Q9Y6Y0 · NS1BP_HUMAN
- ProteinInfluenza virus NS1A-binding protein
- GeneIVNS1ABP
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids642 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in many cell functions, including pre-mRNA splicing, the aryl hydrocarbon receptor (AHR) pathway, F-actin organization and protein ubiquitination. Plays a role in the dynamic organization of the actin skeleton as a stabilizer of actin filaments by association with F-actin through Kelch repeats (By similarity).
Protects cells from cell death induced by actin destabilization (By similarity).
Functions as modifier of the AHR/Aryl hydrocarbon receptor pathway increasing the concentration of AHR available to activate transcription (PubMed:16582008).
In addition, functions as a negative regulator of BCR(KLHL20) E3 ubiquitin ligase complex to prevent ubiquitin-mediated proteolysis of PML and DAPK1, two tumor suppressors (PubMed:25619834).
Inhibits pre-mRNA splicing (in vitro) (PubMed:9696811).
May play a role in mRNA nuclear export (PubMed:30538201).
Protects cells from cell death induced by actin destabilization (By similarity).
Functions as modifier of the AHR/Aryl hydrocarbon receptor pathway increasing the concentration of AHR available to activate transcription (PubMed:16582008).
In addition, functions as a negative regulator of BCR(KLHL20) E3 ubiquitin ligase complex to prevent ubiquitin-mediated proteolysis of PML and DAPK1, two tumor suppressors (PubMed:25619834).
Inhibits pre-mRNA splicing (in vitro) (PubMed:9696811).
May play a role in mRNA nuclear export (PubMed:30538201).
(Microbial infection) Involved in the alternative splicing of influenza A virus M1 mRNA through interaction with HNRNPK, thereby facilitating the generation of viral M2 protein (PubMed:23825951, PubMed:9696811).
The BTB and Kelch domains are required for splicing activity (PubMed:30538201).
Promotes export of viral M mRNA and RNP via its interaction with mRNA export factor ALYREF (PubMed:30538201).
The BTB and Kelch domains are required for splicing activity (PubMed:30538201).
Promotes export of viral M mRNA and RNP via its interaction with mRNA export factor ALYREF (PubMed:30538201).
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 | cytoskeleton | |
Cellular Component | cytosol | |
Cellular Component | nucleoplasm | |
Cellular Component | spliceosomal complex | |
Cellular Component | transcription regulator complex | |
Biological Process | intrinsic apoptotic signaling pathway | |
Biological Process | mRNA processing | |
Biological Process | negative regulation of intrinsic apoptotic signaling pathway | |
Biological Process | negative regulation of protein ubiquitination | |
Biological Process | response to virus | |
Biological Process | RNA splicing | |
Biological Process | transcription by RNA polymerase III |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameInfluenza virus NS1A-binding protein
- Short namesNS1-BP; NS1-binding protein
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9Y6Y0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Associated with actin filaments (By similarity).
Localization related to speckle domains which correspond to interchromatin granules and are enriched in factors involved in pre-mRNA splicing (PubMed:9696811).
Following influenza A virus infection, redistribution from speckles to a more diffuse distribution in the nucleoplasm (PubMed:9696811).
Localization related to speckle domains which correspond to interchromatin granules and are enriched in factors involved in pre-mRNA splicing (PubMed:9696811).
Following influenza A virus infection, redistribution from speckles to a more diffuse distribution in the nucleoplasm (PubMed:9696811).
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Immunodeficiency 70 (IMD70)
- Note
- DescriptionA primary immunodeficiency clinically characterized by human papillomavirus-associated warts on the hands, feet and face, recurrent bacterial infections, and autoinflammatory features, such as colitis, celiac disease, and retinal vasculitis. Immunologic workup shows decreased CD4+ T cells, decreased CD19+ B cells, and hypogammaglobulinemia. IMD70 inheritance is autosomal dominant with incomplete penetrance.
- See alsoMIM:618969
Natural variants in IMD70
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_084531 | 358-642 | missing | in IMD70; uncertain significance; strong decrease in protein expression | |
VAR_084532 | 633-642 | missing | in IMD70; uncertain significance; strong decrease in protein expression |
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 1-12 | Destabilises dimer and impairs splicing of viral M1 mRNA. | ||||
Sequence: Missing | ||||||
Mutagenesis | 198 | Significant inhibition of interaction with AHR; partial decrease of AHR signaling induced by IVNS1ABP. | ||||
Sequence: V → M | ||||||
Mutagenesis | 288 | Significant inhibition of interaction with AHR; partial decrease of AHR signaling induced by IVNS1ABP. | ||||
Sequence: E → K | ||||||
Natural variant | VAR_084531 | 358-642 | in IMD70; uncertain significance; strong decrease in protein expression | |||
Sequence: Missing | ||||||
Natural variant | VAR_084532 | 633-642 | in IMD70; uncertain significance; strong decrease in protein expression | |||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 493 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000285077 | 1-642 | UniProt | Influenza virus NS1A-binding protein | |||
Sequence: MIPNGYLMFEDENFIESSVAKLNALRKSGQFCDVRLQVCGHEMLAHRAVLACCSPYLFEIFNSDSDPHGISHVKFDDLNPEAVEVLLNYAYTAQLKADKELVKDVYSAAKKLKMDRVKQVCGDYLLSRMDVTSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKLEVMLEDNVCLPSNGKLYTKVINWVQRSIWENGDSLEELMEEVQTLYYSADHKLLDGNLLDGQAEVFGSDDDHIQFVQKKPPRENGHKQISSSSTGCLSSPNATVQSPKHEWKIVASEKTSNNTYLCLAVLDGIFCVIFLHGRNSPQSSPTSTPKLSKSLSFEMQQDELIEKPMSPMQYARSGLGTAEMNGKLIAAGGYNREECLRTVECYNPHTDHWSFLAPMRTPRARFQMAVLMGQLYVVGGSNGHSDDLSCGEMYDSNIDDWIPVPELRTNRCNAGVCALNGKLYIVGGSDPYGQKGLKNCDVFDPVTKLWTSCAPLNIRRHQSAVCELGGYLYIIGGAESWNCLNTVERYNPENNTWTLIAPMNVARRGAGVAVLNGKLFVCGGFDGSHAISCVEMYDPTRNEWKMMGNMTSPRSNAGIATVGNTIYAVGGFDGNEFLNTVEVYNLESNEWSPYTKIFQF | |||||||
Modified residue (large scale data) | 28 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 246 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 246 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 268 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 269 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 276 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 277 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 277 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 284 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 322 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 322 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 326 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 336 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 336 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 338 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 338 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 352 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Homodimer; through the BTB domain (PubMed:30538201).
Interacts with AHR/Aryl hydrocarbon receptor (PubMed:16582008).
Interacts (via BACK domain) with pre-mRNA-binding protein HNRNPK; the interaction is direct (PubMed:23825951, PubMed:30538201).
Interacts (via BACK domain) with splicing factor PTBP1; the interaction is direct (PubMed:30538201).
Interacts (via Kelch repeats) with RNA polymerase POLR2A (via C-terminal domain) (PubMed:30538201).
Interacts (via BACK domain) with splicing factor SNRPA; the interaction is indirect (PubMed:30538201).
Interacts (via Kelch repeats) with splicing factor SART1 (PubMed:30538201).
Interacts (via BACK domain) with ALYREF; the interaction is indirect and likely plays a role in mRNA nuclear export (PubMed:30538201).
Interacts (via Kelch repeats) with KLHL20 (via Kelch repeats); this interaction blocks the assembly of Cul3-KLHL20 complex (PubMed:25619834).
Interacts with AHR/Aryl hydrocarbon receptor (PubMed:16582008).
Interacts (via BACK domain) with pre-mRNA-binding protein HNRNPK; the interaction is direct (PubMed:23825951, PubMed:30538201).
Interacts (via BACK domain) with splicing factor PTBP1; the interaction is direct (PubMed:30538201).
Interacts (via Kelch repeats) with RNA polymerase POLR2A (via C-terminal domain) (PubMed:30538201).
Interacts (via BACK domain) with splicing factor SNRPA; the interaction is indirect (PubMed:30538201).
Interacts (via Kelch repeats) with splicing factor SART1 (PubMed:30538201).
Interacts (via BACK domain) with ALYREF; the interaction is indirect and likely plays a role in mRNA nuclear export (PubMed:30538201).
Interacts (via Kelch repeats) with KLHL20 (via Kelch repeats); this interaction blocks the assembly of Cul3-KLHL20 complex (PubMed:25619834).
