Mothers against decapentaplegic homolog 2 Recombinant Protein | SMAD2 recombinant protein

Recombinant Human Mothers against decapentaplegic homolog 2 protein

• Gene Names: SMAD2; JV18; MADH2; MADR2; JV18-1; hMAD-2; hSMAD2
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Mothers against decapentaplegic homolog 2; Recombinant Human Mothers against decapentaplegic homolog 2 protein; JV18-1; Mad-related protein 2; hMAD-2; SMAD family member 2; SMAD 2; Smad2; hSMAD2; SMAD2 recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 2-467
• Sequence: SSILPFTPPVVKRLLGWKKSAGGSGGAGGGEQNGQEEKWCEKAVKSLVKKLKKTGRLDELEKAITTQNCNTKCVTIPSTCSEIWGLSTPNTIDQWDTTGLYSFSEQTRSLDGRLQVSHRKGLPHVIYCRLWRWPDLHSHHELKAIENCEYAFNLKKDEVCVNPYHYQRVETPVLPPVLVPRHTEILTELPPLDDYTHSIPENTNFPAGIEPQSNYIPETPPPGYISEDGETSDQQLNQSMDTGSPAELSPTTLSP
• Sequence Length: 467

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

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Related Product Information for SMAD2 recombinant protein

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.

