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Q9H0I9

- TKTL2_HUMAN

UniProt

Q9H0I9 - TKTL2_HUMAN

Protein

Transketolase-like protein 2

Gene

TKTL2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Plays an essential role in total transketolase activity and cell proliferation in cancer cells; after transfection with anti-TKTL1 siRNA, total transketolase activity dramatically decreases and proliferation was significantly inhibited in cancer cells. Plays a pivotal role in carcinogenesis.1 Publication

    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+ By similarity.By similarity
    Binds 1 thiamine pyrophosphate per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei41 – 411Thiamine pyrophosphateBy similarity
    Binding sitei78 – 781Thiamine pyrophosphateBy similarity
    Metal bindingi156 – 1561MagnesiumBy similarity
    Binding sitei157 – 1571Thiamine pyrophosphate; via amide nitrogenBy similarity
    Metal bindingi186 – 1861MagnesiumBy similarity
    Binding sitei186 – 1861Thiamine pyrophosphateBy similarity
    Metal bindingi188 – 1881Magnesium; via carbonyl oxygenBy similarity
    Binding sitei248 – 2481Thiamine pyrophosphateBy similarity
    Binding sitei262 – 2621SubstrateBy similarity
    Binding sitei262 – 2621Thiamine pyrophosphateBy similarity
    Sitei262 – 2621Important for catalytic activityBy similarity
    Binding sitei349 – 3491SubstrateBy similarity
    Active sitei370 – 3701Proton donorBy similarity
    Binding sitei370 – 3701Thiamine pyrophosphateBy similarity
    Binding sitei396 – 3961Thiamine pyrophosphateBy similarity
    Binding sitei420 – 4201SubstrateBy similarity
    Binding sitei428 – 4281SubstrateBy similarity
    Binding sitei432 – 4321Thiamine pyrophosphateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi124 – 1263Thiamine pyrophosphateBy similarity

    GO - Molecular functioni

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

    Keywords - Molecular functioni

    Transferase

    Keywords - Ligandi

    Calcium, Magnesium, Metal-binding, Thiamine pyrophosphate

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transketolase-like protein 2 (EC:2.2.1.1)
    Gene namesi
    Name:TKTL2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:25313. TKTL2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: LIFEdb

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142670806.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 626626Transketolase-like protein 2PRO_0000285200Add
    BLAST

    Proteomic databases

    PaxDbiQ9H0I9.
    PRIDEiQ9H0I9.

    PTM databases

    PhosphoSiteiQ9H0I9.

    Expressioni

    Tissue specificityi

    Overexpressed in hepatoma cancer cells.1 Publication

    Gene expression databases

    ArrayExpressiQ9H0I9.
    BgeeiQ9H0I9.
    CleanExiHS_TKTL2.
    GenevestigatoriQ9H0I9.

    Organism-specific databases

    HPAiHPA043797.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi123871. 1 interaction.
    IntActiQ9H0I9. 1 interaction.
    MINTiMINT-1451143.
    STRINGi9606.ENSP00000280605.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H0I9.
    SMRiQ9H0I9. Positions 7-620.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the transketolase family.Curated

    Phylogenomic databases

    eggNOGiCOG0021.
    HOGENOMiHOG000243868.
    HOVERGENiHBG004036.
    InParanoidiQ9H0I9.
    KOiK00615.
    OMAiHGADIYQ.
    OrthoDBiEOG72RMXF.
    PhylomeDBiQ9H0I9.
    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.
    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.

    Sequencei

    Sequence statusi: Complete.

    Q9H0I9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMANDAKPDV KTVQVLRDTA NRLRIHSIRA TCASGSGQLT SCCSAAEVVS    50
    VLFFHTMKYK QTDPEHPDND RFILSRGHAA PILYAAWVEV GDISESDLLN 100
    LRKLHSDLER HPTPRLPFVD VATGSLGQGL GTACGMAYTG KYLDKASYRV 150
    FCLMGDGESS EGSVWEAFAF ASHYNLDNLV AVFDVNRLGQ SGPAPLEHGA 200
    DIYQNCCEAF GWNTYLVDGH DVEALCQAFW QASQVKNKPT AIVAKTFKGR 250
    GIPNIEDAEN WHGKPVPKER ADAIVKLIES QIQTNENLIP KSPVEDSPQI 300
    SITDIKMTSP PAYKVGDKIA TQKTYGLALA KLGRANERVI VLSGDTMNST 350
    FSEIFRKEHP ERFIECIIAE QNMVSVALGC ATRGRTIAFA GAFAAFFTRA 400
    FDQLRMGAIS QANINLIGSH CGVSTGEDGV SQMALEDLAM FRSIPNCTVF 450
    YPSDAISTEH AIYLAANTKG MCFIRTSQPE TAVIYTPQEN FEIGQAKVVR 500
    HGVNDKVTVI GAGVTLHEAL EAADHLSQQG ISVRVIDPFT IKPLDAATII 550
    SSAKATGGRV ITVEDHYREG GIGEAVCAAV SREPDILVHQ LAVSGVPQRG 600
    KTSELLDMFG ISTRHIIAAV TLTLMK 626
    Length:626
    Mass (Da):67,877
    Last modified:March 1, 2001 - v1
    Checksum:i446C4EC81EDC0EA4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti54 – 541F → L in BAB71427. (PubMed:14702039)Curated
    Sequence conflicti302 – 3021I → V in AAH28707. (PubMed:15489334)Curated
    Sequence conflicti311 – 3111P → H in AAH28707. (PubMed:15489334)Curated
    Sequence conflicti406 – 4061M → I in BAB71427. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti442 – 4421R → Q.
    Corresponds to variant rs3811750 [ dbSNP | Ensembl ].
    VAR_031990
    Natural varianti590 – 5901Q → H.1 Publication
    Corresponds to variant rs11735477 [ dbSNP | Ensembl ].
    VAR_031991

