MAGI3_HUMAN
ID MAGI3_HUMAN Reviewed; 1481 AA.
AC Q5TCQ9; A0A024R0E9; A0A024R0H3; Q5TCQ8; Q5TCR0; Q9H2V6; Q9H5Y8; Q9HBC4;
AC Q9HCD8;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3;
DE AltName: Full=Membrane-associated guanylate kinase inverted 3;
DE Short=MAGI-3;
GN Name=MAGI3; Synonyms=KIAA1634;
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 2), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INTERACTION WITH PTEN; ADGRB1 AND GRIN2B.
RC TISSUE=Mammary gland;
RX PubMed=10748157; DOI=10.1074/jbc.m909741199;
RA Wu Y., Dowbenko D., Spencer S., Laura R., Lee J., Gu Q., Lasky L.A.;
RT "Interaction of the tumor suppressor PTEN/MMAC with a PDZ domain of MAGI3,
RT a novel membrane-associated guanylate kinase.";
RL J. Biol. Chem. 275:21477-21485(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=15652357; DOI=10.1016/j.yexcr.2004.10.007;
RA Franklin J.L., Yoshiura K., Dempsey P.J., Bogatcheva G., Jeyakumar L.,
RA Meise K.S., Pearsall R.S., Threadgill D., Coffey R.J.;
RT "Identification of MAGI-3 as a transforming growth factor-alpha tail
RT binding protein.";
RL Exp. Cell Res. 303:457-470(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 252-1481 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 928-1481 (ISOFORMS 1 AND 4).
RC TISSUE=Ileal mucosa;
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 [8]
RP SUBCELLULAR LOCATION.
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 [9]
RP INTERACTION WITH HPV E6 (MICROBIAL INFECTION), AND PROBABLE UBIQUITINATION.
RX PubMed=12140759; DOI=10.1038/sj.onc.1205668;
RA Thomas M., Laura R., Hepner K., Guccione E., Sawyers C., Lasky L.,
RA Banks L.;
RT "Oncogenic human papillomavirus E6 proteins target the MAGI-2 and MAGI-3
RT proteins for degradation.";
RL Oncogene 21:5088-5096(2002).
RN [10]
RP INTERACTION WITH HPV E6 (MICROBIAL INFECTION).
RX PubMed=15507623; DOI=10.1128/jvi.78.22.12366-12377.2004;
RA Lee C., Laimins L.A.;
RT "Role of the PDZ domain-binding motif of the oncoprotein E6 in the
RT pathogenesis of human papillomavirus type 31.";
RL J. Virol. 78:12366-12377(2004).
RN [11]
RP INTERACTION WITH HPV E6 (MICROBIAL INFECTION).
RX PubMed=15378012; DOI=10.1038/sj.onc.1207977;
RA Massimi P., Gammoh N., Thomas M., Banks L.;
RT "HPV E6 specifically targets different cellular pools of its PDZ domain-
RT containing tumour suppressor substrates for proteasome-mediated
RT degradation.";
RL Oncogene 23:8033-8039(2004).
RN [12]
RP INTERACTION WITH HTLV1 TAX (MICROBIAL INFECTION).
RX PubMed=15003862; DOI=10.1016/j.virol.2003.11.014;
RA Ohashi M., Sakurai M., Higuchi M., Mori N., Fukushi M., Oie M.,
RA Coffey R.J., Yoshiura K., Tanaka Y., Uchiyama M., Hatanaka M., Fujii M.;
RT "Human T-cell leukemia virus type 1 Tax oncoprotein induces and interacts
RT with a multi-PDZ domain protein, MAGI-3.";
RL Virology 320:52-62(2004).
RN [13]
RP LIGANDS THAT BIND AND INHIBIT PDZ DOMAINS.
RX PubMed=17055267; DOI=10.1016/j.bmcl.2006.10.006;
RA Fujii N., Haresco J.J., Novak K.A., Gage R.M., Pedemonte N., Stokoe D.,
RA Kuntz I.D., Guy R.K.;
RT "Rational design of a nonpeptide general chemical scaffold for reversible
RT inhibition of PDZ domain interactions.";
RL Bioorg. Med. Chem. Lett. 17:549-552(2007).
RN [14]
RP INTERACTION WITH LPAR2.
