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Q9H0I9 (TKTL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transketolase-like protein 2

EC=2.2.1.1
Gene names
Name:TKTL2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length626 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. Ref.5

Catalytic activity

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

Cofactor

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

Binds 1 thiamine pyrophosphate per subunit By similarity.

Subunit structure

Homodimer By similarity.

Tissue specificity

Overexpressed in hepatoma cancer cells. Ref.5

Sequence similarities

Belongs to the transketolase family.

Ontologies

Keywords
   Coding sequence diversityPolymorphism
   LigandCalcium
Magnesium
Metal-binding
Thiamine pyrophosphate
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from direct assay. Source: LIFEdb

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

transketolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 626626Transketolase-like protein 2
PRO_0000285200

Regions

Nucleotide binding124 – 1263Thiamine pyrophosphate By similarity

Sites

Active site3701Proton donor By similarity
Metal binding1561Magnesium By similarity
Metal binding1861Magnesium By similarity
Metal binding1881Magnesium; via carbonyl oxygen By similarity
Binding site411Thiamine pyrophosphate By similarity
Binding site781Thiamine pyrophosphate By similarity
Binding site1571Thiamine pyrophosphate; via amide nitrogen By similarity
Binding site1861Thiamine pyrophosphate By similarity
Binding site2481Thiamine pyrophosphate By similarity
Binding site2621Substrate By similarity
Binding site2621Thiamine pyrophosphate By similarity
Binding site3491Substrate By similarity
Binding site3701Thiamine pyrophosphate By similarity
Binding site3961Thiamine pyrophosphate By similarity
Binding site4201Substrate By similarity
Binding site4281Substrate By similarity
Binding site4321Thiamine pyrophosphate By similarity
Site2621Important for catalytic activity By similarity

Natural variations

Natural variant4421R → Q.
Corresponds to variant rs3811750 [ dbSNP | Ensembl ].
VAR_031990
Natural variant5901Q → H. Ref.4
Corresponds to variant rs11735477 [ dbSNP | Ensembl ].
VAR_031991

Experimental info

Sequence conflict541F → L in BAB71427. Ref.2
Sequence conflict3021I → V in AAH28707. Ref.4
Sequence conflict3111P → H in AAH28707. Ref.4
Sequence conflict4061M → I in BAB71427. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9H0I9 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 446C4EC81EDC0EA4

FASTA62667,877
        10         20         30         40         50         60 
MMANDAKPDV KTVQVLRDTA NRLRIHSIRA TCASGSGQLT SCCSAAEVVS VLFFHTMKYK 

        70         80         90        100        110        120 
QTDPEHPDND RFILSRGHAA PILYAAWVEV GDISESDLLN LRKLHSDLER HPTPRLPFVD 

       130        140        150        160        170        180 
VATGSLGQGL GTACGMAYTG KYLDKASYRV FCLMGDGESS EGSVWEAFAF ASHYNLDNLV 

       190        200        210        220        230        240 
AVFDVNRLGQ SGPAPLEHGA DIYQNCCEAF GWNTYLVDGH DVEALCQAFW QASQVKNKPT 

       250        260        270        280        290        300 
AIVAKTFKGR GIPNIEDAEN WHGKPVPKER ADAIVKLIES QIQTNENLIP KSPVEDSPQI 

       310        320        330        340        350        360 
SITDIKMTSP PAYKVGDKIA TQKTYGLALA KLGRANERVI VLSGDTMNST FSEIFRKEHP 

       370        380        390        400        410        420 
ERFIECIIAE QNMVSVALGC ATRGRTIAFA GAFAAFFTRA FDQLRMGAIS QANINLIGSH 

       430        440        450        460        470        480 
CGVSTGEDGV SQMALEDLAM FRSIPNCTVF YPSDAISTEH AIYLAANTKG MCFIRTSQPE 

       490        500        510        520        530        540 
TAVIYTPQEN FEIGQAKVVR HGVNDKVTVI GAGVTLHEAL EAADHLSQQG ISVRVIDPFT 

       550        560        570        580        590        600 
IKPLDAATII SSAKATGGRV ITVEDHYREG GIGEAVCAAV SREPDILVHQ LAVSGVPQRG 

       610        620 
KTSELLDMFG ISTRHIIAAV TLTLMK 

« Hide

References

« Hide 'large scale' references
[1]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_115512.3. NM_032136.4.
UniGeneHs.303923.

3D structure databases

ProteinModelPortalQ9H0I9.
SMRQ9H0I9. Positions 7-620.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123871. 1 interaction.
IntActQ9H0I9. 1 interaction.
MINTMINT-1451143.
STRING9606.ENSP00000280605.

PTM databases

PhosphoSiteQ9H0I9.

Polymorphism databases

DMDM74717985.

Proteomic databases

PaxDbQ9H0I9.
PRIDEQ9H0I9.

Protocols and materials databases

DNASU84076.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000280605; ENSP00000280605; ENSG00000151005.
GeneID84076.
KEGGhsa:84076.
UCSCuc003iqp.4. human.

Organism-specific databases

CTD84076.
GeneCardsGC04M164392.
HGNCHGNC:25313. TKTL2.
HPAHPA043797.
neXtProtNX_Q9H0I9.
PharmGKBPA142670806.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0021.
HOGENOMHOG000243868.
HOVERGENHBG004036.
InParanoidQ9H0I9.
KOK00615.
OMAHGADIYQ.
OrthoDBEOG72RMXF.
PhylomeDBQ9H0I9.
TreeFamTF313097.

Gene expression databases

ArrayExpressQ9H0I9.
BgeeQ9H0I9.
CleanExHS_TKTL2.
GenevestigatorQ9H0I9.

Family and domain databases

Gene3D3.40.50.920. 1 hit.
InterProIPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
IPR005474. Transketolase_N.
[Graphical view]
PfamPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
PF00456. Transketolase_N. 1 hit.
[Graphical view]
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMSSF52922. SSF52922. 1 hit.
ProtoNetSearch...

Other

GeneWikiTKTL2.
GenomeRNAi84076.
NextBio73287.
PROQ9H0I9.

Entry information

Entry nameTKTL2_HUMAN
AccessionPrimary (citable) accession number: Q9H0I9
Secondary accession number(s): A4FVB4, Q8NCT0, Q96M82
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: March 1, 2001
Last modified: February 19, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM