F1N4E5 · TOIP1_BOVIN
- ProteinTorsin-1A-interacting protein 1
- GeneTOR1AIP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids600 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Required for nuclear membrane integrity. Induces TOR1A and TOR1B ATPase activity and is required for their location on the nuclear membrane. Binds to A- and B-type lamins. Possible role in membrane attachment and assembly of the nuclear lamina (By similarity).
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 | nuclear inner membrane | |
Cellular Component | nuclear membrane | |
Cellular Component | nucleus | |
Molecular Function | ATPase activator activity | |
Biological Process | nuclear membrane organization | |
Biological Process | positive regulation of ATP-dependent activity | |
Biological Process | protein localization to nucleus |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTorsin-1A-interacting protein 1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionF1N4E5
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Nucleus inner membrane ; Single-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-354 | Nuclear | ||||
Sequence: MAGEGQRAEPEREGWALYVTPRAPLREGRPRLAPQNGGSGDVPAYGTPTPSRHGRREVRFSEEPPEVYGDFEPRAAKEKARVGRQIPLEGFRPDSAKEEVRESAYYLRSRQRRQPRLHEAEEMQTRRAALLQQQPHSPPPPLRPSPVTTRRGLRDSHSSEEDEPPSQTVLSQTVTKKAIRRTQETPVMSEDPLISLRRPPLRSSRSEAASVQQKVNFLEEGETEENDQDSFDSDVTVKVRSGDSVESGDQTTRSSSQYKESFWQSSQSGDFTAFDEQPLKLSSGYQKTPQEWAEKTVRIRTRMLTSSPGMRSIYGSFSDDDSVQKSELGNQSPSTSNQQMTGQPKSVSSVKTKR | ||||||
Transmembrane | 355-371 | Helical | ||||
Sequence: YWPFAVIAALLIGGFLY | ||||||
Topological domain | 372-600 | Perinuclear space | ||||
Sequence: TRPPEAETTAVQEFQNQMKQLMNKYQGQDEKLWKRSQTFLEKHLNGSQSRPQPAILLLTAARDAEEALRCLSEQIADAYSSFRSVPAIRIDGASKATRDSDTVKEEVDQELSNGFRNGQNAAVVHRFESLPAGSTLIFYKYCDHESAAFKDVALVLTVLLEEETLGTSLGLKEIEEKVRDFLQVKFTNSDTPNSYKHMDPDKLSGLWSRISHLVLPVQPENDLKKGICL |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue, cross-link, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000417025 | 1-600 | Torsin-1A-interacting protein 1 | |||
Sequence: MAGEGQRAEPEREGWALYVTPRAPLREGRPRLAPQNGGSGDVPAYGTPTPSRHGRREVRFSEEPPEVYGDFEPRAAKEKARVGRQIPLEGFRPDSAKEEVRESAYYLRSRQRRQPRLHEAEEMQTRRAALLQQQPHSPPPPLRPSPVTTRRGLRDSHSSEEDEPPSQTVLSQTVTKKAIRRTQETPVMSEDPLISLRRPPLRSSRSEAASVQQKVNFLEEGETEENDQDSFDSDVTVKVRSGDSVESGDQTTRSSSQYKESFWQSSQSGDFTAFDEQPLKLSSGYQKTPQEWAEKTVRIRTRMLTSSPGMRSIYGSFSDDDSVQKSELGNQSPSTSNQQMTGQPKSVSSVKTKRYWPFAVIAALLIGGFLYTRPPEAETTAVQEFQNQMKQLMNKYQGQDEKLWKRSQTFLEKHLNGSQSRPQPAILLLTAARDAEEALRCLSEQIADAYSSFRSVPAIRIDGASKATRDSDTVKEEVDQELSNGFRNGQNAAVVHRFESLPAGSTLIFYKYCDHESAAFKDVALVLTVLLEEETLGTSLGLKEIEEKVRDFLQVKFTNSDTPNSYKHMDPDKLSGLWSRISHLVLPVQPENDLKKGICL | ||||||
Modified residue | 61 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 137 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 145 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 156 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 158 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 159 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 189 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 223 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 230 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 233 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 244 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 322 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 325 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 332 | Phosphoserine | ||||
Sequence: S | ||||||
Glycosylation | 416 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Interacts with ATP1B4. Interacts with TOR1A (ATP-bound). Interacts with TOR1B, TOR2A and TOR3A. Interacts with VIM (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-261 | Disordered | ||||
Sequence: MAGEGQRAEPEREGWALYVTPRAPLREGRPRLAPQNGGSGDVPAYGTPTPSRHGRREVRFSEEPPEVYGDFEPRAAKEKARVGRQIPLEGFRPDSAKEEVRESAYYLRSRQRRQPRLHEAEEMQTRRAALLQQQPHSPPPPLRPSPVTTRRGLRDSHSSEEDEPPSQTVLSQTVTKKAIRRTQETPVMSEDPLISLRRPPLRSSRSEAASVQQKVNFLEEGETEENDQDSFDSDVTVKVRSGDSVESGDQTTRSSSQYKES | ||||||
Compositional bias | 52-125 | Basic and acidic residues | ||||
Sequence: RHGRREVRFSEEPPEVYGDFEPRAAKEKARVGRQIPLEGFRPDSAKEEVRESAYYLRSRQRRQPRLHEAEEMQT | ||||||
Compositional bias | 163-182 | Polar residues | ||||
Sequence: EPPSQTVLSQTVTKKAIRRT | ||||||
Compositional bias | 243-261 | Polar residues | ||||
Sequence: DSVESGDQTTRSSSQYKES | ||||||
Region | 310-346 | Disordered | ||||
Sequence: MRSIYGSFSDDDSVQKSELGNQSPSTSNQQMTGQPKS | ||||||
Region | 373-600 | Interaction with TOR1A | ||||
Sequence: RPPEAETTAVQEFQNQMKQLMNKYQGQDEKLWKRSQTFLEKHLNGSQSRPQPAILLLTAARDAEEALRCLSEQIADAYSSFRSVPAIRIDGASKATRDSDTVKEEVDQELSNGFRNGQNAAVVHRFESLPAGSTLIFYKYCDHESAAFKDVALVLTVLLEEETLGTSLGLKEIEEKVRDFLQVKFTNSDTPNSYKHMDPDKLSGLWSRISHLVLPVQPENDLKKGICL | ||||||
Coiled coil | 376-452 | |||||
Sequence: EAETTAVQEFQNQMKQLMNKYQGQDEKLWKRSQTFLEKHLNGSQSRPQPAILLLTAARDAEEALRCLSEQIADAYSS |
Sequence similarities
Belongs to the TOR1AIP family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length600
- Mass (Da)67,468
- Last updated2011-11-16 v2
- Checksum0BDC048C3B12CD28
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A3Q1MJM3 | A0A3Q1MJM3_BOVIN | TOR1AIP1 | 600 | ||
A0A3Q1LTR8 | A0A3Q1LTR8_BOVIN | TOR1AIP1 | 615 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 52-125 | Basic and acidic residues | ||||
Sequence: RHGRREVRFSEEPPEVYGDFEPRAAKEKARVGRQIPLEGFRPDSAKEEVRESAYYLRSRQRRQPRLHEAEEMQT | ||||||
Compositional bias | 163-182 | Polar residues | ||||
Sequence: EPPSQTVLSQTVTKKAIRRT | ||||||
Compositional bias | 243-261 | Polar residues | ||||
Sequence: DSVESGDQTTRSSSQYKES |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DAAA02043477 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |