DLG2

Protein-coding gene in the species Homo sapiens
DLG2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2BYG, 2HE2

Identifiers
AliasesDLG2, PPP1R58, PSD-93, PSD93, chapsyn-110, discs large homolog 2, discs large MAGUK scaffold protein 2
External IDsOMIM: 603583; MGI: 1344351; HomoloGene: 1046; GeneCards: DLG2; OMA:DLG2 - orthologs
Gene location (Human)
Chromosome 11 (human)
Chr.Chromosome 11 (human)[1]
Chromosome 11 (human)
Genomic location for DLG2
Genomic location for DLG2
Band11q14.1Start83,455,012 bp[1]
End85,627,922 bp[1]
Gene location (Mouse)
Chromosome 7 (mouse)
Chr.Chromosome 7 (mouse)[2]
Chromosome 7 (mouse)
Genomic location for DLG2
Genomic location for DLG2
Band7 E1|7 51.07 cMStart90,476,672 bp[2]
End92,449,247 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • endothelial cell

  • corpus callosum

  • inferior ganglion of vagus nerve

  • prefrontal cortex

  • right frontal lobe

  • entorhinal cortex

  • middle temporal gyrus

  • nucleus accumbens

  • hippocampus proper

  • Brodmann area 23
Top expressed in
  • superior frontal gyrus

  • lateral septal nucleus

  • lobe of cerebellum

  • piriform cortex

  • dentate gyrus of hippocampal formation granule cell

  • olfactory tubercle

  • cerebellar vermis

  • anterior amygdaloid area

  • primary motor cortex

  • neural layer of retina
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • guanylate kinase activity
  • kinase binding
  • protein binding
  • ionotropic glutamate receptor binding
  • structural constituent of postsynaptic density
Cellular component
  • postsynaptic membrane
  • cell projection
  • membrane
  • postsynaptic density
  • voltage-gated potassium channel complex
  • plasma membrane
  • synapse
  • axon
  • cell junction
  • basolateral plasma membrane
  • ionotropic glutamate receptor complex
  • juxtaparanode region of axon
  • cytosol
  • neuromuscular junction
  • neuron projection
  • postsynaptic density membrane
  • glutamatergic synapse
  • axon cytoplasm
Biological process
  • chemical synaptic transmission
  • receptor localization to synapse
  • negative regulation of phosphatase activity
  • receptor clustering
  • nervous system development
  • establishment or maintenance of epithelial cell apical/basal polarity
  • sensory perception of pain
  • GDP metabolic process
  • GMP metabolic process
  • MAPK cascade
  • cellular response to potassium ion
  • cell-cell adhesion
  • maintenance of postsynaptic density structure
  • anterograde axonal protein transport
  • retrograde axonal protein transport
  • neurotransmitter receptor localization to postsynaptic specialization membrane
  • regulation of NMDA receptor activity
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

1740

23859

Ensembl

ENSG00000150672

ENSMUSG00000052572

UniProt

Q15700

Q91XM9

RefSeq (mRNA)
NM_001142699
NM_001142700
NM_001142702
NM_001206769
NM_001300983

NM_001364
NM_001351274
NM_001351275
NM_001351276
NM_001377966
NM_001377967
NM_001377968
NM_001377970
NM_001377971
NM_001377972
NM_001377973
NM_001377974
NM_001377975
NM_001377976
NM_001377977
NM_001377978
NM_001377979
NM_001377980
NM_001377981
NM_001377982
NM_001377983
NM_175892

NM_001243046
NM_001243047
NM_011807

RefSeq (protein)
NP_001136171
NP_001136172
NP_001136174
NP_001193698
NP_001287912

NP_001355
NP_001338203
NP_001338204
NP_001338205
NP_001364895
NP_001364896
NP_001364897
NP_001364899
NP_001364900
NP_001364901
NP_001364902
NP_001364903
NP_001364904
NP_001364905
NP_001364906
NP_001364907
NP_001364908
NP_001364909
NP_001364910
NP_001364911
NP_001364912

NP_001229975
NP_001229976
NP_035937

Location (UCSC)Chr 11: 83.46 – 85.63 MbChr 7: 90.48 – 92.45 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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.[5][6]

