ID MAGI1_HUMAN Reviewed; 1491 AA. AC Q96QZ7; A8K188; O00309; O43863; O75085; Q96QZ8; Q96QZ9; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2009, sequence version 3. DT 27-MAR-2024, entry version 206. DE RecName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1; DE AltName: Full=Atrophin-1-interacting protein 3; DE Short=AIP-3; DE AltName: Full=BAI1-associated protein 1; DE Short=BAP-1; DE AltName: Full=Membrane-associated guanylate kinase inverted 1; DE Short=MAGI-1; DE AltName: Full=Trinucleotide repeat-containing gene 19 protein; DE AltName: Full=WW domain-containing protein 3; DE Short=WWP3; GN Name=MAGI1; Synonyms=AIP3, BAIAP1, BAP1, TNRC19; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, AND INTERACTION RP WITH ADGRB1. RC TISSUE=Brain; RX PubMed=9647739; DOI=10.1006/bbrc.1998.8603; RA Shiratsuchi T., Futamura M., Oda K., Nishimori H., Nakamura Y., Tokino T.; RT "Cloning and characterization of BAI-associated protein 1: a PDZ domain- RT containing protein that interacts with BAI1."; RL Biochem. Biophys. Res. Commun. 247:597-604(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4 AND 5), ALTERNATIVE SPLICING RP (ISOFORMS 6 AND 7), SUBCELLULAR LOCATION, PHOSPHORYLATION, AND TISSUE RP SPECIFICITY. RX PubMed=11969287; DOI=10.1006/excr.2002.5475; RA Laura R.P., Ross S., Koeppen H., Lasky L.A.; RT "MAGI-1: a widely expressed, alternatively spliced tight junction RT protein."; RL Exp. Cell Res. 275:155-170(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 150-826 (ISOFORMS 1/3), TISSUE SPECIFICITY, RP AND INTERACTION WITH DRPLA. RX PubMed=9647693; DOI=10.1006/mcne.1998.0677; RA Wood J.D., Yuan J., Margolis R.L., Colomer V., Duan K., Kushi J., RA Kaminsky Z., Kleiderlein J.J. Jr., Sharp A.H., Ross C.A.; RT "Atrophin-1, the DRPLA gene product, interacts with two families of WW RT domain-containing proteins."; RL Mol. Cell. Neurosci. 11:149-160(1998). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 152-371. RX PubMed=9169421; DOI=10.1074/jbc.272.23.14611; RA Pirozzi G., McConnell S.J., Uveges A.J., Carter J.M., Sparks A.B., RA Kay B.K., Fowlkes D.M.; RT "Identification of novel human WW domain-containing proteins by cloning of RT ligand targets."; RL J. Biol. Chem. 272:14611-14616(1997). RN [7] RP INTERACTION WITH RAPGEF2. RX PubMed=11168587; DOI=10.1046/j.1365-2443.2000.00385.x; RA Mino A., Ohtsuka T., Inoue E., Takai Y.; RT "Membrane-associated guanylate kinase with inverted orientation (MAGI)- RT 1/brain angiogenesis inhibitor 1-associated protein (BAP1) as a scaffolding RT molecule for Rap small G protein GDP/GTP exchange protein at tight RT junctions."; RL Genes Cells 5:1009-1016(2000). RN [8] RP INTERACTION WITH SYNPO AND ACTN4. RX PubMed=12042308; DOI=10.1074/jbc.m203072200; RA Patrie K.M., Drescher A.J., Welihinda A., Mundel P., Margolis B.; RT "Interaction of two actin-binding proteins, synaptopodin and alpha-actinin- RT 4, with the tight junction protein MAGI-1."; RL J. Biol. Chem. 277:30183-30190(2002). RN [9] RP INTERACTION WITH IGSF5. RX