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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.
31-JAN-2018, entry version 186.
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]
UniGene; Mm.152699; -.
UniGene; Mm.490934; -.
ProteinModelPortal; Q62432; -.
SMR; Q62432; -.
BioGrid; 201275; 35.
CORUM; Q62432; -.
IntAct; Q62432; 5.
MINT; MINT-99148; -.
STRING; 10090.ENSMUSP00000025453; -.
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; ENSGT00760000119091; -.
HOGENOM; HOG000286018; -.
HOVERGEN; HBG053353; -.
InParanoid; Q62432; -.
KO; K04500; -.
OMA; DEICINP; -.
OrthoDB; EOG091G082C; -.
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.
ChiTaRS; Smad2; mouse.
PRO; PR:Q62432; -.
Proteomes; UP000000589; Chromosome 18.
Bgee; ENSMUSG00000024563; -.
CleanEx; MM_SMAD2; -.
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:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein 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: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:0046982; F:protein heterodimerization activity; IDA:MGI.
GO; GO:0042803; F:protein homodimerization activity; IDA:MGI.
GO; GO:0070412; F:R-SMAD binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; ISO:MGI.
GO; GO:0046332; F:SMAD binding; IPI:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; ISO:MGI.
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: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 proliferation; IEA:Ensembl.
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:0060021; P:palate development; IMP:BHF-UCL.
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 from RNA polymerase II promoter; 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:0023019; P:signal transduction involved in regulation of gene expression; IEA:Ensembl.
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.
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; 2.
PROSITE; PS51075; MH1; 1.
PROSITE; PS51076; MH2; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation; Zinc.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q15796}.
CHAIN 2 467 Mothers against decapentaplegic homolog
2.
/FTId=PRO_0000090853.
DOMAIN 10 176 MH1. {ECO:0000255|PROSITE-
ProRule:PRU00438}.
DOMAIN 274 467 MH2. {ECO:0000255|PROSITE-
ProRule:PRU00439}.
MOTIF 221 225 PY-motif. {ECO:0000250}.
METAL 74 74 Zinc. {ECO:0000250}.
METAL 149 149 Zinc. {ECO:0000250}.
METAL 161 161 Zinc. {ECO:0000250}.
METAL 166 166 Zinc. {ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:Q15796}.
MOD_RES 8 8 Phosphothreonine.
{ECO:0000250|UniProtKB:Q15796}.
MOD_RES 19 19 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q15796}.
MOD_RES 240 240 Phosphoserine; by CAMK2.
{ECO:0000250|UniProtKB:Q15796,
ECO:0000255|PROSITE-ProRule:PRU00439}.
MOD_RES 458 458 Phosphoserine.
{ECO:0000250|UniProtKB:Q15796,
ECO:0000255|PROSITE-ProRule:PRU00439}.
MOD_RES 460 460 Phosphoserine.
{ECO:0000250|UniProtKB:Q15796,
ECO:0000255|PROSITE-ProRule:PRU00439}.
MOD_RES 464 464 Phosphoserine.
{ECO:0000250|UniProtKB:Q15796,
ECO:0000255|PROSITE-ProRule:PRU00439}.
MOD_RES 465 465 Phosphoserine; by TGFBR1.
{ECO:0000250|UniProtKB:Q15796,
ECO:0000255|PROSITE-ProRule:PRU00439}.
MOD_RES 467 467 Phosphoserine; by TGFBR1.
{ECO:0000250|UniProtKB:Q15796,
ECO:0000255|PROSITE-ProRule:PRU00439}.
VAR_SEQ 79 108 Missing (in isoform Short).
{ECO:0000303|PubMed:14701940}.
/FTId=VSP_021571.
CONFLICT 42 42 E -> Q (in Ref. 1; AAB03612 and 2;
AAB62269). {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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