MAP3K2: Difference between revisions

Jump to navigation Jump to search
VisualWikitext
WikiBot (talk | contribs)
Bots, Bureaucrats, bureaucrats, interwiki, nocaptcha, Administrators
57,550 edits
m Robot: Automated text replacement (-{{WikiDoc Cardiology Network Infobox}} +, -<references /> +{{reflist|2}}, -{{reflist}} +{{reflist|2}})
 
 
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Mitogen-activated protein kinase kinase kinase 2''' is an [[enzyme]] that in humans is encoded by the ''MAP3K2'' [[gene]].<ref name="pmid8621389">{{cite journal | vauthors = Blank JL, Gerwins P, Elliott EM, Sather S, Johnson GL | title = Molecular cloning of mitogen-activated protein/ERK kinase kinases (MEKK) 2 and 3. Regulation of sequential phosphorylation pathways involving mitogen-activated protein kinase and c-Jun kinase | journal = The Journal of Biological Chemistry | volume = 271 | issue = 10 | pages = 5361–8 | date = Mar 1996 | pmid = 8621389 | pmc =  | doi = 10.1074/jbc.271.10.5361 }}</ref><ref name="pmid10085062">{{cite journal | vauthors = Zhao Q, Lee FS | title = Mitogen-activated protein kinase/ERK kinase kinases 2 and 3 activate nuclear factor-kappaB through IkappaB kinase-alpha and IkappaB kinase-beta | journal = The Journal of Biological Chemistry | volume = 274 | issue = 13 | pages = 8355–8 | date = Mar 1999 | pmid = 10085062 | pmc =  | doi = 10.1074/jbc.274.13.8355 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: MAP3K2 mitogen-activated protein kinase kinase kinase 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10746| accessdate = }}</ref>
| update_page = yes
| 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. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_MAP3K2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2cu1.
| PDB = {{PDB2|2cu1}}, {{PDB2|2npt}}
| Name = Mitogen-activated protein kinase kinase kinase 2
| HGNCid = 6854
| Symbol = MAP3K2
| AltSymbols =; MEKK2; MEKK2B
| OMIM = 609487
| ECnumber = 
| Homologene = 74576
| MGIid = 1346873
| GeneAtlas_image1 = PBB_GE_MAP3K2_221695_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:0004672 |text = protein kinase activity}} {{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:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007257 |text = activation of JNK activity}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 10746
    | Hs_Ensembl = ENSG00000169967
    | Hs_RefseqProtein = XP_001128799
    | Hs_RefseqmRNA = XM_001128799
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 127779993
    | Hs_GenLoc_end = 127813100
    | Hs_Uniprot = Q9Y2U5
    | Mm_EntrezGene = 26405
    | Mm_Ensembl = ENSMUSG00000024383
    | Mm_RefseqmRNA = NM_011946
    | Mm_RefseqProtein = NP_036076
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 18
    | Mm_GenLoc_start = 32306206
    | Mm_GenLoc_end = 32371521
    | Mm_Uniprot = Q61083
  }}
}}
'''Mitogen-activated protein kinase kinase kinase 2''', also known as '''MAP3K2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MAP3K2 mitogen-activated protein kinase kinase kinase 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10746| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The protein encoded by this gene is a member of [[serine/threonine protein kinase]] family. This [[kinase]] preferentially activates other kinases involved in the [[MAP kinase]] [[signaling pathway]]. This kinase has been shown to directly phosphorylate and activate [[IkappaB kinase]]s, and thus plays a role in [[NF-kappa B]] signaling pathway. This kinase has also been found to bind and activate [[protein kinase C]][[PRK2|-related kinase 2]], which suggests its involvement in a regulated signaling process.<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of serine/threonine protein kinase family. This kinase preferentially activates other kinases involved in the MAP kinase signaling pathway. This kinase has been shown to directly phosphorylate and activate Ikappa B kinases, and thus plays a role in NF-kappa B signaling pathway. This kinase has also been found to bind and activate protein kinase C-related kinase 2, which suggests its involvement in a regulated signaling process.<ref name="entrez">{{cite web | title = Entrez Gene: MAP3K2 mitogen-activated protein kinase kinase kinase 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10746| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
