TKTL2_HUMAN
ID TKTL2_HUMAN Reviewed; 626 AA.
AC Q9H0I9; A4FVB4; Q8NCT0; Q96M82;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Transketolase-like protein 2;
DE EC=2.2.1.1;
GN Name=TKTL2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-590.
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17321041; DOI=10.1016/j.canlet.2007.01.010;
RA Zhang S., Yang J.-H., Guo C.-K., Cai P.-C.;
RT "Gene silencing of TKTL1 by RNAi inhibits cell proliferation in human
RT hepatoma cells.";
RL Cancer Lett. 253:108-114(2007).
CC -!- FUNCTION: Plays an essential role in total transketolase activity and
CC cell proliferation in cancer cells; after transfection with anti-TKTL1
CC siRNA, total transketolase activity dramatically decreases and
CC proliferation was significantly inhibited in cancer cells. Plays a
CC pivotal role in carcinogenesis. {ECO:0000269|PubMed:17321041}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent
CC metal cations, such as Ca(2+), Mn(2+) and Co(2+). {ECO:0000250};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Overexpressed in hepatoma cancer cells.
CC {ECO:0000269|PubMed:17321041}.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR EMBL; AL136779; CAB66713.1; -; mRNA.
DR EMBL; AK057325; BAB71427.1; -; mRNA.
DR EMBL; CR533560; CAG38591.1; -; mRNA.
DR EMBL; BC028707; AAH28707.4; -; mRNA.
DR EMBL; BC125101; AAI25102.1; -; mRNA.
DR EMBL; BC142943; AAI42944.1; -; mRNA.
DR CCDS; CCDS3805.1; -.
DR RefSeq; NP_115512.3; NM_032136.4.
DR AlphaFoldDB; Q9H0I9; -.
DR SMR; Q9H0I9; -.
DR BioGRID; 123871; 18.
DR IntAct; Q9H0I9; 5.
DR STRING; 9606.ENSP00000280605; -.
DR iPTMnet; Q9H0I9; -.
DR PhosphoSitePlus; Q9H0I9; -.
DR BioMuta; TKTL2; -.
DR DMDM; 74717985; -.
DR jPOST; Q9H0I9; -.
DR MassIVE; Q9H0I9; -.
DR MaxQB; Q9H0I9; -.
DR PaxDb; Q9H0I9; -.
DR PeptideAtlas; Q9H0I9; -.
DR PRIDE; Q9H0I9; -.
DR ProteomicsDB; 80285; -.
DR Antibodypedia; 28268; 138 antibodies from 19 providers.
DR DNASU; 84076; -.
DR Ensembl; ENST00000280605.5; ENSP00000280605.3; ENSG00000151005.5.
DR GeneID; 84076; -.
DR KEGG; hsa:84076; -.
DR MANE-Select; ENST00000280605.5; ENSP00000280605.3; NM_032136.5; NP_115512.3.
DR UCSC; uc003iqp.5; human.
DR CTD; 84076; -.
DR DisGeNET; 84076; -.
DR GeneCards; TKTL2; -.
DR HGNC; HGNC:25313; TKTL2.
DR HPA; ENSG00000151005; Tissue enriched (testis).
DR neXtProt; NX_Q9H0I9; -.
DR OpenTargets; ENSG00000151005; -.
DR PharmGKB; PA142670806; -.
DR VEuPathDB; HostDB:ENSG00000151005; -.
DR eggNOG; KOG0523; Eukaryota.
DR GeneTree; ENSGT00940000161969; -.
DR HOGENOM; CLU_009227_3_0_1; -.
DR InParanoid; Q9H0I9; -.
DR OMA; YAPHTPD; -.
DR OrthoDB; 354970at2759; -.
DR PhylomeDB; Q9H0I9; -.
DR TreeFam; TF313097; -.
DR BRENDA; 2.2.1.1; 2681.
DR PathwayCommons; Q9H0I9; -.
DR SignaLink; Q9H0I9; -.
DR BioGRID-ORCS; 84076; 5 hits in 1063 CRISPR screens.
DR GeneWiki; TKTL2; -.
DR GenomeRNAi; 84076; -.
DR Pharos; Q9H0I9; Tbio.
DR PRO; PR:Q9H0I9; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9H0I9; protein.
DR Bgee; ENSG00000151005; Expressed in adult organism and 24 other tissues.
DR ExpressionAtlas; Q9H0I9; baseline and differential.
DR Genevisible; Q9H0I9; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IBA:GO_Central.
DR GO; GO:0004802; F:transketolase activity; IBA:GO_Central.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR005474; Transketolase_N.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR SUPFAM; SSF52922; SSF52922; 1.
PE 2: Evidence at transcript level;
KW Calcium; Magnesium; Metal-binding; Reference proteome;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..626
FT /note="Transketolase-like protein 2"
FT /id="PRO_0000285200"
FT ACT_SITE 370
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 41
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 124..126
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 370
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 396
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 428
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 432
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT SITE 262
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT VARIANT 442
FT /note="R -> Q (in dbSNP:rs3811750)"
FT /id="VAR_031990"
FT VARIANT 590
FT /note="Q -> H (in dbSNP:rs11735477)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031991"
FT CONFLICT 54
FT /note="F -> L (in Ref. 2; BAB71427)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="I -> V (in Ref. 4; AAH28707)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="P -> H (in Ref. 4; AAH28707)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="M -> I (in Ref. 2; BAB71427)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 626 AA; 67877 MW; 446C4EC81EDC0EA4 CRC64;
MMANDAKPDV KTVQVLRDTA NRLRIHSIRA TCASGSGQLT SCCSAAEVVS VLFFHTMKYK
QTDPEHPDND RFILSRGHAA PILYAAWVEV GDISESDLLN LRKLHSDLER HPTPRLPFVD
VATGSLGQGL GTACGMAYTG KYLDKASYRV FCLMGDGESS EGSVWEAFAF ASHYNLDNLV
AVFDVNRLGQ SGPAPLEHGA DIYQNCCEAF GWNTYLVDGH DVEALCQAFW QASQVKNKPT
AIVAKTFKGR GIPNIEDAEN WHGKPVPKER ADAIVKLIES QIQTNENLIP KSPVEDSPQI
SITDIKMTSP PAYKVGDKIA TQKTYGLALA KLGRANERVI VLSGDTMNST FSEIFRKEHP
ERFIECIIAE QNMVSVALGC ATRGRTIAFA GAFAAFFTRA FDQLRMGAIS QANINLIGSH
CGVSTGEDGV SQMALEDLAM FRSIPNCTVF YPSDAISTEH AIYLAANTKG MCFIRTSQPE
TAVIYTPQEN FEIGQAKVVR HGVNDKVTVI GAGVTLHEAL EAADHLSQQG ISVRVIDPFT
IKPLDAATII SSAKATGGRV ITVEDHYREG GIGEAVCAAV SREPDILVHQ LAVSGVPQRG
KTSELLDMFG ISTRHIIAAV TLTLMK
