TKT_HUMAN
ID TKT_HUMAN Reviewed; 623 AA.
AC P29401; A8K089; B4DE31; E7EPA7; Q8TBA3; Q96HH3;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 3.
DT 03-AUG-2022, entry version 223.
DE RecName: Full=Transketolase;
DE Short=TK;
DE EC=2.2.1.1 {ECO:0000269|PubMed:27259054};
GN Name=TKT;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=8419340; DOI=10.1016/s0021-9258(18)54089-8;
RA McCool B.A., Plonk S.G., Martin P.R., Singleton C.K.;
RT "Cloning of human transketolase cDNAs and comparison of the nucleotide
RT sequence of the coding region in Wernicke-Korsakoff and non-Wernicke-
RT Korsakoff individuals.";
RL J. Biol. Chem. 268:1397-1404(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Jung E.-H., Sheu K.-F.R.E., Szabo P., Blass J.P.;
RT "Molecular cloning, sequence and chromosome localization of human
RT transketolase.";
RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9115179; DOI=10.1007/pl00006179;
RA Schenk G., Layfield R., Candy J.M., Duggleby R.G., Nixon P.F.;
RT "Molecular evolutionary analysis of the thiamine-diphosphate-dependent
RT enzyme, transketolase.";
RL J. Mol. Evol. 44:552-572(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Kidney, and Lymph;
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 [8]
RP PROTEIN SEQUENCE OF 1-21.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 224-623 (ISOFORM 1), AND PARTIAL PROTEIN
RP SEQUENCE.
RC TISSUE=Brain;
RX PubMed=1567394; DOI=10.1016/s0006-291x(05)80312-2;
RA Abedinia M., Layfield R., Jones S.M., Nixon P.F., Mattick J.S.;
RT "Nucleotide and predicted amino acid sequence of a cDNA clone encoding part
RT of human transketolase.";
RL Biochem. Biophys. Res. Commun. 183:1159-1166(1992).
RN [10]
RP COFACTOR.
RX PubMed=3248678; DOI=10.1016/0020-711x(88)90228-5;
RA Jung E.H., Takeuchi T., Nishino K., Itokawa Y.;
RT "Studies on the nature of thiamine pyrophosphate binding and dependency on
RT divalent cations of transketolase from human erythrocytes.";
RL Int. J. Biochem. 20:1255-1259(1988).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-275 AND THR-287, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-11; LYS-144; LYS-204;
RP LYS-241; LYS-260 AND LYS-603, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-275; THR-287 AND SER-295, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-104; THR-287 AND
RP SER-295, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [21]
RP INVOLVEMENT IN SDDHD, VARIANT SDDHD CYS-318, CHARACTERIZATION OF VARIANT
RP SDDHD CYS-318, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=27259054; DOI=10.1016/j.ajhg.2016.03.030;
RA Boyle L., Wamelink M.M., Salomons G.S., Roos B., Pop A., Dauber A., Hwa V.,
RA Andrew M., Douglas J., Feingold M., Kramer N., Saitta S., Retterer K.,
RA Cho M.T., Begtrup A., Monaghan K.G., Wynn J., Chung W.K.;
RT "Mutations in TKT are the cause of a syndrome including short stature,
RT developmental delay, and congenital heart defects.";
RL Am. J. Hum. Genet. 98:1235-1242(2016).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-352, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 3-620 IN COMPLEXES WITH CALCIUM
RP AND THIAMINE PYROPHOSPHATE.
RX PubMed=20667822; DOI=10.1074/jbc.m110.149955;
RA Mitschke L., Parthier C., Schroder-Tittmann K., Coy J., Ludtke S.,
RA Tittmann K.;
RT "The crystal structure of human transketolase and new insights into its
RT mode of action.";
RL J. Biol. Chem. 285:31559-31570(2010).
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:0000269|PubMed:27259054}.
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 Evidence={ECO:0000269|PubMed:27259054};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:3248678};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:3248678};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:3248678};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:3248678};
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+).
CC {ECO:0000269|PubMed:3248678};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000269|PubMed:3248678};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000269|PubMed:3248678};
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC P29401; P54274: TERF1; NbExp=2; IntAct=EBI-1050560, EBI-710997;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P29401-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P29401-2; Sequence=VSP_045566;
CC -!- DISEASE: Short stature, developmental delay, and congenital heart
CC defects (SDDHD) [MIM:617044]: An autosomal recessive syndrome
CC characterized by short stature, developmental delay, intellectual
CC disability and congenital heart defects including ventricular septal
CC defect, atrial septal defect and patent foramen ovale. Cataract and
CC uveitis are observed in some patients. {ECO:0000269|PubMed:27259054}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Transketolase entry;
CC URL="https://en.wikipedia.org/wiki/Transketolase";
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DR EMBL; X67688; CAA47919.1; -; mRNA.
