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Dapper homolog 1 (Dapper antagonist of catenin 1) (Frodo homolog) (MDpr1) (Thymus-expressed novel gene 3 protein)

 DACT1_MOUSE             Reviewed;         778 AA.
Q8R4A3; Q80VG9; Q8BP49; Q9JK89;
15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
17-JUN-2020, entry version 131.
RecName: Full=Dapper homolog 1;
AltName: Full=Dapper antagonist of catenin 1;
AltName: Full=Frodo homolog;
AltName: Full=MDpr1;
AltName: Full=Thymus-expressed novel gene 3 protein;
Name=Dact1; Synonyms=Thyex3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Cerebellum;
PubMed=11970895; DOI=10.1016/s1534-5807(02)00140-5;
Cheyette B.N.R., Waxman J.S., Miller J.R., Takemaru K., Sheldahl L.C.,
Khlebtsova N., Fox E.P., Earnest T.N., Moon R.T.;
"Dapper, a Dishevelled-associated antagonist of beta-catenin and JNK
signaling, is required for notochord formation.";
Dev. Cell 2:449-461(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 17-511, AND DEVELOPMENTAL STAGE.
STRAIN=FVB/N;
PubMed=16278878; DOI=10.1002/dvdy.20609;
Hunter N.L., Hikasa H., Dymecki S.M., Sokol S.Y.;
"Vertebrate homologues of Frodo are dynamically expressed during embryonic
development in tissues undergoing extensive morphogenetic movements.";
Dev. Dyn. 235:279-284(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 96-778.
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 189-778.
Gong S., Qian X., Fu W., Chen W.;
"Cloning of a murine cDNA and its human homolog encoding transcription
factor-like proteins.";
Zhongguo Sheng Wu Hua Xue Yu Fen Zi Sheng Wu Xue Bao 17:280-287(2001).
[5]
INTERACTION WITH DVL1, AND DOMAIN.
PubMed=14636582; DOI=10.1016/s1097-2765(03)00427-1;
Wong H.C., Bourdelas A., Krauss A., Lee H.J., Shao Y., Wu D., Mlodzik M.,
Shi D.L., Zheng J.;
"Direct binding of the PDZ domain of Dishevelled to a conserved internal
sequence in the C-terminal region of Frizzled.";
Mol. Cell 12:1251-1260(2003).
[6]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=16881060; DOI=10.1002/dvdy.20917;
Fisher D.A., Kivimaee S., Hoshino J., Suriben R., Martin P.-M., Baxter N.,
Cheyette B.N.R.;
"Three Dact gene family members are expressed during embryonic development
and in the adult brains of mice.";
Dev. Dyn. 235:2620-2630(2006).
[7]
FUNCTION.
PubMed=17197390; DOI=10.1096/fj.06-6246com;
Su Y., Zhang L., Gao X., Meng F., Wen J., Zhou H., Meng A., Chen Y.-G.;
"The evolutionally conserved activity of Dapper2 in antagonizing TGF-beta
signaling.";
FASEB J. 21:682-690(2007).
[8]
FUNCTION.
PubMed=19073771; DOI=10.2337/db08-1180;
Lagathu C., Christodoulides C., Virtue S., Cawthorn W.P., Franzin C.,
Kimber W.A., Nora E.D., Campbell M., Medina-Gomez G., Cheyette B.N.,
Vidal-Puig A.J., Sethi J.K.;
"Dact1, a nutritionally regulated preadipocyte gene, controls adipogenesis
by coordinating the Wnt/beta-catenin signaling network.";
Diabetes 58:609-619(2009).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=19701191; DOI=10.1038/ng.435;
Suriben R., Kivimae S., Fisher D.A., Moon R.T., Cheyette B.N.;
"Posterior malformations in Dact1 mutant mice arise through misregulated
Vangl2 at the primitive streak.";
Nat. Genet. 41:977-985(2009).
[10]
FUNCTION, INTERACTION WITH DVL2 AND VANGL2, AND DISRUPTION PHENOTYPE.
