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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)

 SMAD2_HUMAN             Reviewed;         467 AA.
Q15796;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 205.
RecName: Full=Mothers against decapentaplegic homolog 2;
Short=MAD homolog 2;
Short=Mothers against DPP homolog 2;
AltName: Full=JV18-1;
AltName: Full=Mad-related protein 2;
Short=hMAD-2;
AltName: Full=SMAD family member 2;
Short=SMAD 2;
Short=Smad2;
Short=hSMAD2;
Name=SMAD2; Synonyms=MADH2, MADR2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANT
344-GLU--GLN-358 DEL.
PubMed=8673135; DOI=10.1038/ng0796-347;
Riggins G.J., Thiagalingam S., Rosenblum E., Weinstein C.L.,
Kern S.E., Hamilton S.R., Willson J.K.V., Markowitz S.D.,
Kinzler K.W., Vogelstein B.V.;
"Mad-related genes in the human.";
Nat. Genet. 13:347-349(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
TISSUE=Placenta;
PubMed=8774881; DOI=10.1038/383168a0;
Zhang Y., Feng X.-H., Wu R.-Y., Derynck R.;
"Receptor-associated Mad homologues synergize as effectors of the TGF-
beta response.";
Nature 383:168-172(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), PHOSPHORYLATION BY TGFBR1,
AND VARIANTS CYS-133; ARG-440; HIS-445 AND GLU-450.
TISSUE=Kidney;
PubMed=8752209; DOI=10.1016/S0092-8674(00)80128-2;
Eppert K., Scherer S.W., Ozcelik H., Pirone R., Hoodless P., Kim H.,
Tsui L.-C., Bapat B., Gallinger S., Andrulis I.L., Thomsen G.H.,
Wrana J.L., Attisano L.;
"MADR2 maps to 18q21 and encodes a TGFbeta-regulated MAD-related
protein that is functionally mutated in colorectal carcinoma.";
Cell 86:543-552(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
PubMed=9389648; DOI=10.1101/gad.11.23.3157;
Liu F., Pouponnot C., Massague J.;
"Dual role of the Smad4/DPC4 tumor suppressor in TGFbeta-inducible
transcriptional complexes.";
Genes Dev. 11:3157-3167(1997).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS LONG AND SHORT).
PubMed=9503010; DOI=10.1006/geno.1997.5149;
Takenoshita S., Mogi A., Nagashima M., Yang K., Yagi K., Hanyu A.,
Nagamachi Y., Miyazono K., Hagiwara K.;
"Characterization of the MADH2/Smad2 gene, a human Mad homolog
responsible for the transforming growth factor-beta and activin signal
transduction pathway.";
Genomics 48:1-11(1998).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
TISSUE=Kidney, Pancreas, and Spleen;
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).
[7]
PROTEIN SEQUENCE OF 2-14 AND 170-182, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Chronic myeloid leukemia cell;
Bienvenut W.V., von Kriegsheim A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[8]
INTERACTION WITH TGFBR1, PHOSPHORYLATION AT SER-464; SER-465 AND
SER-467, AND MUTAGENESIS OF SER-464; SER-465 AND SER-467.
PubMed=8980228; DOI=10.1016/S0092-8674(00)81817-6;
Macias-Silva M., Abdollah S., Hoodless P.A., Pirone R., Attisano L.,
Wrana J.L.;
"MADR2 is a substrate of the TGFbeta receptor and its phosphorylation
is required for nuclear accumulation and signaling.";
Cell 87:1215-1224(1996).
[9]
INTERACTION WITH ZFYVE9, AND SUBCELLULAR LOCATION.
PubMed=9865696; DOI=10.1016/S0092-8674(00)81701-8;
Tsukazaki T., Chiang T.A., Davison A.F., Attisano L., Wrana J.L.;
"SARA, a FYVE domain protein that recruits Smad2 to the TGFbeta
receptor.";
Cell 95:779-791(1998).
[10]
SUBUNIT.
PubMed=9670020; DOI=10.1093/emboj/17.14.4056;
Kawabata M., Inoue H., Hanyu A., Imamura T., Miyazono K.;
"Smad proteins exist as monomers in vivo and undergo homo- and hetero-
oligomerization upon activation by serine/threonine kinase
receptors.";
EMBO J. 17:4056-4065(1998).
[11]
ALTERNATIVE SPLICING (ISOFORMS LONG AND SHORT).
PubMed=9873005; DOI=10.1074/jbc.274.2.703;
Yagi K., Goto D., Hamamoto T., Takenoshita S., Kato M., Miyazono K.;
"Alternatively spliced variant of Smad2 lacking exon 3. Comparison
with wild-type Smad2 and Smad3.";
J. Biol. Chem. 274:703-709(1999).
[12]
PHOSPHORYLATION AT SER-465 AND SER-467.
PubMed=9136927; DOI=10.1101/gad.11.8.984;
Kretzschmar M., Liu F., Hata A., Doody J., Massague J.;
"The TGF-beta family mediator Smad1 is phosphorylated directly and
activated functionally by the BMP receptor kinase.";
Genes Dev. 11:984-995(1997).
[13]
PHOSPHORYLATION AT SER-465 AND SER-467 BY TGFBR1.
PubMed=9346908; DOI=10.1074/jbc.272.44.27678;
Abdollah S., Macias-Silva M., Tsukazaki T., Hayashi H., Attisano L.,
Wrana J.L.;
"TbetaRI phosphorylation of Smad2 on Ser465 and Ser467 is required for
Smad2-Smad4 complex formation and signaling.";
J. Biol. Chem. 272:27678-27685(1997).
[14]
INTERACTION WITH FOXH1.
