MAPK6: Difference between revisions

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{{Infobox_gene}}
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'''Mitogen-activated protein kinase 6''' is an [[enzyme]] that in humans is encoded by the ''MAPK6'' [[gene]].<ref name="pmid8875998">{{cite journal |vauthors=Meloche S, Beatty BG, Pellerin J | title = Primary structure, expression and chromosomal locus of a human homolog of rat ERK3 | journal = Oncogene | volume = 13 | issue = 7 | pages = 1575–9 |date=Dec 1996 | pmid = 8875998 | pmc =  | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: MAPK6 mitogen-activated protein kinase 6| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5597| accessdate = }}</ref>
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{{GNF_Protein_box
| image = PBB_Protein_MAPK6_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2i6l.
| PDB = {{PDB2|2i6l}}
| Name = Mitogen-activated protein kinase 6
| HGNCid = 6879
| Symbol = MAPK6
| AltSymbols =; ERK3; DKFZp686F03189; HsT17250; PRKM6; p97MAPK
| OMIM = 602904
| ECnumber = 
| Homologene = 55683
| MGIid = 1354946
| GeneAtlas_image1 = PBB_GE_MAPK6_207121_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:0004707 |text = MAP 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:0005737 |text = cytoplasm}}
  | Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007165 |text = signal transduction}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5597
    | Hs_Ensembl = ENSG00000069956
    | Hs_RefseqProtein = NP_002739
    | Hs_RefseqmRNA = NM_002748
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 15
    | Hs_GenLoc_start = 50098739
    | Hs_GenLoc_end = 50145751
    | Hs_Uniprot = Q16659
    | Mm_EntrezGene = 50772
    | Mm_Ensembl = ENSMUSG00000042688
    | Mm_RefseqmRNA = NM_015806
    | Mm_RefseqProtein = NP_056621
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 9
    | Mm_GenLoc_start = 75172810
    | Mm_GenLoc_end = 75195923
    | Mm_Uniprot = Q8R3S3
  }}
}}
'''Mitogen-activated protein kinase 6''', also known as '''MAPK6''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MAPK6 mitogen-activated protein kinase 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5597| 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 Ser/Thr protein kinase family, and is most closely related to mitogen-activated protein kinases (MAP kinases). MAP kinases also known as extracellular signal-regulated kinases (ERKs), are activated through protein phosphorylation cascades and act as integration points for multiple biochemical signals. This kinase is localized in the nucleus, and has been reported to be activated in fibroblasts upon treatment with serum or phorbol esters.<ref name="entrez">{{cite web | title = Entrez Gene: MAPK6 mitogen-activated protein kinase 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5597| accessdate = }}</ref>
| summary_text = The protein encoded by this gene is a member of the Ser/Thr [[protein kinase]] family, and is most closely related to mitogen-activated protein kinases ([[MAP kinases]]). MAP kinases also known as extracellular signal-regulated kinases ([[ERKs]]), are activated through protein phosphorylation cascades and act as integration points for multiple biochemical signals. This kinase is localized in the [[Nucleus (cell)|nucleus]], and has been reported to be activated in [[fibroblasts]] upon treatment with serum or [[phorbol]] esters.<ref name="entrez"/>
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* [http://www.mapkinases.eu MAP Kinase Resource ].
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Boulton TG, Nye SH, Robbins DJ, ''et al.'' |title=ERKs: a family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF. |journal=Cell |volume=65 |issue= 4 |pages= 663-75 |year= 1991 |pmid= 2032290 |doi=  }}
*{{cite journal  | author=Boulton TG |title=ERKs: a family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF |journal=Cell |volume=65 |issue= 4 |pages= 663–675 |year= 1991 |pmid= 2032290 |doi=10.1016/0092-8674(91)90098-J  |name-list-format=vanc| author2=Nye SH  | author3=Robbins DJ  | display-authors=3  | last4=Ip  | first4=Nancy Y.  | last5=Radzlejewska  | first5=Elizabeth  | last6=Morgenbesser  | first6=Sharon D.  | last7=Depinho  | first7=Ronald A.  | last8=Panayotatos  | first8=Nikos  | last9=Cobb  | first9=Melanie H. }}
*{{cite journal  | author=Zhu AX, Zhao Y, Moller DE, Flier JS |title=Cloning and characterization of p97MAPK, a novel human homolog of rat ERK-3. |journal=Mol. Cell. Biol. |volume=14 |issue= 12 |pages= 8202-11 |year= 1994 |pmid= 7969157 |doi=  }}
*{{cite journal  |vauthors=Zhu AX, Zhao Y, Moller DE, Flier JS |title=Cloning and characterization of p97MAPK, a novel human homolog of rat ERK-3 |journal=Mol. Cell. Biol. |volume=14 |issue= 12 |pages= 8202–11 |year= 1994 |pmid= 7969157 |doi= | pmc=359359 }}
*{{cite journal  | author=Cheng M, Boulton TG, Cobb MH |title=ERK3 is a constitutively nuclear protein kinase. |journal=J. Biol. Chem. |volume=271 |issue= 15 |pages= 8951-8 |year= 1996 |pmid= 8621539 |doi=  }}
*{{cite journal  |vauthors=Cheng M, Boulton TG, Cobb MH |title=ERK3 is a constitutively nuclear protein kinase |journal=J. Biol. Chem. |volume=271 |issue= 15 |pages= 8951–8958 |year= 1996 |pmid= 8621539 |doi=10.1074/jbc.271.15.8951 }}
*{{cite journal  | author=Sauma S, Friedman E |title=Increased expression of protein kinase C beta activates ERK3. |journal=J. Biol. Chem. |volume=271 |issue= 19 |pages= 11422-6 |year= 1996 |pmid= 8626698 |doi= }}
*{{cite journal  |vauthors=Sauma S, Friedman E |title=Increased expression of protein kinase C beta activates ERK3 |journal=J. Biol. Chem. |volume=271 |issue= 19 |pages= 11422–11426 |year= 1996 |pmid= 8626698 |doi=10.1074/jbc.271.19.11422 }}
*{{cite journal  | author=Meloche S, Beatty BG, Pellerin J |title=Primary structure, expression and chromosomal locus of a human homolog of rat ERK3. |journal=Oncogene |volume=13 |issue= 7 |pages= 1575-9 |year= 1996 |pmid= 8875998 |doi= }}
*{{cite journal  |vauthors=Zimmermann J, Lamerant N, Grossenbacher R, Furst P |title=Proteasome- and p38-dependent regulation of ERK3 expression |journal=J. Biol. Chem. |volume=276 |issue= 14 |pages= 10759–10766 |year= 2001 |pmid= 11148204 |doi= 10.1074/jbc.M008567200 }}
*{{cite journal  | author=Zimmermann J, Lamerant N, Grossenbacher R, Furst P |title=Proteasome- and p38-dependent regulation of ERK3 expression. |journal=J. Biol. Chem. |volume=276 |issue= 14 |pages= 10759-66 |year= 2001 |pmid= 11148204 |doi= 10.1074/jbc.M008567200 }}
*{{cite journal  |vauthors=Robinson MJ, Xu Be BE, Stippec S, Cobb MH |title=Different domains of the mitogen-activated protein kinases ERK3 and ERK2 direct subcellular localization and upstream specificity in vivo |journal=J. Biol. Chem. |volume=277 |issue= 7 |pages= 5094–5100 |year= 2002 |pmid= 11741894 |doi= 10.1074/jbc.M110935200 }}
