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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)

 SMAD4_HUMAN             Reviewed;         552 AA.
Q13485; A8K405;
04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-APR-2020, entry version 227.
RecName: Full=Mothers against decapentaplegic homolog 4;
Short=MAD homolog 4;
Short=Mothers against DPP homolog 4;
AltName: Full=Deletion target in pancreatic carcinoma 4;
AltName: Full=SMAD family member 4;
Short=SMAD 4;
Short=Smad4;
Short=hSMAD4;
Name=SMAD4; Synonyms=DPC4, MADH4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT PANCREATIC CARCINOMA
HIS-493.
TISSUE=Fetal brain;
PubMed=8553070; DOI=10.1126/science.271.5247.350;
Hahn S.A., Schutte M., Shamsul Hoque A.T.M., Moskaluk C.A., da Costa L.T.,
Rozenblum E., Weinstein C.L., Fischer A., Yeo C.J., Hruban R.H., Kern S.E.;
"DPC4, a candidate tumor suppressor gene at human chromosome 18q21.1.";
Science 271:350-353(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [GENOMIC DNA].
PubMed=9098646; DOI=10.1097/00019606-199704000-00003;
Moskaluk C.A., Hruban R.H., Schutte M., Lietman A.S., Smyrk T., Fusaro L.,
Fusaro R., Lynch J., Yeo C.J., Jackson C.E., Lynch H.T., Kern S.E.;
"Genomic sequencing of DPC4 in the analysis of familial pancreatic
carcinoma.";
Diagn. Mol. Pathol. 6:85-90(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle;
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]
FUNCTION.
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).
[8]
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).
[9]
INTERACTION WITH CITED1.
PubMed=9707553; DOI=10.1073/pnas.95.17.9785;
Shioda T., Lechleider R.J., Dunwoodie S.L., Li H., Yahata T.,
de Caestecker M.P., Fenner M.H., Roberts A.B., Isselbacher K.J.;
"Transcriptional activating activity of Smad4: roles of SMAD hetero-
oligomerization and enhancement by an associating transactivator.";
Proc. Natl. Acad. Sci. U.S.A. 95:9785-9790(1998).
[10]
INTERACTION WITH ZNF423.
PubMed=10660046; DOI=10.1016/s0092-8674(00)81561-5;
Hata A., Seoane J., Lagna G., Montalvo E., Hemmati-Brivanlou A.,
Massague J.;
"OAZ uses distinct DNA- and protein-binding zinc fingers in separate BMP-
Smad and Olf signaling pathways.";
Cell 100:229-240(2000).
[11]
CHARACTERIZATION OF SAD DOMAIN.
PubMed=10636916; DOI=10.1074/jbc.275.3.2115;
de Caestecker M.P., Yahata T., Wang D., Parks W.T., Huang S., Hill C.S.,
Shioda T., Roberts A.B., Lechleider R.J.;
"The Smad4 activation domain (SAD) is a proline-rich, p300-dependent
transcriptional activation domain.";
J. Biol. Chem. 275:2115-2122(2000).
[12]
IDENTIFICATION IN A TERNARY COMPLEX COMPOSED OF STK11/LKB1 AND STK11IP, AND
INTERACTION WITH STK11/LKB1 AND STK11IP.
PubMed=11741830; DOI=10.1093/hmg/10.25.2869;
Smith D.P., Rayter S.I., Niederlander C., Spicer J., Jones C.M.,
Ashworth A.;
"LIP1, a cytoplasmic protein functionally linked to the Peutz-Jeghers
syndrome kinase LKB1.";
Hum. Mol. Genet. 10:2869-2877(2001).
[13]
INTERACTION WITH COPS5.
PubMed=11818334; DOI=10.1093/embo-reports/kvf024;
Wan M., Cao X., Wu Y., Bai S., Wu L., Shi X., Wang N., Cao X.;
"Jab1 antagonizes TGF-beta signaling by inducing Smad4 degradation.";
EMBO Rep. 3:171-176(2002).
[14]
INTERACTION WITH ZNF8.
PubMed=12370310; DOI=10.1128/mcb.22.21.7633-7644.2002;
Jiao K., Zhou Y., Hogan B.L.M.;
"Identification of mZnf8, a mouse Kruppel-like transcriptional repressor,
as a novel nuclear interaction partner of Smad1.";
Mol. Cell. Biol. 22:7633-7644(2002).
[15]
INTERACTION WITH VPS39.
PubMed=12941698; DOI=10.1093/emboj/cdg428;
Felici A., Wurthner J.U., Parks W.T., Giam L.R., Reiss M., Karpova T.S.,
McNally J.G., Roberts A.B.;
"TLP, a novel modulator of TGF-beta signaling, has opposite effects on
Smad2- and Smad3-dependent signaling.";
EMBO J. 22:4465-4477(2003).
[16]
INTERACTION WITH DACH1.
PubMed=14525983; DOI=10.1074/jbc.m310021200;
Wu K., Yang Y., Wang C., Davoli M.A., D'Amico M., Li A., Cveklova K.,
Kozmik Z., Lisanti M.P., Russell R.G., Cvekl A., Pestell R.G.;
"DACH1 inhibits transforming growth factor-beta signaling through binding
Smad4.";
J. Biol. Chem. 278:51673-51684(2003).
[17]
INTERACTION WITH DLX1.
PubMed=14671321; DOI=10.1073/pnas.2536757100;
Chiba S., Takeshita K., Imai Y., Kumano K., Kurokawa M., Masuda S.,
Shimizu K., Nakamura S., Ruddle F.H., Hirai H.;
"Homeoprotein DLX-1 interacts with Smad4 and blocks a signaling pathway
from activin A in hematopoietic cells.";
Proc. Natl. Acad. Sci. U.S.A. 100:15577-15582(2003).
[18]
INTERACTION WITH ZNF521.
PubMed=14630787; DOI=10.1182/blood-2003-07-2388;
Bond H.M., Mesuraca M., Carbone E., Bonelli P., Agosti V., Amodio N.,
De Rosa G., Di Nicola M., Gianni A.M., Moore M.A., Hata A., Grieco M.,
Morrone G., Venuta S.;
"Early hematopoietic zinc finger protein (EHZF), the human homolog to mouse
Evi3, is highly expressed in primitive human hematopoietic cells.";
Blood 103:2062-2070(2004).
[19]
INTERACTION WITH TRIM33.
PubMed=15820681; DOI=10.1016/j.cell.2005.01.033;
Dupont S., Zacchigna L., Cordenonsi M., Soligo S., Adorno M., Rugge M.,
Piccolo S.;
"Germ-layer specification and control of cell growth by Ectodermin, a Smad4
ubiquitin ligase.";
Cell 121:87-99(2005).
[20]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=15799969; DOI=10.1074/jbc.m500362200;
Chen H.B., Rud J.G., Lin K., Xu L.;
"Nuclear targeting of transforming growth factor-beta-activated Smad
complexes.";
J. Biol. Chem. 280:21329-21336(2005).
[21]
INTERACTION WITH ZMIZ1.
PubMed=16777850; DOI=10.1074/jbc.m508365200;
Li X., Thyssen G., Beliakoff J., Sun Z.;
"The novel PIAS-like protein hZimp10 enhances Smad transcriptional
activity.";
J. Biol. Chem. 281:23748-23756(2006).
[22]
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).
[23]
FUNCTION, SUBCELLULAR LOCATION, 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).
[24]
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).
[25]
INTERACTION WITH USP9X, UBIQUITINATION, AND MUTAGENESIS OF LYS-519.
PubMed=19135894; DOI=10.1016/j.cell.2008.10.051;
Dupont S., Mamidi A., Cordenonsi M., Montagner M., Zacchigna L., Adorno M.,
Martello G., Stinchfield M.J., Soligo S., Morsut L., Inui M., Moro S.,
Modena N., Argenton F., Newfeld S.J., Piccolo S.;
"FAM/USP9x, a deubiquitinating enzyme essential for TGFbeta signaling,
controls Smad4 monoubiquitination.";
Cell 136:123-135(2009).
[26]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-37; LYS-428 AND LYS-507, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[27]
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).
[28]
POSSIBLE INVOLVEMENT IN PULMONARY HYPERTENSION, AND VARIANT SER-13.
PubMed=21898662; DOI=10.1002/humu.21605;
Nasim M.T., Ogo T., Ahmed M., Randall R., Chowdhury H.M., Snape K.M.,
Bradshaw T.Y., Southgate L., Lee G.J., Jackson I., Lord G.M., Gibbs J.S.,
Wilkins M.R., Ohta-Ogo K., Nakamura K., Girerd B., Coulet F., Soubrier F.,
Humbert M., Morrell N.W., Trembath R.C., Machado R.D.;
"Molecular genetic characterization of SMAD signaling molecules in
pulmonary arterial hypertension.";
Hum. Mutat. 32:1385-1389(2011).
[29]
INTERACTION WITH ZNF451, IDENTIFICATION IN A COMPLEX WITH ZNF451; SMAD3 AND
SMAD2, AND SUBUNIT.
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).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[31]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-113, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[32]
INTERACTION WITH CREB3L1.
PubMed=25310401; DOI=10.1371/journal.pone.0108528;
Chen Q., Lee C.E., Denard B., Ye J.;
"Sustained induction of collagen synthesis by TGF-beta requires regulated
intramembrane proteolysis of CREB3L1.";
PLoS ONE 9:E108528-E108528(2014).
[33]
FUNCTION, INTERACTION WITH CREBBP; EP300; HDAC1 AND ZBTB7A, AND REGION.
PubMed=25514493; DOI=10.1016/j.bbagrm.2014.12.008;
Yang Y., Cui J., Xue F., Zhang C., Mei Z., Wang Y., Bi M., Shan D.,
Meredith A., Li H., Xu Z.Q.;
"Pokemon (FBI-1) interacts with Smad4 to repress TGF-beta-induced
transcriptional responses.";
Biochim. Biophys. Acta 1849:270-281(2015).
[34]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-113, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.o114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to replication
stress reveals novel small ubiquitin-like modified target proteins and
acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[35]
INTERACTION WITH NUP93 AND IPO7.
PubMed=26878725; DOI=10.1038/ng.3512;
Braun D.A., Sadowski C.E., Kohl S., Lovric S., Astrinidis S.A., Pabst W.L.,
Gee H.Y., Ashraf S., Lawson J.A., Shril S., Airik M., Tan W., Schapiro D.,
Rao J., Choi W.I., Hermle T., Kemper M.J., Pohl M., Ozaltin F., Konrad M.,
Bogdanovic R., Buescher R., Helmchen U., Serdaroglu E., Lifton R.P.,
Antonin W., Hildebrandt F.;
"Mutations in nuclear pore genes NUP93, NUP205 and XPO5 cause steroid-
resistant nephrotic syndrome.";
Nat. Genet. 48:457-465(2016).
[36]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-113, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-modification
with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[37]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 319-543.
PubMed=9214508; DOI=10.1038/40431;
Shi Y., Hata A., Lo R.S., Massague J., Pavletich N.P.;
"A structural basis for mutational inactivation of the tumour suppressor
Smad4.";
Nature 388:87-93(1997).
[38]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 285-552.
PubMed=10647180; DOI=10.1016/s0969-2126(00)88340-9;
Qin B., Lam S.S., Lin K.;
"Crystal structure of a transcriptionally active Smad4 fragment.";
Structure 7:1493-1503(1999).
[39]
X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS) OF 273-552 OF WILD TYPE AND MUTANTS
ARG-416; ARG-502 AND ARG-515 IN COMPLEX WITH SMAD3, SUBUNIT, AND
MUTAGENESIS OF ARG-416; ARG-502 AND ARG-515.
PubMed=11224571; DOI=10.1038/84995;
Chacko B.M., Qin B., Correia J.J., Lam S.S., de Caestecker M.P., Lin K.;
"The L3 loop and C-terminal phosphorylation jointly define Smad protein
trimerization.";
Nat. Struct. Biol. 8:248-253(2001).
[40]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 314-552 IN COMPLEX WITH SMAD2 OR
SMAD3, 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).
[41]
VARIANT JPS CYS-361.
PubMed=9811934; DOI=10.1093/hmg/7.12.1907;
Houlston R., Bevan S., Williams A., Young J., Dunlop M., Rozen P., Eng C.,
Markie D., Woodford-Richens K., Rodriguez-Bigas M.A., Leggett B., Neale K.,
Phillips R., Sheridan E., Hodgson S., Iwama T., Eccles D., Bodmer W.,
Tomlinson I.;
"Mutations in DPC4 (SMAD4) cause juvenile polyposis syndrome, but only
account for a minority of cases.";
Hum. Mol. Genet. 7:1907-1912(1998).
[42]
VARIANTS JPS GLY-330 AND ARG-352.
PubMed=12417513; DOI=10.1007/bf02557528;
Sayed M.G., Ahmed A.F., Ringold J.R., Anderson M.E., Bair J.L.,
Mitros F.A., Lynch H.T., Tinley S.T., Petersen G.M., Giardiello F.M.,
Vogelstein B., Howe J.R.;
"Germline SMAD4 or BMPR1A mutations and phenotype of juvenile polyposis.";
Ann. Surg. Oncol. 9:901-906(2002).
[43]
VARIANTS JP/HHT ARG-352 AND ASP-386.
PubMed=15031030; DOI=10.1016/s0140-6736(04)15732-2;
Gallione C.J., Repetto G.M., Legius E., Rustgi A.K., Schelley S.L.,
Tejpar S., Mitchell G., Drouin E., Westermann C.J.J., Marchuk D.A.;
"A combined syndrome of juvenile polyposis and hereditary haemorrhagic
telangiectasia associated with mutations in MADH4 (SMAD4).";
Lancet 363:852-859(2004).
[44]
VARIANTS [LARGE SCALE ANALYSIS] SER-130; ASN-351 AND HIS-361, AND
INVOLVEMENT IN COLORECTAL CANCER.
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).
[45]
VARIANTS MYHRS THR-500 AND VAL-500.
PubMed=22243968; DOI=10.1016/j.ajhg.2011.12.011;
Caputo V., Cianetti L., Niceta M., Carta C., Ciolfi A., Bocchinfuso G.,
Carrani E., Dentici M.L., Biamino E., Belligni E., Garavelli L.,
Boccone L., Melis D., Andria G., Gelb B.D., Stella L., Silengo M.,
Dallapiccola B., Tartaglia M.;
"A restricted spectrum of mutations in the SMAD4 tumor-suppressor gene
underlies Myhre syndrome.";
Am. J. Hum. Genet. 90:161-169(2012).
[46]
VARIANTS MYHRS MET-500; THR-500 AND VAL-500, AND CHARACTERIZATION OF
VARIANT MYHRS THR-500.
