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Calcium/calmodulin-dependent serine protein kinase (MAGUK family)

PDB rendering based on 1kgd.
Available structures
PDB Ortholog search: PDBe, RCSB
External IDs GeneCards:
EC number
RNA expression pattern
Species Human Mouse
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

Peripheral plasma membrane protein CASK is a protein that in humans is encoded by the CASK gene.[1][2] This gene is also known by several other names: CMG 2 (CAMGUK protein 2), calcium/calmodulin-dependent serine protein kinase 3 and membrane-associated guanylate kinase 2.


This gene is located on the short arm of the X chromosome (Xp11.4). It is 404,253 bases in length and lies on the Crick (minus) strand. The encoded protein has 926 amino acids with a predicted molecular weight of 105,123 Daltons.


This protein is a multidomain scaffolding protein with a role in synaptic transmembrane protein anchoring and ion channel trafficking. It interacts with the transcription factor TBR1 and binds to several cell-surface proteins including amyloid precursor protein, neurexins and syndecans.

Clinical importance

This gene has been implicated in X-linked mental retardation,[3] including specifically mental retardation and microcephaly with pontine and cerebellar hypoplasia.[4]


CASK has been shown to interact with:


  1. ^ Dimitratos SD, Stathakis DG, Nelson CA, Woods DF, Bryant PJ (Nov 1998). "The location of human CASK at Xp11.4 identifies this gene as a candidate for X-linked optic atrophy". Genomics 51 (2): 308–309.  
  2. ^ "Entrez Gene: CASK Calcium/calmodulin-dependent serine protein kinase (MAGUK family)". 
  3. ^ Tarpey PS, Smith R, Pleasance E, Whibley A, Edkins S, Hardy C et al. (May 2009). "A systematic, large-scale resequencing screen of X-chromosome coding exons in mental retardation". Nat. Genet. 41 (5): 535–43.  
  4. ^ Burglen L, Chantot-Bastaraud S, Garel C, Milh M, Touraine R, Zanni G et al. (2012). mutations: confirmation of a recognizable phenotype and first description of a male mosaic patient"CASK"Spectrum of pontocerebellar hypoplasia in 13 girls and boys with . Orphanet Journal of Rare Diseases 7 (18): 18.  
  5. ^ a b Leonoudakis D, Conti LR, Anderson S, Radeke CM, McGuire LM, Adams ME et al. (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.  
  6. ^ a b c d Leonoudakis D, Conti LR, Radeke CM, McGuire LM, Vandenberg CA (April 2004). "A multiprotein trafficking complex composed of SAP97, CASK, Veli, and Mint1 is associated with inward rectifier Kir2 potassium channels". J. Biol. Chem. 279 (18): 19051–63.  
  7. ^ a b Borg JP, Straight SW, Kaech SM, de Taddéo-Borg M, Kroon DE, Karnak D et al. (November 1998). "Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting". J. Biol. Chem. 273 (48): 31633–6.  
  8. ^ Borg JP, Lõpez-Figueroa MO, de Taddèo-Borg M, Kroon DE, Turner RS, Watson SJ et al. (February 1999). "Molecular analysis of the X11-mLin-2/CASK complex in brain". J. Neurosci. 19 (4): 1307–16.  
  9. ^ Schuh K, Uldrijan S, Gambaryan S, Roethlein N, Neyses L (March 2003). "Interaction of the plasma membrane Ca2+ pump 4b/CI with the Ca2+/calmodulin-dependent membrane-associated kinase CASK". J. Biol. Chem. 278 (11): 9778–83.  
  10. ^ Wang GS, Hong CJ, Yen TY, Huang HY, Ou Y, Huang TN et al. (April 2004). "Transcriptional modification by a CASK-interacting nucleosome assembly protein". Neuron 42 (1): 113–28.  
  11. ^ a b Chetkovich DM, Bunn RC, Kuo SH, Kawasaki Y, Kohwi M, Bredt DS (August 2002). "Postsynaptic targeting of alternative postsynaptic density-95 isoforms by distinct mechanisms". J. Neurosci. 22 (15): 6415–25.  
  12. ^ Nix SL, Chishti AH, Anderson JM, Walther Z (December 2000). "hCASK and hDlg associate in epithelia, and their src homology 3 and guanylate kinase domains participate in both intramolecular and intermolecular interactions". J. Biol. Chem. 275 (52): 41192–200.  
  13. ^ Martinez-Estrada OM, Villa A, Breviario F, Orsenigo F, Dejana E, Bazzoni G (March 2001). "Association of junctional adhesion molecule with calcium/calmodulin-dependent serine protein kinase (CASK/LIN-2) in human epithelial caco-2 cells". J. Biol. Chem. 276 (12): 9291–6.  
  14. ^ Ebnet K, Schulz CU, Meyer Zu Brickwedde MK, Pendl GG, Vestweber D (September 2000). "Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1". J. Biol. Chem. 275 (36): 27979–88.  
  15. ^ Qi J, Su Y, Sun R, Zhang F, Luo X, Yang Z et al. (March 2005). "CASK inhibits ECV304 cell growth and interacts with Id1". Biochem. Biophys. Res. Commun. 328 (2): 517–21.  
  16. ^ Lehtonen S, Lehtonen E, Kudlicka K, Holthöfer H, Farquhar MG (September 2004). "Nephrin forms a complex with adherens junction proteins and CASK in podocytes and in Madin-Darby canine kidney cells expressing nephrin". Am. J. Pathol. 165 (3): 923–36.  
  17. ^ Fallon L, Moreau F, Croft BG, Labib N, Gu WJ, Fon EA (January 2002). "Parkin and CASK/LIN-2 associate via a PDZ-mediated interaction and are co-localized in lipid rafts and postsynaptic densities in brain". J. Biol. Chem. 277 (1): 486–91.  
  18. ^ a b Zhang Y, Luan Z, Liu A, Hu G (May 2001). "The scaffolding protein CASK mediates the interaction between rabphilin3a and beta-neurexins". FEBS Lett. 497 (2-3): 99–102.  
  19. ^ Cohen AR, Woods DF, Marfatia SM, Walther Z, Chishti AH, Anderson JM et al. (July 1998). "Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells". J. Cell Biol. 142 (1): 129–38.  

Further reading

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