TKT_MOUSE
ID TKT_MOUSE Reviewed; 623 AA.
AC P40142; Q3U7Y1; Q3UK62; Q545A1; Q9ESA0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Transketolase;
DE Short=TK;
DE EC=2.2.1.1;
DE AltName: Full=P68;
GN Name=Tkt;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=LAF1;
RX PubMed=8617775; DOI=10.1074/jbc.271.9.4993;
RA Schimmer B.P., Tsao J., Czerwinski W.;
RT "Amplification of the transketolase gene in desensitization-resistant
RT mutant Y1 mouse adrenocortical tumor cells.";
RL J. Biol. Chem. 271:4993-4998(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, and C57BL/6J;
RC TISSUE=Bone marrow, Head, Kidney, and Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
RC STRAIN=129/Sv;
RX PubMed=9521875; DOI=10.1006/geno.1997.5187;
RA Salamon C., Chervenak M., Piatigorsky J., Sax C.M.;
RT "The mouse transketolase (TKT) gene: cloning, characterization, and
RT functional promoter analysis.";
RL Genomics 48:209-220(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 65-623.
RC STRAIN=BALB/cJ; TISSUE=Thymus;
RA Su H., He W., Li Y.;
RT "Cloning new genes possibly associated with atrophy of murine thymus.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 175-204; 344-352; 382-395 AND 472-493, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-275, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-6; LYS-232 AND LYS-538,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a
CC ketose donor to an aldose acceptor, via a covalent intermediate with
CC the cofactor thiamine pyrophosphate. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent
CC metal cations, such as Ca(2+), Mn(2+) and Co(2+). {ECO:0000250};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR EMBL; U05809; AAC52443.1; -; mRNA.
DR EMBL; AK002627; BAB22242.1; -; mRNA.
DR EMBL; AK012794; BAB28474.1; -; mRNA.
DR EMBL; AK030446; BAC26968.1; -; mRNA.
DR EMBL; AK140965; BAE24531.1; -; mRNA.
DR EMBL; AK144146; BAE25728.1; -; mRNA.
DR EMBL; AK146157; BAE26940.1; -; mRNA.
DR EMBL; AK150139; BAE29335.1; -; mRNA.
DR EMBL; AK150769; BAE29835.1; -; mRNA.
DR EMBL; AK150844; BAE29902.1; -; mRNA.
DR EMBL; AK150856; BAE29911.1; -; mRNA.
DR EMBL; AK152460; BAE31238.1; -; mRNA.
DR EMBL; AK159922; BAE35484.1; -; mRNA.
DR EMBL; AK167084; BAE39242.1; -; mRNA.
DR EMBL; BC055336; AAH55336.1; -; mRNA.
DR EMBL; U90889; AAC53570.1; -; Genomic_DNA.
DR EMBL; AF195533; AAG28459.1; -; mRNA.
DR CCDS; CCDS26894.1; -.
DR RefSeq; NP_033414.1; NM_009388.6.
DR AlphaFoldDB; P40142; -.
DR SMR; P40142; -.
DR BioGRID; 204213; 18.
DR IntAct; P40142; 12.
DR MINT; P40142; -.
DR STRING; 10090.ENSMUSP00000022529; -.
DR iPTMnet; P40142; -.
DR PhosphoSitePlus; P40142; -.
DR SwissPalm; P40142; -.
DR REPRODUCTION-2DPAGE; P40142; -.
DR SWISS-2DPAGE; P40142; -.
DR CPTAC; non-CPTAC-3621; -.
DR EPD; P40142; -.
DR jPOST; P40142; -.
DR MaxQB; P40142; -.
DR PaxDb; P40142; -.
DR PeptideAtlas; P40142; -.
DR PRIDE; P40142; -.
DR ProteomicsDB; 258891; -.
DR Antibodypedia; 31391; 266 antibodies from 30 providers.
DR DNASU; 21881; -.
DR Ensembl; ENSMUST00000022529; ENSMUSP00000022529; ENSMUSG00000021957.
DR GeneID; 21881; -.
DR KEGG; mmu:21881; -.
DR UCSC; uc007svc.2; mouse.
DR CTD; 7086; -.
DR MGI; MGI:105992; Tkt.
