Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P29401

- TKT_HUMAN

UniProt

P29401 - TKT_HUMAN

Protein

Transketolase

Gene

TKT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 3 (01 Oct 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Binds 1 magnesium ion per subunit. Can also utilize other divalent metal cations, such as Ca2+, Mn2+ and Co2+.1 Publication
    Binds 1 thiamine pyrophosphate per subunit.1 Publication

    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. pentose-phosphate shunt Source: Reactome
    5. pentose-phosphate shunt, non-oxidative branch Source: UniProtKB
    6. regulation of growth Source: Ensembl
    7. small molecule metabolic process Source: Reactome
    8. xylulose biosynthetic process Source: Reactome

    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: UniProt
    3. nucleus Source: HPA
    4. peroxisome Source: UniProtKB
    5. vesicle Source: UniProtKB

    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

    ArrayExpressiP29401.
    BgeeiP29401.
    CleanExiHS_TKT.
    GenevestigatoriP29401.

    Organism-specific databases

    HPAiHPA029480.
    HPA029481.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi112941. 34 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 – 3325
    Helixi38 – 425
    Helixi45 – 539
    Beta strandi70 – 756
    Helixi76 – 783
    Helixi79 – 8810
    Helixi94 – 996
    Helixi128 – 14114
    Beta strandi149 – 1557
    Helixi156 – 1594
    Helixi161 – 17212
    Beta strandi178 – 1847
    Beta strandi189 – 1924
    Turni194 – 1974
    Helixi199 – 20810
    Beta strandi212 – 2176
    Helixi221 – 2299
    Beta strandi236 – 2416
    Turni244 – 2474
    Turni249 – 2535
    Helixi264 – 27512
    Beta strandi314 – 3163
    Helixi317 – 33115
    Beta strandi335 – 3417
    Helixi343 – 3464
    Helixi349 – 3546
    Helixi356 – 3583
    Beta strandi359 – 3613
    Helixi366 – 37712
    Helixi378 – 3803
    Beta strandi383 – 3897
    Helixi390 – 3967
    Helixi397 – 4059
    Beta strandi410 – 4189
    Helixi419 – 4213
    Helixi426 – 4283
    Beta strandi430 – 4323
    Helixi433 – 4386
    Beta strandi443 – 4464
    Helixi451 – 46212
    Beta strandi466 – 4716
    Beta strandi474 – 4785
    Beta strandi493 – 4964
    Beta strandi501 – 5066
    Helixi510 – 52314
    Turni524 – 5263
    Beta strandi528 – 5336
    Beta strandi535 – 5395
    Helixi542 – 55110
    Turni552 – 5543
    Beta strandi555 – 56410
    Helixi568 – 5769
    Beta strandi583 – 5897
    Helixi598 – 6047
    Helixi609 – 62012

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000243868.
    HOVERGENiHBG004036.
    InParanoidiP29401.
    KOiK00615.
    OMAiPPNYKVG.
    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. Align

    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

    MESYHKPDQQ KLQALKDTAN RLRISSIQAT TAAGSGHPTS CCSAAEIMAV    50
    LFFHTMRYKS QDPRNPHNDR FVLSKGHAAP ILYAVWAEAG FLAEAELLNL 100
    RKISSDLDGH PVPKQAFTDV ATGSLGQGLG AACGMAYTGK YFDKASYRVY 150
    CLLGDGELSE GSVWEAMAFA SIYKLDNLVA ILDINRLGQS DPAPLQHQMD 200
    IYQKRCEAFG WHAIIVDGHS VEELCKAFGQ AKHQPTAIIA KTFKGRGITG 250
    VEDKESWHGK PLPKNMAEQI IQEIYSQIQS KKKILATPPQ EDAPSVDIAN 300
    IRMPSLPSYK VGDKIATRKA YGQALAKLGH ASDRIIALDG DTKNSTFSEI 350
    FKKEHPDRFI ECYIAEQNMV SIAVGCATRN RTVPFCSTFA AFFTRAFDQI 400
    RMAAISESNI NLCGSHCGVS IGEDGPSQMA LEDLAMFRSV PTSTVFYPSD 450
    GVATEKAVEL AANTKGICFI RTSRPENAII YNNNEDFQVG QAKVVLKSKD 500
    DQVTVIGAGV TLHEALAAAE LLKKEKINIR VLDPFTIKPL DRKLILDSAR 550
    ATKGRILTVE DHYYEGGIGE AVSSAVVGEP GITVTHLAVN RVPRSGKPAE 600
    LLKMFGIDRD AIAQAVRGLI TKA 623
    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. 1 PublicationCurated
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS2871.1. [P29401-1 ]
    CCDS58834.1. [P29401-2 ]
    PIRi A45050.
    RefSeqi NP_001055.1. NM_001064.3. [P29401-1 ]
    NP_001128527.1. NM_001135055.2. [P29401-1 ]
    NP_001244957.1. NM_001258028.1. [P29401-2 ]
    UniGenei Hs.89643.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3MOS X-ray 1.75 A 3-618 [» ]
    3OOY X-ray 2.05 A/B 10-620 [» ]
    4KXU X-ray 0.98 A 1-623 [» ]
    4KXV X-ray 0.97 A 1-623 [» ]
    4KXW X-ray 0.97 A 1-623 [» ]
    4KXX X-ray 1.03 A 1-623 [» ]
    4KXY X-ray 1.26 A/B 1-623 [» ]
    ProteinModelPortali P29401.
    SMRi P29401. Positions 2-622.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112941. 34 interactions.
    IntActi P29401. 11 interactions.
    MINTi MINT-3011391.
    STRINGi 9606.ENSP00000405455.

