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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Disks large-associated protein 2''' is a [[protein]] that in humans is encoded by the ''DLGAP2'' [[gene]].<ref name="pmid9286858">{{cite journal | vauthors = Satoh K, Yanai H, Senda T, Kohu K, Nakamura T, Okumura N, Matsumine A, Kobayashi S, Toyoshima K, Akiyama T | title = DAP-1, a novel protein that interacts with the guanylate kinase-like domains of hDLG and PSD-95 | journal = Genes Cells | volume = 2 | issue = 6 | pages = 415–24 |date=Oct 1997 | pmid = 9286858 | pmc =  | doi =10.1046/j.1365-2443.1997.1310329.x  }}</ref><ref name="pmid10854099">{{cite journal | vauthors = Ranta S, Zhang Y, Ross B, Takkunen E, Hirvasniemi A, de la Chapelle A, Gilliam TC, Lehesjoki AE | title = Positional cloning and characterisation of the human DLGAP2 gene and its exclusion in progressive epilepsy with mental retardation | journal = Eur J Hum Genet | volume = 8 | issue = 5 | pages = 381–4 |date=Sep 2000 | pmid = 10854099 | pmc = | doi = 10.1038/sj.ejhg.5200440 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: DLGAP2 discs, large (Drosophila) homolog-associated protein 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9228| accessdate = }}</ref>
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| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Discs, large (Drosophila) homolog-associated protein 2
| HGNCid = 2906
| Symbol = DLGAP2
| AltSymbols =; DAP2; SAPAP2
| OMIM = 605438
| ECnumber = 
| Homologene = 3484
| MGIid = 2443181
| GeneAtlas_image1 = PBB_GE_DLGAP2_216916_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003707 |text = steroid hormone receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005883 |text = neurofilament}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007270 |text = nerve-nerve synaptic transmission}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 9228
    | Hs_Ensembl = ENSG00000198010
    | Hs_RefseqProtein = NP_004736
    | Hs_RefseqmRNA = NM_004745
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 8
    | Hs_GenLoc_start = 1436941
    | Hs_GenLoc_end = 1637558
    | Hs_Uniprot = Q9P1A6
    | Mm_EntrezGene = 244310
    | Mm_Ensembl = ENSMUSG00000047495
    | Mm_RefseqmRNA = NM_172910
    | Mm_RefseqProtein = NP_766498
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 14531001
    | Mm_GenLoc_end = 14847657
    | Mm_Uniprot = Q0VF59
  }}
}}
'''Discs, large (Drosophila) homolog-associated protein 2''', also known as '''DLGAP2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DLGAP2 discs, large (Drosophila) homolog-associated protein 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9228| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The product of this gene is one of the membrane-associated guanylate kinases localized at postsynaptic density in neuronal cells. These kinases are a family of signaling molecules expressed at various submembrane domains and contain the PDZ, SH3 and the guanylate kinase domains. This protein may play a role in the molecular organization of synapses and in neuronal cell signaling. Alternatively spliced transcript variants encoding different isoforms have been identified, but their full-length nature is not known.<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = The product of this gene is one of the membrane-associated guanylate kinases localized at postsynaptic density in neuronal cells. These kinases are a family of signaling molecules expressed at various submembrane domains and contain the PDZ, SH3 and the guanylate kinase domains. This protein may play a role in the molecular organization of synapses and in neuronal cell signaling. Alternatively spliced transcript variants encoding different isoforms have been identified, but their full-length nature is not known.<ref name="entrez">{{cite web | title = Entrez Gene: DLGAP2 discs, large (Drosophila) homolog-associated protein 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9228| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
DLGAP2 has been shown to [[Protein-protein interaction|interact]] with [[DLG4]], the canonical synapse marker protein, which in turn binds to N-methyld-aspartate (NMDA) receptors and Shaker-type K+ channels.<ref name="pmid9115257">{{cite journal | vauthors = Takeuchi M, Hata Y, Hirao K, Toyoda A, Irie M, Takai Y | title = SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density | journal = J. Biol. Chem. | volume = 272 | issue = 18 | pages = 11943–51 | year = 1997 | pmid = 9115257 | doi = 10.1074/jbc.272.18.11943 }}</ref>
 
== Clinical significance ==
 
As with many other synaptic genes, including its binding partner Shank2, DLGAP2 has been shown to be associated with Autism.<ref name="pmid20531469">{{cite journal| vauthors=Pinto D, Pagnamenta AT, Klei L, Anney R, Merico D, Regan R| title=Functional impact of global rare copy number variation in autism spectrum disorders. | journal=Nature | year= 2010 | volume= 466 | issue= 7304 | pages= 368–72 | pmid=20531469 | doi=10.1038/nature09146 | pmc=3021798  |display-authors=etal| url=http://www.hal.inserm.fr/inserm-00521387/document}}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal  | vauthors=Takeuchi M, Hata Y, Hirao K |title=SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density |journal=J. Biol. Chem. |volume=272 |issue= 18 |pages= 11943–51 |year= 1997 |pmid= 9115257 |doi=10.1074/jbc.272.18.11943 |display-authors=etal}}
| citations =
*{{cite journal  | vauthors=Naisbitt S, Kim E, Weinberg RJ |title=Characterization of guanylate kinase-associated protein, a postsynaptic density protein at excitatory synapses that interacts directly with postsynaptic density-95/synapse-associated protein 90 |journal=J. Neurosci. |volume=17 |issue= 15 |pages= 5687–96 |year= 1997 |pmid= 9221768 |doi=  |display-authors=etal}}
*{{cite journal  | author=Takeuchi M, Hata Y, Hirao K, ''et al.'' |title=SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density. |journal=J. Biol. Chem. |volume=272 |issue= 18 |pages= 11943-51 |year= 1997 |pmid= 9115257 |doi=  }}
*{{cite journal  | vauthors=Ranta S, Lehesjoki AE, de Fatima Bonaldo M |title=High-resolution mapping and transcript identification at the progressive epilepsy with mental retardation locus on chromosome 8p |journal=Genome Res. |volume=7 |issue= 9 |pages= 887–96 |year= 1997 |pmid= 9314494 |doi= 10.1101/gr.7.9.887 |display-authors=etal}}
*{{cite journal  | author=Naisbitt S, Kim E, Weinberg RJ, ''et al.'' |title=Characterization of guanylate kinase-associated protein, a postsynaptic density protein at excitatory synapses that interacts directly with postsynaptic density-95/synapse-associated protein 90. |journal=J. Neurosci. |volume=17 |issue= 15 |pages= 5687-96 |year= 1997 |pmid= 9221768 |doi=  }}
*{{cite journal  | vauthors=Hirao K, Hata Y, Ide N |title=A novel multiple PDZ domain-containing molecule interacting with N-methyl-D-aspartate receptors and neuronal cell adhesion proteins |journal=J. Biol. Chem. |volume=273 |issue= 33 |pages= 21105–10 |year= 1998 |pmid= 9694864 |doi=10.1074/jbc.273.33.21105 |display-authors=etal}}
*{{cite journal  | author=Satoh K, Yanai H, Senda T, ''et al.'' |title=DAP-1, a novel protein that interacts with the guanylate kinase-like domains of hDLG and PSD-95. |journal=Genes Cells |volume=2 |issue= 6 |pages= 415-24 |year= 1997 |pmid= 9286858 |doi=  }}
*{{cite journal  | vauthors=Kawabe H, Hata Y, Takeuchi M |title=nArgBP2, a novel neural member of ponsin/ArgBP2/vinexin family that interacts with synapse-associated protein 90/postsynaptic density-95-associated protein (SAPAP) |journal=J. Biol. Chem. |volume=274 |issue= 43 |pages= 30914–8 |year= 1999 |pmid= 10521485 |doi=10.1074/jbc.274.43.30914 |display-authors=etal}}
*{{cite journal  | author=Ranta S, Lehesjoki AE, de Fatima Bonaldo M, ''et al.'' |title=High-resolution mapping and transcript identification at the progressive epilepsy with mental retardation locus on chromosome 8p. |journal=Genome Res. |volume=7 |issue= 9 |pages= 887-96 |year= 1997 |pmid= 9314494 |doi= }}
*{{cite journal  | vauthors=Hirao K, Hata Y, Deguchi M |title=Association of synapse-associated protein 90/ postsynaptic density-95-associated protein (SAPAP) with neurofilaments |journal=Genes Cells |volume=5 |issue= 3 |pages= 203–10 |year= 2000 |pmid= 10759891 |doi=10.1046/j.1365-2443.2000.00318.x |display-authors=etal}}
*{{cite journal  | author=Hirao K, Hata Y, Ide N, ''et al.'' |title=A novel multiple PDZ domain-containing molecule interacting with N-methyl-D-aspartate receptors and neuronal cell adhesion proteins. |journal=J. Biol. Chem. |volume=273 |issue= 33 |pages= 21105-10 |year= 1998 |pmid= 9694864 |doi=  }}
*{{cite journal  | vauthors=Wang P, Zhang Q, Tochio H |title=Formation of a native-like beta-hairpin finger structure of a peptide from the extended PDZ domain of neuronal nitric oxide synthase in aqueous solution |journal=Eur. J. Biochem. |volume=267 |issue= 11 |pages= 3116–22 |year= 2000 |pmid= 10824095 |doi=10.1046/j.1432-1327.2000.01318.x  |display-authors=etal}}
