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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_MOUSE             Reviewed;         467 AA.
Q62432; Q6GU18; Q6VP00; Q9D8P6;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
14-NOV-2006, sequence version 2.
26-FEB-2020, entry version 203.
RecName: Full=Mothers against decapentaplegic homolog 2;
Short=MAD homolog 2;
Short=Mothers against DPP homolog 2;
AltName: Full=Mad-related protein 2;
Short=mMad2;
AltName: Full=SMAD family member 2;
Short=SMAD 2;
Short=Smad2;
Name=Smad2; Synonyms=Madh2, Madr2;
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] (ISOFORM LONG).
STRAIN=129/Sv;
PubMed=8756346; DOI=10.1101/gad.10.15.1880;
Baker J.C., Harland R.M.;
"A novel mesoderm inducer, Madr2, functions in the activin signal
transduction pathway.";
Genes Dev. 10:1880-1889(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
STRAIN=A/J, and BALB/cJ;
PubMed=9328171; DOI=10.1093/carcin/18.9.1751;
Devereux T.R., Anna C.H., Patel A.C., White C.M., Festing M.F., You M.;
"Smad4 (homolog of human DPC4) and Smad2 (homolog of human JV18-1):
candidates for murine lung tumor resistance and suppressor genes.";
Carcinogenesis 18:1751-1755(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
PubMed=14701940; DOI=10.1210/me.2003-0264;
Bernard D.J.;
"Both SMAD2 and SMAD3 mediate activin-stimulated expression of the
follicle-stimulating hormone beta subunit in mouse gonadotrope cells.";
Mol. Endocrinol. 18:606-623(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
STRAIN=C57BL/6J; TISSUE=Pancreas;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
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).
[6]
REVIEW.
PubMed=10708952; DOI=10.1016/s1359-6101(99)00028-3;
Weinstein M., Yang X., Deng C.-X.;
"Functions of mammalian Smad genes as revealed by targeted gene disruption
in mice.";
Cytokine Growth Factor Rev. 11:49-58(2000).
[7]
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).
[8]
FUNCTION, 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).
[9]
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).
[10]
ALTERNATIVE SPLICING (ISOFORM SHORT).
PubMed=15630024; DOI=10.1101/gad.1243205;
Dunn N.R., Koonce C.H., Anderson D.C., Islam A., Bikoff E.K.,
Robertson E.J.;
"Mice exclusively expressing the short isoform of Smad2 develop normally
and are viable and fertile.";
Genes Dev. 19:152-163(2005).
[11]
PHOSPHORYLATION AT SER-465 AND SER-467.
PubMed=12672795; DOI=10.1074/jbc.m300075200;
Haller D., Holt L., Kim S.C., Schwabe R.F., Sartor R.B., Jobin C.;
"Transforming growth factor-beta 1 inhibits non-pathogenic Gram negative
bacteria-induced NF-kappa B recruitment to the interleukin-6 gene promoter
in intestinal epithelial cells through modulation of histone acetylation.";
J. Biol. Chem. 278:23851-23860(2003).
[12]
INTERACTION WITH AIP1.
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).
[13]
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).
[14]
INTERACTION WITH NEDD4L, AND UBIQUITINATION.
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).
[15]
INTERACTION WITH RNF111, PHOSPHORYLATION, 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).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
[17]
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).
-!- 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 SMAD2/SMAD4 complex, activates
transcription. May act as a tumor suppressor in colorectal carcinoma.
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:Q15796,
ECO:0000269|PubMed:15356634}.
-!- SUBUNIT: Monomer; the absence of TGF-beta. Interacts with ZNF580.
Heterodimer; in the presence of TGF-beta. Forms a heterodimer with co-
SMAD, SMAD4, in the nucleus to form the transactivation complex
SMAD2/SMAD4. Found in a complex with SMAD3 and TRIM33 upon addition of
TGF-beta. Interacts with ACVR1B, SMAD3 and TRIM33. Interacts (via the
MH2 domain) with ZFYVE9; may form trimers with the SMAD4 co-SMAD.
Interacts with FOXH1, homeobox protein TGIF, PEBP2-alpha subunit, CREB-
binding protein (CBP), EP300, SKI and SNW1. Interacts with SNON; when
phosphorylated at Ser-465/467. Interacts (via PY-motif) with SMURF2.
Interacts with SKOR1 and SKOR2. Interacts with PRDM16. Interacts (via
MH2 domain) with LEMD3. Interacts with RBPMS. 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. Interacts with NEDD4L in response to TGF-beta.
Interacts with WWP1, AIP1 and HGS. Interacts with PML. Interacts with
PDPK1 (via PH domain). Interacts with DAB2; the interactions are
enhanced upon TGF-beta stimulation. Interacts with USP15. Interacts
with PPP5C. Interacts with LDLRAD4 (via the SMAD interaction motif).
Interacts (via MH2 domain) with PMEPA1 (via the SMAD interaction
motif). Interacts with ZFHX3 (By similarity). Interacts with ZNF451.
Identified in a complex that contains at least ZNF451, SMAD2, SMAD3 and
SMAD4 (By similarity). Interacts weakly with ZNF8 (PubMed:12370310).
Interacts (when phosphorylated) with RNF111; RNF111 acts as an enhancer
of the transcriptional responses by mediating ubiquitination and
degradation of SMAD2 inhibitors (PubMed:17341133).
{ECO:0000250|UniProtKB:Q15796, ECO:0000269|PubMed:10681527,
ECO:0000269|PubMed:11094085, ECO:0000269|PubMed:12370310,
ECO:0000269|PubMed:15221015, ECO:0000269|PubMed:15356634,
ECO:0000269|PubMed:15496141, ECO:0000269|PubMed:17341133,
ECO:0000269|PubMed:22781750}.
-!- INTERACTION:
P97471:Smad4; NbExp=3; IntAct=EBI-2337932, EBI-5259270;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q15796}. Nucleus
{ECO:0000250|UniProtKB:Q15796}. Note=Cytoplasmic and nuclear in the
absence of TGF-beta. On TGF-beta stimulation, migrates to the nucleus
when complexed with SMAD4. On dephosphorylation by phosphatase PPM1A,
released from the SMAD2/SMAD4 complex, and exported out of the nucleus
by interaction with RANBP1. {ECO:0000250|UniProtKB:Q15796}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=mRNA corresponding to the isoform Long is approximately
20-fold more abundant. Both forms are coexpressed throughout mouse
development.;
Name=Long;
IsoId=Q62432-1; Sequence=Displayed;
Name=Short; Synonyms=Deltaexon3;
IsoId=Q62432-2; Sequence=VSP_021571;
-!- PTM: In response to TGF-beta, phosphorylated on the C-terminal SXS
motif by TGF-beta and activin type 1 receptor kinases, phosphorylation
declines progressively in a KMT5A-dependent manner. Phosphorylation in
this motif is required for interaction with a number of proteins
including SMURF2, SNON and SMAD4 in response to TGF-beta.
Dephosphorylated in this motif by PPM1A leading to disruption of the
SMAD2/3-SMAD4 complex, nuclear export and termination of the TGF-beta
signaling. In response to decorin, the naturally occurring inhibitor of
TGF-beta signaling, phosphorylated on Ser-240 by CaMK2. Phosphorylated
by MAPK3 upon EGF stimulation; which increases transcriptional activity
and stability, and is blocked by calmodulin. Phosphorylated by PDPK1.
{ECO:0000269|PubMed:12672795, ECO:0000269|PubMed:15356634,
ECO:0000269|PubMed:17341133}.
-!- PTM: In response to TGF-beta, ubiquitinated by NEDD4L; which promotes
its degradation. Monoubiquitinated, leading to prevent DNA-binding
(PubMed:15496141). Deubiquitination by USP15 alleviates inhibition and
promotes activation of TGF-beta target genes (By similarity).
Ubiquitinated by RNF111, leading to its degradation: only SMAD2
proteins that are 'in use' are targeted by RNF111, RNF111 playing a key
role in activating SMAD2 and regulating its turnover (PubMed:17341133).
{ECO:0000250|UniProtKB:Q15796, ECO:0000269|PubMed:15496141,
ECO:0000269|PubMed:17341133}.
-!- PTM: Acetylated on Lys-19 by coactivators in response to TGF-beta
signaling, which increases transcriptional activity.
{ECO:0000250|UniProtKB:Q15796}.