Product Categories/Family for SMAD2 recombinant protein

Transcription

References

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Genet. 13:347-349(1996) Receptor-associated Mad homologues synergize as effectors of the TGF-beta response.Zhang Y., Feng X.-H., Wu R.-Y., Derynck R.Nature 383:168-172(1996) MADR2 maps to 18q21 and encodes a TGFbeta-regulated MAD-related protein that is functionally mutated in colorectal carcinoma.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.Cell 86:543-552(1996) Dual role of the Smad4/DPC4 tumor suppressor in TGFbeta-inducible transcriptional complexes.Liu F., Pouponnot C., Massague J.Genes Dev. 11:3157-3167(1997) Characterization of the MADH2/Smad2 gene, a human Mad homolog responsible for the transforming growth factor-beta and activin signal transduction pathway.Takenoshita S., Mogi A., Nagashima M., Yang K., Yagi K., Hanyu A., Nagamachi Y., Miyazono K., Hagiwara K.Genomics 48:1-11(1998) Bienvenut W.V., von Kriegsheim A., Kolch W.Submitted (DEC-2008) to UniProtKB MADR2 is a substrate of the TGFbeta receptor and its phosphorylation is required for nuclear accumulation and signaling.Macias-Silva M., Abdollah S., Hoodless P.A., Pirone R., Attisano L., Wrana J.L.Cell 87:1215-1224(1996) SARA, a FYVE domain protein that recruits Smad2 to the TGFbeta receptor.Tsukazaki T., Chiang T.A., Davison A.F., Attisano L., Wrana J.L.Cell 95:779-791(1998) Smad proteins exist as monomers in vivo and undergo homo- and hetero-oligomerization upon activation by serine/threonine kinase receptors.Kawabata M., Inoue H., Hanyu A., Imamura T., Miyazono K.EMBO J. 17:4056-4065(1998) Alternatively spliced variant of Smad2 lacking exon 3. 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Endocrinol. 13:15-23(1999) The adaptor molecule Disabled-2 links the transforming growth factor beta receptors to the Smad pathway.Hocevar B.A., Smine A., Xu X.X., Howe P.H.EMBO J. 20:2789-2801(2001) Ski-interacting protein interacts with Smad proteins to augment transforming growth factor-beta-dependent transcription.Leong G.M., Subramaniam N., Figueroa J., Flanagan J.L., Hayman M.J., Eisman J.A., Kouzmenko A.P.J. Biol. Chem. 276:18243-18248(2001) TGF-beta induces assembly of a Smad2-Smurf2 ubiquitin ligase complex that targets SnoN for degradation.Bonni S., Wang H.R., Causing C.G., Kavsak P., Stroschein S.L., Luo K., Wrana J.L.Nat. Cell Biol. 3:587-595(2001) 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.Abdel-Wahab N., Wicks S.J., Mason R.M., Chantry A.Biochem. J. 362:643-649(2002) Modulation of Smad2-mediated signaling by extracellular signal-regulated kinase.Funaba M., Zimmerman C.M., Mathews L.S.J. Biol. Chem. 277:41361-41368(2002) MAN1, an integral protein of the inner nuclear membrane, binds Smad2 and Smad3 and antagonizes transforming growth factor-beta signaling.Lin F., Morrison J.M., Wu W., Worman H.J.Hum. Mol. Genet. 14:437-445(2005) 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.Pan D., Estevez-Salmeron L.D., Stroschein S.L., Zhu X., He J., Zhou S., Luo K.J. Biol. Chem. 280:15992-16001(2005) Cloning and functional characterization of a new Ski homolog, Fussel-18, specifically expressed in neuronal tissues.Arndt S., Poser I., Schubert T., Moser M., Bosserhoff A.-K.Lab. Invest. 85:1330-1341(2005) PPM1A functions as a Smad phosphatase to terminate TGFbeta signaling.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.Cell 125:915-928(2006) Hematopoiesis controlled by distinct TIF1gamma and Smad4 branches of the TGFbeta pathway.He W., Dorn D.C., Erdjument-Bromage H., Tempst P., Moore M.A., Massague J.Cell 125:929-941(2006) The DNA binding activities of Smad2 and Smad3 are regulated by coactivator-mediated acetylation.Simonsson M., Kanduri M., Gronroos E., Heldin C.H., Ericsson J.J. Biol. Chem. 281:39870-39880(2006) Potentiation of Smad-mediated transcriptional activation by the RNA-binding protein RBPMS.Sun Y., Ding L., Zhang H., Han J., Yang X., Yan J., Zhu Y., Li J., Song H., Ye Q.Nucleic Acids Res. 34:6314-6326(2006) 3-Phosphoinositide-dependent PDK1 negatively regulates transforming growth factor-beta-induced signaling in a kinase-dependent manner through physical interaction with Smad proteins.Seong H.A., Jung H., Kim K.T., Ha H.J. Biol. Chem. 282:12272-12289(2007) Fussel-15, a novel Ski/Sno homolog protein, antagonizes BMP signaling.Arndt S., Poser I., Moser M., Bosserhoff A.-K.Mol. Cell. Neurosci. 34:603-611(2007) Smad3 is acetylated by p300/CBP to regulate its transactivation activity.Inoue Y., Itoh Y., Abe K., Okamoto T., Daitoku H., Fukamizu A., Onozaki K., Hayashi H.Oncogene 26:500-508(2007) Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.Mol. Cell 31:438-448(2008) TAZ controls Smad nucleocytoplasmic shuttling and regulates human embryonic stem-cell self-renewal.Varelas X., Sakuma R., Samavarchi-Tehrani P., Peerani R., Rao B.M., Dembowy J., Yaffe M.B., Zandstra P.W., Wrana J.L.Nat. Cell Biol. 10:837-848(2008) A quantitative atlas of mitotic phosphorylation.Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.Anal. Chem. 81:4493-4501(2009) Nuclear export of Smad2 and Smad3 by RanBP3 facilitates termination of TGF-beta signaling.Dai F., Lin X., Chang C., Feng X.H.Dev. Cell 16:345-357(2009) SKI and MEL1 cooperate to inhibit transforming growth factor-beta signal in gastric cancer cells.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.J. Biol. Chem. 284:3334-3344(2009) TMEPAI, a transmembrane TGF-beta-inducible protein, sequesters Smad proteins from active participation in TGF-beta signaling.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.Mol. Cell 37:123-134(2010) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.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.Sci. Signal. 3:RA3-RA3(2010) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) ZNF580, a novel C2H2 zinc-finger transcription factor, interacts with the TGF-beta signal molecule Smad2.Luo Y., Hu W., Xu R., Hou B., Zhang L., Zhang W.Cell Biol. Int. 35:1153-1157(2011) USP15 is a deubiquitylating enzyme for receptor-activated SMADs.Inui M., Manfrin A., Mamidi A., Martello G., Morsut L., Soligo S., Enzo E., Moro S., Polo S., Dupont S., Cordenonsi M., Piccolo S.Nat. Cell Biol. 13:1368-1375(2011) Protein phosphatase 5 modulates SMAD3 function in the transforming growth factor-? pathway.Bruce D.L., Macartney T., Yong W., Shou W., Sapkota G.P.Cell. Signal. 24:1999-2006(2012) Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.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.Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) CRL1-FBXO11 promotes Cdt2 ubiquitylation and degradation and regulates Pr-Set7/Set8-mediated cellular migration.Abbas T., Mueller A.C., Shibata E., Keaton M., Rossi M., Dutta A.Mol. Cell 49:1147-1158(2013) C18 ORF1, a novel negative regulator of transforming growth factor-beta signaling.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.J. Biol. Chem. 289:12680-12692(2014) TGF-beta signal transduction.Massague J.Annu. Rev. Biochem. 67:753-791(1998) Remarkable versatility of Smad proteins in the nucleus of transforming growth factor-beta activated cells.Verschueren K., Huylebroeck D.Cytokine Growth Factor Rev. 10:187-199(1999) The Smad pathway.Wrana J.L., Attisano L.Cytokine Growth Factor Rev. 11:5-13(2000) TGF-beta signaling by Smad proteins.Miyazono K.Cytokine Growth Factor Rev. 11:15-22(2000) Structural basis of Smad2 recognition by the Smad anchor for receptor activation.Wu G., Chen Y.-G., Ozdamar B., Gyuricza C.A., Chong P.A., Wrana J.L., Massague J., Shi Y.Science 287:92-97(2000) Structural basis of heteromeric smad protein assembly in TGF-beta signaling.Chacko B.M., Qin B.Y., Tiwari A., Shi G., Lam S., Hayward L.J., De Caestecker M., Lin K.Mol. Cell 15:813-823(2004) The consensus coding sequences of human breast and colorectal cancers.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.Science 314:268-274(2006) +Additional computationally mapped references.<p>Provides general information on the entry.

