MARK1

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MAP/microtubule affinity-regulating kinase 1
File:PBB Protein MARK1 image.jpg
PDB rendering based on 2hak.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols MARK1 ; KIAA1477; MARK; MGC126512; MGC126513
External IDs Template:OMIM5 Template:MGI HomoloGene49552
RNA expression pattern
File:PBB GE MARK1 221047 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

MAP/microtubule affinity-regulating kinase 1, also known as MARK1, is a human gene.[1]


References

  1. "Entrez Gene: MARK1 MAP/microtubule affinity-regulating kinase 1".

Further reading

  • Drewes G, Trinczek B, Illenberger S; et al. (1995). "Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262". J. Biol. Chem. 270 (13): 7679–88. PMID 7706316.
  • Yang SD, Yu JS, Shiah SG, Huang JJ (1994). "Protein kinase FA/glycogen synthase kinase-3 alpha after heparin potentiation phosphorylates tau on sites abnormally phosphorylated in Alzheimer's disease brain". J. Neurochem. 63 (4): 1416–25. PMID 7931292.
  • Illenberger S, Drewes G, Trinczek B; et al. (1996). "Phosphorylation of microtubule-associated proteins MAP2 and MAP4 by the protein kinase p110mark. Phosphorylation sites and regulation of microtubule dynamics". J. Biol. Chem. 271 (18): 10834–43. PMID 8631898.
  • Paudel HK (1997). "The regulatory Ser262 of microtubule-associated protein tau is phosphorylated by phosphorylase kinase". J. Biol. Chem. 272 (3): 1777–85. PMID 8999860.
  • Drewes G, Ebneth A, Preuss U; et al. (1997). "MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption". Cell. 89 (2): 297–308. PMID 9108484.
  • Sengupta A, Kabat J, Novak M; et al. (1998). "Phosphorylation of tau at both Thr 231 and Ser 262 is required for maximal inhibition of its binding to microtubules". Arch. Biochem. Biophys. 357 (2): 299–309. doi:10.1006/abbi.1998.0813. PMID 9735171.
  • Wang JZ, Wu Q, Smith A; et al. (1998). "Tau is phosphorylated by GSK-3 at several sites found in Alzheimer disease and its biological activity markedly inhibited only after it is prephosphorylated by A-kinase". FEBS Lett. 436 (1): 28–34. PMID 9771888.
  • Hanger DP, Betts JC, Loviny TL; et al. (1998). "New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry". J. Neurochem. 71 (6): 2465–76. PMID 9832145.
  • Schneider A, Biernat J, von Bergen M; et al. (1999). "Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments". Biochemistry. 38 (12): 3549–58. doi:10.1021/bi981874p. PMID 10090741.
  • Reynolds CH, Betts JC, Blackstock WP; et al. (2000). "Phosphorylation sites on tau identified by nanoelectrospray mass spectrometry: differences in vitro between the mitogen-activated protein kinases ERK2, c-Jun N-terminal kinase and P38, and glycogen synthase kinase-3beta". J. Neurochem. 74 (4): 1587–95. PMID 10737616.
  • Nagase T, Kikuno R, Ishikawa K; et al. (2000). "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 7 (2): 143–50. PMID 10819331.
  • Liu F, Iqbal K, Grundke-Iqbal I, Gong CX (2002). "Involvement of aberrant glycosylation in phosphorylation of tau by cdk5 and GSK-3beta". FEBS Lett. 530 (1–3): 209–14. PMID 12387894.
  • Liu F, Zaidi T, Iqbal K; et al. (2003). "Aberrant glycosylation modulates phosphorylation of tau by protein kinase A and dephosphorylation of tau by protein phosphatase 2A and 5". Neuroscience. 115 (3): 829–37. PMID 12435421.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Timm T, Li XY, Biernat J; et al. (2003). "MARKK, a Ste20-like kinase, activates the polarity-inducing kinase MARK/PAR-1". EMBO J. 22 (19): 5090–101. doi:10.1093/emboj/cdg447. PMID 14517247.
  • Trinczek B, Brajenovic M, Ebneth A, Drewes G (2004). "MARK4 is a novel microtubule-associated proteins/microtubule affinity-regulating kinase that binds to the cellular microtubule network and to centrosomes". J. Biol. Chem. 279 (7): 5915–23. doi:10.1074/jbc.M304528200. PMID 14594945.
  • Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Lizcano JM, Göransson O, Toth R; et al. (2005). "LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1". EMBO J. 23 (4): 833–43. doi:10.1038/sj.emboj.7600110. PMID 14976552.
  • Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
  • Benzinger A, Muster N, Koch HB; et al. (2005). "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer". Mol. Cell Proteomics. 4 (6): 785–95. doi:10.1074/mcp.M500021-MCP200. PMID 15778465.

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