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)

P51854

- TKTL1_HUMAN

UniProt

P51854 - TKTL1_HUMAN

Protein

Transketolase-like protein 1

Gene

TKTL1

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 134 (01 Oct 2014)
      Sequence version 2 (09 Jan 2007)
      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.By similarity

    Catalytic activityi

    Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate.1 Publication

    Cofactori

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei46 – 461SubstrateBy similarity
    Sitei46 – 461Important for catalytic activityBy similarity
    Binding sitei49 – 491Thiamine pyrophosphateBy similarity
    Metal bindingi126 – 1261MagnesiumBy similarity
    Binding sitei127 – 1271Thiamine pyrophosphate; via amide nitrogenBy similarity
    Metal bindingi156 – 1561MagnesiumBy similarity
    Binding sitei156 – 1561Thiamine pyrophosphateBy similarity
    Metal bindingi158 – 1581Magnesium; via carbonyl oxygenBy similarity
    Binding sitei218 – 2181Thiamine pyrophosphateBy similarity
    Binding sitei232 – 2321SubstrateBy similarity
    Binding sitei232 – 2321Thiamine pyrophosphateBy similarity
    Sitei232 – 2321Important for catalytic activityBy similarity
    Binding sitei292 – 2921SubstrateBy similarity
    Binding sitei319 – 3191SubstrateBy similarity
    Active sitei340 – 3401Proton donorBy similarity
    Binding sitei366 – 3661Thiamine pyrophosphateBy similarity
    Binding sitei390 – 3901SubstrateBy similarity
    Binding sitei398 – 3981SubstrateBy similarity
    Binding sitei402 – 4021Thiamine pyrophosphateBy similarity
    Binding sitei448 – 4481SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi94 – 963Thiamine pyrophosphateBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. transketolase activity Source: ProtInc

    GO - Biological processi

    1. glucose catabolic process Source: ProtInc
    2. thiamine metabolic process Source: ProtInc

    Keywords - Molecular functioni

    Transferase

    Keywords - Ligandi

    Calcium, Magnesium, Metal-binding, Thiamine pyrophosphate

    Enzyme and pathway databases

    SABIO-RKP51854.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transketolase-like protein 1 (EC:2.2.1.1)
    Alternative name(s):
    Transketolase 2
    Short name:
    TK 2
    Transketolase-related protein
    Gene namesi
    Name:TKTL1
    Synonyms:TKR, TKT2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:11835. TKTL1.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Predominantly cytoplasmic and to a lesser extent also nuclear.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36538.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 596596Transketolase-like protein 1PRO_0000191899Add
    BLAST

    Proteomic databases

    PaxDbiP51854.
    PRIDEiP51854.

    PTM databases

    PhosphoSiteiP51854.

    Expressioni

    Tissue specificityi

    Expressed in fetal and adult heart, brain, lung, liver, and kidney, and in adult placenta, skeletal muscle and pancreas. Up-regulated in various epithelial tumors.4 Publications

    Gene expression databases

    ArrayExpressiP51854.
    BgeeiP51854.
    CleanExiHS_TKTL1.
    GenevestigatoriP51854.

    Organism-specific databases

    HPAiCAB032191.
    HPA000505.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    MINTiMINT-4716864.
    STRINGi9606.ENSP00000358931.

    Structurei

    3D structure databases

    ProteinModelPortaliP51854.
    SMRiP51854. Positions 15-591.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the transketolase family.Curated

    Phylogenomic databases

    eggNOGiCOG0021.
    HOGENOMiHOG000243868.
    HOVERGENiHBG004036.
    InParanoidiP51854.
    KOiK00615.
    OMAiIFNKEYP.
    PhylomeDBiP51854.
    TreeFamiTF313097.

    Family and domain databases

    Gene3Di3.40.50.920. 1 hit.
    3.40.50.970. 3 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. 2 hits.
    [Graphical view]
    SMARTiSM00861. Transket_pyr. 1 hit.
    [Graphical view]
    SUPFAMiSSF52518. SSF52518. 2 hits.
    SSF52922. SSF52922. 1 hit.
    PROSITEiPS00802. TRANSKETOLASE_2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 3 (identifier: P51854-3) [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

