DLG3_HUMAN
ID DLG3_HUMAN Reviewed; 817 AA.
AC Q92796; B4E0H1; D3DVU5; Q5JUW6; Q5JUW7; Q9ULI8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Disks large homolog 3;
DE AltName: Full=Neuroendocrine-DLG;
DE AltName: Full=Synapse-associated protein 102;
DE Short=SAP-102;
DE Short=SAP102;
DE AltName: Full=XLMR;
GN Name=DLG3; Synonyms=KIAA1232;
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), AND INTERACTION WITH APC.
RC TISSUE=Fetal brain;
RX PubMed=9188857; DOI=10.1038/sj.onc.1201087;
RA Makino K., Kuwahara H., Masuko N., Nishiyama Y., Morisaki T., Sasaki J.,
RA Nakao M., Kuwano A., Nakata M., Ushio Y., Saya H.;
RT "Cloning and characterization of NE-dlg: a novel human homolog of the
RT Drosophila discs large (dlg) tumor suppressor protein interacts with the
RT APC protein.";
RL Oncogene 14:2425-2433(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Thymus, and Trachea;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [7]
RP INTERACTION WITH NLGN1; NLGN2 AND NLGN3.
RX PubMed=9278515; DOI=10.1126/science.277.5331.1511;
RA Irie M., Hata Y., Takeuchi M., Ichtchenko K., Toyoda A., Hirao K.,
RA Takai Y., Rosahl T.W., Suedhof T.C.;
RT "Binding of neuroligins to PSD-95.";
RL Science 277:1511-1515(1997).
RN [8]
RP INTERACTION WITH ERBB4.
RX PubMed=10725395; DOI=10.1073/pnas.97.7.3596;
RA Garcia R.A., Vasudevan K., Buonanno A.;
RT "The neuregulin receptor ErbB-4 interacts with PDZ-containing proteins at
RT neuronal synapses.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3596-3601(2000).
RN [9]
RP INVOLVEMENT IN XLID90.
RX PubMed=15185169; DOI=10.1086/422703;
RA Tarpey P., Parnau J., Blow M., Woffendin H., Bignell G., Cox C., Cox J.,
RA Davies H., Edkins S., Holden S., Korny A., Mallya U., Moon J., O'Meara S.,
RA Parker A., Stephens P., Stevens C., Teague J., Donnelly A., Mangelsdorf M.,
RA Mulley J., Partington M., Turner G., Stevenson R., Schwartz C., Young I.,
RA Easton D., Bobrow M., Futreal P.A., Stratton M.R., Gecz J., Wooster R.,
RA Raymond F.L.;
RT "Mutations in the DLG3 gene cause nonsyndromic X-linked mental
RT retardation.";
RL Am. J. Hum. Genet. 75:318-324(2004).
RN [10]
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 [11]
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 [12]
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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND MET-2 (ISOFORM 3), CLEAVAGE
RP OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 3), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP STRUCTURE BY NMR OF 382-475.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the third PDZ domain of synapse-associated protein
RT 102.";
RL Submitted (MAR-2004) to the PDB data bank.
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 223-314.
RG Structural genomics consortium (SGC);
RT "The crystal structure of the second PDZ domain of human DLG3.";
RL Submitted (DEC-2005) to the PDB data bank.
RN [16]
RP VARIANT [LARGE SCALE ANALYSIS] ARG-40.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Required for learning most likely through its role in
CC synaptic plasticity following NMDA receptor signaling.
CC -!- SUBUNIT: Interacts through its PDZ domains with NETO1, GRIN2B and
CC SYNGAP1. Interacts through its guanylate kinase-like domain with
CC DLGAP1, DLGAP2, DLGAP3 and DLGAP4. Interacts with FLTP/C1orf192 (By
CC similarity). Interacts through its PDZ domains with APC. Interacts
CC through its first two PDZ domains with ERBB4. Interacts through its
CC third PDZ domain with NLGN1, and probably with NLGN2 and NLGN3.
CC Interacts with FRMPD4 (via C-terminus). Interacts with LRFN1, LRFN2 and
CC LRFN4. Interacts with DGKI (via PDZ-binding motif) (By similarity).
CC {ECO:0000250|UniProtKB:P70175, ECO:0000250|UniProtKB:Q62936,
CC ECO:0000269|PubMed:10725395, ECO:0000269|PubMed:16630835,
CC ECO:0000269|PubMed:19118189, ECO:0000269|PubMed:9188857,
CC ECO:0000269|PubMed:9278515}.
