DLG2_HUMAN
ID DLG2_HUMAN Reviewed; 870 AA.
AC Q15700; B7WNY8; F8W9V6; Q59G57; Q5H9Q4; Q68CQ8; Q6ZTA8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Disks large homolog 2;
DE AltName: Full=Channel-associated protein of synapse-110;
DE Short=Chapsyn-110;
DE AltName: Full=Postsynaptic density protein PSD-93;
GN Name=DLG2;
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).
RC TISSUE=Brain;
RX PubMed=8755482; DOI=10.1016/s0896-6273(00)80284-6;
RA Kim E., Cho K.-O., Rothschild A., Sheng M.;
RT "Heteromultimerization and NMDA receptor-clustering activity of Chapsyn-
RT 110, a member of the PSD-95 family of proteins.";
RL Neuron 17:103-113(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Cerebellum;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5).
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-542 (ISOFORM 1).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND INTERACTION WITH KCNJ2.
RX PubMed=15304517; DOI=10.1074/jbc.m407575200;
RA Leyland M.L., Dart C.;
RT "An alternatively spliced isoform of PSD-93/chapsyn 110 binds to the
RT inwardly rectifying potassium channel, Kir2.1.";
RL J. Biol. Chem. 279:43427-43436(2004).
RN [7]
RP INTERACTION WITH LRFN1; LRFN2 AND LRFN4.
RX PubMed=16630835; DOI=10.1016/j.neuron.2006.04.005;
RA Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H., Kaang B.-K.,
RA Kim E.;
RT "SALM synaptic cell adhesion-like molecules regulate the differentiation of
RT excitatory synapses.";
RL Neuron 50:233-245(2006).
RN [8]
RP INTERACTION WITH FRMPD4.
RX PubMed=19118189; DOI=10.1523/jneurosci.3112-08.2008;
RA Lee H.W., Choi J., Shin H., Kim K., Yang J., Na M., Choi S.Y., Kang G.B.,
RA Eom S.H., Kim H., Kim E.;
RT "Preso, a novel PSD-95-interacting FERM and PDZ domain protein that
RT regulates dendritic spine morphogenesis.";
RL J. Neurosci. 28:14546-14556(2008).
RN [9]
RP INTERACTION WITH FASLG.
RX PubMed=19807924; DOI=10.1186/1471-2172-10-53;
RA Voss M., Lettau M., Janssen O.;
RT "Identification of SH3 domain interaction partners of human FasL (CD178) by
RT phage display screening.";
RL BMC Immunol. 10:53-53(2009).
RN [10]
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-627 AND SER-635, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [12]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 190-283, AND X-RAY
RP CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 418-513.
RX PubMed=17384233; DOI=10.1110/ps.062657507;
RA Elkins J.M., Papagrigoriou E., Berridge G., Yang X., Phillips C.,
RA Gileadi C., Savitsky P., Doyle D.A.;
RT "Structure of PICK1 and other PDZ domains obtained with the help of self-
RT binding C-terminal extensions.";
RL Protein Sci. 16:683-694(2007).
CC -!- FUNCTION: Required for perception of chronic pain through NMDA receptor
CC signaling. Regulates surface expression of NMDA receptors in dorsal
CC horn neurons of the spinal cord. Interacts with the cytoplasmic tail of
CC NMDA receptor subunits as well as inward rectifying potassium channels.
CC Involved in regulation of synaptic stability at cholinergic synapses.
CC Part of the postsynaptic protein scaffold of excitatory synapses (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts through its PDZ domains with NETO1 (By similarity).
CC Interacts with NOS1/nNOS through second PDZ domain (By similarity).
CC Interacts with KCNJ2/Kir2.1 (via C-terminus) through one of its PDZ
CC domains (PubMed:15304517). Interacts with KCNJ4 (By similarity),
CC Interacts with FRMPD4 (via C-terminus) (PubMed:19118189). Interacts
CC with LRFN1, LRFN2 and LRFN4 (PubMed:16630835). Interacts with FASLG
CC (PubMed:19807924). Interacts with KCNJ4 (By similarity). Interacts with
CC ADAM22 (By similarity). Interacts with DGKI (via PDZ-binding motif) (By
CC similarity). {ECO:0000250|UniProtKB:Q63622,
CC ECO:0000250|UniProtKB:Q91XM9, ECO:0000269|PubMed:15304517,
CC ECO:0000269|PubMed:16630835, ECO:0000269|PubMed:19118189,
CC ECO:0000269|PubMed:19807924}.