TISSUE=Colon adenocarcinoma;
PubMed=9702198; DOI=10.1016/S1097-2765(00)80120-3;
Zhou S., Zawel L., Lengauer C., Kinzler K.W., Vogelstein B.;
"Characterization of human FAST-1, a TGF beta and activin signal
transducer.";
Mol. Cell 2:121-127(1998).
[15]
INTERACTION WITH ACVR1B, AND FUNCTION.
PubMed=9892009; DOI=10.1210/mend.13.1.0218;
Lebrun J.J., Takabe K., Chen Y., Vale W.;
"Roles of pathway-specific and inhibitory Smads in activin receptor
signaling.";
Mol. Endocrinol. 13:15-23(1999).
[16]
INTERACTION WITH DAB2.
PubMed=11387212; DOI=10.1093/emboj/20.11.2789;
Hocevar B.A., Smine A., Xu X.X., Howe P.H.;
"The adaptor molecule Disabled-2 links the transforming growth factor
beta receptors to the Smad pathway.";
EMBO J. 20:2789-2801(2001).
[17]
INTERACTION WITH SNW1.
PubMed=11278756; DOI=10.1074/jbc.M010815200;
Leong G.M., Subramaniam N., Figueroa J., Flanagan J.L., Hayman M.J.,
Eisman J.A., Kouzmenko A.P.;
"Ski-interacting protein interacts with Smad proteins to augment
transforming growth factor-beta-dependent transcription.";
J. Biol. Chem. 276:18243-18248(2001).
[18]
INTERACTION WITH SMURF2, AND MUTAGENESIS OF 221-PRO--TYR-225.
PubMed=11389444; DOI=10.1038/35078562;
Bonni S., Wang H.R., Causing C.G., Kavsak P., Stroschein S.L., Luo K.,
Wrana J.L.;
"TGF-beta induces assembly of a Smad2-Smurf2 ubiquitin ligase complex
that targets SnoN for degradation.";
Nat. Cell Biol. 3:587-595(2001).
[19]
PHOSPHORYLATION AT SER-240.
PubMed=11879191; DOI=10.1042/0264-6021:3620643;
Abdel-Wahab N., Wicks S.J., Mason R.M., Chantry A.;
"Decorin suppresses transforming growth factor-beta-induced expression
of plasminogen activator inhibitor-1 in human mesangial cells through
a mechanism that involves Ca2+-dependent phosphorylation of Smad2 at
serine-240.";
Biochem. J. 362:643-649(2002).
[20]
PHOSPHORYLATION AT THR-8; THR-220; SER-245; SER-250 AND SER-255.
PubMed=12193595; DOI=10.1074/jbc.M204597200;
Funaba M., Zimmerman C.M., Mathews L.S.;
"Modulation of Smad2-mediated signaling by extracellular signal-
regulated kinase.";
J. Biol. Chem. 277:41361-41368(2002).
[21]
INTERACTION WITH LEMD3.
PubMed=15601644; DOI=10.1093/hmg/ddi040;
Lin F., Morrison J.M., Wu W., Worman H.J.;
"MAN1, an integral protein of the inner nuclear membrane, binds Smad2
and Smad3 and antagonizes transforming growth factor-beta signaling.";
Hum. Mol. Genet. 14:437-445(2005).
[22]
INTERACTION WITH LEMD3.
PubMed=15647271; DOI=10.1074/jbc.M411234200;
Pan D., Estevez-Salmeron L.D., Stroschein S.L., Zhu X., He J.,
Zhou S., Luo K.;
"The integral inner nuclear membrane protein MAN1 physically interacts
with the R-Smad proteins to repress signaling by the transforming
growth factor-{beta} superfamily of cytokines.";
J. Biol. Chem. 280:15992-16001(2005).
[23]
INTERACTION WITH SKOR2.
PubMed=16200078; DOI=10.1038/labinvest.3700344;
Arndt S., Poser I., Schubert T., Moser M., Bosserhoff A.-K.;
"Cloning and functional characterization of a new Ski homolog, Fussel-
18, specifically expressed in neuronal tissues.";
Lab. Invest. 85:1330-1341(2005).
[24]
INTERACTION WITH PPM1A, DEPHOSPHORYLATION, FUNCTION, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF VAL-398; SER-465 AND SER-467.
PubMed=16751101; DOI=10.1016/j.cell.2006.03.044;
Lin X., Duan X., Liang Y.Y., Su Y., Wrighton K.H., Long J., Hu M.,
Davis C.M., Wang J., Brunicardi F.C., Shi Y., Chen Y.G., Meng A.,
Feng X.H.;
"PPM1A functions as a Smad phosphatase to terminate TGFbeta
signaling.";
Cell 125:915-928(2006).
[25]
IDENTIFICATION IN A COMPLEX WITH SMAD3 AND TRIM33, AND INTERACTION
WITH TRIM33.
PubMed=16751102; DOI=10.1016/j.cell.2006.03.045;
He W., Dorn D.C., Erdjument-Bromage H., Tempst P., Moore M.A.,
Massague J.;
"Hematopoiesis controlled by distinct TIF1gamma and Smad4 branches of
the TGFbeta pathway.";
Cell 125:929-941(2006).
[26]
ACETYLATION AT LYS-19, AND MUTAGENESIS OF LYS-19 AND LYS-20.
PubMed=17074756; DOI=10.1074/jbc.M607868200;
Simonsson M., Kanduri M., Gronroos E., Heldin C.H., Ericsson J.;
"The DNA binding activities of Smad2 and Smad3 are regulated by
coactivator-mediated acetylation.";
J. Biol. Chem. 281:39870-39880(2006).
[27]
INTERACTION WITH RBPMS.
