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Protein mothers against dpp

 MAD_DROME               Reviewed;         455 AA.
P42003; Q9VQM3;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
02-DEC-2020, entry version 188.
RecName: Full=Protein mothers against dpp;
Name=Mad; ORFNames=CG12399;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; Ephydroidea;
Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, MUTAGENESIS OF
GLY-409 AND SER-421, AND DISRUPTION PHENOTYPE.
PubMed=7768443;
Sekelsky J.J., Newfeld S.J., Raftery L.A., Chartoff E.H., Gelbart W.M.;
"Genetic characterization and cloning of mothers against dpp, a gene
required for decapentaplegic function in Drosophila melanogaster.";
Genetics 139:1347-1358(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic
review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[5]
INTERACTION WITH SMURF.
PubMed=11703946; DOI=10.1016/s1534-5807(01)00057-0;
Podos S.D., Hanson K.K., Wang Y.-C., Ferguson E.L.;
"The DSmurf ubiquitin-protein ligase restricts BMP signaling spatially and
temporally during Drosophila embryogenesis.";
Dev. Cell 1:567-578(2001).
[6]
TISSUE SPECIFICITY.
PubMed=11997505; DOI=10.1128/mcb.22.11.3685-3697.2002;
Sem K.P., Zahedi B., Tan I., Deak M., Lim L., Harden N.;
"ACK family tyrosine kinase activity is a component of Dcdc42 signaling
during dorsal closure in Drosophila melanogaster.";
Mol. Cell. Biol. 22:3685-3697(2002).
[7]
INTERACTION WITH SMURF, PHOSPHORYLATION AT SER-453 AND SER-455, MUTAGENESIS
OF SER-453 AND SER-455, AND UBIQUITINATION.
PubMed=12754252; DOI=10.1074/jbc.c300028200;
Liang Y.-Y., Lin X., Liang M., Brunicardi F.C., ten Dijke P., Chen Z.,
Choi K.-W., Feng X.-H.;
"DSmurf selectively degrades decapentaplegic-activated MAD, and its
overexpression disrupts imaginal disc development.";
J. Biol. Chem. 278:26307-26310(2003).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-25.
PubMed=17507407; DOI=10.1242/dev.02853;
Zeng Y.A., Rahnama M., Wang S., Sosu-Sedzorme W., Verheyen E.M.;
"Drosophila Nemo antagonizes BMP signaling by phosphorylation of Mad and
inhibition of its nuclear accumulation.";
Development 134:2061-2071(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453 AND SER-455, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
[10]
INTERACTION WITH MAN1.
PubMed=20036230; DOI=10.1016/j.ydbio.2009.11.036;
Wagner N., Weyhersmueller A., Blauth A., Schuhmann T., Heckmann M.,
Krohne G., Samakovlis C.;
"The Drosophila LEM-domain protein MAN1 antagonizes BMP signaling at the
neuromuscular junction and the wing crossveins.";
Dev. Biol. 339:1-13(2010).
[11]
INTERACTION WITH SEC13 AND NUP93-1.
PubMed=20547758; DOI=10.1128/mcb.00124-10;
Chen X., Xu L.;
"Specific nucleoporin requirement for Smad nuclear translocation.";
Mol. Cell. Biol. 30:4022-4034(2010).
[12]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 215-455, AND SUBUNIT.
PubMed=19557331; DOI=10.1007/s11427-009-0080-x;
Wang C., Chen L., Wang L., Wu J.;
"Crystal structure of the MH2 domain of Drosophila Mad.";
Sci. China, Ser. C, Life Sci. 52:539-544(2009).
-!- FUNCTION: Required for the function of decapentaplegic. May play an
important role in mediating Dpp signaling. Involved in the BMP
signaling pathway. {ECO:0000269|PubMed:17507407,
ECO:0000269|PubMed:7768443}.
-!- SUBUNIT: Homotrimer (PubMed:19557331). Interacts with MAN1
(PubMed:20036230). Interacts with Sec13 and Nup93-1 (PubMed:20547758).
