DLGAP1

DLGAP1
Identifiers
Aliases	DLGAP1 , DAP-1, DAP-1-ALPHA, DAP-1-BETA, DAP1, DLGAP1A, DLGAP1B, GKAP, SAPAP1, hGKAP, discs large homolog associated protein 1, DLG associated protein 1
External IDs	OMIM: 605445 MGI: 1346065 HomoloGene: 31258 GeneCards: DLGAP1
Gene location (Human)
Chr.	Chromosome 18 (human)
End	4,455,307 bp
Gene location (Mouse)
Chr.	Chromosome 17 (mouse)
End	71,128,408 bp
RNA expression pattern
	Top expressed in
	Brodmann area 23; ; endothelial cell; ; prefrontal cortex; ; pons; ; dorsolateral prefrontal cortex; ; Brodmann area 9; ; parietal lobe; ; superior frontal gyrus; ; ganglionic eminence; ; postcentral gyrus;
	Top expressed in
	piriform cortex; ; subiculum; ; primary motor cortex; ; cingulate gyrus; ; Region I of hippocampus proper; ; cerebellar vermis; ; dentate gyrus; ; prefrontal cortex; ; hippocampus proper; ; superior frontal gyrus;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	protein binding ; protein domain specific binding ; protein-containing complex binding ;
Cellular component	cell junction ; postsynaptic membrane ; postsynaptic density ; membrane ; plasma membrane ; synapse ; cellular component ;
Biological process	signaling ; chemical synaptic transmission ;
	Sources:Amigo / QuickGO
Orthologs
	9229
	224997
	ENSG00000170579
	ENSMUSG00000003279
	O14490
	Q9D415
NM_001003809 ; NM_001242761 ; NM_001242762 ; NM_001242763 ; NM_001242764 ;
	NM_001242765 ; NM_001242766 ; NM_001308390 ; NM_004746
NM_001128180 ; NM_001128181 ; NM_027712 ; NM_177639 ; NM_001347411 ;
	NM_001347412 ; NM_001347413 ; NM_001347414 ; NM_001360665 Contents Function ; Interactions ; References ; Further reading ;
NP_001003809 ; NP_001229690 ; NP_001229691 ; NP_001229692 ; NP_001229693 ;
	NP_001229694 ; NP_001229695 ; NP_001295319 ; NP_004737
NP_001121652 ; NP_001121653 ; NP_001334340 ; NP_001334341 ; NP_001334342 ;
	NP_001334343 ; NP_081988 ; NP_808307 ; NP_001347594
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated September 21, 2023

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.^[5]

Function

This gene encodes the protein called guanylate kinase-associated protein (GKAP). GKAP binds to the SHANK2 and PSD-95 proteins, facilitating the assembly of the post-synaptic density of neurons.^[6] 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^[13] and it has been hypothesized that this might mean it can also interact with other GUK containing proteins.

Related Research Articles

The postsynaptic density (PSD) is a protein dense specialization attached to the postsynaptic membrane. PSDs were originally identified by electron microscopy as an electron-dense region at the membrane of a postsynaptic neuron. The PSD is in close apposition to the presynaptic active zone and ensures that receptors are in close proximity to presynaptic neurotransmitter release sites. PSDs vary in size and composition among brain regions, and have been studied in great detail at glutamatergic synapses. Hundreds of proteins have been identified in the postsynaptic density, including glutamate receptors, scaffold proteins, and many signaling molecules.

Erbb2 interacting protein (ERBB2IP), also known as erbin, is a protein which in humans is encoded by the ERBB2IP gene. Discovered in 1997, erbin is a 200kDa protein containing a PDZ domain.

PSD-95 also known as SAP-90 is a protein that in humans is encoded by the DLG4 gene.

Discs large homolog 1 (DLG1), also known as synapse-associated protein 97 or SAP97, is a scaffold protein that in humans is encoded by the SAP97 gene.

Peripheral plasma membrane protein CASK is a protein that in humans is encoded by the CASK gene. This gene is also known by several other names: CMG 2, calcium/calmodulin-dependent serine protein kinase 3 and membrane-associated guanylate kinase 2. CASK gene mutations are the cause of XL-ID with or without nystagmus and MICPCH, an X-linked neurological disorder.

Protein Interacting with C Kinase - 1 is a protein that in humans is encoded by the PICK1 gene.

Disks large homolog 3 (DLG3) also known as neuroendocrine-DLG or synapse-associated protein 102 (SAP-102) is a protein that in humans is encoded by the DLG3 gene. DLG3 is a member of the membrane-associated guanylate kinase (MAGUK) superfamily of proteins.

Disks large homolog 2 (DLG2) also known as channel-associated protein of synapse-110 (chapsyn-110) or postsynaptic density protein 93 (PSD-93) is a protein that in humans is encoded by the DLG2 gene.

Potassium voltage-gated channel subfamily A member 4 also known as K_v1.4 is a protein that in humans is encoded by the KCNA4 gene. It contributes to the cardiac transient outward potassium current (I_to1), the main contributing current to the repolarizing phase 1 of the cardiac action potential.

Potassium inwardly-rectifying channel, subfamily J, member 4, also known as KCNJ4 or K_ir2.3, is a human gene.

SH3 and multiple ankyrin repeat domains protein 2 is a protein that in humans is encoded by the SHANK2 gene. Two alternative splice variants, encoding distinct isoforms, are reported. Additional splice variants exist but their full-length nature has not been determined.

SH3 and multiple ankyrin repeat domains protein 1 is a protein that in humans is encoded by the SHANK1 gene.

Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2 also known as membrane-associated guanylate kinase inverted 2 (MAGI-2) and atrophin-1-interacting protein 1 (AIP-1) is an enzyme that in humans is encoded by the MAGI2 gene.

Disks large-associated protein 4 (DAP-4) also known as SAP90/PSD-95-associated protein 4 (SAPAP-4) is a protein that in humans is encoded by the DLGAP4 gene.

Lin-7 homolog B is a protein that in humans is encoded by the LIN7B gene.

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

Leucine rich repeat containing 7 also known as LRRC7, Densin-180, or LAP1 is a protein which in humans is encoded by the LRRC7 gene.

Cysteine-rich PDZ-binding protein is a protein that in humans is encoded by the CRIPT gene.

Connector enhancer of kinase suppressor of ras 2, also known as CNK homolog protein 2 (CNK2) or MAGUIN, is an enzyme that in humans is encoded by the CNKSR2 gene.

Mary Bernadette Kennedy is an American biochemist and neuroscientist. She is a member of the American Academy of Arts and Sciences, and is the Allen and Lenabelle Davis Professor of Biology at the California Institute of Technology, where she has been a member of the faculty since 1981. Her research focuses on the molecular mechanisms of synaptic plasticity, the process underlying formation of memory in the central nervous system. Her lab uses biochemical and molecular biological methods to study the protein machinery within a structure called the postsynaptic density. Kennedy has published over 100 papers with over 20,000 total citations.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000170579 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000003279 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Entrez Gene: DLGAP1 discs, large (Drosophila) homolog-associated protein 1".
↑ Hines RM, El-Husseini A (2006). "Mechanisms that regulate neuronal protein clustering at the synapse". In El-Husseini A, Dityatev A (eds.). Molecular mechanisms of synaptogenesis. Berlin: Springer. pp. 72–75. ISBN 978-0-387-32560-6.
1 2 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.
1 2 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.
1 2 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.
1 2 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.
1 2 3 4 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. doi: 10.1523/JNEUROSCI.20-12-04524.2000 . PMC 6772433 . PMID 10844022.
1 2 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.
↑ 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.

