background:
Members of the transforming growth factor-beta (TGF-Beta) superfamily play critical roles in controlling cell growth and differentiation. Effects of TGF-Beta family ligands are mediated by Smad proteins. The Smad nuclear interacting protein (SNIP1) contains a forkhead-associated (FHA) domain and acts as a nuclear inhibitor of CBP/p300. SNIP1 potently inhibits the activity of NF-kappa B, which binds the C/H1 domain of CBP/p300, by competing for the binding site. SNIP1 is also thought to induce expression of Cyclin D1 to promote cellular proliferation. SNIP1 is ubiquitously expressed with high expression in heart and skeletal muscle.
Function:
Down-regulates NF-kappa-B signaling by competing with RELA for CREBBP/EP300 binding. Involved in the microRNA (miRNA) biogenesis.
Subunit:
Binds SMAD4 and CREBBP/EP300. Binds the SMAD1/OAZ1/PSMB4 complex. Interacts with DROSHA and SMARCA4. Component of the SNARP complex which consists at least of SNIP1, SNW1, THRAP3, BCLAF1 and PNN.
Subcellular Location:
Nucleus.
Tissue Specificity:
Tissue specificityUbiquitous, with highest expression in heart and skeletal muscle.
Post-translational modifications:
Degraded by the proteasome upon binding to the SMAD1/OAZ1/PSMB4 complex.
DISEASE:
Defects in SNIP1 are the cause of psychomotor retardation, epilepsy, and craniofacial dysmorphism (PMRED) [MIM:614501]. A disease characterized by severe psychomotor retardation, intractable seizures, dysmorphic features, and a lumpy skull surface. Patients are hypotonic and have poor feeding in the neonatal period.
Similarity:
Contains 1 FHA domain.
Database links:
UniProtKB/Swiss-Prot: Q8TAD8.1
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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