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MAPK10 (mitogen-activated protein kinase 10)

Identity

Other namesJNK3 (C-Jun N-terminal kinase 3)
Stress-activated protein kinase 3 (SAPK3)
Hugo MAPK10
Location 4q21-q23

DNA/RNA

Description The JNK3 gene maps on chromosome 4q22.1-q23 spanning 143716bp. It contains 19 confirmed introns, 16 of which are alternative.
Transcription Through alternative splicing, 7 types of transcripts are generated which produce 7 distinct JNK3 proteins. Due to the alternative splicing, the molecular weight of JNK3 varied from 45 to 57 kD.

Protein

Description All JNK proteins contain a protein kinase domain that belong to a very extensive family of eukaryotic serine/threonine proteins kinase. A number of conserved regions have been identified in the catalytic domain of JNKs. In the N-terminal extremity of the catalytic domain there is a glycine-rich motif in the vicinity of a lysine residue, which has been shown to be involved in ATP binding. A conserved aspartic acid reside that is critical for the catalytic activity of kinase has also been identified in the central part of the catalytic domain.
Expression JNK3 is mainly expressed in nervous system, heart and testis.
Function The members of JNK family act as an integration point for multiple intracellular biochemical signals governing a wide variety of cellular processes such as proliferation, differentiation, apoptosis, migration, transcriptional regulation, and development. JNK targets specific transcription factors and thus mediates immediate-early gene expression in response to various stress signals including ultraviolet (UV) radiation, oxidative stress, protein malfolding in endoplasmic reticulum, osmotical shock, and inflammatory mediators. These transcription factors include AP-1, ATF-2, Elk-1, p53, etc... Several upstream dual specific protein kinases, such as MKK4/SEK1 and MKK7, can activate JNK through phosphorylation of the conversed Thr-Pro-Tyr motif on JNK proteins. In mammalian cells, activated JNK can phosphorylate the N-terminus of c-Jun, which contains both JNK docking site and JNK phosphorylation site (ser63 and ser73), orJunD, which lacks a JNK docking site but contains a JNK phosphorylation site. JNK is unable to phosphorylate JunB due to the lack of a JNK phosphorylation site inJunB, despite there is a functional JNK docking site. Comparison of the binding activity of JNK isoforms demonstrates that JNK2 bind c-Jun approximately 25 times more efficiently than did JNK1. Therefore, individual members of the JNK family may selectively target specific transcription factors in vivo. One of the most important functions of JNK is the regulation of apoptosis. Emerging evidence indicates that JNK activation is obligatory for apoptosis induced by both receptor-mediated ÒextrinsicÓ pathway or mitochondria-mediated ÒintrinsicÓ pathway. JNK activation may contribute to the initiation of Fas-induced apoptosis, possibly through the amplification of autocrine or paracrine Fas signaling by JNK-dependent Fas ligand (FasL) gene expression. In addition, JNK has been indicated in the apoptosis induced by Daxx, a Fas death domain (FADD) interaction protein. Through its serine/threonine kinase activity, JNK may contribute to mitochondria-mediated apoptosis by phosphorylating pro- or anti-apoptoticBcl-2 family proteins. Finally, JNK has also been indicated as an important kinase phosphorylating p53 and subsequently facilitating p53-dependent apoptotic responses. Sustained JNK activation may be responsible for the enhanced apoptosis observed in RelA-/- or Ikkb-/- mouse embryonic fibroblasts treated with TNFa. It was suggested that deficiency of RelA or IKKb caused a decreased expression of XIAP or GADD45b, which may antagonize the activation of JNK activation. However, such speculation contradicts the previous observations indicating that both GADD45b and XIAP are activators, rather than inhibitors for JNK activation. Moreover, gene profiling in our recent studies indicated no substantial difference of basal or inducible GADD45b and XIAP mRNA in wild type cells and Ikkb-/- cells.

Implicated in

Entity Obesity, insulin resistance, neurodegenerative diseases, inflammation, cancer.
Oncogenesis Loss of expression of JNK3 has been found in some brain tumors.
  

