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Triokinase/FMN cyclase (Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing)) [Includes: ATP-dependent dihydroxyacetone kinase (DHA kinase) (EC 2.7.1.28) (EC 2.7.1.29) (Glycerone kinase) (Triokinase) (Triose kinase); FAD-AMP lyase (cyclizing) (EC 4.6.1.15) (FAD-AMP lyase (cyclic FMN forming)) (FMN cyclase)]

 TKFC_HUMAN              Reviewed;         575 AA.
Q3LXA3; Q2L9C1; Q53EQ9; Q9BVA7; Q9H895;
24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
02-NOV-2010, sequence version 2.
23-MAY-2018, entry version 123.
RecName: Full=Triokinase/FMN cyclase {ECO:0000312|HGNC:HGNC:24552};
AltName: Full=Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing);
Includes:
RecName: Full=ATP-dependent dihydroxyacetone kinase;
Short=DHA kinase;
EC=2.7.1.28;
EC=2.7.1.29;
AltName: Full=Glycerone kinase;
AltName: Full=Triokinase;
AltName: Full=Triose kinase;
Includes:
RecName: Full=FAD-AMP lyase (cyclizing);
EC=4.6.1.15;
AltName: Full=FAD-AMP lyase (cyclic FMN forming);
AltName: Full=FMN cyclase;
Name=TKFC {ECO:0000312|HGNC:HGNC:24552};
Synonyms=DAK {ECO:0000312|HGNC:HGNC:24552};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, FAD-AMP LYASE
ACTIVITY, AND VARIANT THR-185.
TISSUE=Brain;
PubMed=16289032; DOI=10.1016/j.bbrc.2005.10.142;
Cabezas A., Costas M.J., Pinto R.M., Couto A., Cameselle J.C.;
"Identification of human and rat FAD-AMP lyase (cyclic FMN forming) as
ATP-dependent dihydroxyacetone kinases.";
Biochem. Biophys. Res. Commun. 338:1682-1689(2005).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT THR-185, AND
ALTERNATIVE SPLICING.
TISSUE=Brain;
Cabezas A., Costas M.J., Pinto R.M., Couto A., Cameselle J.C.;
"Human brain Dha kinase/FMN cyclase splice variant mRNA encoding a
shorter protein inactive as Dha kinase and FMN cyclase.";
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
THR-185.
TISSUE=Thyroid;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
THR-185.
TISSUE=Kidney;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cervix;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
CATALYTIC ACTIVITY, FUNCTION, IDENTITY OF TRIOKINASE AND
DIHYDROXYACETONE KINASE, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
SPECIFICITY.
PubMed=4688871;
Beutler E., Guinto E.;
"Dihydroxyacetone metabolism by human erythrocytes: demonstration of
triokinase activity and its characterization.";
Blood 41:559-568(1973).
[8]
INTERACTION WITH IFIH1.
PubMed=17600090; DOI=10.1073/pnas.0700544104;
Diao F., Li S., Tian Y., Zhang M., Xu L.G., Zhang Y., Wang R.P.,
Chen D., Zhai Z., Zhong B., Tien P., Shu H.B.;
"Negative regulation of MDA5- but not RIG-I-mediated innate antiviral
signaling by the dihydroxyacetone kinase.";
Proc. Natl. Acad. Sci. U.S.A. 104:11706-11711(2007).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, AND MUTAGENESIS OF
THR-112; LYS-204; HIS-221; ASP-401; ASP-403; CYS-404; SER-446 AND
ASP-556.
PubMed=24569995; DOI=10.1074/jbc.M113.525626;
Rodrigues J.R., Couto A., Cabezas A., Pinto R.M., Ribeiro J.M.,
Canales J., Costas M.J., Cameselle J.C.;
"Bifunctional homodimeric triokinase/FMN cyclase: contribution of
protein domains to the activities of the human enzyme and molecular
dynamics simulation of domain movements.";
J. Biol. Chem. 289:10620-10636(2014).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350 AND SER-511, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Catalyzes both the phosphorylation of dihydroxyacetone
and of glyceraldehyde, and the splitting of ribonucleoside
diphosphate-X compounds among which FAD is the best substrate.
