MAGI2_HUMAN
ID MAGI2_HUMAN Reviewed; 1455 AA.
AC Q86UL8; A4D1C1; A7E2C3; O60434; O60510; Q86UI7; Q9NP44; Q9UDQ5; Q9UDU1;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2;
DE AltName: Full=Atrophin-1-interacting protein 1;
DE Short=AIP-1;
DE AltName: Full=Atrophin-1-interacting protein A;
DE AltName: Full=Membrane-associated guanylate kinase inverted 2;
DE Short=MAGI-2;
GN Name=MAGI2; Synonyms=ACVRINP1, AIP1, KIAA0705;
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 1), TISSUE SPECIFICITY, AND INTERACTION
RP WITH DRPLA.
RC TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PTEN.
RX PubMed=10760291; DOI=10.1073/pnas.97.8.4233;
RA Wu X., Hepner K., Castelino-Prabhu S., Do D., Kaye M.B., Yuan X.-J.,
RA Wood J., Ross C., Sawyers C.L., Whang Y.E.;
RT "Evidence for regulation of the PTEN tumor suppressor by a membrane-
RT localized multi-PDZ domain containing scaffold protein MAGI-2.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:4233-4238(2000).
RN [7]
RP INTERACTION WITH PTEN.
RX PubMed=11707428; DOI=10.1074/jbc.c100556200;
RA Vazquez F., Grossman S.R., Takahashi Y., Rokas M.V., Nakamura N.,
RA Sellers W.R.;
RT "Phosphorylation of the PTEN tail acts as an inhibitory switch by
RT preventing its recruitment into a protein complex.";
RL J. Biol. Chem. 276:48627-48630(2001).
RN [8]
RP INTERACTION WITH DDN.
RX PubMed=16464232; DOI=10.1111/j.1471-4159.2006.03679.x;
RA Kremerskothen J., Kindler S., Finger I., Veltel S., Barnekow A.;
RT "Postsynaptic recruitment of Dendrin depends on both dendritic mRNA
RT transport and synaptic anchoring.";
RL J. Neurochem. 96:1659-1666(2006).
RN [9]
RP IDENTIFICATION IN A COMPLEX WITH IGSF9B AND NLGN2.
RX PubMed=23751499; DOI=10.1083/jcb.201209132;
RA Woo J., Kwon S.K., Nam J., Choi S., Takahashi H., Krueger D., Park J.,
RA Lee Y., Bae J.Y., Lee D., Ko J., Kim H., Kim M.H., Bae Y.C., Chang S.,
RA Craig A.M., Kim E.;
RT "The adhesion protein IgSF9b is coupled to neuroligin 2 via S-SCAM to
RT promote inhibitory synapse development.";
RL J. Cell Biol. 201:929-944(2013).
RN [10]
RP INTERACTION WITH USH1G.
RX PubMed=24608321; DOI=10.1093/hmg/ddu104;
RA Bauss K., Knapp B., Jores P., Roepman R., Kremer H., Wijk E.V., Maerker T.,
RA Wolfrum U.;
RT "Phosphorylation of the Usher syndrome 1G protein SANS controls Magi2-
RT mediated endocytosis.";
RL Hum. Mol. Genet. 23:3923-3942(2014).
RN [11]
RP STRUCTURE BY NMR OF 412-1230.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the PDZ domains of human atrophin-1 interacting
RT protein 1 (KIAA0705 protein).";
RL Submitted (FEB-2004) to the PDB data bank.
RN [12]
RP INVOLVEMENT IN NPHS15.
RX PubMed=27932480; DOI=10.1681/asn.2016040387;
RG NephroS;
RG UK study of Nephrotic Syndrome;
RA Bierzynska A., Soderquest K., Dean P., Colby E., Rollason R., Jones C.,
RA Inward C.D., McCarthy H.J., Simpson M.A., Lord G.M., Williams M.,
RA Welsh G.I., Koziell A.B., Saleem M.A.;
RT "MAGI2 mutations cause congenital nephrotic syndrome.";
RL J. Am. Soc. Nephrol. 28:1614-1621(2017).