{ECO:0000269|PubMed:19557331, ECO:0000269|PubMed:20036230,
ECO:0000269|PubMed:20547758}.
-!- INTERACTION:
P42003; Q7KNS3: Lis-1; NbExp=2; IntAct=EBI-162238, EBI-156005;
P42003; Q45VV3: yki; NbExp=2; IntAct=EBI-162238, EBI-141254;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17507407}. Nucleus
{ECO:0000269|PubMed:17507407}.
-!- TISSUE SPECIFICITY: Stage 13 embryos display expression in the dorsal
epidermis (at protein level). {ECO:0000269|PubMed:11997505}.
-!- DEVELOPMENTAL STAGE: Is detected in all developmental stages, though it
appears most abundant in pupae, adult stages and early embryos. Its
abundance decreases throughout embryonic and larval development and
then returns to high levels in pupae and adult females.
{ECO:0000269|PubMed:7768443}.
-!- PTM: Phosphorylation on Ser-453 and/or Ser-455 is required for
interaction with Smurf (PubMed:12754252, PubMed:18327897).
Phosphorylation on Ser-25 by key/Nemo promotes export from nucleus and
antagonizes BMP signaling (PubMed:17507407).
{ECO:0000269|PubMed:12754252, ECO:0000269|PubMed:17507407,
ECO:0000269|PubMed:18327897}.
-!- PTM: Ubiquitinated by Smurf upon phosphorylation; which promotes
proteasomal degradation. {ECO:0000269|PubMed:12754252}.
-!- DISRUPTION PHENOTYPE: Mutants exhibit defects in midgut morphogenesis,
imaginal disk development and embryonic dorsal-ventral patterning that
are very reminiscent of dpp mutant phenotypes.
{ECO:0000269|PubMed:7768443}.
-!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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EMBL; U10328; AAB60230.1; -; mRNA.
EMBL; AE014134; AAF51142.1; -; Genomic_DNA.
EMBL; BT004845; AAO45201.1; -; mRNA.
PIR; S55019; S55019.
RefSeq; NP_477017.1; NM_057669.3.
PDB; 3DIT; X-ray; 3.20 A; A/B/C=259-446.
PDB; 3GMJ; X-ray; 2.80 A; A/B/C/D=215-455.
PDBsum; 3DIT; -.
PDBsum; 3GMJ; -.
SMR; P42003; -.
BioGRID; 59745; 104.
DIP; DIP-18256N; -.
IntAct; P42003; 47.
STRING; 7227.FBpp0304648; -.
iPTMnet; P42003; -.
PaxDb; P42003; -.
EnsemblMetazoa; FBtr0077616; FBpp0077302; FBgn0011648.
GeneID; 33529; -.
KEGG; dme:Dmel_CG12399; -.
CTD; 33529; -.
FlyBase; FBgn0011648; Mad.
eggNOG; KOG3701; Eukaryota.
GeneTree; ENSGT00940000163092; -.
HOGENOM; CLU_026736_0_2_1; -.
InParanoid; P42003; -.
OrthoDB; 608001at2759; -.
PhylomeDB; P42003; -.
Reactome; R-DME-201451; Signaling by BMP.
Reactome; R-DME-5689880; Ub-specific processing proteases.
Reactome; R-DME-8941326; RUNX2 regulates bone development.
SignaLink; P42003; -.
BioGRID-ORCS; 33529; 0 hits in 3 CRISPR screens.
EvolutionaryTrace; P42003; -.
GenomeRNAi; 33529; -.
PRO; PR:P42003; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0011648; Expressed in wing disc (Drosophila) and 44 other tissues.
ExpressionAtlas; P42003; baseline and differential.
Genevisible; P42003; DM.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0005829; C:cytosol; IDA:FlyBase.
GO; GO:0071144; C:heteromeric SMAD protein complex; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0090571; C:RNA polymerase II transcription repressor complex; IPI:FlyBase.
GO; GO:0005667; C:transcription regulator complex; IPI:FlyBase.
GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:FlyBase.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:FlyBase.
GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:FlyBase.
GO; GO:0070411; F:I-SMAD binding; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IPI:FlyBase.
GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:FlyBase.
GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:FlyBase.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
GO; GO:0003713; F:transcription coactivator activity; IDA:FlyBase.
GO; GO:0008134; F:transcription factor binding; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
GO; GO:0030509; P:BMP signaling pathway; IDA:FlyBase.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
GO; GO:0042078; P:germ-line stem cell division; IMP:FlyBase.
GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:FlyBase.
GO; GO:0007507; P:heart development; TAS:FlyBase.
GO; GO:0007488; P:histoblast morphogenesis; IMP:FlyBase.
GO; GO:0007560; P:imaginal disc morphogenesis; IMP:FlyBase.
GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IMP:FlyBase.
GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
GO; GO:0008586; P:imaginal disc-derived wing vein morphogenesis; IMP:FlyBase.
GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IMP:FlyBase.
GO; GO:0045705; P:negative regulation of salivary gland boundary specification; TAS:FlyBase.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:FlyBase.
GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
GO; GO:1904398; P:positive regulation of neuromuscular junction development; IMP:FlyBase.
GO; GO:0045887; P:positive regulation of synaptic growth at neuromuscular junction; IMP:FlyBase.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
GO; GO:0045464; P:R8 cell fate specification; IMP:FlyBase.
GO; GO:0045595; P:regulation of cell differentiation; IMP:FlyBase.
GO; GO:0060395; P:SMAD protein signal transduction; IDA:FlyBase.
GO; GO:0035019; P:somatic stem cell population maintenance; IMP:FlyBase.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IBA:GO_Central.
GO; GO:0060799; P:transforming growth factor beta receptor signaling pathway involved in endodermal cell fate specification; IMP:FlyBase.
GO; GO:0035290; P:trunk segmentation; IMP:FlyBase.
GO; GO:0007419; P:ventral cord development; HMP:FlyBase.
GO; GO:0048100; P:wing disc anterior/posterior pattern formation; IMP:FlyBase.
Gene3D; 2.60.200.10; -; 1.
Gene3D; 3.90.520.10; -; 1.
InterPro; IPR013790; Dwarfin.
InterPro; IPR003619; MAD_homology1_Dwarfin-type.
InterPro; IPR013019; MAD_homology_MH1.
InterPro; IPR017855; SMAD-like_dom_sf.
InterPro; IPR001132; SMAD_dom_Dwarfin-type.
InterPro; IPR008984; SMAD_FHA_dom_sf.
InterPro; IPR036578; SMAD_MH1_sf.
PANTHER; PTHR13703; PTHR13703; 1.
Pfam; PF03165; MH1; 1.
Pfam; PF03166; MH2; 1.
SMART; SM00523; DWA; 1.
SMART; SM00524; DWB; 1.
SUPFAM; SSF49879; SSF49879; 1.
SUPFAM; SSF56366; SSF56366; 1.
PROSITE; PS51075; MH1; 1.
PROSITE; PS51076; MH2; 1.
1: Evidence at protein level;
3D-structure; Cytoplasm; Developmental protein; DNA-binding; Metal-binding;
Nucleus; Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation; Zinc.
CHAIN 1..455
/note="Protein mothers against dpp"
/id="PRO_0000090878"
DOMAIN 26..150
/note="MH1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00438"
DOMAIN 261..455
/note="MH2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00439"
REGION 221..225
/note="Interaction with lack"
METAL 78
/note="Zinc"
/evidence="ECO:0000250"
METAL 123
/note="Zinc"
/evidence="ECO:0000250"
METAL 135
/note="Zinc"
/evidence="ECO:0000250"
METAL 140
/note="Zinc"
/evidence="ECO:0000250"
MOD_RES 25
/note="Phosphoserine"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00439,
ECO:0000269|PubMed:17507407"
MOD_RES 453
/note="Phosphoserine"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00439,
ECO:0000269|PubMed:12754252, ECO:0000269|PubMed:18327897"
MOD_RES 455
/note="Phosphoserine"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00439,
ECO:0000269|PubMed:12754252, ECO:0000269|PubMed:18327897"
MUTAGEN 25
/note="S->A: Abolishes phosphorylation."
MUTAGEN 409
/note="G->S: In allele Mad-10; pupal lethal."
/evidence="ECO:0000269|PubMed:7768443"
MUTAGEN 421
/note="S->L: In allele Mad-9; lethal."
/evidence="ECO:0000269|PubMed:7768443"
MUTAGEN 453
/note="S->A: Abolishes interaction with lack; when
associated with A-455."
/evidence="ECO:0000269|PubMed:12754252"
MUTAGEN 455
/note="S->A: Abolishes interaction with lack; when
associated with A-453."
/evidence="ECO:0000269|PubMed:12754252"
STRAND 261..268
/evidence="ECO:0000244|PDB:3GMJ"
STRAND 271..279
/evidence="ECO:0000244|PDB:3GMJ"
STRAND 281..289
/evidence="ECO:0000244|PDB:3GMJ"
TURN 294..296
/evidence="ECO:0000244|PDB:3GMJ"
STRAND 297..300
/evidence="ECO:0000244|PDB:3GMJ"
HELIX 301..303
/evidence="ECO:0000244|PDB:3GMJ"
HELIX 311..320
/evidence="ECO:0000244|PDB:3GMJ"
STRAND 324..329
/evidence="ECO:0000244|PDB:3GMJ"
STRAND 332..337
/evidence="ECO:0000244|PDB:3GMJ"
STRAND 339..341
/evidence="ECO:0000244|PDB:3GMJ"
STRAND 343..346
/evidence="ECO:0000244|PDB:3GMJ"
HELIX 348..353
/evidence="ECO:0000244|PDB:3GMJ"
STRAND 362..364
/evidence="ECO:0000244|PDB:3GMJ"
STRAND 369..373
/evidence="ECO:0000244|PDB:3GMJ"
HELIX 375..384
/evidence="ECO:0000244|PDB:3GMJ"
HELIX 386..388
/evidence="ECO:0000244|PDB:3GMJ"
HELIX 391..396
/evidence="ECO:0000244|PDB:3GMJ"
HELIX 397..400
/evidence="ECO:0000244|PDB:3GMJ"
STRAND 401..408
/evidence="ECO:0000244|PDB:3GMJ"
STRAND 411..415
/evidence="ECO:0000244|PDB:3DIT"
HELIX 419..421
/evidence="ECO:0000244|PDB:3GMJ"
STRAND 422..430
/evidence="ECO:0000244|PDB:3GMJ"
HELIX 431..441
/evidence="ECO:0000244|PDB:3GMJ"
SEQUENCE 455 AA; 50505 MW; 6C8570674C3AB9D8 CRC64;
MDTDDVESNT SSAMSTLGSL FSFTSPAVKK LLGWKQGDEE EKWAEKAVDS LVKKLKKRKG
AIEELERALS CPGQPSKCVT IPRSLDGRLQ VSHRKGLPHV IYCRVWRWPD LQSHHELKPL
ELCQYPFSAK QKEVCINPYH YKRVESPVLP PVLVPRHSEF APGHSMLQFN HVAEPSMPHN
VSYSNSGFNS HSLSTSNTSV GSPSSVNSNP NSPYDSLAGT PPPAYSPSED GNSNNPNDGG
QLLDAQMGDV AQVSYSEPAF WASIAYYELN CRVGEVFHCN NNSVIVDGFT NPSNNSDRCC
LGQLSNVNRN STIENTRRHI GKGVHLYYVT GEVYAECLSD SAIFVQSRNC NYHHGFHPST
VCKIPPGCSL KIFNNQEFAQ LLSQSVNNGF EAVYELTKMC TIRMSFVKGW GAEYHRQDVT
STPCWIEIHL HGPLQWLDKV LTQMGSPHNA ISSVS


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E0648h ELISA kit Homo sapiens,hSMAD7,Human,MAD homolog 7,MAD homolog 8,MADH7,MADH8,Mothers against decapentaplegic homolog 7,Mothers against decapentaplegic homolog 8,Mothers against DPP homolog 7,Mothers a 96T
18-003-43345 Mothers against decapentaplegic homolog 2 - SMAD 2; Mothers against DPP homolog 2; Mad-related protein 2; hMAD-2; JV18-1; hSMAD2 Polyclonal 0.1 mg Protein A
U0648m CLIA MAD homolog 7,MAD homolog 8,Madh7,Madh8,Mothers against decapentaplegic homolog 7,Mothers against decapentaplegic homolog 8,Mothers against DPP homolog 7,Mothers against DPP homolog 8,Mouse,Mus m 96T
