MAGI1_HUMAN
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 03-AUG-2022, entry version 198.
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 Q96QZ7-3; 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}.
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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 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 AlphaFoldDB; Q96QZ7; -.
DR BMRB; Q96QZ7; -.
DR PCDDB; Q96QZ7; -.
DR SMR; Q96QZ7; -.
DR BioGRID; 114655; 129.
DR ELM; Q96QZ7; -.
DR IntAct; Q96QZ7; 77.
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; Q96QZ7; -.
DR PeptideAtlas; Q96QZ7; -.
DR PRIDE; 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 Antibodypedia; 15389; 193 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 Ensembl; ENST00000634409.1; ENSP00000489444.1; ENSG00000282956.1. [Q96QZ7-2]
DR Ensembl; ENST00000634774.1; ENSP00000489393.1; ENSG00000282956.1. [Q96QZ7-5]
DR Ensembl; ENST00000635378.1; ENSP00000489391.1; ENSG00000282956.1. [Q96QZ7-3]
DR Ensembl; ENST00000635471.1; ENSP00000489322.1; ENSG00000282956.1. [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 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; QQWIEDS; -.
DR OrthoDB; 284488at2759; -.
DR PhylomeDB; Q96QZ7; -.
DR TreeFam; TF316816; -.
DR PathwayCommons; Q96QZ7; -.
DR SignaLink; Q96QZ7; -.
DR BioGRID-ORCS; 9223; 13 hits in 1073 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 110 other tissues.
DR ExpressionAtlas; Q96QZ7; baseline and differential.
DR Genevisible; Q96QZ7; HS.
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:0060090; F:molecular adaptor activity; IEA:InterPro.
DR GO; GO:0008022; F:protein C-terminus binding; TAS:ProtInc.
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; cd00201; WW; 2.
DR Gene3D; 2.30.42.10; -; 6.
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; IPR030033; MAGI1.
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:SF12; PTHR10316:SF12; 1.
DR Pfam; PF00625; Guanylate_kin; 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; SSF50156; SSF50156; 6.
DR SUPFAM; SSF51045; SSF51045; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
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.
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; AAK94064/
FT 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 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