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL136779 mRNA. Translation: CAB66713.1.
    AK057325 mRNA. Translation: BAB71427.1.
    CR533560 mRNA. Translation: CAG38591.1.
    BC028707 mRNA. Translation: AAH28707.4.
    BC125101 mRNA. Translation: AAI25102.1.
    BC142943 mRNA. Translation: AAI42944.1.
    CCDSiCCDS3805.1.
    RefSeqiNP_115512.3. NM_032136.4.
    UniGeneiHs.303923.

    Genome annotation databases

    EnsembliENST00000280605; ENSP00000280605; ENSG00000151005.
    GeneIDi84076.
    KEGGihsa:84076.
    UCSCiuc003iqp.4. human.

    Polymorphism databases

    DMDMi74717985.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL136779 mRNA. Translation: CAB66713.1 .
    AK057325 mRNA. Translation: BAB71427.1 .
    CR533560 mRNA. Translation: CAG38591.1 .
    BC028707 mRNA. Translation: AAH28707.4 .
    BC125101 mRNA. Translation: AAI25102.1 .
    BC142943 mRNA. Translation: AAI42944.1 .
    CCDSi CCDS3805.1.
    RefSeqi NP_115512.3. NM_032136.4.
    UniGenei Hs.303923.

    3D structure databases

    ProteinModelPortali Q9H0I9.
    SMRi Q9H0I9. Positions 7-620.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123871. 1 interaction.
    IntActi Q9H0I9. 1 interaction.
    MINTi MINT-1451143.
    STRINGi 9606.ENSP00000280605.

    PTM databases

    PhosphoSitei Q9H0I9.

    Polymorphism databases

    DMDMi 74717985.

    Proteomic databases

    PaxDbi Q9H0I9.
    PRIDEi Q9H0I9.

    Protocols and materials databases

    DNASUi 84076.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000280605 ; ENSP00000280605 ; ENSG00000151005 .
    GeneIDi 84076.
    KEGGi hsa:84076.
    UCSCi uc003iqp.4. human.

    Organism-specific databases

    CTDi 84076.
    GeneCardsi GC04M164392.
    HGNCi HGNC:25313. TKTL2.
    HPAi HPA043797.
    neXtProti NX_Q9H0I9.
    PharmGKBi PA142670806.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0021.
    HOGENOMi HOG000243868.
    HOVERGENi HBG004036.
    InParanoidi Q9H0I9.
    KOi K00615.
    OMAi HGADIYQ.
    OrthoDBi EOG72RMXF.
    PhylomeDBi Q9H0I9.
    TreeFami TF313097.

    Miscellaneous databases

    GeneWikii TKTL2.
    GenomeRNAii 84076.
    NextBioi 73287.
    PROi Q9H0I9.

    Gene expression databases

    ArrayExpressi Q9H0I9.
    Bgeei Q9H0I9.
    CleanExi HS_TKTL2.
    Genevestigatori Q9H0I9.

    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.
    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.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Testis.
    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].
      Tissue: Testis.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "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], VARIANT HIS-590.
      Tissue: Testis.
    5. "Gene silencing of TKTL1 by RNAi inhibits cell proliferation in human hepatoma cells."
      Zhang S., Yang J.-H., Guo C.-K., Cai P.-C.
      Cancer Lett. 253:108-114(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiTKTL2_HUMAN
    AccessioniPrimary (citable) accession number: Q9H0I9
    Secondary accession number(s): A4FVB4, Q8NCT0, Q96M82
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 2007
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 102 of the entry and version 1 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3