-!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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EMBL; U60530; AAB03612.1; -; mRNA.
EMBL; AF005743; AAB62269.1; -; mRNA.
EMBL; AK007817; BAB25282.1; -; mRNA.
EMBL; AY334552; AAR00933.1; -; mRNA.
EMBL; BC021342; AAH21342.1; -; mRNA.
EMBL; BC089184; AAH89184.1; -; mRNA.
CCDS; CCDS29350.1; -. [Q62432-1]
CCDS; CCDS79664.1; -. [Q62432-2]
RefSeq; NP_001239410.1; NM_001252481.1. [Q62432-1]
RefSeq; NP_001297999.1; NM_001311070.1. [Q62432-2]
RefSeq; NP_034884.2; NM_010754.5. [Q62432-1]
RefSeq; XP_006525762.1; XM_006525699.2. [Q62432-1]
RefSeq; XP_017173331.1; XM_017317842.1. [Q62432-2]
SMR; Q62432; -.
BioGrid; 201275; 34.
ComplexPortal; CPX-10; SMAD2-SMAD3-SMAD4 complex.
ComplexPortal; CPX-13; SMAD2 homotrimer.
ComplexPortal; CPX-3251; SMAD2-SMAD4 complex.
CORUM; Q62432; -.
IntAct; Q62432; 7.
MINT; Q62432; -.
STRING; 10090.ENSMUSP00000130115; -.
iPTMnet; Q62432; -.
PhosphoSitePlus; Q62432; -.
PaxDb; Q62432; -.
PeptideAtlas; Q62432; -.
PRIDE; Q62432; -.
Ensembl; ENSMUST00000025453; ENSMUSP00000025453; ENSMUSG00000024563. [Q62432-1]
Ensembl; ENSMUST00000091831; ENSMUSP00000089439; ENSMUSG00000024563. [Q62432-2]
Ensembl; ENSMUST00000168423; ENSMUSP00000130115; ENSMUSG00000024563. [Q62432-1]
GeneID; 17126; -.
KEGG; mmu:17126; -.
UCSC; uc008fqn.2; mouse. [Q62432-1]
UCSC; uc008fqo.2; mouse. [Q62432-2]
CTD; 4087; -.
MGI; MGI:108051; Smad2.
eggNOG; KOG3701; Eukaryota.
eggNOG; ENOG410XQKU; LUCA.
GeneTree; ENSGT00940000153499; -.
HOGENOM; CLU_026736_0_2_1; -.
InParanoid; Q62432; -.
KO; K04500; -.
OMA; PNNTEYN; -.
OrthoDB; 608001at2759; -.
PhylomeDB; Q62432; -.
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-9617828; FOXO-mediated transcription of cell cycle genes.
ChiTaRS; Smad2; mouse.
PRO; PR:Q62432; -.
Proteomes; UP000000589; Chromosome 18.
RNAct; Q62432; protein.
Bgee; ENSMUSG00000024563; Expressed in cochlea and 332 other tissues.
ExpressionAtlas; Q62432; baseline and differential.
Genevisible; Q62432; MM.
GO; GO:0032444; C:activin responsive factor complex; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0071144; C:heteromeric SMAD protein complex; ISO:MGI.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0071141; C:SMAD protein complex; ISO:MGI.
GO; GO:0005667; C:transcription factor complex; IDA:MGI.
GO; GO:0033613; F:activating transcription factor binding; ISO:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0070410; F:co-SMAD binding; ISO:MGI.
GO; GO:0097718; F:disordered domain specific 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; ISO:MGI.
GO; GO:0003690; F:double-stranded DNA binding; IDA:MGI.
GO; GO:0070411; F:I-SMAD binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019902; F:phosphatase binding; ISO:MGI.
GO; GO:0070878; F:primary miRNA binding; ISO:MGI.
GO; GO:0070412; F:R-SMAD binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0046332; F:SMAD binding; IPI:UniProtKB.
GO; GO:0048156; F:tau protein binding; IDA:ARUK-UCL.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0005160; F:transforming growth factor beta receptor binding; ISO:MGI.
GO; GO:0030618; F:transforming growth factor beta receptor, pathway-specific cytoplasmic mediator activity; ISO:MGI.