Represses IFIH1-mediated cellular antiviral response
(PubMed:17600090). {ECO:0000250|UniProtKB:F1RKQ4,
ECO:0000250|UniProtKB:Q4KLZ6, ECO:0000269|PubMed:16289032,
ECO:0000269|PubMed:17600090, ECO:0000269|PubMed:4688871}.
-!- CATALYTIC ACTIVITY: ATP + glycerone = ADP + glycerone phosphate.
{ECO:0000269|PubMed:4688871}.
-!- CATALYTIC ACTIVITY: ATP + D-glyceraldehyde = ADP + D-
glyceraldehyde 3-phosphate. {ECO:0000269|PubMed:4688871}.
-!- CATALYTIC ACTIVITY: FAD = AMP + riboflavin cyclic-4',5'-phosphate.
{ECO:0000269|PubMed:4688871}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
Note=Manganese or cobalt are requested for FAD-AMP lyase activity.
{ECO:0000250};
-!- ENZYME REGULATION: Each activity is inhibited by the substrate(s)
of the other.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.5 uM for dihydroxyacetone {ECO:0000269|PubMed:4688871};
KM=11 uM for glyceraldehyde {ECO:0000269|PubMed:4688871};
KM=1.55 uM for dihydroxyacetone {ECO:0000269|PubMed:24569995};
KM=43.2 uM for ATP {ECO:0000269|PubMed:24569995};
KM=18.1 uM for glyceraldehyde {ECO:0000269|PubMed:24569995};
KM=7 uM for FAD {ECO:0000269|PubMed:24569995};
KM=12 uM for ADP-glucose {ECO:0000269|PubMed:24569995};
KM=317 uM for UDP-glucose {ECO:0000269|PubMed:24569995};
KM=263 uM for UDP-galactose {ECO:0000269|PubMed:24569995};
pH dependence:
Optimum pH is 6.6. {ECO:0000269|PubMed:4688871};
-!- SUBUNIT: Homodimer (By similarity). Interacts with IFIH1 (via the
CARD domains), the interaction is inhibited by viral infection
(PubMed:17600090). {ECO:0000250|UniProtKB:F1RKQ4,
ECO:0000269|PubMed:17600090}.
-!- INTERACTION:
Q9BYX4:IFIH1; NbExp=5; IntAct=EBI-4291069, EBI-6115771;
O00560:SDCBP; NbExp=3; IntAct=EBI-4291069, EBI-727004;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q3LXA3-1; Sequence=Displayed;
Name=2;
IsoId=Q3LXA3-2; Sequence=VSP_057181;
Note=Inactive as DHA kinase and FMN cyclase.;
-!- TISSUE SPECIFICITY: Detected in erythrocytes (at protein level).
{ECO:0000269|PubMed:4688871}.
-!- DOMAIN: DhaK and DhaL domains have differential roles,
individually DhaK is inactive and DhaL displays cyclase but not
kinase activity. {ECO:0000269|PubMed:24569995}.
-!- SIMILARITY: Belongs to the dihydroxyacetone kinase (DAK) family.
{ECO:0000305}.
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EMBL; DQ138290; ABA10576.1; -; mRNA.
EMBL; DQ344550; ABC70184.1; -; mRNA.
EMBL; AK023915; BAB14722.1; -; mRNA.
EMBL; AK223580; BAD97300.1; -; mRNA.
EMBL; AP003108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001341; AAH01341.1; -; mRNA.
CCDS; CCDS8003.1; -. [Q3LXA3-1]
RefSeq; NP_056348.2; NM_015533.3. [Q3LXA3-1]
RefSeq; XP_016873010.1; XM_017017521.1.
RefSeq; XP_016873012.1; XM_017017523.1.
UniGene; Hs.6278; -.
ProteinModelPortal; Q3LXA3; -.
SMR; Q3LXA3; -.
BioGrid; 117481; 28.
DIP; DIP-60967N; -.
