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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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| 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" | | 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 | {{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 | *{{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 | | *{{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 | | *{{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 | | *{{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 |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 | | *{{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 | | *{{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 | *{{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 | *{{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 | *{{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 | | *{{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 | | *{{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 | *{{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 | *{{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 | *{{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 | |||
}} | }} | ||
{{refend}} | {{refend}} | ||
{{protein- | {{PDB Gallery|geneid=5597}} | ||
{{ | {{Serine/threonine-specific protein kinases}} | ||
{{Enzymes}} | |||
{{Portal bar|Molecular and Cellular Biology|border=no}} | |||
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[[Category:EC 2.7.11]] | |||
{{gene-15-stub}} |
Revision as of 06:07, 4 September 2017
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External IDs | GeneCards: [1] | ||||||
Orthologs | |||||||
Species | Human | Mouse | |||||
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/a | n/a | |||||
PubMed search | n/a | n/a | |||||
Wikidata | |||||||
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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
External links
Further reading
- Boulton TG, Nye SH, Robbins DJ, et al. (1991). "ERKs: a family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF". Cell. 65 (4): 663–675. doi:10.1016/0092-8674(91)90098-J. PMID 2032290.
- Zhu AX, Zhao Y, Moller DE, Flier JS (1994). "Cloning and characterization of p97MAPK, a novel human homolog of rat ERK-3". Mol. Cell. Biol. 14 (12): 8202–11. PMC 359359. PMID 7969157.
- Cheng M, Boulton TG, Cobb MH (1996). "ERK3 is a constitutively nuclear protein kinase". J. Biol. Chem. 271 (15): 8951–8958. doi:10.1074/jbc.271.15.8951. PMID 8621539.
- Sauma S, Friedman E (1996). "Increased expression of protein kinase C beta activates ERK3". J. Biol. Chem. 271 (19): 11422–11426. doi:10.1074/jbc.271.19.11422. PMID 8626698.
- Zimmermann J, Lamerant N, Grossenbacher R, Furst P (2001). "Proteasome- and p38-dependent regulation of ERK3 expression". J. Biol. Chem. 276 (14): 10759–10766. doi:10.1074/jbc.M008567200. PMID 11148204.
- Robinson MJ, Xu Be BE, Stippec S, Cobb MH (2002). "Different domains of the mitogen-activated protein kinases ERK3 and ERK2 direct subcellular localization and upstream specificity in vivo". J. Biol. Chem. 277 (7): 5094–5100. doi:10.1074/jbc.M110935200. PMID 11741894.
- Kinet S, Bernard F, Mongellaz C, et al. (2002). "gp120-mediated induction of the MAPK cascade is dependent on the activation state of CD4(+) lymphocytes". Blood. 100 (7): 2546–2553. doi:10.1182/blood-2002-03-0819. PMID 12239168.
- 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): 16899–16903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Coulombe P, Rodier G, Pelletier S, et al. (2003). "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". Mol. Cell. Biol. 23 (13): 4542–4558. doi:10.1128/MCB.23.13.4542-4558.2003. PMC 164847. PMID 12808096.
- Julien C, Coulombe P, Meloche S (2004). "Nuclear export of ERK3 by a CRM1-dependent mechanism regulates its inhibitory action on cell cycle progression". J. Biol. Chem. 278 (43): 42615–42624. doi:10.1074/jbc.M302724200. PMID 12915405.
- Rai R, Mahale A, Saranath D (2004). "Molecular cloning, isolation and characterisation of ERK3 gene from chewing-tobacco induced oral squamous cell carcinoma". Oral Oncol. 40 (7): 705–712. doi:10.1016/j.oraloncology.2004.01.010. PMID 15172640.
- Coulombe P, Rodier G, Bonneil E, et al. (2004). "N-Terminal ubiquitination of extracellular signal-regulated kinase 3 and p21 directs their degradation by the proteasome". Mol. Cell. Biol. 24 (14): 6140–6150. doi:10.1128/MCB.24.14.6140-6150.2004. PMC 434260. PMID 15226418.
- 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): 2121–2127. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–1178. doi:10.1038/nature04209. PMID 16189514.
- Hoeflich KP, Eby MT, Forrest WF, et al. (2006). "Regulation of ERK3/MAPK6 expression by BRAF". Int. J. Oncol. 29 (4): 839–49. doi:10.3892/ijo.29.4.839. PMID 16964379.
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