PubMed=22158539; DOI=10.1038/ng.1016;
Le Goff C., Mahaut C., Abhyankar A., Le Goff W., Serre V., Afenjar A.,
Destree A., di Rocco M., Heron D., Jacquemont S., Marlin S., Simon M.,
Tolmie J., Verloes A., Casanova J.L., Munnich A., Cormier-Daire V.;
"Mutations at a single codon in Mad homology 2 domain of SMAD4 cause Myhre
syndrome.";
Nat. Genet. 44:85-88(2012).
-!- FUNCTION: In muscle physiology, plays a central role in the balance
between atrophy and hypertrophy. When recruited by MSTN, promotes
atrophy response via phosphorylated SMAD2/4. MSTN decrease causes SMAD4
release and subsequent recruitment by the BMP pathway to promote
hypertrophy via phosphorylated SMAD1/5/8. Acts synergistically with
SMAD1 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-
specific gene expression. Binds to SMAD binding elements (SBEs) (5'-
GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating
regions (By similarity). Common SMAD (co-SMAD) is the coactivator and
mediator of signal transduction by TGF-beta (transforming growth
factor). Component of the heterotrimeric SMAD2/SMAD3-SMAD4 complex that
forms in the nucleus and is required for the TGF-mediated signaling
(PubMed:25514493). Promotes binding of the SMAD2/SMAD4/FAST-1 complex
to DNA and provides an activation function required for SMAD1 or SMAD2
to stimulate transcription. Component of the multimeric
SMAD3/SMAD4/JUN/FOS complex which forms at the AP1 promoter site;
required for synergistic transcriptional activity in response to TGF-
beta. May act as a tumor suppressor. Positively regulates PDPK1 kinase
activity by stimulating its dissociation from the 14-3-3 protein YWHAQ
which acts as a negative regulator. {ECO:0000250,
ECO:0000269|PubMed:17327236, ECO:0000269|PubMed:25514493,
ECO:0000269|PubMed:9389648}.
-!- SUBUNIT: Found in a complex with SMAD1 and YY1 (By similarity).
Interacts with CITED2 (By similarity). Monomer; in the absence of TGF-
beta activation. Heterodimer; on TGF-beta activation. Composed of two
molecules of a C-terminally phosphorylated R-SMAD molecule, SMAD2 or
SMAD3, and one molecule of SMAD4 to form the transcriptional active
SMAD2/SMAD3-SMAD4 complex. Found in a ternary complex composed of
SMAD4, STK11/LKB1 and STK11IP. Interacts with ATF2, COPS5, DACH1, MSG1,
SKI, STK11/LKB1, STK11IP and TRIM33. Interacts with ZNF423; the
interaction takes place in response to BMP2 leading to activation of
transcription of BMP target genes. Interacts with ZNF521; the
interaction takes place in response to BMP2 leading to activation of
transcription of BMP target genes. Interacts with USP9X. Interacts (via
the MH1 and MH2 domains) with RBPMS. Interacts with WWTR1 (via coiled-
coil domain). Component of the multimeric complex SMAD3/SMAD4/JUN/FOS
which forms at the AP1 promoter site; required for synergistic
transcriptional activity in response to TGF-beta. Interacts with
CITED1. Interacts with PDPK1 (via PH domain) (By similarity). Interacts
with VPS39; this interaction affects heterodimer formation with SMAD3,
but not with SMAD2, and leads to inhibition of SMAD3-dependent
transcription activation. Interactions with VPS39 and SMAD2 may be
mutually exclusive. Interacts with ZC3H3 (By similarity). Interacts
(via MH2 domain) with ZNF451 (via N-terminal zinc-finger domains)
(PubMed:24324267). Identified in a complex that contains at least
ZNF451, SMAD2, SMAD3 and SMAD4 (PubMed:24324267). Interacts weakly with
ZNF8 (PubMed:12370310). Interacts with NUP93 and IPO7; translocates
SMAD4 to the nucleus through the NPC upon BMP7 stimulation resulting in
activation of SMAD4 signaling (PubMed:26878725). Interacts with
CREB3L1, the interaction takes place upon TGFB1 induction and SMAD4
acts as CREB3L1 coactivator to induce the expression of genes involved
in the assembly of collagen extracellular matrix (PubMed:25310401).
Interacts with DLX1 (PubMed:14671321). Interacts with ZBTB7A; the
interaction is direct and stimulated by TGFB1 (PubMed:25514493).
Interacts with CREBBP; the recruitment of this transcriptional
coactivator is negatively regulated by ZBTB7A (PubMed:25514493).
Interacts with EP300; the interaction with this transcriptional
coactivator is negatively regulated by ZBTB7A (PubMed:25514493).
Interacts with HDAC1 (PubMed:25514493). Interacts (via MH2 domain) with
ZMIZ1 (via SP-RING-type domain); in the TGF-beta signaling pathway
increases the activity of the SMAD3/SMAD4 transcriptional complex
(PubMed:16777850). {ECO:0000250|UniProtKB:O70437,
ECO:0000250|UniProtKB:P97471, ECO:0000269|PubMed:10660046,
ECO:0000269|PubMed:11224571, ECO:0000269|PubMed:11741830,
ECO:0000269|PubMed:11818334, ECO:0000269|PubMed:12370310,
ECO:0000269|PubMed:12941698, ECO:0000269|PubMed:14525983,
ECO:0000269|PubMed:14630787, ECO:0000269|PubMed:14671321,
ECO:0000269|PubMed:15350224, ECO:0000269|PubMed:15799969,
ECO:0000269|PubMed:15820681, ECO:0000269|PubMed:16777850,
ECO:0000269|PubMed:17099224, ECO:0000269|PubMed:17327236,
ECO:0000269|PubMed:18568018, ECO:0000269|PubMed:19135894,
ECO:0000269|PubMed:24324267, ECO:0000269|PubMed:25310401,
ECO:0000269|PubMed:25514493, ECO:0000269|PubMed:26878725,
ECO:0000269|PubMed:9670020, ECO:0000269|PubMed:9707553}.
