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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)

 SMAD7_HUMAN             Reviewed;         426 AA.
O15105; B7Z773; K7EQ10; O14740; Q6DK23;
04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
22-APR-2020, entry version 201.
RecName: Full=Mothers against decapentaplegic homolog 7;
Short=MAD homolog 7;
Short=Mothers against DPP homolog 7;
AltName: Full=Mothers against decapentaplegic homolog 8;
Short=MAD homolog 8;
Short=Mothers against DPP homolog 8;
AltName: Full=SMAD family member 7;
Short=SMAD 7;
Short=Smad7;
Short=hSMAD7;
Name=SMAD7; Synonyms=MADH7, MADH8;
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), AND MUTAGENESIS OF
409-ARG--ARG-426.
TISSUE=Umbilical vein endothelial cell;
PubMed=9215638; DOI=10.1016/s0092-8674(00)80303-7;
Hayashi H., Abdollah S., Qiu Y., Cai J., Xu Y.-Y., Grinnell B.W.,
Richardson M.A., Topper J.N., Gimbrone M.A. Jr., Wrana J.L., Falb D.;
"The MAD-related protein Smad7 associates with the TGFbeta receptor and
functions as an antagonist of TGFbeta signaling.";
Cell 89:1165-1173(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Umbilical vein endothelial cell;
PubMed=9256479; DOI=10.1073/pnas.94.17.9314;
Topper J.N., Cai J., Qui Y., Anderson K.R., Xu Y.-Y., Deeds J.D.,
Feeley R., Gimeno C.J., Woolf E.A., Tayber O., Mays G.G., Sampson B.A.,
Schoen F.J., Gimbrone M.A. Jr., Falb D.;
"Vascular MADs: two novel MAD-related genes selectively inducible by flow
in human vascular endothelium.";
Proc. Natl. Acad. Sci. U.S.A. 94:9314-9319(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9335507; DOI=10.1038/39369;
Nakao A., Afrakhte M., Moren A., Nakayama T., Christian J.L., Heuchel R.,
Itoh S., Kawabata M., Heldin N.-E., Heldin C.-H., ten Dijke P.;
"Identification of Smad7, a TGFbeta-inducible antagonist of TGF-beta
signalling.";
Nature 389:631-635(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Hagiwara K., Yang K., McMenamin M.G., Freeman A.H., Bennett W.P.,
Nagashima M., Minter A.R., Miyazono K., Takenoshita S., Harris C.C.;
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
[LARGE SCALE MRNA] OF 98-271 (ISOFORM 3).
TISSUE=Pulmonary artery;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16177791; DOI=10.1038/nature03983;
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
"DNA sequence and analysis of human chromosome 18.";
Nature 437:551-555(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
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).
[8]
REVIEW.
PubMed=9759503; DOI=10.1146/annurev.biochem.67.1.753;
Massague J.;
"TGF-beta signal transduction.";
Annu. Rev. Biochem. 67:753-791(1998).
[9]
REVIEW.
PubMed=10647776; DOI=10.1016/s1359-6101(99)00012-x;
Verschueren K., Huylebroeck D.;
"Remarkable versatility of Smad proteins in the nucleus of transforming
growth factor-beta activated cells.";
Cytokine Growth Factor Rev. 10:187-199(1999).
[10]
INTERACTION WITH ACVR1B, AND FUNCTION.
PubMed=9892009; DOI=10.1210/mend.13.1.0218;
Lebrun J.J., Takabe K., Chen Y., Vale W.;
"Roles of pathway-specific and inhibitory Smads in activin receptor
signaling.";
Mol. Endocrinol. 13:15-23(1999).
[11]
REVIEW.
PubMed=10708948; DOI=10.1016/s1359-6101(99)00024-6;
Wrana J.L., Attisano L.;
"The Smad pathway.";
Cytokine Growth Factor Rev. 11:5-13(2000).
[12]
REVIEW.
PubMed=10708949; DOI=10.1016/s1359-6101(99)00025-8;
Miyazono K.;
"TGF-beta signaling by Smad proteins.";
Cytokine Growth Factor Rev. 11:15-22(2000).
[13]
FUNCTION, MUTAGENESIS OF TYR-211 AND 207-PRO--TYR-211, AND INTERACTION WITH
SMURF2 AND TGFBR1.
