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{{Infobox_gene}}
{{PBB_Controls
'''MAP kinase-activated protein kinase 3''' is an [[enzyme]] that in humans is encoded by the ''MAPKAPK3'' [[gene]].<ref name="pmid8626550">{{cite journal | vauthors = McLaughlin MM, Kumar S, McDonnell PC, Van Horn S, Lee JC, Livi GP, Young PR | title = Identification of mitogen-activated protein (MAP) kinase-activated protein kinase-3, a novel substrate of CSBP p38 MAP kinase | journal = J Biol Chem | volume = 271 | issue = 14 | pages = 8488–92 | date = June 1996 | pmid = 8626550 | pmc =  | doi = 10.1074/jbc.271.14.8488 }}</ref><ref name="pmid8622688">{{cite journal | vauthors = Sithanandam G, Latif F, Duh FM, Bernal R, Smola U, Li H, Kuzmin I, Wixler V, Geil L, Shrestha S | title = 3pK, a new mitogen-activated protein kinase-activated protein kinase located in the small cell lung cancer tumor suppressor gene region | journal = Mol Cell Biol | volume = 16 | issue = 3 | pages = 868–76 | date = June 1996 | pmid = 8622688 | pmc = 231067 | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: MAPKAPK3 mitogen-activated protein kinase-activated protein kinase 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7867| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Mitogen-activated protein kinase-activated protein kinase 3
| HGNCid = 6888
| Symbol = MAPKAPK3
| AltSymbols =; 3PK; MAPKAP3
| OMIM = 602130
| ECnumber = 
| Homologene = 55836
| MGIid = 2143163
| GeneAtlas_image1 = PBB_GE_MAPKAPK3_202787_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_MAPKAPK3_202788_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:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| 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 = 7867
    | Hs_Ensembl = ENSG00000114738
    | Hs_RefseqProtein = NP_004626
    | Hs_RefseqmRNA = NM_004635
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 3
    | Hs_GenLoc_start = 50624343
    | Hs_GenLoc_end = 50661724
    | Hs_Uniprot = Q16644
    | Mm_EntrezGene = 102626
    | Mm_Ensembl = ENSMUSG00000032577
    | Mm_RefseqmRNA = NM_178907
    | Mm_RefseqProtein = NP_849238
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 9
    | Mm_GenLoc_start = 107113028
    | Mm_GenLoc_end = 107147978
    | Mm_Uniprot = Q3UMW7
  }}
}}
'''Mitogen-activated protein kinase-activated protein kinase 3''', also known as '''MAPKAPK3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MAPKAPK3 mitogen-activated protein kinase-activated protein kinase 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7867| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
This gene encodes a member of the Ser/Thr protein kinase family. This kinase functions as a mitogen-activated protein kinase (MAP kinase)- activated protein kinase. MAP kinases are also known as extracellular signal-regulated kinases (ERKs), act as an integration point for multiple biochemical signals. This kinase was shown to be activated by growth inducers and stress stimulation of cells. In vitro studies demonstrated that ERK, p38 MAP kinase and Jun N-terminal kinase were all able to phosphorylate and activate this kinase, which suggested the role of this kinase as an integrative element of signaling in both mitogen and stress responses. This kinase was reported to interact with, phosphorylate and repress the activity of E47, which is a basic helix-loop-helix transcription factor known to be involved in the regulation of tissue-specific gene expression and cell differentiation.<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the Ser/Thr protein kinase family. This kinase functions as a mitogen-activated protein kinase (MAP kinase)- activated protein kinase. MAP kinases are also known as extracellular signal-regulated kinases (ERKs), act as an integration point for multiple biochemical signals. This kinase was shown to be activated by growth inducers and stress stimulation of cells. In vitro studies demonstrated that ERK, p38 MAP kinase and Jun N-terminal kinase were all able to phosphorylate and activate this kinase, which suggested the role of this kinase as an integrative element of signaling in both mitogen and stress responses. This kinase was reported to interact with, phosphorylate and repress the activity of E47, which is a basic helix-loop-helix transcription factor known to be involved in the regulation of tissue-specific gene expression and cell differentiation.<ref name="entrez">{{cite web | title = Entrez Gene: MAPKAPK3 mitogen-activated protein kinase-activated protein kinase 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7867| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
MAPKAPK3 has been shown to [[Protein-protein interaction|interact]] with [[MAPK14]]<ref name=pmid11157753>{{cite journal | vauthors = Tanoue T, Maeda R, Adachi M, Nishida E | title = Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions | journal = EMBO J. | volume = 20 | issue = 3 | pages = 466–79 | date = February 2001 | pmid = 11157753 | pmc = 133461 | doi = 10.1093/emboj/20.3.466 }}</ref> and [[TCF3]].<ref name=pmid10781029>{{cite journal | vauthors = Neufeld B, Grosse-Wilde A, Hoffmeyer A, Jordan BW, Chen P, Dinev D, Ludwig S, Rapp UR | title = Serine/Threonine kinases 3pK and MAPK-activated protein kinase 2 interact with the basic helix-loop-helix transcription factor E47 and repress its transcriptional activity | journal = J. Biol. Chem. | volume = 275 | issue = 27 | pages = 20239–42 | date = July 2000 | pmid = 10781029 | doi = 10.1074/jbc.C901040199 }}</ref>
{{refbegin | 2}}
 