PubMed=20145239; DOI=10.1074/jbc.m109.085381;
Wen J., Chiang Y.J., Gao C., Xue H., Xu J., Ning Y., Hodes R.J., Gao X.,
Chen Y.G.;
"Loss of Dact1 disrupts planar cell polarity signaling by altering
dishevelled activity and leads to posterior malformation in mice.";
J. Biol. Chem. 285:11023-11030(2010).
[11]
PHOSPHORYLATION, SELF-ASSOCIATION, AND INTERACTION WITH DACT2; DACT3;
CSNK1D; CSNK2A1; PKA; PKC; CSNK2B; GSK3B; DVL1; DLV2; DVL3; VANGL1; VANGL2;
CTNND1 AND HDAC1.
PubMed=21718540; DOI=10.1186/1471-2091-12-33;
Kivimae S., Yang X.Y., Cheyette B.N.;
"All Dact (Dapper/Frodo) scaffold proteins dimerize and exhibit conserved
interactions with Vangl, Dvl, and serine/threonine kinases.";
BMC Biochem. 12:33-33(2011).
[12]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20335472; DOI=10.1523/jneurosci.0354-10.2010;
Okerlund N.D., Kivimae S., Tong C.K., Peng I.F., Ullian E.M.,
Cheyette B.N.;
"Dact1 is a postsynaptic protein required for dendrite, spine, and
excitatory synapse development in the mouse forebrain.";
J. Neurosci. 30:4362-4368(2010).
-!- FUNCTION: Involved in regulation of intracellular signaling pathways
during development. Specifically thought to play a role in canonical
and/or non-canonical Wnt signaling pathways through interaction with
DSH (Dishevelled) family proteins. The activation/inhibition of Wnt
signaling may depend on the phosphorylation status. Proposed to
regulate the degradation of CTNNB1/beta-catenin, thereby modulating the
transcriptional activation of target genes of the Wnt signaling
pathway. Its function in stabilizing CTNNB1 may involve inhibition of
GSK3B activity. Promotes the membrane localization of CTNNB1. The
cytoplasmic form can induce DVL2 degradation via a lysosome-dependent
mechanism; the function is inhibited by PKA-induced binding to 14-3-3
proteins, such as YWHAB (By similarity). Seems to be involved in
morphogenesis at the primitive streak by regulating VANGL2 and DVL2;
the function seems to be independent of canonical Wnt signaling and
rather involves the non-canonical Wnt/planar cell polarity (PCP)
pathway. The nuclear form may prevent the formation of LEF1:CTNNB1
complex and recruit HDAC1 to LEF1 at target gene promoters to repress
transcription thus antagonizing Wnt signaling (By similarity). May be
involved in positive regulation of fat cell differentiation. During
neuronal differentiation may be involved in excitatory synapse
organization, and dendrite formation and establishment of spines.
{ECO:0000250, ECO:0000269|PubMed:17197390, ECO:0000269|PubMed:19073771,
ECO:0000269|PubMed:19701191, ECO:0000269|PubMed:20145239,
ECO:0000269|PubMed:20335472}.
-!- SUBUNIT: Can form homodimers and heterodimers with DACT2 or DACT3.
Interacts with CSNK1D, PKA catalytic subunit, PKC-type kinase, CSNK2A1,
CSNK2B, DVL1, DLV2, DVAL3, VANGL1, VANGL2, CTNND1 and HDAC1. Interacts
with GSK3B; the interaction is indicative for an association of DACT1
with the beta-catenin destruction complex. Interacts with GSK3A.
Interacts with YWHAB; the interaction is enhanced by PKA
phosphorylating DACT1 at Ser-769. Interacts with CTNNB1 (By
similarity). {ECO:0000250}.
-!- INTERACTION:
Q8R4A3; Q0PHV7: Dact3; NbExp=2; IntAct=EBI-3870250, EBI-6392520;
Q8R4A3; P51141: Dvl1; NbExp=4; IntAct=EBI-3870250, EBI-1538407;
Q8R4A3; Q60838: Dvl2; NbExp=3; IntAct=EBI-3870250, EBI-641940;
Q8R4A3; Q91ZD4: Vangl2; NbExp=3; IntAct=EBI-3870250, EBI-1750744;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Cell junction, synapse {ECO:0000269|PubMed:20335472}. Note=Shuttles
between the nucleus and the cytoplasm. Seems to be nuclear in the
absence of Wnt signaling and to translocate to the cytoplasm in its
presence (By similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in multiple tissues including brain,
heart, kidney, liver and testis. {ECO:0000269|PubMed:11970895,
ECO:0000269|PubMed:16881060}.
