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Database: UniProt
Entry: Q86UL8
LinkDB: Q86UL8
Original site: Q86UL8 
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   29-SEP-2021, entry version 183.
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   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   [11]
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 scaffold molecule at synaptic junctions by
CC       assembling neurotransmitter receptors and cell adhesion proteins. May
CC       play a role in regulating activin-mediated signaling in neuronal cells.
CC       Enhances the ability of PTEN to suppress AKT1 activation. Plays a role
CC       in nerve growth factor (NGF)-induced recruitment of RAPGEF2 to late
CC       endosomes and neurite outgrowth. {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). {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: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}. Cell junction, synapse, synaptosome {ECO:0000250}. Cell
CC       membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC       Note=Localized diffusely in the cytoplasm before nerve growth factor
CC       (NGF) stimulation. Recruited to late endosomes after NGF stimulation.
CC       Membrane-associated 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   SMR; Q86UL8; -.
DR   BioGRID; 115197; 27.
DR   CORUM; Q86UL8; -.
DR   IntAct; Q86UL8; 19.
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   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; 271 antibodies.
DR   DNASU; 9863; -.
DR   Ensembl; ENST00000354212; ENSP00000346151; ENSG00000187391. [Q86UL8-1]
DR   Ensembl; ENST00000419488; ENSP00000405766; ENSG00000187391. [Q86UL8-2]
DR   GeneID; 9863; -.
DR   KEGG; hsa:9863; -.
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, parathyroid gland).
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; KYCPDYK; -.
DR   OrthoDB; 284488at2759; -.
DR   PhylomeDB; Q86UL8; -.
DR   TreeFam; TF316816; -.
DR   PathwayCommons; Q86UL8; -.
DR   Reactome; R-HSA-373753; Nephrin family interactions.
DR   SignaLink; Q86UL8; -.
DR   BioGRID-ORCS; 9863; 5 hits in 1010 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 metanephric glomerulus and 222 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: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: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:0072015; P:glomerular visceral epithelial cell development; 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: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:0051726; P:regulation of cell cycle; 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 junction; Cell membrane;
KW   Cytoplasm; Endosome; Membrane; Neurogenesis; Phosphoprotein;
KW   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
//
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