GO; GO:0034713; F:type I transforming growth factor beta receptor binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0032924; P:activin receptor signaling pathway; ISO:MGI.
GO; GO:0030325; P:adrenal gland development; ISO:MGI.
GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
GO; GO:0045165; P:cell fate commitment; IMP:MGI.
GO; GO:0007182; P:common-partner SMAD protein phosphorylation; 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:0001706; P:endoderm formation; IMP:MGI.
GO; GO:0007369; P:gastrulation; IGI:MGI.
GO; GO:0007507; P:heart development; IGI:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0030073; P:insulin secretion; IGI:MGI.
GO; GO:0035556; P:intracellular signal transduction; IDA:MGI.
GO; GO:0030324; P:lung development; IGI:MGI.
GO; GO:0001707; P:mesoderm formation; IMP:MGI.
GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0038092; P:nodal signaling pathway; ISO:MGI.
GO; GO:0035265; P:organ growth; IGI:MGI.
GO; GO:0031016; P:pancreas development; IGI:MGI.
GO; GO:0048340; P:paraxial mesoderm morphogenesis; IMP:MGI.
GO; GO:0007389; P:pattern specification process; IGI:MGI.
GO; GO:0060039; P:pericardium development; IGI:MGI.
GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISO:MGI.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
GO; GO:1900224; P:positive regulation of nodal signaling pathway involved in determination of lateral mesoderm left/right asymmetry; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0009791; P:post-embryonic development; IGI:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0051098; P:regulation of binding; IDA:MGI.
GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
GO; GO:0070723; P:response to cholesterol; ISO:MGI.
GO; GO:0009749; P:response to glucose; IGI:MGI.
GO; GO:0062009; P:secondary palate development; IMP:BHF-UCL.
GO; GO:0023019; P:signal transduction involved in regulation of gene expression; ISO:MGI.
GO; GO:0007183; P:SMAD protein complex assembly; ISO:MGI.
GO; GO:0060395; P:SMAD protein signal transduction; IGI:MGI.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:MGI.
GO; GO:0001657; P:ureteric bud development; IEP:UniProtKB.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
GO; GO:0007352; P:zygotic specification of dorsal/ventral axis; ISO:MGI.
Gene3D; 2.60.200.10; -; 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; Alternative splicing; Cytoplasm; DNA-binding; Metal-binding;
Nucleus; Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation; Zinc.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000250|UniProtKB:Q15796"
CHAIN 2..467
/note="Mothers against decapentaplegic homolog 2"
/id="PRO_0000090853"
DOMAIN 10..176
/note="MH1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00438"
DOMAIN 274..467
/note="MH2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00439"
MOTIF 221..225
/note="PY-motif"
/evidence="ECO:0000250"
METAL 74
/note="Zinc"
/evidence="ECO:0000250"
METAL 149
/note="Zinc"
/evidence="ECO:0000250"
METAL 161
/note="Zinc"
/evidence="ECO:0000250"
METAL 166
/note="Zinc"
/evidence="ECO:0000250"
MOD_RES 2
/note="N-acetylserine"
/evidence="ECO:0000250|UniProtKB:Q15796"
MOD_RES 8
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:Q15796"
MOD_RES 19
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:Q15796"
MOD_RES 220
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:Q15796"
MOD_RES 240
/note="Phosphoserine; by CAMK2"
/evidence="ECO:0000250|UniProtKB:Q15796,
ECO:0000255|PROSITE-ProRule:PRU00439"
MOD_RES 245
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q15796"
MOD_RES 250
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q15796"
MOD_RES 255
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q15796"
MOD_RES 458
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q15796,
ECO:0000255|PROSITE-ProRule:PRU00439"
MOD_RES 460
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q15796,