E0648m ELISA MAD homolog 7,MAD homolog 8,Madh7,Madh8,Mothers against decapentaplegic homolog 7,Mothers against decapentaplegic homolog 8,Mothers against DPP homolog 7,Mothers against DPP homolog 8,Mouse,Mus 96T
E0648m ELISA kit MAD homolog 7,MAD homolog 8,Madh7,Madh8,Mothers against decapentaplegic homolog 7,Mothers against decapentaplegic homolog 8,Mothers against DPP homolog 7,Mothers against DPP homolog 8,Mouse 96T
E0647h ELISA kit BSP1,BSP-1,Homo sapiens,hSMAD1,Human,JV4-1,MAD homolog 1,MADH1,MADR1,Mad-related protein 1,Mothers against decapentaplegic homolog 1,Mothers against DPP homolog 1,SMAD 1,SMAD family member 96T
E0647h ELISA BSP1,BSP-1,Homo sapiens,hSMAD1,Human,JV4-1,MAD homolog 1,MADH1,MADR1,Mad-related protein 1,Mothers against decapentaplegic homolog 1,Mothers against DPP homolog 1,SMAD 1,SMAD family member 1,Sma 96T
U2184h CLIA kit hMAD-2,Homo sapiens,hSMAD2,Human,JV18-1,MAD homolog 2,MADH2,MADR2,Mad-related protein 2,Mothers against decapentaplegic homolog 2,Mothers against DPP homolog 2,SMAD 2,SMAD family member 2,Sm 96T
E2184h ELISA kit hMAD-2,Homo sapiens,hSMAD2,Human,JV18-1,MAD homolog 2,MADH2,MADR2,Mad-related protein 2,Mothers against decapentaplegic homolog 2,Mothers against DPP homolog 2,SMAD 2,SMAD family member 2,S 96T
U2184h CLIA hMAD-2,Homo sapiens,hSMAD2,Human,JV18-1,MAD homolog 2,MADH2,MADR2,Mad-related protein 2,Mothers against decapentaplegic homolog 2,Mothers against DPP homolog 2,SMAD 2,SMAD family member 2,Smad2,S 96T
E2184h ELISA hMAD-2,Homo sapiens,hSMAD2,Human,JV18-1,MAD homolog 2,MADH2,MADR2,Mad-related protein 2,Mothers against decapentaplegic homolog 2,Mothers against DPP homolog 2,SMAD 2,SMAD family member 2,Smad2, 96T
U0647h CLIA BSP1,BSP-1,Homo sapiens,hSMAD1,Human,JV4-1,MAD homolog 1,MADH1,MADR1,Mad-related protein 1,Mothers against decapentaplegic homolog 1,Mothers against DPP homolog 1,SMAD 1,SMAD family member 1,Smad 96T
E2184m ELISA MAD homolog 2,Madh2,Madr2,Mad-related protein 2,mMad2,Mothers against decapentaplegic homolog 2,Mothers against DPP homolog 2,Mouse,Mus musculus,SMAD 2,SMAD family member 2,Smad2,Smad2 96T
E2184m ELISA kit MAD homolog 2,Madh2,Madr2,Mad-related protein 2,mMad2,Mothers against decapentaplegic homolog 2,Mothers against DPP homolog 2,Mouse,Mus musculus,SMAD 2,SMAD family member 2,Smad2,Smad2 96T
U2184m CLIA MAD homolog 2,Madh2,Madr2,Mad-related protein 2,mMad2,Mothers against decapentaplegic homolog 2,Mothers against DPP homolog 2,Mouse,Mus musculus,SMAD 2,SMAD family member 2,Smad2,Smad2 96T
U2184m CLIA kit MAD homolog 2,Madh2,Madr2,Mad-related protein 2,mMad2,Mothers against decapentaplegic homolog 2,Mothers against DPP homolog 2,Mouse,Mus musculus,SMAD 2,SMAD family member 2,Smad2,Smad2 96T
E2184h hMAD-2,Homo sapiens,hSMAD2,Human,JV18-1,MAD homolog 2,MADH2,MADR2,Mad-related protein 2,Mothers against decapentaplegic homolog 2,Mothers against DPP homolog 2,SMAD 2,SMAD family member 2,Smad2,SMAD2
