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Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (mMad3) (SMAD family member 3) (SMAD 3) (Smad3)

 SMAD3_MOUSE             Reviewed;         425 AA.
Q8BUN5; O09064; O09144; O14510; O35273; Q8BX84; Q92940; Q93002; Q9GKR4;
05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 2.
02-DEC-2020, entry version 177.
RecName: Full=Mothers against decapentaplegic homolog 3;
Short=MAD homolog 3;
Short=Mad3;
Short=Mothers against DPP homolog 3;
Short=mMad3;
AltName: Full=SMAD family member 3;
Short=SMAD 3;
Short=Smad3;
Name=Smad3; Synonyms=Madh3;
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=Brain;
PubMed=10331191; DOI=10.1292/jvms.61.213;
Kano K., Notani A., Nam S.-Y., Fujisawa M., Kurohmaru M., Hayashi Y.;
"Cloning and studies of the mouse cDNA encoding Smad3.";
J. Vet. Med. Sci. 61:213-219(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J;
Yang X., Xu X., Shen S., Deng C.;
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Head, and Hippocampus;
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 [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo;
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).
[5]
PHOSPHORYLATION AT SER-422; SER-423 AND SER-425.
PubMed=9380693; DOI=10.1073/pnas.94.20.10669;
Liu X., Sun Y., Constantinescu S.N., Karam E., Weinberg R.A., Lodish H.F.;
"Transforming growth factor beta-induced phosphorylation of Smad3 is
required for growth inhibition and transcriptional induction in epithelial
cells.";
Proc. Natl. Acad. Sci. U.S.A. 94:10669-10674(1997).
[6]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=10559937; DOI=10.1038/12971;
Ashcroft G.S., Yang X., Glick A.B., Weinstein M., Letterio J.L.,
Mizel D.E., Anzano M., Greenwell-Wild T., Wahl S.M., Deng C., Roberts A.B.;
"Mice lacking Smad3 show accelerated wound healing and an impaired local
inflammatory response.";
Nat. Cell Biol. 1:260-266(1999).
[7]
INTERACTION WITH AIP1, AND IDENTIFICATION IN A COMPLEX WITH AIP1; ACVR2A
AND ACVR1B.
PubMed=10681527; DOI=10.1074/jbc.275.8.5485;
Shoji H., Tsuchida K., Kishi H., Yamakawa N., Matsuzaki T., Liu Z.,
Nakamura T., Sugino H.;
"Identification and characterization of a PDZ protein that interacts with
activin types II receptors.";
J. Biol. Chem. 275:5485-5492(2000).
[8]
INTERACTION WITH HGS.
PubMed=11094085; DOI=10.1128/mcb.20.24.9346-9355.2000;
Miura S., Takeshita T., Asao H., Kimura Y., Murata K., Sasaki Y., Hanai J.,
Beppu H., Tsukazaki T., Wrana J.L., Miyazono K., Sugamura K.;
"Hgs (Hrs), a FYVE domain protein, is involved in Smad signaling through
cooperation with SARA.";
Mol. Cell. Biol. 20:9346-9355(2000).
[9]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=11585338; DOI=10.1359/jbmr.2001.16.10.1754;
Borton A.J., Frederick J.P., Datto M.B., Wang X.F., Weinstein R.S.;
"The loss of Smad3 results in a lower rate of bone formation and osteopenia
through dysregulation of osteoblast differentiation and apoptosis.";
J. Bone Miner. Res. 16:1754-1764(2001).
[10]
INTERACTION WITH ZNF8.
PubMed=12370310; DOI=10.1128/mcb.22.21.7633-7644.2002;
Jiao K., Zhou Y., Hogan B.L.M.;
"Identification of mZnf8, a mouse Kruppel-like transcriptional repressor,
as a novel nuclear interaction partner of Smad1.";
Mol. Cell. Biol. 22:7633-7644(2002).
[11]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=14617288; DOI=10.1046/j.1524-475x.2003.11614.x;
Ashcroft G.S., Mills S.J., Flanders K.C., Lyakh L.A., Anzano M.A.,
Gilliver S.C., Roberts A.B.;
"Role of Smad3 in the hormonal modulation of in vivo wound healing
responses.";
Wound Repair Regen. 11:468-473(2003).
[12]
INTERACTION WITH TGFB1I1.
PubMed=14755691; DOI=10.1002/jcb.10754;
Shibanuma M., Kim-Kaneyama J.-R., Sato S., Nose K.;
"A LIM protein, Hic-5, functions as a potential coactivator for Sp1.";
J. Cell. Biochem. 91:633-645(2004).
[13]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH PML
AND ZFYVE9/SARA.
PubMed=15356634; DOI=10.1038/nature02783;
Lin H.K., Bergmann S., Pandolfi P.P.;
"Cytoplasmic PML function in TGF-beta signalling.";
Nature 431:205-211(2004).