PubMed=12773569; DOI=10.1128/mcb.23.12.4267-4282.2003; RA Hirabayashi S., Tajima M., Yao I., Nishimura W., Mori H., Hata Y.; RT "JAM4, a junctional cell adhesion molecule interacting with a tight RT junction protein, MAGI-1."; RL Mol. Cell. Biol. 23:4267-4282(2003). RN [10] RP INTERACTION WITH FCHSD2. RX PubMed=14627983; DOI=10.1038/sj.onc.1206996; RA Ohno H., Hirabayashi S., Kansaku A., Yao I., Tajima M., Nishimura W., RA Ohnishi H., Mashima H., Fujita T., Omata M., Hata Y.; RT "Carom: a novel membrane-associated guanylate kinase-interacting protein RT with two SH3 domains."; RL Oncogene 22:8422-8431(2003). RN [11] RP INTERACTION WITH ASIC3. RX PubMed=15317815; DOI=10.1074/jbc.m405874200; RA Hruska-Hageman A.M., Benson C.J., Leonard A.S., Price M.P., Welsh M.J.; RT "PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have RT opposite effects on H+- gated current."; RL J. Biol. Chem. 279:46962-46968(2004). RN [12] RP INTERACTION WITH AMOT. RX PubMed=16043488; DOI=10.1074/jbc.m503915200; RA Bratt A., Birot O., Sinha I., Veitonmaeki N., Aase K., Ernkvist M., RA Holmgren L.; RT "Angiomotin regulates endothelial cell-cell junctions and cell motility."; RL J. Biol. Chem. 280:34859-34869(2005). RN [13] RP INTERACTION WITH DDN. RX PubMed=16751601; DOI=10.1093/jb/mvj105; RA Kawata A., Iida J., Ikeda M., Sato Y., Mori H., Kansaku A., Sumita K., RA Fujiwara N., Rokukawa C., Hamano M., Hirabayashi S., Hata Y.; RT "CIN85 is localized at synapses and forms a complex with S-SCAM via RT dendrin."; RL J. Biochem. 139:931-939(2006). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-730; SER-741 AND SER-1361, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [15] RP INTERACTION WITH PRRG4. RX PubMed=23873930; DOI=10.1074/jbc.m113.484683; RA Yazicioglu M.N., Monaldini L., Chu K., Khazi F.R., Murphy S.L., Huang H., RA Margaritis P., High K.A.; RT "Cellular localization and characterization of cytosolic binding partners RT for Gla domain-containing proteins PRRG4 and PRRG2."; RL J. Biol. Chem. 288:25908-25914(2013). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1412, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [17] RP INTERACTION WITH KCNJ10. RX PubMed=24561201; DOI=10.1016/j.febslet.2014.02.024; RA Tanemoto M., Abe T., Uchida S., Kawahara K.; RT "Mislocalization of K+ channels causes the renal salt wasting in RT EAST/SeSAME syndrome."; RL FEBS Lett. 588:899-905(2014). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357 AND SER-1071, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [19] RP STRUCTURE BY NMR OF 295-401. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of WW domains from the human membrane-associated RT guanylate kinase, WW and PDZ domain-containing protein 1. MAGI-1."; RL Submitted (APR-2008) to the PDB data bank. CC -!