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P51854 (TKTL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transketolase-like protein 1

EC=2.2.1.1
Alternative name(s):
Transketolase 2
Short name=TK 2
Transketolase-related protein
Gene names
Name:TKTL1
Synonyms:TKR, TKT2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length596 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

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.

Subcellular location

Cytoplasm. Nucleus. Note: Predominantly cytoplasmic and to a lesser extent also nuclear. Ref.7 Ref.8 Ref.9

Tissue specificity

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. Ref.1 Ref.7 Ref.8 Ref.9

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.

Sequence similarities

Belongs to the transketolase family.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandCalcium
Magnesium
Metal-binding
Thiamine pyrophosphate
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglucose catabolic process

Traceable author statement Ref.1. Source: ProtInc

thiamine metabolic process

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

transketolase activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 3 (identifier: P51854-3)

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.
Isoform 2 (identifier: P51854-1)

Also known as: Brain specific;

The sequence of this isoform differs from the canonical sequence as follows:
     1-56: Missing.
     467-467: K → KGVSMLQDSWSSVISYQK
Isoform 1 (identifier: P51854-2)

Also known as: Heart specific;

The sequence of this isoform is not available.
Note: Lacks the N-terminal.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 596596Transketolase-like protein 1
PRO_0000191899

Regions

Nucleotide binding94 – 963Thiamine pyrophosphate By similarity

Sites

Active site3401Proton donor By similarity
Metal binding1261Magnesium By similarity
Metal binding1561Magnesium By similarity
Metal binding1581Magnesium; via carbonyl oxygen By similarity
Binding site461Substrate By similarity
Binding site491Thiamine pyrophosphate By similarity
Binding site1271Thiamine pyrophosphate; via amide nitrogen By similarity
Binding site1561Thiamine pyrophosphate By similarity
Binding site2181Thiamine pyrophosphate By similarity
Binding site2321Substrate By similarity
Binding site2321Thiamine pyrophosphate By similarity
Binding site2921Substrate By similarity
Binding site3191Substrate By similarity
Binding site3661Thiamine pyrophosphate By similarity
Binding site3901Substrate By similarity
Binding site3981Substrate By similarity
Binding site4021Thiamine pyrophosphate By similarity
Binding site4481Substrate By similarity
Site461Important for catalytic activity By similarity
Site2321Important for catalytic activity By similarity

Natural variations

Alternative sequence1 – 5656Missing in isoform 2.
VSP_022290
Alternative sequence4671K → KGVSMLQDSWSSVISYQK in isoform 2.
VSP_022291
Natural variant241L → F. Ref.3 Ref.5
Corresponds to variant rs17855509 [ dbSNP | Ensembl ].
VAR_029867
Natural variant1521I → T. Ref.5
Corresponds to variant rs17852259 [ dbSNP | Ensembl ].
VAR_029868

Experimental info

Sequence conflict5191I → N in AAA21557. Ref.6
Sequence conflict5321T → S in AAA21557. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 3 [UniParc].

Last modified January 9, 2007. Version 2.
Checksum: F492A902441E2A14

FASTA59665,333
        10         20         30         40         50         60 
MADAEARAEF PEEARPDRGT LQVLQDMASR LRIHSIRATC STSSGHPTSC SSSSEIMSVL 

        70         80         90        100        110        120 
FFYIMRYKQS DPENPDNDRF VLAKRLSFVD VATGWLGQGL GVACGMAYTG KYFDRASYRV 

       130        140        150        160        170        180 
FCLMSDGESS EGSVWEAMAF ASYYSLDNLV AIFDVNRLGH SGALPAEHCI NIYQRRCEAF 

       190        200        210        220        230        240 
GWNTYVVDGR DVEALCQVFW QASQVKHKPT AVVAKTFKGR GTPSIEDAES WHAKPMPRER 