CC -!- INTERACTION:
CC Q15700; P28039: AOAH; NbExp=3; IntAct=EBI-80426, EBI-1222067;
CC Q15700; Q6IS01: DLGAP1; NbExp=3; IntAct=EBI-80426, EBI-11961832;
CC Q15700; Q9P1A6-3: DLGAP2; NbExp=3; IntAct=EBI-80426, EBI-12019838;
CC Q15700; O95886: DLGAP3; NbExp=3; IntAct=EBI-80426, EBI-1752541;
CC Q15700; Q7L5A8: FA2H; NbExp=3; IntAct=EBI-80426, EBI-11337888;
CC Q15700; P24390: KDELR1; NbExp=3; IntAct=EBI-80426, EBI-1043076;
CC Q15700; Q9HB19: PLEKHA2; NbExp=3; IntAct=EBI-80426, EBI-4401947;
CC Q15700; Q8WUA2: PPIL4; NbExp=3; IntAct=EBI-80426, EBI-2513119;
CC Q15700; P10153: RNASE2; NbExp=3; IntAct=EBI-80426, EBI-12286629;
CC Q15700; Q9H7B2: RPF2; NbExp=3; IntAct=EBI-80426, EBI-1051960;
CC Q15700; P62241: RPS8; NbExp=3; IntAct=EBI-80426, EBI-351811;
CC Q15700; Q9UIV8: SERPINB13; NbExp=3; IntAct=EBI-80426, EBI-3048588;
CC Q15700; P04004: VTN; NbExp=3; IntAct=EBI-80426, EBI-1036653;
CC Q15700-4; P35561: Kcnj2; Xeno; NbExp=6; IntAct=EBI-663057, EBI-703793;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q63622};
CC Lipid-anchor {ECO:0000250|UniProtKB:Q63622}. Postsynaptic density
CC {ECO:0000250|UniProtKB:Q63622}. Synapse {ECO:0000250}. Membrane
CC {ECO:0000250|UniProtKB:Q63622}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q63622}. Perikaryon
CC {ECO:0000250|UniProtKB:Q63622}. Note=Concentrated in soma and
CC postsynaptic density of a subset of neurons.
CC {ECO:0000250|UniProtKB:Q63622}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=PSD93-alpha;
CC IsoId=Q15700-1; Sequence=Displayed;
CC Name=2; Synonyms=PSD93-beta;
CC IsoId=Q15700-2; Sequence=VSP_015513;
CC Name=3;
CC IsoId=Q15700-3; Sequence=VSP_015512, VSP_015514, VSP_015515,
CC VSP_015516;
CC Name=4; Synonyms=PSD93-delta;
CC IsoId=Q15700-4; Sequence=VSP_015511;
CC Name=5;
CC IsoId=Q15700-5; Sequence=VSP_045634, VSP_015516;
CC -!- DOMAIN: An N-terminally truncated L27 domain is predicted in isoform 2
CC at positions 1 through 27.
CC -!- PTM: Palmitoylation of isoform 1 is not required for targeting to
CC postsynaptic density. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92489.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U32376; AAB04949.1; -; mRNA.
DR EMBL; AK126776; BAC86685.1; -; mRNA.
DR EMBL; CR749820; CAH18680.1; -; mRNA.
DR EMBL; CR933674; CAI45970.1; -; mRNA.
DR EMBL; AC023118; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000639; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000642; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000857; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001791; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001984; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP003026; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP003035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP003093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP003095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP003305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB209252; BAD92489.1; ALT_INIT; mRNA.
DR CCDS; CCDS41696.1; -. [Q15700-1]
DR CCDS; CCDS44690.1; -. [Q15700-2]
DR CCDS; CCDS44691.1; -. [Q15700-3]
DR CCDS; CCDS44692.1; -. [Q15700-5]
DR CCDS; CCDS55782.1; -. [Q15700-4]
DR PIR; G01974; G01974.
DR PIR; S60315; S60315.