    Chemistry

    BindingDBi P29401.
    ChEMBLi CHEMBL4983.
    DrugBanki DB00152. Thiamine.

    PTM databases

    PhosphoSitei P29401.

    Polymorphism databases

    DMDMi 1729976.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00643920.

    Proteomic databases

    MaxQBi P29401.
    PaxDbi P29401.
    PRIDEi P29401.

    Protocols and materials databases

    DNASUi 7086.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000423516 ; ENSP00000391481 ; ENSG00000163931 . [P29401-2 ]
    ENST00000423525 ; ENSP00000405455 ; ENSG00000163931 . [P29401-1 ]
    ENST00000462138 ; ENSP00000417773 ; ENSG00000163931 . [P29401-1 ]
    GeneIDi 7086.
    KEGGi hsa:7086.
    UCSCi uc003dgo.3. human. [P29401-1 ]

    Organism-specific databases

    CTDi 7086.
    GeneCardsi GC03M053258.
    HGNCi HGNC:11834. TKT.
    HPAi HPA029480.
    HPA029481.
    MIMi 606781. gene.
    neXtProti NX_P29401.
    PharmGKBi PA36537.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0021.
    HOGENOMi HOG000243868.
    HOVERGENi HBG004036.
    InParanoidi P29401.
    KOi K00615.
    OMAi PPNYKVG.
    OrthoDBi EOG72RMXF.
    PhylomeDBi P29401.
    TreeFami TF313097.

    Enzyme and pathway databases

    Reactomei REACT_1859. Pentose phosphate pathway (hexose monophosphate shunt).
    REACT_939. Insulin effects increased synthesis of Xylulose-5-Phosphate.
    SABIO-RK P29401.

    Miscellaneous databases

    ChiTaRSi TKT. human.
    EvolutionaryTracei P29401.
    GenomeRNAii 7086.
    NextBioi 27715.
    PROi P29401.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P29401.
    Bgeei P29401.
    CleanExi HS_TKT.
    Genevestigatori P29401.

    Family and domain databases

    Gene3Di 3.40.50.920. 1 hit.
    3.40.50.970. 2 hits.
    InterProi IPR029061. THDP-binding.
    IPR009014. Transketo_C/Pyr-ferredox_oxred.
    IPR005475. Transketolase-like_Pyr-bd.
    IPR020826. Transketolase_BS.
    IPR005476. Transketolase_C.
    IPR005474. Transketolase_N.
    [Graphical view ]
    Pfami PF02779. Transket_pyr. 1 hit.
    PF02780. Transketolase_C. 1 hit.
    PF00456. Transketolase_N. 1 hit.
    [Graphical view ]
    SMARTi SM00861. Transket_pyr. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52518. SSF52518. 2 hits.
    SSF52922. SSF52922. 1 hit.
    PROSITEi PS00801. TRANSKETOLASE_1. 1 hit.
    PS00802. TRANSKETOLASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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: October 1, 2014
    This is version 157 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