[14]
INTERACTION WITH WWP1.
PubMed=15221015; DOI=10.1038/sj.onc.1207885;
Komuro A., Imamura T., Saitoh M., Yoshida Y., Yamori T., Miyazono K.,
Miyazawa K.;
"Negative regulation of transforming growth factor-beta (TGF-beta)
signaling by WW domain-containing protein 1 (WWP1).";
Oncogene 23:6914-6923(2004).
[15]
INTERACTION WITH NEDD4L.
PubMed=15496141; DOI=10.1042/bj20040738;
Kuratomi G., Komuro A., Goto K., Shinozaki M., Miyazawa K., Miyazono K.,
Imamura T.;
"NEDD4-2 (neural precursor cell expressed, developmentally down-regulated
4-2) negatively regulates TGF-beta (transforming growth factor-beta)
signalling by inducing ubiquitin-mediated degradation of Smad2 and TGF-beta
type I receptor.";
Biochem. J. 386:461-470(2005).
[16]
INTERACTION WITH ZC3H3.
PubMed=16115198; DOI=10.1111/j.1365-2443.2005.00887.x;
Collart C., Remacle J.E., Barabino S., van Grunsven L.A., Nelles L.,
Schellens A., Van de Putte T., Pype S., Huylebroeck D., Verschueren K.;
"Smicl is a novel Smad interacting protein and cleavage and polyadenylation
specificity factor associated protein.";
Genes Cells 10:897-906(2005).
[17]
INTERACTION WITH PRDM16.
PubMed=17467076; DOI=10.1016/j.bbamcr.2007.03.016;
Warner D.R., Horn K.H., Mudd L., Webb C.L., Greene R.M., Pisano M.M.;
"PRDM16/MEL1: a novel Smad binding protein expressed in murine embryonic
orofacial tissue.";
Biochim. Biophys. Acta 1773:814-820(2007).
[18]
INTERACTION WITH TTRAP.
PubMed=18039968; DOI=10.1242/dev.000026;
Esguerra C.V., Nelles L., Vermeire L., Ibrahimi A., Crawford A.D.,
Derua R., Janssens E., Waelkens E., Carmeliet P., Collen D.,
Huylebroeck D.;
"Ttrap is an essential modulator of Smad3-dependent Nodal signaling during
zebrafish gastrulation and left-right axis determination.";
Development 134:4381-4393(2007).
[19]
INTERACTION WITH FOXL2.
PubMed=19106105; DOI=10.1074/jbc.m806676200;
Blount A.L., Schmidt K., Justice N.J., Vale W.W., Fischer W.H.,
Bilezikjian L.M.;
"FoxL2 and Smad3 coordinately regulate follistatin gene transcription.";
J. Biol. Chem. 284:7631-7645(2009).
[20]
INTERACTION WITH YAP1 AND SMAD4, AND SUBCELLULAR LOCATION.
PubMed=21145499; DOI=10.1016/j.devcel.2010.11.012;
Varelas X., Samavarchi-Tehrani P., Narimatsu M., Weiss A., Cockburn K.,
Larsen B.G., Rossant J., Wrana J.L.;
"The Crumbs complex couples cell density sensing to Hippo-dependent control
of the TGF-beta-SMAD pathway.";
Dev. Cell 19:831-844(2010).
[21]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=21035443; DOI=10.1016/j.yexmp.2010.10.011;
Kawakatsu M., Kanno S., Gui T., Gai Z., Itoh S., Tanishima H., Oikawa K.,
Muragaki Y.;
"Loss of Smad3 gives rise to poor soft callus formation and accelerates
early fracture healing.";
Exp. Mol. Pathol. 90:107-115(2011).
[22]
INTERACTION WITH PPP5C, AND SUBCELLULAR LOCATION.
PubMed=22781750; DOI=10.1016/j.cellsig.2012.07.003;
Bruce D.L., Macartney T., Yong W., Shou W., Sapkota G.P.;
"Protein phosphatase 5 modulates SMAD3 function in the transforming growth
factor-beta pathway.";
Cell. Signal. 24:1999-2006(2012).
[23]
INTERACTION WITH RNF111, AND UBIQUITINATION.
PubMed=17341133; DOI=10.1371/journal.pbio.0050067;
Mavrakis K.J., Andrew R.L., Lee K.L., Petropoulou C., Dixon J.E.,
Navaratnam N., Norris D.P., Episkopou V.;
"Arkadia enhances Nodal/TGF-beta signaling by coupling phospho-Smad2/3
activity and turnover.";
PLoS Biol. 5:E67-E67(2007).
-!- FUNCTION: Receptor-regulated SMAD (R-SMAD) that is an intracellular
signal transducer and transcriptional modulator activated by TGF-beta
(transforming growth factor) and activin type 1 receptor kinases. Binds
the TRE element in the promoter region of many genes that are regulated
by TGF-beta and, on formation of the SMAD3/SMAD4 complex, activates
transcription. Also can form a SMAD3/SMAD4/JUN/FOS complex at the AP-
1/SMAD site to regulate TGF-beta-mediated transcription. Has an
inhibitory effect on wound healing probably by modulating both growth
and migration of primary keratinocytes and by altering the TGF-mediated
chemotaxis of monocytes. This effect on wound healing appears to be
hormone-sensitive. Regulator of chondrogenesis and osteogenesis and
inhibits early healing of bone fractures. Positively regulates PDPK1
kinase activity by stimulating its dissociation from the 14-3-3 protein
YWHAQ which acts as a negative regulator (By similarity).
{ECO:0000250|UniProtKB:P84022, ECO:0000269|PubMed:10559937,
ECO:0000269|PubMed:11585338, ECO:0000269|PubMed:14617288,
ECO:0000269|PubMed:15356634, ECO:0000269|PubMed:21035443}.
-!- SUBUNIT: Monomer; in the absence of TGF-beta (By similarity).
Homooligomer; in the presence of TGF-beta (By similarity).
Heterotrimer; forms a heterotrimer in the presence of TGF-beta
consisting of two molecules of C-terminally phosphorylated SMAD2 or
SMAD3 and one of SMAD4 to form the transcriptionally active
SMAD2/SMAD3-SMAD4 complex (PubMed:21145499). Part of a complex
consisting of AIP1, ACVR2A, ACVR1B and SMAD3 (PubMed:15496141). Forms a
complex with SMAD2 and TRIM33 upon addition of TGF-beta (By
similarity). Found in a complex composed of SMAD3, RAN and XPO4; within
the complex interacts directly with XPO4 (By similarity). Component of
the multimeric complex SMAD3/SMAD4/JUN/FOS which forms at the AP1
promoter site; required for synergistic transcriptional activity in
response to TGF-beta (By similarity). Interacts (via an N-terminal
domain) with JUN (via its basic DNA binding and leucine zipper
domains); this interaction is essential for DNA binding and cooperative
transcriptional activity in response to TGF-beta (By similarity).
Identified in a complex that contains at least ZNF451, SMAD2, SMAD3 and
SMAD4 (By similarity). Interacts with PPM1A; the interaction
dephosphorylates SMAD3 in the C-terminal SXS motif leading to
disruption of the SMAD2/3-SMAD4 complex, nuclear export and termination
of TGF-beta signaling (By similarity). Interacts (via MH2 domain) with
ZMIZ1 (via SP-RING-type domain); in the TGF-beta signaling pathway
increases the activity of the SMAD3/SMAD4 transcriptional complex (By
similarity). Interacts (when phosphorylated) with RNF111; RNF111 acts
as an enhancer of the transcriptional responses by mediating
ubiquitination and degradation of SMAD3 inhibitors (PubMed:17341133).
Interacts (dephosphorylated form via the MH1 and MH2 domains) with
RANBP3 (via its C-terminal R domain); the interaction results in the
export of dephosphorylated SMAD3 out of the nucleus and termination of
the TGF-beta signaling (By similarity). Interacts (via MH2 domain) with
LEMD3; the interaction represses SMAD3 transcriptional activity through
preventing the formation of the heteromeric complex with SMAD4 and
translocation to the nucleus (By similarity). Interacts (via the linker
region) with EP300 (C-terminal); the interaction promotes SMAD3
acetylation and is enhanced by TGF-beta phosphorylation in the C-
terminal of SMAD3 (By similarity). This interaction can be blocked by
competitive binding of adenovirus oncoprotein E1A to the same C-
terminal site on EP300, which then results in partially inhibited
SMAD3/SMAD4 transcriptional activity (By similarity). Interacts with
TGFBR1 (By similarity). Interacts with TGFB1I1 (PubMed:14755691).
Interacts with PRDM16 (PubMed:17467076). Interacts with SNW1 (By
similarity). Interacts (via MH2 domain) with ZFYVE9 (PubMed:15356634).
Interacts with HDAC1 (By similarity). Interacts with TGIF2 (By
similarity). Interacts with SKOR1 (By similarity). Interacts with SKOR2
(By similarity). Interacts with DACH1; the interaction inhibits the
TGF-beta signaling (By similarity). Interacts with RBPMS (By
similarity). Interacts (via MH2 domain) with MECOM (By similarity).
Interacts with WWTR1 (via its coiled-coil domain) (By similarity).
Interacts with SKI; the interaction represses SMAD3 transcriptional
activity (By similarity). Interacts with MEN1 (By similarity).
Interacts with IL1F7 (By similarity). Interaction with CSNK1G2 (By
similarity). Interacts with PDPK1 (via PH domain) (By similarity).
Interacts with DAB2; the interactions are enhanced upon TGF-beta
stimulation (By similarity). Interacts with USP15 (By similarity).
Interacts with PPP5C; the interaction decreases SMAD3 phosphorylation
and protein levels (PubMed:22781750). Interacts with LDLRAD4 (via the
SMAD interaction motif) (By similarity). Interacts with PMEPA1 (By
similarity). Interacts with ZNF451 (By similarity). Interacts with
ZFHX3 (By similarity). Interacts weakly with ZNF8 (PubMed:12370310).
Interacts with STUB1, HSPA1A, HSPA1B, HSP90AA1 and HSP90AB1 (By
similarity). Interacts with YAP1 (when phosphorylated at 'Ser-112')
(PubMed:21145499). Interacts with AIP1 (PubMed:10681527). Interacts
(via MH2 domain) with CITED2 (via C-terminus) (By similarity).
Interacts with HGS (PubMed:11094085). Interacts with WWP1
(PubMed:15221015). Interacts with TTRAP (PubMed:18039968). Interacts
with FOXL2 (PubMed:19106105). Interacts with PML (PubMed:15356634).
Interacts with NEDD4L; the interaction requires TGF-beta stimulation
(PubMed:15496141). Interacts with ZC3H3 (PubMed:16115198). Interacts
with TGIF. Interacts with CREBBP. Interacts with ATF2.
{ECO:0000250|UniProtKB:P84022, ECO:0000250|UniProtKB:P84025,
ECO:0000269|PubMed:10681527, ECO:0000269|PubMed:11094085,
ECO:0000269|PubMed:12370310, ECO:0000269|PubMed:14755691,
ECO:0000269|PubMed:15221015, ECO:0000269|PubMed:15356634,
ECO:0000269|PubMed:15496141, ECO:0000269|PubMed:16115198,
ECO:0000269|PubMed:17341133, ECO:0000269|PubMed:17467076,
ECO:0000269|PubMed:18039968, ECO:0000269|PubMed:19106105,
ECO:0000269|PubMed:21145499, ECO:0000269|PubMed:22781750}.
-!- INTERACTION:
Q8BUN5; O35625: Axin1; NbExp=2; IntAct=EBI-2337983, EBI-2365912;
Q8BUN5; P20263: Pou5f1; NbExp=13; IntAct=EBI-2337983, EBI-1606219;
Q8BUN5; P97471: Smad4; NbExp=6; IntAct=EBI-2337983, EBI-5259270;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15356634,
ECO:0000269|PubMed:21145499, ECO:0000269|PubMed:22781750}. Nucleus
{ECO:0000269|PubMed:15356634, ECO:0000269|PubMed:21145499,
ECO:0000269|PubMed:22781750}. Note=Cytoplasmic and nuclear in the
absence of TGF-beta (PubMed:21145499). On TGF-beta stimulation,
migrates to the nucleus when complexed with SMAD4 (PubMed:21145499).
Through the action of the phosphatase PPM1A, released from the
SMAD2/SMAD4 complex, and exported out of the nucleus by interaction
with RANBP1 (By similarity). Co-localizes with LEMD3 at the nucleus
inner membrane (By similarity). MAPK-mediated phosphorylation appears
to have no effect on nuclear import. PDPK1 prevents its nuclear
translocation in response to TGF-beta (By similarity). Localized mainly
to the nucleus in the early stages of embryo development with
expression becoming evident in the cytoplasm of the inner cell mass at
the blastocyst stage (PubMed:21145499). {ECO:0000250|UniProtKB:P84022,
ECO:0000269|PubMed:21145499}.
-!- TISSUE SPECIFICITY: Highly expressed in the brain and ovary. Detected
in the pyramidal cells of the hippocampus, granule cells of the dentate
gyrus, granular cells of the cerebral cortex and the granulosa cells of
the ovary. {ECO:0000269|PubMed:10331191}.
-!- DOMAIN: The MH1 domain is required for DNA binding (By similarity).
Also binds zinc ions which are necessary for the DNA binding.
{ECO:0000250}.
-!- DOMAIN: The MH2 domain is required for both homomeric and heteromeric
interactions and for transcriptional regulation. Sufficient for nuclear
import (By similarity). {ECO:0000250}.
-!- DOMAIN: The linker region is required for the TGFbeta-mediated
transcriptional activity and acts synergistically with the MH2 domain.
{ECO:0000250}.