PubMed=17099224; DOI=10.1093/nar/gkl914;
Sun Y., Ding L., Zhang H., Han J., Yang X., Yan J., Zhu Y., Li J.,
Song H., Ye Q.;
"Potentiation of Smad-mediated transcriptional activation by the RNA-
binding protein RBPMS.";
Nucleic Acids Res. 34:6314-6326(2006).
[28]
FUNCTION, PHOSPHORYLATION BY PDPK1, AND INTERACTION WITH PDPK1.
PubMed=17327236; DOI=10.1074/jbc.M609279200;
Seong H.A., Jung H., Kim K.T., Ha H.;
"3-Phosphoinositide-dependent PDK1 negatively regulates transforming
growth factor-beta-induced signaling in a kinase-dependent manner
through physical interaction with Smad proteins.";
J. Biol. Chem. 282:12272-12289(2007).
[29]
INTERACTION WITH SKOR1.
PubMed=17292623; DOI=10.1016/j.mcn.2007.01.002;
Arndt S., Poser I., Moser M., Bosserhoff A.-K.;
"Fussel-15, a novel Ski/Sno homolog protein, antagonizes BMP
signaling.";
Mol. Cell. Neurosci. 34:603-611(2007).
[30]
ACETYLATION, AND FUNCTION.
PubMed=16862174; DOI=10.1038/sj.onc.1209826;
Inoue Y., Itoh Y., Abe K., Okamoto T., Daitoku H., Fukamizu A.,
Onozaki K., Hayashi H.;
"Smad3 is acetylated by p300/CBP to regulate its transactivation
activity.";
Oncogene 26:500-508(2007).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[32]
INTERACTION WITH WWTR1.
PubMed=18568018; DOI=10.1038/ncb1748;
Varelas X., Sakuma R., Samavarchi-Tehrani P., Peerani R., Rao B.M.,
Dembowy J., Yaffe M.B., Zandstra P.W., Wrana J.L.;
"TAZ controls Smad nucleocytoplasmic shuttling and regulates human
embryonic stem-cell self-renewal.";
Nat. Cell Biol. 10:837-848(2008).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[34]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[35]
INTERACTION WITH RANBP3, SUBCELLULAR LOCATION, FUNCTION, AND
MUTAGENESIS OF 465-SER--SER-467.
PubMed=19289081; DOI=10.1016/j.devcel.2009.01.022;
Dai F., Lin X., Chang C., Feng X.H.;
"Nuclear export of Smad2 and Smad3 by RanBP3 facilitates termination
of TGF-beta signaling.";
Dev. Cell 16:345-357(2009).
[36]
INTERACTION WITH PRDM16.
PubMed=19049980; DOI=10.1074/jbc.M808989200;
Takahata M., Inoue Y., Tsuda H., Imoto I., Koinuma D., Hayashi M.,
Ichikura T., Yamori T., Nagasaki K., Yoshida M., Matsuoka M.,
Morishita K., Yuki K., Hanyu A., Miyazawa K., Inazawa J., Miyazono K.,
Imamura T.;
"SKI and MEL1 cooperate to inhibit transforming growth factor-beta
signal in gastric cancer cells.";
J. Biol. Chem. 284:3334-3344(2009).
[37]
INTERACTION WITH PMEPA1, AND MUTAGENESIS OF TRP-368.
PubMed=20129061; DOI=10.1016/j.molcel.2009.10.028;
Watanabe Y., Itoh S., Goto T., Ohnishi E., Inamitsu M., Itoh F.,
Satoh K., Wiercinska E., Yang W., Shi L., Tanaka A., Nakano N.,
Mommaas A.M., Shibuya H., Ten Dijke P., Kato M.;
"TMEPAI, a transmembrane TGF-beta-inducible protein, sequesters Smad
proteins from active participation in TGF-beta signaling.";
Mol. Cell 37:123-134(2010).
[38]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT THR-8; SER-458 AND SER-460, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[39]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[40]
INTERACTION WITH ZNF580, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=21599657; DOI=10.1042/CBI20110050;
Luo Y., Hu W., Xu R., Hou B., Zhang L., Zhang W.;
"ZNF580, a novel C2H2 zinc-finger transcription factor, interacts with
the TGF-beta signal molecule Smad2.";
Cell Biol. Int. 35:1153-1157(2011).
[41]
UBIQUITINATION, DEUBIQUITINATION BY USP15, DNA-BINDING, AND
INTERACTION WITH USP15.
PubMed=21947082; DOI=10.1038/ncb2346;
Inui M., Manfrin A., Mamidi A., Martello G., Morsut L., Soligo S.,
Enzo E., Moro S., Polo S., Dupont S., Cordenonsi M., Piccolo S.;
"USP15 is a deubiquitylating enzyme for receptor-activated SMADs.";
Nat. Cell Biol. 13:1368-1375(2011).
[42]
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).
[43]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[44]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[45]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8 AND SER-458, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[46]
PHOSPHORYLATION AT SER-465 AND SER-467.
PubMed=23478445; DOI=10.1016/j.molcel.2013.02.003;
Abbas T., Mueller A.C., Shibata E., Keaton M., Rossi M., Dutta A.;
"CRL1-FBXO11 promotes Cdt2 ubiquitylation and degradation and
regulates Pr-Set7/Set8-mediated cellular migration.";
Mol. Cell 49:1147-1158(2013).
[47]
INTERACTION WITH ZNF451, AND IDENTIFICATION IN A COMPLEX WITH ZNF451;
SMAD3 AND SMAD4.
PubMed=24324267; DOI=10.1074/jbc.M113.526905;
Feng Y., Wu H., Xu Y., Zhang Z., Liu T., Lin X., Feng X.H.;
"Zinc finger protein 451 is a novel Smad corepressor in transforming
growth factor-beta signaling.";
J. Biol. Chem. 289:2072-2083(2014).
[48]
INTERACTION WITH LDLRAD4.