MAP3K2 has been shown to [[Protein-protein interaction|interact]] with:
{{div col|colwidth=20em}}
* [[MAP2K5]],<ref name = pmid11073940/>
* [[MAP2K7]],<ref name = pmid10713157>{{cite journal | vauthors = Cheng J, Yang J, Xia Y, Karin M, Su B | title = Synergistic interaction of MEK kinase 2, c-Jun N-terminal kinase (JNK) kinase 2, and JNK1 results in efficient and specific JNK1 activation | journal = Molecular and Cellular Biology | volume = 20 | issue = 7 | pages = 2334–42 | date = Apr 2000 | pmid = 10713157 | pmc = 85399 | doi =  10.1128/mcb.20.7.2334-2342.2000}}</ref>
* [[MAPK8]],<ref name = pmid10713157/>
* [[SH2D2A]],<ref name = pmid11073940>{{cite journal | vauthors = Sun W, Kesavan K, Schaefer BC, Garrington TP, Ware M, Johnson NL, Gelfand EW, Johnson GL | title = MEKK2 associates with the adapter protein Lad/RIBP and regulates the MEK5-BMK1/ERK5 pathway | journal = The Journal of Biological Chemistry | volume = 276 | issue = 7 | pages = 5093–100 | date = Feb 2001 | pmid = 11073940 | doi = 10.1074/jbc.M003719200 }}</ref>  and
* [[XIAP]]<ref name = pmid18761086>{{cite journal | vauthors = Winsauer G, Resch U, Hofer-Warbinek R, Schichl YM, de Martin R | title = XIAP regulates bi-phasic NF-kappaB induction involving physical interaction and ubiquitination of MEKK2 | journal = Cellular Signalling | volume = 20 | issue = 11 | pages = 2107–12 | date = Nov 2008 | pmid = 18761086 | doi = 10.1016/j.cellsig.2008.08.004 }}</ref>
{{Div col end}}
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Yan M, Dai T, Deak JC, Kyriakis JM, Zon LI, Woodgett JR, Templeton DJ | title = Activation of stress-activated protein kinase by MEKK1 phosphorylation of its activator SEK1 | journal = Nature | volume = 372 | issue = 6508 | pages = 798–800 | year = 1995 | pmid = 7997270 | doi = 10.1038/372798a0 }}
| citations =
* {{cite journal | vauthors = Wu Z, Wu J, Jacinto E, Karin M | title = Molecular cloning and characterization of human JNKK2, a novel Jun NH2-terminal kinase-specific kinase | journal = Molecular and Cellular Biology | volume = 17 | issue = 12 | pages = 7407–16 | date = Dec 1997 | pmid = 9372971 | pmc = 232596 | doi =  10.1128/mcb.17.12.7407}}
*{{cite journal | author=Yan M, Dai T, Deak JC, ''et al.'' |title=Activation of stress-activated protein kinase by MEKK1 phosphorylation of its activator SEK1. |journal=Nature |volume=372 |issue= 6508 |pages= 798-800 |year= 1995 |pmid= 7997270 |doi= }}
* {{cite journal | vauthors = Fanger GR, Widmann C, Porter AC, Sather S, Johnson GL, Vaillancourt RR | title = 14-3-3 proteins interact with specific MEK kinases | journal = The Journal of Biological Chemistry | volume = 273 | issue = 6 | pages = 3476–83 | date = Feb 1998 | pmid = 9452471 | doi = 10.1074/jbc.273.6.3476 }}
*{{cite journal  | author=Blank JL, Gerwins P, Elliott EM, ''et al.'' |title=Molecular cloning of mitogen-activated protein/ERK kinase kinases (MEKK) 2 and 3. Regulation of sequential phosphorylation pathways involving mitogen-activated protein kinase and c-Jun kinase. |journal=J. Biol. Chem. |volume=271 |issue= 10 |pages= 5361-8 |year= 1996 |pmid= 8621389 |doi=  }}
* {{cite journal | vauthors = Cheng J, Yang J, Xia Y, Karin M, Su B | title = Synergistic interaction of MEK kinase 2, c-Jun N-terminal kinase (JNK) kinase 2, and JNK1 results in efficient and specific JNK1 activation | journal = Molecular and Cellular Biology | volume = 20 | issue = 7 | pages = 2334–42 | date = Apr 2000 | pmid = 10713157 | pmc = 85399 | doi = 10.1128/MCB.20.7.2334-2342.2000 }}
*{{cite journal | author=Wu Z, Wu J, Jacinto E, Karin M |title=Molecular cloning and characterization of human JNKK2, a novel Jun NH2-terminal kinase-specific kinase. |journal=Mol. Cell. Biol. |volume=17 |issue= 12 |pages= 7407-16 |year= 1997 |pmid= 9372971 |doi=  }}