{{PBB_Further_reading
== References ==
| citations =  
{{reflist}}
*{{cite journal | author=Wei MH, Latif F, Bader S, ''et al.'' |title=Construction of a 600-kilobase cosmid clone contig and generation of a transcriptional map surrounding the lung cancer tumor suppressor gene (TSG) locus on human chromosome 3p21.3: progress toward the isolation of a lung cancer TSG. |journal=Cancer Res. |volume=56 |issue= 7 |pages= 1487-92 |year= 1996 |pmid= 8603390 |doi= }}
 
*{{cite journal | author=Sithanandam G, Latif F, Duh FM, ''et al.'' |title=3pK, a new mitogen-activated protein kinase-activated protein kinase located in the small cell lung cancer tumor suppressor gene region. |journal=Mol. Cell. Biol. |volume=16 |issue= 3 |pages= 868-76 |year= 1996 |pmid= 8622688 |doi= }}
== Further reading ==
*{{cite journal | author=McLaughlin MM, Kumar S, McDonnell PC, ''et al.'' |title=Identification of mitogen-activated protein (MAP) kinase-activated protein kinase-3, a novel substrate of CSBP p38 MAP kinase. |journal=J. Biol. Chem. |volume=271 |issue= 14 |pages= 8488-92 |year= 1996 |pmid= 8626550 |doi=  }}
{{refbegin|35em}}
*{{cite journal | author=Clifton AD, Young PR, Cohen P |title=A comparison of the substrate specificity of MAPKAP kinase-2 and MAPKAP kinase-3 and their activation by cytokines and cellular stress. |journal=FEBS Lett. |volume=392 |issue= 3 |pages= 209-14 |year= 1996 |pmid= 8774846 |doi= }}
* {{cite journal | vauthors = Wei MH, Latif F, Bader S, Kashuba V, Chen JY, Duh FM, Sekido Y, Lee CC, Geil L, Kuzmin I, Zabarovsky E, Klein G, Zbar B, Minna JD, Lerman MI | title = Construction of a 600-kilobase cosmid clone contig and generation of a transcriptional map surrounding the lung cancer tumor suppressor gene (TSG) locus on human chromosome 3p21.3: progress toward the isolation of a lung cancer TSG | journal = Cancer Res. | volume = 56 | issue = 7 | pages = 1487–92 | year = 1996 | pmid = 8603390 | doi =  }}
*{{cite journal | author=Ludwig S, Engel K, Hoffmeyer A, ''et al.'' |title=3pK, a novel mitogen-activated protein (MAP) kinase-activated protein kinase, is targeted by three MAP kinase pathways. |journal=Mol. Cell. Biol. |volume=16 |issue= 12 |pages= 6687-97 |year= 1997 |pmid= 8943323 |doi=  }}
* {{cite journal | vauthors = Clifton AD, Young PR, Cohen P | title = A comparison of the substrate specificity of MAPKAP kinase-2 and MAPKAP kinase-3 and their activation by cytokines and cellular stress | journal = FEBS Lett. | volume = 392 | issue = 3 | pages = 209–14 | year = 1996 | pmid = 8774846 | doi = 10.1016/0014-5793(96)00816-2 }}
*{{cite journal | author=Kumar S, McDonnell PC, Gum RJ, ''et al.'' |title=Novel homologues of CSBP/p38 MAP kinase: activation, substrate specificity and sensitivity to inhibition by pyridinyl imidazoles. |journal=Biochem. Biophys. Res. Commun. |volume=235 |issue= 3 |pages= 533-8 |year= 1997 |pmid= 9207191 |doi= 10.1006/bbrc.1997.6849 }}
* {{cite journal | vauthors = Ludwig S, Engel K, Hoffmeyer A, Sithanandam G, Neufeld B, Palm D, Gaestel M, Rapp UR | title = 3pK, a novel mitogen-activated protein (MAP) kinase-activated protein kinase, is targeted by three MAP kinase pathways | journal = Mol. Cell. Biol. | volume = 16 | issue = 12 | pages = 6687–97 | year = 1997 | pmid = 8943323 | pmc = 231671 | doi =  }}
*{{cite journal | author=Neufeld B, Grosse-Wilde A, Hoffmeyer A, ''et al.'' |title=Serine/Threonine kinases 3pK and MAPK-activated protein kinase 2 interact with the basic helix-loop-helix transcription factor E47 and repress its transcriptional activity. |journal=J. Biol. Chem. |volume=275 |issue= 27 |pages= 20239-42 |year= 2000 |pmid= 10781029 |doi= 10.1074/jbc.C901040199 }}
