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{{Infobox_gene}}
{{Infobox_gene}}
'''Disks large-associated protein 1''' ('''DAP-1'''), also known as '''guanylate kinase-associated protein''' ('''GKAP'''), is a [[protein]] that in humans is encoded by the ''DLGAP1'' [[gene]]. DAP-1 is known to be highly enriched in synaptosomal preparations of the brain, and present in the [[post synaptic density]].<ref name="entrez">{{cite web | title = Entrez Gene: DLGAP1 discs, large (Drosophila) homolog-associated protein 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9229| accessdate = }}</ref>
'''Disks large-associated protein 1''' ('''DAP-1'''), also known as '''guanylate kinase-associated protein''' ('''GKAP'''), is a [[protein]] that in humans is encoded by the ''DLGAP1'' [[gene]]. DAP-1 is known to be highly enriched in synaptosomal preparations of the brain, and present in the [[post-synaptic density]].<ref name="entrez">{{cite web | title = Entrez Gene: DLGAP1 discs, large (Drosophila) homolog-associated protein 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9229| accessdate = }}</ref>


== Function ==
== Function ==


This gene encodes the protein called guanylate kinase-associated protein (GKAP).  GKAP binds to the [[SHANK]] and [[PSD-95]] proteins, facilitating the assembly of the post synaptic density of neurons.<ref name="isbn0-387-32560-3">{{cite book | veditors = El-Husseini A, Dityatev A | title = Molecular mechanisms of synaptogenesis | publisher = Springer | location = Berlin | year = 2006 | chapter =  Mechanisms that regulate neuronal protein clustering at the synapse| vauthors =  Hines RM, El-Husseini A | isbn = 0-387-32560-3 | pages = 72–75 }}</ref> Dlgap1 has five 14-amino-acid repeats and three Pro-rich portions.
This gene encodes the protein called guanylate kinase-associated protein (GKAP).  GKAP binds to the [[SHANK]] and [[PSD-95]] proteins, facilitating the assembly of the post-synaptic density of neurons.<ref name="isbn0-387-32560-3">{{cite book | veditors = El-Husseini A, Dityatev A | title = Molecular mechanisms of synaptogenesis | publisher = Springer | location = Berlin | year = 2006 | chapter =  Mechanisms that regulate neuronal protein clustering at the synapse| vauthors =  Hines RM, El-Husseini A | isbn = 0-387-32560-3 | pages = 72–75 }}</ref> Dlgap1 has five 14-amino-acid repeats and three Pro-rich portions.