DR VEuPathDB; HostDB:ENSMUSG00000021957; -.
DR eggNOG; KOG0523; Eukaryota.
DR GeneTree; ENSGT00940000155552; -.
DR HOGENOM; CLU_009227_3_0_1; -.
DR InParanoid; P40142; -.
DR OMA; YALQQTD; -.
DR OrthoDB; 354970at2759; -.
DR PhylomeDB; P40142; -.
DR TreeFam; TF313097; -.
DR BRENDA; 2.2.1.1; 3474.
DR Reactome; R-MMU-163754; Insulin effects increased synthesis of Xylulose-5-Phosphate.
DR Reactome; R-MMU-71336; Pentose phosphate pathway.
DR BioGRID-ORCS; 21881; 18 hits in 76 CRISPR screens.
DR ChiTaRS; Tkt; mouse.
DR PRO; PR:P40142; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P40142; protein.
DR Bgee; ENSMUSG00000021957; Expressed in substantia propria of cornea and 275 other tissues.
DR ExpressionAtlas; P40142; baseline and differential.
DR Genevisible; P40142; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISO:MGI.
DR GO; GO:0048029; F:monosaccharide binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; ISO:MGI.
DR GO; GO:0004802; F:transketolase activity; IDA:MGI.
DR GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; ISO:MGI.
DR GO; GO:0006098; P:pentose-phosphate shunt; IDA:MGI.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; ISO:MGI.
DR GO; GO:0040008; P:regulation of growth; IMP:MGI.
DR GO; GO:0046390; P:ribose phosphate biosynthetic process; ISO:MGI.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR005474; Transketolase_N.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR SUPFAM; SSF52922; SSF52922; 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Calcium; Direct protein sequencing; Isopeptide bond;
KW Magnesium; Metal-binding; Phosphoprotein; Reference proteome;
KW Thiamine pyrophosphate; Transferase; Ubl conjugation.
FT CHAIN 1..623
FT /note="Transketolase"
FT /id="PRO_0000191896"
FT ACT_SITE 366
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 123..125
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 416
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 424
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 428
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 474
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 37
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 258
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 6
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 11
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29401"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29401"
FT MOD_RES 144
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29401"
FT MOD_RES 204
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29401"
FT MOD_RES 232
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 241
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29401"
FT MOD_RES 260
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29401"
FT MOD_RES 275
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 287
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29401"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50137"
FT MOD_RES 538
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 603
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29401"
FT CROSSLNK 352
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P29401"
FT CONFLICT 555
FT /note="R -> G (in Ref. 2; BAE26940)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 623 AA; 67630 MW; 870045AD5C58FA09 CRC64;
MEGYHKPDQQ KLQALKDTAN RLRISSIQAT TAAGSGHPTS CCSAAEIMAV LFFHTMRYKA
LDPRNPHNDR FVLSKGHAAP ILYAVWAEAG FLPEAELLNL RKISSDLDGH PVPKQAFTDV
ATGSLGQGLG AACGMAYTGK YFDKASYRVY CMLGDGEVSE GSVWEAMAFA GIYKLDNLVA
IFDINRLGQS DPAPLQHQVD IYQKRCEAFG WHTIIVDGHS VEELCKAFGQ AKHQPTAIIA
KTFKGRGITG IEDKEAWHGK PLPKNMAEQI IQEIYSQVQS KKKILATPPQ EDAPSVDIAN
IRMPTPPSYK VGDKIATRKA YGLALAKLGH ASDRIIALDG DTKNSTFSEL FKKEHPDRFI
ECYIAEQNMV SIAVGCATRD RTVPFCSTFA AFFTRAFDQI RMAAISESNI NLCGSHCGVS
IGEDGPSQMA LEDLAMFRSV PMSTVFYPSD GVATEKAVEL AANTKGICFI RTSRPENAII
YSNNEDFQVG QAKVVLKSKD DQVTVIGAGV TLHEALAAAE SLKKDKISIR VLDPFTIKPL
DRKLILDSAR ATKGRILTVE DHYYEGGIGE AVSAAVVGEP GVTVTRLAVS QVPRSGKPAE
LLKMFGIDKD AIVQAVKGLV TKG