CC -!- INTERACTION:
CC Q92796; Q6UWP2-2: DHRS11; NbExp=3; IntAct=EBI-80440, EBI-12225017;
CC Q92796; Q6IS01: DLGAP1; NbExp=3; IntAct=EBI-80440, EBI-11961832;
CC Q92796; Q9P1A6-3: DLGAP2; NbExp=3; IntAct=EBI-80440, EBI-12019838;
CC Q92796; Q15056-2: EIF4H; NbExp=3; IntAct=EBI-80440, EBI-12222405;
CC Q92796; P24390: KDELR1; NbExp=3; IntAct=EBI-80440, EBI-1043076;
CC Q92796; Q969R2-2: OSBP2; NbExp=3; IntAct=EBI-80440, EBI-12211505;
CC Q92796; Q9HB19: PLEKHA2; NbExp=3; IntAct=EBI-80440, EBI-4401947;
CC Q92796; P62136: PPP1CA; NbExp=2; IntAct=EBI-80440, EBI-357253;
CC Q92796; P62241: RPS8; NbExp=3; IntAct=EBI-80440, EBI-351811;
CC Q92796; P04004: VTN; NbExp=3; IntAct=EBI-80440, EBI-1036653;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q92796-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92796-2; Sequence=VSP_035940, VSP_035941, VSP_035942;
CC Name=3;
CC IsoId=Q92796-3; Sequence=VSP_043717, VSP_035942;
CC -!- DISEASE: Intellectual developmental disorder, X-linked 90 (XLID90)
CC [MIM:300850]: A disorder characterized by significantly below average
CC general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period.
CC Intellectual deficiency is the only primary symptom of non-syndromic X-
CC linked intellectual disability, while syndromic forms presents with
CC associated physical, neurological and/or psychiatric manifestations.
CC {ECO:0000269|PubMed:15185169}. 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=BAA86546.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U49089; AAB61453.1; -; mRNA.
DR EMBL; AB033058; BAA86546.1; ALT_INIT; mRNA.
DR EMBL; AK303377; BAG64433.1; -; mRNA.
DR EMBL; AK304020; BAG64935.1; -; mRNA.
DR EMBL; AK316518; BAH14889.1; -; mRNA.
DR EMBL; AL139109; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471132; EAX05333.1; -; Genomic_DNA.
DR EMBL; CH471132; EAX05335.1; -; Genomic_DNA.
DR EMBL; CH471132; EAX05337.1; -; Genomic_DNA.
DR EMBL; CH471132; EAX05338.1; -; Genomic_DNA.
DR EMBL; BC093864; AAH93864.1; -; mRNA.
DR EMBL; BC093866; AAH93866.1; -; mRNA.
DR CCDS; CCDS14403.1; -. [Q92796-1]
DR CCDS; CCDS43967.1; -. [Q92796-2]
DR CCDS; CCDS55439.1; -. [Q92796-3]
DR RefSeq; NP_001159750.1; NM_001166278.1. [Q92796-3]
DR RefSeq; NP_065781.1; NM_020730.2. [Q92796-2]
DR RefSeq; NP_066943.2; NM_021120.3. [Q92796-1]
DR RefSeq; XP_005262305.1; XM_005262248.3. [Q92796-3]
DR RefSeq; XP_016884815.1; XM_017029326.1. [Q92796-3]
DR PDB; 1UM7; NMR; -; A=382-475.
DR PDB; 2FE5; X-ray; 1.10 A; A=223-314.
DR PDB; 2I1N; X-ray; 1.85 A; A/B=126-222.
DR PDBsum; 1UM7; -.
DR PDBsum; 2FE5; -.
DR PDBsum; 2I1N; -.
DR AlphaFoldDB; Q92796; -.
DR SMR; Q92796; -.
DR BioGRID; 108085; 98.
DR ComplexPortal; CPX-6185; Scribble cell polarity complex, DLG3-LLGL2-SCRIB variant.
DR ComplexPortal; CPX-6190; Scribble cell polarity complex, DLG3-LLGL1-SCRIB variant.
DR IntAct; Q92796; 42.
DR MINT; Q92796; -.
DR STRING; 9606.ENSP00000363480; -.
DR iPTMnet; Q92796; -.