* {{cite journal | vauthors = Kumar S, McDonnell PC, Gum RJ, Hand AT, Lee JC, Young PR | title = Novel homologues of CSBP/p38 MAP kinase: activation, substrate specificity and sensitivity to inhibition by pyridinyl imidazoles | journal = Biochem. Biophys. Res. Commun. | volume = 235 | issue = 3 | pages = 533–8 | year = 1997 | pmid = 9207191 | doi = 10.1006/bbrc.1997.6849 }}
*{{cite journal | author=Tanoue T, Maeda R, Adachi M, Nishida E |title=Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions. |journal=EMBO J. |volume=20 |issue= 3 |pages= 466-79 |year= 2001 |pmid= 11157753 |doi= 10.1093/emboj/20.3.466 }}
* {{cite journal | vauthors = Neufeld B, Grosse-Wilde A, Hoffmeyer A, Jordan BW, Chen P, Dinev D, Ludwig S, Rapp UR | title = Serine/Threonine kinases 3pK and MAPK-activated protein kinase 2 interact with the basic helix-loop-helix transcription factor E47 and repress its transcriptional activity | journal = J. Biol. Chem. | volume = 275 | issue = 27 | pages = 20239–42 | year = 2000 | pmid = 10781029 | doi = 10.1074/jbc.C901040199 }}
*{{cite journal | author=Simkhovich BZ, Abdishoo S, Poizat C, ''et al.'' |title=Gene activity changes in ischemically preconditioned rabbit heart gene: discovery array study. |journal=Heart disease (Hagerstown, Md.) |volume=4 |issue= 2 |pages= 63-9 |year= 2002 |pmid= 11975836 |doi= }}
* {{cite journal | vauthors = Tanoue T, Maeda R, Adachi M, Nishida E | title = Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions | journal = EMBO J. | volume = 20 | issue = 3 | pages = 466–79 | year = 2001 | pmid = 11157753 | pmc = 133461 | doi = 10.1093/emboj/20.3.466 }}
*{{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 = Simkhovich BZ, Abdishoo S, Poizat C, Hale SL, Kedes LH, Kloner RA | title = Gene activity changes in ischemically preconditioned rabbit heart gene: discovery array study | journal = Heart disease (Hagerstown, Md.) | volume = 4 | issue = 2 | pages = 63–9 | year = 2002 | pmid = 11975836 | doi = 10.1097/00132580-200203000-00002 }}
*{{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 = 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 | pmc = 1222910 | doi = 10.1042/BJ20020916 }}
*{{cite journal  | author=Zakowski V, Keramas G, Kilian K, ''et al.'' |title=Mitogen-activated 3p kinase is active in the nucleus. |journal=Exp. Cell Res. |volume=299 |issue= 1 |pages= 101-9 |year= 2004 |pmid= 15302577 |doi= 10.1016/j.yexcr.2004.05.027 }}
* {{cite journal | vauthors = Zakowski V, Keramas G, Kilian K, Rapp UR, Ludwig S | title = Mitogen-activated 3p kinase is active in the nucleus | journal = Exp. Cell Res. | volume = 299 | issue = 1 | pages = 101–9 | year = 2004 | pmid = 15302577 | doi = 10.1016/j.yexcr.2004.05.027 }}
*{{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 = Voncken JW, Niessen H, Neufeld B, Rennefahrt U, Dahlmans V, Kubben N, Holzer B, Ludwig S, Rapp UR | title = MAPKAP kinase 3pK phosphorylates and regulates chromatin association of the polycomb group protein Bmi1 | journal = J. Biol. Chem. | volume = 280 | issue = 7 | pages = 5178–87 | year = 2005 | pmid = 15563468 | doi = 10.1074/jbc.M407155200 }}
*{{cite journal  | author=Voncken JW, Niessen H, Neufeld B, ''et al.'' |title=MAPKAP kinase 3pK phosphorylates and regulates chromatin association of the polycomb group protein Bmi1. |journal=J. Biol. Chem. |volume=280 |issue= 7 |pages= 5178-87 |year= 2005 |pmid= 15563468 |doi= 10.1074/jbc.M407155200 }}
* {{cite journal|authorlink30=Huda Zoghbi | vauthors = Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M | 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=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 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{Serine/threonine-specific protein kinases}}
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{{gene-3-stub}}