    MADAEARAEF PEEARPDRGT LQVLQDMASR LRIHSIRATC STSSGHPTSC    50
    SSSSEIMSVL FFYIMRYKQS DPENPDNDRF VLAKRLSFVD VATGWLGQGL 100
    GVACGMAYTG KYFDRASYRV FCLMSDGESS EGSVWEAMAF ASYYSLDNLV 150
    AIFDVNRLGH SGALPAEHCI NIYQRRCEAF GWNTYVVDGR DVEALCQVFW 200
    QASQVKHKPT AVVAKTFKGR GTPSIEDAES WHAKPMPRER ADAIIKLIES 250
    QIQTSRNLDP QPPIEDSPEV NITDVRMTSP PDYRVGDKIA TRKACGLALA 300
    KLGYANNRVV VLDGDTRYST FSEIFNKEYP ERFIECFMAE QNMVSVALGC 350
    ASRGRTIAFA STFAAFLTRA FDHIRIGGLA ESNINIIGSH CGVSVGDDGA 400
    SQMALEDIAM FRTIPKCTIF YPTDAVSTEH AVALAANAKG MCFIRTTRPE 450
    TMVIYTPQER FEIGQAKVLR HCVSDKVTVI GAGITVYEAL AAADELSKQD 500
    IFIRVIDLFT IKPLDVATIV SSAKATEGRI ITVEDHYPQG GIGEAVCAAV 550
    SMDPDIQVHS LAVSGVPQSG KSEELLDMYG ISARHIIVAV KCMLLN 596
    Length:596
    Mass (Da):65,333
    Last modified:January 9, 2007 - v2
    Checksum:iF492A902441E2A14
    GO
    Isoform 2 (identifier: P51854-1) [UniParc]FASTAAdd to Basket

    Also known as: Brain specific

    The sequence of this isoform differs from the canonical sequence as follows:
         1-56: Missing.
         467-467: K → KGVSMLQDSWSSVISYQK

    Show »
    Length:557
    Mass (Da):61,200
    Checksum:i3F773DB8469447F7
    GO
    Isoform 1 (identifier: P51854-2)

    Also known as: Heart specific

    Sequence is not available

    Note: Lacks the N-terminal.

    Length:
    Mass (Da):
    Isoform 4 (identifier: P51854-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-56: Missing.

    Note: No experimental confirmation available. Gene prediction based on partial EST data.

    Show »
    Length:540
    Mass (Da):59,303
    Checksum:i8F68BE950479A611
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti519 – 5191I → N in AAA21557. 1 PublicationCurated
    Sequence conflicti532 – 5321T → S in AAA21557. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti24 – 241L → F.2 Publications
    Corresponds to variant rs17855509 [ dbSNP | Ensembl ].
    VAR_029867
    Natural varianti152 – 1521I → T.1 Publication
    Corresponds to variant rs17852259 [ dbSNP | Ensembl ].
    VAR_029868

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5656Missing in isoform 2 and isoform 4. 1 PublicationVSP_022290Add
    BLAST
    Alternative sequencei467 – 4671K → KGVSMLQDSWSSVISYQK in isoform 2. 1 PublicationVSP_022291

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91817, X91818 mRNA. Translation: CAA62925.1.
    AK292261 mRNA. Translation: BAF84950.1.
    BX664723 Genomic DNA. No translation available.
    Z49258 Genomic DNA. Translation: CAH69899.1.
    Z49258 Genomic DNA. Translation: CAH69900.1.
    CH471172 Genomic DNA. Translation: EAW72752.1.
    BC025382 mRNA. Translation: AAH25382.2.
    U14622 Genomic DNA. Translation: AAA21557.1.
    CCDSiCCDS35448.1. [P51854-3]
    CCDS55541.1. [P51854-4]
    RefSeqiNP_001139406.1. NM_001145934.1.
    NP_036385.3. NM_012253.3. [P51854-3]
    UniGeneiHs.102866.

    Genome annotation databases

    EnsembliENST00000369912; ENSP00000358928; ENSG00000007350. [P51854-4]
    ENST00000369915; ENSP00000358931; ENSG00000007350. [P51854-3]
    GeneIDi8277.
    KEGGihsa:8277.
    UCSCiuc004fkg.3. human. [P51854-3]

    Polymorphism databases

    DMDMi122066426.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91817 , X91818 mRNA. Translation: CAA62925.1 .
    AK292261 mRNA. Translation: BAF84950.1 .
    BX664723 Genomic DNA. No translation available.
    Z49258 Genomic DNA. Translation: CAH69899.1 .
    Z49258 Genomic DNA. Translation: CAH69900.1 .
    CH471172 Genomic DNA. Translation: EAW72752.1 .
    BC025382 mRNA. Translation: AAH25382.2 .
    U14622 Genomic DNA. Translation: AAA21557.1 .
    CCDSi CCDS35448.1. [P51854-3 ]
    CCDS55541.1. [P51854-4 ]
    RefSeqi NP_001139406.1. NM_001145934.1.
    NP_036385.3. NM_012253.3. [P51854-3 ]
    UniGenei Hs.102866.

