BAIAP2: Difference between revisions

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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Brain-specific angiogenesis inhibitor 1-associated protein 2''' is a [[protein]] that in humans is encoded by the ''BAIAP2'' [[gene]].<ref name="pmid10343108">{{cite journal | vauthors = Oda K, Shiratsuchi T, Nishimori H, Inazawa J, Yoshikawa H, Taketani Y, Nakamura Y, Tokino T | title = Identification of BAIAP2 (BAI-associated protein 2), a novel human homologue of hamster IRSp53, whose SH3 domain interacts with the cytoplasmic domain of BAI1 | journal = Cytogenet Cell Genet | volume = 84 | issue = 1–2 | pages = 75–82 |date=June 1999 | pmid = 10343108 | pmc = | doi =10.1159/000015219  }}</ref><ref name="entrez"/>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_BAIAP2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1wdz.
| PDB = {{PDB2|1wdz}}, {{PDB2|1y2o}}
| Name = BAI1-associated protein 2
| HGNCid = 947
| Symbol = BAIAP2
| AltSymbols =; BAP2; IRSP53
| OMIM = 605475
| ECnumber = 
| Homologene = 9697
| MGIid = 2137336
| GeneAtlas_image1 = PBB_GE_BAIAP2_207832_at_tn.png
| GeneAtlas_image2 = PBB_GE_BAIAP2_209502_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_BAIAP2_205294_at_tn.png
| Function = {{GNF_GO|id=GO:0008022 |text = protein C-terminus binding}} {{GNF_GO|id=GO:0008093 |text = cytoskeletal adaptor activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}}
| Process = {{GNF_GO|id=GO:0007409 |text = axonogenesis}} {{GNF_GO|id=GO:0008286 |text = insulin receptor signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 10458
    | Hs_Ensembl = ENSG00000175866
    | Hs_RefseqProtein = NP_006331
    | Hs_RefseqmRNA = NM_006340
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 17
    | Hs_GenLoc_start = 76623557
    | Hs_GenLoc_end = 76705827
    | Hs_Uniprot = Q9UQB8
    | Mm_EntrezGene = 108100
    | Mm_Ensembl = ENSMUSG00000025372
    | Mm_RefseqmRNA = NM_001037754
    | Mm_RefseqProtein = NP_001032843
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 119758853
    | Mm_GenLoc_end = 119822869
    | Mm_Uniprot = Q3TV50
  }}
}}
'''BAI1-associated protein 2''', also known as '''BAIAP2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: BAIAP2 BAI1-associated protein 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10458| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The protein encoded by this gene has been identified as a brain-specific angiogenesis inhibitor ([[Brain-specific angiogenesis inhibitor 1|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.<ref name="entrez">{{cite web | title = Entrez Gene: BAIAP2 BAI1-associated protein 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10458| accessdate = }}</ref>
{{PBB_Summary
 
| section_title =
==Interactions==
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: BAIAP2 BAI1-associated protein 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10458| accessdate = }}</ref>
BAIAP2 has been shown to [[Protein-protein interaction|interact]] with:
}}
{{div col|colwidth=20em}}
* [[ATN1]],<ref name = pmid10332026>{{cite journal | date = June 1999 | vauthors = Okamura-Oho Y, Miyashita T, Ohmi K, Yamada M | title = Dentatorubral-pallidoluysian atrophy protein interacts through a proline-rich region near polyglutamine with the SH3 domain of an insulin receptor tyrosine kinase substrate | journal = Hum. Mol. Genet. | volume = 8 | issue = 6 | pages = 947–57 | pmid = 10332026 | doi = 10.1093/hmg/8.6.947}}</ref>
* [[CDC42]],<ref name = pmid11130076/><ref name = pmid12504591/><ref name = pmid11696321>{{cite journal | date = October 2001 | vauthors = Krugmann S, Jordens I, Gevaert K, Driessens M, Vandekerckhove J, Hall A | title = Cdc42 induces filopodia by promoting the formation of an IRSp53:Mena complex | journal = Curr. Biol. | volume = 11 | issue = 21 | pages = 1645–55 | pmid = 11696321 | doi = 10.1016/S0960-9822(01)00506-1}}</ref>
* [[EPS8]],<ref name = pmid16189514>{{cite journal | date = October 2005 | vauthors = 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 | title = Towards a proteome-scale map of the human protein-protein interaction network | journal = Nature | volume = 437 | issue = 7062 | pages = 1173–8 | pmid = 16189514 | doi = 10.1038/nature04209}}</ref><ref name = pmid15289329>{{cite journal | date = August 2004 | vauthors = Funato Y, Terabayashi T, Suenaga N, Seiki M, Takenawa T, Miki H | title = IRSp53/Eps8 complex is important for positive regulation of Rac and cancer cell motility/invasiveness | journal = Cancer Res. | volume = 64 | issue = 15 | pages = 5237–44 | pmid = 15289329 | doi = 10.1158/0008-5472.CAN-04-0327}}</ref>
* [[RAC1]],<ref name = pmid11130076/>
* [[SHANK1]],<ref name = pmid12504591>{{cite journal | date = Dec 2002 | vauthors = Soltau M, Richter D, Kreienkamp HJ | title = The insulin receptor substrate IRSp53 links postsynaptic shank1 to the small G-protein cdc42 | journal = Mol. Cell. Neurosci. | volume = 21 | issue = 4 | pages = 575–83 | pmid = 12504591 | doi = 10.1006/mcne.2002.1201}}</ref>
* [[WASF1]],<ref name = pmid11130076>{{cite journal | date = Dec 2000 | vauthors = Miki H, Yamaguchi H, Suetsugu S, Takenawa T | title = IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling | journal = Nature | volume = 408 | issue = 6813 | pages = 732–5 | pmid = 11130076 | doi = 10.1038/35047107}}</ref>  and
* [[WASF2]].<ref name = pmid11130076/>
{{Div col end}}