Latest revision as of 16:13, 8 October 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

MAP kinase-activated protein kinase 3 is an enzyme that in humans is encoded by the MAPKAPK3 gene.[1][2][3]

Function

This gene encodes a member of the Ser/Thr protein kinase family. This kinase functions as a mitogen-activated protein kinase (MAP kinase)- activated protein kinase. MAP kinases are also known as extracellular signal-regulated kinases (ERKs), act as an integration point for multiple biochemical signals. This kinase was shown to be activated by growth inducers and stress stimulation of cells. In vitro studies demonstrated that ERK, p38 MAP kinase and Jun N-terminal kinase were all able to phosphorylate and activate this kinase, which suggested the role of this kinase as an integrative element of signaling in both mitogen and stress responses. This kinase was reported to interact with, phosphorylate and repress the activity of E47, which is a basic helix-loop-helix transcription factor known to be involved in the regulation of tissue-specific gene expression and cell differentiation.[3]

Interactions

MAPKAPK3 has been shown to interact with MAPK14[4] and TCF3.[5]

References

  1. ↑ McLaughlin MM, Kumar S, McDonnell PC, Van Horn S, Lee JC, Livi GP, Young PR (June 1996). "Identification of mitogen-activated protein (MAP) kinase-activated protein kinase-3, a novel substrate of CSBP p38 MAP kinase". J Biol Chem. 271 (14): 8488–92. doi:10.1074/jbc.271.14.8488. PMID 8626550.
  2. ↑ Sithanandam G, Latif F, Duh FM, Bernal R, Smola U, Li H, Kuzmin I, Wixler V, Geil L, Shrestha S (June 1996). "3pK, a new mitogen-activated protein kinase-activated protein kinase located in the small cell lung cancer tumor suppressor gene region". Mol Cell Biol. 16 (3): 868–76. PMC 231067. PMID 8622688.
  3. ↑ 3.0 3.1 "Entrez Gene: MAPKAPK3 mitogen-activated protein kinase-activated protein kinase 3".
  4. ↑ Tanoue T, Maeda R, Adachi M, Nishida E (February 2001). "Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions". EMBO J. 20 (3): 466–79. doi:10.1093/emboj/20.3.466. PMC 133461. PMID 11157753.
  5. ↑ Neufeld B, Grosse-Wilde A, Hoffmeyer A, Jordan BW, Chen P, Dinev D, Ludwig S, Rapp UR (July 2000). "Serine/Threonine kinases 3pK and MAPK-activated protein kinase 2 interact with the basic helix-loop-helix transcription factor E47 and repress its transcriptional activity". J. Biol. Chem. 275 (27): 20239–42. doi:10.1074/jbc.C901040199. PMID 10781029.

Further reading


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