IntAct; Q3LXA3; 3.
STRING; 9606.ENSP00000378360; -.
iPTMnet; Q3LXA3; -.
PhosphoSitePlus; Q3LXA3; -.
BioMuta; DAK; -.
DMDM; 311033370; -.
REPRODUCTION-2DPAGE; IPI00551024; -.
EPD; Q3LXA3; -.
MaxQB; Q3LXA3; -.
PaxDb; Q3LXA3; -.
PeptideAtlas; Q3LXA3; -.
PRIDE; Q3LXA3; -.
TopDownProteomics; Q3LXA3; -.
DNASU; 26007; -.
Ensembl; ENST00000394900; ENSP00000378360; ENSG00000149476. [Q3LXA3-1]
GeneID; 26007; -.
KEGG; hsa:26007; -.
UCSC; uc001nre.4; human. [Q3LXA3-1]
CTD; 26007; -.
DisGeNET; 26007; -.
EuPathDB; HostDB:ENSG00000149476.14; -.
GeneCards; TKFC; -.
HGNC; HGNC:24552; TKFC.
HPA; HPA039486; -.
HPA; HPA048186; -.
MIM; 615844; gene.
neXtProt; NX_Q3LXA3; -.
OpenTargets; ENSG00000149476; -.
PharmGKB; PA142672014; -.
eggNOG; KOG2426; Eukaryota.
eggNOG; COG2376; LUCA.
GeneTree; ENSGT00390000015415; -.
HOGENOM; HOG000234158; -.
HOVERGEN; HBG079502; -.
InParanoid; Q3LXA3; -.
KO; K00863; -.
OMA; AWPNVAK; -.
PhylomeDB; Q3LXA3; -.
TreeFam; TF313821; -.
BRENDA; 2.7.1.29; 2681.
BRENDA; 4.6.1.15; 2681.
Reactome; R-HSA-168928; DDX58/IFIH1-mediated induction of interferon-alpha/beta.
Reactome; R-HSA-70350; Fructose catabolism.
ChiTaRS; TKFC; human.
GeneWiki; DAK_(gene); -.
GenomeRNAi; 26007; -.
PMAP-CutDB; Q3LXA3; -.
PRO; PR:Q3LXA3; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000149476; -.
CleanEx; HS_DAK; -.
ExpressionAtlas; Q3LXA3; baseline and differential.
Genevisible; Q3LXA3; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005634; C:nucleus; HDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0034012; F:FAD-AMP lyase (cyclizing) activity; IDA:UniProtKB.
GO; GO:0004371; F:glycerone kinase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0050354; F:triokinase activity; IDA:UniProtKB.
GO; GO:0046835; P:carbohydrate phosphorylation; IDA:UniProtKB.
GO; GO:0044262; P:cellular carbohydrate metabolic process; IDA:UniProtKB.
GO; GO:0061624; P:fructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate; TAS:Reactome.
GO; GO:0006071; P:glycerol metabolic process; IEA:InterPro.
GO; GO:0045087; P:innate immune response; TAS:Reactome.
GO; GO:0039534; P:negative regulation of MDA-5 signaling pathway; IDA:UniProtKB.
GO; GO:0045088; P:regulation of innate immune response; IDA:UniProtKB.
Gene3D; 1.25.40.340; -; 1.
InterPro; IPR012734; DhaK_ATP.
InterPro; IPR004006; DhaK_dom.
InterPro; IPR004007; DhaL_dom.
InterPro; IPR036117; DhaL_dom_sf.
Pfam; PF02733; Dak1; 1.
Pfam; PF02734; Dak2; 1.
SMART; SM01120; Dak2; 1.
SUPFAM; SSF101473; SSF101473; 1.
TIGRFAMs; TIGR02361; dak_ATP; 1.
PROSITE; PS51481; DHAK; 1.
PROSITE; PS51480; DHAL; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cobalt; Complete proteome; FAD;
Flavoprotein; Kinase; Lyase; Magnesium; Manganese; Metal-binding;
Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
Polymorphism; Reference proteome; Transferase.
CHAIN 1 575 Triokinase/FMN cyclase.
/FTId=PRO_0000121525.
DOMAIN 9 336 DhaK. {ECO:0000255|PROSITE-
ProRule:PRU00814}.
DOMAIN 372 571 DhaL. {ECO:0000255|PROSITE-
ProRule:PRU00813}.
NP_BIND 401 404 ATP. {ECO:0000250}.
NP_BIND 446 447 ATP. {ECO:0000250}.
NP_BIND 494 495 ATP. {ECO:0000250}.
NP_BIND 556 558 ATP. {ECO:0000250}.
REGION 56 59 Dihydroxyacetone binding. {ECO:0000250}.
ACT_SITE 221 221 Tele-hemiaminal-histidine intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00814}.
BINDING 109 109 Dihydroxyacetone. {ECO:0000255|PROSITE-
ProRule:PRU00814}.
BINDING 114 114 Dihydroxyacetone. {ECO:0000255|PROSITE-
ProRule:PRU00814}.
BINDING 486 486 ATP; via carbonyl oxygen. {ECO:0000250}.
MOD_RES 350 350 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 511 511 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 545 545 Phosphoserine.
{ECO:0000250|UniProtKB:Q4KLZ6}.
VAR_SEQ 526 575 SAEAAAEATKNMEAGAGRASYISSARLEQPDPGAVAAAAIL
RAILEVLQS -> EGGGLVICP (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_057181.
VARIANT 185 185 A -> T (in dbSNP:rs2260655).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:16289032,
ECO:0000269|Ref.2, ECO:0000269|Ref.4}.
/FTId=VAR_028108.
VARIANT 334 334 A -> G (in dbSNP:rs35723406).
/FTId=VAR_054780.
MUTAGEN 112 112 T->A: Highly decreases kinase activity.
No effect on FMN cyclase activity.
{ECO:0000269|PubMed:24569995}.
MUTAGEN 204 204 K->A: Slightly decreases kinase activity.
No effect on FMN cyclase activity.
{ECO:0000269|PubMed:24569995}.
MUTAGEN 221 221 H->A: Abolishes kinase activity but not
FMN cyclase activity.
{ECO:0000269|PubMed:24569995}.
MUTAGEN 401 401 D->A: Abolishes both kinase and FMN
cyclase activities.
{ECO:0000269|PubMed:24569995}.
MUTAGEN 403 403 D->A: Abolishes both kinase and FMN
cyclase activities.
{ECO:0000269|PubMed:24569995}.
MUTAGEN 404 404 C->A: Decreases both kinase and FMN
cyclase activities.
{ECO:0000269|PubMed:24569995}.
MUTAGEN 446 446 S->A: Decreases both kinase and FMN
cyclase activities.
{ECO:0000269|PubMed:24569995}.
MUTAGEN 556 556 D->A: Abolishes both kinase and FMN
cyclase activities.
{ECO:0000269|PubMed:24569995}.
CONFLICT 7 7 V -> A (in Ref. 3; BAB14722).
{ECO:0000305}.
CONFLICT 19 19 A -> S (in Ref. 4; BAD97300).
{ECO:0000305}.
CONFLICT 75 75 V -> A (in Ref. 3; BAB14722).
{ECO:0000305}.
CONFLICT 376 376 L -> P (in Ref. 3; BAB14722).
{ECO:0000305}.
CONFLICT 497 497 D -> G (in Ref. 3; BAB14722).
{ECO:0000305}.