==References==
==References==
{{reflist|2}}
{{Reflist}}
 
==External links==
* {{UCSC gene info|BAIAP2}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{Refbegin | 2}}
{{PBB_Further_reading
*{{cite journal  | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
| citations =
*{{cite journal  | vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 |display-authors=etal}}
*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
*{{cite journal  | vauthors=Okamura-Oho Y, Miyashita T, Ohmi K, Yamada M |title=Dentatorubral-pallidoluysian atrophy protein interacts through a proline-rich region near polyglutamine with the SH3 domain of an insulin receptor tyrosine kinase substrate |journal=Hum. Mol. Genet. |volume=8 |issue= 6 |pages= 947–57 |year= 1999 |pmid= 10332026 |doi=10.1093/hmg/8.6.947 }}
*{{cite journal  | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi=  }}
*{{cite journal  | vauthors=Abbott MA, Wells DG, Fallon JR |title=The insulin receptor tyrosine kinase substrate p58/53 and the insulin receptor are components of CNS synapses |journal=J. Neurosci. |volume=19 |issue= 17 |pages= 7300–8 |year= 1999 |pmid= 10460236 |doi=  }}
*{{cite journal  | author=Okamura-Oho Y, Miyashita T, Ohmi K, Yamada M |title=Dentatorubral-pallidoluysian atrophy protein interacts through a proline-rich region near polyglutamine with the SH3 domain of an insulin receptor tyrosine kinase substrate. |journal=Hum. Mol. Genet. |volume=8 |issue= 6 |pages= 947-57 |year= 1999 |pmid= 10332026 |doi=  }}
*{{cite journal  | vauthors=Fujiwara T, Mammoto A, Kim Y, Takai Y |title=Rho small G-protein-dependent binding of mDia to an Src homology 3 domain-containing IRSp53/BAIAP2 |journal=Biochem. Biophys. Res. Commun. |volume=271 |issue= 3 |pages= 626–9 |year= 2000 |pmid= 10814512 |doi= 10.1006/bbrc.2000.2671 }}
*{{cite journal  | author=Oda K, Shiratsuchi T, Nishimori H, ''et al.'' |title=Identification of BAIAP2 (BAI-associated protein 2), a novel human homologue of hamster IRSp53, whose SH3 domain interacts with the cytoplasmic domain of BAI1. |journal=Cytogenet. Cell Genet. |volume=84 |issue= 1-2 |pages= 75-82 |year= 1999 |pmid= 10343108 |doi=  }}
*{{cite journal  | vauthors=Miki H, Yamaguchi H, Suetsugu S, Takenawa T |title=IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling |journal=Nature |volume=408 |issue= 6813 |pages= 732–5 |year= 2001 |pmid= 11130076 |doi= 10.1038/35047107 }}
*{{cite journal  | author=Abbott MA, Wells DG, Fallon JR |title=The insulin receptor tyrosine kinase substrate p58/53 and the insulin receptor are components of CNS synapses. |journal=J. Neurosci. |volume=19 |issue= 17 |pages= 7300-8 |year= 1999 |pmid= 10460236 |doi= }}
*{{cite journal  | vauthors=Govind S, Kozma R, Monfries C |title=Cdc42hs Facilitates Cytoskeletal Reorganization and Neurite Outgrowth by Localizing the 58-Kd Insulin Receptor Substrate to Filamentous Actin |journal=J. Cell Biol. |volume=152 |issue= 3 |pages= 579–94 |year= 2001 |pmid= 11157984 |doi=10.1083/jcb.152.3.579  | pmc=2195994  |display-authors=etal}}
*{{cite journal  | author=Fujiwara T, Mammoto A, Kim Y, Takai Y |title=Rho small G-protein-dependent binding of mDia to an Src homology 3 domain-containing IRSp53/BAIAP2. |journal=Biochem. Biophys. Res. Commun. |volume=271 |issue= 3 |pages= 626-9 |year= 2000 |pmid= 10814512 |doi= 10.1006/bbrc.2000.2671 }}
*{{cite journal  | vauthors=Krugmann S, Jordens I, Gevaert K |title=Cdc42 induces filopodia by promoting the formation of an IRSp53:Mena complex |journal=Curr. Biol. |volume=11 |issue= 21 |pages= 1645–55 |year= 2002 |pmid= 11696321 |doi=10.1016/S0960-9822(01)00506-1  |display-authors=etal}}
*{{cite journal  | author=Miki H, Yamaguchi H, Suetsugu S, Takenawa T |title=IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling. |journal=Nature |volume=408 |issue= 6813 |pages= 732-5 |year= 2001 |pmid= 11130076 |doi= 10.1038/35047107 }}
