MARK1

Serine/threonine-protein kinase MARK1 is an enzyme that in humans is encoded by the MARK1 gene.

MARK1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2HAK, 3OSE
Identifiers
Aliases	MARK1, MARK, Par-1c, Par1c, microtubule affinity regulating kinase 1
External IDs	OMIM: 606511; MGI: 2664902; HomoloGene: 49552; GeneCards: MARK1; OMA:MARK1 - orthologs
Gene location (Human) Chr. Chromosome 1 (human) Band 1q41 Start 220,528,136 bp End 220,664,461 bp
Gene location (Mouse) Chr. Chromosome 1 (mouse) Band 1|1 H5 Start 184,628,986 bp End 184,731,767 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ganglionic eminence ventricular zone corpus epididymis pons cerebellar vermis Brodmann area 23 superior frontal gyrus spinal ganglia endothelial cell primary visual cortex Top expressed in trigeminal ganglion motor neuron barrel cortex substantia nigra fossa external carotid artery condyle internal carotid artery tunica media of zone of aorta ascending aorta More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity nucleotide binding protein kinase activity phosphatidylserine binding metal ion binding kinase activity phosphatidic acid binding protein serine/threonine kinase activity tau-protein kinase activity phosphatidylinositol-4,5-bisphosphate binding ATP binding magnesium ion binding lipid binding protein binding tau protein binding Cellular component cytoplasm membrane microtubule cytoskeleton plasma membrane cytoskeleton dendrite cell projection Biological process intracellular signal transduction phosphorylation neuron migration Wnt signaling pathway protein phosphorylation cytoskeleton organization establishment of cell polarity microtubule cytoskeleton organization regulation of neuron projection development peptidyl-serine phosphorylation regulation of dendrite development establishment of mitochondrion localization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 4139 226778 Ensembl ENSG00000116141 ENSMUSG00000026620 UniProt Q9P0L2 Q8VHJ5 RefSeq (mRNA) NM_001286124 NM_001286126 NM_001286128 NM_001286129 NM_018650 NM_145515 NM_001378876 RefSeq (protein) NP_001273053 NP_001273055 NP_001273057 NP_001273058 NP_061120 NP_663490 NP_001365805 Location (UCSC) Chr 1: 220.53 – 220.66 Mb Chr 1: 184.63 – 184.73 Mb PubMed search
Wikidata
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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. doi:10.1074/jbc.270.13.7679. 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. doi:10.1046/j.1471-4159.1994.63041416.x. PMID 7931292. S2CID 85176778.
• 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. doi:10.1074/jbc.271.18.10834. 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. doi:10.1016/S0021-9258(19)67481-8. PMID 8999860.
• 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. doi:10.1016/S0014-5793(98)01090-4. 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. doi:10.1046/j.1471-4159.1998.71062465.x. 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. doi:10.1046/j.1471-4159.2000.0741587.x. 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. doi:10.1093/dnares/7.2.143. 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. doi:10.1016/S0014-5793(02)03487-7. 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. doi:10.1016/S0306-4522(02)00510-9. PMID 12435421. S2CID 26118803.
• 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. 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. PMC 204455. 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. PMC 381014. 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. PMC 528928. 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.