- FUNCTION: May play a role as scaffolding protein at cell-cell CC junctions. May regulate acid-induced ASIC3 currents by modulating its CC expression at the cell surface (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts through its WW 2 domain with SYNPO and through its CC PDZ 5 domain with ACTN4 (PubMed:12042308). Interacts with cytoplasmic CC domain of ADGRB1 (PubMed:9647739). Interacts via its WW domains with CC DRPLA (PubMed:9647693). Interacts with ESAM, LRP2 and CXADR (By CC similarity). May interact with CTNNB1 (By similarity). Interacts CC through its PDZ 1 domain with NET1 (By similarity). Interacts with CC ASIC3 and AMOT (PubMed:15317815, PubMed:16043488). Interacts with CC FCHSD2 (PubMed:14627983). Interacts with IGSF5/JAM4 and through its PDZ CC 2 and 3 domains with NPHS1 forming a tripartite complex (By similarity) CC (PubMed:12773569). Interacts with DDN (PubMed:16751601). Isoform 3 (via CC PDZ domain) interacts with RAPGEF2 (PubMed:11168587). Interacts with CC DLL1 (By similarity). Interacts with KCNJ10 and possibly with CC KCNJ10/KCNJ16 heterodimer; this interaction may facilitate CC KCNJ10/KCNJ16 potassium channel expression at the basolateral membrane CC in kidney tubular cells. Interacts with PRRG4 (via cytoplasmic domain) CC (PubMed:23873930). {ECO:0000250|UniProtKB:Q4L1J4, CC ECO:0000250|UniProtKB:Q6RHR9, ECO:0000269|PubMed:11168587, CC ECO:0000269|PubMed:12042308, ECO:0000269|PubMed:12773569, CC ECO:0000269|PubMed:14627983, ECO:0000269|PubMed:15317815, CC ECO:0000269|PubMed:16043488, ECO:0000269|PubMed:16751601, CC ECO:0000269|PubMed:23873930, ECO:0000269|PubMed:9647693, CC ECO:0000269|PubMed:9647739}. CC -!- INTERACTION: CC Q96QZ7; O94868: FCHSD2; NbExp=5; IntAct=EBI-924464, EBI-1215612; CC Q96QZ7; P46940: IQGAP1; NbExp=4; IntAct=EBI-924464, EBI-297509; CC Q96QZ7; O60333-3: KIF1B; NbExp=3; IntAct=EBI-924464, EBI-465669; CC Q96QZ7; P03126: E6; Xeno; NbExp=2; IntAct=EBI-924464, EBI-1177242; CC Q96QZ7; P06463: E6; Xeno; NbExp=4; IntAct=EBI-924464, EBI-1186926; CC Q96QZ7; P0DOF2: M; Xeno; NbExp=2; IntAct=EBI-924464, EBI-25567776; CC Q96QZ7-3; Q9Y4G8: RAPGEF2; NbExp=2; IntAct=EBI-8769674, EBI-307079; CC Q96QZ7-3; Q9BPW5: RASL11B; NbExp=3; IntAct=EBI-8769674, EBI-745409; CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction CC {ECO:0000269|PubMed:11969287}. Cell membrane CC {ECO:0000269|PubMed:11969287}; Peripheral membrane protein CC {ECO:0000269|PubMed:11969287}. Note=Localizes to epithelial cells tight CC junctions. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Comment=Additional isoforms seem to exist.; CC Name=1; Synonyms=MAGI-1C-alpha-beta1; CC IsoId=Q96QZ7-1; Sequence=Displayed; CC Name=2; Synonyms=MAGI-1C-beta; CC IsoId=Q96QZ7-2; Sequence=VSP_011664, VSP_011666; CC Name=3; Synonyms=MAGI-1A-alpha-beta1; CC IsoId=Q96QZ7-3; Sequence=VSP_011670, VSP_011671, VSP_011672; CC Name=4; Synonyms=MAGI-1A-alpha; CC IsoId=Q96QZ7-4; Sequence=VSP_011664, VSP_011666, VSP_011667, CC VSP_011668, VSP_011670, VSP_011671, CC VSP_011672; CC Name=5; Synonyms=MAGI-1B-alpha-beta; CC IsoId=Q96QZ7-5; Sequence=VSP_011666, VSP_011669, VSP_011672; CC Name=6; Synonyms=MAGI-1C-beta2; CC IsoId=Q96QZ7-6; Sequence=VSP_011664, VSP_011666, VSP_011667; CC Name=7; Synonyms=MAGI-1C-beta3; CC IsoId=Q96QZ7-7; Sequence=VSP_011664, VSP_011665; CC -!