-!- DEVELOPMENTAL STAGE: Expression strongly increases from 9.5 dpc, peaks
between 11.5 dpc and 13.5 dpc and diminishes slowly thereafter.
Expressed in the somites during segmentation, limb bud mesenchyme, and
developing central nervous system. Expressed in primitive streak
mesoderm, neuroectoderm, neural crest, presomitic mesoderm and somites.
{ECO:0000269|PubMed:16278878, ECO:0000269|PubMed:16881060}.
-!- DOMAIN: The C-terminal PDZ-binding motif mediates interaction with the
PDZ domains of DSH (Dishevelled) family proteins.
{ECO:0000269|PubMed:14636582}.
-!- DISRUPTION PHENOTYPE: Mice die within a day of birth with malformations
involving the spine, genitourinary system and distal digestive tract
due to disrupted germ-layer morphogenesis at the primitive streak where
cells undergo an epithelial-mesenchymal transition. Urogenital defects
due to impaired hindgut formation start at embryonic day 8.25. Dvl2 and
Vangl2 are found increased at the primitive streak, associated with
abnormal distribution of E-cadherin. {ECO:0000269|PubMed:19701191,
ECO:0000269|PubMed:20145239}.
-!- SIMILARITY: Belongs to the dapper family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF65568.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
Sequence=BAC36958.1; Type=Frameshift; Evidence={ECO:0000305};
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EMBL; AF488775; AAM12547.1; -; mRNA.
EMBL; AY208970; AAO49712.1; -; mRNA.
EMBL; AK077691; BAC36958.1; ALT_SEQ; mRNA.
EMBL; AF251078; AAF65568.1; ALT_INIT; mRNA.
CCDS; CCDS25963.1; -.
RefSeq; NP_067507.2; NM_021532.4.
IntAct; Q8R4A3; 20.
STRING; 10090.ENSMUSP00000117169; -.
iPTMnet; Q8R4A3; -.
PhosphoSitePlus; Q8R4A3; -.
PaxDb; Q8R4A3; -.
PRIDE; Q8R4A3; -.
Antibodypedia; 66; 146 antibodies.
Ensembl; ENSMUST00000061273; ENSMUSP00000058943; ENSMUSG00000044548.
GeneID; 59036; -.
KEGG; mmu:59036; -.
UCSC; uc007nup.2; mouse.
CTD; 51339; -.
MGI; MGI:1891740; Dact1.
eggNOG; ENOG410IGBZ; Eukaryota.
eggNOG; ENOG4110UQH; LUCA.
GeneTree; ENSGT00950000183181; -.
HOGENOM; CLU_021211_1_0_1; -.
InParanoid; Q8R4A3; -.
KO; K22154; -.
PhylomeDB; Q8R4A3; -.
Reactome; R-MMU-4641258; Degradation of DVL.
BioGRID-ORCS; 59036; 0 hits in 12 CRISPR screens.
PRO; PR:Q8R4A3; -.
Proteomes; UP000000589; Chromosome 12.
RNAct; Q8R4A3; protein.
Bgee; ENSMUSG00000044548; Expressed in presomitic mesoderm and 278 other tissues.
ExpressionAtlas; Q8R4A3; baseline and differential.
Genevisible; Q8R4A3; MM.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
GO; GO:0008013; F:beta-catenin binding; ISS:UniProtKB.
GO; GO:0070097; F:delta-catenin binding; IDA:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
GO; GO:0051018; F:protein kinase A binding; IDA:UniProtKB.
GO; GO:0005080; F:protein kinase C binding; IDA:UniProtKB.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; ISO:MGI.
GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
GO; GO:0048619; P:embryonic hindgut morphogenesis; IMP:UniProtKB.
