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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.
26-FEB-2020, entry version 225.
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]
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.
PDB; 5XOD; X-ray; 1.85 A; A=262-458.
PDB; 5ZOJ; X-ray; 2.79 A; A/B/C=262-458.
PDBsum; 1DEV; -.
PDBsum; 1KHX; -.
PDBsum; 1U7V; -.
PDBsum; 2LB3; -.
PDBsum; 5XOD; -.
PDBsum; 5ZOJ; -.
SMR; Q15796; -.
BioGrid; 110262; 275.
ComplexPortal; CPX-1; SMAD2-SMAD3-SMAD4 complex.
ComplexPortal; CPX-11; SMAD2 homotrimer.
ComplexPortal; CPX-3208; SMAD2-SMAD4 complex.
CORUM; Q15796; -.
DIP; DIP-29716N; -.
IntAct; Q15796; 226.
MINT; Q15796; -.
STRING; 9606.ENSP00000262160; -.
ChEMBL; CHEMBL2396512; -.
DrugBank; DB04522; Dexfosfoserine.
iPTMnet; Q15796; -.
PhosphoSitePlus; Q15796; -.
BioMuta; SMAD2; -.
DMDM; 13633914; -.
EPD; Q15796; -.
jPOST; Q15796; -.
MassIVE; Q15796; -.
PaxDb; Q15796; -.
PeptideAtlas; Q15796; -.
PRIDE; Q15796; -.
ProteomicsDB; 60764; -. [Q15796-1]
ProteomicsDB; 60765; -. [Q15796-2]
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; -.
GeneCards; SMAD2; -.
GeneReviews; SMAD2; -.
HGNC; HGNC:6768; SMAD2.
HPA; CAB025507; -.
HPA; CAB073546; -.
HPA; HPA067203; -.
MIM; 601366; gene.
neXtProt; NX_Q15796; -.
OpenTargets; ENSG00000175387; -.
PharmGKB; PA134959722; -.
eggNOG; KOG3701; Eukaryota.
eggNOG; ENOG410XQKU; LUCA.
GeneTree; ENSGT00940000153499; -.
HOGENOM; CLU_026736_0_2_1; -.
InParanoid; Q15796; -.
KO; K04500; -.
OMA; PNNTEYN; -.
OrthoDB; 608001at2759; -.
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.
Reactome; R-HSA-9615017; FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes.
Reactome; R-HSA-9617828; FOXO-mediated transcription of cell cycle genes.
SignaLink; Q15796; -.
SIGNOR; Q15796; -.
ChiTaRS; SMAD2; human.
EvolutionaryTrace; Q15796; -.
GeneWiki; Mothers_against_decapentaplegic_homolog_2; -.
GenomeRNAi; 4087; -.
Pharos; Q15796; Tbio.
PRO; PR:Q15796; -.
Proteomes; UP000005640; Chromosome 18.
RNAct; Q15796; protein.
Bgee; ENSG00000175387; Expressed in kidney and 232 other tissues.
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:0071144; C:heteromeric SMAD protein complex; IDA:BHF-UCL.
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:0032991; C:protein-containing complex; IMP:CAFA.
GO; GO:0071141; C:SMAD protein complex; IDA:UniProtKB.
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:0035326; F:cis-regulatory region binding; IC:BHF-UCL.
GO; GO:0070410; F:co-SMAD binding; IPI:BHF-UCL.
GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
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:0070412; F:R-SMAD binding; IPI:BHF-UCL.
GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0046332; F:SMAD binding; IPI:UniProtKB.
GO; GO:0048156; F:tau protein binding; ISS:ARUK-UCL.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
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:0030325; P:adrenal gland development; IEA:Ensembl.
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 population proliferation; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; 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: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 by RNA polymerase II; 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:0062009; P:secondary palate development; ISS:BHF-UCL.
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.
DisProt; DP01319; -.