PubMed=24627487; DOI=10.1074/jbc.M114.558981;
Nakano N., Maeyama K., Sakata N., Itoh F., Akatsu R., Nakata M.,
Katsu Y., Ikeno S., Togawa Y., Vo Nguyen T.T., Watanabe Y., Kato M.,
Itoh S.;
"C18 ORF1, a novel negative regulator of transforming growth factor-
beta signaling.";
J. Biol. Chem. 289:12680-12692(2014).
[49]
REVIEW.
PubMed=9759503; DOI=10.1146/annurev.biochem.67.1.753;
Massague J.;
"TGF-beta signal transduction.";
Annu. Rev. Biochem. 67:753-791(1998).
[50]
REVIEW.
PubMed=10647776; DOI=10.1016/S1359-6101(99)00012-X;
Verschueren K., Huylebroeck D.;
"Remarkable versatility of Smad proteins in the nucleus of
transforming growth factor-beta activated cells.";
Cytokine Growth Factor Rev. 10:187-199(1999).
[51]
REVIEW.
PubMed=10708948; DOI=10.1016/S1359-6101(99)00024-6;
Wrana J.L., Attisano L.;
"The Smad pathway.";
Cytokine Growth Factor Rev. 11:5-13(2000).
[52]
REVIEW.
PubMed=10708949; DOI=10.1016/S1359-6101(99)00025-8;
Miyazono K.;
"TGF-beta signaling by Smad proteins.";
Cytokine Growth Factor Rev. 11:15-22(2000).
[53]
INTERACTION WITH ZFHX3.
PubMed=25105025; DOI=10.1155/2014/970346;
Sakata N., Kaneko S., Ikeno S., Miura Y., Nakabayashi H., Dong X.Y.,
Dong J.T., Tamaoki T., Nakano N., Itoh S.;
"TGF-beta signaling cooperates with AT motif-binding factor-1 for
repression of the alpha -fetoprotein promoter.";
J. Signal Transduct. 2014:970346-970346(2014).
[54]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 261-456 IN COMPLEX WITH
ZFYVE9, INTERACTION WITH SARA, AND MUTAGENESIS OF ASN-381.
PubMed=10615055; DOI=10.1126/science.287.5450.92;
Wu G., Chen Y.-G., Ozdamar B., Gyuricza C.A., Chong P.A., Wrana J.L.,
Massague J., Shi Y.;
"Structural basis of Smad2 recognition by the Smad anchor for receptor
activation.";
Science 287:92-97(2000).
[55]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 270-466 IN COMPLEX WITH
SMAD4, AND SUBUNIT.
PubMed=15350224; DOI=10.1016/j.molcel.2004.07.016;
Chacko B.M., Qin B.Y., Tiwari A., Shi G., Lam S., Hayward L.J.,
De Caestecker M., Lin K.;
"Structural basis of heteromeric smad protein assembly in TGF-beta
signaling.";
Mol. Cell 15:813-823(2004).
[56]
VARIANT [LARGE SCALE ANALYSIS] VAL-300.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- 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.
{ECO:0000269|PubMed:16751101, ECO:0000269|PubMed:16862174,
ECO:0000269|PubMed:17327236, ECO:0000269|PubMed:19289081,
ECO:0000269|PubMed:9892009}.
-!- SUBUNIT: Monomer; the absence of TGF-beta. Heterodimer; in the
presence of TGF-beta. Forms a heterodimer with co-SMAD, SMAD4, in
the nucleus to form the transactivation complex SMAD2/SMAD4.
Interacts with AIP1, HGS, PML and WWP1 (By similarity). Interacts
with NEDD4L in response to TGF-beta (By similarity). 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 with SKOR1 and SKOR2.
Interacts with PRDM16. Interacts (via MH2 domain) with LEMD3.
Interacts with RBPMS. Interacts with WWP1. 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 PDPK1 (via
PH domain). Interacts with DAB2; the interactions are enhanced
upon TGF-beta stimulation. Interacts with USP15. Interacts with
PPP5C. Interacts with ZNF580. Interacts with LDLRAD4 (via the SMAD
interaction motif). Interacts (via MH2 domain) with PMEPA1 (via
the SMAD interaction motif). Interacts with ZFHX3. Interacts with
ZNF451 (PubMed:24324267). Identified in a complex that contains at
least ZNF451, SMAD2, SMAD3 and SMAD4 (PubMed:24324267). Interacts
weakly with ZNF8 (By similarity). Interacts (when phosphorylated)
with RNF111; RNF111 acts as an enhancer of the transcriptional
responses by mediating ubiquitination and degradation of SMAD2
inhibitors (By similarity). {ECO:0000250|UniProtKB:Q62432,
ECO:0000269|PubMed:10615055, ECO:0000269|PubMed:11278756,
ECO:0000269|PubMed:11387212, ECO:0000269|PubMed:11389444,
ECO:0000269|PubMed:15350224, ECO:0000269|PubMed:15601644,
ECO:0000269|PubMed:15647271, ECO:0000269|PubMed:16200078,
ECO:0000269|PubMed:16751101, ECO:0000269|PubMed:16751102,
ECO:0000269|PubMed:17099224, ECO:0000269|PubMed:17292623,
ECO:0000269|PubMed:17327236, ECO:0000269|PubMed:18568018,
ECO:0000269|PubMed:19049980, ECO:0000269|PubMed:19289081,
ECO:0000269|PubMed:20129061, ECO:0000269|PubMed:21599657,
ECO:0000269|PubMed:21947082, ECO:0000269|PubMed:22781750,
ECO:0000269|PubMed:24324267, ECO:0000269|PubMed:24627487,
ECO:0000269|PubMed:25105025, ECO:0000269|PubMed:8980228,
ECO:0000269|PubMed:9670020, ECO:0000269|PubMed:9702198,
ECO:0000269|PubMed:9865696, ECO:0000269|PubMed:9892009}.
-!- INTERACTION:
Q12955:ANK3; NbExp=2; IntAct=EBI-1040141, EBI-2691178;
P05060:CHGB; NbExp=2; IntAct=EBI-1040141, EBI-712619;
O15111:CHUK; NbExp=2; IntAct=EBI-1040141, EBI-81249;
P98082:DAB2; NbExp=4; IntAct=EBI-1040141, EBI-1171238;
Q9BZ29:DOCK9; NbExp=3; IntAct=EBI-1040141, EBI-2695893;
O75593:FOXH1; NbExp=3; IntAct=EBI-1040141, EBI-1759806;
P70056:foxh1 (xeno); NbExp=4; IntAct=EBI-1040141, EBI-9969973;
P05412:JUN; NbExp=3; IntAct=EBI-1040141, EBI-852823;
Q9NYA4:MTMR4; NbExp=2; IntAct=EBI-1040141, EBI-1052346;
P07197:NEFM; NbExp=3; IntAct=EBI-1040141, EBI-1105035;
Q8TAK6:OLIG1; NbExp=2; IntAct=EBI-1040141, EBI-3867416;
P35813:PPM1A; NbExp=2; IntAct=EBI-1040141, EBI-989143;
Q9H6Z4:RANBP3; NbExp=2; IntAct=EBI-1040141, EBI-992681;
P61586:RHOA; NbExp=2; IntAct=EBI-1040141, EBI-446668;
P12755:SKI; NbExp=10; IntAct=EBI-1040141, EBI-347281;
P84022:SMAD3; NbExp=2; IntAct=EBI-1040141, EBI-347161;
Q13485:SMAD4; NbExp=20; IntAct=EBI-1040141, EBI-347263;
Q9HAU4:SMURF2; NbExp=6; IntAct=EBI-1040141, EBI-396727;
Q13573:SNW1; NbExp=3; IntAct=EBI-1040141, EBI-632715;
P04637:TP53; NbExp=7; IntAct=EBI-1040141, EBI-366083;
Q9H3D4:TP63; NbExp=3; IntAct=EBI-1040141, EBI-2337775;
Q9UPN9:TRIM33; NbExp=6; IntAct=EBI-1040141, EBI-2214398;
O00308:WWP2; NbExp=4; IntAct=EBI-1040141, EBI-743923;
Q96KR1:ZFR; NbExp=2; IntAct=EBI-1040141, EBI-2513582;
O95405:ZFYVE9; NbExp=2; IntAct=EBI-1040141, EBI-296817;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16751101,
ECO:0000269|PubMed:19289081, ECO:0000269|PubMed:9865696}. Nucleus
{ECO:0000269|PubMed:16751101, ECO:0000269|PubMed:19289081,
ECO:0000269|PubMed:21599657, ECO:0000269|PubMed:22781750,
ECO:0000269|PubMed:9865696}. Note=Cytoplasmic and nuclear in the
absence of TGF-beta. On TGF-beta stimulation, migrates to the
nucleus when complexed with SMAD4 (PubMed:9865696). On
dephosphorylation by phosphatase PPM1A, released from the
SMAD2/SMAD4 complex, and exported out of the nucleus by
interaction with RANBP1 (PubMed:16751101, PubMed:19289081).
{ECO:0000269|PubMed:16751101, ECO:0000269|PubMed:19289081,
ECO:0000269|PubMed:9865696}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=Q15796-1; Sequence=Displayed;
Name=Short; Synonyms=Smad2Deltaexon3;
IsoId=Q15796-2; Sequence=VSP_006178;
-!- TISSUE SPECIFICITY: Expressed at high levels in skeletal muscle,
endothelial cells, heart and placenta.
{ECO:0000269|PubMed:21599657}.
-!- PTM: Phosphorylated on one or several of Thr-220, Ser-245, Ser-
250, and Ser-255. In response to TGF-beta, phosphorylated on Ser-
465/467 by TGF-beta and activin type 1 receptor kinases. TGF-beta-
induced Ser-465/467 phosphorylation declines progressively in a
KMT5A-dependent manner. Able to interact with SMURF2 when
phosphorylated on Ser-465/467, recruiting other proteins, such as
SNON, for degradation. 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:11879191, ECO:0000269|PubMed:12193595,
ECO:0000269|PubMed:17327236, ECO:0000269|PubMed:23478445,
ECO:0000269|PubMed:8752209, ECO:0000269|PubMed:8980228,
ECO:0000269|PubMed:9136927, ECO:0000269|PubMed:9346908}.
-!- PTM: In response to TGF-beta, ubiquitinated by NEDD4L; which
promotes its degradation. Monoubiquitinated, leading to prevent
DNA-binding (By similarity). Deubiquitination by USP15 alleviates
inhibition and promotes activation of TGF-beta target genes
(PubMed:21947082). 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 (By similarity).
{ECO:0000250|UniProtKB:Q62432, ECO:0000269|PubMed:21947082}.
-!- PTM: Acetylated on Lys-19 by coactivators in response to TGF-beta
signaling, which increases transcriptional activity. Isoform
short: Acetylation increases DNA binding activity in vitro and
enhances its association with target promoters in vivo.
Acetylation in the nucleus by EP300 is enhanced by TGF-beta.
{ECO:0000269|PubMed:16862174, ECO:0000269|PubMed:17074756,
ECO:0000269|Ref.7}.
-!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/SMAD2ID370.html";
-----------------------------------------------------------------------
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EMBL; U59911; AAC50789.1; -; mRNA.