- TISSUE SPECIFICITY: Widely expressed with the exception of skeletal CC muscle. Isoform 1, isoform 2 and isoform 6 are highly expressed in CC colon, kidney, lung, liver, and pancreas. Isoform 5 is predominantly CC expressed in brain and heart. Isoform 3 and isoform 4 are highly CC expressed in pancreas and brain. {ECO:0000269|PubMed:11969287, CC ECO:0000269|PubMed:9647693, ECO:0000269|PubMed:9647739}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB010894; BAA32002.1; -; mRNA. DR EMBL; AF401655; AAK94065.1; -; mRNA. DR EMBL; AF401656; AAK94066.1; -; mRNA. DR EMBL; AF401654; AAK94064.1; -; mRNA. DR EMBL; AK289803; BAF82492.1; -; mRNA. DR EMBL; AC104438; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC112516; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC121493; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC145425; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; U80754; AAC04844.1; -; mRNA. DR EMBL; U96115; AAC51326.1; ALT_TERM; mRNA. DR CCDS; CCDS2904.1; -. [Q96QZ7-3] DR CCDS; CCDS33780.1; -. [Q96QZ7-2] DR CCDS; CCDS33781.1; -. [Q96QZ7-5] DR PIR; JE0209; JE0209. DR RefSeq; NP_001028229.1; NM_001033057.1. [Q96QZ7-2] DR RefSeq; NP_004733.2; NM_004742.2. [Q96QZ7-3] DR RefSeq; NP_056335.1; NM_015520.1. [Q96QZ7-5] DR RefSeq; XP_005265621.1; XM_005265564.1. DR PDB; 1WBP; X-ray; 2.40 A; B=1382-1390. DR PDB; 2KPK; NMR; -; A=455-580. DR PDB; 2KPL; NMR; -; A=455-580. DR PDB; 2Q9V; X-ray; 2.00 A; A=839-922. DR PDB; 2R4H; X-ray; 2.05 A; A/B/C=1149-1233. DR PDB; 2YSD; NMR; -; A=295-338. DR PDB; 2YSE; NMR; -; A=355-401. DR PDB; 2ZAJ; NMR; -; A=355-390. DR PDB; 3BPU; X-ray; 1.60 A; A=640-721. DR PDB; 5N7D; X-ray; 2.30 A; A/B=455-558. DR PDB; 5N7F; X-ray; 2.30 A; A/B=454-558. DR PDB; 5N7G; X-ray; 2.95 A; A/B=455-558. DR PDB; 6TWU; X-ray; 2.40 A; A/B=458-558. DR PDB; 6TWX; X-ray; 2.30 A; A/B=455-558. DR PDB; 6TWY; X-ray; 2.30 A; A/B=458-558. DR PDB; 7P71; X-ray; 2.60 A; A/B=455-558. DR PDBsum; 1WBP; -. DR PDBsum; 2KPK; -. DR PDBsum; 2KPL; -. DR PDBsum; 2Q9V; -. DR PDBsum; 2R4H; -. DR PDBsum; 2YSD; -. DR PDBsum; 2YSE; -. DR PDBsum; 2ZAJ; -. DR PDBsum; 3BPU; -. DR PDBsum; 5N7D; -. DR PDBsum; 5N7F; -. DR PDBsum; 5N7G; -. DR PDBsum; 6TWU; -. DR PDBsum; 6TWX; -. DR PDBsum; 6TWY; -. DR PDBsum; 7P71; -. DR AlphaFoldDB; Q96QZ7; -. DR BMRB; Q96QZ7; -. DR PCDDB; Q96QZ7; -. DR SMR; Q96QZ7; -. DR BioGRID; 114655; 134. DR ELM; Q96QZ7; -. DR IntAct; Q96QZ7; 99. DR MINT; Q96QZ7; -. DR STRING; 9606.ENSP00000385450; -. DR ChEMBL; CHEMBL4295927; -. DR iPTMnet; Q96QZ7; -. DR PhosphoSitePlus; Q96QZ7; -. DR BioMuta; MAGI1; -. DR DMDM; 281185501; -. DR EPD; Q96QZ7; -. DR jPOST; Q96QZ7; -. DR MassIVE; Q96QZ7; -. DR MaxQB; Q96QZ7; -. DR PaxDb; 9606-ENSP00000385450; -. DR PeptideAtlas; Q96QZ7; -. DR ProteomicsDB; 77914; -. [Q96QZ7-1] DR ProteomicsDB; 77915; -. [Q96QZ7-2] DR ProteomicsDB; 77916; -. [Q96QZ7-3] DR ProteomicsDB; 77917; -. [Q96QZ7-4] DR ProteomicsDB; 77918; -. [Q96QZ7-5] DR ProteomicsDB; 77919; -. [Q96QZ7-6] DR ProteomicsDB; 77920; -. [Q96QZ7-7] DR Pumba; Q96QZ7; -. DR Antibodypedia; 15389; 214 antibodies from 26 providers. DR DNASU; 