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Disks large homolog 3 (Neuroendocrine-DLG) (Synapse-associated protein 102) (SAP-102) (SAP102) (XLMR)

 DLG3_HUMAN              Reviewed;         817 AA.
Q92796; B4E0H1; D3DVU5; Q5JUW6; Q5JUW7; Q9ULI8;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
16-DEC-2008, sequence version 2.
27-SEP-2017, entry version 182.
RecName: Full=Disks large homolog 3;
AltName: Full=Neuroendocrine-DLG;
AltName: Full=Synapse-associated protein 102;
Short=SAP-102;
Short=SAP102;
AltName: Full=XLMR;
Name=DLG3; Synonyms=KIAA1232;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH APC.
TISSUE=Fetal brain;
PubMed=9188857; DOI=10.1038/sj.onc.1201087;
Makino K., Kuwahara H., Masuko N., Nishiyama Y., Morisaki T.,
Sasaki J., Nakao M., Kuwano A., Nakata M., Ushio Y., Saya H.;
"Cloning and characterization of NE-dlg: a novel human homolog of the
Drosophila discs large (dlg) tumor suppressor protein interacts with
the APC protein.";
Oncogene 14:2425-2433(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=10574462; DOI=10.1093/dnares/6.5.337;
Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XV.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:337-345(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Thymus, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
INTERACTION WITH NLGN1; NLGN2 AND NLGN3.
PubMed=9278515; DOI=10.1126/science.277.5331.1511;
Irie M., Hata Y., Takeuchi M., Ichtchenko K., Toyoda A., Hirao K.,
Takai Y., Rosahl T.W., Suedhof T.C.;
"Binding of neuroligins to PSD-95.";
Science 277:1511-1515(1997).
[8]
INTERACTION WITH ERBB4.
PubMed=10725395; DOI=10.1073/pnas.97.7.3596;
Garcia R.A., Vasudevan K., Buonanno A.;
"The neuregulin receptor ErbB-4 interacts with PDZ-containing proteins
at neuronal synapses.";
Proc. Natl. Acad. Sci. U.S.A. 97:3596-3601(2000).
[9]
INVOLVEMENT IN MRX90.
PubMed=15185169; DOI=10.1086/422703;
Tarpey P., Parnau J., Blow M., Woffendin H., Bignell G., Cox C.,
Cox J., Davies H., Edkins S., Holden S., Korny A., Mallya U., Moon J.,
O'Meara S., Parker A., Stephens P., Stevens C., Teague J.,
Donnelly A., Mangelsdorf M., Mulley J., Partington M., Turner G.,
Stevenson R., Schwartz C., Young I., Easton D., Bobrow M.,
Futreal P.A., Stratton M.R., Gecz J., Wooster R., Raymond F.L.;
"Mutations in the DLG3 gene cause nonsyndromic X-linked mental
retardation.";
Am. J. Hum. Genet. 75:318-324(2004).
[10]
INTERACTION WITH LRFN1; LRFN2 AND LRFN4.
PubMed=16630835; DOI=10.1016/j.neuron.2006.04.005;
Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H.,
Kaang B.-K., Kim E.;
"SALM synaptic cell adhesion-like molecules regulate the
differentiation of excitatory synapses.";
Neuron 50:233-245(2006).
[11]
INTERACTION WITH FRMPD4.
PubMed=19118189; DOI=10.1523/JNEUROSCI.3112-08.2008;
Lee H.W., Choi J., Shin H., Kim K., Yang J., Na M., Choi S.Y.,
Kang G.B., Eom S.H., Kim H., Kim E.;
"Preso, a novel PSD-95-interacting FERM and PDZ domain protein that
regulates dendritic spine morphogenesis.";
J. Neurosci. 28:14546-14556(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND MET-2 (ISOFORM 3),
CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 3),
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[14]
STRUCTURE BY NMR OF 382-475.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the third PDZ domain of synapse-associated
protein 102.";
Submitted (MAR-2004) to the PDB data bank.
[15]
X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 223-314.
Structural genomics consortium (SGC);
"The crystal structure of the second PDZ domain of human DLG3.";
Submitted (DEC-2005) to the PDB data bank.