PubMed=11163210; DOI=10.1016/s1097-2765(00)00134-9;
Kavsak P., Rasmussen R.K., Causing C.G., Bonni S., Zhu H., Thomsen G.H.,
Wrana J.L.;
"Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF-
beta receptor for degradation.";
Mol. Cell 6:1365-1375(2000).
[14]
INTERACTION WITH STAMBP.
PubMed=11483516; DOI=10.1093/emboj/20.15.4132;
Itoh F., Asao H., Sugamura K., Heldin C.-H., ten Dijke P., Itoh S.;
"Promoting bone morphogenetic protein signaling through negative regulation
of inhibitory Smads.";
EMBO J. 20:4132-4142(2001).
[15]
INTERACTION WITH SMURF1 AND TGFBR1, AND UBIQUITINATION.
PubMed=11278251; DOI=10.1074/jbc.c100008200;
Ebisawa T., Fukuchi M., Murakami G., Chiba T., Tanaka K., Imamura T.,
Miyazono K.;
"Smurf1 interacts with transforming growth factor-beta type I receptor
through Smad7 and induces receptor degradation.";
J. Biol. Chem. 276:12477-12480(2001).
[16]
INTERACTION WITH ACVR1B, AND FUNCTION.
PubMed=12023024; DOI=10.1016/s0014-5793(02)02718-7;
Liu X., Nagarajan R.P., Vale W., Chen Y.;
"Phosphorylation regulation of the interaction between Smad7 and activin
type I receptor.";
FEBS Lett. 519:93-98(2002).
[17]
INTERACTION WITH EP300, ACETYLATION AT LYS-64 AND LYS-70, UBIQUITINATION AT
LYS-64 AND LYS-70, AND MUTAGENESIS OF LYS-64 AND LYS-70.
PubMed=12408818; DOI=10.1016/s1097-2765(02)00639-1;
Gronroos E., Hellman U., Heldin C.H., Ericsson J.;
"Control of Smad7 stability by competition between acetylation and
ubiquitination.";
Mol. Cell 10:483-493(2002).
[18]
INTERACTION WITH RNF111, UBIQUITINATION, AND SUBCELLULAR LOCATION.
PubMed=14657019; DOI=10.1093/emboj/cdg632;
Koinuma D., Shinozaki M., Komuro A., Goto K., Saitoh M., Hanyu A.,
Ebina M., Nukiwa T., Miyazawa K., Imamura T., Miyazono K.;
"Arkadia amplifies TGF-beta superfamily signaling through degradation of
Smad7.";
EMBO J. 22:6458-6470(2003).
[19]
FUNCTION, AND INTERACTION WITH PPP1R15A.
PubMed=14718519; DOI=10.1083/jcb.200307151;
Shi W., Sun C., He B., Xiong W., Shi X., Yao D., Cao X.;
"GADD34-PP1c recruited by Smad7 dephosphorylates TGFbeta type I receptor.";
J. Cell Biol. 164:291-300(2004).
[20]
INTERACTION WITH COPS5.
PubMed=14993265; DOI=10.1128/mcb.24.6.2251-2262.2004;
Kim B.-C., Lee H.-J., Park S.H., Lee S.R., Karpova T.S., McNally J.G.,
Felici A., Lee D.K., Kim S.-J.;
"Jab1/CSN5, a component of the COP9 signalosome, regulates transforming
growth factor beta signaling by binding to Smad7 and promoting its
degradation.";
Mol. Cell. Biol. 24:2251-2262(2004).
[21]
INTERACTION WITH SMURF2.
PubMed=16061177; DOI=10.1016/j.molcel.2005.06.028;
Ogunjimi A.A., Briant D.J., Pece-Barbara N., Le Roy C., Di Guglielmo G.M.,
Kavsak P., Rasmussen R.K., Seet B.T., Sicheri F., Wrana J.L.;
"Regulation of Smurf2 ubiquitin ligase activity by anchoring the E2 to the
HECT domain.";
Mol. Cell 19:297-308(2005).
[22]
INTERACTION WITH AXIN1 AND AXIN2, UBIQUITINATION, AND SUBCELLULAR LOCATION.
PubMed=16601693; DOI=10.1038/sj.emboj.7601057;
Liu W., Rui H., Wang J., Lin S., He Y., Chen M., Li Q., Ye Z., Zhang S.,
Chan S.C., Chen Y.-G., Han J., Lin S.-C.;
"Axin is a scaffold protein in TGF-beta signaling that promotes degradation
of Smad7 by Arkadia.";
EMBO J. 25:1646-1658(2006).