DR PhosphoSitePlus; Q92796; -.
DR BioMuta; DLG3; -.
DR DMDM; 218512007; -.
DR EPD; Q92796; -.
DR jPOST; Q92796; -.
DR MassIVE; Q92796; -.
DR MaxQB; Q92796; -.
DR PaxDb; Q92796; -.
DR PeptideAtlas; Q92796; -.
DR PRIDE; Q92796; -.
DR ProteomicsDB; 75474; -. [Q92796-1]
DR ProteomicsDB; 75475; -. [Q92796-2]
DR ProteomicsDB; 75476; -. [Q92796-3]
DR ABCD; Q92796; 2 sequenced antibodies.
DR Antibodypedia; 342; 341 antibodies from 34 providers.
DR DNASU; 1741; -.
DR Ensembl; ENST00000374355.7; ENSP00000363475.3; ENSG00000082458.12. [Q92796-2]
DR Ensembl; ENST00000374360.8; ENSP00000363480.3; ENSG00000082458.12. [Q92796-1]
DR Ensembl; ENST00000542398.1; ENSP00000441393.1; ENSG00000082458.12. [Q92796-3]
DR GeneID; 1741; -.
DR KEGG; hsa:1741; -.
DR MANE-Select; ENST00000374360.8; ENSP00000363480.3; NM_021120.4; NP_066943.2.
DR UCSC; uc004dyi.3; human. [Q92796-1]
DR CTD; 1741; -.
DR DisGeNET; 1741; -.
DR GeneCards; DLG3; -.
DR HGNC; HGNC:2902; DLG3.
DR HPA; ENSG00000082458; Low tissue specificity.
DR MalaCards; DLG3; -.
DR MIM; 300189; gene.
DR MIM; 300850; phenotype.
DR neXtProt; NX_Q92796; -.
DR OpenTargets; ENSG00000082458; -.
DR Orphanet; 777; X-linked non-syndromic intellectual disability.
DR PharmGKB; PA164741439; -.
DR VEuPathDB; HostDB:ENSG00000082458; -.
DR eggNOG; KOG0708; Eukaryota.
DR GeneTree; ENSGT00940000159565; -.
DR HOGENOM; CLU_001715_4_2_1; -.
DR InParanoid; Q92796; -.
DR OMA; VPANEMF; -.
DR OrthoDB; 807583at2759; -.
DR PhylomeDB; Q92796; -.
DR TreeFam; TF323171; -.
DR PathwayCommons; Q92796; -.
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-447038; NrCAM interactions.
DR Reactome; R-HSA-451308; Activation of Ca-permeable Kainate Receptor.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR Reactome; R-HSA-8849932; Synaptic adhesion-like molecules.
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; Q92796; -.
DR SIGNOR; Q92796; -.
DR BioGRID-ORCS; 1741; 9 hits in 708 CRISPR screens.
DR ChiTaRS; DLG3; human.
DR EvolutionaryTrace; Q92796; -.
DR GenomeRNAi; 1741; -.
DR Pharos; Q92796; Tbio.
DR PRO; PR:Q92796; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q92796; protein.
DR Bgee; ENSG00000082458; Expressed in cortical plate and 195 other tissues.
DR ExpressionAtlas; Q92796; baseline and differential.
DR Genevisible; Q92796; HS.
DR GO; GO:0005912; C:adherens junction; IC:ComplexPortal.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; IEA:Ensembl.
DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR GO; GO:0005923; C:bicellular tight junction; IEA:Ensembl.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0019900; F:kinase binding; IDA:MGI.
DR GO; GO:0019902; F:phosphatase binding; IDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0001736; P:establishment of planar polarity; IEA:Ensembl.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; NAS:UniProtKB.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; ISS:ARUK-UCL.
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:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; IEA:Ensembl.