-!- INTERACTION:
Q13485; Q13485; NbExp=3; IntAct=EBI-347263, EBI-347263;
Q13485; P31749: AKT1; NbExp=2; IntAct=EBI-347263, EBI-296087;
Q13485; Q9Y297: BTRC; NbExp=2; IntAct=EBI-347263, EBI-307461;
Q13485; Q9UI36: DACH1; NbExp=3; IntAct=EBI-347263, EBI-347111;
Q13485; Q9NPI6: DCP1A; NbExp=5; IntAct=EBI-347263, EBI-374238;
Q13485; Q92988: DLX4; NbExp=5; IntAct=EBI-347263, EBI-1752755;
Q13485; P43268-3: ETV4; NbExp=3; IntAct=EBI-347263, EBI-12130722;
Q13485; Q01844: EWSR1; NbExp=3; IntAct=EBI-347263, EBI-739737;
Q13485; P70056: foxh1; Xeno; NbExp=2; IntAct=EBI-347263, EBI-9969973;
Q13485; O43524: FOXO3; NbExp=9; IntAct=EBI-347263, EBI-1644164;
Q13485; P98177: FOXO4; NbExp=2; IntAct=EBI-347263, EBI-4481939;
Q13485; P23769: GATA2; NbExp=2; IntAct=EBI-347263, EBI-2806671;
Q13485; P61968: LMO4; NbExp=8; IntAct=EBI-347263, EBI-2798728;
Q13485; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-347263, EBI-10271199;
Q13485; Q9UBE8: NLK; NbExp=6; IntAct=EBI-347263, EBI-366978;
Q13485; P24468: NR2F2; NbExp=4; IntAct=EBI-347263, EBI-2795198;
Q13485; Q8WWW0: RASSF5; NbExp=5; IntAct=EBI-347263, EBI-367390;
Q13485; P12755: SKI; NbExp=13; IntAct=EBI-347263, EBI-347281;
Q13485; P12757: SKIL; NbExp=3; IntAct=EBI-347263, EBI-2902468;
Q13485; Q15797: SMAD1; NbExp=12; IntAct=EBI-347263, EBI-1567153;
Q13485; Q15796: SMAD2; NbExp=20; IntAct=EBI-347263, EBI-1040141;
Q13485; P84022: SMAD3; NbExp=33; IntAct=EBI-347263, EBI-347161;
Q13485; O15198: SMAD9; NbExp=4; IntAct=EBI-347263, EBI-748763;
Q13485; O15198-2: SMAD9; NbExp=3; IntAct=EBI-347263, EBI-12273450;
Q13485; P08047: SP1; NbExp=2; IntAct=EBI-347263, EBI-298336;
Q13485; Q08117-2: TLE5; NbExp=3; IntAct=EBI-347263, EBI-11741437;
Q13485; Q9UPN9: TRIM33; NbExp=6; IntAct=EBI-347263, EBI-2214398;
Q13485; P63279: UBE2I; NbExp=6; IntAct=EBI-347263, EBI-80168;
Q13485; Q93008: USP9X; NbExp=2; IntAct=EBI-347263, EBI-302524;
Q13485; P70398: Usp9x; Xeno; NbExp=4; IntAct=EBI-347263, EBI-2214043;
Q13485; Q15915: ZIC1; NbExp=3; IntAct=EBI-347263, EBI-11963196;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15799969,
ECO:0000269|PubMed:17327236}. Nucleus {ECO:0000269|PubMed:15799969}.
Note=Cytoplasmic in the absence of ligand. Migrates to the nucleus when
complexed with R-SMAD (PubMed:15799969). PDPK1 prevents its nuclear
translocation in response to TGF-beta (PubMed:17327236).
{ECO:0000269|PubMed:15799969, ECO:0000269|PubMed:17327236}.
-!- DOMAIN: The MH1 domain is required for DNA binding.
-!- DOMAIN: The MH2 domain is required for both homomeric and heteromeric
interactions and for transcriptional regulation. Sufficient for nuclear
import.
-!- PTM: Phosphorylated by PDPK1. {ECO:0000269|PubMed:17327236}.
-!- PTM: Monoubiquitinated on Lys-519 by E3 ubiquitin-protein ligase
TRIM33. Monoubiquitination hampers its ability to form a stable complex
with activated SMAD2/3 resulting in inhibition of TGF-beta/BMP
signaling cascade. Deubiquitination by USP9X restores its competence to
mediate TGF-beta signaling. {ECO:0000269|PubMed:19135894}.
-!- DISEASE: Pancreatic cancer (PNCA) [MIM:260350]: A malignant neoplasm of
the pancreas. Tumors can arise from both the exocrine and endocrine
portions of the pancreas, but 95% of them develop from the exocrine
portion, including the ductal epithelium, acinar cells, connective
tissue, and lymphatic tissue. {ECO:0000269|PubMed:8553070}. Note=The
gene represented in this entry may be involved in disease pathogenesis.
-!- DISEASE: Juvenile polyposis syndrome (JPS) [MIM:174900]: Autosomal
dominant gastrointestinal hamartomatous polyposis syndrome in which
patients are at risk for developing gastrointestinal cancers. The
lesions are typified by a smooth histological appearance, predominant
stroma, cystic spaces and lack of a smooth muscle core. Multiple
juvenile polyps usually occur in a number of Mendelian disorders.
Sometimes, these polyps occur without associated features as in JPS;
here, polyps tend to occur in the large bowel and are associated with
an increased risk of colon and other gastrointestinal cancers.
{ECO:0000269|PubMed:12417513, ECO:0000269|PubMed:9811934}. Note=The
disease is caused by mutations affecting the gene represented in this
entry.
-!- DISEASE: Juvenile polyposis/hereditary hemorrhagic telangiectasia
syndrome (JP/HHT) [MIM:175050]: JP/HHT syndrome phenotype consists of
the coexistence of juvenile polyposis (JIP) and hereditary hemorrhagic
telangiectasia (HHT) [MIM:187300] in a single individual. JIP and HHT
are autosomal dominant disorders with distinct and non-overlapping
clinical features. The former, an inherited gastrointestinal malignancy
predisposition, is caused by mutations in SMAD4 or BMPR1A, and the
latter is a vascular malformation disorder caused by mutations in ENG
or ACVRL1. All four genes encode proteins involved in the transforming-
growth-factor-signaling pathway. Although there are reports of patients
and families with phenotypes of both disorders combined, the genetic
etiology of this association is unknown. {ECO:0000269|PubMed:15031030}.
Note=The disease is caused by mutations affecting the gene represented
in this entry.
-!- DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease
characterized by malignant lesions arising from the inner wall of the
large intestine (the colon) and the rectum. Genetic alterations are
often associated with progression from premalignant lesion (adenoma) to
invasive adenocarcinoma. Risk factors for cancer of the colon and
rectum include colon polyps, long-standing ulcerative colitis, and
genetic family history. {ECO:0000269|PubMed:16959974}. Note=The disease
may be caused by mutations affecting the gene represented in this
entry.
-!- DISEASE: Note=SMAD4 variants may be associated with susceptibility to
pulmonary hypertension, a disorder characterized by plexiform lesions
of proliferating endothelial cells in pulmonary arterioles. The lesions
lead to elevated pulmonary arterial pression, right ventricular
failure, and death. The disease can occur from infancy throughout life
and it has a mean age at onset of 36 years. Penetrance is reduced.
Although familial pulmonary hypertension is rare, cases secondary to
known etiologies are more common and include those associated with the
appetite-suppressant drugs. {ECO:0000269|PubMed:21898662}.
-!- DISEASE: Myhre syndrome (MYHRS) [MIM:139210]: A syndrome characterized
by pre- and postnatal growth deficiency, mental retardation,
generalized muscle hypertrophy and striking muscular build, decreased
joint mobility, cryptorchidism, and unusual facies. Dysmorphic facial
features include microcephaly, midface hypoplasia, prognathism, and
blepharophimosis. Typical skeletal anomalies are short stature, square
body shape, broad ribs, iliac hypoplasia, brachydactyly, flattened
vertebrae, and thickened calvaria. Other features, such as congenital
heart disease, may also occur. {ECO:0000269|PubMed:22158539,
ECO:0000269|PubMed:22243968}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- 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/SMAD4ID371.html";
-!- WEB RESOURCE: Name=Mendelian genes SMAD family member 4 (SMAD4);
Note=Leiden Open Variation Database (LOVD);
URL="http://www.lovd.nl/SMAD4";
---------------------------------------------------------------------------
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EMBL; AF045447; AAC03051.1; -; Genomic_DNA.
EMBL; AF045438; AAC03051.1; JOINED; Genomic_DNA.
EMBL; AF045439; AAC03051.1; JOINED; Genomic_DNA.
EMBL; AF045440; AAC03051.1; JOINED; Genomic_DNA.
EMBL; AF045441; AAC03051.1; JOINED; Genomic_DNA.
EMBL; AF045442; AAC03051.1; JOINED; Genomic_DNA.
EMBL; AF045443; AAC03051.1; JOINED; Genomic_DNA.