9223; -. DR Ensembl; ENST00000330909.12; ENSP00000331157.7; ENSG00000151276.24. [Q96QZ7-5] DR Ensembl; ENST00000402939.7; ENSP00000385450.2; ENSG00000151276.24. [Q96QZ7-2] DR Ensembl; ENST00000483466.5; ENSP00000420323.1; ENSG00000151276.24. [Q96QZ7-3] DR Ensembl; ENST00000497477.6; ENSP00000424369.1; ENSG00000151276.24. [Q96QZ7-4] DR GeneID; 9223; -. DR KEGG; hsa:9223; -. DR MANE-Select; ENST00000402939.7; ENSP00000385450.2; NM_001033057.2; NP_001028229.1. [Q96QZ7-2] DR UCSC; uc003dmm.4; human. [Q96QZ7-1] DR AGR; HGNC:946; -. DR CTD; 9223; -. DR DisGeNET; 9223; -. DR GeneCards; MAGI1; -. DR HGNC; HGNC:946; MAGI1. DR HPA; ENSG00000151276; Low tissue specificity. DR MIM; 602625; gene. DR neXtProt; NX_Q96QZ7; -. DR OpenTargets; ENSG00000151276; -. DR PharmGKB; PA164742006; -. DR VEuPathDB; HostDB:ENSG00000151276; -. DR eggNOG; KOG3209; Eukaryota. DR GeneTree; ENSGT00940000155820; -. DR HOGENOM; CLU_004562_1_0_1; -. DR InParanoid; Q96QZ7; -. DR OMA; PPTYLYN; -. DR OrthoDB; 2902917at2759; -. DR PhylomeDB; Q96QZ7; -. DR TreeFam; TF316816; -. DR PathwayCommons; Q96QZ7; -. DR SignaLink; Q96QZ7; -. DR SIGNOR; Q96QZ7; -. DR BioGRID-ORCS; 9223; 15 hits in 1151 CRISPR screens. DR ChiTaRS; MAGI1; human. DR EvolutionaryTrace; Q96QZ7; -. DR GeneWiki; MAGI1; -. DR GenomeRNAi; 9223; -. DR Pharos; Q96QZ7; Tbio. DR PRO; PR:Q96QZ7; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q96QZ7; Protein. DR Bgee; ENSG00000151276; Expressed in ventricular zone and 112 other cell types or tissues. DR ExpressionAtlas; Q96QZ7; baseline and differential. DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB. DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell. DR GO; GO:0030054; C:cell junction; IDA:HPA. DR GO; GO:0071944; C:cell periphery; IDA:ARUK-UCL. DR GO; GO:0042995; C:cell projection; IDA:UniProtKB. DR GO; GO:0005911; C:cell-cell junction; IDA:ARUK-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL. DR GO; GO:0051393; F:alpha-actinin binding; IPI:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc. DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc. DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IDA:ARUK-UCL. DR GO; GO:0065003; P:protein-containing complex assembly; NAS:ProtInc. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR CDD; cd00992; PDZ_signaling; 5. DR CDD; cd00201; WW; 2. DR Gene3D; 2.20.70.10; -; 2. DR Gene3D; 2.30.42.10; -; 6. DR Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1. DR IDEAL; IID00420; -. DR InterPro; IPR008145; GK/Ca_channel_bsu. DR InterPro; IPR008144; Guanylate_kin-like_dom. DR InterPro; IPR020590; Guanylate_kinase_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR InterPro; IPR001202; WW_dom. DR InterPro; IPR036020; WW_dom_sf. DR PANTHER; PTHR10316; MEMBRANE ASSOCIATED GUANYLATE KINASE-RELATED; 1. DR PANTHER; PTHR10316:SF12; MEMBRANE-ASSOCIATED GUANYLATE KINASE, WW AND PDZ DOMAIN-CONTAINING PROTEIN 1; 1. DR Pfam; PF00625; Guanylate_kin; 1. DR Pfam; PF16663; MAGI_u1; 1. DR Pfam; PF16666; MAGI_u5; 1. DR Pfam; PF00595; PDZ; 5. DR Pfam; PF00397; WW; 2. DR SMART; SM00072; GuKc; 1. DR SMART; SM00228; PDZ; 6. DR SMART; SM00456; WW; 2. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50156; PDZ domain-like; 6. DR SUPFAM; SSF51045; WW domain; 2. DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1. DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1. DR PROSITE; PS50106; PDZ; 6. DR PROSITE; PS01159; WW_DOMAIN_1; 2. DR PROSITE; PS50020; WW_DOMAIN_2; 2. DR Genevisible; Q96QZ7; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Cell junction; KW Cell membrane; Membrane; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Repeat; Tight junction. FT CHAIN 1..1491 FT /note="Membrane-associated guanylate kinase, WW and PDZ FT domain-containing protein 1" FT /id="PRO_0000094589" FT DOMAIN 17..105 FT /note="PDZ 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 96..287 FT /note="Guanylate kinase-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100" FT DOMAIN 300..333 FT /note="WW 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224" FT DOMAIN 359..392 FT /note="WW 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224" FT DOMAIN 472..554 FT /note="PDZ 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 643..721 FT /note="PDZ 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 813..895 FT /note="PDZ 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 970..1066 FT /note="PDZ 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 1124..1206 FT /note="PDZ 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT REGION 236..267 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 411..462 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 586..623 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 720..832 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 932..987 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 970..1066 FT /note="Interaction with FCHSD2" FT /evidence="ECO:0000269|PubMed:14627983" FT REGION 1112..1143 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1234..1491 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 411..427 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 587..601 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 737..766 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 935..982 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1281..1338 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1346..1485 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 103..110 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100" FT MOD_RES 357 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 730 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 741 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 800 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6RHR9" FT MOD_RES 1071 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 1361 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 1412 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 806..834 FT /note="PMSPSPASGLSKGEREREINSTNFGECPI -> L (in isoform 2, FT isoform 4, isoform 6 and isoform 7)" FT /evidence="ECO:0000303|PubMed:11969287" FT /id="VSP_011664" FT VAR_SEQ 1023..1099 FT /note="GTTFAGNACVAMPHKIGRIIEGSPADRCGKLKVGDRILAVNGCSITNKSHSD FT IVNLIKEAGNTVTLRIIPGDESSNA -> VMQCQPPSWCHSALGGSKHCNSVMGAASLE FT VQIYSCNNP (in isoform 7)" FT /evidence="ECO:0000305" FT /id="VSP_011665" FT VAR_SEQ 1027 FT /note="Missing (in isoform 2, isoform 4, isoform 5 and FT isoform 6)" FT /evidence="ECO:0000303|PubMed:11969287" FT /id="VSP_011666" FT VAR_SEQ 1028..1038 FT /note="Missing (in isoform 4 and isoform 6)" FT /evidence="ECO:0000303|PubMed:11969287" FT /id="VSP_011667" FT VAR_SEQ 1039..1094 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:11969287" FT /id="VSP_011668" FT VAR_SEQ 1241..1288 FT /note="DPSSDRHGPATGPQGVPEVRAGPDRRQHPSLESSYPPDLHKSSPHGEK -> FT AMIPPNIAACMRNEKLGEACFYLMGHNQTTTPAATATAPPPVHKVFRK (in FT isoform 5)" FT /evidence="ECO:0000303|PubMed:11969287" FT /id="VSP_011669" FT VAR_SEQ 1241..1256 FT /note="DPSSDRHGPATGPQGV -> GGSNYENIPSFPGMTP (in isoform 3 FT and isoform 4)" FT /evidence="ECO:0000303|PubMed:11969287, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:9647739" FT /id="VSP_011670" FT VAR_SEQ 1257..1288 FT /note="Missing (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:11969287, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:9647739" FT /id="VSP_011671" FT VAR_SEQ 1289..1491 FT /note="Missing (in isoform 3, isoform 4 and isoform 5)" FT /evidence="ECO:0000303|PubMed:11969287, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:9647739" FT /id="VSP_011672" FT CONFLICT 124 FT /note="S -> F (in Ref. 1; BAA32002 and 2; FT AAK94064/AAK94065/AAK94066/AAC51326)" FT /evidence="ECO:0000305" FT CONFLICT 428 FT /note="D -> H (in Ref. 3; BAF82492)" FT /evidence="ECO:0000305" FT CONFLICT 775 FT /note="A -> G (in Ref. 5; AAC04844)" FT /evidence="ECO:0000305" FT CONFLICT 1001 FT /note="I -> T (in Ref. 3; BAF82492)" FT /evidence="ECO:0000305" FT STRAND 304..310 FT /evidence="ECO:0007829|PDB:2YSD" FT STRAND 316..320 FT /evidence="ECO:0007829|PDB:2YSD" FT TURN 321..324 FT /evidence="ECO:0007829|PDB:2YSD" FT STRAND 325..329 FT /evidence="ECO:0007829|PDB:2YSD" FT TURN 331..333 FT /evidence="ECO:0007829|PDB:2YSD" FT STRAND 363..369 FT /evidence="ECO:0007829|PDB:2YSE" FT STRAND 371..373 FT /evidence="ECO:0007829|PDB:2YSE" FT STRAND 375..379 FT /evidence="ECO:0007829|PDB:2YSE" FT TURN 380..383 FT /evidence="ECO:0007829|PDB:2YSE" FT STRAND 384..388 FT /evidence="ECO:0007829|PDB:2YSE" FT HELIX 390..398 FT /evidence="ECO:0007829|PDB:2YSE" FT HELIX 463..465 FT /evidence="ECO:0007829|PDB:5N7D" FT STRAND 468..476 FT /evidence="ECO:0007829|PDB:5N7D" FT STRAND 479..481 FT /evidence="ECO:0007829|PDB:2KPL" FT STRAND 483..487 FT /evidence="ECO:0007829|PDB:5N7D" FT STRAND 491..493 FT /evidence="ECO:0007829|PDB:6TWX" FT STRAND 497..501 FT /evidence="ECO:0007829|PDB:5N7D" FT STRAND 503..505 FT /evidence="ECO:0007829|PDB:7P71" FT HELIX 506..510 FT /evidence="ECO:0007829|PDB:5N7D" FT STRAND 518..522 FT /evidence="ECO:0007829|PDB:5N7D" FT HELIX 532..541 FT /evidence="ECO:0007829|PDB:5N7D" FT STRAND 547..554 FT /evidence="ECO:0007829|PDB:5N7D" FT STRAND 568..570 FT /evidence="ECO:0007829|PDB:2KPK" FT STRAND 640..647 FT /evidence="ECO:0007829|PDB:3BPU" FT STRAND 652..654 FT /evidence="ECO:0007829|PDB:3BPU" FT STRAND 656..659 FT /evidence="ECO:0007829|PDB:3BPU" FT STRAND 663..670 FT /evidence="ECO:0007829|PDB:3BPU" FT STRAND 685..689 FT /evidence="ECO:0007829|PDB:3BPU" FT HELIX 699..707 FT /evidence="ECO:0007829|PDB:3BPU" FT STRAND 714..721 FT /evidence="ECO:0007829|PDB:3BPU" FT STRAND 839..845 FT /evidence="ECO:0007829|PDB:2Q9V" FT STRAND 853..857 FT /evidence="ECO:0007829|PDB:2Q9V" FT STRAND 865..870 FT /evidence="ECO:0007829|PDB:2Q9V" FT HELIX 875..879 FT /evidence="ECO:0007829|PDB:2Q9V" FT STRAND 887..891 FT /evidence="ECO:0007829|PDB:2Q9V" FT HELIX 901..914 FT /evidence="ECO:0007829|PDB:2Q9V" FT STRAND 916..922 FT /evidence="ECO:0007829|PDB:2Q9V" FT STRAND 1150..1156 FT /evidence="ECO:0007829|PDB:2R4H" FT STRAND 1163..1168 FT /evidence="ECO:0007829|PDB:2R4H" FT HELIX 1170..1172 FT /evidence="ECO:0007829|PDB:2R4H" FT STRAND 1176..1181 FT /evidence="ECO:0007829|PDB:2R4H" FT HELIX 1186..1189 FT /evidence="ECO:0007829|PDB:2R4H" FT STRAND 1198..1202 FT /evidence="ECO:0007829|PDB:2R4H" FT HELIX 1212..1220 FT /evidence="ECO:0007829|PDB:2R4H" FT TURN 1221..1224 FT /evidence="ECO:0007829|PDB:2R4H" FT STRAND 1225..1231 FT /evidence="ECO:0007829|PDB:2R4H" SQ SEQUENCE 1491 AA; 164581 MW; 4B2EE05243A6FA65 CRC64; MSKVIQKKNH WTSRVHECTV KRGPQGELGV TVLGGAEHGE FPYVGAVAAV EAAGLPGGGE GPRLGEGELL LEVQGVRVSG LPRYDVLGVI DSCKEAVTFK AVRQGGRLNK DLRHFLNQRF QKGSPDHELQ QTIRDNLYRH AVPCTTRSPR EGEVPGVDYN FLTVKEFLDL EQSGTLLEVG TYEGNYYGTP KPPSQPVSGK VITTDALHSL QSGSKQSTPK RTKSYNDMQN AGIVHAENEE EDDVPEMNSS FTADSGEQEE HTLQETALPP VNSSIIAAPI TDPSQKFPQY LPLSAEDNLG PLPENWEMAY TENGEVYFID HNTKTTSWLD PRCLNKQQKP LEECEDDEGV HTEELDSELE LPAGWEKIED PVYGIYYVDH INRKTQYENP VLEAKRKKQL EQQQQQQQQQ QQQQQQQQQQ QTEEWTEDHS ALVPPVIPNH PPSNPEPARE VPLQGKPFFT RNPSELKGKF IHTKLRKSSR GFGFTVVGGD EPDEFLQIKS LVLDGPAALD GKMETGDVIV SVNDTCVLGH THAQVVKIFQ SIPIGASVDL ELCRGYPLPF DPDDPNTSLV TSVAILDKEP IIVNGQETYD SPASHSSKTG KVNGMKDARP SSPADVASNS SHGYPNDTVS LASSIATQPE LITVHIVKGP MGFGFTIADS PGGGGQRVKQ IVDSPRCRGL KEGDLIVEVN KKNVQALTHN QVVDMLVECP KGSEVTLLVQ RGGLPVPKKS PKSQPLERKD SQNSSQHSVS SHRSLHTASP SHSTQVLPEF PPAEAQAPDQ TDSSGQKKPD PFKIWAQSRS MYENRPMSPS PASGLSKGER EREINSTNFG ECPIPDYQEQ DIFLWRKETG FGFRILGGNE PGEPIYIGHI VPLGAADTDG RLRSGDELIC VDGTPVIGKS HQLVVQLMQQ AAKQGHVNLT VRRKVVFAVP KTENEVPSPA SSHHSSNQPA SLTEEKRTPQ GSQNSLNTVS SGSGSTSGIG SGGGGGSGVV STVVQPYDVE IRRGENEGFG FVIVSSVSRP EAGTTFAGNA CVAMPHKIGR IIEGSPADRC GKLKVGDRIL AVNGCSITNK SHSDIVNLIK EAGNTVTLRI IPGDESSNAT LLTNAEKIAT ITTTHTPSQQ GTQETRNTTK PKQESQFEFK APQATQEQDF YTVELERGAK GFGFSLRGGR EYNMDLYVLR LAEDGPAERC GKMRIGDEIL EINGETTKNM KHSRAIELIK NGGRRVRLFL KRGDGSVPEY DPSSDRHGPA TGPQGVPEVR AGPDRRQHPS LESSYPPDLH KSSPHGEKRA HARDPKGSRE YSRQPNEHHT WNGTSRKPDS GACRPKDRAP EGRRDAQAER AAAANGPKRR SPEKRREGTR SADNTLERRE KHEKRRDVSP ERRRERSPTR RRDGSPSRRR RSLERLLEQR RSPERRRGGS PERRAKSTDR RRARSPERRR ERSLDKRNRE DRASHREREE ANLKQDAGRS SRHPPEQRRR PYKECSTDLS I //