[16]
VARIANT [LARGE SCALE ANALYSIS] ARG-40.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Required for learning most likely through its role in
synaptic plasticity following NMDA receptor signaling.
-!- SUBUNIT: Interacts through its PDZ domains with NETO1, GRIN2B and
SYNGAP1. Interacts through its guanylate kinase-like domain with
DLGAP1, DLGAP2, DLGAP3 and DLGAP4. Interacts with FLTP/C1orf192
(By similarity). Interacts through its PDZ domains with APC.
Interacts through its first two PDZ domains with ERBB4. Interacts
through its third PDZ domain with NLGN1, and probably with NLGN2
and NLGN3. Interacts with FRMPD4 (via C-terminus). Interacts with
LRFN1, LRFN2 and LRFN4. {ECO:0000250|UniProtKB:P70175,
ECO:0000269|PubMed:10725395, ECO:0000269|PubMed:16630835,
ECO:0000269|PubMed:19118189, ECO:0000269|PubMed:9188857,
ECO:0000269|PubMed:9278515}.
-!- INTERACTION:
Q9Y2T3:GDA; NbExp=6; IntAct=EBI-80440, EBI-7125239;
Q969R2-2:OSBP2; NbExp=4; IntAct=EBI-80440, EBI-12211505;
P62136:PPP1CA; NbExp=2; IntAct=EBI-80440, EBI-357253;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q92796-1; Sequence=Displayed;
Name=2;
IsoId=Q92796-2; Sequence=VSP_035940, VSP_035941, VSP_035942;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q92796-3; Sequence=VSP_043717, VSP_035942;
Note=No experimental confirmation available. Contains a
N-acetylmethionine at position 1. Initiator Met-1 is removed.
Contains a N-acetylmethionine at position 2.
{ECO:0000244|PubMed:22814378};
-!- DISEASE: Mental retardation, X-linked 90 (MRX90) [MIM:300850]: A
disorder characterized by significantly below average general
intellectual functioning associated with impairments in adaptive
behavior and manifested during the developmental period.
Intellectual deficiency is the only primary symptom of non-
syndromic X-linked mental retardation, while syndromic mental
retardation presents with associated physical, neurological and/or
psychiatric manifestations. {ECO:0000269|PubMed:15185169}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA86546.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; U49089; AAB61453.1; -; mRNA.
EMBL; AB033058; BAA86546.1; ALT_INIT; mRNA.
EMBL; AK303377; BAG64433.1; -; mRNA.
EMBL; AK304020; BAG64935.1; -; mRNA.
EMBL; AK316518; BAH14889.1; -; mRNA.
EMBL; AL139109; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL139398; CAI41022.1; -; Genomic_DNA.
EMBL; AL139398; CAI41023.1; -; Genomic_DNA.
EMBL; CH471132; EAX05333.1; -; Genomic_DNA.
EMBL; CH471132; EAX05335.1; -; Genomic_DNA.
EMBL; CH471132; EAX05337.1; -; Genomic_DNA.
EMBL; CH471132; EAX05338.1; -; Genomic_DNA.
EMBL; BC093864; AAH93864.1; -; mRNA.
EMBL; BC093866; AAH93866.1; -; mRNA.
CCDS; CCDS14403.1; -. [Q92796-1]
CCDS; CCDS43967.1; -. [Q92796-2]
CCDS; CCDS55439.1; -. [Q92796-3]
RefSeq; NP_001159750.1; NM_001166278.1. [Q92796-3]
RefSeq; NP_065781.1; NM_020730.2. [Q92796-2]
RefSeq; NP_066943.2; NM_021120.3. [Q92796-1]
RefSeq; XP_005262305.1; XM_005262248.3. [Q92796-3]
RefSeq; XP_016884815.1; XM_017029326.1. [Q92796-3]
UniGene; Hs.721586; -.
PDB; 1UM7; NMR; -; A=382-475.
PDB; 2FE5; X-ray; 1.10 A; A=223-314.
PDB; 2I1N; X-ray; 1.85 A; A/B=126-222.
PDBsum; 1UM7; -.
PDBsum; 2FE5; -.
