E3 ubiquitin-protein ligase SMURF2 Recombinant Protein | SMURF2 recombinant protein

Recombinant Human E3 ubiquitin-protein ligase SMURF2

Cat. Num. AAA1357228

• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: E3 ubiquitin-protein ligase SMURF2; Recombinant Human E3 ubiquitin-protein ligase SMURF2; SMAD ubiquitination regulatory factor 2; SMAD-specific E3 ubiquitin-protein ligase 2; SMURF2 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 1-748. Full Length
• Sequence: MSNPGGRRNGPVKLRLTVLCAKNLVKKDFFRLPDPFAKVVVDGSGQCHSTDTVKNTLDPKWNQHYDLYIGKSDSVTISVWNHKKIHKKQGAGFLGCVRLLSNAINRLKDTGYQRLDLCKLGPNDNDTVRGQIVVSLQSRDRIGTGGQVVDCSRLFDNDLPDGWEERRTASGRIQYLNHITRTTQWERPTRPASEYSSPGRPLSCFVDENTPISGTNGATCGQSSDPRLAERRVRSQRHRNYMSRTHLHTPPDLPEGYEQRTTQQGQVYFLHTQTGVSTWHDPRVPRDLSNINCEELGPLPPGWEIRNTATGRVYFVDHNNRTTQFTDPRLSANLHLVLNRQNQLKDQQQQQVVSLCPDDTECLTVPRYKRDLVQKLKILRQELSQQQPQAGHCRIEVSREEIFEESYRQVMKMRPKDLWKRLMIKFRGEEGLDYGGVAREWLYLLSHEMLNPYYGLFQYSRDDIYTLQINPDSAVNPEHLSYFHFVGRIMGMAVFHGHYIDGGFTLPFYKQLLGKSITLDDMELVDPDLHNSLVWILENDITGVLDHTFCVEHNAYGEIIQHELKPNGKSIPVNEENKKEYVRLYVNWRFLRGIEAQFLALQKGFNEVIPQHLLKTFDEKELELIICGLGKIDVNDWKVNTRLKHCTPDSNIVKWFWKAVEFFDEERRARLLQFVTGSSRVPLQGFKALQGAAGPRLFTIHQIDACTNNLPKAHTCFNRIDIPPYESYEKLYEKLLTAIEETCGFAVE

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

SDS-PAGE

Related Product Information for SMURF2 recombinant protein

E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Interacts with SMAD1 and SMAD7 in order to trigger their ubiquitination and proteasome-dependent degradation. In addition, interaction with SMAD7 activates autocatalytic degradation, which is prevented by interaction with SCYE1. Forms a stable complex with the TGF-beta receptor-mediated phosphorylated SMAD2 and SMAD3. In this way, SMAD2 may recruit substrates, such as SNON, for ubiquitin-mediated degradation. Enhances the inhibitory activity of SMAD7 and reduces the transcriptional activity of SMAD2. Coexpression of SMURF2 with SMAD1 results in considerable decrease in steady-state level of SMAD1 protein and a smaller decrease of SMAD2 level.

Product Categories/Family for SMURF2 recombinant protein

Epigenetics and Nuclear Signaling

References

Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF-beta receptor for degradation.Kavsak P., Rasmussen R.K., Causing C.G., Bonni S., Zhu H., Thomsen G.H., Wrana J.L.Mol. Cell 6:1365-1375(2000) Smurf2 Is a ubiquitin E3 ligase mediating proteasome-dependent degradation of Smad2 in transforming growth factor-beta signaling.Lin X., Liang M., Feng X.-H.J. Biol. Chem. 275:36818-36822(2000) Regulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase.Zhang Y., Chang C., Gehling D.J., Hemmati-Brivanlou A., Derynck R.Proc. Natl. Acad. Sci. U.S.A. 98:974-979(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) Distinct endocytic pathways regulate TGF-beta receptor signalling and turnover.Di Guglielmo G.M., Le Roy C., Goodfellow A.F., Wrana J.L.Nat. Cell Biol. 5:410-421(2003) ErratumDi Guglielmo G.M., Le Roy C., Goodfellow A.F., Wrana J.L.Nat. Cell Biol. 5:680-680(2003) The RING-H2 protein RNF11 is overexpressed in breast cancer and is a target of Smurf2 E3 ligase.Subramaniam V., Li H., Wong M.J., Kitching R., Attisano L., Wrana J., Zubovits J., Burger A.M., Seth A.K.Br. J. Cancer 89:1538-1544(2003) An RNF11 Smurf2 complex mediates ubiquitination of the AMSH protein.Li H., Seth A.K.Oncogene 23:1801-1808(2004) AIMP1/p43 downregulates TGF-beta signaling via stabilization of smurf2.Lee Y.S., Han J.M., Son S.H., Choi J.W., Jeon E.J., Bae S.-C., Park Y.I., Kim S.Biochem. Biophys. Res. Commun. 371:395-400(2008) Control of the activity of WW-HECT domain E3 ubiquitin ligases by NDFIP proteins.Mund T., Pelham H.R.EMBO Rep. 10:501-507(2009) SCF(FBXL15) regulates BMP signalling by directing the degradation of HECT-type ubiquitin ligase Smurf1.Cui Y., He S., Xing C., Lu K., Wang J., Xing G., Meng A., Jia S., He F., Zhang L.EMBO J. 30:2675-2689(2011) Regulation of Smurf2 ubiquitin ligase activity by anchoring the E2 to the HECT domain.Ogunjimi A.A., Briant D.J., Pece-Barbara N., Le Roy C., Di Guglielmo G.M., Kavsak P., Rasmussen R.K., Seet B.T., Sicheri F., Wrana J.L.Mol. Cell 19:297-308(2005) An expanded WW domain recognition motif revealed by the interaction between Smad7 and the E3 ubiquitin ligase Smurf2.Chong P.A., Lin H., Wrana J.L., Forman-Kay J.D.J. Biol. Chem. 281:17069-17075(2006) Autoinhibition of the HECT-type ubiquitin ligase Smurf2 through its C2 domain.Wiesner S., Ogunjimi A.A., Wang H.R., Rotin D., Sicheri F., Wrana J.L., Forman-Kay J.D.Cell 130:651-662(2007)

NCBI and Uniprot Product Information

• NCBI GI #: 12232397
• NCBI GeneID: 64750
• NCBI Accession #: NP_073576.1
• NCBI GenBank Nucleotide #: NM_022739.3
• UniProt Accession #: Q9HAU4; Q52LL1; Q9H260
• Molecular Weight: 113.2 kDa
• NCBI Official Full Name: E3 ubiquitin-protein ligase SMURF2
• NCBI Official Synonym Full Names: SMAD specific E3 ubiquitin protein ligase 2
• NCBI Official Symbol: SMURF2
• NCBI Protein Information: E3 ubiquitin-protein ligase SMURF2
• UniProt Protein Name: E3 ubiquitin-protein ligase SMURF2
• Protein Family: E3 ubiquitin-protein ligase
• UniProt Gene Name: SMURF2
• UniProt Synonym Gene Names: hSMURF2
• UniProt Entry Name: SMUF2_HUMAN

Uniprot Description

SMURF2: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Interacts with SMAD1 and SMAD7 in order to trigger their ubiquitination and proteasome-dependent degradation. In addition, interaction with SMAD7 activates autocatalytic degradation, which is prevented by interaction with SCYE1. Forms a stable complex with the TGF-beta receptor-mediated phosphorylated SMAD2 and SMAD3. In this way, SMAD2 may recruit substrates, such as SNON, for ubiquitin-mediated degradation. Enhances the inhibitory activity of SMAD7 and reduces the transcriptional activity of SMAD2. Coexpression of SMURF2 with SMAD1 results in considerable decrease in steady-state level of SMAD1 protein and a smaller decrease of SMAD2 level.

Protein type: EC 6.3.2.-; EC 6.3.2.19; Ubiquitin conjugating system; Ubiquitin ligase; Ligase

Chromosomal Location of Human Ortholog: 17q22-q23

Cellular Component: cytosol; lipid raft; nucleoplasm; nucleus; plasma membrane; ubiquitin ligase complex

Molecular Function: identical protein binding; ligase activity; protein binding; SMAD binding; transforming growth factor beta receptor binding; ubiquitin-protein ligase activity

Biological Process: BMP signaling pathway; gene expression; 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; protein ubiquitination during ubiquitin-dependent protein catabolic process; regulation of transforming growth factor beta receptor signaling pathway; transcription initiation from RNA polymerase II promoter; transcription, DNA-dependent; transforming growth factor beta receptor signaling pathway; ubiquitin-dependent protein catabolic process; ubiquitin-dependent SMAD protein catabolic process