*{{cite journal  | author=Kawabe H, Hata Y, Takeuchi M, ''et al.'' |title=nArgBP2, a novel neural member of ponsin/ArgBP2/vinexin family that interacts with synapse-associated protein 90/postsynaptic density-95-associated protein (SAPAP). |journal=J. Biol. Chem. |volume=274 |issue= 43 |pages= 30914-8 |year= 1999 |pmid= 10521485 |doi=  }}
*{{cite journal  | vauthors=Bolliger MF, Frei K, Winterhalter KH, Gloor SM |title=Identification of a novel neuroligin in humans which binds to PSD-95 and has a widespread expression |journal=Biochem. J. |volume=356 |issue= Pt 2 |pages= 581–8 |year= 2001 |pmid= 11368788 |doi=10.1042/0264-6021:3560581  | pmc=1221872 }}
*{{cite journal  | author=Hirao K, Hata Y, Deguchi M, ''et al.'' |title=Association of synapse-associated protein 90/ postsynaptic density-95-associated protein (SAPAP) with neurofilaments. |journal=Genes Cells |volume=5 |issue= 3 |pages= 203-10 |year= 2000 |pmid= 10759891 |doi=  }}
*{{cite journal  | vauthors=Hu LA, Chen W, Premont RT |title=G protein-coupled receptor kinase 5 regulates beta 1-adrenergic receptor association with PSD-95 |journal=J. Biol. Chem. |volume=277 |issue= 2 |pages= 1607–13 |year= 2002 |pmid= 11700307 |doi= 10.1074/jbc.M107297200 |display-authors=etal}}
*{{cite journal  | author=Wang P, Zhang Q, Tochio H, ''et al.'' |title=Formation of a native-like beta-hairpin finger structure of a peptide from the extended PDZ domain of neuronal nitric oxide synthase in aqueous solution. |journal=Eur. J. Biochem. |volume=267 |issue= 11 |pages= 3116-22 |year= 2000 |pmid= 10824095 |doi= }}
*{{cite journal  | vauthors=Ohtakara K, Nishizawa M, Izawa I |title=Densin-180, a synaptic protein, links to PSD-95 through its direct interaction with MAGUIN-1 |journal=Genes Cells |volume=7 |issue= 11 |pages= 1149–60 |year= 2003 |pmid= 12390249 |doi=10.1046/j.1365-2443.2002.00589.x |display-authors=etal}}
*{{cite journal  | author=Ranta S, Zhang Y, Ross B, ''et al.'' |title=Positional cloning and characterisation of the human DLGAP2 gene and its exclusion in progressive epilepsy with mental retardation. |journal=Eur. J. Hum. Genet. |volume=8 |issue= 5 |pages= 381-4 |year= 2000 |pmid= 10854099 |doi= 10.1038/sj.ejhg.5200440 }}
*{{cite journal  | vauthors=Verhoeven K, De Jonghe P, Van de Putte T |title=Slowed conduction and thin myelination of peripheral nerves associated with mutant rho Guanine-nucleotide exchange factor 10 |journal=Am. J. Hum. Genet. |volume=73 |issue= 4 |pages= 926–32 |year= 2003 |pmid= 14508709 |doi= 10.1086/378159 | pmc=1180612 |display-authors=etal}}
*{{cite journal  | author=Bolliger MF, Frei K, Winterhalter KH, Gloor SM |title=Identification of a novel neuroligin in humans which binds to PSD-95 and has a widespread expression. |journal=Biochem. J. |volume=356 |issue= Pt 2 |pages= 581-8 |year= 2001 |pmid= 11368788 |doi=  }}
*{{cite journal  | vauthors=Ying Z, Bingaman W, Najm IM |title=Increased numbers of coassembled PSD-95 to NMDA-receptor subunits NR2B and NR1 in human epileptic cortical dysplasia |journal=Epilepsia |volume=45 |issue= 4 |pages= 314–21 |year= 2004 |pmid= 15030493 |doi= 10.1111/j.0013-9580.2004.37703.x }}
*{{cite journal  | author=Hu LA, Chen W, Premont RT, ''et al.'' |title=G protein-coupled receptor kinase 5 regulates beta 1-adrenergic receptor association with PSD-95. |journal=J. Biol. Chem. |volume=277 |issue= 2 |pages= 1607-13 |year= 2002 |pmid= 11700307 |doi= 10.1074/jbc.M107297200 }}
*{{cite journal  | author=Ohtakara K, Nishizawa M, Izawa I, ''et al.'' |title=Densin-180, a synaptic protein, links to PSD-95 through its direct interaction with MAGUIN-1. |journal=Genes Cells |volume=7 |issue= 11 |pages= 1149-60 |year= 2003 |pmid= 12390249 |doi=  }}
*{{cite journal  | author=Verhoeven K, De Jonghe P, Van de Putte T, ''et al.'' |title=Slowed conduction and thin myelination of peripheral nerves associated with mutant rho Guanine-nucleotide exchange factor 10. |journal=Am. J. Hum. Genet. |volume=73 |issue= 4 |pages= 926-32 |year= 2003 |pmid= 14508709 |doi= 10.1086/378159 }}
*{{cite journal  | author=Ying Z, Bingaman W, Najm IM |title=Increased numbers of coassembled PSD-95 to NMDA-receptor subunits NR2B and NR1 in human epileptic cortical dysplasia. |journal=Epilepsia |volume=45 |issue= 4 |pages= 314-21 |year= 2004 |pmid= 15030493 |doi= 10.1111/j.0013-9580.2004.37703.x }}
}}
{{refend}}
{{refend}}


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Latest revision as of 08:45, 10 January 2019

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Disks large-associated protein 2 is a protein that in humans is encoded by the DLGAP2 gene.[1][2][3]

Function

The product of this gene is one of the membrane-associated guanylate kinases localized at postsynaptic density in neuronal cells. These kinases are a family of signaling molecules expressed at various submembrane domains and contain the PDZ, SH3 and the guanylate kinase domains. This protein may play a role in the molecular organization of synapses and in neuronal cell signaling. Alternatively spliced transcript variants encoding different isoforms have been identified, but their full-length nature is not known.[3]

Interactions

DLGAP2 has been shown to interact with DLG4, the canonical synapse marker protein, which in turn binds to N-methyld-aspartate (NMDA) receptors and Shaker-type K+ channels.[4]

Clinical significance

As with many other synaptic genes, including its binding partner Shank2, DLGAP2 has been shown to be associated with Autism.[5]

References

  1. ↑ Satoh K, Yanai H, Senda T, Kohu K, Nakamura T, Okumura N, Matsumine A, Kobayashi S, Toyoshima K, Akiyama T (Oct 1997). "DAP-1, a novel protein that interacts with the guanylate kinase-like domains of hDLG and PSD-95". Genes Cells. 2 (6): 415–24. doi:10.1046/j.1365-2443.1997.1310329.x. PMID 9286858.
  2. ↑ Ranta S, Zhang Y, Ross B, Takkunen E, Hirvasniemi A, de la Chapelle A, Gilliam TC, Lehesjoki AE (Sep 2000). "Positional cloning and characterisation of the human DLGAP2 gene and its exclusion in progressive epilepsy with mental retardation". Eur J Hum Genet. 8 (5): 381–4. doi:10.1038/sj.ejhg.5200440. PMID 10854099.
  3. ↑ 3.0 3.1 "Entrez Gene: DLGAP2 discs, large (Drosophila) homolog-associated protein 2".
  4. ↑ Takeuchi M, Hata Y, Hirao K, Toyoda A, Irie M, Takai Y (1997). "SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density". J. Biol. Chem. 272 (18): 11943–51. doi:10.1074/jbc.272.18.11943. PMID 9115257.
  5. ↑ Pinto D, Pagnamenta AT, Klei L, Anney R, Merico D, Regan R, et al. (2010). "Functional impact of global rare copy number variation in autism spectrum disorders". Nature. 466 (7304): 368–72. doi:10.1038/nature09146. PMC 3021798. PMID 20531469.

Further reading


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