MARK1: Difference between revisions

VALUE_ERROR (nil)
Identifiers
Aliases
External IDs	GeneCards: [1]
Orthologs
	n/a
	n/a
	n/a
	n/a
	n/a
	n/a
	n/a
	n/a
	n/a
	n/a
	Wikidata
View/Edit Human

VisualWikitext

Revision as of 06:09, 4 September 2017

Serine/threonine-protein kinase MARK1 is an enzyme that in humans is encoded by the MARK1 gene.^[1]^[2]

References

↑ Drewes G, Ebneth A, Preuss U, Mandelkow EM, Mandelkow E (May 1997). "MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption". Cell. 89 (2): 297–308. doi:10.1016/S0092-8674(00)80208-1. PMID 9108484.
↑ "Entrez Gene: MARK1 MAP/microtubule affinity-regulating kinase 1".

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.
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:10.1074/jbc.272.3.1777. 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.
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. 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.

This article on a gene on human chromosome 1 is a stub. You can help Wikipedia by expanding it.

[pmid9108484-1] Drewes G, Ebneth A, Preuss U, Mandelkow EM, Mandelkow E (May 1997). "MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption". Cell. 89 (2): 297–308. doi:10.1016/S0092-8674(00)80208-1. PMID 9108484.

[entrez-2] "Entrez Gene: MARK1 MAP/microtubule affinity-regulating kinase 1".

[1]

[2]

