DCLK1

Protein-coding gene in the species Homo sapiens
DCLK1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1MFW, 1MG4, 1UF0

Identifiers
AliasesDCLK1, CL1, CLICK1, DCAMKL1, DCDC3A, DCLK, doublecortin like kinase 1
External IDsOMIM: 604742; MGI: 1330861; HomoloGene: 130530; GeneCards: DCLK1; OMA:DCLK1 - orthologs
Gene location (Human)
Chromosome 13 (human)
Chr.Chromosome 13 (human)[1]
Chromosome 13 (human)
Genomic location for DCLK1
Genomic location for DCLK1
Band13q13.3Start35,768,652 bp[1]
End36,131,382 bp[1]
Gene location (Mouse)
Chromosome 3 (mouse)
Chr.Chromosome 3 (mouse)[2]
Chromosome 3 (mouse)
Genomic location for DCLK1
Genomic location for DCLK1
Band3|3 CStart55,149,785 bp[2]
End55,446,489 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • endothelial cell

  • frontal pole

  • Brodmann area 10

  • Brodmann area 23

  • pars reticulata

  • Pars compacta

  • occipital lobe

  • middle temporal gyrus

  • superior vestibular nucleus

  • primary visual cortex
Top expressed in
  • stria vascularis

  • piriform cortex

  • habenula

  • visual cortex

  • superior frontal gyrus

  • primary motor cortex

  • prefrontal cortex

  • olfactory tubercle

  • temporal lobe

  • subiculum
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • transferase activity
  • protein kinase activity
  • nucleotide binding
  • kinase activity
  • ATP binding
  • protein serine/threonine kinase activity
Cellular component
  • integral component of plasma membrane
  • intracellular anatomical structure
  • postsynaptic density
Biological process
  • cell differentiation
  • axonogenesis
  • dendrite morphogenesis
  • phosphorylation
  • response to virus
  • neuron migration
  • nervous system development
  • multicellular organism development
  • endosomal transport
  • protein phosphorylation
  • central nervous system development
  • brain development
  • axon extension
  • forebrain development
  • central nervous system projection neuron axonogenesis
  • negative regulation of protein localization to nucleus
  • peptidyl-serine phosphorylation
  • peptidyl-threonine phosphorylation
  • intracellular signal transduction
  • neuron projection morphogenesis
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

9201

13175

Ensembl

ENSG00000133083

ENSMUSG00000027797

UniProt

O15075

Q9JLM8

RefSeq (mRNA)
NM_001195415
NM_001195416
NM_001195430
NM_004734
NM_001330071

NM_001330072

NM_001111051
NM_001111052
NM_001111053
NM_001195538
NM_001195539

NM_001195540
NM_019978
NM_001357466
NM_001357468
NM_001357469
NM_001357475
NM_001357476

RefSeq (protein)
NP_001182344
NP_001182345
NP_001182359
NP_001317000
NP_001317001

NP_004725

NP_001104521
NP_001104522
NP_001104523
NP_001182467
NP_001182468

NP_001182469
NP_064362
NP_001344395
NP_001344397
NP_001344398
NP_001344404
NP_001344405

Location (UCSC)Chr 13: 35.77 – 36.13 MbChr 3: 55.15 – 55.45 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Doublecortin-like kinase protein 1 (DCLK1)[5][6][7][8] is an enzyme that in humans is encoded by the DCLK1 gene.[5][6][8] Its C-terminal domain in rats is expressed independently from an alternative transcript, cpg16, and can function alone as a serine/threonine protein kinase that is cyclic AMP dependent.[9][10]