EMBL; U68018; AAB17087.1; -; mRNA.
EMBL; U65019; AAB17054.1; -; mRNA.
EMBL; AF027964; AAC51918.1; -; mRNA.
EMBL; U78733; AAC39657.1; -; Genomic_DNA.
EMBL; U78727; AAC39657.1; JOINED; Genomic_DNA.
EMBL; U78728; AAC39657.1; JOINED; Genomic_DNA.
EMBL; U78729; AAC39657.1; JOINED; Genomic_DNA.
EMBL; U78730; AAC39657.1; JOINED; Genomic_DNA.
EMBL; U78731; AAC39657.1; JOINED; Genomic_DNA.
EMBL; U78732; AAC39657.1; JOINED; Genomic_DNA.
EMBL; BC014840; AAH14840.1; -; mRNA.
EMBL; BC025699; AAH25699.1; -; mRNA.
CCDS; CCDS11934.1; -. [Q15796-1]
PIR; S71797; S71797.
RefSeq; NP_001003652.1; NM_001003652.3. [Q15796-1]
RefSeq; NP_005892.1; NM_005901.5. [Q15796-1]
RefSeq; XP_005258316.1; XM_005258259.3. [Q15796-1]
RefSeq; XP_006722514.1; XM_006722451.3. [Q15796-1]
RefSeq; XP_016881234.1; XM_017025745.1. [Q15796-1]
RefSeq; XP_016881235.1; XM_017025746.1. [Q15796-2]
UniGene; Hs.12253; -.
UniGene; Hs.705764; -.
UniGene; Hs.741342; -.
PDB; 1DEV; X-ray; 2.20 A; A/C=261-456.
PDB; 1KHX; X-ray; 1.80 A; A=241-467.
PDB; 1U7V; X-ray; 2.70 A; A/C=270-467.
PDB; 2LB3; NMR; -; B=217-224.
PDBsum; 1DEV; -.
PDBsum; 1KHX; -.
PDBsum; 1U7V; -.
PDBsum; 2LB3; -.
ProteinModelPortal; Q15796; -.
SMR; Q15796; -.
BioGrid; 110262; 264.
CORUM; Q15796; -.
DIP; DIP-29716N; -.
IntAct; Q15796; 225.
MINT; MINT-5006109; -.
STRING; 9606.ENSP00000262160; -.
ChEMBL; CHEMBL2396512; -.
DrugBank; DB04522; Phosphonoserine.
iPTMnet; Q15796; -.
PhosphoSitePlus; Q15796; -.
BioMuta; SMAD2; -.
DMDM; 13633914; -.
EPD; Q15796; -.
PaxDb; Q15796; -.
PeptideAtlas; Q15796; -.
PRIDE; Q15796; -.
DNASU; 4087; -.
Ensembl; ENST00000262160; ENSP00000262160; ENSG00000175387. [Q15796-1]
Ensembl; ENST00000356825; ENSP00000349282; ENSG00000175387. [Q15796-2]
Ensembl; ENST00000402690; ENSP00000384449; ENSG00000175387. [Q15796-1]
Ensembl; ENST00000586040; ENSP00000466193; ENSG00000175387. [Q15796-2]
GeneID; 4087; -.
KEGG; hsa:4087; -.
UCSC; uc010xdc.4; human. [Q15796-1]
CTD; 4087; -.
DisGeNET; 4087; -.
EuPathDB; HostDB:ENSG00000175387.15; -.
GeneCards; SMAD2; -.
HGNC; HGNC:6768; SMAD2.
HPA; CAB025507; -.
HPA; CAB073546; -.
HPA; HPA067203; -.
MalaCards; SMAD2; -.
MIM; 601366; gene.
neXtProt; NX_Q15796; -.
OpenTargets; ENSG00000175387; -.
PharmGKB; PA134959722; -.
eggNOG; KOG3701; Eukaryota.
eggNOG; ENOG410XQKU; LUCA.
GeneTree; ENSGT00760000119091; -.
HOGENOM; HOG000286018; -.
HOVERGEN; HBG053353; -.
InParanoid; Q15796; -.
KO; K04500; -.
OMA; DEICINP; -.
OrthoDB; EOG091G082C; -.
PhylomeDB; Q15796; -.
TreeFam; TF314923; -.
Reactome; R-HSA-1181150; Signaling by NODAL.
Reactome; R-HSA-1502540; Signaling by Activin.
Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling.
Reactome; R-HSA-2173789; TGF-beta receptor signaling activates SMADs.
Reactome; R-HSA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
Reactome; R-HSA-3304356; SMAD2/3 Phosphorylation Motif Mutants in Cancer.
Reactome; R-HSA-3311021; SMAD4 MH2 Domain Mutants in Cancer.
Reactome; R-HSA-3315487; SMAD2/3 MH2 Domain Mutants in Cancer.
Reactome; R-HSA-3656532; TGFBR1 KD Mutants in Cancer.
Reactome; R-HSA-452723; Transcriptional regulation of pluripotent stem cells.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
SignaLink; Q15796; -.
SIGNOR; Q15796; -.
ChiTaRS; SMAD2; human.
EvolutionaryTrace; Q15796; -.
GeneWiki; Mothers_against_decapentaplegic_homolog_2; -.
GenomeRNAi; 4087; -.
PRO; PR:Q15796; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000175387; -.
CleanEx; HS_SMAD2; -.
ExpressionAtlas; Q15796; baseline and differential.
Genevisible; Q15796; HS.
GO; GO:0032444; C:activin responsive factor complex; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IMP:CAFA.
GO; GO:0071141; C:SMAD protein complex; IDA:UniProtKB.
GO; GO:0071144; C:SMAD2-SMAD3 protein complex; IDA:BHF-UCL.
