Q8VC66 · ADIP_MOUSE

  • Protein
    Afadin- and alpha-actinin-binding protein
  • Gene
    Ssx2ip
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Belongs to an adhesion system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs). May connect the nectin-afadin and E-cadherin-catenin system through alpha-actinin and may be involved in organization of the actin cytoskeleton at AJs through afadin and alpha-actinin (PubMed:12446711).
Acts as a centrosome maturation factor, probably by maintaining the integrity of the pericentriolar material and proper microtubule nucleation at mitotic spindle poles. The function seems to implicate at least in part WRAP73; the SSX2IP:WRAP73 complex is proposed to act as regulator of spindle anchoring at the mitotic centrosome (By similarity).
Involved in cell movement: localizes at the leading edge of moving cells in response to PDGF and is required for the formation of the leading edge and the promotion of cell movement, possibly via activation of Rac signaling (PubMed:22027834).
Involved in ciliogenesis (By similarity).
It is required for targeted recruitment of the BBSome, CEP290, RAB8, and SSTR3 to the cilia (By similarity).

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 Componentadherens junction
Cellular Componentcell leading edge
Cellular Componentcentriolar satellite
Cellular Componentciliary basal body
Cellular Componentcytoplasm
Cellular Componentnucleus
Cellular Componentprotein-containing complex
Molecular Functionprotein domain specific binding
Biological Processcell adhesion
Biological Processcentrosome cycle
Biological Processcilium assembly
Biological Processintraciliary transport involved in cilium assembly
Biological Processregulation of cell motility
Biological Processregulation of Rac protein signal transduction

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Afadin- and alpha-actinin-binding protein
  • Short names
    ADIP
  • Alternative names
    • Afadin DIL domain-interacting protein

Gene names

    • Name
      Ssx2ip

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • FVB/N
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q8VC66
  • Secondary accessions
    • Q8BG59
    • Q8C7X0
    • Q8K2F7

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000644561-615Afadin- and alpha-actinin-binding protein
Modified residue290Phosphoserine
Modified residue293Phosphoserine
Modified residue313Phosphoserine
Modified residue319Phosphoserine
Modified residue537Phosphoserine
Modified residue541Phosphoserine
Modified residue543Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Widely expressed.

Gene expression databases

Interaction

Subunit

Interacts with SSX2 and SSX3 (By similarity).
Does not interact with SSX1 and SSX4 (By similarity).
Interacts with afadin and alpha-actinin (PubMed:12446711).
Interacts with VAV2 (PubMed:22027834).
Interacts with PCM1 (PubMed:24356449).
Interacts with WRAP73 (By similarity).

Binary interactions

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for coiled coil, compositional bias, region.

TypeIDPosition(s)Description
Coiled coil126-227
Coiled coil266-293
Compositional bias293-307Basic and acidic residues
Region293-316Disordered
Coiled coil375-461
Region567-615Disordered
Compositional bias579-599Polar residues

Sequence similarities

Belongs to the ADIP family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    615
  • Mass (Da)
    70,956
  • Last updated
    2002-03-01 v1
  • Checksum
    CC41D7078591919F
MGDWMTVTDPVLCTENKNLSQYTSETKMSPSSLYSQQVLCSSVPLSKNVHGVFGVFCTGENIEQSISYLDQELTTFGFPSLYEESKSKEAKRELNIVAVLNCMNELLVLQRKNLLAQESVETQNLKLGSDMDHLQSCYAKLKEQLETSRREMIGLQERDRQLQCKNRSLHQLLKNEKDEVQKLQNIIASRATQYNHDVKRKEREYNKLKERLHQLVMNKKDKNIAMDVLNYVGRADGKRGSWRTDKTEARNEDEMYKILLNDYEYRQKQILMENAELKKVLQQMKKEMISLLSPQKKKPRERAEDGTGTVAISDIEDDSGELSRDSVWGLSCDTVREQLTNSIRKQWRILKSHVEKLDNQASKVHSEGLNEEDVISRQDHEQETEKLELEIERCKEMIKAQQQLLQQQLATTCDDDTTSLLRDCYLLEEKERLKEEWTLFKEQKKNFERERRSFTEAAIRLGLERKAFEEERASWVKQQFLNMTNFDHQNSENVKLFSAFSGSSDPDNLIVHSRPRQKKLHSVANGVPACTSKLTKSLPASPSTSDFRQTHSCVSEHSSISVLNITPEESKPSEVARESTDQKWSVQSRPSSREGCYSGCSSAFRSAHGDRDDLP

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0R4J1A9A0A0R4J1A9_MOUSESsx2ip614
D3Z6T5D3Z6T5_MOUSESsx2ip44
D3Z474D3Z474_MOUSESsx2ip134

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict47in Ref. 3; AAH31527
Compositional bias293-307Basic and acidic residues
Sequence conflict406in Ref. 2; BAC33536/BAC27363
Sequence conflict503in Ref. 2; BAC33536
Compositional bias579-599Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF532969
EMBL· GenBank· DDBJ
AAO15015.1
EMBL· GenBank· DDBJ
mRNA
AK049080
EMBL· GenBank· DDBJ
BAC33536.1
EMBL· GenBank· DDBJ
mRNA
AK031356
EMBL· GenBank· DDBJ
BAC27363.1
EMBL· GenBank· DDBJ
mRNA
AK043865
EMBL· GenBank· DDBJ
BAC31684.1
EMBL· GenBank· DDBJ
mRNA
BC021749
EMBL· GenBank· DDBJ
AAH21749.1
EMBL· GenBank· DDBJ
mRNA
BC031527
EMBL· GenBank· DDBJ
AAH31527.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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