Q08AE8 · SPIR1_HUMAN
- ProteinProtein spire homolog 1
- GeneSPIRE1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids756 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport (PubMed:11747823).
Required for asymmetric spindle positioning and asymmetric cell division during meiosis (PubMed:21620703).
Required for normal formation of the cleavage furrow and for polar body extrusion during female germ cell meiosis (PubMed:21620703).
Also acts in the nucleus: together with FMN2, promotes assembly of nuclear actin filaments in response to DNA damage in order to facilitate movement of chromatin and repair factors after DNA damage (PubMed:26287480).
In addition, promotes innate immune signaling downstream of dsRNA sensing (PubMed:35148361).
Mechanistically, contributes to IRF3 phosphorylation and activation downstream of MAVS and upstream of TBK1 (PubMed:35148361).
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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Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein spire homolog 1
- Short namesSpir-1
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ08AE8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Punctate spots in perinuclear region and cytoplasm, colocalized with Rab11 (By similarity).
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 131 | Strongly reduces interaction with FMN2. | ||||
Sequence: I → K | ||||||
Mutagenesis | 134 | Abolishes interaction with FMN2. | ||||
Sequence: Y → K | ||||||
Mutagenesis | 138 | Abolishes interaction with FMN2. | ||||
Sequence: D → N | ||||||
Mutagenesis | 146 | Abolishes interaction with FMN2. | ||||
Sequence: E → A or K | ||||||
Natural variant | VAR_058695 | 249 | in dbSNP:rs1785296 | |||
Sequence: Q → P |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 732 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 initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000309569 | 2-756 | UniProt | Protein spire homolog 1 | |||
Sequence: AQAAGPAGGGEPRTEAVGGEGPREPGAAGGAAGGSRDALSLEEILRLYNQPINEEQAWAVCYQCCGSLRAAARRRQPRHRVRSAAQIRVWRDGAVTLAPAADDAGEPPPVAGKLGYSQCMETEVIESLGIIIYKALDYGLKENEERELSPPLEQLIDHMANTVEADGSNDEGYEAAEEGLGDEDEKRKISAIRSYRDVMKLCAAHLPTESDAPNHYQAVCRALFAETMELHTFLTKIKSAKENLKKIQEMEKSDESSTDLEELKNADWARFWVQVMRDLRNGVKLKKVQERQYNPLPIEYQLTPYEMLMDDIRCKRYTLRKVMVNGDIPPRLKKSAHEIILDFIRSRPPLNPVSARKLKPTPPRPRSLHERILEEIKAERKLRPVSPEEIRRSRLAMRPLSMSYSFDLSDVTTPESTKNLVESSMVNGGLTSQTKENGLSTSQQVPAQRKKLLRAPTLAELDSSESEEETLHKSTSSSSVSPSFPEEPVLEAVSTRKKPPKFLPISSTPQPERRQPPQRRHSIEKETPTNVRQFLPPSRQSSRSLEEFCYPVECLALTVEEVMHIRQVLVKAELEKYQQYKDIYTALKKGKLCFCCRTRRFSFFTWSYTCQFCKRPVCSQCCKKMRLPSKPYSTLPIFSLGPSALQRGESSMRSEKPSTAHHRPLRSIARFSSKSKSMDKSDEELQFPKELMEDWSTMEVCVDCKKFISEIISSSRRSLVLANKRARLKRKTQSFYMSSPGPSEYCPSERTISEI | |||||||
Modified residue (large scale data) | 169 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 174 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 257 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 387 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 387 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 406 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 433 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 464 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 464 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 465 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 465 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 467 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 467 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 471 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 477 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 508 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 509 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 