SEQUENCE 575 AA; 58947 MW; 4DB8C5326F65122C CRC64;
MTSKKLVNSV AGCADDALAG LVACNPNLQL LQGHRVALRS DLDSLKGRVA LLSGGGSGHE
PAHAGFIGKG MLTGVIAGAV FTSPAVGSIL AAIRAVAQAG TVGTLLIVKN YTGDRLNFGL
AREQARAEGI PVEMVVIGDD SAFTVLKKAG RRGLCGTVLI HKVAGALAEA GVGLEEIAKQ
VNVVAKAMGT LGVSLSSCSV PGSKPTFELS ADEVELGLGI HGEAGVRRIK MATADEIVKL
MLDHMTNTTN ASHVPVQPGS SVVMMVNNLG GLSFLELGII ADATVRSLEG RGVKIARALV
GTFMSALEMP GISLTLLLVD EPLLKLIDAE TTAAAWPNVA AVSITGRKRS RVAPAEPQEA
PDSTAAGGSA SKRMALVLER VCSTLLGLEE HLNALDRAAG DGDCGTTHSR AARAIQEWLK
EGPPPASPAQ LLSKLSVLLL EKMGGSSGAL YGLFLTAAAQ PLKAKTSLPA WSAAMDAGLE
AMQKYGKAAP GDRTMLDSLW AAGQELQAWK SPGADLLQVL TKAVKSAEAA AEATKNMEAG
AGRASYISSA RLEQPDPGAV AAAAILRAIL EVLQS


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EIAAB24783 GCK family kinase MiNK,Map4k6,MAPK_ERK kinase kinase kinase 6,MEK kinase kinase 6,MEKKK 6,Mink,Mink1,Misshapen_NIK-related kinase,Misshapen-like kinase 1,Mitogen-activated protein kinase kinase kinase
EIAAB24784 GCK family kinase MiNK,Map4k6,MAPK_ERK kinase kinase kinase 6,MEK kinase kinase 6,MEKKK 6,Mink,Mink1,Misshapen_NIK-related kinase,Misshapen-like kinase 1,Mitogen-activated protein kinase kinase kinase
EIAAB25244 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,JNK kinase 2,JNK-activating kinase 2,JNKK 2,MAP kinase kinase 7,Map2k7,MAPK_ERK kinase 7,MAPKK 7,MEK 7,Mkk7,
EIAAB25239 C-JUN N-terminal kinase kinase 1,Dual specificity mitogen-activated protein kinase kinase 4,JNK kinase 1,JNK-activating kinase 1,JNKK 1,Jnkk1,MAP kinase kinase 4,Map2k4,MAPK_ERK kinase 4,MAPKK 4,MEK 4
EIAAB25245 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,JNK kinase 2,JNK-activating kinase 2,JNKK 2,MAP kinase kinase 7,Map2k7,MAPK_ERK kinase 7,MAPKK 7,MEK 7,Rat,R
EIAAB06523 CAK-kinase p42,Ccrk,Cdch,Cdk20,CDK-activating kinase p42,CDK-related protein kinase PNQLARE,Cell cycle-related kinase,Cell division protein kinase 20,Cyclin-dependent kinase 20,Cyclin-dependent protei
EIAAB06524 CAK-kinase p42,CCRK,CDCH,CDK20,CDK-activating kinase p42,Cell cycle-related kinase,Cell division protein kinase 20,Cyclin-dependent kinase 20,Cyclin-dependent protein kinase H,Cyclin-kinase-activating
EIAAB25246 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,Homo sapiens,Human,JNK kinase 2,JNK-activating kinase 2,JNKK 2,JNKK2,MAP kinase kinase 7,MAP2K7,MAPK_ERK kin
YSGKAMCC107E Cyclin Dependent Kinase 2 (cdk2), Cyclin Dependent Kinase 5 (cdk5), NO X w_Cyclin Dependent Kinase (cdk)1, ~33kD, Clone 8A12, Mab anti_Human, Mouse; WB 100 µg.
EIAAB25240 c-Jun N-terminal kinase kinase 1,Dual specificity mitogen-activated protein kinase kinase 4,Homo sapiens,Human,JNK-activating kinase 1,JNKK,JNKK1,MAP kinase kinase 4,MAP2K4,MAPK_ERK kinase 4,MAPKK 4,M
EIAAB06559 CDI1,CDK2-associated dual-specificity phosphatase,CDKN3,CIP2,Cyclin-dependent kinase inhibitor 3,Cyclin-dependent kinase interactor 1,Cyclin-dependent kinase-interacting protein 2,Homo sapiens,Human,K


 

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