[23]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION BY PDPK1, AND INTERACTION
WITH PDPK1.
PubMed=17327236; DOI=10.1074/jbc.m609279200;
Seong H.A., Jung H., Kim K.T., Ha H.;
"3-Phosphoinositide-dependent PDK1 negatively regulates transforming growth
factor-beta-induced signaling in a kinase-dependent manner through physical
interaction with Smad proteins.";
J. Biol. Chem. 282:12272-12289(2007).
[24]
STRUCTURE BY NMR OF 203-217 IN COMPLEX WITH SMURF2.
PubMed=16641086; DOI=10.1074/jbc.m601493200;
Chong P.A., Lin H., Wrana J.L., Forman-Kay J.D.;
"An expanded WW domain recognition motif revealed by the interaction
between Smad7 and the E3 ubiquitin ligase Smurf2.";
J. Biol. Chem. 281:17069-17075(2006).
[25]
INVOLVEMENT IN CRCS3.
PubMed=17934461; DOI=10.1038/ng.2007.18;
Members of the CORGI consortium;
Broderick P., Carvajal-Carmona L., Pittman A.M., Webb E., Howarth K.,
Rowan A., Lubbe S., Spain S., Sullivan K., Fielding S., Jaeger E.,
Vijayakrishnan J., Kemp Z., Gorman M., Chandler I., Papaemmanuil E.,
Penegar S., Wood W., Sellick G., Qureshi M., Teixeira A., Domingo E.,
Barclay E., Martin L., Sieber O., Kerr D., Gray R., Peto J., Cazier J.-B.,
Tomlinson I., Houlston R.S.;
"A genome-wide association study shows that common alleles of SMAD7
influence colorectal cancer risk.";
Nat. Genet. 39:1315-1317(2007).
-!- FUNCTION: Antagonist of signaling by TGF-beta (transforming growth
factor) type 1 receptor superfamily members; has been shown to inhibit
TGF-beta (Transforming growth factor) and activin signaling by
associating with their receptors thus preventing SMAD2 access.
Functions as an adapter to recruit SMURF2 to the TGF-beta receptor
complex. Also acts by recruiting the PPP1R15A-PP1 complex to TGFBR1,
which promotes its dephosphorylation. Positively regulates PDPK1 kinase
activity by stimulating its dissociation from the 14-3-3 protein YWHAQ
which acts as a negative regulator. {ECO:0000269|PubMed:11163210,
ECO:0000269|PubMed:12023024, ECO:0000269|PubMed:14718519,
ECO:0000269|PubMed:17327236, ECO:0000269|PubMed:9892009}.
-!- SUBUNIT: Interacts with WWP1 (By similarity). Interacts with COPS5.
Interacts with NEDD4L. Interacts with STAMBP. Interacts with RNF111,
AXIN1 and AXIN2. Interacts with PPP1R15A. Interacts (via MH2 domain)
with EP300. Interacts with ACVR1B, SMURF1, SMURF2 and TGFBR1; SMAD7
recruits SMURF1 and SMURF2 to the TGF-beta receptor and regulates its
degradation. Interacts with PDPK1 (via PH domain). {ECO:0000250,
ECO:0000269|PubMed:11163210, ECO:0000269|PubMed:11278251,
ECO:0000269|PubMed:11483516, ECO:0000269|PubMed:12023024,
ECO:0000269|PubMed:12408818, ECO:0000269|PubMed:14657019,
ECO:0000269|PubMed:14718519, ECO:0000269|PubMed:14993265,
ECO:0000269|PubMed:16061177, ECO:0000269|PubMed:16601693,
ECO:0000269|PubMed:16641086, ECO:0000269|PubMed:17327236,
ECO:0000269|PubMed:9892009}.