509 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 523 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 678 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 678 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 682 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 682 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 735 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 735 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 740 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q08AE8 | ATP1A3 P13637 | 3 | EBI-1055655, EBI-948169 | |
BINARY | Q08AE8 | BBS4 Q96RK4 | 3 | EBI-1055655, EBI-1805814 | |
BINARY | Q08AE8 | PECAM1 P16284 | 3 | EBI-1055655, EBI-716404 | |
BINARY | Q08AE8 | PLD1 Q13393 | 3 | EBI-1055655, EBI-2827556 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, coiled coil, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-35 | Disordered | ||||
Sequence: MAQAAGPAGGGEPRTEAVGGEGPREPGAAGGAAGG | ||||||
Domain | 40-231 | KIND | ||||
Sequence: LSLEEILRLYNQPINEEQAWAVCYQCCGSLRAAARRRQPRHRVRSAAQIRVWRDGAVTLAPAADDAGEPPPVAGKLGYSQCMETEVIESLGIIIYKALDYGLKENEERELSPPLEQLIDHMANTVEADGSNDEGYEAAEEGLGDEDEKRKISAIRSYRDVMKLCAAHLPTESDAPNHYQAVCRALFAETMEL | ||||||
Region | 131-138 | Important for interaction with FMN2 | ||||
Sequence: IIIYKALD | ||||||
Coiled coil | 229-257 | |||||
Sequence: MELHTFLTKIKSAKENLKKIQEMEKSDES | ||||||
Domain | 305-323 | WH2 1 | ||||
Sequence: PYEMLMDDIRCKRYTLRKV | ||||||
Domain | 369-386 | WH2 2 | ||||
Sequence: LHERILEEIKAERKLRPV | ||||||
Compositional bias | 425-449 | Polar residues | ||||
Sequence: SMVNGGLTSQTKENGLSTSQQVPAQ | ||||||
Region | 425-538 | Disordered | ||||
Sequence: SMVNGGLTSQTKENGLSTSQQVPAQRKKLLRAPTLAELDSSESEEETLHKSTSSSSVSPSFPEEPVLEAVSTRKKPPKFLPISSTPQPERRQPPQRRHSIEKETPTNVRQFLPP | ||||||
Region | 556-576 | Spir-box | ||||
Sequence: LALTVEEVMHIRQVLVKAELE |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative splicing.
Q08AE8-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length756
- Mass (Da)85,544
- Last updated2012-11-28 v3
- Checksum1379B39C8CA9DDB3
Q08AE8-5
- Name5
Q08AE8-2
- Name2
- Differences from canonical
- 397-410: Missing
Q08AE8-3
- Name3
Q08AE8-4
- Name4
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_054464 | 1-120 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_037925 | 1-159 | in isoform 3 and isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_052595 | 397-410 | in isoform 2, isoform 3, isoform 4 and isoform 5 | |||
Sequence: Missing | ||||||
Compositional bias | 425-449 | Polar residues | ||||
Sequence: SMVNGGLTSQTKENGLSTSQQVPAQ | ||||||
Alternative sequence | VSP_037926 | 616-756 | in isoform 4 | |||
Sequence: RPVCSQCCKKMRLPSKPYSTLPIFSLGPSALQRGESSMRSEKPSTAHHRPLRSIARFSSKSKSMDKSDEELQFPKELMEDWSTMEVCVDCKKFISEIISSSRRSLVLANKRARLKRKTQSFYMSSPGPSEYCPSERTISEI → SDCLFNGTAHCQFYLG |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB032961 EMBL· GenBank· DDBJ | BAA86449.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK290180 EMBL· GenBank· DDBJ | BAF82869.1 EMBL· GenBank· DDBJ | mRNA | ||
AL833817 EMBL· GenBank· DDBJ | CAD38680.1 EMBL· GenBank· DDBJ | mRNA | ||
AP001028 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AP001029 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AP005482 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471113 EMBL· GenBank· DDBJ | EAX01546.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC115005 EMBL· GenBank· DDBJ | AAI15006.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC125206 EMBL· GenBank· DDBJ | AAI25207.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC125207 EMBL· GenBank· DDBJ | AAI25208.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AJ277587 EMBL· GenBank· DDBJ | CAB96370.1 EMBL· GenBank· DDBJ | mRNA |