GO; GO:0048598; P:embryonic morphogenesis; IMP:MGI.
GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI.
GO; GO:1904864; P:negative regulation of beta-catenin-TCF complex assembly; ISO:MGI.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:MGI.
GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
GO; GO:0046329; P:negative regulation of JNK cascade; IDA:UniProtKB.
GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IDA:UniProtKB.
GO; GO:0021915; P:neural tube development; ISO:MGI.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
GO; GO:1903364; P:positive regulation of cellular protein catabolic process; ISO:MGI.
GO; GO:0045600; P:positive regulation of fat cell differentiation; IMP:MGI.
GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISS:UniProtKB.
GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
GO; GO:0030111; P:regulation of Wnt signaling pathway; IBA:GO_Central.
GO; GO:2000095; P:regulation of Wnt signaling pathway, planar cell polarity pathway; IMP:UniProtKB.
GO; GO:0050808; P:synapse organization; IMP:MGI.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
InterPro; IPR024848; Dact1.
InterPro; IPR024843; Dapper.
PANTHER; PTHR15919; PTHR15919; 2.
PANTHER; PTHR15919:SF12; PTHR15919:SF12; 2.
Pfam; PF15268; Dapper; 2.
1: Evidence at protein level;
Cell junction; Coiled coil; Cytoplasm; Developmental protein; Neurogenesis;
Nucleus; Phosphoprotein; Reference proteome; Synapse;
Wnt signaling pathway.
CHAIN 1..778
/note="Dapper homolog 1"
/id="PRO_0000191354"
REGION 85..149
/note="Required for self-association"
COILED 85..149
/evidence="ECO:0000255"
MOTIF 125..134
/note="Nuclear export signal"
/evidence="ECO:0000250"
MOTIF 551..564
/note="Bipartite nuclear localization signal"
/evidence="ECO:0000250"
MOTIF 768..778
/note="PDZ-binding"
MOD_RES 769
/note="Phosphoserine; by PKA"
/evidence="ECO:0000250|UniProtKB:Q9NYF0"
CONFLICT 18..19
/note="AE -> SN (in Ref. 2; AAO49712)"
/evidence="ECO:0000305"
CONFLICT 333
/note="C -> F (in Ref. 2; AAO49712)"
/evidence="ECO:0000305"
CONFLICT 343
/note="G -> V (in Ref. 4; AAF65568)"
/evidence="ECO:0000305"
CONFLICT 430
/note="M -> I (in Ref. 2; AAO49712)"
/evidence="ECO:0000305"
CONFLICT 510
/note="A -> G (in Ref. 4; AAF65568)"
/evidence="ECO:0000305"
CONFLICT 511
/note="R -> S (in Ref. 2; AAO49712)"
/evidence="ECO:0000305"
CONFLICT 681
/note="V -> G (in Ref. 4; AAF65568)"
/evidence="ECO:0000305"
SEQUENCE 778 AA; 84306 MW; 31EAD7E9BBA77DE7 CRC64;
MKPDAAREPE PLSPGRGAEA EGRWRERGEA DTERQRTRER QEATLAGLAE LGYLRQRQEL
LVRGALRCSG TVGTVAPRSG ELRGDAAQRS RLEEKFLEEN ILLLRRQLNC LRRRDAGLLN
QLQELDKQIS DLRLDVEKTS EEHLETDSRP SSGFYELSDG ASGSLSNSSN SVFSECLSSC
HSSTCFCSPL EAALTISDGC PKSADVNPKY QCDLVSKNGN DVYRYPSPLH AVAVQSPMFL
LCLTGNTLRE EEGLGSHASD ICIGSELNAT KTDNSLPSPS SLWSASHPAS SKKMDGYILS
LVQKKTHPVR TNKPRTSVNA DPTKGLLRNG SVCVRAPSGV PPGSSVNFKN TKQMCLPAGG
ITSLENGPFS PPKQRSKDSK TDQLESKRLA LPESCSAGAA MEPQSKHVPK AAKAASQELT
RCQAGLGESM KESNQASAVS PKTSPGRGPV APAESKALQL PKKMSQKNSL QAVPALDRPA
LDFKSEGSSQ SLEEGHLVKA QFIPGQQAAA RPHRAHRNPG VARSATLKAR GQAAMEHGLP
TVREKPRAAG KKCRFPDDSD TNKKFRKTSA KGRRSGGLQD AGLPGRALGT GGHRAGSRAH
AHGREPVVAK PKHKRTDYRR WKSSAEVSYE EALRRARRAR REHGAAYRVA VALPYASPYA
YVPSDSEYSA ECESLFHSTV VDTSEDEQSN YTTNCFGDSE SSVSEGDFVG ESTTTSDSEE
SGGLIWSQFV QTLPIQTVTA PDLHTRPTKT FVKIKASHNL KKKILRFRSG SLKLMTTV


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WP1012: IL-7 Signaling Pathway
WP1625: Base excision repair
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WP215: noncanonical wnt pathway
WP800: IL-3 Signaling Pathway
WP1374: Id Signaling Pathway
WP1694: Pyrimidine metabolism
WP1049: G Protein Signaling Pathways
WP1654: gamma-Hexachlorocyclohexane degradation
WP355: IL-1 Signaling Pathway
WP1131: IL-7 Signaling Pathway
WP1661: Glyoxylate and dicarboxylate metabolism
WP2218: sGC
WP818: IL-4 signaling Pathway
WP1449: Regulation of toll-like receptor signaling pathway
WP1714: Tyrosine metabolism
WP913: IL-3 Signaling Pathway
WP1531: Vitamin D synthesis

Related Genes :
[Dact1 Thyex3] Dapper homolog 1 (Dapper antagonist of catenin 1) (Frodo homolog) (MDpr1) (Thymus-expressed novel gene 3 protein)
[DACT1 DPR1 HNG3] Dapper homolog 1 (hDPR1) (Dapper antagonist of catenin 1) (Hepatocellular carcinoma novel gene 3 protein)
[Dact2 Dpr2 Frd2] Dapper homolog 2 (mDpr2) (Dapper antagonist of catenin 2)
[Dact3] Dapper homolog 3 (Dapper antagonist of catenin 3)
[DACT3 RRR1] Dapper homolog 3 (Antagonist of beta-catenin Dapper homolog 3) (Arginine-rich region 1 protein) (Dapper antagonist of catenin 3)
[dact2 dpr2 frd2 zgc:152832] Dapper homolog 2 (Frodo 2)
[dact1-a] Dapper 1-A (Dapper1b) (XDpr1b) (Functional regulator of dsh in ontogenesis) (Frodo)
[DACT2 C6orf116 PP13671] Dapper homolog 2 (Dapper antagonist of catenin 2)
[dact1 dpr1 frd1] Dapper homolog 1 (Frodo 1)
[dact1-b] Dapper 1-B (xDpr) (Dapper1a) (XDpr1a)
[dvl2 dsh] Segment polarity protein dishevelled homolog DVL-2 (Dishevelled-2) (DSH homolog 2) (Xdsh)
[Dmbx1 Cdmx Mbx Otx3 PaxB] Diencephalon/mesencephalon homeobox protein 1 (Diencephalon/mesencephalon-expressed brain homeobox gene 1 protein) (Orthodenticle homolog 3) (Paired-like homeobox protein DMBX1) (Paired-type homeobox Atx)
[IL36RN FIL1D IL1F5 IL1HY1 IL1L1 IL1RP3 UNQ1896/PRO4342] Interleukin-36 receptor antagonist protein (IL-36Ra) (FIL1 delta) (IL-1-related protein 3) (IL-1RP3) (Interleukin-1 HY1) (IL-1HY1) (Interleukin-1 delta) (IL-1 delta) (Interleukin-1 family member 5) (IL-1F5) (Interleukin-1 receptor antagonist homolog 1) (IL-1ra homolog 1) (Interleukin-1-like protein 1) (IL-1L1)
[Ooep Oep19 Sddr] Oocyte-expressed protein homolog (Factor located in oocytes permitting embryonic development) (Floped) (Oocyte- and embryo-specific protein 19) (mOEP19) (STAT3 downstream gene and differentiation regulator)
