SMAD2 Protein, Human (His-SUMO)

The SMAD2 protein functions as a receptor-regulated SMAD (R-SMAD), serving as an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. It binds the TRE element in the promoter region of numerous genes regulated by TGF-beta, and upon forming the SMAD2/SMAD4 complex, it activates transcription. SMAD2 plays a role in promoting TGFB1-mediated transcription of odontoblastic differentiation genes in dental papilla cells. Additionally, it positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ, acting as a negative regulator. There is evidence suggesting its potential function as a tumor suppressor in colorectal carcinoma. SMAD2 exists as a monomer in the absence of TGF-beta and forms a heterodimer with co-SMAD, SMAD4, in the nucleus to constitute the transactivation complex SMAD2/SMAD4. It interacts with various proteins, including ZFYVE9, TAZ/WWRT1, FOXH1, SNW1, CREB-binding protein (CBP), EP300, SNON, ALK4/ACVR1B, SKOR1, SKOR2, PRDM16, LEMD3, RBPMS, WWP1, RANBP3, PDPK1, DAB2, USP15, PPP5C, LDLRAD4, PMEPA1, ZFHX3, ZNF451, SMURF2, PPM1A, TGF-beta, TGFBR1, TGIF, TRIM33, ZNF580, NEDD4L, HGS, AIP1, WWP1, PML, ZNF8, RNF111, and YAP1, participating in diverse cellular processes, including signal transduction, transcriptional regulation, and protein-protein interactions.