GO; GO:0005667; C:transcription factor complex; IDA:BHF-UCL.
GO; GO:0033613; F:activating transcription factor binding; IPI:UniProtKB.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0070410; F:co-SMAD binding; IPI:BHF-UCL.
GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
GO; GO:0035326; F:enhancer binding; IC:BHF-UCL.
GO; GO:0070411; F:I-SMAD binding; IPI:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019902; F:phosphatase binding; IPI:UniProtKB.
GO; GO:0070878; F:primary miRNA binding; IPI:BHF-UCL.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0070412; F:R-SMAD binding; IPI:BHF-UCL.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0046332; F:SMAD binding; IPI:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0005160; F:transforming growth factor beta receptor binding; IPI:BHF-UCL.
GO; GO:0030618; F:transforming growth factor beta receptor, pathway-specific cytoplasmic mediator activity; IDA:BHF-UCL.
GO; GO:0034713; F:type I transforming growth factor beta receptor binding; IPI:BHF-UCL.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL.
GO; GO:0032924; P:activin receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0009952; P:anterior/posterior pattern specification; ISS:UniProtKB.
GO; GO:0045165; P:cell fate commitment; ISS:UniProtKB.
GO; GO:0007182; P:common-partner SMAD protein phosphorylation; IDA:MGI.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl.
GO; GO:0048617; P:embryonic foregut morphogenesis; IEA:Ensembl.
GO; GO:0001706; P:endoderm formation; IEA:Ensembl.
GO; GO:0007369; P:gastrulation; TAS:BHF-UCL.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
GO; GO:0030324; P:lung development; IEA:Ensembl.
GO; GO:0001707; P:mesoderm formation; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:BHF-UCL.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; TAS:Reactome.
GO; GO:0038092; P:nodal signaling pathway; IMP:BHF-UCL.
GO; GO:0035265; P:organ growth; IEA:Ensembl.
GO; GO:0060021; P:palate development; ISS:BHF-UCL.
GO; GO:0031016; P:pancreas development; IEA:Ensembl.
GO; GO:0048340; P:paraxial mesoderm morphogenesis; ISS:UniProtKB.
GO; GO:0060039; P:pericardium development; IEA:Ensembl.
GO; GO:0030513; P:positive regulation of BMP signaling pathway; IMP:BHF-UCL.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISS:BHF-UCL.
GO; GO:1900224; P:positive regulation of nodal signaling pathway involved in determination of lateral mesoderm left/right asymmetry; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
GO; GO:0031053; P:primary miRNA processing; TAS:BHF-UCL.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0051098; P:regulation of binding; ISS:UniProtKB.
GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0070723; P:response to cholesterol; IDA:BHF-UCL.
GO; GO:0009749; P:response to glucose; IEA:Ensembl.
GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IEA:Ensembl.
GO; GO:0007183; P:SMAD protein complex assembly; IDA:BHF-UCL.
GO; GO:0060395; P:SMAD protein signal transduction; IEA:Ensembl.
GO; GO:0035019; P:somatic stem cell population maintenance; TAS:Reactome.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
GO; GO:0007352; P:zygotic specification of dorsal/ventral axis; IMP:BHF-UCL.
Gene3D; 2.60.200.10; -; 1.
Gene3D; 3.90.520.10; -; 1.
InterPro; IPR013790; Dwarfin.
InterPro; IPR003619; MAD_homology1_Dwarfin-type.
InterPro; IPR013019; MAD_homology_MH1.
InterPro; IPR017855; SMAD-like_dom_sf.
InterPro; IPR001132; SMAD_dom_Dwarfin-type.
InterPro; IPR008984; SMAD_FHA_dom_sf.
InterPro; IPR036578; SMAD_MH1_sf.
PANTHER; PTHR13703; PTHR13703; 1.
Pfam; PF03165; MH1; 1.
Pfam; PF03166; MH2; 1.
SMART; SM00523; DWA; 1.
SMART; SM00524; DWB; 1.
SUPFAM; SSF49879; SSF49879; 1.
SUPFAM; SSF56366; SSF56366; 2.
PROSITE; PS51075; MH1; 1.
PROSITE; PS51076; MH2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; DNA-binding; Metal-binding;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Transcription; Transcription regulation; Ubl conjugation; Zinc.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.7}.
CHAIN 2 467 Mothers against decapentaplegic homolog
2.
/FTId=PRO_0000090852.
DOMAIN 10 176 MH1. {ECO:0000255|PROSITE-
ProRule:PRU00438}.
DOMAIN 274 467 MH2. {ECO:0000255|PROSITE-
ProRule:PRU00439}.
MOTIF 221 225 PY-motif.
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:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.7}.
MOD_RES 8 8 Phosphothreonine; by MAPK3.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:12193595}.
MOD_RES 19 19 N6-acetyllysine.
{ECO:0000269|PubMed:17074756}.
MOD_RES 220 220 Phosphothreonine.
{ECO:0000305|PubMed:12193595}.
MOD_RES 240 240 Phosphoserine; by CAMK2.
{ECO:0000255|PROSITE-ProRule:PRU00439,
ECO:0000269|PubMed:11879191}.
MOD_RES 245 245 Phosphoserine.
{ECO:0000305|PubMed:12193595}.
MOD_RES 250 250 Phosphoserine.
{ECO:0000305|PubMed:12193595}.
MOD_RES 255 255 Phosphoserine.
{ECO:0000305|PubMed:12193595}.
MOD_RES 458 458 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 460 460 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 464 464 Phosphoserine. {ECO:0000255|PROSITE-
ProRule:PRU00439,
ECO:0000269|PubMed:8980228}.
MOD_RES 465 465 Phosphoserine; by TGFBR1.