(Microbial infection) Interacts (via BACK domain) with influenza A virus non-structural protein 1 (NS1); the interaction is direct and bridges the interaction between NS1 and HNRNPK.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9Y6Y0 | CUL3 Q13618 | 2 | EBI-715774, EBI-456129 | |
BINARY | Q9Y6Y0 | KLHL20 Q9Y2M5 | 9 | EBI-715774, EBI-714379 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-131 | BTB | ||||
Sequence: MIPNGYLMFEDENFIESSVAKLNALRKSGQFCDVRLQVCGHEMLAHRAVLACCSPYLFEIFNSDSDPHGISHVKFDDLNPEAVEVLLNYAYTAQLKADKELVKDVYSAAKKLKMDRVKQVCGDYLLSRMDV | ||||||
Domain | 132-350 | BACK | ||||
Sequence: TSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKLEVMLEDNVCLPSNGKLYTKVINWVQRSIWENGDSLEELMEEVQTLYYSADHKLLDGNLLDGQAEVFGSDDDHIQFVQKKPPRENGHKQISSSSTGCLSSPNATVQSPKHEWKIVASEKTSNNTYLCLAVLDGIFCVIFLHGRNSPQSSPTSTPKLSKSLSFEMQQDELIEKP | ||||||
Region | 164-368 | Sufficient for AHR interaction and signaling | ||||
Sequence: ISEEEEFLKLPRLKLEVMLEDNVCLPSNGKLYTKVINWVQRSIWENGDSLEELMEEVQTLYYSADHKLLDGNLLDGQAEVFGSDDDHIQFVQKKPPRENGHKQISSSSTGCLSSPNATVQSPKHEWKIVASEKTSNNTYLCLAVLDGIFCVIFLHGRNSPQSSPTSTPKLSKSLSFEMQQDELIEKPMSPMQYARSGLGTAEMNG | ||||||
Region | 257-281 | Disordered | ||||
Sequence: KPPRENGHKQISSSSTGCLSSPNAT | ||||||
Compositional bias | 264-281 | Polar residues | ||||
Sequence: HKQISSSSTGCLSSPNAT | ||||||
Repeat | 384-421 | Kelch 1 | ||||
Sequence: TVECYNPHTDHWSFLAPMRTPRARFQMAVLMGQLYVVG | ||||||
Repeat | 432-469 | Kelch 2 | ||||
Sequence: CGEMYDSNIDDWIPVPELRTNRCNAGVCALNGKLYIVG | ||||||
Repeat | 481-518 | Kelch 3 | ||||
Sequence: NCDVFDPVTKLWTSCAPLNIRRHQSAVCELGGYLYIIG | ||||||
Repeat | 527-565 | Kelch 4 | ||||
Sequence: NTVERYNPENNTWTLIAPMNVARRGAGVAVLNGKLFVCG | ||||||
Repeat | 575-612 | Kelch 5 | ||||
Sequence: CVEMYDPTRNEWKMMGNMTSPRSNAGIATVGNTIYAVG | ||||||
Repeat | 622-642 | Kelch 6 | ||||
Sequence: TVEVYNLESNEWSPYTKIFQF |
Domain
When the BTB domain is lacking, AHR signaling induction promoted by IVNS1ABP is massively increased; Thus, the BTB domain inhibits AHR signaling induced by IVNS1ABP (PubMed:16582008).
Dimerization is necessary for proper splicing activity of IVNS1ABP and this is mediated by the BTB domain (PubMed:30538201).
The BACK domain is necessary for proper viral M mRNA export (PubMed:30538201).
Dimerization is necessary for proper splicing activity of IVNS1ABP and this is mediated by the BTB domain (PubMed:30538201).
The BACK domain is necessary for proper viral M mRNA export (PubMed:30538201).
Sequence similarities
Belongs to the BTB-kelch protein family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length642
- Mass (Da)71,729
- Last updated2007-05-01 v3
- Checksum456E30DC4E351CCD
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 111 | in Ref. 1; CAA10029 | ||||
Sequence: K → E | ||||||
Sequence conflict | 148 | in Ref. 1; CAA10029 | ||||
Sequence: R → H | ||||||
Sequence conflict | 218 | in Ref. 10; AAH67739 | ||||
Sequence: E → G | ||||||
Compositional bias | 264-281 | Polar residues | ||||
Sequence: HKQISSSSTGCLSSPNAT | ||||||
Sequence conflict | 579 | in Ref. 2; ABE03889/ABE03890 | ||||
Sequence: Y → H | ||||||
Sequence conflict | 591 | in Ref. 1; CAA10029 | ||||
Sequence: N → H | ||||||
Sequence conflict | 623 | in Ref. 1; CAA10029 | ||||
Sequence: V → A |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ012449 EMBL· GenBank· DDBJ | CAA10029.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
DQ443528 EMBL· GenBank· DDBJ | ABE03889.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ443529 EMBL· GenBank· DDBJ | ABE03890.1 EMBL· GenBank· DDBJ | mRNA | ||
AF205218 EMBL· GenBank· DDBJ | AAG43485.1 EMBL· GenBank· DDBJ | mRNA | ||
AB020657 EMBL· GenBank· DDBJ | BAA74873.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AF161553 EMBL· GenBank· DDBJ | AAF29040.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AL078644 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL356273 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AK292431 EMBL· GenBank· DDBJ | BAF85120.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471067 EMBL· GenBank· DDBJ | EAW91194.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC067739 EMBL· GenBank· DDBJ | AAH67739.1 EMBL· GenBank· DDBJ | mRNA |