* {{cite journal | vauthors = Sun W, Vincent S, Settleman J, Johnson GL | title = MEK kinase 2 binds and activates protein kinase C-related kinase 2. Bifurcation of kinase regulatory pathways at the level of an MAPK kinase kinase | journal = The Journal of Biological Chemistry | volume = 275 | issue = 32 | pages = 24421–8 | date = Aug 2000 | pmid = 10818102 | doi = 10.1074/jbc.M003148200 }}
*{{cite journal | author=Fanger GR, Widmann C, Porter AC, ''et al.'' |title=14-3-3 proteins interact with specific MEK kinases. |journal=J. Biol. Chem. |volume=273 |issue= 6 |pages= 3476-83 |year= 1998 |pmid= 9452471 |doi= }}
* {{cite journal | vauthors = Garrington TP, Ishizuka T, Papst PJ, Chayama K, Webb S, Yujiri T, Sun W, Sather S, Russell DM, Gibson SB, Keller G, Gelfand EW, Johnson GL | title = MEKK2 gene disruption causes loss of cytokine production in response to IgE and c-Kit ligand stimulation of ES cell-derived mast cells | journal = The EMBO Journal | volume = 19 | issue = 20 | pages = 5387–95 | date = Oct 2000 | pmid = 11032806 | pmc = 314024 | doi = 10.1093/emboj/19.20.5387 }}
*{{cite journal  | author=Zhao Q, Lee FS |title=Mitogen-activated protein kinase/ERK kinase kinases 2 and 3 activate nuclear factor-kappaB through IkappaB kinase-alpha and IkappaB kinase-beta. |journal=J. Biol. Chem. |volume=274 |issue= 13 |pages= 8355-8 |year= 1999 |pmid= 10085062 |doi=  }}
* {{cite journal | vauthors = Huang J, Tu Z, Lee FS | title = Mutations in protein kinase subdomain X differentially affect MEKK2 and MEKK1 activity | journal = Biochemical and Biophysical Research Communications | volume = 303 | issue = 2 | pages = 532–40 | date = Apr 2003 | pmid = 12659851 | doi = 10.1016/S0006-291X(03)00387-5 }}
*{{cite journal | author=Cheng J, Yang J, Xia Y, ''et al.'' |title=Synergistic interaction of MEK kinase 2, c-Jun N-terminal kinase (JNK) kinase 2, and JNK1 results in efficient and specific JNK1 activation. |journal=Mol. Cell. Biol. |volume=20 |issue= 7 |pages= 2334-42 |year= 2000 |pmid= 10713157 |doi= }}
* {{cite journal | vauthors = Nakamura K, Johnson GL | title = PB1 domains of MEKK2 and MEKK3 interact with the MEK5 PB1 domain for activation of the ERK5 pathway | journal = The Journal of Biological Chemistry | volume = 278 | issue = 39 | pages = 36989–92 | date = Sep 2003 | pmid = 12912994 | doi = 10.1074/jbc.C300313200 }}
*{{cite journal | author=Sun W, Vincent S, Settleman J, Johnson GL |title=MEK kinase 2 binds and activates protein kinase C-related kinase 2. Bifurcation of kinase regulatory pathways at the level of an MAPK kinase kinase. |journal=J. Biol. Chem. |volume=275 |issue= 32 |pages= 24421-8 |year= 2000 |pmid= 10818102 |doi= 10.1074/jbc.M003148200 }}
* {{cite journal | vauthors = Hammaker DR, Boyle DL, Chabaud-Riou M, Firestein GS | title = Regulation of c-Jun N-terminal kinase by MEKK-2 and mitogen-activated protein kinase kinase kinases in rheumatoid arthritis | journal = Journal of Immunology | volume = 172 | issue = 3 | pages = 1612–8 | date = Feb 2004 | pmid = 14734742 | doi = 10.4049/jimmunol.172.3.1612 }}
*{{cite journal | author=Garrington TP, Ishizuka T, Papst PJ, ''et al.'' |title=MEKK2 gene disruption causes loss of cytokine production in response to IgE and c-Kit ligand stimulation of ES cell-derived mast cells. |journal=EMBO J. |volume=19 |issue= 20 |pages= 5387-95 |year= 2000 |pmid= 11032806 |doi= 10.1093/emboj/19.20.5387 }}
* {{cite journal | vauthors = Raviv Z, Kalie E, Seger R | title = MEK5 and ERK5 are localized in the nuclei of resting as well as stimulated cells, while MEKK2 translocates from the cytosol to the nucleus upon stimulation | journal = Journal of Cell Science | volume = 117 | issue = Pt 9 | pages = 1773–84 | date = Apr 2004 | pmid = 15075238 | doi = 10.1242/jcs.01040 }}
*{{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 = Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T | title = Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization | journal = Current Biology | volume = 14 | issue = 16 | pages = 1436–50 | date = Aug 2004 | pmid = 15324660 | doi = 10.1016/j.cub.2004.07.051 }}
