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P51854

- TKTL1_HUMAN

UniProt

P51854 - TKTL1_HUMAN

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Protein
Transketolase-like protein 1
Gene
TKTL1, TKR, TKT2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.
Binds 1 thiamine pyrophosphate per subunit By similarity.

Sites

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

Regions

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

GO - Molecular functioni

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

GO - Biological processi

  1. glucose catabolic process Source: ProtInc
  2. thiamine metabolic process Source: ProtInc
Complete GO annotation...

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.3 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

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 1
PRO_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.

Family & Domainsi

Sequence similaritiesi

Belongs to the transketolase family.

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

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.
VSP_022290Add
BLAST
Alternative sequencei467 – 4671K → KGVSMLQDSWSSVISYQK in isoform 2.
VSP_022291

Sequence conflict

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

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]
RefSeqiNP_001139406.1. NM_001145934.1.
NP_036385.3. NM_012253.3. [P51854-3]
UniGeneiHs.102866.

Genome annotation databases

EnsembliENST00000369912; ENSP00000358928; ENSG00000007350.
ENST00000369915; ENSP00000358931; ENSG00000007350. [P51854-3]
ENST00000596987; ENSP00000472763; ENSG00000268013. [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 ]
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 .
ENST00000369915 ; ENSP00000358931 ; ENSG00000007350 . [P51854-3 ]
ENST00000596987 ; ENSP00000472763 ; ENSG00000268013 . [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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 133 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

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