ID:BAIP2_HUMAN DESCRIPTION: RecName: Full=Brain-specific angiogenesis inhibitor 1-associated protein 2; Short=BAI-associated protein 2; Short=BAI1-associated protein 2; Short=Protein BAP2; AltName: Full=Fas ligand-associated factor 3; Short=FLAF3; AltName: Full=Insulin receptor substrate p53/p58; Short=IRS-58; Short=IRSp53/58; AltName: Full=Insulin receptor substrate protein of 53 kDa; Short=IRSp53; Short=Insulin receptor substrate p53; FUNCTION: Adapter protein that links membrane-bound small G- proteins to cytoplasmic effector proteins. Necessary for CDC42- mediated reorganization of the actin cytoskeleton and for RAC1- mediated membrane ruffling. Involved in the regulation of the actin cytoskeleton by WASF family members and the Arp2/3 complex. Plays a role in neurite growth. Acts syngeristically with ENAH to promote filipodia formation. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection. SUBUNIT: Homodimer. Interacts with CDC42 and RAC1 that have been activated by GTP binding. Interacts with ATN1, BAI1, EPS8, SHANK1, SHANK2, SHANK3, WASF1 and WASF2. Interacts with ENAH after recruitment of CDC42. Interacts with TIAM1 and DIAPH1 (By similarity). Interacts (via SH3 domain) with E.coli effector protein EspF(U) (via PXXP motifs). Interacts with E.coli intimin receptor Tir. INTERACTION: Self; NbExp=2; IntAct=EBI-525456, EBI-525456; P60953-2:CDC42; NbExp=2; IntAct=EBI-525456, EBI-287394; Q12929:EPS8; NbExp=4; IntAct=EBI-525456, EBI-375576; Q08509:Eps8 (xeno); NbExp=8; IntAct=EBI-525456, EBI-375596; Q14678:KANK1; NbExp=6; IntAct=EBI-525456, EBI-2556221; Q14678-2:KANK1; NbExp=4; IntAct=EBI-6174091, EBI-6173812; P63000:RAC1; NbExp=3; IntAct=EBI-525456, EBI-413628; Q9Y6W5:WASF2; NbExp=5; IntAct=EBI-6174091, EBI-4290615; SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Cell projection, filopodium. Cell projection, ruffle. Cytoplasm, cytoskeleton. Note=Detected throughout the cytoplasm in the absence of specific binding partners. Detected in filopodia and close to membrane ruffles. Recruited to actin pedestals that are formed upon infection by bacteria at bacterial attachment sites. TISSUE SPECIFICITY: Isoform 1 and isoform 4 are expressed almost exclusively in brain. Isoform 4 is barely detectable in placenta, prostate and testis. A short isoform is ubiquitous, with the highest expression in liver, prostate, testis and placenta. DOMAIN: The IMD domain forms a coiled coil. The isolated domain can induce actin bundling and filopodia formation. In the absence of G-proteins intramolecular interaction between the IMD and the SH3 domain gives rise to an auto-inhibited state of the protein. Interaction of the IMD with RAC1 or CDC42 leads to activation. DOMAIN: The SH3 domain interacts with ATN1, BAI1, WASF1, WASF2, SHANK1, DIAPH1 and ENAH. PTM: Phosphorylated on tyrosine residues by INSR in response to insulin treatment. SIMILARITY: Contains 1 IMD (IRSp53/MIM homology) domain. SIMILARITY: Contains 1 SH3 domain. CAUTION: It is uncertain whether Met-1 or Met-59 is the initiator.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q9UQB8
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.