CC -!- FUNCTION: Seems to act as a scaffold molecule at synaptic junctions by
CC assembling neurotransmitter receptors and cell adhesion proteins (By
CC similarity). Plays a role in nerve growth factor (NGF)-induced
CC recruitment of RAPGEF2 to late endosomes and neurite outgrowth (By
CC similarity). May play a role in regulating activin-mediated signaling
CC in neuronal cells (By similarity). Enhances the ability of PTEN to
CC suppress AKT1 activation (PubMed:10760291). Plays a role in receptor-
CC mediated clathrin-dependent endocytosis which is required for
CC ciliogenesis (By similarity). {ECO:0000250|UniProtKB:O88382,
CC ECO:0000250|UniProtKB:Q9WVQ1, ECO:0000269|PubMed:10760291}.
CC -!- SUBUNIT: Interacts (via its WW domains) with DRPLA (PubMed:9647693).
CC Interacts (via its second PDZ domain) with PTEN (via unphosphorylated
CC C-terminus); this interaction diminishes the degradation rate of PTEN
CC (PubMed:10760291, PubMed:11707428). Interacts (via guanylate kinase
CC domain) with DLGAP1 (By similarity). Interacts (via the PDZ domains)
CC with GRIN2A, GRID2 and NLGN1 (By similarity). Interacts with CTNND2,
CC CTNNB1, MAGUIN-1, ACVR2A, SMAD2 and SMAD3 (By similarity). Part of a
CC complex consisting of AIP1, ACVR2A, ACVR1B and SMAD3 (By similarity).
CC May interact with HTR2A (By similarity). Interacts with IGSF9, RAPGEF2
CC and HTR4 (By similarity). Identified in a complex with ACTN4, CASK,
CC IQGAP1, NPHS1, SPTAN1 and SPTBN1 (By similarity). Found in a complex,
CC at least composed of KIDINS220, MAGI2, NTRK1 and RAPGEF2; the complex
CC is mainly formed at late endosomes in a NGF-dependent manner (By
CC similarity). Interacts with RAPGEF2; the interaction occurs before or
CC after nerve growth factor (NGF) stimulation (By similarity). Interacts
CC (via PDZ domain) with KIDINS220 (via C-terminal domain) (By
CC similarity). Interacts with DDN (PubMed:16464232). Interacts with DLL1
CC (By similarity). Found in a complex with IGSF9B and NLGN2; the
CC interaction with IGSF9B is mediated via the PDZ 5 and PDZ 6 domains,
CC while the interaction with NLGN2 is mediated via the WW1, WW2 and PDZ2
CC domains (PubMed:23751499). Interacts (via PDZ 6 domain) with USH1G (via
CC SAM domain); the interaction is triggered by phosphorylation of USH1G
CC by CK2 and negatively regulates MAGI2-mediated endocytosis
CC (PubMed:24608321). {ECO:0000250|UniProtKB:O88382,
CC ECO:0000250|UniProtKB:Q9WVQ1, ECO:0000269|PubMed:10760291,
CC ECO:0000269|PubMed:11707428, ECO:0000269|PubMed:16464232,
CC ECO:0000269|PubMed:23751499, ECO:0000269|PubMed:24608321,
CC ECO:0000269|PubMed:9647693}.
CC -!- INTERACTION:
CC Q86UL8; P08588: ADRB1; NbExp=3; IntAct=EBI-311035, EBI-991009;
CC Q86UL8-2; Q6IS01: DLGAP1; NbExp=5; IntAct=EBI-12081182, EBI-11961832;
CC Q86UL8-2; Q9P1A6-3: DLGAP2; NbExp=3; IntAct=EBI-12081182, EBI-12019838;
CC Q86UL8-2; O95886: DLGAP3; NbExp=3; IntAct=EBI-12081182, EBI-1752541;
CC Q86UL8-2; Q8NDC4: MORN4; NbExp=3; IntAct=EBI-12081182, EBI-10269566;
CC Q86UL8-2; Q5EBL8: PDZD11; NbExp=3; IntAct=EBI-12081182, EBI-1644207;
CC Q86UL8-2; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-12081182, EBI-742388;
CC Q86UL8-2; P14678-2: SNRPB; NbExp=3; IntAct=EBI-12081182, EBI-372475;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Late endosome
CC {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q9WVQ1}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q9WVQ1}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:Q9WVQ1}. Photoreceptor inner segment
CC {ECO:0000250|UniProtKB:Q9WVQ1}. Cell projection, cilium, photoreceptor
CC outer segment {ECO:0000250|UniProtKB:Q9WVQ1}. Note=Localized diffusely
CC in the cytoplasm before nerve growth factor (NGF) stimulation.
