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Protein

Transketolase-like protein 2

Gene

TKTL2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

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

Protein has several cofactor binding sites:
  • Mg2+By similarity, Ca2+By similarity, Mn2+By similarity, Co2+By similarityNote: Binds 1 Mg2+ ion per subunit. Can also utilize other divalent metal cations, such as Ca2+, Mn2+ and Co2+.By similarity
  • thiamine diphosphateBy similarityNote: Binds 1 thiamine pyrophosphate per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei41Thiamine pyrophosphateBy similarity1
Binding sitei78Thiamine pyrophosphateBy similarity1
Metal bindingi156MagnesiumBy similarity1
Binding sitei157Thiamine pyrophosphate; via amide nitrogenBy similarity1
Metal bindingi186MagnesiumBy similarity1
Binding sitei186Thiamine pyrophosphateBy similarity1
Metal bindingi188Magnesium; via carbonyl oxygenBy similarity1
Binding sitei248Thiamine pyrophosphateBy similarity1
Binding sitei262SubstrateBy similarity1
Binding sitei262Thiamine pyrophosphateBy similarity1
Sitei262Important for catalytic activityBy similarity1
Binding sitei349SubstrateBy similarity1
Active sitei370Proton donorBy similarity1
Binding sitei370Thiamine pyrophosphateBy similarity1
Binding sitei396Thiamine pyrophosphateBy similarity1
Binding sitei420SubstrateBy similarity1
Binding sitei428SubstrateBy similarity1
Binding sitei432Thiamine pyrophosphateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi124 – 126Thiamine pyrophosphateBy similarity3

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
LigandCalcium, Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BRENDAi2.2.1.1. 2681.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

EuPathDBiHostDB:ENSG00000151005.4.
HGNCiHGNC:25313. TKTL2.

Subcellular locationi

Pathology & Biotechi

Organism-specific databases

DisGeNETi84076.
OpenTargetsiENSG00000151005.
PharmGKBiPA142670806.

Polymorphism and mutation databases

BioMutaiTKTL2.
DMDMi74717985.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002852001 – 626Transketolase-like protein 2Add BLAST626

Proteomic databases

MaxQBiQ9H0I9.
PaxDbiQ9H0I9.
PeptideAtlasiQ9H0I9.
PRIDEiQ9H0I9.

PTM databases

iPTMnetiQ9H0I9.
PhosphoSitePlusiQ9H0I9.

Expressioni

Tissue specificityi

Overexpressed in hepatoma cancer cells.1 Publication

Gene expression databases

BgeeiENSG00000151005.
CleanExiHS_TKTL2.
ExpressionAtlasiQ9H0I9. baseline and differential.
GenevisibleiQ9H0I9. HS.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi123871. 14 interactors.
IntActiQ9H0I9. 1 interactor.
MINTiMINT-1451143.
STRINGi9606.ENSP00000280605.

Structurei

3D structure databases

ProteinModelPortaliQ9H0I9.
SMRiQ9H0I9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the transketolase family.Curated

Phylogenomic databases

eggNOGiKOG0523. Eukaryota.
COG0021. LUCA.
GeneTreeiENSGT00390000005240.
HOGENOMiHOG000243868.
HOVERGENiHBG004036.
InParanoidiQ9H0I9.
KOiK00615.
OMAiNSGHSGM.
OrthoDBiEOG091G03M5.
PhylomeDBiQ9H0I9.
TreeFamiTF313097.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
InterProiView protein in InterPro
IPR029061. THDP-binding.
IPR009014. Transketo_C/PFOR_II.
IPR005475. Transketolase-like_Pyr-bd.
IPR033248. Transketolase_C.
IPR005474. Transketolase_N.
PfamiView protein in Pfam
PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
PF00456. Transketolase_N. 1 hit.
SMARTiView protein in SMART
SM00861. Transket_pyr. 1 hit.
SUPFAMiSSF52518. SSF52518. 2 hits.
SSF52922. SSF52922. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9H0I9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMANDAKPDV KTVQVLRDTA NRLRIHSIRA TCASGSGQLT SCCSAAEVVS
60 70 80 90 100
VLFFHTMKYK QTDPEHPDND RFILSRGHAA PILYAAWVEV GDISESDLLN
110 120 130 140 150
LRKLHSDLER HPTPRLPFVD VATGSLGQGL GTACGMAYTG KYLDKASYRV
160 170 180 190 200
FCLMGDGESS EGSVWEAFAF ASHYNLDNLV AVFDVNRLGQ SGPAPLEHGA
210 220 230 240 250
DIYQNCCEAF GWNTYLVDGH DVEALCQAFW QASQVKNKPT AIVAKTFKGR
260 270 280 290 300
GIPNIEDAEN WHGKPVPKER ADAIVKLIES QIQTNENLIP KSPVEDSPQI
310 320 330 340 350
SITDIKMTSP PAYKVGDKIA TQKTYGLALA KLGRANERVI VLSGDTMNST
360 370 380 390 400
FSEIFRKEHP ERFIECIIAE QNMVSVALGC ATRGRTIAFA GAFAAFFTRA
410 420 430 440 450
FDQLRMGAIS QANINLIGSH CGVSTGEDGV SQMALEDLAM FRSIPNCTVF
460 470 480 490 500
YPSDAISTEH AIYLAANTKG MCFIRTSQPE TAVIYTPQEN FEIGQAKVVR
510 520 530 540 550
HGVNDKVTVI GAGVTLHEAL EAADHLSQQG ISVRVIDPFT IKPLDAATII
560 570 580 590 600
SSAKATGGRV ITVEDHYREG GIGEAVCAAV SREPDILVHQ LAVSGVPQRG
610 620
KTSELLDMFG ISTRHIIAAV TLTLMK
Length:626
Mass (Da):67,877
Last modified:March 1, 2001 - v1
Checksum:i446C4EC81EDC0EA4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti54F → L in BAB71427 (PubMed:14702039).Curated1
Sequence conflicti302I → V in AAH28707 (PubMed:15489334).Curated1
Sequence conflicti311P → H in AAH28707 (PubMed:15489334).Curated1
Sequence conflicti406M → I in BAB71427 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_031990442R → Q. Corresponds to variant dbSNP:rs3811750Ensembl.1
Natural variantiVAR_031991590Q → H1 PublicationCorresponds to variant dbSNP:rs11735477Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiTKTL2_HUMAN
AccessioniPrimary (citable) accession number: Q9H0I9
Secondary accession number(s): A4FVB4, Q8NCT0, Q96M82
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: March 1, 2001
Last modified: September 27, 2017
This is version 130 of the entry and version 1 of the sequence. See 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