MAGI1

Membrane associated guanylate kinase, WW and PDZ domain containing 1
PDB rendering based on 2i04.
Available structures PDB 2i04
Identifiers
Symbols	MAGI1; AIP-3; AIP3; BAIAP1; BAP-1; BAP1; MAGI-1; TNRC19; WWP3
External IDs	OMIM: 602625 MGI: 1203522 HomoloGene: 31257 GeneCards: MAGI1 Gene
Gene Ontology Molecular function • nucleotide binding • protein binding • ATP binding • protein C-terminus binding Cellular component • plasma membrane • cell-cell junction • tight junction Biological process • protein complex assembly • cell adhesion • cell surface receptor linked signaling pathway Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	9223	14924
Ensembl	ENSG00000151276	ENSMUSG00000045095
UniProt	Q96QZ7	A0JLR6
RefSeq (mRNA)	NM_001033057.1	NM_001029850
RefSeq (protein)	NP_001028229.1	NP_001025021
Location (UCSC)	Chr 3: 65.34 – 66.02 Mb	Chr 6: 93.63 – 94.23 Mb
PubMed search	[1]	[2]

Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1 is an enzyme that in humans is encoded by the MAGI1 gene.

The protein encoded by this gene is a member of the membrane-associated guanylate kinase homologue (MAGUK) family. MAGUK proteins participate in the assembly of multiprotein complexes on the inner surface of the plasma membrane at regions of cell–cell contact. The product of this gene may play a role as scaffolding protein at cell–cell junctions. Alternatively spliced transcript variants encoding different isoforms have been identified.

Interactions

MAGI1 has been shown to interact with Beta-catenin, Actinin alpha 4, Brain-specific angiogenesis inhibitor 1, LRP2, SYNPO, FCHSD2, ATN1 and ACCN3.

Further reading

• Pirozzi G, McConnell SJ, Uveges AJ et al (1997). "Identification of novel human WW domain-containing proteins by cloning of ligand targets". J. Biol. Chem. 272 (23): 14611–6. doi:10.1074/jbc.272.23.14611. PMID 9169421. 
• Dobrosotskaya I, Guy RK, James GL (1998). "MAGI-1, a membrane-associated guanylate kinase with a unique arrangement of protein-protein interaction domains". J. Biol. Chem. 272 (50): 31589–97. doi:10.1074/jbc.272.50.31589. PMID 9395497. 
• Wood JD, Yuan J, Margolis RL et al (1998). "Atrophin-1, the DRPLA gene product, interacts with two families of WW domain-containing proteins". Mol. Cell. Neurosci. 11 (3): 149–60. doi:10.1006/mcne.1998.0677. PMID 9647693. 
• Dobrosotskaya IY, James GL (2000). "MAGI-1 interacts with beta-catenin and is associated with cell-cell adhesion structures". Biochem. Biophys. Res. Commun. 270 (3): 903–9. doi:10.1006/bbrc.2000.2471. PMID 10772923. 
• Patrie KM, Drescher AJ, Goyal M et al (2001). "The membrane-associated guanylate kinase protein MAGI-1 binds megalin and is present in glomerular podocytes". J. Am. Soc. Nephrol. 12 (4): 667–77. PMID 11274227. 
• Dobrosotskaya IY (2001). "Identification of mNET1 as a candidate ligand for the first PDZ domain of MAGI-1". Biochem. Biophys. Res. Commun. 283 (4): 969–75. doi:10.1006/bbrc.2001.4880. PMID 11350080. 
• Laura RP, Ross S, Koeppen H, Lasky LA (2002). "MAGI-1: a widely expressed, alternatively spliced tight junction protein". Exp. Cell Res. 275 (2): 155–70. doi:10.1006/excr.2002.5475. PMID 11969287. 
• Patrie KM, Drescher AJ, Welihinda A et al (2002). "Interaction of two actin-binding proteins, synaptopodin and alpha-actinin-4, with the tight junction protein MAGI-1". J. Biol. Chem. 277 (33): 30183–90. doi:10.1074/jbc.M203072200. PMID 12042308. 
• 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. 
• Ohno H, Hirabayashi S, Kansaku A et al (2003). "Carom: a novel membrane-associated guanylate kinase-interacting protein with two SH3 domains". Oncogene 22 (52): 8422–31. doi:10.1038/sj.onc.1206996. PMID 14627983. 
• 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. 
• Hruska-Hageman AM, Benson CJ, Leonard AS et al (2004). "PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have opposite effects on H+- gated current". J. Biol. Chem. 279 (45): 46962–8. doi:10.1074/jbc.M405874200. PMID 15317815. 
• Wright GJ, Leslie JD, Ariza-McNaughton L, Lewis J (2005). "Delta proteins and MAGI proteins: an interaction of Notch ligands with intracellular scaffolding molecules and its significance for zebrafish development". Development 131 (22): 5659–69. doi:10.1242/dev.01417. PMID 15509766. 
• Benzinger A, Muster N, Koch HB et al (2005). "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer". Mol. Cell Proteomics 4 (6): 785–95. doi:10.1074/mcp.M500021-MCP200. PMID 15778465. 
• Mizuhara E, Nakatani T, Minaki Y et al (2005). "MAGI1 recruits Dll1 to cadherin-based adherens junctions and stabilizes it on the cell surface". J. Biol. Chem. 280 (28): 26499–507. doi:10.1074/jbc.M500375200. PMID 15908431. 
• Patrie KM (2005). "Identification and characterization of a novel tight junction-associated family of proteins that interacts with a WW domain of MAGI-1". Biochim. Biophys. Acta 1745 (1): 131–44. doi:10.1016/j.bbamcr.2005.05.011. PMID 16019084. 
• Bratt A, Birot O, Sinha I et al (2005). "Angiomotin regulates endothelial cell-cell junctions and cell motility". J. Biol. Chem. 280 (41): 34859–69. doi:10.1074/jbc.M503915200. PMID 16043488. 
• Sakurai A, Fukuhara S, Yamagishi A et al (2006). "MAGI-1 is required for Rap1 activation upon cell-cell contact and for enhancement of vascular endothelial cadherin-mediated cell adhesion". Mol. Biol. Cell 17 (2): 966–76. doi:10.1091/mbc.E05-07-0647. PMC 1356604. PMID 16339077. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1356604.