-!- PTM: Phosphorylated on serine and threonine residues. Enhanced
phosphorylation in the linker region on Thr-179, Ser-204 and Ser-208 on
EGF and TGF-beta treatment. Ser-208 is the main site of MAPK-mediated
phosphorylation. CDK-mediated phosphorylation occurs in a cell-cycle
dependent manner and inhibits both the transcriptional activity and
antiproliferative functions of SMAD3. This phosphorylation is inhibited
by flavopiridol. Maximum phosphorylation at the G(1)/S junction. Also
phosphorylated on serine residues in the C-terminal SXS motif by TGFBR1
and ACVR1. TGFBR1-mediated phosphorylation at these C-terminal sites is
required for interaction with SMAD4, nuclear location and
transactivational activity, and appears to be a prerequisite for the
TGF-beta mediated phosphorylation in the linker region.
Dephosphorylated in the C-terminal SXS motif by PPM1A. This
dephosphorylation disrupts the interaction with SMAD4, promotes nuclear
export and terminates TGF-beta-mediated signaling. Phosphorylation at
Ser-418 by CSNK1G2/CK1 promotes ligand-dependent ubiquitination and
subsequent proteasome degradation, thus inhibiting SMAD3-mediated TGF-
beta responses (By similarity). Phosphorylated by PDPK1 (By
similarity). {ECO:0000250|UniProtKB:P84022}.
-!- PTM: Acetylation in the nucleus by EP300 in the MH2 domain regulates
positively its transcriptional activity and is enhanced by TGF-beta.
{ECO:0000250|UniProtKB:P84022}.
-!- PTM: Ubiquitinated. Monoubiquitinated, leading to prevent DNA-binding.
Deubiquitination by USP15 alleviates inhibition and promotes activation
of TGF-beta target genes (By similarity). Ubiquitinated by RNF111,
leading to its degradation: only SMAD3 proteins that are 'in use' are
targeted by RNF111, RNF111 playing a key role in activating SMAD3 and
regulating its turnover (PubMed:17341133). Undergoes STUB1-mediated
ubiquitination and degradation (By similarity).
{ECO:0000250|UniProtKB:P84022, ECO:0000269|PubMed:17341133}.
-!- PTM: Poly-ADP-ribosylated by PARP1 and PARP2. ADP-ribosylation
negatively regulates SMAD3 transcriptional responses during the course
of TGF-beta signaling. {ECO:0000250|UniProtKB:P84022}.
-!- DISRUPTION PHENOTYPE: SMAD3 null mice exhibit inhibition of
proliferation of mammary gland epithelial cells. Fibrobasts are only
partially growth inhibited. Defects in osteoblast differentiation are
observed. Animals are osteopenic with less cortical and cancellous
bone. Facture healing is accelerated. Decreased bone mineral density
(BMD) reflects the inability of osteoblasts to balance osteoclast
activity. Wound healing is accelerated to about two and a half times
that of normal animals. Wound areas are significantly reduced with less
quantities of granulation tissue. There is reduced local infiltration
of moncytes and keratinocytes show altered patterns of growth and
migration. Accelerated wound healing is observed on castration of null
male mice, while null female mice exhibited delayed healing following
ovariectomy. {ECO:0000269|PubMed:10559937, ECO:0000269|PubMed:11585338,
ECO:0000269|PubMed:14617288, ECO:0000269|PubMed:21035443}.
-!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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EMBL; AB008192; BAA76956.1; -; mRNA.
EMBL; AF016189; AAB81755.1; -; mRNA.
EMBL; AK048626; BAC33398.1; -; mRNA.
EMBL; AK083158; BAC38789.1; -; mRNA.
EMBL; BC066850; AAH66850.1; -; mRNA.
CCDS; CCDS23272.1; -.
RefSeq; NP_058049.3; NM_016769.4.
SMR; Q8BUN5; -.
BioGRID; 201276; 70.
ComplexPortal; CPX-10; SMAD2-SMAD3-SMAD4 complex.
ComplexPortal; CPX-14; SMAD3 homotrimer.
ComplexPortal; CPX-3286; SMAD3-SMAD4 complex.
CORUM; Q8BUN5; -.
DIP; DIP-29717N; -.
IntAct; Q8BUN5; 47.
MINT; Q8BUN5; -.
STRING; 10090.ENSMUSP00000034973; -.
iPTMnet; Q8BUN5; -.
PhosphoSitePlus; Q8BUN5; -.
SwissPalm; Q8BUN5; -.
EPD; Q8BUN5; -.
MaxQB; Q8BUN5; -.
PaxDb; Q8BUN5; -.
PeptideAtlas; Q8BUN5; -.
PRIDE; Q8BUN5; -.
Antibodypedia; 26224; 2236 antibodies.
Ensembl; ENSMUST00000034973; ENSMUSP00000034973; ENSMUSG00000032402.
GeneID; 17127; -.
KEGG; mmu:17127; -.
UCSC; uc009qbi.1; mouse.
CTD; 4088; -.
MGI; MGI:1201674; Smad3.
eggNOG; KOG3701; Eukaryota.
GeneTree; ENSGT00940000153499; -.
HOGENOM; CLU_026736_0_0_1; -.
InParanoid; Q8BUN5; -.
OMA; NPVSPAH; -.
OrthoDB; 608001at2759; -.
PhylomeDB; Q8BUN5; -.
TreeFam; TF314923; -.
Reactome; R-MMU-1181150; Signaling by NODAL.
Reactome; R-MMU-1502540; Signaling by Activin.
Reactome; R-MMU-2173788; Downregulation of TGF-beta receptor signaling.
Reactome; R-MMU-2173789; TGF-beta receptor signaling activates SMADs.
Reactome; R-MMU-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
Reactome; R-MMU-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
Reactome; R-MMU-8941855; RUNX3 regulates CDKN1A transcription.
Reactome; R-MMU-9617828; FOXO-mediated transcription of cell cycle genes.
BioGRID-ORCS; 17127; 1 hit in 19 CRISPR screens.
ChiTaRS; Smad3; mouse.
PRO; PR:Q8BUN5; -.
Proteomes; UP000000589; Chromosome 9.
RNAct; Q8BUN5; protein.
Bgee; ENSMUSG00000032402; Expressed in secondary oocyte and 318 other tissues.
ExpressionAtlas; Q8BUN5; baseline and differential.
Genevisible; Q8BUN5; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0071144; C:heteromeric SMAD protein complex; ISO:MGI.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005637; C:nuclear inner membrane; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0043235; C:receptor complex; ISO:MGI.
GO; GO:0071141; C:SMAD protein complex; ISS:UniProtKB.
GO; GO:0005667; C:transcription regulator complex; ISS:UniProtKB.
GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
GO; GO:0043425; F:bHLH transcription factor binding; ISO:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0031490; F:chromatin DNA binding; IDA:BHF-UCL.
GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0070410; F:co-SMAD binding; ISO:MGI.
GO; GO:0005518; F:collagen binding; IPI:MGI.
GO; GO:0017151; F:DEAD/H-box RNA helicase binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; ISO:MGI.
GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IPI:ARUK-UCL.
GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:MGI.
GO; GO:0003690; F:double-stranded DNA binding; IDA:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0035259; F:glucocorticoid receptor binding; ISO:MGI.
GO; GO:0070411; F:I-SMAD binding; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0031962; F:mineralocorticoid receptor binding; ISO:MGI.
GO; GO:0019902; F:phosphatase binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0070412; F:R-SMAD binding; ISO:MGI.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
GO; GO:0046332; F:SMAD binding; ISO:MGI.
GO; GO:0001223; F:transcription coactivator binding; ISO:MGI.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0005160; F:transforming growth factor beta receptor binding; ISO:MGI.
GO; GO:0043130; F:ubiquitin binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; ISO:MGI.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
GO; GO:0097296; P:activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; ISO:MGI.
GO; GO:0032924; P:activin receptor signaling pathway; ISO:MGI.
GO; GO:0030325; P:adrenal gland development; ISO:MGI.
GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
GO; GO:0007050; P:cell cycle arrest; ISO:MGI.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0045216; P:cell-cell junction organization; ISO:MGI.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:MGI.
GO; GO:0048589; P:developmental growth; IGI:MGI.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IGI:MGI.
GO; GO:0048617; P:embryonic foregut morphogenesis; IGI:MGI.
GO; GO:0009880; P:embryonic pattern specification; IGI:MGI.
GO; GO:0007492; P:endoderm development; IGI:MGI.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:0007369; P:gastrulation; IGI:MGI.
GO; GO:0001947; P:heart looping; IGI:MGI.
GO; GO:0006955; P:immune response; ISO:MGI.
GO; GO:0002520; P:immune system development; IGI:MGI.
GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
GO; GO:0070306; P:lens fiber cell differentiation; IMP:MGI.
GO; GO:0001889; P:liver development; IGI:MGI.
GO; GO:0001707; P:mesoderm formation; IMP:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:1903243; P:negative regulation of cardiac muscle hypertrophy in response to stress; ISO:MGI.
GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; ISO:MGI.
GO; GO:0045599; P:negative regulation of fat cell differentiation; ISO:MGI.
GO; GO:0050728; P:negative regulation of inflammatory response; IMP:UniProtKB.
GO; GO:0061767; P:negative regulation of lung blood pressure; ISO:MGI.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; ISO:MGI.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; IGI:MGI.
GO; GO:0033689; P:negative regulation of osteoblast proliferation; IMP:UniProtKB.
GO; GO:0042177; P:negative regulation of protein catabolic process; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0061045; P:negative regulation of wound healing; IMP:UniProtKB.
GO; GO:0038092; P:nodal signaling pathway; ISO:MGI.
GO; GO:0002076; P:osteoblast development; IGI:MGI.