E2184m MAD homolog 2,Madh2,Madr2,Mad-related protein 2,mMad2,Mothers against decapentaplegic homolog 2,Mothers against DPP homolog 2,Mouse,Mus musculus,SMAD 2,SMAD family member 2,Smad2,Smad2
E2184r ELISA kit MAD homolog 2,Madh2,Mad-related protein 2,Mothers against decapentaplegic homolog 2,Mothers against DPP homolog 2,Rat,Rattus norvegicus,SMAD 2,SMAD family member 2,Smad2,Smad2 96T
Pathways :
WP2324: AGE/RAGE pathway
WP1049: G Protein Signaling Pathways
WP1713: Two-component system
WP1659: Glycine, serine and threonine metabolism
WP1665: Limonene and pinene degradation
WP35: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1892: Protein folding
WP1531: Vitamin D synthesis
WP2032: TSH signaling pathway
WP1675: Nitrogen metabolism
WP731: Sterol regulatory element binding protein related
WP1685: Peptidoglycan biosynthesis
WP1616: ABC transporters
WP211: BMP signaling pathway
WP1644: DNA replication
WP2218: sGC
WP1692: Protein export
WP1700: Selenoamino acid metabolism
WP1657: Glycerolipid metabolism
WP232: G Protein Signaling Pathways
WP1663: Homologous recombination
WP346: Protein Modifications
WP1371: G Protein Signaling Pathways
WP1888: Post-translational protein modification

Related Genes :
[Smad1 Madh1 Madr1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (Dwarfin-A) (Dwf-A) (Mothers-against-DPP-related 1) (Mad-related protein 1) (mMad1) (SMAD family member 1) (SMAD 1) (Smad1)
[Mad CG12399] Protein mothers against dpp
[SMAD7 MADH7 MADH8] Mothers against decapentaplegic homolog 7 (MAD homolog 7) (Mothers against DPP homolog 7) (Mothers against decapentaplegic homolog 8) (MAD homolog 8) (Mothers against DPP homolog 8) (SMAD family member 7) (SMAD 7) (Smad7) (hSMAD7)
[Med Medea CG1775] Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member)
[Smad7 Madh7 Madh8] Mothers against decapentaplegic homolog 7 (MAD homolog 7) (Mothers against DPP homolog 7) (Mothers against decapentaplegic homolog 8) (MAD homolog 8) (Mothers against DPP homolog 8) (SMAD family member 7) (SMAD 7) (Smad7)
[SMAD1 BSP1 MADH1 MADR1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (JV4-1) (Mad-related protein 1) (SMAD family member 1) (SMAD 1) (Smad1) (hSMAD1) (Transforming growth factor-beta-signaling protein 1) (BSP-1)
[SMAD2 MADH2 MADR2] Mothers against decapentaplegic homolog 2 (MAD homolog 2) (Mothers against DPP homolog 2) (JV18-1) (Mad-related protein 2) (hMAD-2) (SMAD family member 2) (SMAD 2) (Smad2) (hSMAD2)
[SMAD3 MADH3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (hMAD-3) (JV15-2) (SMAD family member 3) (SMAD 3) (Smad3) (hSMAD3)
[SMAD4 DPC4 MADH4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (Deletion target in pancreatic carcinoma 4) (SMAD family member 4) (SMAD 4) (Smad4) (hSMAD4)
[SMAD6 MADH6] Mothers against decapentaplegic homolog 6 (MAD homolog 6) (Mothers against DPP homolog 6) (SMAD family member 6) (SMAD 6) (Smad6) (hSMAD6)