== Interactions ==
== Interactions ==


DLGAP1 has been shown to [[Protein-protein interaction|interact]] with:
DLGAP1 has been shown to [[Protein-protein interaction|interact]] with:
* [[DLG1]],<ref name = pmid9115257/><ref name = pmid9286858/><ref name = pmid11060025/><ref name = pmid9024696/>  
* [[DLG1]]<ref name = pmid9115257/><ref name = pmid9286858/><ref name = pmid11060025/><ref name = pmid9024696/>  
* [[DLG4]],<ref name = pmid9115257>{{cite journal | date = May 1997 | 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 | pmid = 9115257 | doi = 10.1074/jbc.272.18.11943}}</ref><ref name = pmid9286858>{{cite journal | date = June 1997 | 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 | pmid = 9286858 | doi = 10.1046/j.1365-2443.1997.1310329.x}}</ref><ref name = pmid11060025>{{cite journal | date = November 2000 | vauthors = Wu H, Reissner C, Kuhlendahl S, Coblentz B, Reuver S, Kindler S, Gundelfinger ED, Garner CC | title = Intramolecular interactions regulate SAP97 binding to GKAP | journal = EMBO J. | volume = 19 | issue = 21 | pages = 5740–51 | pmid = 11060025 | pmc = 305801 | doi = 10.1093/emboj/19.21.5740}}</ref><ref name = pmid9024696>{{cite journal | date = February 1997 | vauthors = Kim E, Naisbitt S, Hsueh YP, Rao A, Rothschild A, Craig AM, Sheng M | title = GKAP, a novel synaptic protein that interacts with the guanylate kinase-like domain of the PSD-95/SAP90 family of channel clustering molecules | journal = J. Cell Biol. | volume = 136 | issue = 3 | pages = 669–78 | pmid = 9024696 | pmc = 2134290 | doi = 10.1083/jcb.136.3.669}}</ref><ref name = pmid10844022>{{cite journal | date = June 2000 | vauthors = Naisbitt S, Valtschanoff J, Allison DW, Sala C, Kim E, Craig AM, Weinberg RJ, Sheng M | title = Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein | journal = J. Neurosci. | volume = 20 | issue = 12 | pages = 4524–34 | pmid = 10844022 | doi = }}</ref><ref name = pmid10527873>{{cite journal | date = October 1999 | vauthors = Boeckers TM, Winter C, Smalla KH, Kreutz MR, Bockmann J, Seidenbecher C, Garner CC, Gundelfinger ED | title = Proline-rich synapse-associated proteins ProSAP1 and ProSAP2 interact with synaptic proteins of the SAPAP/GKAP family | journal = Biochem. Biophys. Res. Commun. | volume = 264 | issue = 1 | pages = 247–52 | pmid = 10527873 | doi = 10.1006/bbrc.1999.1489}}</ref>  
* [[DLG4]]<ref name = pmid9115257>{{cite journal | date = May 1997 | 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 | pmid = 9115257 | doi = 10.1074/jbc.272.18.11943}}</ref><ref name = pmid9286858>{{cite journal | date = June 1997 | 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 | pmid = 9286858 | doi = 10.1046/j.1365-2443.1997.1310329.x}}</ref><ref name = pmid11060025>{{cite journal | date = November 2000 | vauthors = Wu H, Reissner C, Kuhlendahl S, Coblentz B, Reuver S, Kindler S, Gundelfinger ED, Garner CC | title = Intramolecular interactions regulate SAP97 binding to GKAP | journal = EMBO J. | volume = 19 | issue = 21 | pages = 5740–51 | pmid = 11060025 | pmc = 305801 | doi = 10.1093/emboj/19.21.5740}}</ref><ref name = pmid9024696>{{cite journal | date = February 1997 | vauthors = Kim E, Naisbitt S, Hsueh YP, Rao A, Rothschild A, Craig AM, Sheng M | title = GKAP, a novel synaptic protein that interacts with the guanylate kinase-like domain of the PSD-95/SAP90 family of channel clustering molecules | journal = J. Cell Biol. | volume = 136 | issue = 3 | pages = 669–78 | pmid = 9024696 | pmc = 2134290 | doi = 10.1083/jcb.136.3.669}}</ref><ref name = pmid10844022>{{cite journal | date = June 2000 | vauthors = Naisbitt S, Valtschanoff J, Allison DW, Sala C, Kim E, Craig AM, Weinberg RJ, Sheng M | title = Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein | journal = J. Neurosci. | volume = 20 | issue = 12 | pages = 4524–34 | pmid = 10844022 | doi = }}</ref><ref name = pmid10527873>{{cite journal | date = October 1999 | vauthors = Boeckers TM, Winter C, Smalla KH, Kreutz MR, Bockmann J, Seidenbecher C, Garner CC, Gundelfinger ED | title = Proline-rich synapse-associated proteins ProSAP1 and ProSAP2 interact with synaptic proteins of the SAPAP/GKAP family | journal = Biochem. Biophys. Res. Commun. | volume = 264 | issue = 1 | pages = 247–52 | pmid = 10527873 | doi = 10.1006/bbrc.1999.1489}}</ref>  
* [[DYNLL1]],<ref name = pmid10844022/>
* [[DYNLL1]]<ref name = pmid10844022/>
* [[DYNLL2]],<ref name = pmid10844022/> and
* [[DYNLL2]]<ref name = pmid10844022/>
* [[SHANK2]]<ref name = pmid10844022/><ref name = pmid10527873/> and
* [[SHANK2]]<ref name = pmid10844022/><ref name = pmid10527873/>


