Q08AE8 · SPIR1_HUMAN

  • Protein
    Protein spire homolog 1
  • Gene
    SPIRE1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Acts as an actin nucleation factor, remains associated with the slow-growing pointed end of the new filament (PubMed:11747823, PubMed:21620703).
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 annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcell cortex
Cellular Componentcytoplasmic vesicle membrane
Cellular Componentcytoskeleton
Cellular Componentcytosol
Cellular Componentmitochondrial outer membrane
Cellular Componentnucleoplasm
Cellular Componentperinuclear region of cytoplasm
Cellular Componentplasma membrane
Molecular Functionactin binding
Molecular Functionmicrotubule binding
Biological Processactin cytoskeleton organization
Biological Processactin filament network formation
Biological Processactin filament polymerization
Biological Processactin nucleation
Biological Processcleavage furrow formation
Biological Processestablishment of meiotic spindle localization
Biological Processformin-nucleated actin cable assembly
Biological ProcessGolgi vesicle transport
Biological Processinnate immune response
Biological Processintracellular transport
Biological Processpolar body extrusion after meiotic divisions
Biological Processpositive regulation of double-strand break repair
Biological Processpositive regulation of mitochondrial fission
Biological Processprotein transport
Biological Processvesicle-mediated transport

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein spire homolog 1
  • Short names
    Spir-1

Gene names

    • Name
      SPIRE1
    • Synonyms
      KIAA1135, SPIR1

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q08AE8
  • Secondary accessions
    • A8K2B5
    • J3KQ50
    • J3KQR5
    • Q1RMD4
    • Q8NDP1

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Peripheral membrane protein
Cytoplasmic vesicle membrane
; Peripheral membrane protein
Note: Detected at the cleavage furrow during asymmetric oocyte division and polar body extrusion (By similarity).
Punctate spots in perinuclear region and cytoplasm, colocalized with Rab11 (By similarity).

Keywords

Disease & Variants

Features

Showing features for mutagenesis, natural variant.

TypeIDPosition(s)Description
Mutagenesis131Strongly reduces interaction with FMN2.
Mutagenesis134Abolishes interaction with FMN2.
Mutagenesis138Abolishes interaction with FMN2.
Mutagenesis146Abolishes interaction with FMN2.
Natural variantVAR_058695249in dbSNP:rs1785296

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.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
Initiator methionine1UniProtRemoved
Modified residue2UniProtN-acetylalanine
ChainPRO_00003095692-756UniProtProtein spire homolog 1
Modified residue (large scale data)169PRIDEPhosphoserine
Modified residue (large scale data)174PRIDEPhosphotyrosine
Modified residue (large scale data)257PRIDEPhosphoserine
Modified residue387UniProtPhosphoserine
Modified residue (large scale data)387PRIDEPhosphoserine
Modified residue406UniProtPhosphoserine
Modified residue (large scale data)433PRIDEPhosphoserine
Modified residue464UniProtPhosphoserine
Modified residue (large scale data)464PRIDEPhosphoserine
Modified residue465UniProtPhosphoserine
Modified residue (large scale data)465PRIDEPhosphoserine
Modified residue467UniProtPhosphoserine
Modified residue (large scale data)467PRIDEPhosphoserine
Modified residue (large scale data)471PRIDEPhosphothreonine
Modified residue (large scale data)477PRIDEPhosphoserine
Modified residue (large scale data)508PRIDEPhosphoserine
Modified residue509UniProtPhosphothreonine
Modified residue (large scale data)509PRIDEPhosphothreonine
Modified residue (large scale data)523PRIDEPhosphoserine
Modified residue678UniProtPhosphoserine
Modified residue (large scale data)678PRIDEPhosphoserine
Modified residue682UniProtPhosphoserine
Modified residue (large scale data)682PRIDEPhosphoserine
Modified residue735UniProtPhosphoserine
Modified residue (large scale data)735PRIDEPhosphoserine
Modified residue (large scale data)740PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with FMN2.
(Microbial infection) Interacts (via C-terminus) with vaccinia virus protein K7/OPG41; this interaction prevents innate immune signaling activation.

Binary interactions

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, domain, coiled coil, compositional bias.