[SMAD5 MADH5] Mothers against decapentaplegic homolog 5 (MAD homolog 5) (Mothers against DPP homolog 5) (JV5-1) (SMAD family member 5) (SMAD 5) (Smad5) (hSmad5)
[SMAD9 MADH6 MADH9 SMAD8] Mothers against decapentaplegic homolog 9 (MAD homolog 9) (Mothers against DPP homolog 9) (Madh6) (SMAD family member 9) (SMAD 9) (Smad9)
[Smad2 Madh2 Madr2] Mothers against decapentaplegic homolog 2 (MAD homolog 2) (Mothers against DPP homolog 2) (Mad-related protein 2) (mMad2) (SMAD family member 2) (SMAD 2) (Smad2)
[Smad2 Madh2] Mothers against decapentaplegic homolog 2 (MAD homolog 2) (Mothers against DPP homolog 2) (Mad-related protein 2) (SMAD family member 2) (SMAD 2) (Smad2)
[SMAD1 MADH1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (Mad-related protein 1) (SMAD family member 1) (SMAD 1) (Smad1)
[smad5 madh5 sbn] Mothers against decapentaplegic homolog 5 (MAD homolog 5) (Mothers against DPP homolog 5) (Protein somitabun) (SMAD family member 5) (SMAD 5) (Smad5)
[Smad3 Madh3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (mMad3) (SMAD family member 3) (SMAD 3) (Smad3)
[Smad4 Dpc4 Madh4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (Deletion target in pancreatic carcinoma 4 homolog) (SMAD family member 4) (SMAD 4) (Smad4)
[Smad4 Madh4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (SMAD family member 4) (SMAD 4) (Smad4)
[Smad3 Madh3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (SMAD family member 3) (SMAD 3) (Smad3)
[Smad7 Madh7] Mothers against decapentaplegic homolog 7 (MAD homolog 7) (Mothers against DPP homolog 7) (SMAD family member 7) (SMAD 7) (Smad7)
[Smad6 Madh6 Madh7 Msmad6] Mothers against decapentaplegic homolog 6 (MAD homolog 6) (Mothers against DPP homolog 6) (Mad homolog 7) (SMAD family member 6) (SMAD 6) (Smad6)
[Smad5 Madh5 Msmad5] Mothers against decapentaplegic homolog 5 (MAD homolog 5) (Mothers against DPP homolog 5) (Dwarfin-C) (Dwf-C) (SMAD family member 5) (SMAD 5) (Smad5) (mSmad5)
[SMAD4 MADH4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (SMAD family member 4) (SMAD 4) (Smad4)
[Smad1 Mad1 Madh1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (SMAD family member 1) (SMAD 1) (Smad1)
[SMAD1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (SMAD family member 1) (SMAD 1) (Smad1)
[SMAD3 MADH3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (SMAD family member 3) (SMAD 3) (Smad3)
[Smad9 Madh8 Madh9 Smad8] Mothers against decapentaplegic homolog 9 (MAD homolog 9) (Mothers against DPP homolog 9) (SMAD family member 9) (SMAD 9) (Smad9) (Smad8)
[Smad5 Madh5] Mothers against decapentaplegic homolog 5 (MAD homolog 5) (Mothers against DPP homolog 5) (SMAD family member 5) (SMAD 5) (Smad5)
[SMAD3 MADH3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (SMAD family member 3) (SMAD 3) (Smad3)

Bibliography :
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