External links

Nomenclature
HugoMAPK10
GDBMAPK10
Entrez_GeneMAPK10  5602  mitogen-activated protein kinase 10
Cards
AtlasJNK3ID427
GeneCardsMAPK10
EnsemblMAPK10 [Search_View]   ENSG00000109339 [Gene_View]
GenatlasMAPK10
GeneLynxMAPK10
eGenomeMAPK10
euGene5602
Genomic and cartography
GoldenPathMAPK10  -     chr4:87156657-87500240 -  4q22.1-q23   [Description]    (hg18-Mar_2006)
EnsemblMAPK10 - 4q22.1-q23 [CytoView]
NCBIMapview
OMIMDisease map [OMIM]
HomoloGeneMAPK10
Gene and transcription
GenbankAK022161 [ ENTREZ ]
GenbankAK057723 [ ENTREZ ]
GenbankAK091104 [ ENTREZ ]
GenbankAK124791 [ ENTREZ ]
GenbankAK225974 [ ENTREZ ]
RefSeqNM_002753 [ SRS ]    NM_002753 [ ENTREZ ]
RefSeqNM_138980 [ SRS ]    NM_138980 [ ENTREZ ]
RefSeqNM_138981 [ SRS ]    NM_138981 [ ENTREZ ]
RefSeqNM_138982 [ SRS ]    NM_138982 [ ENTREZ ]
RefSeqAC_000047 [ SRS ]    AC_000047 [ ENTREZ ]
RefSeqNC_000004 [ SRS ]    NC_000004 [ ENTREZ ]
RefSeqNT_016354 [ SRS ]    NT_016354 [ ENTREZ ]
RefSeqNW_922162 [ SRS ]    NW_922162 [ ENTREZ ]
AceViewMAPK10 AceView - NCBI
UnigeneHs.125503 [ SRS ]    Hs.125503 [ NCBI ]     HS125503 [ spliceNest ]
Fast-db6970 (alternative variants)
Protein : pattern, domain, 3D structure
SwissProtP53779 [ SRS]    P53779 [ EXPASY ]     P53779 [ INTERPRO ]
PrositePS01351 MAPK [ SRS ]    PS01351 MAPK [ Expasy ]
PrositePS00107 PROTEIN_KINASE_ATP [ SRS ]    PS00107 PROTEIN_KINASE_ATP [ Expasy ]
PrositePS50011 PROTEIN_KINASE_DOM [ SRS ]    PS50011 PROTEIN_KINASE_DOM [ Expasy ]
PrositePS00108 PROTEIN_KINASE_ST [ SRS ]    PS00108 PROTEIN_KINASE_ST [ Expasy ]
InterproIPR008351 JNK_MAPK [ SRS ]    IPR008351 JNK_MAPK [ EBI ]
InterproIPR003527 MAP_kin_CS [ SRS ]    IPR003527 MAP_kin_CS [ EBI ]
InterproIPR000719 Prot_kinase_core [ SRS ]    IPR000719 Prot_kinase_core [ EBI ]
InterproIPR008271 Ser_thr_pkin_AS [ SRS ]    IPR008271 Ser_thr_pkin_AS [ EBI ]
InterproIPR002290 Ser_thr_pkinase [ SRS ]    IPR002290 Ser_thr_pkinase [ EBI ]
CluSTrP53779
PfamPF00069 Pkinase [ SRS ]    PF00069 Pkinase [ Sanger ]    pfam00069 [ NCBI-CDD ]
SmartSM00220 S_TKc [EMBL]
ProdomPD000001 Prot_kinase[INRA-Toulouse]
ProdomP53779 MK10_HUMAN [ Domain structure ]   P53779 MK10_HUMAN  [ sequences sharing at least 1 domain ]
BlocksP53779
PDB1JNK [ SRS ]    1JNK [ PdbSum ],   1JNK [ IMB ]   1JNK [ RSDB ]
PDB1PMN [ SRS ]    1PMN [ PdbSum ],   1PMN [ IMB ]   1PMN [ RSDB ]
PDB1PMQ [ SRS ]    1PMQ [ PdbSum ],   1PMQ [ IMB ]   1PMQ [ RSDB ]
PDB1PMU [ SRS ]    1PMU [ PdbSum ],   1PMU [ IMB ]   1PMU [ RSDB ]
PDB1PMV [ SRS ]    1PMV [ PdbSum ],   1PMV [ IMB ]   1PMV [ RSDB ]
PDB2B1P [ SRS ]    2B1P [ PdbSum ],   2B1P [ IMB ]   2B1P [ RSDB ]
PDB2EXC [ SRS ]    2EXC [ PdbSum ],   2EXC [ IMB ]   2EXC [ RSDB ]
PDB2O0U [ SRS ]    2O0U [ PdbSum ],   2O0U [ IMB ]   2O0U [ RSDB ]
PDB2O2U [ SRS ]    2O2U [ PdbSum ],   2O2U [ IMB ]   2O2U [ RSDB ]
PDB2OK1 [ SRS ]    2OK1 [ PdbSum ],   2OK1 [ IMB ]   2OK1 [ RSDB ]
PDB2P33 [ SRS ]    2P33 [ PdbSum ],   2P33 [ IMB ]   2P33 [ RSDB ]
PDB2R9S [ SRS ]    2R9S [ PdbSum ],   2R9S [ IMB ]   2R9S [ RSDB ]
HPRD04207
Protein Interaction databases
DIPP53779
IntActP53779
Polymorphism : SNP, mutations, diseases
OMIM602897;606369    [ map ]   
GENECLINICS602897;606369
SNPMAPK10 [dbSNP-NCBI]  
SNPNM_002753 [SNP-NCI]  
SNPNM_138980 [SNP-NCI]  
SNPNM_138981 [SNP-NCI]  
SNPNM_138982 [SNP-NCI]  
SNPMAPK10 [GeneSNPs - Utah]  MAPK10] [HGBASE - SRS]
HAPMAPMAPK10 [HAPMAP]  
COSMICMAPK10 [Somatic mutation (COSMIC-CGP-Sanger)]  
HGMDMAPK10
General knowledge
Family BrowserMAPK10 [UCSC Family Browser]
SOURCENM_002753
SOURCENM_138980
SOURCENM_138981
SOURCENM_138982
SMDHs.125503
SAGEHs.125503
Enzyme2.7.11.24 [ Enzyme-SRS ]   2.7.11.24 [ Brenda-SRS ]   2.7.11.24 [ KEGG ]   2.7.11.24 [ WIT ]
GOnucleotide binding [Amigo]  nucleotide binding
GOprotein serine/threonine kinase activity [Amigo]  protein serine/threonine kinase activity
GOJUN kinase activity [Amigo]  JUN kinase activity
GOMAP kinase activity [Amigo]  MAP kinase activity
GOMAP kinase kinase activity [Amigo]  MAP kinase kinase activity
GOATP binding [Amigo]  ATP binding
GOcytoplasm [Amigo]  cytoplasm
GOprotein amino acid phosphorylation [Amigo]  protein amino acid phosphorylation
GOsignal transduction [Amigo]  signal transduction
GOJNK cascade [Amigo]  JNK cascade
GOtransferase activity [Amigo]  transferase activity
BIOCARTAMAPKinase Signaling Pathway    [Genes]
KEGGMAPK signaling pathway
KEGGWnt signaling pathway
KEGGFocal adhesion
KEGGToll-like receptor signaling pathway
KEGGFc epsilon RI signaling pathway
KEGGInsulin signaling pathway
KEGGGnRH signaling pathway
KEGGAdipocytokine signaling pathway
KEGGType II diabetes mellitus
KEGGEpithelial cell signaling in Helicobacter pylori infection
KEGGColorectal cancer
PubGeneMAPK10
TreeFamMAPK10
CTD5602 [Comparative ToxicoGenomics Database]
Other databases
Probes
ProbeMAPK10 Related clones (RZPD - Berlin)
PubMed
PubMed50 Pubmed reference(s) in LocusLink