*{{cite journal  | vauthors=Miki H, Takenawa T |title=WAVE2 serves a functional partner of IRSp53 by regulating its interaction with Rac |journal=Biochem. Biophys. Res. Commun. |volume=293 |issue= 1 |pages= 93–9 |year= 2002 |pmid= 12054568 |doi= 10.1016/S0006-291X(02)00218-8 }}
*{{cite journal  | author=Govind S, Kozma R, Monfries C, ''et al.'' |title=Cdc42Hs facilitates cytoskeletal reorganization and neurite outgrowth by localizing the 58-kD insulin receptor substrate to filamentous actin. |journal=J. Cell Biol. |volume=152 |issue= 3 |pages= 579-94 |year= 2001 |pmid= 11157984 |doi=  }}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |display-authors=etal}}
*{{cite journal  | author=Krugmann S, Jordens I, Gevaert K, ''et al.'' |title=Cdc42 induces filopodia by promoting the formation of an IRSp53:Mena complex. |journal=Curr. Biol. |volume=11 |issue= 21 |pages= 1645-55 |year= 2002 |pmid= 11696321 |doi= }}
*{{cite journal  | vauthors=Soltau M, Richter D, Kreienkamp HJ |title=The insulin receptor substrate IRSp53 links postsynaptic shank1 to the small G-protein cdc42 |journal=Mol. Cell. Neurosci. |volume=21 |issue= 4 |pages= 575–83 |year= 2003 |pmid= 12504591 |doi=10.1006/mcne.2002.1201  }}
*{{cite journal  | author=Miki H, Takenawa T |title=WAVE2 serves a functional partner of IRSp53 by regulating its interaction with Rac. |journal=Biochem. Biophys. Res. Commun. |volume=293 |issue= 1 |pages= 93-9 |year= 2002 |pmid= 12054568 |doi= 10.1016/S0006-291X(02)00218-8 }}
*{{cite journal  | vauthors=Sekerková G, Loomis PA, Changyaleket B |title=Novel Espin Actin-bundling Proteins Are Localized to Purkinje Cell Dendritic Spines and Bind the SH3 Adapter Protein Insulin Receptor Substrate p53 |journal=J. Neurosci. |volume=23 |issue= 4 |pages= 1310–9 |year= 2003 |pmid= 12598619 |doi=  | pmc=2854510  |display-authors=etal}}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | vauthors=Miyahara A, Okamura-Oho Y, Miyashita T |title=Genomic structure and alternative splicing of the insulin receptor tyrosine kinase substrate of 53-kDa protein |journal=J. Hum. Genet. |volume=48 |issue= 8 |pages= 410–4 |year= 2003 |pmid= 12884081 |doi= 10.1007/s10038-003-0047-x |display-authors=etal}}
*{{cite journal  | author=Soltau M, Richter D, Kreienkamp HJ |title=The insulin receptor substrate IRSp53 links postsynaptic shank1 to the small G-protein cdc42. |journal=Mol. Cell. Neurosci. |volume=21 |issue= 4 |pages= 575-83 |year= 2003 |pmid= 12504591 |doi=  }}
*{{cite journal  | vauthors=Hori K, Konno D, Maruoka H, Sobue K |title=MALS is a binding partner of IRSp53 at cell-cell contacts |journal=FEBS Lett. |volume=554 |issue= 1–2 |pages= 30–4 |year= 2003 |pmid= 14596909 |doi=10.1016/S0014-5793(03)01074-3  }}
*{{cite journal  | author=Sekerková G, Loomis PA, Changyaleket B, ''et al.'' |title=Novel espin actin-bundling proteins are localized to Purkinje cell dendritic spines and bind the Src homology 3 adapter protein insulin receptor substrate p53. |journal=J. Neurosci. |volume=23 |issue= 4 |pages= 1310-9 |year= 2003 |pmid= 12598619 |doi= }}
*{{cite journal  | vauthors=Lehner B, Semple JI, Brown SE |title=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 |journal=Genomics |volume=83 |issue= 1 |pages= 153–67 |year= 2004 |pmid= 14667819 |doi=10.1016/S0888-7543(03)00235-0  |display-authors=etal}}
*{{cite journal  | author=Miyahara A, Okamura-Oho Y, Miyashita T, ''et al.'' |title=Genomic structure and alternative splicing of the insulin receptor tyrosine kinase substrate of 53-kDa protein. |journal=J. Hum. Genet. |volume=48 |issue= 8 |pages= 410-4 |year= 2003 |pmid= 12884081 |doi= 10.1007/s10038-003-0047-x }}