EMBL; AF045444; AAC03051.1; JOINED; Genomic_DNA.
EMBL; AF045445; AAC03051.1; JOINED; Genomic_DNA.
EMBL; AF045446; AAC03051.1; JOINED; Genomic_DNA.
EMBL; U44378; AAA91041.1; -; mRNA.
EMBL; AK290770; BAF83459.1; -; mRNA.
EMBL; CH471096; EAW62985.1; -; Genomic_DNA.
EMBL; BC002379; AAH02379.1; -; mRNA.
CCDS; CCDS11950.1; -.
PIR; S71811; S71811.
RefSeq; NP_005350.1; NM_005359.5.
PDB; 1DD1; X-ray; 2.62 A; A/B/C=285-552.
PDB; 1G88; X-ray; 3.00 A; A/B/C=285-552.
PDB; 1MR1; X-ray; 2.85 A; A/B=319-552.
PDB; 1U7F; X-ray; 2.60 A; B=314-552.
PDB; 1U7V; X-ray; 2.70 A; B=314-549.
PDB; 1YGS; X-ray; 2.10 A; A=319-552.
PDB; 5C4V; X-ray; 2.60 A; A/C/E=314-549.
PDB; 5MEY; X-ray; 2.05 A; A=10-140.
PDB; 5MEZ; X-ray; 2.98 A; A/B=10-140.
PDB; 5MF0; X-ray; 3.03 A; A/B=10-140.
PDB; 5UWU; X-ray; 2.24 A; D=133-149.
PDBsum; 1DD1; -.
PDBsum; 1G88; -.
PDBsum; 1MR1; -.
PDBsum; 1U7F; -.
PDBsum; 1U7V; -.
PDBsum; 1YGS; -.
PDBsum; 5C4V; -.
PDBsum; 5MEY; -.
PDBsum; 5MEZ; -.
PDBsum; 5MF0; -.
PDBsum; 5UWU; -.
SMR; Q13485; -.
BioGrid; 110264; 231.
ComplexPortal; CPX-1; SMAD2-SMAD3-SMAD4 complex.
ComplexPortal; CPX-3208; SMAD2-SMAD4 complex.
ComplexPortal; CPX-3252; SMAD3-SMAD4 complex.
ComplexPortal; CPX-54; SMAD1-SMAD4 complex.
CORUM; Q13485; -.
DIP; DIP-31512N; -.
IntAct; Q13485; 125.
MINT; Q13485; -.
STRING; 9606.ENSP00000341551; -.
iPTMnet; Q13485; -.
MetOSite; Q13485; -.
PhosphoSitePlus; Q13485; -.
SwissPalm; Q13485; -.
BioMuta; SMAD4; -.
DMDM; 13959561; -.
CPTAC; CPTAC-1268; -.
CPTAC; CPTAC-1269; -.
EPD; Q13485; -.
jPOST; Q13485; -.
MassIVE; Q13485; -.
MaxQB; Q13485; -.
PaxDb; Q13485; -.
PeptideAtlas; Q13485; -.
PRIDE; Q13485; -.
ProteomicsDB; 59479; -.
Antibodypedia; 3711; 1002 antibodies.
DNASU; 4089; -.
Ensembl; ENST00000342988; ENSP00000341551; ENSG00000141646.
Ensembl; ENST00000398417; ENSP00000381452; ENSG00000141646.
GeneID; 4089; -.
KEGG; hsa:4089; -.
UCSC; uc010xdp.3; human.
CTD; 4089; -.
DisGeNET; 4089; -.
GeneCards; SMAD4; -.
GeneReviews; SMAD4; -.
HGNC; HGNC:6770; SMAD4.
HPA; ENSG00000141646; Low tissue specificity.
MalaCards; SMAD4; -.
MIM; 114500; phenotype.
MIM; 139210; phenotype.
MIM; 174900; phenotype.
MIM; 175050; phenotype.
MIM; 260350; phenotype.
MIM; 600993; gene.
neXtProt; NX_Q13485; -.
OpenTargets; ENSG00000141646; -.
Orphanet; 1333; Familial pancreatic carcinoma.
Orphanet; 91387; Familial thoracic aortic aneurysm and aortic dissection.
Orphanet; 329971; Generalized juvenile polyposis/juvenile polyposis coli.
Orphanet; 774; Hereditary hemorrhagic telangiectasia.
Orphanet; 2588; Myhre syndrome.
PharmGKB; PA30527; -.
eggNOG; KOG3701; Eukaryota.
eggNOG; ENOG410XQKU; LUCA.
GeneTree; ENSGT00940000157435; -.
InParanoid; Q13485; -.
KO; K04501; -.
OMA; PQMGPGT; -.
OrthoDB; 905048at2759; -.
PhylomeDB; Q13485; -.
TreeFam; TF314923; -.
Reactome; R-HSA-1181150; Signaling by NODAL.
Reactome; R-HSA-1502540; Signaling by Activin.
Reactome; R-HSA-201451; Signaling by BMP.
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-3311021; SMAD4 MH2 Domain Mutants in Cancer.
Reactome; R-HSA-3315487; SMAD2/3 MH2 Domain Mutants in Cancer.
Reactome; R-HSA-452723; Transcriptional regulation of pluripotent stem cells.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-8941326; RUNX2 regulates bone development.
Reactome; R-HSA-8941855; RUNX3 regulates CDKN1A transcription.
Reactome; R-HSA-8952158; RUNX3 regulates BCL2L11 (BIM) transcription.
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; Q13485; -.
SIGNOR; Q13485; -.
ChiTaRS; SMAD4; human.
EvolutionaryTrace; Q13485; -.
GeneWiki; Mothers_against_decapentaplegic_homolog_4; -.
GenomeRNAi; 4089; -.
Pharos; Q13485; Tbio.
PRO; PR:Q13485; -.
Proteomes; UP000005640; Chromosome 18.
RNAct; Q13485; protein.
Bgee; ENSG00000141646; Expressed in kidney and 223 other tissues.
ExpressionAtlas; Q13485; baseline and differential.
Genevisible; Q13485; HS.
GO; GO:0032444; C:activin responsive factor complex; IDA:BHF-UCL.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0005813; C:centrosome; IDA:HPA.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0071141; C:SMAD protein complex; IDA:UniProtKB.
GO; GO:0005667; C:transcription factor complex; IDA:BHF-UCL.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0005518; F:collagen binding; IEA:Ensembl.
GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
GO; GO:0070411; F:I-SMAD binding; IPI:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0098772; F:molecular function regulator; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; 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:0001085; F:RNA polymerase II transcription factor binding; IEA:Ensembl.
GO; GO:0043199; F:sulfate binding; IMP:CAFA.
GO; GO:0001223; F:transcription coactivator binding; IPI:UniProtKB.
GO; GO:0003712; F:transcription coregulator activity; IDA:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
GO; GO:0030616; F:transforming growth factor beta receptor, common-partner cytoplasmic mediator activity; IDA:BHF-UCL.
GO; GO:0036302; P:atrioventricular canal development; ISS:BHF-UCL.
GO; GO:0003190; P:atrioventricular valve formation; ISS:BHF-UCL.
GO; GO:0007411; P:axon guidance; IEA:Ensembl.
GO; GO:0030509; P:BMP signaling pathway; IDA:BHF-UCL.
GO; GO:0003360; P:brainstem development; IEA:Ensembl.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl.
GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
GO; GO:0006879; P:cellular iron ion homeostasis; ISS:BHF-UCL.
GO; GO:0071773; P:cellular response to BMP stimulus; NAS:BHF-UCL.