DR RefSeq; NP_001136171.1; NM_001142699.1. [Q15700-2]
DR RefSeq; NP_001136172.1; NM_001142700.1. [Q15700-3]
DR RefSeq; NP_001136174.1; NM_001142702.1. [Q15700-5]
DR RefSeq; NP_001193698.1; NM_001206769.1. [Q15700-4]
DR RefSeq; NP_001355.2; NM_001364.3. [Q15700-1]
DR PDB; 2BYG; X-ray; 1.85 A; A=190-283.
DR PDB; 2HE2; X-ray; 1.50 A; A/B=418-513.
DR PDBsum; 2BYG; -.
DR PDBsum; 2HE2; -.
DR AlphaFoldDB; Q15700; -.
DR SMR; Q15700; -.
DR BioGRID; 108084; 41.
DR ComplexPortal; CPX-6184; Scribble cell polarity complex, DLG2-LLGL2-SCRIB variant.
DR ComplexPortal; CPX-6191; Scribble cell polarity complex, DLG2-LLGL1-SCRIB variant.
DR ELM; Q15700; -.
DR IntAct; Q15700; 27.
DR MINT; Q15700; -.
DR STRING; 9606.ENSP00000365272; -.
DR iPTMnet; Q15700; -.
DR PhosphoSitePlus; Q15700; -.
DR SwissPalm; Q15700; -.
DR BioMuta; DLG2; -.
DR DMDM; 215274165; -.
DR EPD; Q15700; -.
DR jPOST; Q15700; -.
DR MassIVE; Q15700; -.
DR MaxQB; Q15700; -.
DR PaxDb; Q15700; -.
DR PeptideAtlas; Q15700; -.
DR PRIDE; Q15700; -.
DR ProteomicsDB; 30388; -.
DR ProteomicsDB; 60709; -. [Q15700-1]
DR ProteomicsDB; 60710; -. [Q15700-2]
DR ProteomicsDB; 60711; -. [Q15700-3]
DR ProteomicsDB; 60712; -. [Q15700-4]
DR ABCD; Q15700; 2 sequenced antibodies.
DR Antibodypedia; 8247; 367 antibodies from 35 providers.
DR DNASU; 1740; -.
DR Ensembl; ENST00000280241.12; ENSP00000280241.8; ENSG00000150672.18. [Q15700-4]
DR Ensembl; ENST00000376104.7; ENSP00000365272.2; ENSG00000150672.18. [Q15700-2]
DR Ensembl; ENST00000398309.6; ENSP00000381355.2; ENSG00000150672.18. [Q15700-1]
DR Ensembl; ENST00000418306.6; ENSP00000402275.2; ENSG00000150672.18. [Q15700-3]
DR Ensembl; ENST00000426717.6; ENSP00000393049.2; ENSG00000150672.18. [Q15700-5]
DR GeneID; 1740; -.
DR KEGG; hsa:1740; -.
DR MANE-Select; ENST00000376104.7; ENSP00000365272.2; NM_001142699.3; NP_001136171.1. [Q15700-2]
DR UCSC; uc001pai.3; human. [Q15700-1]
DR CTD; 1740; -.
DR DisGeNET; 1740; -.
DR GeneCards; DLG2; -.
DR HGNC; HGNC:2901; DLG2.
DR HPA; ENSG00000150672; Tissue enhanced (brain).
DR MIM; 603583; gene.
DR neXtProt; NX_Q15700; -.
DR OpenTargets; ENSG00000150672; -.
DR PharmGKB; PA164741388; -.
DR VEuPathDB; HostDB:ENSG00000150672; -.
DR eggNOG; KOG0708; Eukaryota.
DR GeneTree; ENSGT00940000155156; -.
DR HOGENOM; CLU_001715_4_1_1; -.
DR InParanoid; Q15700; -.
DR OMA; XYARFEA; -.
DR OrthoDB; 807583at2759; -.
DR PhylomeDB; Q15700; -.
DR TreeFam; TF323171; -.
DR PathwayCommons; Q15700; -.
DR Reactome; R-HSA-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-HSA-442982; Ras activation upon Ca2+ influx through NMDA receptor.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR Reactome; R-HSA-9609736; Assembly and cell surface presentation of NMDA receptors.