ECO:0000255|PROSITE-ProRule:PRU00439"
MOD_RES 464
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q15796,
ECO:0000255|PROSITE-ProRule:PRU00439"
MOD_RES 465
/note="Phosphoserine; by TGFBR1"
/evidence="ECO:0000250|UniProtKB:Q15796,
ECO:0000255|PROSITE-ProRule:PRU00439"
MOD_RES 467
/note="Phosphoserine; by TGFBR1"
/evidence="ECO:0000250|UniProtKB:Q15796,
ECO:0000255|PROSITE-ProRule:PRU00439"
VAR_SEQ 79..108
/note="Missing (in isoform Short)"
/evidence="ECO:0000303|PubMed:14701940"
/id="VSP_021571"
CONFLICT 42
/note="E -> Q (in Ref. 1; AAB03612 and 2; AAB62269)"
/evidence="ECO:0000305"
SEQUENCE 467 AA; 52266 MW; 31A2A36D463DB3E9 CRC64;
MSSILPFTPP VVKRLLGWKK SAGGSGGAGG GEQNGQEEKW CEKAVKSLVK KLKKTGRLDE
LEKAITTQNC NTKCVTIPST CSEIWGLSTA NTVDQWDTTG LYSFSEQTRS LDGRLQVSHR
KGLPHVIYCR LWRWPDLHSH HELKAIENCE YAFNLKKDEV CVNPYHYQRV ETPVLPPVLV
PRHTEILTEL PPLDDYTHSI PENTNFPAGI EPQSNYIPET PPPGYISEDG ETSDQQLNQS
MDTGSPAELS PTTLSPVNHS LDLQPVTYSE PAFWCSIAYY ELNQRVGETF HASQPSLTVD
GFTDPSNSER FCLGLLSNVN RNATVEMTRR HIGRGVRLYY IGGEVFAECL SDSAIFVQSP
NCNQRYGWHP ATVCKIPPGC NLKIFNNQEF AALLAQSVNQ GFEAVYQLTR MCTIRMSFVK
GWGAEYRRQT VTSTPCWIEL HLNGPLQWLD KVLTQMGSPS VRCSSMS


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Pathways :
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP32: Translation Factors
WP1596: Iron Homeostasis
WP2199: Seed Development
WP2272: Pathogenic Escherichia coli infection
WP1909: Signal regulatory protein (SIRP) family interactions
WP731: Sterol regulatory element binding protein related
WP860: EGFR1 Signaling Pathway
WP1493: Carbon assimilation C4 pathway
WP1714: Tyrosine metabolism
WP35: G Protein Signaling Pathways
WP1045: TGF-beta Receptor Signaling Pathway
WP1661: Glyoxylate and dicarboxylate metabolism
WP211: BMP signaling pathway
WP1096: EGFR1 Signaling Pathway
WP1672: Mismatch repair
WP2218: sGC
WP930: TGF Beta Signaling Pathway
WP1531: Vitamin D synthesis
WP1799: Costimulation by the CD28 family
WP488: Alpha6-Beta4 Integrin Signaling Pathway
WP1892: Protein folding
WP525: Mitochondrial Unfolded-Protein Response
WP1161: TGF-beta Receptor Signaling Pathway

Related Genes :
[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)
[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)
[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 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)
[SMAD6 MADH6] Mothers against decapentaplegic homolog 6 (MAD homolog 6) (Mothers against DPP homolog 6) (SMAD family member 6) (SMAD 6) (Smad6) (hSMAD6)
[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)
[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) (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)
[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)
[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)
[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)
[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)
[lin-35 C32F10.2] Retinoblastoma-like protein homolog lin-35 (Abnormal cell lineage protein 35) (Synthetic multivulva protein lin-35)
[Dyak\GE17479 Dyak_GE17479] 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)
[Dana\GF20979 dana_GLEANR_4213 Dana_GF20979 GF20979] Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member)
[Dnajb11] DnaJ homolog subfamily B member 11 (APOBEC1-binding protein 2) (ABBP-2) (ER-associated DNAJ) (ER-associated Hsp40 co-chaperone) (Endoplasmic reticulum DNA J domain-containing protein 3) (ER-resident protein ERdj3) (ERdj3) (ERj3p)
[Abcg1 Abc8 Wht1] ATP-binding cassette sub-family G member 1 (EC 7.6.2.-) (ATP-binding cassette transporter 8) (White protein homolog)
[Dvir\GJ18762 Dvir_GJ18762 GJ18762] Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member)
[cdc-48.2 C41C4.8] Transitional endoplasmic reticulum ATPase homolog 2 (EC 3.6.4.6) (Cell division cycle-related protein 48.2) (p97/CDC48 homolog 2)

Bibliography :