaxDbiP40142.
PeptideAtlasiP40142.
PRIDEiP40142.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022529; ENSMUSP00000022529; ENSMUSG00000021957.
GeneIDi21881.
KEGGimmu:21881.
UCSCiuc007svc.2. mouse.

Organism-specific databases

CTDi7086.
MGIiMGI:105992. Tkt.

Phylogenomic databases

eggNOGiKOG0523. Eukaryota.
COG0021. LUCA.
GeneTreeiENSGT00390000005240.
HOGENOMiHOG000243868.
HOVERGENiHBG004036.
InParanoidiP40142.
KOiK00615.
OMAiKAFGQAR.
OrthoDBiEOG72RMXF.
PhylomeDBiP40142.
TreeFamiTF313097.

Enzyme and pathway databases

BRENDAi2.2.1.1. 3474.
ReactomeiR-MMU-163754. Insulin effects increased synthesis of Xylulose-5-Phosphate.
R-MMU-71336. Pentose phosphate pathway (hexose monophosphate shunt).

Miscellaneous databases

ChiTaRSiTkt. mouse.
PROiP40142.
SOURCEiSearch...

Gene expression databases

BgeeiP40142.
CleanExiMM_TKT.
ExpressionAtlasiP40142. baseline and differential.
GenevisibleiP40142. MM.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Amplification of the transketolase gene in desensitization-resistant mutant Y1 mouse adrenocortical tumor cells."
    Schimmer B.P., Tsao J., Czerwinski W.
    J. Biol. Chem. 271:4993-4998(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: LAF1.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BALB/cJ and C57BL/6J.
    Tissue: Bone marrow, Head, Kidney and Pituitary.
  3. "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].
    Strain: C57BL/6J.
    Tissue: Brain.
  4. "The mouse transketolase (TKT) gene: cloning, characterization, and functional promoter analysis."
    Salamon C., Chervenak M., Piatigorsky J., Sax C.M.
    Genomics 48:209-220(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
    Strain: 129/Sv.
  5. "Cloning new genes possibly associated with atrophy of murine thymus."
    Su H., He W., Li Y.
    Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 65-623.
    Strain: BALB/cJ.
    Tissue: Thymus.
  6. Lubec G., Klug S., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 175-204; 344-352; 382-395 AND 472-493, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain and Hippocampus.
  7. "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].
  8. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  10. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-6; LYS-232 AND LYS-538, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiTKT_MOUSE
AccessioniPrimary (citable) accession number: P40142
Secondary accession number(s): Q3U7Y1
, Q3UK62, Q545A1, Q9ESA0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 6, 2016
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.