GO; GO:0048589; P:developmental growth; IEA:Ensembl.
GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
GO; GO:0060956; P:endocardial cell differentiation; ISS:BHF-UCL.
GO; GO:0042118; P:endothelial cell activation; IEA:Ensembl.
GO; GO:0003198; P:epithelial to mesenchymal transition involved in endocardial cushion formation; IEA:Ensembl.
GO; GO:0061040; P:female gonad morphogenesis; IEA:Ensembl.
GO; GO:0048859; P:formation of anatomical boundary; IEA:Ensembl.
GO; GO:0001702; P:gastrulation with mouth forming second; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0070102; P:interleukin-6-mediated signaling pathway; ISS:BHF-UCL.
GO; GO:0035556; P:intracellular signal transduction; IMP:CACAO.
GO; GO:0003220; P:left ventricular cardiac muscle tissue morphogenesis; ISS:BHF-UCL.
GO; GO:0048382; P:mesendoderm development; IEA:Ensembl.
GO; GO:0072133; P:metanephric mesenchyme morphogenesis; IEA:Ensembl.
GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; ISS:BHF-UCL.
GO; GO:1905305; P:negative regulation of cardiac myofibril assembly; ISS:BHF-UCL.
GO; GO:0060548; P:negative regulation of cell death; IEA:Ensembl.
GO; GO:0030308; P:negative regulation of cell growth; IDA:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISS:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0072134; P:nephrogenic mesenchyme morphogenesis; IEA:Ensembl.
GO; GO:0014033; P:neural crest cell differentiation; IEA:Ensembl.
GO; GO:0048663; P:neuron fate commitment; IEA:Ensembl.
GO; GO:0003148; P:outflow tract septum morphogenesis; ISS:BHF-UCL.
GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
GO; GO:0030513; P:positive regulation of BMP signaling pathway; IMP:BHF-UCL.
GO; GO:0003251; P:positive regulation of cell proliferation involved in heart valve morphogenesis; ISS:BHF-UCL.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISS:BHF-UCL.
GO; GO:0046881; P:positive regulation of follicle-stimulating hormone secretion; IEA:Ensembl.
GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; ISS:BHF-UCL.
GO; GO:2000617; P:positive regulation of histone H3-K9 acetylation; ISS:BHF-UCL.
GO; GO:0033686; P:positive regulation of luteinizing hormone secretion; IEA:Ensembl.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISS:BHF-UCL.
GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; ISS:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:1901522; P:positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus; TAS:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0061614; P:pri-miRNA transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0051098; P:regulation of binding; IEA:Ensembl.
GO; GO:0051797; P:regulation of hair follicle development; IEA:Ensembl.
GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0032909; P:regulation of transforming growth factor beta2 production; IMP:BHF-UCL.
GO; GO:0001666; P:response to hypoxia; IMP:BHF-UCL.
GO; GO:0071559; P:response to transforming growth factor beta; IDA:UniProtKB.
GO; GO:0048733; P:sebaceous gland development; IEA:Ensembl.
GO; GO:0062009; P:secondary palate development; ISS:BHF-UCL.
GO; GO:0072520; P:seminiferous tubule development; IEA:Ensembl.
GO; GO:0007338; P:single fertilization; IEA:Ensembl.
GO; GO:0007183; P:SMAD protein complex assembly; IDA:BHF-UCL.
GO; GO:0060395; P:SMAD protein signal transduction; IDA:BHF-UCL.
GO; GO:0035019; P:somatic stem cell population maintenance; TAS:Reactome.
GO; GO:0032525; P:somite rostral/caudal axis specification; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0060065; P:uterus development; IEA:Ensembl.
GO; GO:0060412; P:ventricular septum morphogenesis; ISS:BHF-UCL.
DisProt; DP00464; -.
Gene3D; 2.60.200.10; -; 1.
Gene3D; 3.90.520.10; -; 1.
InterPro; IPR013790; Dwarfin.
InterPro; IPR003619; MAD_homology1_Dwarfin-type.
InterPro; IPR013019; MAD_homology_MH1.
InterPro; IPR017855; SMAD-like_dom_sf.
InterPro; IPR001132; SMAD_dom_Dwarfin-type.
InterPro; IPR008984; SMAD_FHA_dom_sf.
InterPro; IPR036578; SMAD_MH1_sf.
PANTHER; PTHR13703; PTHR13703; 1.
Pfam; PF03165; MH1; 1.
Pfam; PF03166; MH2; 1.
SMART; SM00523; DWA; 1.
SMART; SM00524; DWB; 1.
SUPFAM; SSF49879; SSF49879; 1.
SUPFAM; SSF56366; SSF56366; 1.
PROSITE; PS51075; MH1; 1.
PROSITE; PS51076; MH2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cytoplasm; Disease mutation; DNA-binding;
Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation; Zinc.
CHAIN 1..552
/note="Mothers against decapentaplegic homolog 4"
/id="PRO_0000090861"
DOMAIN 18..142
/note="MH1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00438"
DOMAIN 323..552
/note="MH2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00439"
REGION 1..322
/note="Mediates interaction with ZBTB7A"
/evidence="ECO:0000269|PubMed:25514493"
REGION 275..320
/note="SAD"
COMPBIAS 451..466
/note="Poly-Ala"
METAL 71
/note="Zinc"
/evidence="ECO:0000250"
METAL 115
/note="Zinc"
/evidence="ECO:0000250"
METAL 127
/note="Zinc"
/evidence="ECO:0000250"
METAL 132
/note="Zinc"
/evidence="ECO:0000250"
SITE 515
/note="Necessary for heterotrimerization"
MOD_RES 37
/note="N6-acetyllysine"
/evidence="ECO:0000244|PubMed:19608861"
MOD_RES 428
/note="N6-acetyllysine"
/evidence="ECO:0000244|PubMed:19608861"
MOD_RES 507
/note="N6-acetyllysine"
/evidence="ECO:0000244|PubMed:19608861"
CROSSLNK 113
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297, ECO:0000244|PubMed:28112733"
CROSSLNK 519
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000269|PubMed:19135894"
VARIANT 13
/note="N -> S (rare variant; found in a patient with
pulmonary hypertension; unknown pathological significance;
dbSNP:rs281875323)"
/evidence="ECO:0000269|PubMed:21898662"
/id="VAR_066870"
VARIANT 130
/note="P -> S (in a colorectal cancer sample; somatic
mutation; dbSNP:rs1555685186)"
/evidence="ECO:0000269|PubMed:16959974"
/id="VAR_036475"
VARIANT 330
/note="E -> G (in JPS; dbSNP:rs281875324)"
/evidence="ECO:0000269|PubMed:12417513"
/id="VAR_022833"
VARIANT 351
/note="D -> N (in a colorectal cancer sample; somatic
mutation; dbSNP:rs1057519739)"
/evidence="ECO:0000269|PubMed:16959974"
/id="VAR_036476"
VARIANT 352
/note="G -> R (in JP/HHT and JPS; dbSNP:rs121912581)"
/evidence="ECO:0000269|PubMed:12417513,
ECO:0000269|PubMed:15031030"
/id="VAR_019571"
VARIANT 361
/note="R -> C (in JPS; dbSNP:rs80338963)"
/evidence="ECO:0000269|PubMed:9811934"
/id="VAR_019572"
VARIANT 361
/note="R -> H (in a colorectal cancer sample; somatic
mutation; dbSNP:rs377767347)"
/evidence="ECO:0000269|PubMed:16959974"
/id="VAR_036477"
VARIANT 386
/note="G -> D (in JP/HHT; dbSNP:rs121912580)"
/evidence="ECO:0000269|PubMed:15031030"
/id="VAR_019573"
VARIANT 493
/note="D -> H (in pancreatic carcinoma; dbSNP:rs121912578)"
/evidence="ECO:0000269|PubMed:8553070"
/id="VAR_011380"
VARIANT 500
/note="I -> M (in MYHRS; dbSNP:rs281875320)"
/evidence="ECO:0000269|PubMed:22158539"
/id="VAR_067602"
VARIANT 500
/note="I -> T (in MYHRS; there is an enhanced levels of
SMAD4 protein with lower levels of ubiquitinated SMAD4
fibroblasts compared to controls suggesting stabilization
of the mutant protein; 8-fold increase in phosphorylated
SMAD2 and SMAD3; 11-fold increase in phosphorylated SMAD1,
SMAD5 and SMAD8 in cell nuclei compared to controls;
dbSNP:rs281875321)"
/evidence="ECO:0000269|PubMed:22158539,
ECO:0000269|PubMed:22243968"
/id="VAR_067603"
VARIANT 500
/note="I -> V (in MYHRS; dbSNP:rs281875322)"
/evidence="ECO:0000269|PubMed:22158539,
ECO:0000269|PubMed:22243968"
/id="VAR_067604"
MUTAGEN 416
/note="R->S: No effect on heterotrimerization. Partially
diminished transcriptional activation."
/evidence="ECO:0000269|PubMed:11224571"
MUTAGEN 496
/note="R->S: No effect on heterotrimerization. Partially
diminished transcriptional activation."
MUTAGEN 502
/note="R->S: No effect on heterotrimerization. Greatly
reduced transcriptional activation."
/evidence="ECO:0000269|PubMed:11224571"
MUTAGEN 515
/note="R->S: Reduced heterotrimerization."
/evidence="ECO:0000269|PubMed:11224571"
MUTAGEN 519
/note="K->R: Abolishes ubiquitination."
/evidence="ECO:0000269|PubMed:19135894"
HELIX 16..24
/evidence="ECO:0000244|PDB:5MEY"
STRAND 29..31
/evidence="ECO:0000244|PDB:5MEY"
HELIX 33..47
/evidence="ECO:0000244|PDB:5MEY"
HELIX 51..62
/evidence="ECO:0000244|PDB:5MEY"
TURN 63..65
/evidence="ECO:0000244|PDB:5MEY"
STRAND 73..75
/evidence="ECO:0000244|PDB:5MEY"
STRAND 78..80
/evidence="ECO:0000244|PDB:5MEY"
STRAND 82..84
/evidence="ECO:0000244|PDB:5MEY"
STRAND 87..89
/evidence="ECO:0000244|PDB:5MEY"
HELIX 91..99
/evidence="ECO:0000244|PDB:5MEY"
STRAND 109..111
/evidence="ECO:0000244|PDB:5MEY"
HELIX 119..121
/evidence="ECO:0000244|PDB:5MEY"
STRAND 124..127
/evidence="ECO:0000244|PDB:5MEY"
HELIX 130..132
/evidence="ECO:0000244|PDB:5MEY"
STRAND 133..135
/evidence="ECO:0000244|PDB:5MEY"
HELIX 143..145
/evidence="ECO:0000244|PDB:5UWU"
STRAND 288..291
/evidence="ECO:0000244|PDB:1DD1"
STRAND 321..330
/evidence="ECO:0000244|PDB:1YGS"
STRAND 333..342
/evidence="ECO:0000244|PDB:1YGS"
STRAND 346..353
/evidence="ECO:0000244|PDB:1YGS"
STRAND 359..363
/evidence="ECO:0000244|PDB:1YGS"
HELIX 364..366
/evidence="ECO:0000244|PDB:1U7F"
HELIX 374..380
/evidence="ECO:0000244|PDB:1YGS"
TURN 381..385
/evidence="ECO:0000244|PDB:1YGS"
STRAND 387..392
/evidence="ECO:0000244|PDB:1YGS"
TURN 393..395
/evidence="ECO:0000244|PDB:1YGS"
STRAND 396..401
/evidence="ECO:0000244|PDB:1YGS"
STRAND 403..405
/evidence="ECO:0000244|PDB:1YGS"
STRAND 407..410
/evidence="ECO:0000244|PDB:1YGS"
HELIX 412..416
/evidence="ECO:0000244|PDB:1YGS"
TURN 417..419
/evidence="ECO:0000244|PDB:1YGS"
STRAND 427..429
/evidence="ECO:0000244|PDB:1YGS"
STRAND 434..438
/evidence="ECO:0000244|PDB:1YGS"
HELIX 440..454
/evidence="ECO:0000244|PDB:1YGS"
TURN 455..458
/evidence="ECO:0000244|PDB:1DD1"
HELIX 461..464
/evidence="ECO:0000244|PDB:1DD1"
HELIX 493..497
/evidence="ECO:0000244|PDB:1YGS"
STRAND 500..506
/evidence="ECO:0000244|PDB:1YGS"
HELIX 518..520
/evidence="ECO:0000244|PDB:1YGS"
STRAND 521..529
/evidence="ECO:0000244|PDB:1YGS"
HELIX 530..541
/evidence="ECO:0000244|PDB:1YGS"
SEQUENCE 552 AA; 60439 MW; 7EE3C4647712DA90 CRC64;
MDNMSITNTP TSNDACLSIV HSLMCHRQGG ESETFAKRAI ESLVKKLKEK KDELDSLITA
ITTNGAHPSK CVTIQRTLDG RLQVAGRKGF PHVIYARLWR WPDLHKNELK HVKYCQYAFD
LKCDSVCVNP YHYERVVSPG IDLSGLTLQS NAPSSMMVKD EYVHDFEGQP SLSTEGHSIQ
TIQHPPSNRA STETYSTPAL LAPSESNATS TANFPNIPVA STSQPASILG GSHSEGLLQI
ASGPQPGQQQ NGFTGQPATY HHNSTTTWTG SRTAPYTPNL PHHQNGHLQH HPPMPPHPGH
YWPVHNELAF QPPISNHPAP EYWCSIAYFE MDVQVGETFK VPSSCPIVTV DGYVDPSGGD
RFCLGQLSNV HRTEAIERAR LHIGKGVQLE CKGEGDVWVR CLSDHAVFVQ SYYLDREAGR
APGDAVHKIY PSAYIKVFDL RQCHRQMQQQ AATAQAAAAA QAAAVAGNIP GPGSVGGIAP
AISLSAAAGI GVDDLRRLCI LRMSFVKGWG PDYPRQSIKE TPCWIEIHLH RALQLLDEVL
HTMPIADPQP LD


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EIAAB38719 Deletion target in pancreatic carcinoma 4 homolog,Dpc4,MAD homolog 4,Madh4,Mothers against decapentaplegic homolog 4,Mothers against DPP homolog 4,Mouse,Mus musculus,SMAD 4,SMAD family member 4,Smad4,
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EIAAB38715 MAD homolog 4,Madh4,Mothers against decapentaplegic homolog 4,Mothers against DPP homolog 4,Rat,Rattus norvegicus,SMAD 4,SMAD family member 4,Smad4,Smad4
EIAAB38717 Bos taurus,Bovine,MAD homolog 4,Mothers against decapentaplegic homolog 4,Mothers against DPP homolog 4,SMAD 4,SMAD family member 4,Smad4,SMAD4
EIAAB38718 MAD homolog 4,MADH4,Mothers against decapentaplegic homolog 4,Mothers against DPP homolog 4,Pig,SMAD 4,SMAD family member 4,Smad4,SMAD4,Sus scrofa
U0647h CLIA BSP1,BSP-1,Homo sapiens,hSMAD1,Human,JV4-1,MAD homolog 1,MADH1,MADR1,Mad-related protein 1,Mothers against decapentaplegic homolog 1,Mothers against DPP homolog 1,SMAD 1,SMAD family member 1,Smad 96T
E0647h ELISA BSP1,BSP-1,Homo sapiens,hSMAD1,Human,JV4-1,MAD homolog 1,MADH1,MADR1,Mad-related protein 1,Mothers against decapentaplegic homolog 1,Mothers against DPP homolog 1,SMAD 1,SMAD family member 1,Sma 96T
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U2184h CLIA kit hMAD-2,Homo sapiens,hSMAD2,Human,JV18-1,MAD homolog 2,MADH2,MADR2,Mad-related protein 2,Mothers against decapentaplegic homolog 2,Mothers against DPP homolog 2,SMAD 2,SMAD family member 2,Sm 96T
E2184h ELISA kit hMAD-2,Homo sapiens,hSMAD2,Human,JV18-1,MAD homolog 2,MADH2,MADR2,Mad-related protein 2,Mothers against decapentaplegic homolog 2,Mothers against DPP homolog 2,SMAD 2,SMAD family member 2,S 96T
E2184h ELISA hMAD-2,Homo sapiens,hSMAD2,Human,JV18-1,MAD homolog 2,MADH2,MADR2,Mad-related protein 2,Mothers against decapentaplegic homolog 2,Mothers against DPP homolog 2,SMAD 2,SMAD family member 2,Smad2, 96T