       250        260        270        280        290        300 
ADAIIKLIES QIQTSRNLDP QPPIEDSPEV NITDVRMTSP PDYRVGDKIA TRKACGLALA 

       310        320        330        340        350        360 
KLGYANNRVV VLDGDTRYST FSEIFNKEYP ERFIECFMAE QNMVSVALGC ASRGRTIAFA 

       370        380        390        400        410        420 
STFAAFLTRA FDHIRIGGLA ESNINIIGSH CGVSVGDDGA SQMALEDIAM FRTIPKCTIF 

       430        440        450        460        470        480 
YPTDAVSTEH AVALAANAKG MCFIRTTRPE TMVIYTPQER FEIGQAKVLR HCVSDKVTVI 

       490        500        510        520        530        540 
GAGITVYEAL AAADELSKQD IFIRVIDLFT IKPLDVATIV SSAKATEGRI ITVEDHYPQG 

       550        560        570        580        590 
GIGEAVCAAV SMDPDIQVHS LAVSGVPQSG KSEELLDMYG ISARHIIVAV KCMLLN 

« Hide

Isoform 2 (Brain specific) [UniParc].

Checksum: 3F773DB8469447F7
Show »

FASTA55761,200
Isoform 1 (Heart specific) (Sequence not available).

References

« Hide 'large scale' references
[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. 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] (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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X91817, X91818 mRNA. Translation: CAA62925.1.
AK292261 mRNA. Translation: BAF84950.1.
Z49258 Genomic DNA. Translation: CAH69899.1.
CH471172 Genomic DNA. Translation: EAW72752.1.
BC025382 mRNA. Translation: AAH25382.2.
U14622 Genomic DNA. Translation: AAA21557.1.
RefSeqNP_001139406.1. NM_001145934.1.
NP_036385.3. NM_012253.3.
UniGeneHs.102866.

3D structure databases

ProteinModelPortalP51854.
SMRP51854. Positions 15-591.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4716864.
STRING9606.ENSP00000358931.

PTM databases

PhosphoSiteP51854.

Polymorphism databases

DMDM122066426.

Proteomic databases

PaxDbP51854.
PRIDEP51854.

Protocols and materials databases

DNASU8277.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369915; ENSP00000358931; ENSG00000007350. [P51854-3]
ENST00000596987; ENSP00000472763; ENSG00000268013. [P51854-3]
GeneID8277.
KEGGhsa:8277.
UCSCuc004fkg.3. human. [P51854-3]

Organism-specific databases

CTD8277.
GeneCardsGC0XP153524.
H-InvDBHIX0017149.
HGNCHGNC:11835. TKTL1.
HPACAB032191.
HPA000505.
MIM300044. gene.
neXtProtNX_P51854.
PharmGKBPA36538.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0021.
HOGENOMHOG000243868.
HOVERGENHBG004036.
InParanoidP51854.
KOK00615.
OMADHIRIGG.
PhylomeDBP51854.
TreeFamTF313097.

Enzyme and pathway databases

SABIO-RKP51854.

Gene expression databases

ArrayExpressP51854.
BgeeP51854.
CleanExHS_TKTL1.
GenevestigatorP51854.

Family and domain databases

Gene3D3.40.50.920. 1 hit.
InterProIPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR020826. Transketolase_BS.
IPR005476. Transketolase_C.
IPR005474. Transketolase_N.
[Graphical view]
PfamPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
PF00456. Transketolase_N. 2 hits.
[Graphical view]
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMSSF52922. SSF52922. 1 hit.
PROSITEPS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiTKTL1.
GenomeRNAi8277.
NextBio31045.
PROP51854.
SOURCESearch...

Entry information

Entry nameTKTL1_HUMAN
AccessionPrimary (citable) accession number: P51854
Secondary accession number(s): A8K896, Q5TYJ9, Q8TC75
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 9, 2007
Last modified: April 16, 2014
This is version 129 of the entry and version 2 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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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 X

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