The interaction with PSD95 and S-SCAM is mediated by the GUK domain<ref name="pmid9694864">{{cite journal| vauthors=Hirao K, Hata Y, Ide N, Takeuchi M, Irie M, Yao I| title=A novel multiple PDZ domain-containing molecule interacting with N-methyl-D-aspartate receptors and neuronal cell adhesion proteins. | journal=J Biol Chem | year= 1998 | volume= 273 | issue= 33 | pages= 21105–10 | pmid=9694864 | doi= 10.1074/jbc.273.33.21105| pmc= | url= |display-authors=etal}}</ref> and it has been hypothesized that this might mean it can also interact with other GUK containing proteins.
The interaction with PSD95 and S-SCAM is mediated by the GUK domain<ref name="pmid9694864">{{cite journal| vauthors=Hirao K, Hata Y, Ide N, Takeuchi M, Irie M, Yao I| title=A novel multiple PDZ domain-containing molecule interacting with N-methyl-D-aspartate receptors and neuronal cell adhesion proteins. | journal=J Biol Chem | year= 1998 | volume= 273 | issue= 33 | pages= 21105–10 | pmid=9694864 | doi= 10.1074/jbc.273.33.21105| pmc= | url= |display-authors=etal}}</ref> and it has been hypothesized that this might mean it can also interact with other GUK containing proteins.

Latest revision as of 09:03, 9 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
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Disks large-associated protein 1 (DAP-1), also known as guanylate kinase-associated protein (GKAP), is a protein that in humans is encoded by the DLGAP1 gene. DAP-1 is known to be highly enriched in synaptosomal preparations of the brain, and present in the post-synaptic density.[1]

Function

This gene encodes the protein called guanylate kinase-associated protein (GKAP). GKAP binds to the SHANK and PSD-95 proteins, facilitating the assembly of the post-synaptic density of neurons.[2] Dlgap1 has five 14-amino-acid repeats and three Pro-rich portions.

Interactions

DLGAP1 has been shown to interact with:

The interaction with PSD95 and S-SCAM is mediated by the GUK domain[9] and it has been hypothesized that this might mean it can also interact with other GUK containing proteins.

References

  1. ↑ "Entrez Gene: DLGAP1 discs, large (Drosophila) homolog-associated protein 1".
  2. ↑ Hines RM, El-Husseini A (2006). "Mechanisms that regulate neuronal protein clustering at the synapse". In El-Husseini A, Dityatev A. Molecular mechanisms of synaptogenesis. Berlin: Springer. pp. 72–75. ISBN 0-387-32560-3.
  3. ↑ 3.0 3.1 Takeuchi M, Hata Y, Hirao K, Toyoda A, Irie M, Takai Y (May 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.
  4. ↑ 4.0 4.1 Satoh K, Yanai H, Senda T, Kohu K, Nakamura T, Okumura N, Matsumine A, Kobayashi S, Toyoshima K, Akiyama T (June 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.
  5. ↑ 5.0 5.1 Wu H, Reissner C, Kuhlendahl S, Coblentz B, Reuver S, Kindler S, Gundelfinger ED, Garner CC (November 2000). "Intramolecular interactions regulate SAP97 binding to GKAP". EMBO J. 19 (21): 5740–51. doi:10.1093/emboj/19.21.5740. PMC 305801. PMID 11060025.
  6. ↑ 6.0 6.1 Kim E, Naisbitt S, Hsueh YP, Rao A, Rothschild A, Craig AM, Sheng M (February 1997). "GKAP, a novel synaptic protein that interacts with the guanylate kinase-like domain of the PSD-95/SAP90 family of channel clustering molecules". J. Cell Biol. 136 (3): 669–78. doi:10.1083/jcb.136.3.669. PMC 2134290. PMID 9024696.
  7. ↑ 7.0 7.1 7.2 7.3 Naisbitt S, Valtschanoff J, Allison DW, Sala C, Kim E, Craig AM, Weinberg RJ, Sheng M (June 2000). "Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein". J. Neurosci. 20 (12): 4524–34. PMID 10844022.
  8. ↑ 8.0 8.1 Boeckers TM, Winter C, Smalla KH, Kreutz MR, Bockmann J, Seidenbecher C, Garner CC, Gundelfinger ED (October 1999). "Proline-rich synapse-associated proteins ProSAP1 and ProSAP2 interact with synaptic proteins of the SAPAP/GKAP family". Biochem. Biophys. Res. Commun. 264 (1): 247–52. doi:10.1006/bbrc.1999.1489. PMID 10527873.
  9. ↑ Hirao K, Hata Y, Ide N, Takeuchi M, Irie M, Yao I, et al. (1998). "A novel multiple PDZ domain-containing molecule interacting with N-methyl-D-aspartate receptors and neuronal cell adhesion proteins". J Biol Chem. 273 (33): 21105–10. doi:10.1074/jbc.273.33.21105. PMID 9694864.

Further reading


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