*{{cite journal  | author=Robinson MJ, Xu Be BE, Stippec S, Cobb MH |title=Different domains of the mitogen-activated protein kinases ERK3 and ERK2 direct subcellular localization and upstream specificity in vivo. |journal=J. Biol. Chem. |volume=277 |issue= 7 |pages= 5094-100 |year= 2002 |pmid= 11741894 |doi= 10.1074/jbc.M110935200 }}
*{{cite journal  | author=Kinet S |title=gp120-mediated induction of the MAPK cascade is dependent on the activation state of CD4(+) lymphocytes |journal=Blood |volume=100 |issue= 7 |pages= 2546–2553 |year= 2002 |pmid= 12239168 |doi= 10.1182/blood-2002-03-0819 |name-list-format=vanc| author2=Bernard F  | author3=Mongellaz C  | display-authors=3  | last4=Perreau  | first4=M  | last5=Goldman  | first5=FD  | last6=Taylor  | first6=N }}
*{{cite journal  | author=Kinet S, Bernard F, Mongellaz C, ''et al.'' |title=gp120-mediated induction of the MAPK cascade is dependent on the activation state of CD4(+) lymphocytes. |journal=Blood |volume=100 |issue= 7 |pages= 2546-53 |year= 2002 |pmid= 12239168 |doi= 10.1182/blood-2002-03-0819 }}
*{{cite journal  | author=Strausberg RL |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= 16899–16903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
*{{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  | author=Coulombe P |title=Rapid turnover of extracellular signal-regulated kinase 3 by the ubiquitin-proteasome pathway defines a novel paradigm of mitogen-activated protein kinase regulation during cellular differentiation |journal=Mol. Cell. Biol. |volume=23 |issue= 13 |pages= 4542–4558 |year= 2003 |pmid= 12808096 |doi=10.1128/MCB.23.13.4542-4558.2003  | pmc=164847  |name-list-format=vanc| author2=Rodier G  | author3=Pelletier S  | display-authors=3  | last4=Pellerin  | first4=J.  | last5=Meloche  | first5=S. }}
*{{cite journal  | author=Coulombe P, Rodier G, Pelletier S, ''et al.'' |title=Rapid turnover of extracellular signal-regulated kinase 3 by the ubiquitin-proteasome pathway defines a novel paradigm of mitogen-activated protein kinase regulation during cellular differentiation. |journal=Mol. Cell. Biol. |volume=23 |issue= 13 |pages= 4542-58 |year= 2003 |pmid= 12808096 |doi=  }}
*{{cite journal  |vauthors=Julien C, Coulombe P, Meloche S |title=Nuclear export of ERK3 by a CRM1-dependent mechanism regulates its inhibitory action on cell cycle progression |journal=J. Biol. Chem. |volume=278 |issue= 43 |pages= 42615–42624 |year= 2004 |pmid= 12915405 |doi= 10.1074/jbc.M302724200 }}
*{{cite journal  | author=Julien C, Coulombe P, Meloche S |title=Nuclear export of ERK3 by a CRM1-dependent mechanism regulates its inhibitory action on cell cycle progression. |journal=J. Biol. Chem. |volume=278 |issue= 43 |pages= 42615-24 |year= 2004 |pmid= 12915405 |doi= 10.1074/jbc.M302724200 }}
*{{cite journal  |vauthors=Rai R, Mahale A, Saranath D |title=Molecular cloning, isolation and characterisation of ERK3 gene from chewing-tobacco induced oral squamous cell carcinoma |journal=Oral Oncol. |volume=40 |issue= 7 |pages= 705–712 |year= 2004 |pmid= 15172640 |doi= 10.1016/j.oraloncology.2004.01.010 }}
*{{cite journal  | author=Rai R, Mahale A, Saranath D |title=Molecular cloning, isolation and characterisation of ERK3 gene from chewing-tobacco induced oral squamous cell carcinoma. |journal=Oral Oncol. |volume=40 |issue= 7 |pages= 705-12 |year= 2004 |pmid= 15172640 |doi= 10.1016/j.oraloncology.2004.01.010 }}