GO; GO:0001649; P:osteoblast differentiation; IMP:UniProtKB.
GO; GO:0048340; P:paraxial mesoderm morphogenesis; IMP:MGI.
GO; GO:0060039; P:pericardium development; IGI:MGI.
GO; GO:0010694; P:positive regulation of alkaline phosphatase activity; ISO:MGI.
GO; GO:0030501; P:positive regulation of bone mineralization; ISO:MGI.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IMP:UniProtKB.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISO:MGI.
GO; GO:1901203; P:positive regulation of extracellular matrix assembly; ISO:MGI.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISO:MGI.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
GO; GO:0050927; P:positive regulation of positive chemotaxis; ISO:MGI.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription by RNA polymerase II; ISO:MGI.
GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0032916; P:positive regulation of transforming growth factor beta3 production; ISO:MGI.
GO; GO:0050821; P:protein stabilization; ISO:MGI.
GO; GO:0051098; P:regulation of binding; IDA:MGI.
GO; GO:0050678; P:regulation of epithelial cell proliferation; IMP:MGI.
GO; GO:0050776; P:regulation of immune response; IMP:UniProtKB.
GO; GO:0016202; P:regulation of striated muscle tissue development; IDA:MGI.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IDA:MGI.
GO; GO:0032909; P:regulation of transforming growth factor beta2 production; ISO:MGI.
GO; GO:0001666; P:response to hypoxia; ISO:MGI.
GO; GO:0023019; P:signal transduction involved in regulation of gene expression; ISO:MGI.
GO; GO:0001501; P:skeletal system development; IGI:MGI.
GO; GO:0007183; P:SMAD protein complex assembly; ISO:MGI.
GO; GO:0060395; P:SMAD protein signal transduction; IGI:MGI.
GO; GO:0001756; P:somitogenesis; IMP:MGI.
GO; GO:0042110; P:T cell activation; IMP:UniProtKB.
GO; GO:0030878; P:thyroid gland development; IGI:MGI.
GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
GO; GO:0060290; P:transdifferentiation; ISO:MGI.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:MGI.
GO; GO:0001657; P:ureteric bud development; IEP:UniProtKB.
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;
Acetylation; ADP-ribosylation; Cytoplasm; Isopeptide bond; Metal-binding;
Nucleus; Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation; Zinc.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000250|UniProtKB:P84022"
CHAIN 2..425
/note="Mothers against decapentaplegic homolog 3"
/id="PRO_0000090857"
DOMAIN 10..136
/note="MH1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00438"
DOMAIN 232..425
/note="MH2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00439"
REGION 137..231
/note="Linker"
REGION 271..324
/note="Sufficient for interaction with XPO4"
/evidence="ECO:0000250"
METAL 64
/note="Zinc"
/evidence="ECO:0000250"
METAL 109
/note="Zinc"
/evidence="ECO:0000250"
METAL 121
/note="Zinc"
/evidence="ECO:0000250"
METAL 126
/note="Zinc"
/evidence="ECO:0000250"
SITE 40
/note="Required for trimerization"
/evidence="ECO:0000250"
SITE 41
/note="Required for interaction with DNA and JUN and for
functional cooperation with JUN"
/evidence="ECO:0000250"
MOD_RES 2
/note="N-acetylserine"
/evidence="ECO:0000250|UniProtKB:P84022"
MOD_RES 8
/note="Phosphothreonine; by CDK2 and CDK4"
/evidence="ECO:0000250|UniProtKB:P84022"
MOD_RES 179
/note="Phosphothreonine; by CDK2, CDK4 and MAPK"
/evidence="ECO:0000250|UniProtKB:P84022"
MOD_RES 204
/note="Phosphoserine; by GSK3 and MAPK"
/evidence="ECO:0000250|UniProtKB:P84022,
ECO:0000255|PROSITE-ProRule:PRU00439"
MOD_RES 208
/note="Phosphoserine; by MAPK"
/evidence="ECO:0000250|UniProtKB:P84022,
ECO:0000255|PROSITE-ProRule:PRU00439"
MOD_RES 213
/note="Phosphoserine; by CDK2 and CDK4"
/evidence="ECO:0000250|UniProtKB:P84022,
ECO:0000255|PROSITE-ProRule:PRU00439"
MOD_RES 378
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P84022"
MOD_RES 416
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P84022,
ECO:0000255|PROSITE-ProRule:PRU00439"
MOD_RES 418
/note="Phosphoserine; by CK1"
/evidence="ECO:0000250|UniProtKB:P84022,
ECO:0000255|PROSITE-ProRule:PRU00439"
MOD_RES 422
/note="Phosphoserine; by TGFBR1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00439,
ECO:0000269|PubMed:9380693"
MOD_RES 423
/note="Phosphoserine; by TGFBR1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00439,
