DLGAP1

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DLGAP1
Identifiers
AliasesDLGAP1, 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 IDsOMIM: 605445 MGI: 1346065 HomoloGene: 31258 GeneCards: DLGAP1
Gene location (Human)
Chromosome 18 (human)
Chr.Chromosome 18 (human)[1]
Chromosome 18 (human)
Genomic location for DLGAP1
Genomic location for DLGAP1
Band18p11.31Start3,496,032 bp[1]
End4,455,307 bp[1]
RNA expression pattern
PBB GE DLGAP1 210750 s at fs.png

PBB GE DLGAP1 206489 s at fs.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)Chr 18: 3.5 – 4.46 MbChr 17: 69.97 – 70.82 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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[edit]

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.[6] Dlgap1 has five 14-amino-acid repeats and three Pro-rich portions.

Interactions[edit]

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.

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000170579 - Ensembl, May 2017
  2. ^ a b c 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.
  5. ^ "Entrez Gene: DLGAP1 discs, large (Drosophila) homolog-associated protein 1".
  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.
  7. ^ a b 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.
  8. ^ a b 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.
  9. ^ a b 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.
  10. ^ a b 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.
  11. ^ a b c d 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. PMID 10844022.
  12. ^ a b 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.
  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.

Further reading[edit]