@@ Line 1: / Line 1: @@
-<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{Underlinked|date=March 2017}}
-{{PBB_Controls
+{{Infobox_gene}}
-| update_page = yes
+'''Serine/threonine-protein kinase MARK1''' is an [[enzyme]] that in humans is encoded by the ''MARK1'' [[gene]].<ref name="pmid9108484">{{cite journal |vauthors=Drewes G, Ebneth A, Preuss U, Mandelkow EM, Mandelkow E | title = MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption | journal = Cell | volume = 89 | issue = 2 | pages = 297–308 |date=May 1997 | pmid = 9108484 | pmc =  | doi =10.1016/S0092-8674(00)80208-1  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: MARK1 MAP/microtubule affinity-regulating kinase 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4139| accessdate = }}</ref>
-| require_manual_inspection = no
-| update_protein_box = yes
-| update_summary = yes
-| update_citations = yes
-}}
-<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
-{{GNF_Protein_box
- | image = PBB_Protein_MARK1_image.jpg
- | image_source = [[Protein_Data_Bank|PDB]] rendering based on 2hak.
- | PDB = {{PDB2|2hak}}
- | Name = MAP/microtubule affinity-regulating kinase 1
- | HGNCid = 6896
- | Symbol = MARK1
- | AltSymbols =; KIAA1477; MARK; MGC126512; MGC126513
- | OMIM = 606511
- | ECnumber =
- | Homologene = 49552
- | MGIid = 2664902
- | GeneAtlas_image1 = PBB_GE_MARK1_221047_s_at_tn.png
- | Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
- | Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0015630 |text = microtubule cytoskeleton}}
- | Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007010 |text = cytoskeleton organization and biogenesis}} {{GNF_GO|id=GO:0007243 |text = protein kinase cascade}}
- | Orthologs = {{GNF_Ortholog_box
-    | Hs_EntrezGene = 4139
-    | Hs_Ensembl = ENSG00000116141
-    | Hs_RefseqProtein = NP_061120
-    | Hs_RefseqmRNA = NM_018650
-    | Hs_GenLoc_db =
-    | Hs_GenLoc_chr = 1
-    | Hs_GenLoc_start = 218768191
-    | Hs_GenLoc_end = 218904426
-    | Hs_Uniprot = Q9P0L2
-    | Mm_EntrezGene = 226778
-    | Mm_Ensembl = ENSMUSG00000026620
-    | Mm_RefseqmRNA = NM_145515
-    | Mm_RefseqProtein = NP_663490
-    | Mm_GenLoc_db =
-    | Mm_GenLoc_chr = 1
-    | Mm_GenLoc_start = 186599312
-    | Mm_GenLoc_end = 186645788
-    | Mm_Uniprot = Q14DQ3
-  }}
-}}
-'''MAP/microtubule affinity-regulating kinase 1''', also known as '''MARK1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MARK1 MAP/microtubule affinity-regulating kinase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4139| accessdate = }}</ref>
 <!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
@@ Line 55: / Line 10: @@
 ==References==
-{{reflist|2}}
+{{reflist}}
 ==Further reading==
 {{refbegin | 2}}
 {{PBB_Further_reading
 | citations =
-*{{cite journal  | author=Drewes G, Trinczek B, Illenberger S, ''et al.'' |title=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. |journal=J. Biol. Chem. |volume=270 |issue= 13 |pages= 7679-88 |year= 1995 |pmid= 7706316 |doi=  }}
+*{{cite journal   |vauthors=Drewes G, Trinczek B, Illenberger S, etal |title=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. |journal=J. Biol. Chem. |volume=270 |issue= 13 |pages= 7679–88 |year= 1995 |pmid= 7706316 |doi=  10.1074/jbc.270.13.7679}}
-*{{cite journal  | author=Yang SD, Yu JS, Shiah SG, Huang JJ |title=Protein kinase FA/glycogen synthase kinase-3 alpha after heparin potentiation phosphorylates tau on sites abnormally phosphorylated in Alzheimer's disease brain. |journal=J. Neurochem. |volume=63 |issue= 4 |pages= 1416-25 |year= 1994 |pmid= 7931292 |doi=  }}
+*{{cite journal  |vauthors=Yang SD, Yu JS, Shiah SG, Huang JJ |title=Protein kinase FA/glycogen synthase kinase-3 alpha after heparin potentiation phosphorylates tau on sites abnormally phosphorylated in Alzheimer's disease brain. |journal=J. Neurochem. |volume=63 |issue= 4 |pages= 1416–25 |year= 1994 |pmid= 7931292 |doi=10.1046/j.1471-4159.1994.63041416.x  }}
-*{{cite journal  | author=Illenberger S, Drewes G, Trinczek B, ''et al.'' |title=Phosphorylation of microtubule-associated proteins MAP2 and MAP4 by the protein kinase p110mark. Phosphorylation sites and regulation of microtubule dynamics. |journal=J. Biol. Chem. |volume=271 |issue= 18 |pages= 10834-43 |year= 1996 |pmid= 8631898 |doi=  }}