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;
3D-structure; Acetylation; Alternative splicing; Cytoplasm;
Direct protein sequencing; DNA-binding; Metal-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation; Zinc.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378, ECO:0000269|Ref.7"
CHAIN 2..467
/note="Mothers against decapentaplegic homolog 2"
/id="PRO_0000090852"
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"
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:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378, ECO:0000269|Ref.7"
MOD_RES 8
/note="Phosphothreonine; by MAPK3"
/evidence="ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:12193595"
MOD_RES 19
/note="N6-acetyllysine"
/evidence="ECO:0000269|PubMed:17074756"
MOD_RES 220
/note="Phosphothreonine"
/evidence="ECO:0000305|PubMed:12193595"
MOD_RES 240
/note="Phosphoserine; by CAMK2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00439,
ECO:0000269|PubMed:11879191"
MOD_RES 245
/note="Phosphoserine"
/evidence="ECO:0000305|PubMed:12193595"
MOD_RES 250
/note="Phosphoserine"
/evidence="ECO:0000305|PubMed:12193595"
MOD_RES 255
/note="Phosphoserine"
/evidence="ECO:0000305|PubMed:12193595"
MOD_RES 458
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163"
MOD_RES 460
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:20068231"
MOD_RES 464
/note="Phosphoserine"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00439,
ECO:0000269|PubMed:8980228"
MOD_RES 465
/note="Phosphoserine; by TGFBR1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00439,
ECO:0000269|PubMed:23478445, ECO:0000269|PubMed:8980228,
ECO:0000269|PubMed:9136927, ECO:0000269|PubMed:9346908"
MOD_RES 467
/note="Phosphoserine; by TGFBR1"
/evidence="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
/note="Missing (in isoform Short)"
/evidence="ECO:0000305"
/id="VSP_006178"
VARIANT 133
/note="R -> C (in a colorectal carcinoma sample)"
/evidence="ECO:0000269|PubMed:8752209"
/id="VAR_011375"
VARIANT 300
/note="D -> V (in a colorectal cancer sample; somatic
mutation)"
/evidence="ECO:0000269|PubMed:16959974"
/id="VAR_036473"
VARIANT 344..358
/note="Missing (in a colorectal carcinoma sample)"
/evidence="ECO:0000269|PubMed:8673135"
/id="VAR_011376"
VARIANT 440
/note="L -> R (in a colorectal carcinoma sample)"
/evidence="ECO:0000269|PubMed:8752209"
/id="VAR_011377"
VARIANT 445
/note="P -> H (in a colorectal carcinoma sample)"
/evidence="ECO:0000269|PubMed:8752209"
/id="VAR_011378"
VARIANT 450
/note="D -> E (in a colorectal carcinoma sample)"
/evidence="ECO:0000269|PubMed:8752209"
/id="VAR_011379"
MUTAGEN 19
/note="K->R: Loss of acetylation."
/evidence="ECO:0000269|PubMed:17074756"
MUTAGEN 20
/note="K->R: No effect on acetylation."
/evidence="ECO:0000269|PubMed:17074756"
MUTAGEN 221..225
/note="Missing: Loss of binding to SMURF2."
/evidence="ECO:0000269|PubMed:11389444"
MUTAGEN 368
/note="W->A: Loss of interaction with PMEPA1."
/evidence="ECO:0000269|PubMed:20129061"
MUTAGEN 381
/note="N->S: Loss of binding to SARA."
/evidence="ECO:0000269|PubMed:10615055"
MUTAGEN 398
/note="V->R: Increased binding to PPM1A."
/evidence="ECO:0000269|PubMed:16751101"
MUTAGEN 464
/note="S->A: Loss of phosphorylation by TGFBR1; when
associated with A-465 and A-467."
/evidence="ECO:0000269|PubMed:8980228"
MUTAGEN 465..467
/note="SMS->AMA: Binds RANBP3."
/evidence="ECO:0000269|PubMed:19289081"
MUTAGEN 465..467
/note="SMS->DMD: Greatly reduced RANBP2 binding."
/evidence="ECO:0000269|PubMed:19289081"
MUTAGEN 465
/note="S->A: No change in binding to PPM1A. Loss of
phosphorylation by TGFBR1; when associated with A-464 and
A-467."
/evidence="ECO:0000269|PubMed:16751101,
ECO:0000269|PubMed:8980228"
MUTAGEN 465
/note="S->D: No change in binding to PPM1A."
/evidence="ECO:0000269|PubMed:16751101,
ECO:0000269|PubMed:8980228"
MUTAGEN 467
/note="S->A: No change in binding to PPM1A. Loss of
phosphorylation by TGFBR1; when associated with A-464 and
A-465."
/evidence="ECO:0000269|PubMed:16751101,
ECO:0000269|PubMed:8980228"
MUTAGEN 467
/note="S->D: No change in binding to PPM1A."