NCBI and Uniprot Product Information

• NCBI GI #: 51173730
• NCBI GeneID: 4087
• NCBI Accession #: NP_001003652.1
• NCBI GenBank Nucleotide #: NM_001003652.3
• UniProt Accession #: Q15796
• Molecular Weight: 56.2kD
• NCBI Official Full Name: mothers against decapentaplegic homolog 2 isoform 1
• NCBI Official Synonym Full Names: SMAD family member 2
• NCBI Official Symbol: SMAD2
• NCBI Official Synonym Symbols: JV18; MADH2; MADR2; JV18-1; hMAD-2; hSMAD2
• NCBI Protein Information: mothers against decapentaplegic homolog 2
• UniProt Protein Name: Mothers against decapentaplegic homolog 2
• Protein Family: Mothers against decapentaplegic
• UniProt Gene Name: SMAD2
• UniProt Synonym Gene Names: MADH2; MADR2; MAD homolog 2; Mothers against DPP homolog 2; hMAD-2; SMAD 2; Smad2; hSMAD2
• UniProt Entry Name: SMAD2_HUMAN

NCBI Description

The protein encoded by this gene belongs to the SMAD, a family of proteins similar to the gene products of the Drosophila gene 'mothers against decapentaplegic' (Mad) and the C. elegans gene Sma. SMAD proteins are signal transducers and transcriptional modulators that mediate multiple signaling pathways. This protein mediates the signal of the transforming growth factor (TGF)-beta, and thus regulates multiple cellular processes, such as cell proliferation, apoptosis, and differentiation. This protein is recruited to the TGF-beta receptors through its interaction with the SMAD anchor for receptor activation (SARA) protein. In response to TGF-beta signal, this protein is phosphorylated by the TGF-beta receptors. The phosphorylation induces the dissociation of this protein with SARA and the association with the family member SMAD4. The association with SMAD4 is important for the translocation of this protein into the nucleus, where it binds to target promoters and forms a transcription repressor complex with other cofactors. This protein can also be phosphorylated by activin type 1 receptor kinase, and mediates the signal from the activin. Alternatively spliced transcript variants have been observed for this gene. [provided by RefSeq, May 2012]

Uniprot Description

SMAD2: ubiquitously expressed transcription factor phosphorylated and activated by TGF-beta receptor-type kinases. Participates in a wide range of critical processes including morphogenesis, cell-fate determination, proliferation, differentiation and apoptosis. Phosphorylated Smads dimerize with collaborating Smad4 and are translocated into the nucleus, where the transcription of target genes is stimulated. Two alternatively spliced isoforms have been described.

Protein type: DNA-binding; Transcription factor

Chromosomal Location of Human Ortholog: 18q21.1

Cellular Component: cytoplasm; cytosol; nuclear chromatin; nucleoplasm; nucleus; transcription factor complex

Molecular Function: chromatin binding; DNA binding; double-stranded DNA binding; metal ion binding; phosphatase binding; protein binding; protein heterodimerization activity; protein homodimerization activity; SMAD binding; transcription activator binding; transcription factor activity; transcription factor binding; transforming growth factor beta receptor binding; transforming growth factor beta receptor, pathway-specific cytoplasmic mediator activity; ubiquitin protein ligase binding

Biological Process: activin receptor signaling pathway; anterior/posterior pattern formation; cell fate commitment; common-partner SMAD protein phosphorylation; embryonic cranial skeleton morphogenesis; embryonic foregut morphogenesis; endoderm formation; gastrulation; gene expression; in utero embryonic development; insulin secretion; lung development; mesoderm formation; negative regulation of cell proliferation; negative regulation of transcription from RNA polymerase II promoter; negative regulation of transcription, DNA-dependent; negative regulation of transforming growth factor beta receptor signaling pathway; organ growth; palate development; pancreas development; paraxial mesoderm morphogenesis; pericardium development; positive regulation of BMP signaling pathway; positive regulation of transcription from RNA polymerase II promoter; positive regulation of transcription, DNA-dependent; post-embryonic development; primary microRNA processing; regulation of binding; regulation of transforming growth factor beta receptor signaling pathway; response to glucose stimulus; SMAD protein complex assembly; somatic stem cell maintenance; transcription initiation from RNA polymerase II promoter; transcription, DNA-dependent; transforming growth factor beta receptor signaling pathway; ureteric bud development; zygotic determination of dorsal/ventral axis