DR CDD; cd12029; SH3_DLG3; 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; IPR035763; DLG3_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; 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; Acetylation; Alternative splicing; Intellectual disability;
KW Phosphoprotein; Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..817
FT /note="Disks large homolog 3"
FT /id="PRO_0000094557"
FT DOMAIN 130..217
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 226..311
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 379..465
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 501..571
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 627..802
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT REGION 33..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70175"
FT MOD_RES 673
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P70175"
FT VAR_SEQ 1..483
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043717"
FT VAR_SEQ 1..336
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10574462,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_035940"
FT VAR_SEQ 337..381
FT /note="HISHNSSLGYLGAVESKVSYPAPPQVPPTRYSPIPRHMLAEEDFT -> MER
FT ARKFSGSGLAMGLGSASASAWRRASQRWAWPLRSLRPGGDA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10574462,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_035941"
FT VAR_SEQ 592..606
FT /note="DFPGLSDDYYGAKNL -> SIKTKRKKSFRLSRKFPFYKSKENMAQESSIQE
FT QGVTSNTSDSESSS (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10574462,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_035942"
FT VARIANT 40
FT /note="G -> R (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs1449722258)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036591"
FT CONFLICT 87
FT /note="P -> L (in Ref. 1; AAB61453)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="D -> E (in Ref. 1; AAB61453)"
FT /evidence="ECO:0000305"
FT STRAND 127..135
FT /evidence="ECO:0007829|PDB:2I1N"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:2I1N"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:2I1N"
FT HELIX 170..174
FT /evidence="ECO:0007829|PDB:2I1N"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:2I1N"
FT HELIX 196..205
FT /evidence="ECO:0007829|PDB:2I1N"
FT STRAND 208..217
FT /evidence="ECO:0007829|PDB:2I1N"
FT STRAND 224..230
FT /evidence="ECO:0007829|PDB:2FE5"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:2FE5"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:2FE5"
FT HELIX 265..269
FT /evidence="ECO:0007829|PDB:2FE5"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:2FE5"
FT HELIX 291..299
FT /evidence="ECO:0007829|PDB:2FE5"
FT STRAND 303..310
FT /evidence="ECO:0007829|PDB:2FE5"
FT STRAND 383..390
FT /evidence="ECO:0007829|PDB:1UM7"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:1UM7"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:1UM7"
FT HELIX 419..422
FT /evidence="ECO:0007829|PDB:1UM7"
FT STRAND 431..437
FT /evidence="ECO:0007829|PDB:1UM7"
FT HELIX 445..453
FT /evidence="ECO:0007829|PDB:1UM7"
FT STRAND 457..464
FT /evidence="ECO:0007829|PDB:1UM7"
FT HELIX 467..475
FT /evidence="ECO:0007829|PDB:1UM7"
FT INIT_MET Q92796-3:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES Q92796-3:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES Q92796-3:2
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 817 AA; 90314 MW; CE125E9BEE3EEC66 CRC64;
MHKHQHCCKC PECYEVTRLA ALRRLEPPGY GDWQVPDPYG PGGGNGASAG YGGYSSQTLP
SQAGATPTPR TKAKLIPTGR DVGPVPPKPV PGKSTPKLNG SGPSWWPECT CTNRDWYEQV
NGSDGMFKYE EIVLERGNSG LGFSIAGGID NPHVPDDPGI FITKIIPGGA AAMDGRLGVN
DCVLRVNEVD VSEVVHSRAV EALKEAGPVV RLVVRRRQPP PETIMEVNLL KGPKGLGFSI
AGGIGNQHIP GDNSIYITKI IEGGAAQKDG RLQIGDRLLA VNNTNLQDVR HEEAVASLKN
TSDMVYLKVA KPGSLHLNDM YAPPDYASTF TALADNHISH NSSLGYLGAV ESKVSYPAPP
QVPPTRYSPI PRHMLAEEDF TREPRKIILH KGSTGLGFNI VGGEDGEGIF VSFILAGGPA
DLSGELRRGD RILSVNGVNL RNATHEQAAA ALKRAGQSVT IVAQYRPEEY SRFESKIHDL
REQMMNSSMS SGSGSLRTSE KRSLYVRALF DYDRTRDSCL PSQGLSFSYG DILHVINASD
DEWWQARLVT PHGESEQIGV IPSKKRVEKK ERARLKTVKF HARTGMIESN RDFPGLSDDY
YGAKNLKGQE DAILSYEPVT RQEIHYARPV IILGPMKDRV NDDLISEFPH KFGSCVPHTT
RPRRDNEVDG QDYHFVVSRE QMEKDIQDNK FIEAGQFNDN LYGTSIQSVR AVAERGKHCI
LDVSGNAIKR LQQAQLYPIA IFIKPKSIEA LMEMNRRQTY EQANKIYDKA MKLEQEFGEY
FTAIVQGDSL EEIYNKIKQI IEDQSGHYIW VPSPEKL
