BAIAP2

BAI1-associated protein 2
PDB rendering based on 1wdz.
Available structures PDB 1WDZ, 1Y2O
Identifiers
Symbols	BAIAP2; BAP2; FLAF3; IRSP53
External IDs	OMIM: 605475 MGI: 2137336 HomoloGene: 9697 GeneCards: BAIAP2 Gene
Gene Ontology Molecular function • protein binding • protein C-terminus binding • cytoskeletal adaptor activity • SH3 domain binding • proline-rich region binding Cellular component • ruffle • nucleus • nucleolus • cytoplasm • cytosol • plasma membrane • actin cytoskeleton • cell junction • filopodium Biological process • signal transduction • axonogenesis • insulin receptor signaling pathway • response to bacterium • regulation of actin cytoskeleton organization • filopodium assembly Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	10458	108100
Ensembl	ENSG00000175866	ENSMUSG00000025372
UniProt	Q9UQB8	Q3TV50
RefSeq (mRNA)	NM_001144888.1	NM_001037754
RefSeq (protein)	NP_001138360.1	NP_001032843
Location (UCSC)	Chr 17: 79.01 – 79.09 Mb	Chr 11: 119.8 – 119.87 Mb
PubMed search	[1]	[2]

Brain-specific angiogenesis inhibitor 1-associated protein 2 is a protein that in humans is encoded by the BAIAP2 gene.

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.

Interactions

BAIAP2 has been shown to interact with WASF1, EPS8, SHANK1, RAC1, WASF2, ATN1 and CDC42.

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): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
• Okamura-Oho Y, Miyashita T, Ohmi K, Yamada M (1999). "Dentatorubral-pallidoluysian atrophy protein interacts through a proline-rich region near polyglutamine with the SH3 domain of an insulin receptor tyrosine kinase substrate". Hum. Mol. Genet. 8 (6): 947–57. doi:10.1093/hmg/8.6.947. PMID 10332026. 
• Abbott MA, Wells DG, Fallon JR (1999). "The insulin receptor tyrosine kinase substrate p58/53 and the insulin receptor are components of CNS synapses". J. Neurosci. 19 (17): 7300–8. 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". Biochem. Biophys. Res. Commun. 271 (3): 626–9. doi:10.1006/bbrc.2000.2671. PMID 10814512. 
• Miki H, Yamaguchi H, Suetsugu S, Takenawa T (2001). "IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling". Nature 408 (6813): 732–5. doi:10.1038/35047107. PMID 11130076. 
• Govind S, Kozma R, Monfries C, et al. (2001). "Cdc42hs Facilitates Cytoskeletal Reorganization and Neurite Outgrowth by Localizing the 58-Kd Insulin Receptor Substrate to Filamentous Actin". J. Cell Biol. 152 (3): 579–94. doi:10.1083/jcb.152.3.579. PMC 2195994. PMID 11157984. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2195994. 
• Krugmann S, Jordens I, Gevaert K, et al. (2002). "Cdc42 induces filopodia by promoting the formation of an IRSp53:Mena complex". Curr. Biol. 11 (21): 1645–55. doi:10.1016/S0960-9822(01)00506-1. PMID 11696321. 
• Miki H, Takenawa T (2002). "WAVE2 serves a functional partner of IRSp53 by regulating its interaction with Rac". Biochem. Biophys. Res. Commun. 293 (1): 93–9. doi:10.1016/S0006-291X(02)00218-8. PMID 12054568. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Soltau M, Richter D, Kreienkamp HJ (2003). "The insulin receptor substrate IRSp53 links postsynaptic shank1 to the small G-protein cdc42". Mol. Cell. Neurosci. 21 (4): 575–83. doi:10.1006/mcne.2002.1201. PMID 12504591. 
• Sekerková G, Loomis PA, Changyaleket B, et al. (2003). "Novel Espin Actin-bundling Proteins Are Localized to Purkinje Cell Dendritic Spines and Bind the SH3 Adapter Protein Insulin Receptor Substrate p53". J. Neurosci. 23 (4): 1310–9. PMC 2854510. PMID 12598619. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2854510. 
• Miyahara A, Okamura-Oho Y, Miyashita T, et al. (2003). "Genomic structure and alternative splicing of the insulin receptor tyrosine kinase substrate of 53-kDa protein". J. Hum. Genet. 48 (8): 410–4. 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 Lett. 554 (1–2): 30–4. doi:10.1016/S0014-5793(03)01074-3. PMID 14596909. 
• Lehner B, Semple JI, Brown SE, et al. (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): 153–67. doi:10.1016/S0888-7543(03)00235-0. PMID 14667819. 
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
• Yamagishi A, Masuda M, Ohki T, et al. (2004). "A novel actin bundling/filopodium-forming domain conserved in insulin receptor tyrosine kinase substrate p53 and missing in metastasis protein". J. Biol. Chem. 279 (15): 14929–36. doi:10.1074/jbc.M309408200. PMID 14752106. 
• Funato Y, Terabayashi T, Suenaga N, et al. (2004). "IRSp53/Eps8 complex is important for positive regulation of Rac and cancer cell motility/invasiveness". Cancer Res. 64 (15): 5237–44. doi:10.1158/0008-5472.CAN-04-0327. PMID 15289329. 
• Jin J, Smith FD, Stark C, et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.