/evidence="ECO:0000269|PubMed:16751101,
ECO:0000269|PubMed:8980228"
STRAND 264..267
/evidence="ECO:0000244|PDB:1DEV"
STRAND 274..281
/evidence="ECO:0000244|PDB:1KHX"
STRAND 290..292
/evidence="ECO:0000244|PDB:1KHX"
STRAND 294..302
/evidence="ECO:0000244|PDB:1KHX"
STRAND 305..307
/evidence="ECO:0000244|PDB:1U7V"
STRAND 310..312
/evidence="ECO:0000244|PDB:1KHX"
HELIX 313..315
/evidence="ECO:0000244|PDB:1KHX"
HELIX 323..329
/evidence="ECO:0000244|PDB:1KHX"
TURN 330..334
/evidence="ECO:0000244|PDB:1KHX"
STRAND 336..341
/evidence="ECO:0000244|PDB:1KHX"
STRAND 344..349
/evidence="ECO:0000244|PDB:1KHX"
STRAND 351..353
/evidence="ECO:0000244|PDB:1KHX"
STRAND 355..358
/evidence="ECO:0000244|PDB:1KHX"
HELIX 360..365
/evidence="ECO:0000244|PDB:1KHX"
STRAND 374..376
/evidence="ECO:0000244|PDB:1KHX"
STRAND 381..386
/evidence="ECO:0000244|PDB:1KHX"
HELIX 387..397
/evidence="ECO:0000244|PDB:1KHX"
HELIX 398..400
/evidence="ECO:0000244|PDB:1KHX"
HELIX 402..406
/evidence="ECO:0000244|PDB:1KHX"
HELIX 407..412
/evidence="ECO:0000244|PDB:1KHX"
STRAND 413..419
/evidence="ECO:0000244|PDB:1KHX"
STRAND 423..427
/evidence="ECO:0000244|PDB:1KHX"
HELIX 431..433
/evidence="ECO:0000244|PDB:1KHX"
STRAND 434..442
/evidence="ECO:0000244|PDB:1KHX"
HELIX 443..453
/evidence="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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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
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
WP860: 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
WP1096: EGFR1 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)
[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)
[SMAD4 DPC4 MADH4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (Deletion target in pancreatic carcinoma 4) (SMAD family member 4) (SMAD 4) (Smad4) (hSMAD4)
[SMAD1 BSP1 MADH1 MADR1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (JV4-1) (Mad-related protein 1) (SMAD family member 1) (SMAD 1) (Smad1) (hSMAD1) (Transforming growth factor-beta-signaling protein 1) (BSP-1)
[SMAD6 MADH6] Mothers against decapentaplegic homolog 6 (MAD homolog 6) (Mothers against DPP homolog 6) (SMAD family member 6) (SMAD 6) (Smad6) (hSMAD6)
[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)
[Smox Dmel\CG2262 DSMAD2 DSmad2 dSMAD2 dSmad2 dsmad2 l(1)G0348 Sad sad Smad SMAD2 Smad2 smad2 SMOX SmoX smox ted tmp CG2262 Dmel_CG2262] Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member)
[Smad4 Dpc4 Madh4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (Deletion target in pancreatic carcinoma 4 homolog) (SMAD family member 4) (SMAD 4) (Smad4)
[SMAD4 MADH4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (SMAD family member 4) (SMAD 4) (Smad4)
[Smad4 Madh4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (SMAD family member 4) (SMAD 4) (Smad4)
[Smad7 Madh7] Mothers against decapentaplegic homolog 7 (MAD homolog 7) (Mothers against DPP homolog 7) (SMAD family member 7) (SMAD 7) (Smad7)
[Smad1 Mad1 Madh1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (SMAD family member 1) (SMAD 1) (Smad1)
[SMAD1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (SMAD family member 1) (SMAD 1) (Smad1)
[SMAD3 MADH3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (SMAD family member 3) (SMAD 3) (Smad3)
[MAD2L1 MAD2] Mitotic spindle assembly checkpoint protein MAD2A (HsMAD2) (Mitotic arrest deficient 2-like protein 1) (MAD2-like protein 1)
[SMAD4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (SMAD family member 4) (SMAD 4) (Smad4)
[MAD2L2 MAD2B REV7] Mitotic spindle assembly checkpoint protein MAD2B (Mitotic arrest deficient 2-like protein 2) (MAD2-like protein 2) (REV7 homolog) (hREV7)
[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)
[lin-35 C32F10.2] Retinoblastoma-like protein homolog lin-35 (Abnormal cell lineage protein 35) (Synthetic multivulva protein lin-35)
[BUB1B BUBR1 MAD3L SSK1] Mitotic checkpoint serine/threonine-protein kinase BUB1 beta (EC 2.7.11.1) (MAD3/BUB1-related protein kinase) (hBUBR1) (Mitotic checkpoint kinase MAD3L) (Protein SSK1)
[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)
[MAD1L1 MAD1 TXBP181] Mitotic spindle assembly checkpoint protein MAD1 (Mitotic arrest deficient 1-like protein 1) (MAD1-like protein 1) (Mitotic checkpoint MAD1 protein homolog) (HsMAD1) (hMAD1) (Tax-binding protein 181)
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO) (SARS coronavirus main proteinase); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[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)

Bibliography :