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SMAD2 — SP1

Pathways - manually collected, often from reviews:

• OpenBEL Selventa BEL large corpus: SP1 → SMAD2 (increases, SMAD2 Activity) Feng et al., EMBO J 2000
  Evidence: In the nucleoprotein complex, Smad2 interacted through its C-domain with Sp1 and enhanced the DNA binding and transcriptional activity of Sp1
• OpenBEL Selventa BEL large corpus: SP1 → Complex of SMAD2-SP1 (directlyIncreases, SMAD2/SP1 Activity) Feng et al., EMBO J 2000
  Evidence: In the nucleoprotein complex, Smad2 interacted through its C-domain with Sp1 and enhanced the DNA binding and transcriptional activity of Sp1
• FastForward regulation: SP1 → SMAD2 (transcriptional regulation, unknown)
  Evidence: DNABINDING
• KEGG TGF-beta signaling pathway: Complex of SMAD2-SMAD3-SMAD4 → Complex of CREBBP-EP300-SP1 (protein-protein, activation)
  
• NCI Pathway Database Regulation of nuclear SMAD2/3 signaling: AP1 complex (FOS-JUN) → SMAD2-3/SMAD4/SP1 complex (SMAD2_SMAD3-SMAD4-SP1) (transcription, activates)
  Brodin et al., J Biol Chem 2000
  Evidence: mutant phenotype, reporter gene, physical interaction, other species
• NCI Pathway Database Regulation of nuclear SMAD2/3 signaling: SMAD2-3/SMAD4/SP1/MIZ-1 complex (SMAD2_SMAD3-SMAD4-SP1-ZBTB17) → SMAD2-3/SMAD4/SP1 complex (SMAD2_SMAD3-SMAD4-SP1) (modification, collaborate)
  Seoane et al., Nat Cell Biol 2001
  Evidence: mutant phenotype, physical interaction
• NCI Pathway Database Regulation of nuclear SMAD2/3 signaling: SMAD2-3/SMAD4/SP1/MIZ-1 complex (SMAD2_SMAD3-SMAD4-SP1-ZBTB17) → MIZ-1 (ZBTB17) (modification, collaborate) Seoane et al., Nat Cell Biol 2001
  Evidence: mutant phenotype, physical interaction
• NCI Pathway Database Regulation of nuclear SMAD2/3 signaling: SMAD2-3/SMAD4/SP1 complex (SMAD2_SMAD3-SMAD4-SP1) → MIZ-1 (ZBTB17) (modification, collaborate) Seoane et al., Nat Cell Biol 2001
  Evidence: mutant phenotype, physical interaction
• NCI Pathway Database Regulation of nuclear SMAD2/3 signaling: MYC/MIZ-1 complex (MYC-ZBTB17) → SMAD2-3/SMAD4/SP1/MIZ-1 complex (SMAD2_SMAD3-SMAD4-SP1-ZBTB17) (transcription, inhibits)
  Feng et al., EMBO J 2000, Seoane et al., Nat Cell Biol 2001, Matsuura et al., Nature 2004
  Evidence: mutant phenotype, reporter gene, physical interaction
• NCI Pathway Database Regulation of nuclear SMAD2/3 signaling: SMAD3/SMAD4 complex (SMAD3-SMAD4) → SMAD2-3/SMAD4/SP1/MIZ-1 complex (SMAD2_SMAD3-SMAD4-SP1-ZBTB17) (transcription, inhibits)
  Feng et al., EMBO J 2000, Seoane et al., Nat Cell Biol 2001, Matsuura et al., Nature 2004
  Evidence: mutant phenotype, reporter gene, physical interaction
• NCI Pathway Database Validated targets of C-MYC transcriptional repression: SMAD2-3/SMAD4/MYC/Max/MIZ-1 complex (MYC-MAX-ZBTB17-SMAD2_SMAD3-SMAD4) → SMAD2-3/SMAD4/SP1 complex (SMAD2_SMAD3-SMAD4-SP1) (transcription, inhibits)
  Staller et al., Nat Cell Biol 2001, Seoane et al., Nat Cell Biol 2001, Feng et al., Mol Cell 2002
  Evidence: mutant phenotype, reporter gene, physical interaction
• NCI Pathway Database Regulation of nuclear SMAD2/3 signaling: SP1 (SP1) → SMAD2-3/SMAD4 complex (SMAD2_SMAD3-SMAD4) (modification, collaborate)
  Feng et al., EMBO J 2000
  Evidence: physical interaction
• NCI Pathway Database Regulation of nuclear SMAD2/3 signaling: SP1 (SP1) → SMAD2-3/SMAD4/SP1 complex (SMAD2_SMAD3-SMAD4-SP1) (modification, collaborate)
  Feng et al., EMBO J 2000
  Evidence: physical interaction
• NCI Pathway Database Regulation of nuclear SMAD2/3 signaling: SMAD2-3/SMAD4 complex (SMAD2_SMAD3-SMAD4) → SMAD2-3/SMAD4/SP1 complex (SMAD2_SMAD3-SMAD4-SP1) (modification, collaborate)
  Feng et al., EMBO J 2000
  Evidence: physical interaction
• Reactome Reaction: SP1 → SMAD2 (reaction) Feng et al., EMBO J 2000
• Reactome Reaction: SP1 → SMAD2 (indirect_complex) Feng et al., EMBO J 2000

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: SMAD2 — SP1 (physical association, affinity chromatography technology) Poncelet et al., J Biol Chem 2001*
• IRef Biogrid Interaction: SMAD2 — SP1 (direct interaction, two hybrid) Pardali et al., J Biol Chem 2000*
• IRef Biogrid Interaction: SMAD2 — SP1 (direct interaction, pull down) Pardali et al., J Biol Chem 2000*
• IRef Biogrid Interaction: SMAD2 — SP1 (physical association, affinity chromatography technology) Pardali et al., J Biol Chem 2000*
• IRef Biogrid Interaction: SMAD2 — SP1 (physical association, affinity chromatography technology) Barrasa et al., Biochim Biophys Acta 2012*
• IRef Hprd Interaction: SP1 — SMAD2 (in vivo) Poncelet et al., J Biol Chem 2001*
• IRef Ophid Interaction: SMAD2 — SP1 (aggregation, interologs mapping) Brown et al., Bioinformatics 2005

Text-mined interactions from Literome

Feng et al., EMBO J 2000 : In the nucleoprotein complex, Smad2 interacted through its C-domain with Sp1 and enhanced the DNA binding and transcriptional activity of Sp1
Jungert et al., Carcinogenesis 2006 (Pancreatic Neoplasms) : Moreover, inhibition of Sp1-DNA binding or transfection of Sp1-specific siRNA prevents TGFbeta induced Smad7 expression and consequently enhances Smad signaling in pancreatic cancer cells, as indicated by increased receptor mediated phosphorylation of Smad3
Wang et al., Differentiation 2011 : The increase of Sp1 , but not Smad 2/3 activation was almost completely blocked by the addition of TSA