[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/baiap2-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/baiap2-wikipedia\/","headline":"BAIAP2 – Wikipedia","name":"BAIAP2 – Wikipedia","description":"before-content-x4 From Wikipedia, the free encyclopedia after-content-x4 Protein-coding gene in the species Homo sapiens Brain-specific angiogenesis inhibitor 1-associated protein 2","datePublished":"2017-06-18","dateModified":"2017-06-18","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/upload.wikimedia.org\/wikipedia\/commons\/thumb\/a\/aa\/PDB_1wdz_EBI.jpg\/180px-PDB_1wdz_EBI.jpg","url":"https:\/\/upload.wikimedia.org\/wikipedia\/commons\/thumb\/a\/aa\/PDB_1wdz_EBI.jpg\/180px-PDB_1wdz_EBI.jpg","height":"135","width":"180"},"url":"https:\/\/wiki.edu.vn\/en\/wiki24\/baiap2-wikipedia\/","wordCount":7277,"articleBody":"     (adsbygoogle = window.adsbygoogle || []).push({});before-content-x4From Wikipedia, the free encyclopedia       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Protein-coding gene in the species Homo sapiensBrain-specific angiogenesis inhibitor 1-associated protein 2 is a protein that in humans is encoded by the BAIAP2 gene.[5][6]       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Table of ContentsFunction[edit]Interactions[edit]References[edit]External links[edit]Further reading[edit]Function[edit]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.[6]Interactions[edit]BAIAP2 has been shown to interact with:       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4References[edit]^ a b c GRCh38: Ensembl release 89: ENSG00000175866 – Ensembl, May 2017^ a b c GRCm38: Ensembl release 89: ENSMUSG00000025372 – Ensembl, May 2017^ “Human PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.^ “Mouse PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.^ Oda K, Shiratsuchi T, Nishimori H, Inazawa J, Yoshikawa H, Taketani Y, Nakamura Y, Tokino T (June 1999). “Identification of BAIAP2 (BAI-associated protein 2), a novel human homologue of hamster IRSp53, whose SH3 domain interacts with the cytoplasmic domain of BAI1”. Cytogenet Cell Genet. 84 (1\u20132): 75\u201382. doi:10.1159\/000015219. PMID\u00a010343108. S2CID\u00a027688560.^ a b “Entrez Gene: BAIAP2 BAI1-associated protein 2”.^ Okamura-Oho Y, Miyashita T, Ohmi K, Yamada M (June 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\u201357. doi:10.1093\/hmg\/8.6.947. PMID\u00a010332026.^ a b c d Miki H, Yamaguchi H, Suetsugu S, Takenawa T (Dec 2000). “IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling”. Nature. 408 (6813): 732\u20135. Bibcode:2000Natur.408..732M. doi:10.1038\/35047107. PMID\u00a011130076. S2CID\u00a04426046.^ a b Soltau M, Richter D, Kreienkamp HJ (Dec 2002). “The insulin receptor substrate IRSp53 links postsynaptic shank1 to the small G-protein cdc42”. Mol. Cell. Neurosci. 21 (4): 575\u201383. doi:10.1006\/mcne.2002.1201. PMID\u00a012504591. S2CID\u00a0572407.^ Krugmann S, Jordens I, Gevaert K, Driessens M, Vandekerckhove J, Hall A (October 2001). “Cdc42 induces filopodia by promoting the formation of an IRSp53:Mena complex”. Curr. Biol. 11 (21): 1645\u201355. doi:10.1016\/S0960-9822(01)00506-1. PMID\u00a011696321. S2CID\u00a011290377.^ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). “Towards a proteome-scale map of the human protein-protein interaction network”. Nature. 437 (7062): 1173\u20138. Bibcode:2005Natur.437.1173R. doi:10.1038\/nature04209. PMID\u00a016189514. S2CID\u00a04427026.^ Funato Y, Terabayashi T, Suenaga N, Seiki M, Takenawa T, Miki H (August 2004). “IRSp53\/Eps8 complex is important for positive regulation of Rac and cancer cell motility\/invasiveness”. Cancer Res. 64 (15): 5237\u201344. doi:10.1158\/0008-5472.CAN-04-0327. PMID\u00a015289329. S2CID\u00a09844872.External links[edit]Further reading[edit]Maruyama K, Sugano S (1994). “Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides”. Gene. 138 (1\u20132): 171\u20134. doi:10.1016\/0378-1119(94)90802-8. PMID\u00a08125298.Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K,  et\u00a0al. (1997). “Construction and characterization of a full length-enriched and a 5′-end-enriched cDNA library”. Gene. 200 (1\u20132): 149\u201356. doi:10.1016\/S0378-1119(97)00411-3. PMID\u00a09373149.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\u201357. doi:10.1093\/hmg\/8.6.947. PMID\u00a010332026.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\u20138. doi:10.1523\/JNEUROSCI.19-17-07300.1999. PMC\u00a06782521. PMID\u00a010460236.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\u20139. doi:10.1006\/bbrc.2000.2671. PMID\u00a010814512.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\u20135. Bibcode:2000Natur.408..732M. doi:10.1038\/35047107. PMID\u00a011130076. S2CID\u00a04426046.Govind S, Kozma R, Monfries C,  et\u00a0al. (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\u201394. doi:10.1083\/jcb.152.3.579. PMC\u00a02195994. PMID\u00a011157984.Krugmann S, Jordens I, Gevaert K,  et\u00a0al. (2002). “Cdc42 induces filopodia by promoting the formation of an IRSp53:Mena complex”. Curr. Biol. 11 (21): 1645\u201355. doi:10.1016\/S0960-9822(01)00506-1. PMID\u00a011696321. S2CID\u00a011290377.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\u20139. doi:10.1016\/S0006-291X(02)00218-8. PMID\u00a012054568.Strausberg RL, Feingold EA, Grouse LH,  et\u00a0al. (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\u2013903. Bibcode:2002PNAS…9916899M. doi:10.1073\/pnas.242603899. PMC\u00a0139241. PMID\u00a012477932.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\u201383. doi:10.1006\/mcne.2002.1201. PMID\u00a012504591. S2CID\u00a0572407.Sekerkov\u00e1 G, Loomis PA, Changyaleket B,  et\u00a0al. (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\u20139. doi:10.1523\/JNEUROSCI.23-04-01310.2003. PMC\u00a02854510. PMID\u00a012598619.Miyahara A, Okamura-Oho Y, Miyashita T,  et\u00a0al. (2003). “Genomic structure and alternative splicing of the insulin receptor tyrosine kinase substrate of 53-kDa protein”. J. Hum. Genet. 48 (8): 410\u20134. doi:10.1007\/s10038-003-0047-x. PMID\u00a012884081.Hori K, Konno D, Maruoka H, Sobue K (2003). “MALS is a binding partner of IRSp53 at cell-cell contacts”. FEBS Lett. 554 (1\u20132): 30\u20134. doi:10.1016\/S0014-5793(03)01074-3. PMID\u00a014596909. S2CID\u00a030329043.Lehner B, Semple JI, Brown SE,  et\u00a0al. (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\u201367. doi:10.1016\/S0888-7543(03)00235-0. PMID\u00a014667819.Ota T, Suzuki Y, Nishikawa T,  et\u00a0al. (2004). “Complete sequencing and characterization of 21,243 full-length human cDNAs”. Nat. Genet. 36 (1): 40\u20135. doi:10.1038\/ng1285. PMID\u00a014702039.Yamagishi A, Masuda M, Ohki T,  et\u00a0al. (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\u201336. doi:10.1074\/jbc.M309408200. PMID\u00a014752106.Funato Y, Terabayashi T, Suenaga N,  et\u00a0al. (2004). “IRSp53\/Eps8 complex is important for positive regulation of Rac and cancer cell motility\/invasiveness”. Cancer Res. 64 (15): 5237\u201344. doi:10.1158\/0008-5472.CAN-04-0327. PMID\u00a015289329. S2CID\u00a09844872.Jin J, Smith FD, Stark C,  et\u00a0al. (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\u201350. doi:10.1016\/j.cub.2004.07.051. PMID\u00a015324660. S2CID\u00a02371325.PDB gallery1wdz: Crystal structure of RCB domain of IRSp531y2o: Structure of N-terminal domain IRSp53\/BAIAP2       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4"},{"@context":"http:\/\/schema.org\/","@type":"BreadcrumbList","itemListElement":[{"@type":"ListItem","position":1,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/#breadcrumbitem","name":"Enzyklop\u00e4die"}},{"@type":"ListItem","position":2,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/baiap2-wikipedia\/#breadcrumbitem","name":"BAIAP2 – Wikipedia"}}]}]