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 27-MAR-2024, entry version 219. 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; O60469: DSCAM; NbExp=3; IntAct=EBI-80426, EBI-19949317; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 29. DR MINT; Q15700; -. DR STRING; 9606.ENSP00000365272; -. DR GlyGen; Q15700; 1 site, 1 O-linked glycan (1 site). 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; 9606-ENSP00000365272; -. DR PeptideAtlas; 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; 429 antibodies from 35 providers. DR DNASU; 1740; -. DR Ensembl; ENST00000280241.12; ENSP00000280241.8; ENSG00000150672.19. [Q15700-4] DR Ensembl; ENST00000376104.7; ENSP00000365272.2; ENSG00000150672.19. [Q15700-2] DR Ensembl; ENST00000398309.6; ENSP00000381355.2; ENSG00000150672.19. [Q15700-1] DR Ensembl; ENST00000418306.6; ENSP00000402275.2; ENSG00000150672.19. [Q15700-3] DR Ensembl; ENST00000426717.6; ENSP00000393049.2; ENSG00000150672.19. [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 AGR; HGNC:2901; -. 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; 2879721at2759; -. 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 1143 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 135 other cell types or tissues. DR ExpressionAtlas; Q15700; baseline and differential. DR GO; GO:0005912; C:adherens junction; NAS:ComplexPortal. DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC. DR GO; GO:0016323; C:basolateral plasma membrane; 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; cd00071; GMPK; 1. DR CDD; cd00992; PDZ_signaling; 3. DR CDD; cd12032; SH3_DLG2; 1. DR Gene3D; 2.30.42.10; -; 3. DR Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 2. DR InterPro; IPR019583; DLG1-4_PDZ_assoc. 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; IPR036034; PDZ_sf. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR PANTHER; PTHR23119; DISCS LARGE; 1. DR PANTHER; PTHR23119:SF6; DISKS LARGE HOMOLOG 2; 1. 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50156; PDZ domain-like; 3. DR SUPFAM; SSF50044; SH3-domain; 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. DR Genevisible; Q15700; HS. 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 //