-!- INTERACTION:
O15105; P36896: ACVR1B; NbExp=2; IntAct=EBI-3861591, EBI-1384128;
O15105; O15169: AXIN1; NbExp=8; IntAct=EBI-3861591, EBI-710484;
O15105; Q92905: COPS5; NbExp=10; IntAct=EBI-3861591, EBI-594661;
O15105; P62942: FKBP1A; NbExp=3; IntAct=EBI-3861591, EBI-1027571;
O15105; Q96PU5-5: NEDD4L; NbExp=3; IntAct=EBI-3861591, EBI-7196393;
O15105; Q99ML9: Rnf111; Xeno; NbExp=2; IntAct=EBI-3861591, EBI-646015;
O15105; Q9HCE7-1: SMURF1; NbExp=4; IntAct=EBI-3861591, EBI-15884081;
O15105; Q9HAU4: SMURF2; NbExp=7; IntAct=EBI-3861591, EBI-396727;
O15105; O00308: WWP2; NbExp=5; IntAct=EBI-3861591, EBI-743923;
O15105; P46937: YAP1; NbExp=7; IntAct=EBI-3861591, EBI-1044059;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14657019,
ECO:0000269|PubMed:16601693, ECO:0000269|PubMed:17327236}. Cytoplasm
{ECO:0000269|PubMed:14657019, ECO:0000269|PubMed:16601693,
ECO:0000269|PubMed:17327236}. Note=Interaction with NEDD4L or RNF111
induces translocation from the nucleus to the cytoplasm
(PubMed:16601693). TGF-beta stimulates its translocation from the
nucleus to the cytoplasm. PDPK1 inhibits its translocation from the
nucleus to the cytoplasm in response to TGF-beta (PubMed:17327236).
{ECO:0000269|PubMed:16601693, ECO:0000269|PubMed:17327236}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O15105-1; Sequence=Displayed;
Name=2;
IsoId=O15105-2; Sequence=VSP_045197;
Name=3;
IsoId=O15105-3; Sequence=VSP_047540;
-!- TISSUE SPECIFICITY: Ubiquitous with higher expression in the lung and
vascular endothelium.
-!- INDUCTION: By TGFB1.
-!- PTM: Phosphorylation on Ser-249 does not affect its stability, nuclear
localization or inhibitory function in TGFB signaling; however it
affects its ability to regulate transcription (By similarity).
Phosphorylated by PDPK1. {ECO:0000250|UniProtKB:O35253,
ECO:0000269|PubMed:17327236}.
-!- PTM: Ubiquitinated by WWP1 (By similarity). Polyubiquitinated by
RNF111, which is enhanced by AXIN1 and promotes proteasomal degradation
(PubMed:14657019, PubMed:16601693). In response to TGF-beta,
ubiquitinated by SMURF1; which promotes its degradation
(PubMed:11278251). {ECO:0000250|UniProtKB:O35253,
ECO:0000269|PubMed:11278251, ECO:0000269|PubMed:14657019,
ECO:0000269|PubMed:16601693}.
-!- PTM: Acetylation prevents ubiquitination and degradation mediated by
SMURF1. {ECO:0000269|PubMed:12408818}.
-!- DISEASE: Colorectal cancer 3 (CRCS3) [MIM:612229]: A complex disease
characterized by malignant lesions arising from the inner wall of the
large intestine (the colon) and the rectum. Genetic alterations are
often associated with progression from premalignant lesion (adenoma) to
invasive adenocarcinoma. Risk factors for cancer of the colon and
rectum include colon polyps, long-standing ulcerative colitis, and
genetic family history. {ECO:0000269|PubMed:17934461}. Note=Disease
susceptibility is associated with variations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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EMBL; AF010193; AAB81246.1; -; mRNA.
EMBL; AF015261; AAB81354.1; -; mRNA.
EMBL; AF026559; AAL68977.1; -; Genomic_DNA.
EMBL; AF026556; AAL68977.1; JOINED; Genomic_DNA.
EMBL; AF026557; AAL68977.1; JOINED; Genomic_DNA.
EMBL; AF026558; AAL68977.1; JOINED; Genomic_DNA.
EMBL; AK301535; BAH13509.1; -; mRNA.
EMBL; DA882147; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC114684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC074818; AAH74818.2; -; mRNA.
EMBL; BC074819; AAH74819.2; -; mRNA.
CCDS; CCDS11936.1; -. [O15105-1]
CCDS; CCDS54186.1; -. [O15105-2]
CCDS; CCDS59317.1; -. [O15105-3]
RefSeq; NP_001177750.1; NM_001190821.1. [O15105-3]
RefSeq; NP_001177751.1; NM_001190822.1. [O15105-2]
RefSeq; NP_001177752.1; NM_001190823.1.
RefSeq; NP_005895.1; NM_005904.3. [O15105-1]
PDB; 2DJY; NMR; -; B=203-217.
PDB; 2KXQ; NMR; -; B=203-217.
PDB; 2LTV; NMR; -; B=206-217.
PDB; 2LTW; NMR; -; B=205-217.