*{{cite journal  | author=Coulombe P |title=N-Terminal ubiquitination of extracellular signal-regulated kinase 3 and p21 directs their degradation by the proteasome |journal=Mol. Cell. Biol. |volume=24 |issue= 14 |pages= 6140–6150 |year= 2004 |pmid= 15226418 |doi= 10.1128/MCB.24.14.6140-6150.2004 | pmc=434260  |name-list-format=vanc| author2=Rodier G  | author3=Bonneil E  | display-authors=3  | last4=Thibault  | first4=P.  | last5=Meloche  | first5=S. }}
*{{cite journal  | author=Coulombe P, Rodier G, Bonneil E, ''et al.'' |title=N-Terminal ubiquitination of extracellular signal-regulated kinase 3 and p21 directs their degradation by the proteasome. |journal=Mol. Cell. Biol. |volume=24 |issue= 14 |pages= 6140-50 |year= 2004 |pmid= 15226418 |doi= 10.1128/MCB.24.14.6140-6150.2004 }}
*{{cite journal  | author=Gerhard DS |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= 2121–2127 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928  |name-list-format=vanc| author2=Wagner L  | author3=Feingold EA  | display-authors=3  | last4=Shenmen  | first4=CM  | last5=Grouse  | first5=LH  | last6=Schuler  | first6=G  | last7=Klein  | first7=SL  | last8=Old  | first8=S  | last9=Rasooly  | first9=R }}
*{{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  | author=Rual JF |title=Towards a proteome-scale map of the human protein-protein interaction network |journal=Nature |volume=437 |issue= 7062 |pages= 1173–1178 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 |name-list-format=vanc| author2=Venkatesan K  | author3=Hao T  | display-authors=3  | last4=Hirozane-Kishikawa  | first4=Tomoko  | last5=Dricot  | first5=Amélie  | last6=Li  | first6=Ning  | last7=Berriz  | first7=Gabriel F.  | last8=Gibbons  | first8=Francis D.  | last9=Dreze  | first9=Matija }}
*{{cite journal  | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal  | author=Hoeflich KP |title=Regulation of ERK3/MAPK6 expression by BRAF |journal=Int. J. Oncol. |volume=29 |issue= 4 |pages= 839–49 |year= 2006 |pmid= 16964379 |doi= 10.3892/ijo.29.4.839|name-list-format=vanc| author2=Eby MT  | author3=Forrest WF  | display-authors=3  | last4=Gray  | first4=DC  | last5=Tien  | first5=JY  | last6=Stern  | first6=HM  | last7=Murray  | first7=LJ  | last8=Davis  | first8=DP  | last9=Modrusan  | first9=Z }}
*{{cite journal  | author=Hoeflich KP, Eby MT, Forrest WF, ''et al.'' |title=Regulation of ERK3/MAPK6 expression by BRAF. |journal=Int. J. Oncol. |volume=29 |issue= 4 |pages= 839-49 |year= 2006 |pmid= 16964379 |doi=  }}
}}
}}
{{refend}}
{{refend}}


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[[Category:EC 2.7.11]]
 
 
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Revision as of 06:07, 4 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Mitogen-activated protein kinase 6 is an enzyme that in humans is encoded by the MAPK6 gene.[1][2]

The protein encoded by this gene is a member of the Ser/Thr protein kinase family, and is most closely related to mitogen-activated protein kinases (MAP kinases). MAP kinases also known as extracellular signal-regulated kinases (ERKs), are activated through protein phosphorylation cascades and act as integration points for multiple biochemical signals. This kinase is localized in the nucleus, and has been reported to be activated in fibroblasts upon treatment with serum or phorbol esters.[2]

References

  1. ↑ Meloche S, Beatty BG, Pellerin J (Dec 1996). "Primary structure, expression and chromosomal locus of a human homolog of rat ERK3". Oncogene. 13 (7): 1575–9. PMID 8875998.
  2. ↑ 2.0 2.1 "Entrez Gene: MAPK6 mitogen-activated protein kinase 6".

External links

Further reading


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