CC Recruited to late endosomes after NGF stimulation. Membrane-associated
CC in synaptosomes (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86UL8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86UL8-2; Sequence=VSP_008435;
CC -!- TISSUE SPECIFICITY: Specifically expressed in brain.
CC {ECO:0000269|PubMed:9647693}.
CC -!- DISEASE: Nephrotic syndrome 15 (NPHS15) [MIM:617609]: A form of
CC nephrotic syndrome, a renal disease clinically characterized by severe
CC proteinuria, resulting in complications such as hypoalbuminemia,
CC hyperlipidemia and edema. Kidney biopsies show non-specific histologic
CC changes such as focal segmental glomerulosclerosis and diffuse
CC mesangial proliferation. NPHS15 is an autosomal recessive form with
CC onset in the first months of life. Disease severity is variable. Some
CC patients show rapid progression to end-stage renal failure.
CC {ECO:0000269|PubMed:27932480}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31680.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF038563; AAC05370.1; -; mRNA.
DR EMBL; AB014605; BAA31680.2; ALT_INIT; mRNA.
DR EMBL; AC004808; AAC23438.1; -; Genomic_DNA.
DR EMBL; AC004945; AAC61488.1; -; Genomic_DNA.
DR EMBL; AC004990; AAC79151.1; -; Genomic_DNA.
DR EMBL; AC005246; AAC25530.1; -; Genomic_DNA.
DR EMBL; AC006043; AAD15413.2; -; Genomic_DNA.
DR EMBL; AC006324; AAF66080.1; -; Genomic_DNA.
DR EMBL; AC007237; AAP21886.1; -; Genomic_DNA.
DR EMBL; AC073200; AAP22360.1; -; Genomic_DNA.
DR EMBL; CH236949; EAL24194.1; -; Genomic_DNA.
DR EMBL; BC150277; AAI50278.1; -; mRNA.
DR CCDS; CCDS5594.1; -. [Q86UL8-1]
DR CCDS; CCDS75623.1; -. [Q86UL8-2]
DR RefSeq; NP_001288057.1; NM_001301128.1. [Q86UL8-2]
DR RefSeq; NP_036433.2; NM_012301.3. [Q86UL8-1]
DR PDB; 1UEP; NMR; -; A=774-863.
DR PDB; 1UEQ; NMR; -; A=412-522.
DR PDB; 1UEW; NMR; -; A=915-1015.
DR PDB; 1UJV; NMR; -; A=600-682.
DR PDB; 1WFV; NMR; -; A=1141-1230.
DR PDBsum; 1UEP; -.
DR PDBsum; 1UEQ; -.
DR PDBsum; 1UEW; -.
DR PDBsum; 1UJV; -.
DR PDBsum; 1WFV; -.
DR AlphaFoldDB; Q86UL8; -.
DR SMR; Q86UL8; -.
DR BioGRID; 115197; 28.
DR CORUM; Q86UL8; -.
DR IntAct; Q86UL8; 22.
DR MINT; Q86UL8; -.
DR STRING; 9606.ENSP00000346151; -.
DR TCDB; 8.A.24.1.6; the ezrin/radixin/moesin-binding phosphoprotein 50 (ebp50) family.
DR iPTMnet; Q86UL8; -.
DR PhosphoSitePlus; Q86UL8; -.
DR BioMuta; MAGI2; -.
DR DMDM; 88909269; -.
DR EPD; Q86UL8; -.
DR jPOST; Q86UL8; -.
DR MassIVE; Q86UL8; -.
DR MaxQB; Q86UL8; -.
DR PaxDb; Q86UL8; -.
DR PeptideAtlas; Q86UL8; -.
DR PRIDE; Q86UL8; -.
DR ProteomicsDB; 69831; -. [Q86UL8-1]
DR ProteomicsDB; 69832; -. [Q86UL8-2]
DR Antibodypedia; 2880; 247 antibodies from 33 providers.
DR DNASU; 9863; -.
DR Ensembl; ENST00000354212.9; ENSP00000346151.4; ENSG00000187391.22. [Q86UL8-1]
DR Ensembl; ENST00000419488.5; ENSP00000405766.1; ENSG00000187391.22. [Q86UL8-2]
DR GeneID; 9863; -.
DR KEGG; hsa:9863; -.
DR MANE-Select; ENST00000354212.9; ENSP00000346151.4; NM_012301.4; NP_036433.2.
DR UCSC; uc003ugx.3; human. [Q86UL8-1]
DR CTD; 9863; -.
DR DisGeNET; 9863; -.