RX PubMed=16904289; DOI=10.1016/j.cellsig.2006.06.008;
RA Zhang H., Wang D., Sun H., Hall R.A., Yun C.C.;
RT "MAGI-3 regulates LPA-induced activation of Erk and RhoA.";
RL Cell. Signal. 19:261-268(2007).
RN [15]
RP INTERACTION WITH HPV E6 (MICROBIAL INFECTION), AND PROBABLE UBIQUITINATION.
RX PubMed=17934525; DOI=10.1038/sj.onc.1210810;
RA Massimi P., Shai A., Lambert P., Banks L.;
RT "HPV E6 degradation of p53 and PDZ containing substrates in an E6AP null
RT background.";
RL Oncogene 27:1800-1804(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-595 AND SER-832, AND
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Acts as a scaffolding protein at cell-cell junctions, thereby
CC regulating various cellular and signaling processes. Cooperates with
CC PTEN to modulate the kinase activity of AKT1. Its interaction with
CC PTPRB and tyrosine phosphorylated proteins suggests that it may link
CC receptor tyrosine phosphatase with its substrates at the plasma
CC membrane. In polarized epithelial cells, involved in efficient
CC trafficking of TGFA to the cell surface. Regulates the ability of LPAR2
CC to activate ERK and RhoA pathways. Regulates the JNK signaling cascade
CC via its interaction with FZD4 and VANGL2.
CC {ECO:0000269|PubMed:10748157}.
CC -!- SUBUNIT: Interacts with ADRB1, FZD4, FZD7, PTPRB, TGFA and VANGL2.
CC Interacts with unidentified tyrosine phosphorylated proteins (By
CC similarity). Interacts with ADGRB1, LPAR2/EDG4, GRIN2B and PTEN. Does
CC not interact with HTLV TAX2 or TAX3 proteins. Interacts with DLL1 (By
CC similarity). Interacts with PRRG4 (via cytoplasmic domain)
CC (PubMed:23873930). {ECO:0000250, ECO:0000250|UniProtKB:Q9EQJ9,
CC ECO:0000269|PubMed:10748157, ECO:0000269|PubMed:16904289,
CC ECO:0000269|PubMed:23873930}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HTLV1 Tax protein,
CC possibly affecting the transformation ability of Tax.
CC {ECO:0000269|PubMed:15003862}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human papillomavirus/HPV
CC type 16 and 18 E6 proteins. {ECO:0000269|PubMed:12140759,
CC ECO:0000269|PubMed:15378012, ECO:0000269|PubMed:15507623,
CC ECO:0000269|PubMed:17934525}.
CC -!- INTERACTION:
CC Q5TCQ9; P08588: ADRB1; NbExp=5; IntAct=EBI-310506, EBI-991009;
CC Q5TCQ9; P07550: ADRB2; NbExp=9; IntAct=EBI-310506, EBI-491169;
CC Q5TCQ9; Q9H204: MED28; NbExp=2; IntAct=EBI-310506, EBI-514199;
CC Q5TCQ9; Q9BZD6: PRRG4; NbExp=2; IntAct=EBI-310506, EBI-3918643;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Cell
CC junction, tight junction. Nucleus {ECO:0000250}. Note=Concentrates in
CC specific sites at the plasma membrane and in the nucleus. In epithelial
CC cells, it localizes at tight junctions (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q5TCQ9-4; Sequence=Displayed;
CC Name=4;
CC IsoId=Q5TCQ9-1; Sequence=VSP_059502;
CC Name=2;
CC IsoId=Q5TCQ9-2; Sequence=VSP_059502, VSP_059503, VSP_059504;
CC Name=3;
CC IsoId=Q5TCQ9-3; Sequence=VSP_059503, VSP_059504;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10748157}.
CC -!- PTM: Ubiquitinated following interaction with HPV E6 protein, leading
CC to its degradation by the proteasome. Degradation is independent of
CC E6AP ubiquitin ligase complex.
CC -!- MISCELLANEOUS: MAGI3 PDZ domains are used to design peptide ligands
CC that bind and inhibit PDZ domains.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15479.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15479.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF257238; AAG24545.1; -; mRNA.
DR EMBL; AF213259; AAG43837.1; -; mRNA.
DR EMBL; AL133517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL365225; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL389921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL390759; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471122; EAW56561.1; -; Genomic_DNA.
DR EMBL; CH471122; EAW56559.1; -; Genomic_DNA.
DR EMBL; CH471122; EAW56560.1; -; Genomic_DNA.
DR EMBL; CH471122; EAW56563.1; -; Genomic_DNA.
DR EMBL; CH471122; EAW56562.1; -; Genomic_DNA.
DR EMBL; BC130409; AAI30410.1; -; mRNA.
DR EMBL; AB046854; BAB13460.1; -; mRNA.
DR EMBL; AK026417; BAB15479.1; ALT_SEQ; mRNA.
DR CCDS; CCDS44196.1; -. [Q5TCQ9-4]
DR CCDS; CCDS860.1; -. [Q5TCQ9-3]
DR RefSeq; NP_001136254.1; NM_001142782.1. [Q5TCQ9-4]
DR RefSeq; NP_690864.2; NM_152900.2. [Q5TCQ9-3]
DR RefSeq; XP_005270794.1; XM_005270737.3. [Q5TCQ9-3]
DR PDB; 3SOE; X-ray; 1.60 A; A=576-666.
DR PDBsum; 3SOE; -.
DR AlphaFoldDB; Q5TCQ9; -.
DR SMR; Q5TCQ9; -.
DR BioGRID; 129277; 38.
DR IntAct; Q5TCQ9; 22.
DR MINT; Q5TCQ9; -.
DR STRING; 9606.ENSP00000304604; -.
DR ChEMBL; CHEMBL5212; -.
DR iPTMnet; Q5TCQ9; -.
DR PhosphoSitePlus; Q5TCQ9; -.
DR BioMuta; MAGI3; -.
DR DMDM; 190359882; -.
DR EPD; Q5TCQ9; -.
DR jPOST; Q5TCQ9; -.
DR MassIVE; Q5TCQ9; -.
DR MaxQB; Q5TCQ9; -.
DR PaxDb; Q5TCQ9; -.
DR PeptideAtlas; Q5TCQ9; -.
DR PRIDE; Q5TCQ9; -.
DR ProteomicsDB; 64973; -. [Q5TCQ9-1]
DR ProteomicsDB; 64974; -. [Q5TCQ9-2]
DR ProteomicsDB; 64975; -. [Q5TCQ9-3]
DR ProteomicsDB; 64976; -. [Q5TCQ9-4]
DR Antibodypedia; 1896; 76 antibodies from 22 providers.
DR DNASU; 260425; -.
DR Ensembl; ENST00000307546.14; ENSP00000304604.9; ENSG00000081026.19. [Q5TCQ9-4]
DR Ensembl; ENST00000369611.4; ENSP00000358624.4; ENSG00000081026.19. [Q5TCQ9-3]
DR Ensembl; ENST00000369615.5; ENSP00000358628.1; ENSG00000081026.19. [Q5TCQ9-3]
DR Ensembl; ENST00000369617.8; ENSP00000358630.4; ENSG00000081026.19. [Q5TCQ9-2]
DR GeneID; 260425; -.
DR KEGG; hsa:260425; -.
DR MANE-Select; ENST00000307546.14; ENSP00000304604.9; NM_001142782.2; NP_001136254.1.
DR UCSC; uc001edh.4; human. [Q5TCQ9-4]
DR CTD; 260425; -.
DR DisGeNET; 260425; -.
DR GeneCards; MAGI3; -.
DR HGNC; HGNC:29647; MAGI3.
DR HPA; ENSG00000081026; Tissue enhanced (retina).
DR MIM; 615943; gene.
DR neXtProt; NX_Q5TCQ9; -.
DR OpenTargets; ENSG00000081026; -.
DR PharmGKB; PA142671485; -.
DR VEuPathDB; HostDB:ENSG00000081026; -.
DR eggNOG; KOG0707; Eukaryota.
DR eggNOG; KOG3209; Eukaryota.
DR GeneTree; ENSGT00940000156496; -.
DR HOGENOM; CLU_004562_1_0_1; -.
DR InParanoid; Q5TCQ9; -.
DR OMA; ASYRHSW; -.
DR OrthoDB; 284488at2759; -.
DR PhylomeDB; Q5TCQ9; -.
DR TreeFam; TF316816; -.
DR PathwayCommons; Q5TCQ9; -.
DR SignaLink; Q5TCQ9; -.
DR BioGRID-ORCS; 260425; 7 hits in 1079 CRISPR screens.