Function

Chapsyn-110/PSD-93 a member of the membrane-associated guanylate kinase (MAGUK) family. The protein forms a heterodimer with a related family member that may interact at postsynaptic sites to form a multimeric scaffold for the clustering of receptors, ion channels, and associated signaling proteins. Alternatively spliced transcript variants encoding distinct isoforms have been described but their full-length nature has yet to be completely determined.[7]

Interactions

DLG2 has been shown to interact with GRIN2B,[8][9] KCNJ12.[10]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000150672 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000052572 – 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. ^ Kim E, Cho KO, Rothschild A, Sheng M (December 1996). "Heteromultimerization and NMDA receptor-clustering activity of Chapsyn-110, a member of the PSD-95 family of proteins". Neuron. 17 (1): 103–13. doi:10.1016/S0896-6273(00)80284-6. PMID 8755482. S2CID 14852857.
  6. ^ Stathakis DG, Lee D, Bryant PJ (January 1999). "Fine-scale physical map of the 11q21 region surrounding the human DLG2 locus, the gene encoding Chapsyn-110". Genomics. 54 (1): 186–8. doi:10.1006/geno.1998.5527. PMID 9806853.
  7. ^ "Entrez Gene: DLG2 discs, large homolog 2, chapsyn-110 (Drosophila)".
  8. ^ Inanobe A, Fujita A, Ito M, Tomoike H, Inageda K, Kurachi Y (June 2002). "Inward rectifier K+ channel Kir2.3 is localized at the postsynaptic membrane of excitatory synapses". Am. J. Physiol., Cell Physiol. 282 (6): C1396-403. doi:10.1152/ajpcell.00615.2001. PMID 11997254.
  9. ^ Irie M, Hata Y, Takeuchi M, Ichtchenko K, Toyoda A, Hirao K, Takai Y, Rosahl TW, Südhof TC (September 1997). "Binding of neuroligins to PSD-95". Science. 277 (5331): 1511–5. doi:10.1126/science.277.5331.1511. PMID 9278515.
  10. ^ Leonoudakis D, Conti LR, Anderson S, Radeke CM, McGuire LM, Adams ME, Froehner SC, Yates JR, Vandenberg CA (May 2004). "Protein trafficking and anchoring complexes revealed by proteomic analysis of inward rectifier potassium channel (Kir2.x)-associated proteins". J. Biol. Chem. 279 (21): 22331–46. doi:10.1074/jbc.M400285200. PMID 15024025.