DR GeneCards; MAGI2; -.
DR HGNC; HGNC:18957; MAGI2.
DR HPA; ENSG00000187391; Tissue enhanced (brain).
DR MalaCards; MAGI2; -.
DR MIM; 606382; gene.
DR MIM; 617609; phenotype.
DR neXtProt; NX_Q86UL8; -.
DR OpenTargets; ENSG00000187391; -.
DR Orphanet; 656; Genetic steroid-resistant nephrotic syndrome.
DR PharmGKB; PA142671484; -.
DR VEuPathDB; HostDB:ENSG00000187391; -.
DR eggNOG; KOG3209; Eukaryota.
DR GeneTree; ENSGT00940000155057; -.
DR InParanoid; Q86UL8; -.
DR OMA; LPQNIPY; -.
DR OrthoDB; 284488at2759; -.
DR PhylomeDB; Q86UL8; -.
DR TreeFam; TF316816; -.
DR PathwayCommons; Q86UL8; -.
DR Reactome; R-HSA-373753; Nephrin family interactions.
DR SignaLink; Q86UL8; -.
DR SIGNOR; Q86UL8; -.
DR BioGRID-ORCS; 9863; 10 hits in 1074 CRISPR screens.
DR ChiTaRS; MAGI2; human.
DR EvolutionaryTrace; Q86UL8; -.
DR GeneWiki; MAGI2; -.
DR GenomeRNAi; 9863; -.
DR Pharos; Q86UL8; Tbio.
DR PRO; PR:Q86UL8; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q86UL8; protein.
DR Bgee; ENSG00000187391; Expressed in calcaneal tendon and 185 other tissues.
DR ExpressionAtlas; Q86UL8; baseline and differential.
DR Genevisible; Q86UL8; HS.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0097546; C:ciliary base; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; ISS:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0036057; C:slit diaphragm; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0031697; F:beta-1 adrenergic receptor binding; IPI:UniProtKB.
DR GO; GO:0019902; F:phosphatase binding; IPI:UniProtKB.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IDA:UniProtKB.
DR GO; GO:0046332; F:SMAD binding; ISS:UniProtKB.
DR GO; GO:0070699; F:type II activin receptor binding; ISS:UniProtKB.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; ISS:UniProtKB.
DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; IDA:UniProtKB.
DR GO; GO:0038180; P:nerve growth factor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0003402; P:planar cell polarity pathway involved in axis elongation; NAS:UniProtKB.
DR GO; GO:0072015; P:podocyte development; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IDA:UniProtKB.
DR GO; GO:0002092; P:positive regulation of receptor internalization; IDA:UniProtKB.
DR GO; GO:0043113; P:receptor clustering; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0060395; P:SMAD protein signal transduction; ISS:UniProtKB.
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; IPR030036; MAGI2.
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:SF27; PTHR10316:SF27; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 6.
DR Pfam; PF00397; WW; 1.
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; Cell membrane; Cell projection;
KW Cytoplasm; Cytoskeleton; Endocytosis; Endosome; Membrane; Neurogenesis;
KW Phosphoprotein; Reference proteome; Repeat; Synapse; Synaptosome.
FT CHAIN 1..1455
FT /note="Membrane-associated guanylate kinase, WW and PDZ
FT domain-containing protein 2"
FT /id="PRO_0000094586"
FT DOMAIN 17..101
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 109..283
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT DOMAIN 302..335
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 348..381
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 426..510
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 605..683
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 778..860
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 920..1010
FT /note="PDZ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1147..1229
FT /note="PDZ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 205..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..381
FT /note="Interaction with DDN"
FT /evidence="ECO:0000269|PubMed:16464232"
FT REGION 869..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..913
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1042
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1057
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1085
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 362
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVQ1"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88382"
FT MOD_RES 827
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVQ1"
FT MOD_RES 884
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88382"
FT MOD_RES 885
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88382"
FT MOD_RES 1014
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVQ1"
FT VAR_SEQ 757..771
FT /note="QQVPPRTSFRMDSSG -> R (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9734811"
FT /id="VSP_008435"
FT CONFLICT 1234
FT /note="E -> Q (in Ref. 1; AAC05370)"
FT /evidence="ECO:0000305"
FT CONFLICT 1250
FT /note="G -> C (in Ref. 1; AAC05370)"
FT /evidence="ECO:0000305"
FT CONFLICT 1291
FT /note="E -> K (in Ref. 1; AAC05370)"
FT /evidence="ECO:0000305"
FT CONFLICT 1383
FT /note="P -> L (in Ref. 1; AAC05370)"
FT /evidence="ECO:0000305"
FT CONFLICT 1389..1394
FT /note="FAGPGG -> SADPAD (in Ref. 1; AAC05370)"
FT /evidence="ECO:0000305"
FT CONFLICT 1401
FT /note="E -> A (in Ref. 1; AAC05370)"
FT /evidence="ECO:0000305"
FT CONFLICT 1411
FT /note="G -> A (in Ref. 1; AAC05370)"
FT /evidence="ECO:0000305"
FT CONFLICT 1414..1415
FT /note="PG -> SV (in Ref. 1; AAC05370)"
FT /evidence="ECO:0000305"
FT CONFLICT 1420
FT /note="G -> A (in Ref. 1; AAC05370)"
FT /evidence="ECO:0000305"
FT CONFLICT 1423
FT /note="P -> A (in Ref. 1; AAC05370)"
FT /evidence="ECO:0000305"
FT CONFLICT 1426
FT /note="K -> R (in Ref. 1; AAC05370)"
FT /evidence="ECO:0000305"
FT CONFLICT 1429
FT /note="V -> G (in Ref. 1; AAC05370)"
FT /evidence="ECO:0000305"
FT CONFLICT 1437
FT /note="P -> R (in Ref. 1; AAC05370)"
FT /evidence="ECO:0000305"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:1UEQ"
FT STRAND 422..430
FT /evidence="ECO:0007829|PDB:1UEQ"
FT STRAND 437..441
FT /evidence="ECO:0007829|PDB:1UEQ"
FT STRAND 444..447
FT /evidence="ECO:0007829|PDB:1UEQ"
FT STRAND 451..455
FT /evidence="ECO:0007829|PDB:1UEQ"
FT HELIX 460..463
FT /evidence="ECO:0007829|PDB:1UEQ"
FT STRAND 472..476
FT /evidence="ECO:0007829|PDB:1UEQ"
FT HELIX 486..494
FT /evidence="ECO:0007829|PDB:1UEQ"
FT STRAND 501..509
FT /evidence="ECO:0007829|PDB:1UEQ"
FT STRAND 604..609
FT /evidence="ECO:0007829|PDB:1UJV"