DR EMBL; L12711; AAA61222.1; -; mRNA.
DR EMBL; U55017; AAA98961.1; -; mRNA.
DR EMBL; AK289454; BAF82143.1; -; mRNA.
DR EMBL; AK293438; BAG56942.1; -; mRNA.
DR EMBL; AC097015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW65281.1; -; Genomic_DNA.
DR EMBL; BC008615; AAH08615.1; -; mRNA.
DR EMBL; BC009970; AAH09970.1; -; mRNA.
DR EMBL; BC024026; AAH24026.2; -; mRNA.
DR CCDS; CCDS2871.1; -. [P29401-1]
DR CCDS; CCDS58834.1; -. [P29401-2]
DR PIR; A45050; A45050.
DR RefSeq; NP_001055.1; NM_001064.3. [P29401-1]
DR RefSeq; NP_001128527.1; NM_001135055.2. [P29401-1]
DR RefSeq; NP_001244957.1; NM_001258028.1. [P29401-2]
DR RefSeq; XP_011532356.1; XM_011534054.1. [P29401-2]
DR PDB; 3MOS; X-ray; 1.75 A; A=3-618.
DR PDB; 3OOY; X-ray; 2.05 A; A/B=10-620.
DR PDB; 4KXU; X-ray; 0.98 A; A=1-623.
DR PDB; 4KXV; X-ray; 0.97 A; A=1-623.
DR PDB; 4KXW; X-ray; 0.97 A; A=1-623.
DR PDB; 4KXX; X-ray; 1.03 A; A=1-623.
DR PDB; 4KXY; X-ray; 1.26 A; A/B=1-623.
DR PDB; 6HA3; X-ray; 1.08 A; A=1-623.
DR PDB; 6HAD; X-ray; 1.04 A; A=1-623.
DR PDB; 6RJB; X-ray; 1.15 A; A/B=1-623.
DR PDBsum; 3MOS; -.
DR PDBsum; 3OOY; -.
DR PDBsum; 4KXU; -.
DR PDBsum; 4KXV; -.
DR PDBsum; 4KXW; -.
DR PDBsum; 4KXX; -.
DR PDBsum; 4KXY; -.
DR PDBsum; 6HA3; -.
DR PDBsum; 6HAD; -.
DR PDBsum; 6RJB; -.
DR AlphaFoldDB; P29401; -.
DR SMR; P29401; -.
DR BioGRID; 112941; 278.
DR IntAct; P29401; 76.
DR MINT; P29401; -.
DR STRING; 9606.ENSP00000391481; -.
DR BindingDB; P29401; -.
DR ChEMBL; CHEMBL4983; -.
DR DrugBank; DB09130; Copper.
DR DrugCentral; P29401; -.
DR GlyGen; P29401; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P29401; -.
DR MetOSite; P29401; -.
DR PhosphoSitePlus; P29401; -.
DR SwissPalm; P29401; -.
DR BioMuta; TKT; -.
DR DMDM; 1729976; -.
DR REPRODUCTION-2DPAGE; IPI00643920; -.
DR EPD; P29401; -.
DR jPOST; P29401; -.
DR MassIVE; P29401; -.
DR MaxQB; P29401; -.
DR PaxDb; P29401; -.
DR PeptideAtlas; P29401; -.
DR PRIDE; P29401; -.
DR ProteomicsDB; 17317; -.
DR ProteomicsDB; 54568; -. [P29401-1]
DR TopDownProteomics; P29401-1; -. [P29401-1]
DR Antibodypedia; 31391; 266 antibodies from 30 providers.
DR DNASU; 7086; -.
DR Ensembl; ENST00000423516.5; ENSP00000391481.1; ENSG00000163931.17. [P29401-2]
DR Ensembl; ENST00000423525.6; ENSP00000405455.2; ENSG00000163931.17. [P29401-1]
DR Ensembl; ENST00000462138.6; ENSP00000417773.1; ENSG00000163931.17. [P29401-1]
DR GeneID; 7086; -.
DR KEGG; hsa:7086; -.
DR MANE-Select; ENST00000462138.6; ENSP00000417773.1; NM_001064.4; NP_001055.1.
DR UCSC; uc011beq.4; human. [P29401-1]
DR CTD; 7086; -.
DR DisGeNET; 7086; -.
DR GeneCards; TKT; -.
DR HGNC; HGNC:11834; TKT.
DR HPA; ENSG00000163931; Tissue enhanced (bone).
DR MalaCards; TKT; -.
DR MIM; 606781; gene.