DR Reactome; R-HSA-9617324; Negative regulation of NMDA receptor-mediated neuronal transmission.
DR Reactome; R-HSA-9620244; Long-term potentiation.
DR SignaLink; Q15700; -.
DR SIGNOR; Q15700; -.
DR BioGRID-ORCS; 1740; 7 hits in 1065 CRISPR screens.
DR ChiTaRS; DLG2; human.
DR EvolutionaryTrace; Q15700; -.
DR GeneWiki; DLG2; -.
DR GenomeRNAi; 1740; -.
DR Pharos; Q15700; Tbio.
DR PRO; PR:Q15700; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q15700; protein.
DR Bgee; ENSG00000150672; Expressed in cortical plate and 133 other tissues.
DR ExpressionAtlas; Q15700; baseline and differential.
DR Genevisible; Q15700; HS.
DR GO; GO:0005912; C:adherens junction; IC:ComplexPortal.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0044224; C:juxtaparanode region of axon; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0014069; C:postsynaptic density; ISS:ARUK-UCL.
DR GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR GO; GO:0004385; F:guanylate kinase activity; TAS:ProtInc.
DR GO; GO:0019900; F:kinase binding; IDA:MGI.
DR GO; GO:0099641; P:anterograde axonal protein transport; ISS:ARUK-UCL.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0035865; P:cellular response to potassium ion; ISS:ARUK-UCL.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
DR GO; GO:0043113; P:receptor clustering; IBA:GO_Central.
DR GO; GO:0097120; P:receptor localization to synapse; IBA:GO_Central.
DR GO; GO:0099642; P:retrograde axonal protein transport; ISS:ARUK-UCL.
DR CDD; cd12032; SH3_DLG2; 1.
DR Gene3D; 2.30.42.10; -; 3.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR016313; DLG1-like.
DR InterPro; IPR019590; DLG1_PEST_dom.
DR InterPro; IPR035759; DLG2_SH3.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR019583; PDZ_assoc.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF10608; MAGUK_N_PEST; 1.
DR Pfam; PF00595; PDZ; 3.
DR Pfam; PF10600; PDZ_assoc; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PIRSF; PIRSF001741; MAGUK_DLGH; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM01277; MAGUK_N_PEST; 1.
DR SMART; SM00228; PDZ; 3.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50156; SSF50156; 3.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS50106; PDZ; 3.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Reference proteome;
KW Repeat; SH3 domain; Synapse.
FT CHAIN 1..870
FT /note="Disks large homolog 2"
FT /id="PRO_0000094553"
FT DOMAIN 98..184
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 193..279
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 421..501
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 536..606
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 680..855
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XM9"
FT MOD_RES 58
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q91XM9"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XM9"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XM9"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XM9"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63622"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XM9"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63622"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XM9"
FT MOD_RES 505
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q91XM9"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63622"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63622"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XM9"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 750
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q91XM9"
FT MOD_RES 755
