Q8VC66 · ADIP_MOUSE
- ProteinAfadin- and alpha-actinin-binding protein
- GeneSsx2ip
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids615 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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 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 | adherens junction | |
Cellular Component | cell leading edge | |
Cellular Component | centriolar satellite | |
Cellular Component | ciliary basal body | |
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Cellular Component | protein-containing complex | |
Molecular Function | protein domain specific binding | |
Biological Process | cell adhesion | |
Biological Process | centrosome cycle | |
Biological Process | cilium assembly | |
Biological Process | intraciliary transport involved in cilium assembly | |
Biological Process | regulation of cell motility | |
Biological Process | regulation of Rac protein signal transduction |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameAfadin- and alpha-actinin-binding protein
- Short namesADIP
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8VC66
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000064456 | 1-615 | Afadin- and alpha-actinin-binding protein | |||
Sequence: MGDWMTVTDPVLCTENKNLSQYTSETKMSPSSLYSQQVLCSSVPLSKNVHGVFGVFCTGENIEQSISYLDQELTTFGFPSLYEESKSKEAKRELNIVAVLNCMNELLVLQRKNLLAQESVETQNLKLGSDMDHLQSCYAKLKEQLETSRREMIGLQERDRQLQCKNRSLHQLLKNEKDEVQKLQNIIASRATQYNHDVKRKEREYNKLKERLHQLVMNKKDKNIAMDVLNYVGRADGKRGSWRTDKTEARNEDEMYKILLNDYEYRQKQILMENAELKKVLQQMKKEMISLLSPQKKKPRERAEDGTGTVAISDIEDDSGELSRDSVWGLSCDTVREQLTNSIRKQWRILKSHVEKLDNQASKVHSEGLNEEDVISRQDHEQETEKLELEIERCKEMIKAQQQLLQQQLATTCDDDTTSLLRDCYLLEEKERLKEEWTLFKEQKKNFERERRSFTEAAIRLGLERKAFEEERASWVKQQFLNMTNFDHQNSENVKLFSAFSGSSDPDNLIVHSRPRQKKLHSVANGVPACTSKLTKSLPASPSTSDFRQTHSCVSEHSSISVLNITPEESKPSEVARESTDQKWSVQSRPSSREGCYSGCSSAFRSAHGDRDDLP | ||||||
Modified residue | 290 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 293 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 313 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 319 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 537 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 541 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 543 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
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).
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
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | Q8VC66 | ACTN1 P12814 | 3 | EBI-6654049, EBI-351710 | |
XENO | Q8VC66 | Afdn O35889 | 4 | EBI-6654049, EBI-6654073 | |
XENO | Q8VC66 | WRAP73 Q9P2S5 | 4 | EBI-6654049, EBI-1054904 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for coiled coil, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 126-227 | |||||
Sequence: KLGSDMDHLQSCYAKLKEQLETSRREMIGLQERDRQLQCKNRSLHQLLKNEKDEVQKLQNIIASRATQYNHDVKRKEREYNKLKERLHQLVMNKKDKNIAMD | ||||||
Coiled coil | 266-293 | |||||
Sequence: RQKQILMENAELKKVLQQMKKEMISLLS | ||||||
Compositional bias | 293-307 | Basic and acidic residues | ||||
Sequence: SPQKKKPRERAEDGT | ||||||
Region | 293-316 | Disordered | ||||
Sequence: SPQKKKPRERAEDGTGTVAISDIE | ||||||
Coiled coil | 375-461 | |||||
Sequence: ISRQDHEQETEKLELEIERCKEMIKAQQQLLQQQLATTCDDDTTSLLRDCYLLEEKERLKEEWTLFKEQKKNFERERRSFTEAAIRL | ||||||
Region | 567-615 | Disordered | ||||
Sequence: PEESKPSEVARESTDQKWSVQSRPSSREGCYSGCSSAFRSAHGDRDDLP | ||||||
Compositional bias | 579-599 | Polar residues | ||||
Sequence: STDQKWSVQSRPSSREGCYSG |
Sequence similarities
Belongs to the ADIP family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length615
- Mass (Da)70,956
- Last updated2002-03-01 v1
- ChecksumCC41D7078591919F
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0R4J1A9 | A0A0R4J1A9_MOUSE | Ssx2ip | 614 | ||
D3Z6T5 | D3Z6T5_MOUSE | Ssx2ip | 44 | ||
D3Z474 | D3Z474_MOUSE | Ssx2ip | 134 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 47 | in Ref. 3; AAH31527 | ||||
Sequence: K → R | ||||||
Compositional bias | 293-307 | Basic and acidic residues | ||||
Sequence: SPQKKKPRERAEDGT | ||||||
Sequence conflict | 406 | in Ref. 2; BAC33536/BAC27363 | ||||
Sequence: Missing | ||||||
Sequence conflict | 503 | in Ref. 2; BAC33536 | ||||
Sequence: S → SKPG | ||||||
Compositional bias | 579-599 | Polar residues | ||||
Sequence: STDQKWSVQSRPSSREGCYSG |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |