Q8TAD8 · SNIP1_HUMAN
- ProteinSmad nuclear-interacting protein 1
- GeneSNIP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids396 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Required for pre-mRNA splicing as component of the spliceosome (PubMed:29360106).
As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). Down-regulates NF-kappa-B signaling by competing with RELA for CREBBP/EP300 binding. Involved in the microRNA (miRNA) biogenesis. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA
As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). Down-regulates NF-kappa-B signaling by competing with RELA for CREBBP/EP300 binding. Involved in the microRNA (miRNA) biogenesis. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | spliceosomal complex | |
Cellular Component | U2 snRNP | |
Cellular Component | U2-type precatalytic spliceosome | |
Molecular Function | mRNA binding | |
Molecular Function | RNA binding | |
Molecular Function | transcription regulator inhibitor activity | |
Biological Process | miRNA processing | |
Biological Process | mRNA splicing, via spliceosome | |
Biological Process | negative regulation of canonical NF-kappaB signal transduction | |
Biological Process | U2-type prespliceosome assembly |
Keywords
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameSmad nuclear-interacting protein 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8TAD8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Neurodevelopmental disorder with hypotonia, craniofacial abnormalities, and seizures (NEDHCS)
- Note
- DescriptionAn autosomal recessive 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.
- See alsoMIM:614501
Natural variants in NEDHCS
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_067542 | 366 | E>G | in NEDHCS; dbSNP:rs387906986 |
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 30 | Abolishes sumoylation. | ||||
Sequence: K → R | ||||||
Natural variant | VAR_067542 | 366 | in NEDHCS; dbSNP:rs387906986 | |||
Sequence: E → G |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 460 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, cross-link, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000072009 | 1-396 | UniProt | Smad nuclear-interacting protein 1 | |||
Sequence: MKAVKSERERGSRRRHRDGDVVLPAGVVVKQERLSPEVAPPAHRRPDHSGGSPSPPTSEPARSGHRGNRARGVSRSPPKKKNKASGRRSKSPRSKRNRSPHHSTVKVKQEREDHPRRGREDRQHREPSEQEHRRARNSDRDRHRGHSHQRRTSNERPGSGQGQGRDRDTQNLQAQEEEREFYNARRREHRQRNDVGGGGSESQELVPRPGGNNKEKEVPAKEKPSFELSGALLEDTNTFRGVVIKYSEPPEARIPKKRWRLYPFKNDEVLPVMYIHRQSAYLLGRHRRIADIPIDHPSCSKQHAVFQYRLVEYTRADGTVGRRVKPYIIDLGSGNGTFLNNKRIEPQRYYELKEKDVLKFGFSSREYVLLHESSDTSEIDRKDDEDEEEEEEVSDS | |||||||
Cross-link | 30 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate | ||||
Sequence: K | |||||||
Cross-link | 30 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K | |||||||
Cross-link | 30 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 35 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 35 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 49 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 49 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 52 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 52 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 54 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 54 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 57 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 57 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 58 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 58 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 99 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 99 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 108 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 128 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 152 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 153 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 153 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 159 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 202 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 202 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 223 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 377 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 394 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 394 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 396 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Degraded by the proteasome upon binding to the SMAD1/OAZ1/PSMB4 complex.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitous, with highest expression in heart and skeletal muscle.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Component of activated spliceosome complexes (PubMed:29360106).
Component of the minor spliceosome, which splices U12-type introns (PubMed:33509932).
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
Component of the minor spliceosome, which splices U12-type introns (PubMed:33509932).
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
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, coiled coil, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-21 | Basic and acidic residues | ||||
Sequence: MKAVKSERERGSRRRHRDGDV | ||||||
Region | 1-227 | Disordered | ||||
Sequence: MKAVKSERERGSRRRHRDGDVVLPAGVVVKQERLSPEVAPPAHRRPDHSGGSPSPPTSEPARSGHRGNRARGVSRSPPKKKNKASGRRSKSPRSKRNRSPHHSTVKVKQEREDHPRRGREDRQHREPSEQEHRRARNSDRDRHRGHSHQRRTSNERPGSGQGQGRDRDTQNLQAQEEEREFYNARRREHRQRNDVGGGGSESQELVPRPGGNNKEKEVPAKEKPSFE | ||||||
Compositional bias | 68-102 | Basic residues | ||||
Sequence: NRARGVSRSPPKKKNKASGRRSKSPRSKRNRSPHH | ||||||
Compositional bias | 103-138 | Basic and acidic residues | ||||
Sequence: STVKVKQEREDHPRRGREDRQHREPSEQEHRRARNS | ||||||
Compositional bias | 154-169 | Polar residues | ||||
Sequence: NERPGSGQGQGRDRDT | ||||||
Coiled coil | 165-196 | |||||
Sequence: RDRDTQNLQAQEEEREFYNARRREHRQRNDVG | ||||||
Compositional bias | 170-195 | Basic and acidic residues | ||||
Sequence: QNLQAQEEEREFYNARRREHRQRNDV | ||||||
Domain | 281-344 | FHA | ||||
Sequence: YLLGRHRRIADIPIDHPSCSKQHAVFQYRLVEYTRADGTVGRRVKPYIIDLGSGNGTFLNNKRI | ||||||
Region | 373-396 | Disordered | ||||
Sequence: SSDTSEIDRKDDEDEEEEEEVSDS | ||||||
Compositional bias | 379-396 | Acidic residues | ||||
Sequence: IDRKDDEDEEEEEEVSDS |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length396
- Mass (Da)45,778
- Last updated2002-06-01 v1
- ChecksumB183F83EC3184676
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1W2PRA0 | A0A1W2PRA0_HUMAN | SNIP1 | 68 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-21 | Basic and acidic residues | ||||
Sequence: MKAVKSERERGSRRRHRDGDV | ||||||
Compositional bias | 68-102 | Basic residues | ||||
Sequence: NRARGVSRSPPKKKNKASGRRSKSPRSKRNRSPHH | ||||||
Compositional bias | 103-138 | Basic and acidic residues | ||||
Sequence: STVKVKQEREDHPRRGREDRQHREPSEQEHRRARNS | ||||||
Compositional bias | 154-169 | Polar residues | ||||
Sequence: NERPGSGQGQGRDRDT | ||||||
Compositional bias | 170-195 | Basic and acidic residues | ||||
Sequence: QNLQAQEEEREFYNARRREHRQRNDV | ||||||
Sequence conflict | 181 | in Ref. 2; BAB55241 | ||||
Sequence: F → S | ||||||
Sequence conflict | 364 | in Ref. 2; BAB14134 | ||||
Sequence: S → I | ||||||
Compositional bias | 379-396 | Acidic residues | ||||
Sequence: IDRKDDEDEEEEEEVSDS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY081909 EMBL· GenBank· DDBJ | AAL91140.1 EMBL· GenBank· DDBJ | mRNA | ||
AK022615 EMBL· GenBank· DDBJ | BAB14134.1 EMBL· GenBank· DDBJ | mRNA | ||
AK027622 EMBL· GenBank· DDBJ | BAB55241.1 EMBL· GenBank· DDBJ | mRNA | ||
BC027040 EMBL· GenBank· DDBJ | AAH27040.1 EMBL· GenBank· DDBJ | mRNA |