BAIAP2

BAIAP2
Identifiers
Aliases	BAIAP2, BAP2, FLAF3, IRSP53, BAI1 associated protein 2, BAR/IMD domain containing adaptor protein 2, WAML
External IDs	OMIM: 605475; MGI: 2137336; GeneCards: BAIAP2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1WDZ, 1Y2O, 2YKT, 3RNJ, 4JS0
Gene location (Human) Chr. Chromosome 17 (human) Band 17q25.3 Start 81,035,122 bp End 81,117,432 bp
Gene location (Mouse) Chr. Chromosome 11 (mouse) Band 11|11 E2 Start 119,833,589 bp End 119,897,608 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Brodmann area 10 frontal pole middle frontal gyrus right frontal lobe skin of abdomen anterior cingulate cortex skin of leg Brodmann area 9 caudate nucleus nucleus accumbens Top expressed in superior frontal gyrus olfactory tubercle dentate gyrus of hippocampal formation granule cell primary visual cortex piriform cortex corneal stroma nucleus accumbens perirhinal cortex entorhinal cortex primary motor cortex More reference expression data BioGPS More reference expression data
Gene ontology Molecular function PDZ domain binding protein C-terminus binding protein binding identical protein binding cytoskeletal anchor activity proline-rich region binding cadherin binding involved in cell-cell adhesion transcription coregulator binding scaffold protein binding Cellular component cytosol cell projection postsynaptic density membrane filopodium ruffle dendritic spine secretory granule soma actin cytoskeleton neuron projection extracellular exosome cytoskeleton cytoplasm rough endoplasmic reticulum Golgi apparatus microtubule plasma membrane dendritic shaft neuron projection terminus excitatory synapse synaptic membrane postsynapse neuron projection branch point dendritic spine cytoplasm presynapse nucleoplasm Schaffer collateral - CA1 synapse glutamatergic synapse postsynaptic density, intracellular component presynaptic cytosol postsynaptic cytosol Biological process insulin receptor signaling pathway positive regulation of actin filament polymerization regulation of actin cytoskeleton organization response to bacterium axonogenesis Fc-gamma receptor signaling pathway involved in phagocytosis dendrite development actin filament bundle assembly regulation of synaptic plasticity vascular endothelial growth factor receptor signaling pathway actin crosslink formation regulation of cell shape plasma membrane organization positive regulation of actin cytoskeleton reorganization positive regulation of dendritic spine morphogenesis cell-cell adhesion brain development positive regulation of neuron projection development neuron differentiation protein localization to synapse cellular response to epidermal growth factor stimulus cellular response to L-glutamate positive regulation of excitatory postsynaptic potential modulation of chemical synaptic transmission modification of synaptic structure, modulating synaptic transmission regulation of modification of postsynaptic actin cytoskeleton Sources:Amigo / QuickGO
Orthologs Databases NCBI: entry; OMA: entry Species Human Mouse Entrez 10458 108100 Ensembl ENSG00000175866 ENSMUSG00000025372 UniProt Q9UQB8 Q8BKX1 RefSeq (mRNA) NM_001144888 NM_006340 NM_017450 NM_017451 NM_001037754 NM_001037755 NM_130862 RefSeq (protein) NP_001138360 NP_006331 NP_059344 NP_059345 NP_001032843 NP_001032844 NP_570932 Location (UCSC) Chr 17: 81.04 – 81.12 Mb Chr 11: 119.83 – 119.9 Mb PubMed search
Wikidata
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Brain-specific angiogenesis inhibitor 1-associated protein 2 is a protein that in humans is encoded by the BAIAP2 gene.

