MAPKAPK5: Difference between revisions

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{{Infobox_gene}}
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'''MAP kinase-activated protein kinase 5''' is an [[enzyme]] that in humans is encoded by the ''MAPKAPK5'' [[gene]].<ref name="pmid9628874">{{cite journal |vauthors=New L, Jiang Y, Zhao M, Liu K, Zhu W, Flood LJ, Kato Y, Parry GC, Han J | title = PRAK, a novel protein kinase regulated by the p38 MAP kinase | journal = EMBO J | volume = 17 | issue = 12 | pages = 3372–84 |date=Jul 1998 | pmid = 9628874 | pmc = 1170675 | doi = 10.1093/emboj/17.12.3372 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: MAPKAPK5 mitogen-activated protein kinase-activated protein kinase 5| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8550| accessdate = }}</ref>
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{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Mitogen-activated protein kinase-activated protein kinase 5
| HGNCid = 6889
| Symbol = MAPKAPK5
| AltSymbols =; PRAK
| OMIM = 606723
| ECnumber = 
| Homologene = 69077
| MGIid = 1333110
| GeneAtlas_image1 = PBB_GE_MAPKAPK5_212871_at_tn.png
| GeneAtlas_image2 = PBB_GE_MAPKAPK5_gnf1h00042_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004708 |text = MAP kinase kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006950 |text = response to stress}} {{GNF_GO|id=GO:0007165 |text = signal transduction}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 8550
    | Hs_Ensembl = ENSG00000089022
    | Hs_RefseqProtein = NP_003659
    | Hs_RefseqmRNA = NM_003668
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 12
    | Hs_GenLoc_start = 110787435
    | Hs_GenLoc_end = 110815543
    | Hs_Uniprot = Q8IW41
    | Mm_EntrezGene = 17165
    | Mm_Ensembl = ENSMUSG00000029454
    | Mm_RefseqmRNA = XM_990515
    | Mm_RefseqProtein = XP_995609
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 5
    | Mm_GenLoc_start = 121785668
    | Mm_GenLoc_end = 121806509
    | Mm_Uniprot = Q3UV25
  }}
}}
'''Mitogen-activated protein kinase-activated protein kinase 5''', also known as '''MAPKAPK5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MAPKAPK5 mitogen-activated protein kinase-activated protein kinase 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8550| accessdate = }}</ref>
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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = The protein encoded by this gene is a member of the serine/threonine kinase family. In response to cellular stress and proinflammatory cytokines, this kinase is activated through its phosphorylation by MAP kinases including MAPK1/ERK, MAPK14/p38-alpha, and MAPK11/p38-beta. In vitro, this kinase phosphorylates heat shock protein HSP27 at its physiologically relevant sites. Two alternately spliced transcript variants of this gene encoding distinct isoforms have been reported.<ref name="entrez">{{cite web | title = Entrez Gene: MAPKAPK5 mitogen-activated protein kinase-activated protein kinase 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8550| accessdate = }}</ref>
| summary_text = The protein encoded by this gene is a member of the serine/threonine kinase family. In response to cellular stress and proinflammatory cytokines, this kinase is activated through its phosphorylation by MAP kinases including MAPK1/ERK, MAPK14/p38-alpha, and MAPK11/p38-beta. In vitro, this kinase phosphorylates heat shock protein HSP27 at its physiologically relevant sites. Two alternately spliced transcript variants of this gene encoding distinct isoforms have been reported.<ref name="entrez">{{cite web | title = Entrez Gene: MAPKAPK5 mitogen-activated protein kinase-activated protein kinase 5| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8550| accessdate = }}</ref>
 