FT STRAND 612..622
FT /evidence="ECO:0007829|PDB:1UJV"
FT STRAND 625..632
FT /evidence="ECO:0007829|PDB:1UJV"
FT HELIX 634..636
FT /evidence="ECO:0007829|PDB:1UJV"
FT STRAND 645..649
FT /evidence="ECO:0007829|PDB:1UJV"
FT HELIX 659..668
FT /evidence="ECO:0007829|PDB:1UJV"
FT STRAND 673..680
FT /evidence="ECO:0007829|PDB:1UJV"
FT STRAND 774..777
FT /evidence="ECO:0007829|PDB:1UEP"
FT STRAND 780..787
FT /evidence="ECO:0007829|PDB:1UEP"
FT STRAND 790..792
FT /evidence="ECO:0007829|PDB:1UEP"
FT STRAND 803..807
FT /evidence="ECO:0007829|PDB:1UEP"
FT HELIX 814..816
FT /evidence="ECO:0007829|PDB:1UEP"
FT STRAND 824..828
FT /evidence="ECO:0007829|PDB:1UEP"
FT HELIX 838..851
FT /evidence="ECO:0007829|PDB:1UEP"
FT STRAND 853..861
FT /evidence="ECO:0007829|PDB:1UEP"
FT STRAND 919..924
FT /evidence="ECO:0007829|PDB:1UEW"
FT STRAND 933..936
FT /evidence="ECO:0007829|PDB:1UEW"
FT STRAND 953..957
FT /evidence="ECO:0007829|PDB:1UEW"
FT HELIX 964..966
FT /evidence="ECO:0007829|PDB:1UEW"
FT STRAND 974..978
FT /evidence="ECO:0007829|PDB:1UEW"
FT TURN 983..985
FT /evidence="ECO:0007829|PDB:1UEW"
FT HELIX 988..997
FT /evidence="ECO:0007829|PDB:1UEW"
FT TURN 998..1000
FT /evidence="ECO:0007829|PDB:1UEW"
FT STRAND 1001..1006
FT /evidence="ECO:0007829|PDB:1UEW"
FT STRAND 1156..1159
FT /evidence="ECO:0007829|PDB:1WFV"
FT STRAND 1162..1164
FT /evidence="ECO:0007829|PDB:1WFV"
FT TURN 1165..1168
FT /evidence="ECO:0007829|PDB:1WFV"
FT STRAND 1169..1172
FT /evidence="ECO:0007829|PDB:1WFV"
FT HELIX 1181..1185
FT /evidence="ECO:0007829|PDB:1WFV"
FT STRAND 1193..1197
FT /evidence="ECO:0007829|PDB:1WFV"
FT HELIX 1207..1217
FT /evidence="ECO:0007829|PDB:1WFV"
FT STRAND 1219..1221
FT /evidence="ECO:0007829|PDB:1WFV"
FT STRAND 1223..1226
FT /evidence="ECO:0007829|PDB:1WFV"
SQ SEQUENCE 1455 AA; 158754 MW; 93E170D070A70A9C CRC64;
MSKSLKKKSH WTSKVHESVI GRNPEGQLGF ELKGGAENGQ FPYLGEVKPG KVAYESGSKL
VSEELLLEVN ETPVAGLTIR DVLAVIKHCK DPLRLKCVKQ GGIVDKDLRH YLNLRFQKGS
VDHELQQIIR DNLYLRTVPC TTRPHKEGEV PGVDYIFITV EDFMELEKSG ALLESGTYED
NYYGTPKPPA EPAPLLLNVT DQILPGATPS AEGKRKRNKS VSNMEKASIE PPEEEEEERP
VVNGNGVVVT PESSEHEDKS AGASGEMPSQ PYPAPVYSQP EELKEQMDDT KPTKPEDNEE
PDPLPDNWEM AYTEKGEVYF IDHNTKTTSW LDPRLAKKAK PPEECKENEL PYGWEKIDDP
IYGTYYVDHI NRRTQFENPV LEAKRKLQQH NMPHTELGTK PLQAPGFREK PLFTRDASQL
KGTFLSTTLK KSNMGFGFTI IGGDEPDEFL QVKSVIPDGP AAQDGKMETG DVIVYINEVC
VLGHTHADVV KLFQSVPIGQ SVNLVLCRGY PLPFDPEDPA NSMVPPLAIM ERPPPVMVNG
RHNYETYLEY ISRTSQSVPD ITDRPPHSLH SMPTDGQLDG TYPPPVHDDN VSMASSGATQ
AELMTLTIVK GAQGFGFTIA DSPTGQRVKQ ILDIQGCPGL CEGDLIVEIN QQNVQNLSHT
EVVDILKDCP IGSETSLIIH RGGFFSPWKT PKPIMDRWEN QGSPQTSLSA PAIPQNLPFP
PALHRSSFPD STEAFDPRKP DPYELYEKSR AIYESRQQVP PRTSFRMDSS GPDYKELDVH
LRRMESGFGF RILGGDEPGQ PILIGAVIAM GSADRDGRLH PGDELVYVDG IPVAGKTHRY
VIDLMHHAAR NGQVNLTVRR KVLCGGEPCP ENGRSPGSVS THHSSPRSDY ATYTNSNHAA
PSSNASPPEG FASHSLQTSD VVIHRKENEG FGFVIISSLN RPESGSTITV PHKIGRIIDG
SPADRCAKLK VGDRILAVNG QSIINMPHAD IVKLIKDAGL SVTLRIIPQE ELNSPTSAPS
SEKQSPMAQQ SPLAQQSPLA QPSPATPNSP IAQPAPPQPL QLQGHENSYR SEVKARQDVK
PDIRQPPFTD YRQPPLDYRQ PPGGDYQQPP PLDYRQPPLL DYRQHSPDTR QYPLSDYRQP
QDFDYFTVDM EKGAKGFGFS IRGGREYKMD LYVLRLAEDG PAIRNGRMRV GDQIIEINGE
STRDMTHARA IELIKSGGRR VRLLLKRGTG QVPEYDEPAP WSSPAAAAPG LPEVGVSLDD
GLAPFSPSHP APPSDPSHQI SPGPTWDIKR EHDVRKPKEL SACGQKKQRL GEQRERSASP
QRAARPRLEE APGGQGRPEA GRPASEARAP GLAAADAADA ARAGGKEAPR AAAGSELCRR
EGPGAAPAFA GPGGGGSGAL EAEGRAGARA GPRPGPRPPG GAPARKAAVA PGPWKVPGSD
KLPSVLKPGA SAASR