PDB; 2LTX; NMR; -; B=203-217.
PDB; 2LTY; NMR; -; B=203-217.
PDB; 2LTZ; NMR; -; B=203-217.
PDBsum; 2DJY; -.
PDBsum; 2KXQ; -.
PDBsum; 2LTV; -.
PDBsum; 2LTW; -.
PDBsum; 2LTX; -.
PDBsum; 2LTY; -.
PDBsum; 2LTZ; -.
SMR; O15105; -.
BioGrid; 110267; 99.
CORUM; O15105; -.
DIP; DIP-42252N; -.
IntAct; O15105; 30.
MINT; O15105; -.
STRING; 9606.ENSP00000262158; -.
iPTMnet; O15105; -.
PhosphoSitePlus; O15105; -.
BioMuta; SMAD7; -.
MassIVE; O15105; -.
PaxDb; O15105; -.
PeptideAtlas; O15105; -.
PRIDE; O15105; -.
ProteomicsDB; 48448; -. [O15105-1]
ProteomicsDB; 6838; -.
Antibodypedia; 9268; 511 antibodies.
Ensembl; ENST00000262158; ENSP00000262158; ENSG00000101665. [O15105-1]
Ensembl; ENST00000589634; ENSP00000467621; ENSG00000101665. [O15105-3]
Ensembl; ENST00000591805; ENSP00000466902; ENSG00000101665. [O15105-2]
GeneID; 4092; -.
KEGG; hsa:4092; -.
UCSC; uc002ldg.3; human. [O15105-1]
CTD; 4092; -.
DisGeNET; 4092; -.
GeneCards; SMAD7; -.
HGNC; HGNC:6773; SMAD7.
HPA; ENSG00000101665; Low tissue specificity.
MalaCards; SMAD7; -.
MIM; 602932; gene.
MIM; 612229; phenotype.
neXtProt; NX_O15105; -.
OpenTargets; ENSG00000101665; -.
PharmGKB; PA134875286; -.
eggNOG; KOG3701; Eukaryota.
eggNOG; ENOG410XQKU; LUCA.
GeneTree; ENSGT00940000159872; -.
HOGENOM; CLU_026736_5_0_1; -.
InParanoid; O15105; -.
KO; K19631; -.
OMA; GCCMGKS; -.
OrthoDB; 395665at2759; -.
PhylomeDB; O15105; -.
TreeFam; TF314923; -.
Reactome; R-HSA-201451; Signaling by BMP.
Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling.
Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
SignaLink; O15105; -.
SIGNOR; O15105; -.
ChiTaRS; SMAD7; human.
EvolutionaryTrace; O15105; -.
GeneWiki; Mothers_against_decapentaplegic_homolog_7; -.
GenomeRNAi; 4092; -.
Pharos; O15105; Tbio.
PRO; PR:O15105; -.
Proteomes; UP000005640; Chromosome 18.
RNAct; O15105; protein.
Bgee; ENSG00000101665; Expressed in left coronary artery and 215 other tissues.
ExpressionAtlas; O15105; baseline and differential.
Genevisible; O15105; HS.
GO; GO:0005813; C:centrosome; IDA:HPA.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0000790; C:nuclear chromatin; ISA:NTNU_SB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0032991; C:protein-containing complex; IDA:MGI.
GO; GO:0005667; C:transcription factor complex; IEA:InterPro.
GO; GO:0048185; F:activin binding; IPI:BHF-UCL.
GO; GO:0008013; F:beta-catenin binding; IPI:BHF-UCL.
GO; GO:0005518; F:collagen binding; IEA:Ensembl.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
GO; GO:0070411; F:I-SMAD binding; IPI:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
GO; GO:0030617; F:transforming growth factor beta receptor, inhibitory cytoplasmic mediator activity; IDA:BHF-UCL.
GO; GO:0034713; F:type I transforming growth factor beta receptor binding; IPI:BHF-UCL.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL.
GO; GO:0034333; P:adherens junction assembly; IMP:BHF-UCL.
GO; GO:0048844; P:artery morphogenesis; ISS:BHF-UCL.
GO; GO:0030509; P:BMP signaling pathway; TAS:Reactome.
GO; GO:0034629; P:cellular protein-containing complex localization; IDA:BHF-UCL.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IMP:BHF-UCL.
GO; GO:0030514; P:negative regulation of BMP signaling pathway; IDA:BHF-UCL.