DR MIM; 617044; phenotype.
DR neXtProt; NX_P29401; -.
DR OpenTargets; ENSG00000163931; -.
DR Orphanet; 488618; Transketolase deficiency.
DR PharmGKB; PA36537; -.
DR VEuPathDB; HostDB:ENSG00000163931; -.
DR eggNOG; KOG0523; Eukaryota.
DR GeneTree; ENSGT00940000155552; -.
DR HOGENOM; CLU_009227_3_0_1; -.
DR InParanoid; P29401; -.
DR OMA; NSGHSGM; -.
DR OrthoDB; 354970at2759; -.
DR PhylomeDB; P29401; -.
DR TreeFam; TF313097; -.
DR BRENDA; 2.2.1.1; 2681.
DR PathwayCommons; P29401; -.
DR Reactome; R-HSA-163754; Insulin effects increased synthesis of Xylulose-5-Phosphate.
DR Reactome; R-HSA-71336; Pentose phosphate pathway.
DR Reactome; R-HSA-9759194; Nuclear events mediated by NFE2L2.
DR SABIO-RK; P29401; -.
DR SignaLink; P29401; -.
DR SIGNOR; P29401; -.
DR BioGRID-ORCS; 7086; 315 hits in 1091 CRISPR screens.
DR ChiTaRS; TKT; human.
DR EvolutionaryTrace; P29401; -.
DR GenomeRNAi; 7086; -.
DR Pharos; P29401; Tchem.
DR PRO; PR:P29401; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P29401; protein.
DR Bgee; ENSG00000163931; Expressed in monocyte and 209 other tissues.
DR ExpressionAtlas; P29401; baseline and differential.
DR Genevisible; P29401; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0031982; C:vesicle; HDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IBA:GO_Central.
DR GO; GO:0004802; F:transketolase activity; IDA:UniProtKB.
DR GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006098; P:pentose-phosphate shunt; IDA:UniProtKB.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IBA:GO_Central.
DR GO; GO:0040008; P:regulation of growth; IEA:Ensembl.
DR GO; GO:0046390; P:ribose phosphate biosynthetic process; IBA:GO_Central.
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 3D-structure; Acetylation; Alternative splicing; Calcium;
KW Direct protein sequencing; Disease variant; Dwarfism; 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_0000191894"
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 BINDING 77
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT BINDING 123..125
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 156
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT BINDING 185
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 185
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT BINDING 187
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 244
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT BINDING 258
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
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 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 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:22814378"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 6
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 11
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 144
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 204
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 232
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P40142"
FT MOD_RES 241
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 260
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 275
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 287
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50137"
FT MOD_RES 538
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P40142"
FT MOD_RES 603
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 352
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 146
FT /note="S -> SLPSSWDYS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045566"
FT VARIANT 181
FT /note="I -> V (in dbSNP:rs17052920)"
FT /id="VAR_052634"
FT VARIANT 318
FT /note="R -> C (in SDDHD; decreased of transketolase
FT activity; dbSNP:rs782092363)"
FT /evidence="ECO:0000269|PubMed:27259054"
FT /id="VAR_077030"
FT CONFLICT 30..31
FT /note="TT -> SS (in Ref. 1; CAA47919)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="E -> V (in Ref. 1; CAA47919)"
FT /evidence="ECO:0000305"
FT CONFLICT 224..230
FT /note="LCKAFGQ -> AVQGLCE (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="E -> G (in Ref. 4; BAG56942)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="P -> A (in Ref. 1; CAA47919)"