*{{cite journal  | author=Huang J, Tu Z, Lee FS |title=Mutations in protein kinase subdomain X differentially affect MEKK2 and MEKK1 activity. |journal=Biochem. Biophys. Res. Commun. |volume=303 |issue= 2 |pages= 532-40 |year= 2003 |pmid= 12659851 |doi= }}
* {{cite journal | vauthors = Benzinger A, Muster N, Koch HB, Yates JR, Hermeking H | title = Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer | journal = Molecular & Cellular Proteomics | volume = 4 | issue = 6 | pages = 785–95 | date = Jun 2005 | pmid = 15778465 | doi = 10.1074/mcp.M500021-MCP200 }}
*{{cite journal | author=Nakamura K, Johnson GL |title=PB1 domains of MEKK2 and MEKK3 interact with the MEK5 PB1 domain for activation of the ERK5 pathway. |journal=J. Biol. Chem. |volume=278 |issue= 39 |pages= 36989-92 |year= 2003 |pmid= 12912994 |doi= 10.1074/jbc.C300313200 }}
* {{cite journal | vauthors = Cheng J, Zhang D, Kim K, Zhao Y, Zhao Y, Su B | title = Mip1, an MEKK2-interacting protein, controls MEKK2 dimerization and activation | journal = Molecular and Cellular Biology | volume = 25 | issue = 14 | pages = 5955–64 | date = Jul 2005 | pmid = 15988011 | pmc = 1168836 | doi = 10.1128/MCB.25.14.5955-5964.2005 }}
*{{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 = Pelkmans L, Zerial M | title = Kinase-regulated quantal assemblies and kiss-and-run recycling of caveolae | journal = Nature | volume = 436 | issue = 7047 | pages = 128–33 | date = Jul 2005 | pmid = 16001074 | doi = 10.1038/nature03866 }}
*{{cite journal  | author=Hammaker DR, Boyle DL, Chabaud-Riou M, Firestein GS |title=Regulation of c-Jun N-terminal kinase by MEKK-2 and mitogen-activated protein kinase kinase kinases in rheumatoid arthritis. |journal=J. Immunol. |volume=172 |issue= 3 |pages= 1612-8 |year= 2004 |pmid= 14734742 |doi= }}
* {{cite journal | vauthors = Wissing J, Jänsch L, Nimtz M, Dieterich G, Hornberger R, Kéri G, Wehland J, Daub H | title = Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry | journal = Molecular & Cellular Proteomics | volume = 6 | issue = 3 | pages = 537–47 | date = Mar 2007 | pmid = 17192257 | doi = 10.1074/mcp.T600062-MCP200 }}
*{{cite journal | author=Raviv Z, Kalie E, Seger R |title=MEK5 and ERK5 are localized in the nuclei of resting as well as stimulated cells, while MEKK2 translocates from the cytosol to the nucleus upon stimulation. |journal=J. Cell. Sci. |volume=117 |issue= Pt 9 |pages= 1773-84 |year= 2004 |pmid= 15075238 |doi= 10.1242/jcs.01040 }}
*{{cite journal | author=Jin J, Smith FD, Stark C, ''et al.'' |title=Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization. |journal=Curr. Biol. |volume=14 |issue= 16 |pages= 1436-50 |year= 2004 |pmid= 15324660 |doi= 10.1016/j.cub.2004.07.051 }}
*{{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 }}
*{{cite journal | author=Hillier LW, Graves TA, Fulton RS, ''et al.'' |title=Generation and annotation of the DNA sequences of human chromosomes 2 and 4. |journal=Nature |volume=434 |issue= 7034 |pages= 724-31 |year= 2005 |pmid= 15815621 |doi= 10.1038/nature03466 }}
*{{cite journal  | author=Cheng J, Zhang D, Kim K, ''et al.'' |title=Mip1, an MEKK2-interacting protein, controls MEKK2 dimerization and activation. |journal=Mol. Cell. Biol. |volume=25 |issue= 14 |pages= 5955-64 |year= 2005 |pmid= 15988011 |doi= 10.1128/MCB.25.14.5955-5964.2005 }}
*{{cite journal | author=Pelkmans L, Zerial M |title=Kinase-regulated quantal assemblies and kiss-and-run recycling of caveolae. |journal=Nature |volume=436 |issue= 7047 |pages= 128-33 |year= 2005 |pmid= 16001074 |doi= 10.1038/nature03866 }}
*{{cite journal | author=Wissing J, Jänsch L, Nimtz M, ''et al.'' |title=Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry. |journal=Mol. Cell Proteomics |volume=6 |issue= 3 |pages= 537-47 |year= 2007 |pmid= 17192257 |doi= 10.1074/mcp.T600062-MCP200 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=10746}}
{{WikiDoc Sources}}
{{Serine/threonine-specific protein kinases}}
{{Enzymes}}
{{Portal bar|Molecular and Cellular Biology|border=no}}
 