Kim E, Naisbitt S, Hsueh YP, et al. (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.
Takeuchi M, Hata Y, Hirao K, et al. (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.
Naisbitt S, Kim E, Weinberg RJ, et al. (1997). "Characterization of guanylate kinase-associated protein, a postsynaptic density protein at excitatory synapses that interacts directly with postsynaptic density-95/synapse-associated protein 90". J. Neurosci. 17 (15): 5687–96. doi: 10.1523/JNEUROSCI.17-15-05687.1997 . PMC 6573205 . PMID 9221768.
Satoh K, Yanai H, Senda T, et al. (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.
Hirao K, Hata Y, Ide N, 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.
Deguchi M, Hata Y, Takeuchi M, et al. (1998). "BEGAIN (brain-enriched guanylate kinase-associated protein), a novel neuronal PSD-95/SAP90-binding protein". J. Biol. Chem. 273 (41): 26269–72. doi: 10.1074/jbc.273.41.26269 . PMID 9756850.
Kawabe H, Hata Y, Takeuchi M, et al. (1999). "nArgBP2, a novel neural member of ponsin/ArgBP2/vinexin family that interacts with synapse-associated protein 90/postsynaptic density-95-associated protein (SAPAP)". J. Biol. Chem. 274 (43): 30914–8. doi: 10.1074/jbc.274.43.30914 . PMID 10521485.
Boeckers TM, Winter C, Smalla KH, et al. (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.
Naisbitt S, Valtschanoff J, Allison DW, et al. (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. doi: 10.1523/JNEUROSCI.20-12-04524.2000 . PMC 6772433 . PMID 10844022.
Wu H, Reissner C, Kuhlendahl S, et al. (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.
Haraguchi K, Satoh K, Yanai H, et al. (2001). "The hDLG-associated protein DAP interacts with dynein light chain and neuronal nitric oxide synthase". Genes Cells. 5 (11): 905–911. doi: 10.1046/j.1365-2443.2000.00374.x . PMID 11122378.
Lo KW, Naisbitt S, Fan JS, et al. (2001). "The 8-kDa dynein light chain binds to its targets via a conserved (K/R)XTQT motif". J. Biol. Chem. 276 (17): 14059–66. doi: 10.1074/jbc.M010320200 . PMID 11148209.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC 139241 . PMID 12477932.
Im YJ, Lee JH, Park SH, et al. (2004). "Crystal structure of the Shank PDZ-ligand complex reveals a class I PDZ interaction and a novel PDZ-PDZ dimerization". J. Biol. Chem. 278 (48): 48099–104. doi: 10.1074/jbc.M306919200 . PMID 12954649.
Ballif BA, Villén J, Beausoleil SA, et al. (2005). "Phosphoproteomic analysis of the developing mouse brain". Mol. Cell. Proteomics. 3 (11): 1093–101. doi: 10.1074/mcp.M400085-MCP200 . PMID 15345747.
Suzuki T, Li W, Zhang JP, et al. (2005). "A novel scaffold protein, TANC, possibly a rat homolog of Drosophila rolling pebbles (rols), forms a multiprotein complex with various postsynaptic density proteins". Eur. J. Neurosci. 21 (2): 339–50. doi:10.1111/j.1460-9568.2005.03856.x. PMID 15673434. S2CID 28773407.
Sabio G; Arthur JS; Kuma Y; et al. (2005). "p38gamma regulates the localisation of SAP97 in the cytoskeleton by modulating its interaction with GKAP". EMBO J. 24 (6): 1134–45. doi:10.1038/sj.emboj.7600578. PMC 556394 . PMID 15729360.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000170579 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000003279 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-5] "Entrez Gene: DLGAP1 discs, large (Drosophila) homolog-associated protein 1".

[isbn0-387-32560-3-6] Hines RM, El-Husseini A (2006). "Mechanisms that regulate neuronal protein clustering at the synapse". In El-Husseini A, Dityatev A (eds.). Molecular mechanisms of synaptogenesis. Berlin: Springer. pp. 72–75. ISBN 978-0-387-32560-6.

[pmid9115257-7] 1 2 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.

[pmid9286858-8] 1 2 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.

[pmid11060025-9] 1 2 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.

[pmid9024696-10] 1 2 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.

[pmid10844022-11] 1 2 3 4 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. doi: 10.1523/JNEUROSCI.20-12-04524.2000 . PMC 6772433 . PMID 10844022.

[pmid10527873-12] 1 2 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.

[pmid9694864-13] 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.

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DLGAP1

Contents

Function

Interactions

Related Research Articles

References

Further reading