U2184h CLIA hMAD-2,Homo sapiens,hSMAD2,Human,JV18-1,MAD homolog 2,MADH2,MADR2,Mad-related protein 2,Mothers against decapentaplegic homolog 2,Mothers against DPP homolog 2,SMAD 2,SMAD family member 2,Smad2,S 96T
U2187m CLIA kit MAD homolog 6,Mad homolog 7,Madh6,Madh7,Mothers against decapentaplegic homolog 6,Mothers against DPP homolog 6,Mouse,Msmad6,Mus musculus,SMAD 6,SMAD family member 6,Smad6,Smad6 96T
E2187m ELISA MAD homolog 6,Mad homolog 7,Madh6,Madh7,Mothers against decapentaplegic homolog 6,Mothers against DPP homolog 6,Mouse,Msmad6,Mus musculus,SMAD 6,SMAD family member 6,Smad6,Smad6 96T
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Pathways :
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP32: Translation Factors
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP2256: Integrated Pancreatic Cancer Pathway
WP2377: Integrated Pancreatic Cancer Pathway
WP1596: Iron Homeostasis
WP505: TGF Beta Signaling Pathway
WP1045: TGF-beta Receptor Signaling Pathway
WP926: TGF-beta Receptor Signaling Pathway
WP1425: BMP signalling and regulation
WP940: Senescence and Autophagy
WP1591: Heart Development
WP560: TGF Beta Signaling Pathway
WP1058: Senescence and Autophagy
WP1098: Wnt Signaling Pathway
WP252: Androgen Receptor Signaling Pathway
WP980: Wnt Signaling Pathway NetPath
WP179: Cell cycle
WP710: DNA damage response (only ATM dependent)
WP190: Cell cycle
WP809: TGF-beta Receptor Signaling Pathway
WP1164: TGF Beta Signaling Pathway
WP1180: Delta-Notch Signaling Pathway
WP362: TGF-beta Receptor Signaling Pathway
WP199: Delta-Notch Signaling Pathway

Related Genes :
[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)
[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)
[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)
[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)
[Smad1 Madh1 Madr1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (Dwarfin-A) (Dwf-A) (Mothers-against-DPP-related 1) (Mad-related protein 1) (mMad1) (SMAD family member 1) (SMAD 1) (Smad1)
[SMAD6 MADH6] Mothers against decapentaplegic homolog 6 (MAD homolog 6) (Mothers against DPP homolog 6) (SMAD family member 6) (SMAD 6) (Smad6) (hSMAD6)
[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 Mad1 Madh1] 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)
[Smad3 Madh3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (mMad3) (SMAD family member 3) (SMAD 3) (Smad3)
[SMAD1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (SMAD family member 1) (SMAD 1) (Smad1)
[Smad7 Madh7] Mothers against decapentaplegic homolog 7 (MAD homolog 7) (Mothers against DPP homolog 7) (SMAD family member 7) (SMAD 7) (Smad7)
[SMAD4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (SMAD family member 4) (SMAD 4) (Smad4)
[SMAD3 MADH3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (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)
[Dcp1a Mitc1 Smif] mRNA-decapping enzyme 1A (EC 3.-.-.-) (MAD homolog 4-interacting transcription coactivator 1) (Smad4-interacting transcriptional co-activator) (Transcription factor SMIF)
[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)
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[Mad CG12399] Protein mothers against dpp
[DNAJA1 DNAJ2 HDJ2 HSJ2 HSPF4] DnaJ homolog subfamily A member 1 (DnaJ protein homolog 2) (HSDJ) (Heat shock 40 kDa protein 4) (Heat shock protein J2) (HSJ-2) (Human DnaJ protein 2) (hDj-2)
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[KMT2B HRX2 KIAA0304 MLL2 MLL4 TRX2 WBP7] Histone-lysine N-methyltransferase 2B (Lysine N-methyltransferase 2B) (EC 2.1.1.354) (Myeloid/lymphoid or mixed-lineage leukemia protein 4) (Trithorax homolog 2) (WW domain-binding protein 7) (WBP-7)
[NSMCE3 HCA4 MAGEG1 NDNL2] Non-structural maintenance of chromosomes element 3 homolog (Non-SMC element 3 homolog) (Hepatocellular carcinoma-associated protein 4) (MAGE-G1 antigen) (Melanoma-associated antigen G1) (Necdin-like protein 2)
[repD ercc2 DDB_G0267414] General transcription and DNA repair factor IIH helicase subunit XPD (TFIIH subunit XPD) (EC 3.6.4.12) (DNA excision repair cross-complementing protein-2 homolog) (DNA repair protein D) (TFIIH basal transcription factor complex helicase repD subunit)
[PLAAT3 HRASLS3 HREV107 PLA2G16] Phospholipase A and acyltransferase 3 (EC 2.3.1.-) (EC 3.1.1.32) (EC 3.1.1.4) (Adipose-specific phospholipase A2) (AdPLA) (Group XVI phospholipase A1/A2) (H-rev 107 protein homolog) (H-REV107) (HREV107-1) (HRAS-like suppressor 1) (HRAS-like suppressor 3) (HRSL3) (HREV107-3) (Renal carcinoma antigen NY-REN-65)
[DNAJB11 EDJ ERJ3 HDJ9 PSEC0121 UNQ537/PRO1080] DnaJ homolog subfamily B member 11 (APOBEC1-binding protein 2) (ABBP-2) (DnaJ protein homolog 9) (ER-associated DNAJ) (ER-associated Hsp40 co-chaperone) (Endoplasmic reticulum DNA J domain-containing protein 3) (ER-resident protein ERdj3) (ERdj3) (ERj3p) (HEDJ) (Human DnaJ protein 9) (hDj-9) (PWP1-interacting protein 4)

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