GO; GO:0030336; P:negative regulation of cell migration; TAS:BHF-UCL.
GO; GO:1902731; P:negative regulation of chondrocyte proliferation; IEA:Ensembl.
GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; TAS:BHF-UCL.
GO; GO:0030279; P:negative regulation of ossification; IEA:Ensembl.
GO; GO:0060394; P:negative regulation of pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IDA:BHF-UCL.
GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; IDA:BHF-UCL.
GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:BHF-UCL.
GO; GO:0002725; P:negative regulation of T cell cytokine production; ISS:BHF-UCL.
GO; GO:2000320; P:negative regulation of T-helper 17 cell differentiation; ISS:BHF-UCL.
GO; GO:2000317; P:negative regulation of T-helper 17 type immune response; ISS:BHF-UCL.
GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; IDA:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; IDA:BHF-UCL.
GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; ISS:BHF-UCL.
GO; GO:0022409; P:positive regulation of cell-cell adhesion; IDA:BHF-UCL.
GO; GO:1903043; P:positive regulation of chondrocyte hypertrophy; IEA:Ensembl.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:BHF-UCL.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; TAS:Reactome.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0050821; P:protein stabilization; IDA:BHF-UCL.
GO; GO:0032925; P:regulation of activin receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0055117; P:regulation of cardiac muscle contraction; ISS:BHF-UCL.
GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; IMP:BHF-UCL.
GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IC:BHF-UCL.
GO; GO:0060373; P:regulation of ventricular cardiac muscle cell membrane depolarization; IC:BHF-UCL.
GO; GO:0034616; P:response to laminar fluid shear stress; IEP:BHF-UCL.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISS:BHF-UCL.
GO; GO:0060412; P:ventricular septum morphogenesis; ISS:BHF-UCL.
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; Acetylation; Alternative splicing; Cytoplasm; DNA-binding;
Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation; Zinc.
CHAIN 1..426
/note="Mothers against decapentaplegic homolog 7"
/id="PRO_0000090872"
DOMAIN 64..207
/note="MH1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00438"
DOMAIN 261..426
/note="MH2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00439"
REGION 208..217
/note="Important for interaction with SMURF2"
MOTIF 208..211
/note="PY-motif"
COMPBIAS 27..35
/note="Poly-Gly"
COMPBIAS 49..56
/note="Poly-Gly"
COMPBIAS 207..210
/note="Poly-Pro"
METAL 125
/note="Zinc"
/evidence="ECO:0000250"
METAL 180
/note="Zinc"
/evidence="ECO:0000250"
METAL 192
/note="Zinc"
/evidence="ECO:0000250"
METAL 197
/note="Zinc"
/evidence="ECO:0000250"
MOD_RES 64
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000269|PubMed:12408818"
MOD_RES 70
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000269|PubMed:12408818"
MOD_RES 249
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O35253,
ECO:0000255|PROSITE-ProRule:PRU00439"
CROSSLNK 64
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin); alternate"
/evidence="ECO:0000269|PubMed:12408818"
CROSSLNK 70
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin); alternate"
/evidence="ECO:0000269|PubMed:12408818"
VAR_SEQ 1..215
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_045197"
VAR_SEQ 223
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_047540"
MUTAGEN 64
/note="K->A: Loss of acetylation, and of SMURF1-dependent
degradation; when associated with A-70."
/evidence="ECO:0000269|PubMed:12408818"
MUTAGEN 70
/note="K->A: Loss of acetylation, and of SMURF1-dependent
degradation; when associated with A-64."
/evidence="ECO:0000269|PubMed:12408818"
MUTAGEN 207..211
/note="Missing: Diminishes interaction with SMURF2."
/evidence="ECO:0000269|PubMed:11163210"
MUTAGEN 211
/note="Y->A: Diminishes interaction with SMURF2 and reduces
inhibition of TGF-beta signaling."
/evidence="ECO:0000269|PubMed:11163210"
MUTAGEN 409..426
/note="Missing: 90% reduction in TGF-beta receptor
binding."
