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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]
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Monomer; in the absence of TGF-beta (By similarity). Heterodimer; in the presence of TGF-beta (By similarity). Forms a heterodimer with co-SMAD, SMAD4, in the nucleus to form the transactivation complex SMAD2/SMAD4 (By similarity). Found in a complex with SMAD3 and TRIM33 upon addition of TGF-beta (By similarity). Identified in a complex that contains at least ZNF451, SMAD2, SMAD3 and SMAD4 (By similarity). Interacts (via the MH2 domain) with ZFYVE9; may form trimers with the SMAD4 co-SMAD (By similarity). Interacts with TAZ/WWRT1 (By similarity). Interacts with FOXH1 (By similarity). Interacts with SNW1 (By similarity). Interacts with CREB-binding protein (CBP) and EP300 (By similarity). Interacts with SNON (By similarity). Interacts with ALK4/ACVR1B (By similarity). Interacts with SKOR1 (By similarity). Interacts with SKOR2 (By similarity). Interacts with PRDM16 (By similarity). Interacts (via MH2 domain) with LEMD3 (By similarity). Interacts with RBPMS (By similarity). Interacts with WWP1. Interacts (dephosphorylated form, via the MH1 and MH2 domains) with RANBP3 (via its C-terminal R domain); the interaction results in the export of dephosphorylated SMAD3 out of the nucleus and termination of the TGF-beta signaling (By similarity). Interacts with PDPK1 (via PH domain) (By similarity). Interacts with DAB2; the interactions are enhanced upon TGF-beta stimulation (By similarity). Interacts with USP15 (By similarity). Interacts with PPP5C (By similarity). Interacts with LDLRAD4 (via the SMAD interaction motif) (By similarity). Interacts (via MH2 domain) with PMEPA1 (via the SMAD interaction motif) (By similarity). Interacts with ZFHX3 (By similarity). Interacts with ZNF451 (By similarity). Interacts with SMURF2 when phosphorylated on Ser-465/467 (By similarity). Interacts with PPM1A (By similarity). Interacts with TGF-beta (By similarity). Interacts with TGFBR1 (By similarity). Interacts with TGIF (By similarity). Interacts with SMAD3 and TRIM33 (By similarity). Interacts with ZNF580 (By similarity). Interacts with NEDD4L in response to TGF-beta (By similarity). Interacts with HGS (By similarity). Interacts with AIP1 (By similarity). Interacts with WWP1 (By similarity). Interacts with PML (By similarity). Interacts weakly with ZNF8 (By similarity). Interacts (when phosphorylated) with RNF111; RNF111 acts as an enhancer of the transcriptional responses by mediating ubiquitination and degradation of SMAD2 inhibitors (By similarity). Interacts with YAP1 (when phosphorylated at 'Ser-55') (By similarity). Interacts when phosphorylated with IPO7; the interaction facilitates translocation of SMAD2 to the nucleus (By similarity). Interacts with MTMR4; negatively regulates TGF-beta signaling through SMAD2 dephosphorylation and retention in endosomes (By similarity).
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NUCLEOTIDE SEQUENCE [MRNA]
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No specific effect on enzymatic activity and iron-binding.
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Insulin-like growth factor-binding protein 7
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http://purl.obolibrary.org/obo/ECO_0000269
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http://purl.uniprot.org/uniprot/P48029#attribution-0CF377638F5A1CBD41F0057AA63E263C
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http://purl.uniprot.org/uniprot/Q9H244#attribution-11D96901DD92069C24F2AA2875C0AFD5
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Involved in mRNA export coupled transcription activation by association with both the AMEX and the SAGA complexes. The SAGA complex is a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates histone H2B. The SAGA complex is recruited to specific gene promoters by activators, where it is required for transcription. Required for nuclear receptor-mediated transactivation. Involved in transcription elongation by recruiting the THO complex onto nascent mRNA. The AMEX complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). AMEX participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery (By similarity).
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http://purl.uniprot.org/uniprot/Q9JLN6
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null