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Available structures
PDB Ortholog search: PDBe RCSB
Aliases DCLK1, CL1, CLICK1, DCAMKL1, DCDC3A, DCLK, doublecortin like kinase 1
External IDs MGI: 1330861 HomoloGene: 130530 GeneCards: DCLK1
Genetically Related Diseases
RNA expression pattern
PBB GE DCAMKL1 215303 at fs.png

PBB GE DCAMKL1 205399 at fs.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC) Chr 13: 35.77 – 36.13 Mb Chr 3: 55.24 – 55.54 Mb
PubMed search [2] [3]
View/Edit Human View/Edit Mouse

Serine/threonine-protein kinase DCLK1 is an enzyme that in humans is encoded by the DCLK1 gene.[4][5][6]


  1. ^ "Diseases that are genetically associated with DCLK1 view/edit references on wikidata". 
  2. ^ "Human PubMed Reference:". 
  3. ^ "Mouse PubMed Reference:". 
  4. ^ Omori Y, Suzuki M, Ozaki K, Harada Y, Nakamura Y, Takahashi E, Fujiwara T (Oct 1998). "Expression and chromosomal localization of KIAA0369, a putative kinase structurally related to Doublecortin". J Hum Genet. 43 (3): 169–77. doi:10.1007/s100380050063. PMID 9747029. 
  5. ^ Sossey-Alaoui K, Srivastava AK (May 1999). "DCAMKL1, a brain-specific transmembrane protein on 13q12.3 that is similar to doublecortin (DCX)". Genomics. 56 (1): 121–6. doi:10.1006/geno.1998.5718. PMID 10036192. 
  6. ^ "Entrez Gene: DCAMKL1 doublecortin and CaM kinase-like 1". 

Further reading[edit]

  • Nagase T, Ishikawa K, Nakajima D, et al. (1997). "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro.". DNA Res. 4 (2): 141–50. doi:10.1093/dnares/4.2.141. PMID 9205841. 
  • Matsumoto N, Pilz DT, Ledbetter DH (1999). "Genomic structure, chromosomal mapping, and expression pattern of human DCAMKL1 (KIAA0369), a homologue of DCX (XLIS).". Genomics. 56 (2): 179–83. doi:10.1006/geno.1998.5673. PMID 10051403. 
  • Lin PT, Gleeson JG, Corbo JC, et al. (2001). "DCAMKL1 encodes a protein kinase with homology to doublecortin that regulates microtubule polymerization.". J. Neurosci. 20 (24): 9152–61. PMID 11124993. 
  • Burgess HA, Reiner O (2002). "Alternative splice variants of doublecortin-like kinase are differentially expressed and have different kinase activities.". J. Biol. Chem. 277 (20): 17696–705. doi:10.1074/jbc.M111981200. PMID 11884394. 
  • Kim MH, Derewenda U, Devedjiev Y, et al. (2003). "Purification and crystallization of the N-terminal domain from the human doublecortin-like kinase.". Acta Crystallogr. D. 59 (Pt 3): 502–5. doi:10.1107/S0907444903000027. PMID 12595708. 
  • Kim MH, Cierpicki T, Derewenda U, et al. (2003). "The DCX-domain tandems of doublecortin and doublecortin-like kinase.". Nat. Struct. Biol. 10 (5): 324–33. doi:10.1038/nsb918. PMID 12692530. 
  • Seet LF, Liu N, Hanson BJ, Hong W (2004). "Endofin recruits TOM1 to endosomes.". J. Biol. Chem. 279 (6): 4670–9. doi:10.1074/jbc.M311228200. PMID 14613930. 
  • 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.