DR ChiTaRS; MAGI3; human.
DR GeneWiki; MAGI3; -.
DR GenomeRNAi; 260425; -.
DR Pharos; Q5TCQ9; Tbio.
DR PRO; PR:Q5TCQ9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5TCQ9; protein.
DR Bgee; ENSG00000081026; Expressed in lower lobe of lung and 183 other tissues.
DR Genevisible; Q5TCQ9; HS.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004385; F:guanylate kinase activity; NAS:UniProtKB.
DR GO; GO:0060090; F:molecular adaptor activity; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; NAS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; NAS:UniProtKB.
DR GO; GO:0046328; P:regulation of JNK cascade; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.30.42.10; -; 6.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR030035; MAGI3.
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:SF10; PTHR10316:SF10; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 4.
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; Host-virus interaction; Membrane; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Tight junction;
KW Ubl conjugation.
FT CHAIN 1..1481
FT /note="Membrane-associated guanylate kinase, WW and PDZ
FT domain-containing protein 3"
FT /id="PRO_0000341407"
FT DOMAIN 18..106
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 114..288
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT DOMAIN 293..326
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 339..372
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 410..492
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 578..654
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 726..808
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 851..938
FT /note="PDZ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1021..1103
FT /note="PDZ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 18..106
FT /note="Interaction with ADRB1 and TGFA"
FT /evidence="ECO:0000250"
FT REGION 182..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..492
FT /note="Interaction with PTEN"
FT /evidence="ECO:0000269|PubMed:10748157"
FT REGION 542..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..808
FT /note="Interaction with ADGRB1"
FT /evidence="ECO:0000269|PubMed:10748157"
FT REGION 821..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..938
FT /note="Interaction with LPAR2 and GRIN2B"
FT /evidence="ECO:0000269|PubMed:10748157,
FT ECO:0000269|PubMed:16904289"
FT REGION 939..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1170..1481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..970
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1328..1366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1403..1447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 121..128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQJ9"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 699
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JK71"
FT MOD_RES 832
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 915
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQJ9"
FT VAR_SEQ 359
FT /note="D -> DFTLVAQAGVQWHDLGSLQPPPPGFN (in isoform 4 and
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:10748157,
FT ECO:0000303|PubMed:10997877, ECO:0000303|PubMed:15489334"
FT /id="VSP_059502"
FT VAR_SEQ 1111..1125
FT /note="DWDINNPSSSNVIYD -> LAPSGLCSYVKPEQH (in isoform 3 and
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:10748157,
FT ECO:0000303|PubMed:10997877, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15652357"
