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

Regions

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

GO - Molecular functioni

  1. cofactor binding Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW
  3. protein homodimerization activity Source: UniProtKB
  4. transketolase activity Source: UniProtKB

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. energy reserve metabolic process Source: Reactome
  3. glyceraldehyde-3-phosphate biosynthetic process Source: UniProtKB
  4. pathogenesis Source: Reactome
  5. pentose-phosphate shunt Source: Reactome
  6. pentose-phosphate shunt, non-oxidative branch Source: UniProtKB
  7. regulation of growth Source: Ensembl
  8. small molecule metabolic process Source: Reactome
  9. xylulose biosynthetic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Calcium, Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

ReactomeiREACT_1859. Pentose phosphate pathway (hexose monophosphate shunt).
REACT_939. Insulin effects increased synthesis of Xylulose-5-Phosphate.
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
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:11834. TKT.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProtKB
  3. nucleoplasm Source: HPA
  4. nucleus Source: HPA
  5. peroxisome Source: UniProtKB
  6. vesicle Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36537.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 623623TransketolasePRO_0000191894Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei6 – 61N6-acetyllysine1 Publication
Modified residuei11 – 111N6-acetyllysine1 Publication
Modified residuei144 – 1441N6-acetyllysine1 Publication
Modified residuei204 – 2041N6-acetyllysine1 Publication
Modified residuei232 – 2321N6-acetyllysineBy similarity
Modified residuei241 – 2411N6-acetyllysine1 Publication
Modified residuei260 – 2601N6-acetyllysine1 Publication
Modified residuei275 – 2751Phosphotyrosine2 Publications
Modified residuei287 – 2871Phosphothreonine2 Publications
Modified residuei295 – 2951Phosphoserine2 Publications
Modified residuei538 – 5381N6-acetyllysineBy similarity
Modified residuei603 – 6031N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP29401.
PaxDbiP29401.
PRIDEiP29401.

2D gel databases

REPRODUCTION-2DPAGEIPI00643920.

PTM databases

PhosphoSiteiP29401.

Expressioni

Gene expression databases

BgeeiP29401.
CleanExiHS_TKT.
ExpressionAtlasiP29401. baseline and differential.
GenevestigatoriP29401.

Organism-specific databases

HPAiHPA029480.
HPA029481.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi112941. 35 interactions.
IntActiP29401. 11 interactions.
MINTiMINT-3011391.
STRINGi9606.ENSP00000405455.

Structurei

Secondary structure

1
623
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 3325Combined sources
Helixi38 – 425Combined sources
Helixi45 – 539Combined sources
Beta strandi70 – 756Combined sources
Helixi76 – 783Combined sources
Helixi79 – 8810Combined sources
Helixi94 – 996Combined sources
Helixi128 – 14114Combined sources
Beta strandi149 – 1557Combined sources
Helixi156 – 1594Combined sources
Helixi161 – 17212Combined sources
Beta strandi178 – 1847Combined sources
Beta strandi189 – 1924Combined sources
Turni194 – 1974Combined sources
Helixi199 – 20810Combined sources
Beta strandi212 – 2176Combined sources
Helixi221 – 2299Combined sources
Beta strandi236 – 2416Combined sources
Turni244 – 2474Combined sources
Turni249 – 2535Combined sources
Helixi264 – 27512Combined sources
Beta strandi314 – 3163Combined sources
Helixi317 – 33115Combined sources
Beta strandi335 – 3417Combined sources
Helixi343 – 3464Combined sources
Helixi349 – 3546Combined sources
Helixi356 – 3583Combined sources
Beta strandi359 – 3613Combined sources
Helixi366 – 37712Combined sources
Helixi378 – 3803Combined sources
Beta strandi383 – 3897Combined sources
Helixi390 – 3967Combined sources
Helixi397 – 4059Combined sources
Beta strandi410 – 4189Combined sources
Helixi419 – 4213Combined sources
Helixi426 – 4283Combined sources
Beta strandi430 – 4323Combined sources
Helixi433 – 4386Combined sources
Beta strandi443 – 4464Combined sources
Helixi451 – 46212Combined sources
Beta strandi466 – 4716Combined sources
Beta strandi474 – 4785Combined sources
Beta strandi493 – 4964Combined sources
Beta strandi501 – 5066Combined sources
Helixi510 – 52314Combined sources
Turni524 – 5263Combined sources
Beta strandi528 – 5336Combined sources
Beta strandi535 – 5395Combined sources
Helixi542 – 55110Combined sources
Turni552 – 5543Combined sources
Beta strandi555 – 56410Combined sources
Helixi568 – 5769Combined sources
Beta strandi583 – 5897Combined sources
Helixi598 – 6047Combined sources
Helixi609 – 62012Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-622.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29401.