FT /evidence="ECO:0000305"
FT CONFLICT 585..587
FT /note="THL -> KTM (in Ref. 2; AAA61222)"
FT /evidence="ECO:0000305"
FT CONFLICT 608..623
FT /note="DRDAIAQAVRGLITKA -> TGMPLHKL (in Ref. 9; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT HELIX 9..33
FT /evidence="ECO:0007829|PDB:4KXV"
FT HELIX 38..42
FT /evidence="ECO:0007829|PDB:4KXV"
FT HELIX 45..53
FT /evidence="ECO:0007829|PDB:4KXV"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:4KXV"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:4KXV"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:4KXV"
FT HELIX 94..99
FT /evidence="ECO:0007829|PDB:4KXV"
FT HELIX 128..141
FT /evidence="ECO:0007829|PDB:4KXV"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:4KXV"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:4KXV"
FT HELIX 161..172
FT /evidence="ECO:0007829|PDB:4KXV"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:4KXV"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:4KXV"
FT TURN 194..197
FT /evidence="ECO:0007829|PDB:4KXV"
FT HELIX 199..208
FT /evidence="ECO:0007829|PDB:4KXV"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:4KXV"
FT HELIX 221..229
FT /evidence="ECO:0007829|PDB:4KXV"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:4KXV"
FT TURN 244..247
FT /evidence="ECO:0007829|PDB:4KXV"
FT TURN 249..253
FT /evidence="ECO:0007829|PDB:4KXV"
FT HELIX 264..275
FT /evidence="ECO:0007829|PDB:4KXV"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:4KXV"
FT HELIX 317..331
FT /evidence="ECO:0007829|PDB:4KXV"
FT STRAND 335..341
FT /evidence="ECO:0007829|PDB:4KXV"
FT HELIX 343..346
FT /evidence="ECO:0007829|PDB:4KXV"
FT HELIX 349..354
FT /evidence="ECO:0007829|PDB:4KXV"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:4KXV"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:4KXV"
FT HELIX 366..377
FT /evidence="ECO:0007829|PDB:4KXV"
FT HELIX 378..380
FT /evidence="ECO:0007829|PDB:4KXV"
FT STRAND 383..389
FT /evidence="ECO:0007829|PDB:4KXV"
FT HELIX 390..396
FT /evidence="ECO:0007829|PDB:4KXV"
FT HELIX 397..405
FT /evidence="ECO:0007829|PDB:4KXV"
FT STRAND 410..418
FT /evidence="ECO:0007829|PDB:4KXV"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:4KXV"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:4KXV"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:4KXV"
FT HELIX 433..438
FT /evidence="ECO:0007829|PDB:4KXV"
FT STRAND 443..446
FT /evidence="ECO:0007829|PDB:4KXV"
FT HELIX 451..462
FT /evidence="ECO:0007829|PDB:4KXV"
FT STRAND 466..471
FT /evidence="ECO:0007829|PDB:4KXV"
FT STRAND 474..478
FT /evidence="ECO:0007829|PDB:4KXV"
FT STRAND 493..496
FT /evidence="ECO:0007829|PDB:4KXV"
FT STRAND 501..506
FT /evidence="ECO:0007829|PDB:4KXV"
FT HELIX 510..523
FT /evidence="ECO:0007829|PDB:4KXV"
FT TURN 524..526
FT /evidence="ECO:0007829|PDB:4KXV"
FT STRAND 528..533
FT /evidence="ECO:0007829|PDB:4KXV"
FT STRAND 535..539
FT /evidence="ECO:0007829|PDB:4KXV"
FT HELIX 542..551
FT /evidence="ECO:0007829|PDB:4KXV"
FT TURN 552..554
FT /evidence="ECO:0007829|PDB:4KXV"
FT STRAND 555..564
FT /evidence="ECO:0007829|PDB:4KXV"
FT HELIX 568..576
FT /evidence="ECO:0007829|PDB:4KXV"
FT STRAND 583..589
FT /evidence="ECO:0007829|PDB:4KXV"
FT HELIX 598..604
FT /evidence="ECO:0007829|PDB:4KXV"
FT HELIX 609..620
FT /evidence="ECO:0007829|PDB:4KXV"
SQ SEQUENCE 623 AA; 67878 MW; 176C89C02FD2712B CRC64;
MESYHKPDQQ KLQALKDTAN RLRISSIQAT TAAGSGHPTS CCSAAEIMAV LFFHTMRYKS
QDPRNPHNDR FVLSKGHAAP ILYAVWAEAG FLAEAELLNL RKISSDLDGH PVPKQAFTDV
ATGSLGQGLG AACGMAYTGK YFDKASYRVY CLLGDGELSE GSVWEAMAFA SIYKLDNLVA
ILDINRLGQS DPAPLQHQMD IYQKRCEAFG WHAIIVDGHS VEELCKAFGQ AKHQPTAIIA
KTFKGRGITG VEDKESWHGK PLPKNMAEQI IQEIYSQIQS KKKILATPPQ EDAPSVDIAN
IRMPSLPSYK VGDKIATRKA YGQALAKLGH ASDRIIALDG DTKNSTFSEI FKKEHPDRFI
ECYIAEQNMV SIAVGCATRN RTVPFCSTFA AFFTRAFDQI RMAAISESNI NLCGSHCGVS
IGEDGPSQMA LEDLAMFRSV PTSTVFYPSD GVATEKAVEL AANTKGICFI RTSRPENAII
YNNNEDFQVG QAKVVLKSKD DQVTVIGAGV TLHEALAAAE LLKKEKINIR VLDPFTIKPL
DRKLILDSAR ATKGRILTVE DHYYEGGIGE AVSSAVVGEP GITVTHLAVN RVPRSGKPAE
LLKMFGIDRD AIAQAVRGLI TKA