Bibliography

Daxx, a novel Fas-binding protein that activates JNK and apoptosis.
Yang X, Khosravi-Far R, Chang HY, Baltimore D
Cell. 1997 ; 89 (7) : 1067-1076.
PMID 9215629
 
Stress-induced Fas ligand expression in T cells is mediated through a MEK kinase 1-regulated response element in the Fas ligand promoter.
Faris M, Latinis KM, Kempiak SJ, Koretzky GA, Nel A
Molecular and cellular biology. 1998 ; 18 (9) : 5414-5424.
PMID 9710625
 
JNK targets p53 ubiquitination and degradation in nonstressed cells.
Fuchs SY, Adler V, Buschmann T, Yin Z, Wu X, Jones SN, Ronai Z
Genes & development. 1998 ; 12 (17) : 2658-2663.
PMID 9732264
 
A family of stress-inducible GADD45-like proteins mediate activation of the stress-responsive MTK1/MEKK4 MAPKKK.
Takekawa M, Saito H
Cell. 1998 ; 95 (4) : 521-530.
PMID 9827804
 
Multiple docking sites on substrate proteins form a modular system that mediates recognition by ERK MAP kinase.
Jacobs D, Glossip D, Xing H, Muslin AJ, Kornfeld K
Genes & development. 1999 ; 13 (2) : 163-175.
PMID 9925641
 
Signal transduction by the JNK group of MAP kinases.
Davis RJ
Cell. 2000 ; 103 (2) : 239-252.
PMID 11057897
 
Induction of gadd45beta by NF-kappaB downregulates pro-apoptotic JNK signalling.
De Smaele E, Zazzeroni F, Papa S, Nguyen DU, Jin R, Jones J, Cong R, Franzoso G
Nature. 2001 ; 414 (6861) : 308-313.
PMID 11713530
 
Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death.
Suzuki Y, Nakabayashi Y, Takahashi R
Proceedings of the National Academy of Sciences of the United States of America. 2001 ; 98 (15) : 8662-8667.
PMID 11447297
 
Inhibition of JNK activation through NF-kappaB target genes.
Tang G, Minemoto Y, Dibling B, Purcell NH, Li Z, Karin M, Lin A
Nature. 2001 ; 414 (6861) : 313-317.
PMID 11713531
 
The c-Jun NH2-terminal kinase3 (JNK3) gene: genomic structure, chromosomal assignment, and loss of expression in brain tumors.
Yoshida S, Fukino K, Harada H, Nagai H, Imoto I, Inazawa J, Takahashi H, Teramoto A, Emi M
Journal of human genetics. 2001 ; 46 (4) : 182-187.
PMID 11322657
 
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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Contributor(s)

Written01-2003Fei Chen

Citation

This paper should be referenced as such :
Chen F . MAPK10 (mitogen-activated protein kinase 10). Atlas Genet Cytogenet Oncol Haematol. January 2003 .
URL : http://AtlasGeneticsOncology.org/Genes/JNK3ID427.html

© Atlas of Genetics and Cytogenetics in Oncology and Haematology
indexed on : Wed Jul 2 08:24:26 2008


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