Function

The protein encoded by this gene has been identified as a brain-specific angiogenesis inhibitor (BAI1)-binding protein. This interaction at the cytoplasmic membrane is crucial to the function of this protein, which may be involved in neuronal growth-cone guidance. This protein functions as an insulin receptor tyrosine kinase substrate and suggests a role for insulin in the central nervous system. This protein has also been identified as interacting with the dentatorubral-pallidoluysian atrophy gene, which is associated with an autosomal dominant neurodegenerative disease. It also associates with a downstream effector of Rho small G proteins, which is associated with the formation of stress fibers and cytokinesis. Alternative splicing of the 3'-end of this gene results in three products of undetermined function. The I-BAR/IMD domain of BAIAP2/IRSp53 binds to and deform the plasma membrane for cellular protrusions.

Interactions

BAIAP2 has been shown to interact with:

• ATN1,
• CDC42,
• EPS8,
• RAC1,
• SHANK1,
• WASF1, and
• WASF2.

External links

• Human BAIAP2 genome location and BAIAP2 gene details page in the UCSC Genome Browser.

Further reading

• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–174. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–156. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Abbott MA, Wells DG, Fallon JR (1999). "The insulin receptor tyrosine kinase substrate p58/53 and the insulin receptor are components of CNS synapses". The Journal of Neuroscience. 19 (17): 7300–7308. doi:10.1523/JNEUROSCI.19-17-07300.1999. PMC 6782521. PMID 10460236.
• Fujiwara T, Mammoto A, Kim Y, Takai Y (2000). "Rho small G-protein-dependent binding of mDia to an Src homology 3 domain-containing IRSp53/BAIAP2". Biochemical and Biophysical Research Communications. 271 (3): 626–629. doi:10.1006/bbrc.2000.2671. PMID 10814512.
• Govind S, Kozma R, Monfries C, Lim L, Ahmed S (February 2001). "Cdc42Hs facilitates cytoskeletal reorganization and neurite outgrowth by localizing the 58-kD insulin receptor substrate to filamentous actin". The Journal of Cell Biology. 152 (3): 579–594. doi:10.1083/jcb.152.3.579. PMC 2195994. PMID 11157984.
• Miki H, Takenawa T (2002). "WAVE2 serves a functional partner of IRSp53 by regulating its interaction with Rac". Biochemical and Biophysical Research Communications. 293 (1): 93–99. doi:10.1016/S0006-291X(02)00218-8. PMID 12054568.
• Sekerková G, Loomis PA, Changyaleket B, Zheng L, Eytan R, Chen B, et al. (February 2003). "Novel espin actin-bundling proteins are localized to Purkinje cell dendritic spines and bind the Src homology 3 adapter protein insulin receptor substrate p53". The Journal of Neuroscience. 23 (4): 1310–1319. doi:10.1523/JNEUROSCI.23-04-01310.2003. PMC 2854510. PMID 12598619.
• Miyahara A, Okamura-Oho Y, Miyashita T, Hoshika A, Yamada M (2003). "Genomic structure and alternative splicing of the insulin receptor tyrosine kinase substrate of 53-kDa protein". Journal of Human Genetics. 48 (8): 410–414. doi:10.1007/s10038-003-0047-x. PMID 12884081.
• Hori K, Konno D, Maruoka H, Sobue K (2003). "MALS is a binding partner of IRSp53 at cell-cell contacts". FEBS Letters. 554 (1–2): 30–34. doi:10.1016/S0014-5793(03)01074-3. PMID 14596909. S2CID 30329043.
• Lehner B, Semple JI, Brown SE, Counsell D, Campbell RD, Sanderson CM (January 2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region". Genomics. 83 (1): 153–167. doi:10.1016/S0888-7543(03)00235-0. PMID 14667819.
• Yamagishi A, Masuda M, Ohki T, Onishi H, Mochizuki N (April 2004). "A novel actin bundling/filopodium-forming domain conserved in insulin receptor tyrosine kinase substrate p53 and missing in metastasis protein". The Journal of Biological Chemistry. 279 (15): 14929–14936. doi:10.1074/jbc.M309408200. PMID 14752106.
• Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, et al. (August 2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Current Biology. 14 (16): 1436–1450. doi:10.1016/j.cub.2004.07.051. PMID 15324660. S2CID 2371325.