+*{{cite journal   |vauthors=Illenberger S, Drewes G, Trinczek B, etal |title=Phosphorylation of microtubule-associated proteins MAP2 and MAP4 by the protein kinase p110mark. Phosphorylation sites and regulation of microtubule dynamics. |journal=J. Biol. Chem. |volume=271 |issue= 18 |pages= 10834–43 |year= 1996 |pmid= 8631898 |doi=  10.1074/jbc.271.18.10834}}
-*{{cite journal  | author=Paudel HK |title=The regulatory Ser262 of microtubule-associated protein tau is phosphorylated by phosphorylase kinase. |journal=J. Biol. Chem. |volume=272 |issue= 3 |pages= 1777-85 |year= 1997 |pmid= 8999860 |doi=  }}
+*{{cite journal  | author=Paudel HK |title=The regulatory Ser262 of microtubule-associated protein tau is phosphorylated by phosphorylase kinase. |journal=J. Biol. Chem. |volume=272 |issue= 3 |pages= 1777–85 |year= 1997 |pmid= 8999860 |doi=10.1074/jbc.272.3.1777  }}
-*{{cite journal  | author=Drewes G, Ebneth A, Preuss U, ''et al.'' |title=MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption. |journal=Cell |volume=89 |issue= 2 |pages= 297-308 |year= 1997 |pmid= 9108484 |doi=  }}
+*{{cite journal   |vauthors=Sengupta A, Kabat J, Novak M, etal |title=Phosphorylation of tau at both Thr 231 and Ser 262 is required for maximal inhibition of its binding to microtubules. |journal=Arch. Biochem. Biophys. |volume=357 |issue= 2 |pages= 299–309 |year= 1998 |pmid= 9735171 |doi= 10.1006/abbi.1998.0813 }}
-*{{cite journal  | author=Sengupta A, Kabat J, Novak M, ''et al.'' |title=Phosphorylation of tau at both Thr 231 and Ser 262 is required for maximal inhibition of its binding to microtubules. |journal=Arch. Biochem. Biophys. |volume=357 |issue= 2 |pages= 299-309 |year= 1998 |pmid= 9735171 |doi= 10.1006/abbi.1998.0813 }}
+*{{cite journal   |vauthors=Wang JZ, Wu Q, Smith A, etal |title=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. |journal=FEBS Lett. |volume=436 |issue= 1 |pages= 28–34 |year= 1998 |pmid= 9771888 |doi=10.1016/S0014-5793(98)01090-4  }}
-*{{cite journal  | author=Wang JZ, Wu Q, Smith A, ''et al.'' |title=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. |journal=FEBS Lett. |volume=436 |issue= 1 |pages= 28-34 |year= 1998 |pmid= 9771888 |doi=  }}
+*{{cite journal   |vauthors=Hanger DP, Betts JC, Loviny TL, etal |title=New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry. |journal=J. Neurochem. |volume=71 |issue= 6 |pages= 2465–76 |year= 1998 |pmid= 9832145 |doi=10.1046/j.1471-4159.1998.71062465.x  }}
-*{{cite journal  | author=Hanger DP, Betts JC, Loviny TL, ''et al.'' |title=New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry. |journal=J. Neurochem. |volume=71 |issue= 6 |pages= 2465-76 |year= 1998 |pmid= 9832145 |doi=  }}
+*{{cite journal   |vauthors=Schneider A, Biernat J, von Bergen M, etal |title=Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments. |journal=Biochemistry |volume=38 |issue= 12 |pages= 3549–58 |year= 1999 |pmid= 10090741 |doi= 10.1021/bi981874p }}
-*{{cite journal  | author=Schneider A, Biernat J, von Bergen M, ''et al.'' |title=Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments. |journal=Biochemistry |volume=38 |issue= 12 |pages= 3549-58 |year= 1999 |pmid= 10090741 |doi= 10.1021/bi981874p }}
+*{{cite journal   |vauthors=Reynolds CH, Betts JC, Blackstock WP, etal |title=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. |journal=J. Neurochem. |volume=74 |issue= 4 |pages= 1587–95 |year= 2000 |pmid= 10737616 |doi=10.1046/j.1471-4159.2000.0741587.x  }}
-*{{cite journal  | author=Reynolds CH, Betts JC, Blackstock WP, ''et al.'' |title=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. |journal=J. Neurochem. |volume=74 |issue= 4 |pages= 1587-95 |year= 2000 |pmid= 10737616 |doi=  }}
+*{{cite journal   |vauthors=Nagase T, Kikuno R, Ishikawa K, etal |title=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. |journal=DNA Res. |volume=7 |issue= 2 |pages= 143–50 |year= 2000 |pmid= 10819331 |doi=10.1093/dnares/7.2.143  }}
-*{{cite journal  | author=Nagase T, Kikuno R, Ishikawa K, ''et al.'' |title=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. |journal=DNA Res. |volume=7 |issue= 2 |pages= 143-50 |year= 2000 |pmid= 10819331 |doi=  }}
