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Database: UniProt
Entry: Q96QZ7
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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   29-SEP-2021, entry version 195.
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   BMRB; Q96QZ7; -.
DR   PCDDB; Q96QZ7; -.
DR   SMR; Q96QZ7; -.
DR   BioGRID; 114655; 108.
DR   ELM; Q96QZ7; -.
DR   IntAct; Q96QZ7; 74.
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; 190 antibodies.
DR   DNASU; 9223; -.
DR   Ensembl; ENST00000330909; ENSP00000331157; ENSG00000151276. [Q96QZ7-5]
DR   Ensembl; ENST00000402939; ENSP00000385450; ENSG00000151276. [Q96QZ7-2]
DR   Ensembl; ENST00000483466; ENSP00000420323; ENSG00000151276. [Q96QZ7-3]
DR   Ensembl; ENST00000497477; ENSP00000424369; ENSG00000151276. [Q96QZ7-4]
DR   Ensembl; ENST00000634409; ENSP00000489444; ENSG00000282956. [Q96QZ7-2]
DR   Ensembl; ENST00000634774; ENSP00000489393; ENSG00000282956. [Q96QZ7-5]
DR   Ensembl; ENST00000635378; ENSP00000489391; ENSG00000282956. [Q96QZ7-3]
DR   Ensembl; ENST00000635471; ENSP00000489322; ENSG00000282956. [Q96QZ7-4]
DR   GeneID; 9223; -.
DR   KEGG; hsa:9223; -.
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; HNAGIGP; -.
DR   OrthoDB; 284488at2759; -.
DR   PhylomeDB; Q96QZ7; -.
DR   TreeFam; TF316816; -.
DR   PathwayCommons; Q96QZ7; -.
DR   SignaLink; Q96QZ7; -.
DR   BioGRID-ORCS; 9223; 6 hits in 1012 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 stomach and 235 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   NP_BIND         103..110
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
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   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
//
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