*{{cite journal  | vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}}
*{{cite journal  | author=Hori K, Konno D, Maruoka H, Sobue K |title=MALS is a binding partner of IRSp53 at cell-cell contacts. |journal=FEBS Lett. |volume=554 |issue= 1-2 |pages= 30-4 |year= 2003 |pmid= 14596909 |doi= }}
*{{cite journal  | vauthors=Yamagishi A, Masuda M, Ohki T |title=A novel actin bundling/filopodium-forming domain conserved in insulin receptor tyrosine kinase substrate p53 and missing in metastasis protein |journal=J. Biol. Chem. |volume=279 |issue= 15 |pages= 14929–36 |year= 2004 |pmid= 14752106 |doi= 10.1074/jbc.M309408200 |display-authors=etal}}
*{{cite journal  | author=Lehner B, Semple JI, Brown SE, ''et al.'' |title=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. |journal=Genomics |volume=83 |issue= 1 |pages= 153-67 |year= 2004 |pmid= 14667819 |doi= }}
*{{cite journal  | vauthors=Funato Y, Terabayashi T, Suenaga N |title=IRSp53/Eps8 complex is important for positive regulation of Rac and cancer cell motility/invasiveness |journal=Cancer Res. |volume=64 |issue= 15 |pages= 5237–44 |year= 2004 |pmid= 15289329 |doi= 10.1158/0008-5472.CAN-04-0327 |display-authors=etal}}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | vauthors=Jin J, Smith FD, Stark C |title=Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization |journal=Curr. Biol. |volume=14 |issue= 16 |pages= 1436–50 |year= 2004 |pmid= 15324660 |doi= 10.1016/j.cub.2004.07.051 |display-authors=etal}}
*{{cite journal  | author=Yamagishi A, Masuda M, Ohki T, ''et al.'' |title=A novel actin bundling/filopodium-forming domain conserved in insulin receptor tyrosine kinase substrate p53 and missing in metastasis protein. |journal=J. Biol. Chem. |volume=279 |issue= 15 |pages= 14929-36 |year= 2004 |pmid= 14752106 |doi= 10.1074/jbc.M309408200 }}
{{Refend}}
*{{cite journal  | author=Funato Y, Terabayashi T, Suenaga N, ''et al.'' |title=IRSp53/Eps8 complex is important for positive regulation of Rac and cancer cell motility/invasiveness. |journal=Cancer Res. |volume=64 |issue= 15 |pages= 5237-44 |year= 2004 |pmid= 15289329 |doi= 10.1158/0008-5472.CAN-04-0327 }}
*{{cite journal  | author=Jin J, Smith FD, Stark C, ''et al.'' |title=Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization. |journal=Curr. Biol. |volume=14 |issue= 16 |pages= 1436-50 |year= 2004 |pmid= 15324660 |doi= 10.1016/j.cub.2004.07.051 }}
}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=10458}}
{{WikiDoc Sources}}

Latest revision as of 15:33, 24 April 2018

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

n/a

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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

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.[2]

Interactions

BAIAP2 has been shown to interact with:

References

  1. ↑ 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 (1–2): 75–82. doi:10.1159/000015219. PMID 10343108.
  2. ↑ 2.0 2.1 "Entrez Gene: BAIAP2 BAI1-associated protein 2".
  3. ↑ 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): 947–57. doi:10.1093/hmg/8.6.947. PMID 10332026.
  4. ↑ 4.0 4.1 4.2 4.3 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): 732–5. doi:10.1038/35047107. PMID 11130076.
  5. ↑ 5.0 5.1 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): 575–83. doi:10.1006/mcne.2002.1201. PMID 12504591.
  6. ↑ 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): 1645–55. doi:10.1016/S0960-9822(01)00506-1. PMID 11696321.
  7. ↑ 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): 1173–8. doi:10.1038/nature04209. PMID 16189514.
  8. ↑ 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): 5237–44. doi:10.1158/0008-5472.CAN-04-0327. PMID 15289329.

External links

Further reading

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