    3D structure databases

    ProteinModelPortali P51854.
    SMRi P51854. Positions 15-591.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-4716864.
    STRINGi 9606.ENSP00000358931.

    PTM databases

    PhosphoSitei P51854.

    Polymorphism databases

    DMDMi 122066426.

    Proteomic databases

    PaxDbi P51854.
    PRIDEi P51854.

    Protocols and materials databases

    DNASUi 8277.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369912 ; ENSP00000358928 ; ENSG00000007350 . [P51854-4 ]
    ENST00000369915 ; ENSP00000358931 ; ENSG00000007350 . [P51854-3 ]
    GeneIDi 8277.
    KEGGi hsa:8277.
    UCSCi uc004fkg.3. human. [P51854-3 ]

    Organism-specific databases

    CTDi 8277.
    GeneCardsi GC0XP153524.
    H-InvDB HIX0017149.
    HGNCi HGNC:11835. TKTL1.
    HPAi CAB032191.
    HPA000505.
    MIMi 300044. gene.
    neXtProti NX_P51854.
    PharmGKBi PA36538.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0021.
    HOGENOMi HOG000243868.
    HOVERGENi HBG004036.
    InParanoidi P51854.
    KOi K00615.
    OMAi IFNKEYP.
    PhylomeDBi P51854.
    TreeFami TF313097.

    Enzyme and pathway databases

    SABIO-RK P51854.

    Miscellaneous databases

    GeneWikii TKTL1.
    GenomeRNAii 8277.
    NextBioi 31045.
    PROi P51854.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P51854.
    Bgeei P51854.
    CleanExi HS_TKTL1.
    Genevestigatori P51854.

    Family and domain databases

    Gene3Di 3.40.50.920. 1 hit.
    3.40.50.970. 3 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. 2 hits.
    [Graphical view ]
    SMARTi SM00861. Transket_pyr. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52518. SSF52518. 2 hits.
    SSF52922. SSF52922. 1 hit.
    PROSITEi PS00802. TRANSKETOLASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of tissue-specific transcripts of a transketolase-related gene: implications for the evolution of new vertebrate genes."
      Coy J.F., Duebel S., Kioschis P., Thomas K., Micklem G., Delius H., Poustka A.
      Genomics 32:309-316(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
      Tissue: Fetal brain.
    2. "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] (ISOFORM 3).
      Tissue: Testis.
    3. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PHE-24.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 3), VARIANTS PHE-24 AND THR-152.
      Tissue: Testis.
    6. Hochgeschwender U.
      Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 475-537 (ISOFORMS 1/2).
    7. "Mutations in the transketolase-like gene TKTL1: clinical implications for neurodegenerative diseases, diabetes and cancer."
      Coy J.F., Dressler D., Wilde J., Schubert P.
      Clin. Lab. 51:257-273(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    8. "Expression of transketolase TKTL1 predicts colon and urothelial cancer patient survival: Warburg effect reinterpreted."
      Langbein S., Zerilli M., Zur Hausen A., Staiger W., Rensch-Boschert K., Lukan N., Popa J., Ternullo M.P., Steidler A., Weiss C., Grobholz R., Willeke F., Alken P., Stassi G., Schubert P., Coy J.F.
      Br. J. Cancer 94:578-585(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    9. "Expression of the mutated transketolase TKTL1, a molecular marker in gastric cancer."
      Staiger W.I., Coy J.F., Grobholz R., Hofheinz R.-D., Lukan N., Post S., Schwarzbach M.H., Willeke F.
      Oncol. Rep. 16:657-661(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiTKTL1_HUMAN
    AccessioniPrimary (citable) accession number: P51854
    Secondary accession number(s): A8K896
    , Q5TYJ8, Q5TYJ9, Q8TC75
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 9, 2007
    Last modified: October 1, 2014
    This is version 134 of the entry and version 2 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

    Miscellaneous

    Strong TKTL1 protein expression has been correlated with a certain type of glucose metabolism (aerobic glycolysis; Warburg effect) and to cells which are affected by chronic complications of diabetic patients.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3