DCLK1 expression is a marker for tuft cells, a type of chemosensory cell of the intestinal epithelium.[7][11]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000133083 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027797 – 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. ^ a b 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.
  6. ^ a b 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.
  7. ^ a b Ding L, Weygant N, Ding C, Lai Y, Li H (2023). "DCLK1 and tuft cells: Immune-related functions and implications for cancer immunotherapy". Critical Reviews in Oncology and Hematology. 191. doi:10.1016/j.critrevonc.2023.104118. PMID 37660932. Art. No. 104118.
  8. ^ a b "Entrez Gene: DCAMKL1 doublecortin and CaM kinase-like 1". Gene. National Library of Medicine. 7 April 2024. Retrieved 30 May 2024.
  9. ^ Silverman MA, Benard O, Jaaro H, Rattner A, Citri Y, Seger R (1999). "CPG16, a novel protein serine/threonine kinase downstream of cAMP-dependent protein kinase". Journal of Biological Chemistry. 274 (5): 2631–2636. doi:10.1074/jbc.274.5.2631. PMID 9915791.
  10. ^ 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. doi:10.1523/JNEUROSCI.20-24-09152.2000. PMC 6773030. PMID 11124993.
  11. ^ Gerbe F, Legraverend C, Jay P (2012). "The intestinal epithelium tuft cells: specification and function". Cellular and Molecular Life Sciences. 69 (17): 2907–2917. doi:10.1007/s00018-012-0984-7. PMC 3417095. PMID 22527717.

Further reading

  • 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.
  • 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. Bibcode:2003AcCrD..59..502K. 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. S2CID 10173864.
  • 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.

External links

  • Overview of all the structural information available in the PDB for UniProt: O15075 (Serine/threonine-protein kinase DCLK1) at the PDBe-KB.
  • v
  • t
  • e
  • 1mfw: STRUCTURE OF N-TERMINAL DOUBLECORTIN DOMAIN FROM DCLK: SELENOMETHIONINE LABELED PROTEIN
    1mfw: STRUCTURE OF N-TERMINAL DOUBLECORTIN DOMAIN FROM DCLK: SELENOMETHIONINE LABELED PROTEIN
  • 1mg4: STRUCTURE OF N-TERMINAL DOUBLECORTIN DOMAIN FROM DCLK: WILD TYPE PROTEIN
    1mg4: STRUCTURE OF N-TERMINAL DOUBLECORTIN DOMAIN FROM DCLK: WILD TYPE PROTEIN
  • 1uf0: Solution structure of the N-terminal DCX domain of human doublecortin-like kinase
    1uf0: Solution structure of the N-terminal DCX domain of human doublecortin-like kinase
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Non-specific serine/threonine protein kinases (EC 2.7.11.1)
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Dephospho-(reductase kinase) kinase (EC 2.7.11.3)
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)
(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)
(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)
Myosin-heavy-chain kinase (EC 2.7.11.7)
Fas-activated serine/threonine kinase (EC 2.7.11.8)
Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)
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IκB kinase (EC 2.7.11.10)
cAMP-dependent protein kinase (EC 2.7.11.11)
cGMP-dependent protein kinase (EC 2.7.11.12)
Protein kinase C (EC 2.7.11.13)
Rhodopsin kinase (EC 2.7.11.14)
Beta adrenergic receptor kinase (EC 2.7.11.15)
G-protein coupled receptor kinases (EC 2.7.11.16)
Ca2+/calmodulin-dependent (EC 2.7.11.17)
Myosin light-chain kinase (EC 2.7.11.18)
Phosphorylase kinase (EC 2.7.11.19)
Elongation factor 2 kinase (EC 2.7.11.20)
Polo kinase (EC 2.7.11.21)
Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)
Polo kinase (EC 2.7.11.21)
Cyclin-dependent kinase (EC 2.7.11.22)
(RNA-polymerase)-subunit kinase (EC 2.7.11.23)
Mitogen-activated protein kinase (EC 2.7.11.24)
MAP3K (EC 2.7.11.25)
Tau-protein kinase (EC 2.7.11.26)
(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)
  • -
Tropomyosin kinase (EC 2.7.11.28)
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Low-density-lipoprotein receptor kinase (EC 2.7.11.29)
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Receptor protein serine/threonine kinase (EC 2.7.11.30)
MAP2K
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