/evidence="ECO:0000269|PubMed:9215638"
CONFLICT 71
/note="G -> C (in Ref. 3; AAB81354)"
/evidence="ECO:0000305"
STRAND 204..206
/evidence="ECO:0000244|PDB:2DJY"
STRAND 212..214
/evidence="ECO:0000244|PDB:2DJY"
SEQUENCE 426 AA; 46426 MW; 5B76EC986776C102 CRC64;
MFRTKRSALV RRLWRSRAPG GEDEEEGAGG GGGGGELRGE GATDSRAHGA GGGGPGRAGC
CLGKAVRGAK GHHHPHPPAA GAGAAGGAEA DLKALTHSVL KKLKERQLEL LLQAVESRGG
TRTACLLLPG RLDCRLGPGA PAGAQPAQPP SSYSLPLLLC KVFRWPDLRH SSEVKRLCCC
ESYGKINPEL VCCNPHHLSR LCELESPPPP YSRYPMDFLK PTADCPDAVP SSAETGGTNY
LAPGGLSDSQ LLLEPGDRSH WCVVAYWEEK TRVGRLYCVQ EPSLDIFYDL PQGNGFCLGQ
LNSDNKSQLV QKVRSKIGCG IQLTREVDGV WVYNRSSYPI FIKSATLDNP DSRTLLVHKV
FPGFSIKAFD YEKAYSLQRP NDHEFMQQPW TGFTVQISFV KGWGQCYTRQ FISSCPCWLE
VIFNSR


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WP1161: TGF-beta Receptor Signaling Pathway
WP1370: TGF Beta Signaling Pathway
WP362: TGF-beta Receptor Signaling Pathway
WP809: TGF-beta Receptor Signaling Pathway
WP1780: ABC-family proteins mediated transport
WP1909: Signal regulatory protein (SIRP) family interactions
WP930: TGF Beta Signaling Pathway
WP230: TGF Beta Signaling Pathway
WP258: TGF-beta Receptor Signaling Pathway
WP113: TGF Beta Signaling Pathway
WP1367: TGF-beta Receptor Signaling Pathway
WP341: Nodal signaling pathway
WP560: TGF Beta Signaling Pathway
WP1834: Interactions of the immunoglobulin superfamily (IgSF) member proteins
WP926: TGF-beta Receptor Signaling Pathway
WP211: BMP signaling pathway
WP1048: TGF Beta Signaling Pathway
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[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)
[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)
[Smad7 Madh7] Mothers against decapentaplegic homolog 7 (MAD homolog 7) (Mothers against DPP homolog 7) (SMAD family member 7) (SMAD 7) (Smad7)
[SMAD6 MADH6] Mothers against decapentaplegic homolog 6 (MAD homolog 6) (Mothers against DPP homolog 6) (SMAD family member 6) (SMAD 6) (Smad6) (hSMAD6)
[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)
[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)
[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)
[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)
[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)
[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)
[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)
[Smad1 Mad1 Madh1] 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) (mMad3) (SMAD family member 3) (SMAD 3) (Smad3)
[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)
[Smox Dmel\CG2262 DSMAD2 DSmad2 dSMAD2 dSmad2 dsmad2 l(1)G0348 Sad sad Smad SMAD2 Smad2 smad2 SMOX SmoX smox ted tmp CG2262 Dmel_CG2262] Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member)
[SMAD4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (SMAD family member 4) (SMAD 4) (Smad4)
[Mad CG12399] Protein mothers against dpp
[ZFYVE9 MADHIP SARA SMADIP] Zinc finger FYVE domain-containing protein 9 (Mothers against decapentaplegic homolog-interacting protein) (Madh-interacting protein) (Novel serine protease) (NSP) (Receptor activation anchor) (hSARA) (Smad anchor for receptor activation)
[MAD2L2 MAD2B REV7] Mitotic spindle assembly checkpoint protein MAD2B (Mitotic arrest deficient 2-like protein 2) (MAD2-like protein 2) (REV7 homolog) (hREV7)
[ABCG1 ABC8 WHT1] ATP-binding cassette sub-family G member 1 (EC 7.6.2.-) (ATP-binding cassette transporter 8) (White protein homolog)
[Abcg1 Abc8 Wht1] ATP-binding cassette sub-family G member 1 (EC 7.6.2.-) (ATP-binding cassette transporter 8) (White protein homolog)
[Dana\GF20979 dana_GLEANR_4213 Dana_GF20979 GF20979] Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member)
[Dvir\GJ18762 Dvir_GJ18762 GJ18762] Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member)
[Dgri\GH24864 Dgri_GH24864] Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member)
[Dpse\GA15332 Dpse_GA15332 GA15332] Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member)
[Dyak\GE17479 Dyak_GE17479] Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member)
[Dmoj\GI14415 Dmoj_GI14415] Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member)

Bibliography :