{{gene-2-stub}}
 
[[Category:EC 2.7.11]]

Latest revision as of 06:05, 4 September 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

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

Mitogen-activated protein kinase kinase kinase 2 is an enzyme that in humans is encoded by the MAP3K2 gene.[1][2][3]

Function

The protein encoded by this gene is a member of serine/threonine protein kinase family. This kinase preferentially activates other kinases involved in the MAP kinase signaling pathway. This kinase has been shown to directly phosphorylate and activate IkappaB kinases, and thus plays a role in NF-kappa B signaling pathway. This kinase has also been found to bind and activate protein kinase C-related kinase 2, which suggests its involvement in a regulated signaling process.[3]

Interactions

MAP3K2 has been shown to interact with:

References

  1. ↑ Blank JL, Gerwins P, Elliott EM, Sather S, Johnson GL (Mar 1996). "Molecular cloning of mitogen-activated protein/ERK kinase kinases (MEKK) 2 and 3. Regulation of sequential phosphorylation pathways involving mitogen-activated protein kinase and c-Jun kinase". The Journal of Biological Chemistry. 271 (10): 5361–8. doi:10.1074/jbc.271.10.5361. PMID 8621389.
  2. ↑ Zhao Q, Lee FS (Mar 1999). "Mitogen-activated protein kinase/ERK kinase kinases 2 and 3 activate nuclear factor-kappaB through IkappaB kinase-alpha and IkappaB kinase-beta". The Journal of Biological Chemistry. 274 (13): 8355–8. doi:10.1074/jbc.274.13.8355. PMID 10085062.
  3. ↑ 3.0 3.1 "Entrez Gene: MAP3K2 mitogen-activated protein kinase kinase kinase 2".
  4. ↑ 4.0 4.1 Sun W, Kesavan K, Schaefer BC, Garrington TP, Ware M, Johnson NL, Gelfand EW, Johnson GL (Feb 2001). "MEKK2 associates with the adapter protein Lad/RIBP and regulates the MEK5-BMK1/ERK5 pathway". The Journal of Biological Chemistry. 276 (7): 5093–100. doi:10.1074/jbc.M003719200. PMID 11073940.
  5. ↑ 5.0 5.1 Cheng J, Yang J, Xia Y, Karin M, Su B (Apr 2000). "Synergistic interaction of MEK kinase 2, c-Jun N-terminal kinase (JNK) kinase 2, and JNK1 results in efficient and specific JNK1 activation". Molecular and Cellular Biology. 20 (7): 2334–42. doi:10.1128/mcb.20.7.2334-2342.2000. PMC 85399. PMID 10713157.
  6. ↑ Winsauer G, Resch U, Hofer-Warbinek R, Schichl YM, de Martin R (Nov 2008). "XIAP regulates bi-phasic NF-kappaB induction involving physical interaction and ubiquitination of MEKK2". Cellular Signalling. 20 (11): 2107–12. doi:10.1016/j.cellsig.2008.08.004. PMID 18761086.

Further reading

Retrieved from "https://www.wikidoc.org/index.php?title=MAP3K2&oldid=1412258"