Family & Domainsi

Sequence similaritiesi

Belongs to the transketolase family.Curated

Phylogenomic databases

eggNOGiCOG0021.
GeneTreeiENSGT00390000005240.
HOGENOMiHOG000243868.
HOVERGENiHBG004036.
InParanoidiP29401.
KOiK00615.
OMAiESNINFC.
OrthoDBiEOG72RMXF.
PhylomeDBiP29401.
TreeFamiTF313097.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR020826. Transketolase_BS.
IPR005476. Transketolase_C.
IPR005474. Transketolase_N.
[Graphical view]
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 312TT → SS in CAA47919 (PubMed:8419340).Curated
Sequence conflicti46 – 461E → V in CAA47919 (PubMed:8419340).Curated
Sequence conflicti224 – 2307LCKAFGQ → AVQGLCE AA sequence (PubMed:1567394).Curated
Sequence conflicti366 – 3661E → G in BAG56942 (PubMed:14702039).Curated
Sequence conflicti426 – 4261P → A in CAA47919 (PubMed:8419340).Curated
Sequence conflicti585 – 5873THL → KTM in AAA61222 (Ref. 2) Curated
Sequence conflicti608 – 62316DRDAI…LITKA → TGMPLHKL AA sequence (PubMed:1567394).CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti181 – 1811I → V.
Corresponds to variant rs17052920 [ dbSNP | Ensembl ].
VAR_052634

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei146 – 1461S → SLPSSWDYS in isoform 2. 1 PublicationVSP_045566

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]
UniGeneiHs.89643.

Genome annotation databases

EnsembliENST00000423516; ENSP00000391481; ENSG00000163931. [P29401-2]
ENST00000423525; ENSP00000405455; ENSG00000163931. [P29401-1]
ENST00000462138; ENSP00000417773; ENSG00000163931. [P29401-1]
GeneIDi7086.
KEGGihsa:7086.
UCSCiuc003dgo.3. human. [P29401-1]

Polymorphism databases

DMDMi1729976.

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]
UniGeneiHs.89643.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-622.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112941. 35 interactions.
IntActiP29401. 11 interactions.
MINTiMINT-3011391.
STRINGi9606.ENSP00000405455.

Chemistry

BindingDBiP29401.
ChEMBLiCHEMBL4983.

PTM databases

PhosphoSiteiP29401.

Polymorphism databases

DMDMi1729976.

2D gel databases

REPRODUCTION-2DPAGEIPI00643920.

Proteomic databases

MaxQBiP29401.
PaxDbiP29401.
PRIDEiP29401.

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.
UCSCiuc003dgo.3. human. [P29401-1]

Organism-specific databases

CTDi7086.
GeneCardsiGC03M053258.
HGNCiHGNC:11834. TKT.
HPAiHPA029480.
HPA029481.
MIMi606781. gene.
neXtProtiNX_P29401.
PharmGKBiPA36537.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0021.
GeneTreeiENSGT00390000005240.
HOGENOMiHOG000243868.
HOVERGENiHBG004036.
InParanoidiP29401.
KOiK00615.
OMAiESNINFC.
OrthoDBiEOG72RMXF.
PhylomeDBiP29401.
TreeFamiTF313097.

Enzyme and pathway databases

ReactomeiREACT_1859. Pentose phosphate pathway (hexose monophosphate shunt).
REACT_939. Insulin effects increased synthesis of Xylulose-5-Phosphate.
SABIO-RKP29401.

Miscellaneous databases

ChiTaRSiTKT. human.
EvolutionaryTraceiP29401.
GenomeRNAii7086.
NextBioi27715.
PROiP29401.
SOURCEiSearch...

Gene expression databases

BgeeiP29401.
CleanExiHS_TKT.
ExpressionAtlasiP29401. baseline and differential.
GenevestigatoriP29401.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR020826. Transketolase_BS.
IPR005476. Transketolase_C.
IPR005474. Transketolase_N.
[Graphical view]
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. "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.
    , 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.
    , 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "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.

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: March 4, 2015
This is version 162 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

External Data

Dasty 3

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 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.