{ECO:0000255|PROSITE-ProRule:PRU00439,
ECO:0000269|PubMed:23478445,
ECO:0000269|PubMed:8980228,
ECO:0000269|PubMed:9136927,
ECO:0000269|PubMed:9346908}.
MOD_RES 467 467 Phosphoserine; by TGFBR1.
{ECO:0000255|PROSITE-ProRule:PRU00439,
ECO:0000269|PubMed:23478445,
ECO:0000269|PubMed:8980228,
ECO:0000269|PubMed:9136927,
ECO:0000269|PubMed:9346908}.
VAR_SEQ 79 108 Missing (in isoform Short).
{ECO:0000305}.
/FTId=VSP_006178.
VARIANT 133 133 R -> C (in a colorectal carcinoma
sample). {ECO:0000269|PubMed:8752209}.
/FTId=VAR_011375.
VARIANT 300 300 D -> V (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036473.
VARIANT 344 358 Missing (in a colorectal carcinoma
sample). {ECO:0000269|PubMed:8673135}.
/FTId=VAR_011376.
VARIANT 440 440 L -> R (in a colorectal carcinoma
sample). {ECO:0000269|PubMed:8752209}.
/FTId=VAR_011377.
VARIANT 445 445 P -> H (in a colorectal carcinoma
sample). {ECO:0000269|PubMed:8752209}.
/FTId=VAR_011378.
VARIANT 450 450 D -> E (in a colorectal carcinoma
sample). {ECO:0000269|PubMed:8752209}.
/FTId=VAR_011379.
MUTAGEN 19 19 K->R: Loss of acetylation.
{ECO:0000269|PubMed:17074756}.
MUTAGEN 20 20 K->R: No effect on acetylation.
{ECO:0000269|PubMed:17074756}.
MUTAGEN 221 225 Missing: Loss of binding to SMURF2.
{ECO:0000269|PubMed:11389444}.
MUTAGEN 368 368 W->A: Loss of interaction with PMEPA1.
{ECO:0000269|PubMed:20129061}.
MUTAGEN 381 381 N->S: Loss of binding to SARA.
{ECO:0000269|PubMed:10615055}.
MUTAGEN 398 398 V->R: Increased binding to PPM1A.
{ECO:0000269|PubMed:16751101}.
MUTAGEN 464 464 S->A: Loss of phosphorylation by TGFBR1;
when associated with A-465 and A-467.
{ECO:0000269|PubMed:8980228}.
MUTAGEN 465 467 SMS->AMA: Binds RANBP3.
{ECO:0000269|PubMed:19289081}.
MUTAGEN 465 467 SMS->DMD: Greatly reduced RANBP2 binding.
{ECO:0000269|PubMed:19289081}.
MUTAGEN 465 465 S->A: No change in binding to PPM1A. Loss
of phosphorylation by TGFBR1; when
associated with A-464 and A-467.
{ECO:0000269|PubMed:16751101,
ECO:0000269|PubMed:8980228}.
MUTAGEN 465 465 S->D: No change in binding to PPM1A.
{ECO:0000269|PubMed:16751101,
ECO:0000269|PubMed:8980228}.
MUTAGEN 467 467 S->A: No change in binding to PPM1A. Loss
of phosphorylation by TGFBR1; when
associated with A-464 and A-465.
{ECO:0000269|PubMed:16751101,
ECO:0000269|PubMed:8980228}.
MUTAGEN 467 467 S->D: No change in binding to PPM1A.
{ECO:0000269|PubMed:16751101,
ECO:0000269|PubMed:8980228}.
STRAND 264 267 {ECO:0000244|PDB:1DEV}.
STRAND 274 281 {ECO:0000244|PDB:1KHX}.
STRAND 290 292 {ECO:0000244|PDB:1KHX}.
STRAND 294 302 {ECO:0000244|PDB:1KHX}.
STRAND 305 307 {ECO:0000244|PDB:1U7V}.
STRAND 310 312 {ECO:0000244|PDB:1KHX}.
HELIX 313 315 {ECO:0000244|PDB:1KHX}.
HELIX 323 329 {ECO:0000244|PDB:1KHX}.
TURN 330 334 {ECO:0000244|PDB:1KHX}.
STRAND 336 341 {ECO:0000244|PDB:1KHX}.
STRAND 344 349 {ECO:0000244|PDB:1KHX}.
STRAND 351 353 {ECO:0000244|PDB:1KHX}.
STRAND 355 358 {ECO:0000244|PDB:1KHX}.
HELIX 360 365 {ECO:0000244|PDB:1KHX}.
STRAND 374 376 {ECO:0000244|PDB:1KHX}.
STRAND 381 386 {ECO:0000244|PDB:1KHX}.
HELIX 387 397 {ECO:0000244|PDB:1KHX}.
HELIX 398 400 {ECO:0000244|PDB:1KHX}.
HELIX 402 406 {ECO:0000244|PDB:1KHX}.
HELIX 407 412 {ECO:0000244|PDB:1KHX}.
STRAND 413 419 {ECO:0000244|PDB:1KHX}.
STRAND 423 427 {ECO:0000244|PDB:1KHX}.
HELIX 431 433 {ECO:0000244|PDB:1KHX}.
STRAND 434 442 {ECO:0000244|PDB:1KHX}.
HELIX 443 453 {ECO:0000244|PDB:1KHX}.
SEQUENCE 467 AA; 52306 MW; 95406DB5FC0AA4C9 CRC64;
MSSILPFTPP VVKRLLGWKK SAGGSGGAGG GEQNGQEEKW CEKAVKSLVK KLKKTGRLDE
LEKAITTQNC NTKCVTIPST CSEIWGLSTP NTIDQWDTTG 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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