PDBsum; 2I1N; -.
ProteinModelPortal; Q92796; -.
SMR; Q92796; -.
BioGrid; 108085; 71.
IntAct; Q92796; 39.
MINT; MINT-109320; -.
STRING; 9606.ENSP00000363480; -.
iPTMnet; Q92796; -.
PhosphoSitePlus; Q92796; -.
BioMuta; DLG3; -.
DMDM; 218512007; -.
EPD; Q92796; -.
MaxQB; Q92796; -.
PaxDb; Q92796; -.
PeptideAtlas; Q92796; -.
PRIDE; Q92796; -.
DNASU; 1741; -.
Ensembl; ENST00000374355; ENSP00000363475; ENSG00000082458. [Q92796-2]
Ensembl; ENST00000374360; ENSP00000363480; ENSG00000082458. [Q92796-1]
Ensembl; ENST00000542398; ENSP00000441393; ENSG00000082458. [Q92796-3]
GeneID; 1741; -.
KEGG; hsa:1741; -.
UCSC; uc004dyi.3; human. [Q92796-1]
CTD; 1741; -.
DisGeNET; 1741; -.
EuPathDB; HostDB:ENSG00000082458.11; -.
GeneCards; DLG3; -.
H-InvDB; HIX0016853; -.
HGNC; HGNC:2902; DLG3.
HPA; HPA001733; -.
HPA; HPA078130; -.
MalaCards; DLG3; -.
MIM; 300189; gene.
MIM; 300850; phenotype.
neXtProt; NX_Q92796; -.
OpenTargets; ENSG00000082458; -.
Orphanet; 777; X-linked non-syndromic intellectual disability.
PharmGKB; PA164741439; -.
eggNOG; KOG0708; Eukaryota.
eggNOG; COG0194; LUCA.
GeneTree; ENSGT00760000118866; -.
HOGENOM; HOG000232102; -.
HOVERGEN; HBG107814; -.
InParanoid; Q92796; -.
KO; K21098; -.
OMA; ASQRWAW; -.
PhylomeDB; Q92796; -.
TreeFam; TF323171; -.
Reactome; R-HSA-447038; NrCAM interactions.
Reactome; R-HSA-451308; Activation of Ca-permeable Kainate Receptor.
Reactome; R-HSA-6794361; Neurexins and neuroligins.
Reactome; R-HSA-8849932; Synaptic adhesion-like molecules.
ChiTaRS; DLG3; human.
EvolutionaryTrace; Q92796; -.
GenomeRNAi; 1741; -.
PRO; PR:Q92796; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000082458; -.
CleanEx; HS_DLG3; -.
ExpressionAtlas; Q92796; baseline and differential.
Genevisible; Q92796; HS.
GO; GO:0032281; C:AMPA glutamate receptor complex; IEA:Ensembl.
GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
GO; GO:0005923; C:bicellular tight junction; IEA:Ensembl.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0043198; C:dendritic shaft; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0030426; C:growth cone; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0014069; C:postsynaptic density of dendrite; IBA:GO_Central.
GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
GO; GO:0004385; F:guanylate kinase activity; IBA:GO_Central.
GO; GO:0035255; F:ionotropic glutamate receptor binding; IBA:GO_Central.
GO; GO:0019900; F:kinase binding; IDA:MGI.
GO; GO:0015276; F:ligand-gated ion channel activity; TAS:Reactome.
GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
GO; GO:0019902; F:phosphatase binding; IDA:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
GO; GO:0001736; P:establishment of planar polarity; IEA:Ensembl.
GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
GO; GO:0008285; P:negative regulation of cell proliferation; NAS:UniProtKB.
GO; GO:0010923; P:negative regulation of phosphatase activity; IDA:UniProtKB.
GO; GO:0007399; P:nervous system development; IBA:GO_Central.
GO; GO:0043113; P:receptor clustering; IBA:GO_Central.
GO; GO:0097120; P:receptor localization to synapse; IBA:GO_Central.
InterPro; IPR016313; DLG1-like.
InterPro; IPR019590; DLG1_PEST_dom.
InterPro; IPR008145; GK/Ca_channel_bsu.