FT /id="VSP_059503"
FT VAR_SEQ 1126..1481
FT /note="Missing (in isoform 3 and isoform 2)"
FT /evidence="ECO:0000303|PubMed:10748157,
FT ECO:0000303|PubMed:10997877, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15652357"
FT /id="VSP_059504"
FT CONFLICT 9
FT /note="K -> R (in Ref. 2; AAG43837)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="V -> I (in Ref. 1; AAG24545)"
FT /evidence="ECO:0000305"
FT CONFLICT 66..68
FT /note="SPG -> NPS (in Ref. 1; AAG24545)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="E -> G (in Ref. 1; AAG24545)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="R -> G (in Ref. 2; AAG43837)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="L -> F (in Ref. 1; AAG24545)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="L -> S (in Ref. 1; AAG24545)"
FT /evidence="ECO:0000305"
FT CONFLICT 616
FT /note="G -> E (in Ref. 1; AAG24545)"
FT /evidence="ECO:0000305"
FT CONFLICT 660
FT /note="P -> T (in Ref. 1; AAG24545)"
FT /evidence="ECO:0000305"
FT CONFLICT 776
FT /note="I -> V (in Ref. 2; AAG43837)"
FT /evidence="ECO:0000305"
FT CONFLICT 798
FT /note="R -> P (in Ref. 2; AAG43837)"
FT /evidence="ECO:0000305"
FT CONFLICT 917
FT /note="D -> A (in Ref. 1; AAG24545)"
FT /evidence="ECO:0000305"
FT CONFLICT 993
FT /note="S -> P (in Ref. 2; AAG43837)"
FT /evidence="ECO:0000305"
FT STRAND 576..582
FT /evidence="ECO:0007829|PDB:3SOE"
FT STRAND 587..595
FT /evidence="ECO:0007829|PDB:3SOE"
FT STRAND 598..605
FT /evidence="ECO:0007829|PDB:3SOE"
FT HELIX 607..609
FT /evidence="ECO:0007829|PDB:3SOE"
FT STRAND 618..622
FT /evidence="ECO:0007829|PDB:3SOE"
FT HELIX 632..641
FT /evidence="ECO:0007829|PDB:3SOE"
FT STRAND 647..656
FT /evidence="ECO:0007829|PDB:3SOE"
SQ SEQUENCE 1481 AA; 162949 MW; 9C2B604D9B1B1B97 CRC64;
MSKTLKKKKH WLSKVQECAV SWAGPPGDFG AEIRGGAERG EFPYLGRLRE EPGGGTCCVV
SGKAPSPGDV LLEVNGTPVS GLTNRDTLAV IRHFREPIRL KTVKPGKVIN KDLRHYLSLQ
FQKGSIDHKL QQVIRDNLYL RTIPCTTRAP RDGEVPGVDY NFISVEQFKA LEESGALLES
GTYDGNFYGT PKPPAEPSPF QPDPVDQVLF DNEFDAESQR KRTTSVSKME RMDSSLPEEE
EDEDKEAING SGNAENRERH SESSDWMKTV PSYNQTNSSM DFRNYMMRDE TLEPLPKNWE
MAYTDTGMIY FIDHNTKTTT WLDPRLCKKA KAPEDCEDGE LPYGWEKIED PQYGTYYVDH
LNQKTQFENP VEEAKRKKQL GQVEIGSSKP DMEKSHFTRD PSQLKGVLVR ASLKKSTMGF
GFTIIGGDRP DEFLQVKNVL KDGPAAQDGK IAPGDVIVDI NGNCVLGHTH ADVVQMFQLV
PVNQYVNLTL CRGYPLPDDS EDPVVDIVAA TPVINGQSLT KGETCMNPQD FKPGAMVLEQ
NGKSGHTLTG DGLNGPSDAS EQRVSMASSG SSQPELVTIP LIKGPKGFGF AIADSPTGQK
VKMILDSQWC QGLQKGDIIK EIYHQNVQNL THLQVVEVLK QFPVGADVPL LILRGGPPSP
TKTAKMKTDK KENAGSLEAI NEPIPQPMPF PPSIIRSGSP KLDPSEVYLK SKTLYEDKPP
NTKDLDVFLR KQESGFGFRV LGGDGPDQSI YIGAIIPLGA AEKDGRLRAA DELMCIDGIP
VKGKSHKQVL DLMTTAARNG HVLLTVRRKI FYGEKQPEDD SSQAFISTQN GSPRLNRAEV
PARPAPQEPY DVVLQRKENE GFGFVILTSK NKPPPGVIPH KIGRVIEGSP ADRCGKLKVG
DHISAVNGQS IVELSHDNIV QLIKDAGVTV TLTVIAEEEH HGPPSGTNSA RQSPALQHRP
MGQSQANHIP GDRSALEGEI GKDVSTSYRH SWSDHKHLAQ PDTAVISVVG SRHNQNLGCY
PVELERGPRG FGFSLRGGKE YNMGLFILRL AEDGPAIKDG RIHVGDQIVE INGEPTQGIT
HTRAIELIQA GGNKVLLLLR PGTGLIPDHG DWDINNPSSS NVIYDEQSPL PPSSHFASIF
EESHVPVIEE SLRVQICEKA EELKDIVPEK KSTLNENQPE IKHQSLLQKN VSKRDPPSSH
GHSNKKNLLK VENGVTRRGR SVSPKKPASQ HSEEHLDKIP SPLKNNPKRR PRDQSLSPSK
GENKSCQVST RAGSGQDQCR KSRGRSASPK KQQKIEGSKA PSNAEAKLLE GKSRRIAGYT
GSNAEQIPDG KEKSDVIRKD AKQNQLEKSR TRSPEKKIKR MVEKSLPSKM TNKTTSKEVS
ENEKGKKVTT GETSSSNDKI GENVQLSEKR LKQEPEEKVV SNKTEDHKGK ELEAADKNKE
TGRFKPESSS PVKKTLITPG PWKVPSGNKV TGTIGMAEKR Q