Further reading

  • Kim E, Niethammer M, Rothschild A, Jan YN, Sheng M (1995). "Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases". Nature. 378 (6552): 85–8. Bibcode:1995Natur.378...85K. doi:10.1038/378085a0. PMID 7477295. S2CID 4362906.
  • Brenman JE, Chao DS, Gee SH, McGee AW, Craven SE, Santillano DR, Wu Z, Huang F, Xia H, Peters MF, Froehner SC, Bredt DS (1996). "Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and alpha1-syntrophin mediated by PDZ domains". Cell. 84 (5): 757–67. doi:10.1016/S0092-8674(00)81053-3. PMID 8625413. S2CID 15834673.
  • Hsueh YP, Kim E, Sheng M (1997). "Disulfide-linked head-to-head multimerization in the mechanism of ion channel clustering by PSD-95". Neuron. 18 (5): 803–14. doi:10.1016/S0896-6273(00)80319-0. PMID 9182804. S2CID 18331544.
  • Niethammer M, Valtschanoff JG, Kapoor TM, Allison DW, Weinberg RJ, Craig AM, Sheng M (1998). "CRIPT, a novel postsynaptic protein that binds to the third PDZ domain of PSD-95/SAP90". Neuron. 20 (4): 693–707. doi:10.1016/S0896-6273(00)81009-0. PMID 9581762. S2CID 16068361.
  • Leonard AS, Davare MA, Horne MC, Garner CC, Hell JW (1998). "SAP97 is associated with the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor GluR1 subunit". J. Biol. Chem. 273 (31): 19518–24. doi:10.1074/jbc.273.31.19518. PMID 9677374.
  • Butz S, Okamoto M, Südhof TC (1998). "A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain". Cell. 94 (6): 773–82. doi:10.1016/S0092-8674(00)81736-5. PMID 9753324. S2CID 12465062.
  • Brenman JE, Topinka JR, Cooper EC, McGee AW, Rosen J, Milroy T, Ralston HJ, Bredt DS (1998). "Localization of postsynaptic density-93 to dendritic microtubules and interaction with microtubule-associated protein 1A". J. Neurosci. 18 (21): 8805–13. doi:10.1523/JNEUROSCI.18-21-08805.1998. PMC 6793550. PMID 9786987.
  • Craven SE, El-Husseini AE, Bredt DS (1999). "Synaptic targeting of the postsynaptic density protein PSD-95 mediated by lipid and protein motifs". Neuron. 22 (3): 497–509. doi:10.1016/S0896-6273(00)80705-9. PMID 10197530.
  • Sans N, Petralia RS, Wang YX, Blahos J, Hell JW, Wenthold RJ (2000). "A developmental change in NMDA receptor-associated proteins at hippocampal synapses". J. Neurosci. 20 (3): 1260–71. doi:10.1523/JNEUROSCI.20-03-01260.2000. PMC 6774158. PMID 10648730.
  • Garcia RA, Vasudevan K, Buonanno A (2000). "The neuregulin receptor ErbB-4 interacts with PDZ-containing proteins at neuronal synapses". Proc. Natl. Acad. Sci. U.S.A. 97 (7): 3596–601. doi:10.1073/pnas.070042497. PMC 16285. PMID 10725395.
  • Husi H, Ward MA, Choudhary JS, Blackstock WP, Grant SG (2000). "Proteomic analysis of NMDA receptor-adhesion protein signaling complexes". Nat. Neurosci. 3 (7): 661–9. doi:10.1038/76615. hdl:1842/742. PMID 10862698. S2CID 14392630.
  • Firestein BL, Craven SE, Bredt DS (2001). "Postsynaptic targeting of MAGUKs mediated by distinct N-terminal domains". NeuroReport. 11 (16): 3479–84. doi:10.1097/00001756-200011090-00016. PMID 11095503. S2CID 19718975.
  • Haraguchi K, Satoh K, Yanai H, Hamada F, Kawabuchi M, Akiyama T (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. S2CID 37107139.
  • DeMarco SJ, Strehler EE (2001). "Plasma membrane Ca2+-atpase isoforms 2b and 4b interact promiscuously and selectively with members of the membrane-associated guanylate kinase family of PDZ (PSD95/Dlg/ZO-1) domain-containing proteins". J. Biol. Chem. 276 (24): 21594–600. doi:10.1074/jbc.M101448200. PMID 11274188.
  • Russwurm M, Wittau N, Koesling D (2002). "Guanylyl cyclase/PSD-95 interaction: targeting of the nitric oxide-sensitive alpha2beta1 guanylyl cyclase to synaptic membranes". J. Biol. Chem. 276 (48): 44647–52. doi:10.1074/jbc.M105587200. PMID 11572861.
  • Weitzdoerfer R, Dierssen M, Fountoulakis M, Lubec G (2002). "Fetal life in Down Syndrome starts with normal neuronal density but impaired dendritic spines and synaptosomal structure". Protein Expression in Down Syndrome Brain. pp. 59–70. doi:10.1007/978-3-7091-6262-0_5. ISBN 978-3-211-83704-7. PMID 11771761. {{cite book}}: |journal= ignored (help)
  • v
  • t
  • e
  • 1iu0: The first PDZ domain of PSD-95
    1iu0: The first PDZ domain of PSD-95
  • 1iu2: The first PDZ domain of PSD-95
    1iu2: The first PDZ domain of PSD-95
  • 2byg: 2ND PDZ DOMAIN OF DISCS LARGE HOMOLOGUE 2
    2byg: 2ND PDZ DOMAIN OF DISCS LARGE HOMOLOGUE 2
  • 2he2: Crystal structure of the 3rd PDZ domain of human discs large homologue 2, DLG2
    2he2: Crystal structure of the 3rd PDZ domain of human discs large homologue 2, DLG2