[PXDN KIAA0230 MG50 PRG2 VPO VPO1] Peroxidasin homolog (EC 1.11.1.7) (Melanoma-associated antigen MG50) (Vascular peroxidase 1) (p53-responsive gene 2 protein)
[Ift81 Cdv-1 Cdv1] Intraflagellar transport protein 81 homolog (Carnitine deficiency-associated protein expressed in ventricle 1) (CDV-1)
[IL36RN Fil1d Il1f5 Il1h3 Il1hy1] Interleukin-36 receptor antagonist protein (IL-36Ra) (Interleukin-1 HY1) (IL-1HY1) (Interleukin-1 delta) (IL-1 delta) (Interleukin-1 family member 5) (IL-1F5) (Interleukin-1 homolog 3) (IL-1H3) (Interleukin-1-like protein 1) (IL-1L1)
[Atm] Serine-protein kinase ATM (EC 2.7.11.1) (Ataxia telangiectasia mutated homolog) (A-T mutated homolog)
[IFT81 CDV1] Intraflagellar transport protein 81 homolog (Carnitine deficiency-associated protein expressed in ventricle 1) (CDV-1)
[IFT74 CCDC2 CMG1] Intraflagellar transport protein 74 homolog (Capillary morphogenesis gene 1 protein) (CMG-1) (Coiled-coil domain-containing protein 2)
[FERMT2 KIND2 MIG2 PLEKHC1] Fermitin family homolog 2 (Kindlin-2) (Mitogen-inducible gene 2 protein) (MIG-2) (Pleckstrin homology domain-containing family C member 1) (PH domain-containing family C member 1)
[Notch1 Motch] Neurogenic locus notch homolog protein 1 (Notch 1) (Motch A) (mT14) (p300) [Cleaved into: Notch 1 extracellular truncation (NEXT); Notch 1 intracellular domain (NICD)]
[LLGL1 DLG4 HUGL HUGL1] Lethal(2) giant larvae protein homolog 1 (LLGL) (DLG4) (Hugl-1) (Human homolog to the D-lgl gene protein)
[Tra2b Sfrs10 Silg41] Transformer-2 protein homolog beta (TRA-2 beta) (TRA2-beta) (Silica-induced gene 41 protein) (SIG-41) (Splicing factor, arginine/serine-rich 10) (Transformer-2 protein homolog B)
[Lin7c Mals3 Veli3] Protein lin-7 homolog C (Lin-7C) (Mammalian lin-seven protein 3) (MALS-3) (Vertebrate lin-7 homolog 3) (Veli-3)
[PRUNE1 PRUNE] Exopolyphosphatase PRUNE1 (EC 3.6.1.1) (Drosophila-related expressed sequence 17) (DRES-17) (DRES17) (HTcD37) (Protein prune homolog 1) (hPrune)
[NAV3 KIAA0938 POMFIL1 STEERIN3] Neuron navigator 3 (Pore membrane and/or filament-interacting-like protein 1) (Steerin-3) (Unc-53 homolog 3) (unc53H3)
[KMT2B HRX2 KIAA0304 MLL2 MLL4 TRX2 WBP7] Histone-lysine N-methyltransferase 2B (Lysine N-methyltransferase 2B) (EC 2.1.1.354) (Myeloid/lymphoid or mixed-lineage leukemia protein 4) (Trithorax homolog 2) (WW domain-binding protein 7) (WBP-7)
[DNAJA3 HCA57 TID1] DnaJ homolog subfamily A member 3, mitochondrial (DnaJ protein Tid-1) (hTid-1) (Hepatocellular carcinoma-associated antigen 57) (Tumorous imaginal discs protein Tid56 homolog)
[NAV2 HELAD1 KIAA1419 POMFIL2 RAINB1 STEERIN2] Neuron navigator 2 (EC 3.6.4.12) (Helicase APC down-regulated 1) (Pore membrane and/or filament-interacting-like protein 2) (Retinoic acid inducible in neuroblastoma 1) (Steerin-2) (Unc-53 homolog 2) (unc53H2)

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