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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 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co2+.By similarity
  • thiamine diphosphateBy similarityNote: 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
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Calcium, 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
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:25313. TKTL2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: LIFEdb
Complete GO annotation...

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

BgeeiQ9H0I9.
CleanExiHS_TKTL2.
ExpressionAtlasiQ9H0I9. baseline and differential.
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.
GeneTreeiENSGT00390000005240.
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

        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)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:
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.4. human.

Polymorphism databases

DMDMi74717985.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

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.

3D structure databases

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

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiQ9H0I9.

Polymorphism databases

DMDMi74717985.

Proteomic databases

PaxDbiQ9H0I9.
PRIDEiQ9H0I9.

Protocols and materials databases

DNASUi84076.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi84076.
GeneCardsiGC04M164392.
HGNCiHGNC:25313. TKTL2.
HPAiHPA043797.
neXtProtiNX_Q9H0I9.
PharmGKBiPA142670806.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0021.
GeneTreeiENSGT00390000005240.
HOGENOMiHOG000243868.
HOVERGENiHBG004036.
InParanoidiQ9H0I9.
KOiK00615.
OMAiHGADIYQ.
OrthoDBiEOG72RMXF.
PhylomeDBiQ9H0I9.
TreeFamiTF313097.

Enzyme and pathway databases

BRENDAi2.2.1.1. 2681.

Miscellaneous databases

GeneWikiiTKTL2.
GenomeRNAii84076.
NextBioi73287.
PROiQ9H0I9.

Gene expression databases

BgeeiQ9H0I9.
CleanExiHS_TKTL2.
ExpressionAtlasiQ9H0I9. baseline and differential.
GenevestigatoriQ9H0I9.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(2003) [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 (MAY-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(2003) [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(2006) [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: April 1, 2015
This is version 106 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.