+*{{cite journal  |vauthors=Liu F, Iqbal K, Grundke-Iqbal I, Gong CX |title=Involvement of aberrant glycosylation in phosphorylation of tau by cdk5 and GSK-3beta. |journal=FEBS Lett. |volume=530 |issue= 1–3 |pages= 209–14 |year= 2002 |pmid= 12387894 |doi=10.1016/S0014-5793(02)03487-7  }}
-*{{cite journal  | author=Liu F, Iqbal K, Grundke-Iqbal I, Gong CX |title=Involvement of aberrant glycosylation in phosphorylation of tau by cdk5 and GSK-3beta. |journal=FEBS Lett. |volume=530 |issue= 1-3 |pages= 209-14 |year= 2002 |pmid= 12387894 |doi=  }}
+*{{cite journal   |vauthors=Liu F, Zaidi T, Iqbal K, etal |title=Aberrant glycosylation modulates phosphorylation of tau by protein kinase A and dephosphorylation of tau by protein phosphatase 2A and 5 |journal=Neuroscience |volume=115 |issue= 3 |pages= 829–37 |year= 2003 |pmid= 12435421 |doi=10.1016/S0306-4522(02)00510-9  }}
-*{{cite journal  | author=Liu F, Zaidi T, Iqbal K, ''et al.'' |title=Aberrant glycosylation modulates phosphorylation of tau by protein kinase A and dephosphorylation of tau by protein phosphatase 2A and 5. |journal=Neuroscience |volume=115 |issue= 3 |pages= 829-37 |year= 2003 |pmid= 12435421 |doi=  }}
+*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 }}
-*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
+*{{cite journal   |vauthors=Timm T, Li XY, Biernat J, etal |title=MARKK, a Ste20-like kinase, activates the polarity-inducing kinase MARK/PAR-1 |journal=EMBO J. |volume=22 |issue= 19 |pages= 5090–101 |year= 2003 |pmid= 14517247 |doi= 10.1093/emboj/cdg447  | pmc=204455 }}
-*{{cite journal  | author=Timm T, Li XY, Biernat J, ''et al.'' |title=MARKK, a Ste20-like kinase, activates the polarity-inducing kinase MARK/PAR-1. |journal=EMBO J. |volume=22 |issue= 19 |pages= 5090-101 |year= 2003 |pmid= 14517247 |doi= 10.1093/emboj/cdg447 }}
+*{{cite journal  |vauthors=Trinczek B, Brajenovic M, Ebneth A, Drewes G |title=MARK4 is a novel microtubule-associated proteins/microtubule affinity-regulating kinase that binds to the cellular microtubule network and to centrosomes |journal=J. Biol. Chem. |volume=279 |issue= 7 |pages= 5915–23 |year= 2004 |pmid= 14594945 |doi= 10.1074/jbc.M304528200 }}
-*{{cite journal  | author=Trinczek B, Brajenovic M, Ebneth A, Drewes G |title=MARK4 is a novel microtubule-associated proteins/microtubule affinity-regulating kinase that binds to the cellular microtubule network and to centrosomes. |journal=J. Biol. Chem. |volume=279 |issue= 7 |pages= 5915-23 |year= 2004 |pmid= 14594945 |doi= 10.1074/jbc.M304528200 }}
+*{{cite journal   |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
-*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
+*{{cite journal   |vauthors=Lizcano JM, Göransson O, Toth R, etal |title=LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1 |journal=EMBO J. |volume=23 |issue= 4 |pages= 833–43 |year= 2005 |pmid= 14976552 |doi= 10.1038/sj.emboj.7600110  | pmc=381014 }}
-*{{cite journal  | author=Lizcano JM, Göransson O, Toth R, ''et al.'' |title=LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1. |journal=EMBO J. |volume=23 |issue= 4 |pages= 833-43 |year= 2005 |pmid= 14976552 |doi= 10.1038/sj.emboj.7600110 }}
+*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 }}
-*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
+*{{cite journal   |vauthors=Benzinger A, Muster N, Koch HB, etal |title=Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer |journal=Mol. Cell. Proteomics |volume=4 |issue= 6 |pages= 785–95 |year= 2005 |pmid= 15778465 |doi= 10.1074/mcp.M500021-MCP200 }}
-*{{cite journal  | author=Benzinger A, Muster N, Koch HB, ''et al.'' |title=Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer. |journal=Mol. Cell Proteomics |volume=4 |issue= 6 |pages= 785-95 |year= 2005 |pmid= 15778465 |doi= 10.1074/mcp.M500021-MCP200 }}
 }}
 {{refend}}
+{{PDB Gallery|geneid=4139}}
+{{Serine/threonine-specific protein kinases}}
+{{Enzymes}}
+{{Portal bar|Molecular and Cellular Biology|border=no}}
+<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{PBB_Controls
+| update_page = yes
+| require_manual_inspection = no
+| update_protein_box = yes
+| update_summary = yes
+| update_citations = yes
+}}
+[[Category:EC 2.7.11]]
-{{protein-stub}}
+{{gene-1-stub}}
-{{WikiDoc Sources}}

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

MARK1: Difference between revisions

Revision as of 06:09, 4 September 2017

References

Further reading

Navigation menu