InterPro; IPR008144; Guanylate_kin-like_dom.
InterPro; IPR020590; Guanylate_kinase_CS.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR001478; PDZ.
InterPro; IPR019583; PDZ_assoc.
InterPro; IPR001452; SH3_domain.
Pfam; PF00625; Guanylate_kin; 1.
Pfam; PF00595; PDZ; 3.
Pfam; PF10600; PDZ_assoc; 1.
Pfam; PF00018; SH3_1; 1.
PIRSF; PIRSF001741; MAGUK_DLGH; 1.
SMART; SM00072; GuKc; 1.
SMART; SM01277; MAGUK_N_PEST; 1.
SMART; SM00228; PDZ; 3.
SMART; SM00326; SH3; 1.
SUPFAM; SSF50044; SSF50044; 2.
SUPFAM; SSF50156; SSF50156; 3.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
PROSITE; PS50106; PDZ; 3.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Mental retardation; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; SH3 domain.
CHAIN 1 817 Disks large homolog 3.
/FTId=PRO_0000094557.
DOMAIN 130 217 PDZ 1. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 226 311 PDZ 2. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 379 465 PDZ 3. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 503 568 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 627 802 Guanylate kinase-like.
{ECO:0000255|PROSITE-ProRule:PRU00100}.
MOD_RES 139 139 Phosphoserine.
{ECO:0000250|UniProtKB:P70175}.
MOD_RES 673 673 Phosphotyrosine.
{ECO:0000250|UniProtKB:P70175}.
VAR_SEQ 1 483 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043717.
VAR_SEQ 1 336 Missing (in isoform 2).
{ECO:0000303|PubMed:10574462,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_035940.
VAR_SEQ 337 381 HISHNSSLGYLGAVESKVSYPAPPQVPPTRYSPIPRHMLAE
EDFT -> MERARKFSGSGLAMGLGSASASAWRRASQRWAW
PLRSLRPGGDA (in isoform 2).
{ECO:0000303|PubMed:10574462,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_035941.
VAR_SEQ 592 606 DFPGLSDDYYGAKNL -> SIKTKRKKSFRLSRKFPFYKSK
ENMAQESSIQEQGVTSNTSDSESSS (in isoform 2
and isoform 3).
{ECO:0000303|PubMed:10574462,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_035942.
VARIANT 40 40 G -> R (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036591.
CONFLICT 87 87 P -> L (in Ref. 1; AAB61453).
{ECO:0000305}.
CONFLICT 190 190 D -> E (in Ref. 1; AAB61453).
{ECO:0000305}.
STRAND 127 135 {ECO:0000244|PDB:2I1N}.
STRAND 142 147 {ECO:0000244|PDB:2I1N}.
STRAND 160 165 {ECO:0000244|PDB:2I1N}.
HELIX 170 174 {ECO:0000244|PDB:2I1N}.
STRAND 182 186 {ECO:0000244|PDB:2I1N}.
HELIX 196 205 {ECO:0000244|PDB:2I1N}.
STRAND 208 217 {ECO:0000244|PDB:2I1N}.
STRAND 224 230 {ECO:0000244|PDB:2FE5}.
STRAND 238 242 {ECO:0000244|PDB:2FE5}.
STRAND 255 260 {ECO:0000244|PDB:2FE5}.
HELIX 265 269 {ECO:0000244|PDB:2FE5}.
STRAND 277 281 {ECO:0000244|PDB:2FE5}.
HELIX 291 299 {ECO:0000244|PDB:2FE5}.
STRAND 303 310 {ECO:0000244|PDB:2FE5}.
STRAND 383 390 {ECO:0000244|PDB:1UM7}.
STRAND 396 398 {ECO:0000244|PDB:1UM7}.
STRAND 416 418 {ECO:0000244|PDB:1UM7}.
HELIX 419 422 {ECO:0000244|PDB:1UM7}.
STRAND 431 437 {ECO:0000244|PDB:1UM7}.
HELIX 445 453 {ECO:0000244|PDB:1UM7}.
STRAND 457 464 {ECO:0000244|PDB:1UM7}.
HELIX 467 475 {ECO:0000244|PDB:1UM7}.
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


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