Description: Homo sapiens Smad nuclear interacting protein 1 (SNIP1), mRNA. RefSeq Summary (NM_024700): This gene encodes a protein that contains a coiled-coil motif and C-terminal forkhead-associated (FHA) domain. The encoded protein functions as a transcriptional coactivator that increases c-Myc activity and inhibits transforming growth factor beta (TGF-beta) and nuclear factor kappa-B (NF-kB) signaling. The encoded protein also regulates the stability of cyclin D1 mRNA, and may play a role in cell proliferation and cancer progression. Mutations in this gene are a cause of psychomotor retardation, epilepsy, and craniofacial dysmorphism (PMRED). [provided by RefSeq, Mar 2012]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Transcript (Including UTRs) Position: hg19 chr1:38,000,050-38,019,945 Size: 19,896 Total Exon Count: 4 Strand: - Coding Region Position: hg19 chr1:38,003,349-38,019,830 Size: 16,482 Coding Exon Count: 4
ID:SNIP1_HUMAN DESCRIPTION: RecName: Full=Smad nuclear-interacting protein 1; AltName: Full=FHA domain-containing protein SNIP1; 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. INTERACTION: P01106:MYC; NbExp=9; IntAct=EBI-749336, EBI-447544; SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Ubiquitous, with highest expression in heart and skeletal muscle. PTM: Degraded by the proteasome upon binding to the SMAD1/OAZ1/PSMB4 complex. PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. 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.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q8TAD8
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Biological Process: GO:0006355 regulation of transcription, DNA-templated GO:0007249 I-kappaB kinase/NF-kappaB signaling GO:0031047 gene silencing by RNA GO:0035196 production of miRNAs involved in gene silencing by miRNA
US Server