TypeIDPosition(s)Description
Region1-35Disordered
Domain40-231KIND
Region131-138Important for interaction with FMN2
Coiled coil229-257
Domain305-323WH2 1
Domain369-386WH2 2
Compositional bias425-449Polar residues
Region425-538Disordered
Region556-576Spir-box

Domain

Binds to actin monomers via the WH2 domain.
The Spir-box targets binding to intracellular membrane structures.

Sequence similarities

Belongs to the spire family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (5)
  • Sequence status
    Complete

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.

  • Length
    756
  • Mass (Da)
    85,544
  • Last updated
    2012-11-28 v3
  • Checksum
    1379B39C8CA9DDB3
MAQAAGPAGGGEPRTEAVGGEGPREPGAAGGAAGGSRDALSLEEILRLYNQPINEEQAWAVCYQCCGSLRAAARRRQPRHRVRSAAQIRVWRDGAVTLAPAADDAGEPPPVAGKLGYSQCMETEVIESLGIIIYKALDYGLKENEERELSPPLEQLIDHMANTVEADGSNDEGYEAAEEGLGDEDEKRKISAIRSYRDVMKLCAAHLPTESDAPNHYQAVCRALFAETMELHTFLTKIKSAKENLKKIQEMEKSDESSTDLEELKNADWARFWVQVMRDLRNGVKLKKVQERQYNPLPIEYQLTPYEMLMDDIRCKRYTLRKVMVNGDIPPRLKKSAHEIILDFIRSRPPLNPVSARKLKPTPPRPRSLHERILEEIKAERKLRPVSPEEIRRSRLAMRPLSMSYSFDLSDVTTPESTKNLVESSMVNGGLTSQTKENGLSTSQQVPAQRKKLLRAPTLAELDSSESEEETLHKSTSSSSVSPSFPEEPVLEAVSTRKKPPKFLPISSTPQPERRQPPQRRHSIEKETPTNVRQFLPPSRQSSRSLEEFCYPVECLALTVEEVMHIRQVLVKAELEKYQQYKDIYTALKKGKLCFCCRTRRFSFFTWSYTCQFCKRPVCSQCCKKMRLPSKPYSTLPIFSLGPSALQRGESSMRSEKPSTAHHRPLRSIARFSSKSKSMDKSDEELQFPKELMEDWSTMEVCVDCKKFISEIISSSRRSLVLANKRARLKRKTQSFYMSSPGPSEYCPSERTISEI

Q08AE8-5

Q08AE8-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q08AE8-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q08AE8-4

  • Name
    4
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-159: Missing
    • 397-410: Missing
    • 616-756: RPVCSQCCKKMRLPSKPYSTLPIFSLGPSALQRGESSMRSEKPSTAHHRPLRSIARFSSKSKSMDKSDEELQFPKELMEDWSTMEVCVDCKKFISEIISSSRRSLVLANKRARLKRKTQSFYMSSPGPSEYCPSERTISEI → SDCLFNGTAHCQFYLG

Computationally mapped potential isoform sequences

There are 5 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
J3KNG6J3KNG6_HUMANSPIRE1545
C9JYR7C9JYR7_HUMANSPIRE1197
K7EMJ7K7EMJ7_HUMANSPIRE1122
K7ENV1K7ENV1_HUMANSPIRE1147
K7EQR2K7EQR2_HUMANSPIRE1122

Sequence caution

The sequence AAI15006.1 differs from that shown. Reason: Erroneous initiation
The sequence AAI25207.1 differs from that shown. Reason: Erroneous initiation
The sequence AAI25208.1 differs from that shown. Reason: Erroneous initiation
The sequence BAA86449.2 differs from that shown. Reason: Erroneous initiation

Features

Showing features for alternative sequence, compositional bias.

TypeIDPosition(s)Description
Alternative sequenceVSP_0544641-120in isoform 5
Alternative sequenceVSP_0379251-159in isoform 3 and isoform 4
Alternative sequenceVSP_052595397-410in isoform 2, isoform 3, isoform 4 and isoform 5
Compositional bias425-449Polar residues
Alternative sequenceVSP_037926616-756in isoform 4

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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