A link between Alzheimer's disease and reduced levels of MAPKAPK5 has been proposed. But clinical trials are needed to confirm if this is the case.
}}
}}
==References==
==References==
{{reflist|2}}
{{reflist|30em}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal | author=de Carvalho MG, McCormack AL, Olson E, ''et al.'' |title=Identification of phosphorylation sites of human 85-kDa cytosolic phospholipase A2 expressed in insect cells and present in human monocytes. |journal=J. Biol. Chem. |volume=271 |issue= 12 |pages= 6987-97 |year= 1996 |pmid= 8636128 |doi=  }}
*{{cite journal   |vauthors=de Carvalho MG, McCormack AL, Olson E, etal |title=Identification of phosphorylation sites of human 85-kDa cytosolic phospholipase A2 expressed in insect cells and present in human monocytes. |journal=J. Biol. Chem. |volume=271 |issue= 12 |pages= 6987–97 |year= 1996 |pmid= 8636128 |doi=10.1074/jbc.271.12.6987 }}
*{{cite journal | author=Börsch-Haubold AG, Bartoli F, Asselin J, ''et al.'' |title=Identification of the phosphorylation sites of cytosolic phospholipase A2 in agonist-stimulated human platelets and HeLa cells. |journal=J. Biol. Chem. |volume=273 |issue= 8 |pages= 4449-58 |year= 1998 |pmid= 9468497 |doi=  }}
*{{cite journal   |vauthors=Börsch-Haubold AG, Bartoli F, Asselin J, etal |title=Identification of the phosphorylation sites of cytosolic phospholipase A2 in agonist-stimulated human platelets and HeLa cells. |journal=J. Biol. Chem. |volume=273 |issue= 8 |pages= 4449–58 |year= 1998 |pmid= 9468497 |doi=10.1074/jbc.273.8.4449 }}
*{{cite journal  | author=Ni H, Wang XS, Diener K, Yao Z |title=MAPKAPK5, a novel mitogen-activated protein kinase (MAPK)-activated protein kinase, is a substrate of the extracellular-regulated kinase (ERK) and p38 kinase. |journal=Biochem. Biophys. Res. Commun. |volume=243 |issue= 2 |pages= 492-6 |year= 1998 |pmid= 9480836 |doi= 10.1006/bbrc.1998.8135 }}
*{{cite journal  |vauthors=Ni H, Wang XS, Diener K, Yao Z |title=MAPKAPK5, a novel mitogen-activated protein kinase (MAPK)-activated protein kinase, is a substrate of the extracellular-regulated kinase (ERK) and p38 kinase. |journal=Biochem. Biophys. Res. Commun. |volume=243 |issue= 2 |pages= 492–6 |year= 1998 |pmid= 9480836 |doi= 10.1006/bbrc.1998.8135 }}
*{{cite journal  | author=New L, Jiang Y, Zhao M, ''et al.'' |title=PRAK, a novel protein kinase regulated by the p38 MAP kinase. |journal=EMBO J. |volume=17 |issue= 12 |pages= 3372-84 |year= 1998 |pmid= 9628874 |doi= 10.1093/emboj/17.12.3372 }}
*{{cite journal  |vauthors=Sudo T, Maruyama M, Osada H |title=p62 functions as a p38 MAP kinase regulator. |journal=Biochem. Biophys. Res. Commun. |volume=269 |issue= 2 |pages= 521–5 |year= 2000 |pmid= 10708586 |doi= 10.1006/bbrc.2000.2333 }}
*{{cite journal  | author=Sudo T, Maruyama M, Osada H |title=p62 functions as a p38 MAP kinase regulator. |journal=Biochem. Biophys. Res. Commun. |volume=269 |issue= 2 |pages= 521-5 |year= 2000 |pmid= 10708586 |doi= 10.1006/bbrc.2000.2333 }}
*{{cite journal   |vauthors=Hefner Y, Borsch-Haubold AG, Murakami M, etal |title=Serine 727 phosphorylation and activation of cytosolic phospholipase A2 by MNK1-related protein kinases. |journal=J. Biol. Chem. |volume=275 |issue= 48 |pages= 37542–51 |year= 2001 |pmid= 10978317 |doi= 10.1074/jbc.M003395200 }}
*{{cite journal | author=Hefner Y, Borsch-Haubold AG, Murakami M, ''et al.'' |title=Serine 727 phosphorylation and activation of cytosolic phospholipase A2 by MNK1-related protein kinases. |journal=J. Biol. Chem. |volume=275 |issue= 48 |pages= 37542-51 |year= 2001 |pmid= 10978317 |doi= 10.1074/jbc.M003395200 }}
*{{cite journal   |vauthors=Zhou J, Lottenbach KR, Barenkamp SJ, etal |title=Recurrent variable region gene usage and somatic mutation in the human antibody response to the capsular polysaccharide of Streptococcus pneumoniae type 23F. |journal=Infect. Immun. |volume=70 |issue= 8 |pages= 4083–91 |year= 2002 |pmid= 12117915 |doi=10.1128/IAI.70.8.4083-4091.2002  | pmc=128163 }}
*{{cite journal | author=Zhou J, Lottenbach KR, Barenkamp SJ, ''et al.'' |title=Recurrent variable region gene usage and somatic mutation in the human antibody response to the capsular polysaccharide of Streptococcus pneumoniae type 23F. |journal=Infect. Immun. |volume=70 |issue= 8 |pages= 4083-91 |year= 2002 |pmid= 12117915 |doi=  }}
*{{cite journal   |vauthors=Perfetti V, Casarini S, Palladini G, etal |title=Analysis of V(lambda)-J(lambda) expression in plasma cells from primary (AL) amyloidosis and normal bone marrow identifies 3r (lambdaIII) as a new amyloid-associated germline gene segment. |journal=Blood |volume=100 |issue= 3 |pages= 948–53 |year= 2002 |pmid= 12130507 |doi= 10.1182/blood-2002-01-0114 }}
*{{cite journal | author=Perfetti V, Casarini S, Palladini G, ''et al.'' |title=Analysis of V(lambda)-J(lambda) expression in plasma cells from primary (AL) amyloidosis and normal bone marrow identifies 3r (lambdaIII) as a new amyloid-associated germline gene segment. |journal=Blood |volume=100 |issue= 3 |pages= 948-53 |year= 2002 |pmid= 12130507 |doi= 10.1182/blood-2002-01-0114 }}
*{{cite journal  |vauthors=Knebel A, Haydon CE, Morrice N, Cohen P |title=Stress-induced regulation of eukaryotic elongation factor 2 kinase by SB 203580-sensitive and -insensitive pathways. |journal=Biochem. J. |volume=367 |issue= Pt 2 |pages= 525–32 |year= 2002 |pmid= 12171600 |doi= 10.1042/BJ20020916 | pmc=1222910 }}
*{{cite journal  | author=Knebel A, Haydon CE, Morrice N, Cohen P |title=Stress-induced regulation of eukaryotic elongation factor 2 kinase by SB 203580-sensitive and -insensitive pathways. |journal=Biochem. J. |volume=367 |issue= Pt 2 |pages= 525-32 |year= 2002 |pmid= 12171600 |doi= 10.1042/BJ20020916 }}
*{{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=New L, Jiang Y, Han J |title=Regulation of PRAK subcellular location by p38 MAP kinases. |journal=Mol. Biol. Cell |volume=14 |issue= 6 |pages= 2603–16 |year= 2004 |pmid= 12808055 |doi= 10.1091/mbc.E02-08-0538 | pmc=194907 }}
*{{cite journal  | author=New L, Jiang Y, Han J |title=Regulation of PRAK subcellular location by p38 MAP kinases. |journal=Mol. Biol. Cell |volume=14 |issue= 6 |pages= 2603-16 |year= 2004 |pmid= 12808055 |doi= 10.1091/mbc.E02-08-0538 }}
*{{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=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=Sun P, Yoshizuka N, New L, etal |title=PRAK is essential for ras-induced senescence and tumor suppression. |journal=Cell |volume=128 |issue= 2 |pages= 295–308 |year= 2007 |pmid= 17254968 |doi= 10.1016/j.cell.2006.11.050 }}
*{{cite journal | author=Sun P, Yoshizuka N, New L, ''et al.'' |title=PRAK is essential for ras-induced senescence and tumor suppression. |journal=Cell |volume=128 |issue= 2 |pages= 295-308 |year= 2007 |pmid= 17254968 |doi= 10.1016/j.cell.2006.11.050 }}
}}
}}
{{refend}}
{{refend}}


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[[Category:EC 2.7.11]]
 
 
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Revision as of 23:33, 7 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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Location (UCSC)n/an/a
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MAP kinase-activated protein kinase 5 is an enzyme that in humans is encoded by the MAPKAPK5 gene.[1][2] The protein encoded by this gene is a member of the serine/threonine kinase family. In response to cellular stress and proinflammatory cytokines, this kinase is activated through its phosphorylation by MAP kinases including MAPK1/ERK, MAPK14/p38-alpha, and MAPK11/p38-beta. In vitro, this kinase phosphorylates heat shock protein HSP27 at its physiologically relevant sites. Two alternately spliced transcript variants of this gene encoding distinct isoforms have been reported.[2]

A link between Alzheimer's disease and reduced levels of MAPKAPK5 has been proposed. But clinical trials are needed to confirm if this is the case.

References

  1. ↑ New L, Jiang Y, Zhao M, Liu K, Zhu W, Flood LJ, Kato Y, Parry GC, Han J (Jul 1998). "PRAK, a novel protein kinase regulated by the p38 MAP kinase". EMBO J. 17 (12): 3372–84. doi:10.1093/emboj/17.12.3372. PMC 1170675. PMID 9628874.
  2. ↑ 2.0 2.1 "Entrez Gene: MAPKAPK5 mitogen-activated protein kinase-activated protein kinase 5".

Further reading


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