ECO:0000269|PubMed:9380693"
MOD_RES 425
/note="Phosphoserine; by TGFBR1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00439,
ECO:0000269|PubMed:9380693"
CROSSLNK 33
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:P84022"
CROSSLNK 81
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:P84022"
CONFLICT 26
/note="Q -> E (in Ref. 3; BAC38789)"
/evidence="ECO:0000305"
CONFLICT 269
/note="F -> L (in Ref. 2; AAB81755)"
/evidence="ECO:0000305"
CONFLICT 408
/note="D -> V (in Ref. 3; BAC33398)"
/evidence="ECO:0000305"
SEQUENCE 425 AA; 48081 MW; 46DF5E8B371321AC CRC64;
MSSILPFTPP IVKRLLGWKK GEQNGQEEKW CEKAVKSLVK KLKKTGQLDE LEKAITTQNV
NTKCITIPRS LDGRLQVSHR KGLPHVIYCR LWRWPDLHSH HELRAMELCE FAFNMKKDEV
CVNPYHYQRV ETPVLPPVLV PRHTEIPAEF PPLDDYSHSI PENTNFPAGI EPQSNIPETP
PPGYLSEDGE TSDHQMNHSM DAGSPNLSPN PMSPAHNNLD LQPVTYCEPA FWCSISYYEL
NQRVGETFHA SQPSMTVDGF TDPSNSERFC LGLLSNVNRN AAVELTRRHI GRGVRLYYIG
GEVFAECLSD SAIFVQSPNC NQRYGWHPAT VCKIPPGCNL KIFNNQEFAA LLAQSVNQGF
EAVYQLTRMC TIRMSFVKGW GAEYRRQTVT STPCWIELHL NGPLQWLDKV LTQMGSPSIR
CSSVS


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Pathways :
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP32: Translation Factors
WP1596: Iron Homeostasis
WP414: Cell Cycle and Cell Division
WP930: TGF Beta Signaling Pathway
WP1003: Ovarian Infertility Genes
WP2039: CDKN1A-EGF-CREB
WP759: Alpha6-Beta4 Integrin Signaling Pathway
WP1174: Senescence and Autophagy
WP783: Androgen Receptor Signaling Pathway
WP1267: Senescence and Autophagy
WP485: Alpha6-Beta4 Integrin Signaling Pathway
WP946: Delta-Notch Signaling Pathway
WP1052: Id Signaling Pathway
WP980: Wnt Signaling Pathway NetPath
WP1083: Cell cycle
WP258: TGF-beta Receptor Signaling Pathway
WP815: Id Signaling Pathway
WP155: Adipogenesis
WP505: TGF Beta Signaling Pathway
WP179: Cell cycle
WP560: TGF Beta Signaling Pathway
WP1103: Alpha6-Beta4 Integrin Signaling Pathway
WP273: Ovarian Infertility Genes

Related Genes :
[Smad3 Madh3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (mMad3) (SMAD family member 3) (SMAD 3) (Smad3)
[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)
[SMAD3 MADH3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (SMAD family member 3) (SMAD 3) (Smad3)
[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 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)
[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)
[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)
[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)
[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)
[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)
[SMAD6 MADH6] Mothers against decapentaplegic homolog 6 (MAD homolog 6) (Mothers against DPP homolog 6) (SMAD family member 6) (SMAD 6) (Smad6) (hSMAD6)
[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)
[Smad7 Madh7] Mothers against decapentaplegic homolog 7 (MAD homolog 7) (Mothers against DPP homolog 7) (SMAD family member 7) (SMAD 7) (Smad7)
[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)
[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)
[BUB1B BUBR1 MAD3L SSK1] Mitotic checkpoint serine/threonine-protein kinase BUB1 beta (EC 2.7.11.1) (MAD3/BUB1-related protein kinase) (hBUBR1) (Mitotic checkpoint kinase MAD3L) (Protein SSK1)
[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)
[Mad CG12399] Protein mothers against dpp
[NFKBIA IKBA MAD3 NFKBI] NF-kappa-B inhibitor alpha (I-kappa-B-alpha) (IkB-alpha) (IkappaBalpha) (Major histocompatibility complex enhancer-binding protein MAD3)
[Dper\GL20193 Dper_GL20193] Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member)
[Dsec\GM11208 Dsec_GM11208] Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member)
[Bcar3] Breast cancer anti-estrogen resistance protein 3 homolog (BCAR3 adapter protein, NSP family member) (Novel SH2-containing protein 2) (SH2 domain-containing protein 3B) (p130Cas-binding protein AND-34)
[Dana\GF20979 dana_GLEANR_4213 Dana_GF20979 GF20979] Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member)
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[Bcar3 And34] Breast cancer anti-estrogen resistance protein 3 homolog (p130Cas-binding protein AND-34)

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