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q91XM9"
FT LIPID 5
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 7
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..518
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_045634"
FT VAR_SEQ 1..68
FT /note="MFFACYCALRTNVKKYRYQDEDAPHDHSLPRLTHEVRGPELVHVSEKNLSQI
FT ENVHGYVLQSHISPLK -> MNAYLTKQHSCSRGSDGMDAVRSAPTLIRDAHCACGWQR
FT NCQGLGYSSQTMPSSGPGGPASNRTGGSSFNRTLWDSVRKSPHKTSTKGKGTCGEHCTC
FT PHGWFSPAQ (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_015511"
FT VAR_SEQ 1..51
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_015512"
FT VAR_SEQ 1..14
FT /note="MFFACYCALRTNVK -> MGIFKSSLFQALLDIQEFYEVTLLNSQKSCEQKI
FT EEANQVLQKWEKTSLLAPCHDRLQKSSELTDCSGSKENASCIEQNKENQSFENETDETT
FT TQNQGRCPAQNCSVEAPAWMPVHHCT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_015513"
FT VAR_SEQ 52..86
FT /note="IENVHGYVLQSHISPLKASPAPIIVNTDTLDTIPY -> MQRPSVSRAENYQ
FT LLWDTIASLKQCEQAMQHAFIP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_015514"
FT VAR_SEQ 341..392
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_015515"
FT VAR_SEQ 627..659
FT /note="SFNDKRKKSFIFSRKFPFYKNKEQSEQETSDPE -> DIPGLGDDGYGTKTL
FT (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_015516"
FT CONFLICT 177
FT /note="V -> A (in Ref. 1; AAB04949)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="K -> N (in Ref. 1; AAB04949)"
FT /evidence="ECO:0000305"
FT CONFLICT 704
FT /note="K -> E (in Ref. 3; CAI45970)"
FT /evidence="ECO:0000305"
FT CONFLICT 803
FT /note="P -> S (in Ref. 1; AAB04949)"
FT /evidence="ECO:0000305"
FT CONFLICT 861
FT /note="F -> L (in Ref. 3; CAH18680)"
FT /evidence="ECO:0000305"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:2BYG"
FT STRAND 202..209
FT /evidence="ECO:0007829|PDB:2BYG"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:2BYG"
FT HELIX 232..236
FT /evidence="ECO:0007829|PDB:2BYG"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:2BYG"
FT HELIX 258..266
FT /evidence="ECO:0007829|PDB:2BYG"
FT STRAND 270..281
FT /evidence="ECO:0007829|PDB:2BYG"
FT STRAND 420..425
FT /evidence="ECO:0007829|PDB:2HE2"
FT STRAND 432..439
FT /evidence="ECO:0007829|PDB:2HE2"
FT STRAND 444..449
FT /evidence="ECO:0007829|PDB:2HE2"
FT HELIX 454..458
FT /evidence="ECO:0007829|PDB:2HE2"
FT STRAND 465..470
FT /evidence="ECO:0007829|PDB:2HE2"
FT HELIX 480..489
FT /evidence="ECO:0007829|PDB:2HE2"
FT STRAND 492..500
FT /evidence="ECO:0007829|PDB:2HE2"
FT HELIX 502..510
FT /evidence="ECO:0007829|PDB:2HE2"
FT CONFLICT Q15700-5:116
FT /note="D -> E (in Ref. 3; CAI45970)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 870 AA; 97552 MW; BC51554590060E48 CRC64;
MFFACYCALR TNVKKYRYQD EDAPHDHSLP RLTHEVRGPE LVHVSEKNLS QIENVHGYVL
QSHISPLKAS PAPIIVNTDT LDTIPYVNGT EIEYEFEEIT LERGNSGLGF SIAGGTDNPH
IGDDPGIFIT KIIPGGAAAE DGRLRVNDCI LRVNEVDVSE VSHSKAVEAL KEAGSIVRLY
VRRRRPILET VVEIKLFKGP KGLGFSIAGG VGNQHIPGDN SIYVTKIIDG GAAQKDGRLQ
VGDRLLMVNN YSLEEVTHEE AVAILKNTSE VVYLKVGKPT TIYMTDPYGP PDITHSYSPP
MENHLLSGNN GTLEYKTSLP PISPGRYSPI PKHMLVDDDY TRPPEPVYST VNKLCDKPAS
PRHYSPVECD KSFLLSAPYS HYHLGLLPDS EMTSHSQHST ATRQPSMTLQ RAVSLEGEPR
KVVLHKGSTG LGFNIVGGED GEGIFVSFIL AGGPADLSGE LQRGDQILSV NGIDLRGASH
EQAAAALKGA GQTVTIIAQY QPEDYARFEA KIHDLREQMM NHSMSSGSGS LRTNQKRSLY
VRAMFDYDKS KDSGLPSQGL SFKYGDILHV INASDDEWWQ ARRVMLEGDS EEMGVIPSKR
RVERKERARL KTVKFNAKPG VIDSKGSFND KRKKSFIFSR KFPFYKNKEQ SEQETSDPER
GQEDLILSYE PVTRQEINYT RPVIILGPMK DRINDDLISE FPDKFGSCVP HTTRPKRDYE
VDGRDYHFVI SREQMEKDIQ EHKFIEAGQY NDNLYGTSVQ SVRFVAERGK HCILDVSGNA
IKRLQVAQLY PIAIFIKPRS LEPLMEMNKR LTEEQAKKTY DRAIKLEQEF GEYFTAIVQG
DTLEDIYNQC KLVIEEQSGP FIWIPSKEKL
