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MAPK7 (mitogen-activated protein kinase 7)

Written2010-02Francisco de Asís Iñesta-Vaquera, Ana Cuenda
Centro Nacional de Biotecnologia-CSIC, Department of Immunology, Oncology, Madrid, Spain

(Note : for Links provided by Atlas : click)

Identity

Alias_namesPRKM7
Alias_symbol (synonym)BMK1
ERK5
Other aliasERK4
HGNC (Hugo) MAPK7
LocusID (NCBI) 5598
Atlas_Id 41294
Location 17p11.2  [Link to chromosome band 17p11]
Location_base_pair Starts at 19378461 and ends at 19383544 bp from pter ( according to hg19-Feb_2009)  [Mapping MAPK7.png]
 
  MAPK7 genomic context (Chromosome 17; location 17p11.2).
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
MAPK7 (17p11.2) / RHOU (1q42.13)MAPK7 (17p11.2) / RNF112 (17p11.2)

DNA/RNA

 
  Genomic organization of MAPK7 gene on chromosome 17p11.2. The boxes indicate coding regions (exons 1-6) of the gene.
Description The MAPK7 entire gene spans 5,82 kb on the short arm of chromosome 17. It contains 6 exons.
Transcription The human MAPK7 gene encodes an 816 amino-acids protein of about 98 kDa. MAPK7 mRNA is 2445 bp. There are 11 transcripts, seven of which are protein coding. In mice, three splice variants (MAPK7a, b and c) have been reported. Mouse splice variants are generated by alternative splicing across introns 1 and/or 2 (Yan et al., 2001).
Pseudogene No human or mouse pseudogene known.

Protein

Note ERK5, also known as MAPK7 or "Big MAP-Kinase 1" (BMK1) belongs to the Mitogen Activated Protein Kinase (MAPK) family, and therefore to the CGMC kinases in the human kinome (Manning et al., 2002). ERK5, at 98 kDa, is twice the size of other MAPKs and hence the largest kinase within its group. It possesses a catalytic N-terminal domain, which share 50% homology with ERK1 (MAPK3) and ERK2 (MAPK1) and a unique C-terminal tail of about 400 amino-acids long. In vivo, ERK5 is activated to the same extent by environmental stresses, such as oxidative and osmotic shock, and by growth factors. In addition, ERK5 may be activated by the cytokine Interleukin-6 in B cells.
 
  Schematic representation of the human ERK5 (MAPK7) protein domains. NES1 and NES2, bipartite nuclear exportation signal; PB1-BD, PB1 (Phox and Bem domain 1) binding domain; Kinase Domain, catalytic kinase domain; TEY, sequence motif containing ERK5 regulatory phosphorylation residues; PR-1 and PR-2, proline rich domains; Transcriptional trans-activation, transcriptional activity domain.
Description Human ERK5 (MAPK7) is a Ser/Thr protein kinase of 816 amino-acids with a predicted mass of 98 kDa. The ERK5 N-terminus domain resembles the typical MAPK catalytic domain and includes the MAPK-conserved TXY activation sequence (T218EY220) in the activation loop. The activation of ERK5 occurs via interaction with and dual phosphorylation in its TEY motif by MKK5 (Mody et al., 2003). MKK5 mediated ERK5 activation leads to ERK5 autophosphorylation in its unique C-terminal domain (Morimoto et al., 2007).
Expression ERK5 (MAPK7) mRNA is widely expressed throughout all tissues.
Localisation Both in tissues and in cultured cells, ERK5 (MAPK7) localizes to the cytoplasm of cells and/or to the nucleus. As shown in the above diagram, ERK5 molecule contains a bipartite nuclear exportation signal. In resting cells, the N- and C-terminal halves of ERK5 interact producing a nuclear export signal (NES) that retains ERK5 in the cytoplasm of the cells. Upon stimulation, the interaction between the N- and the C-terminal halves is disrupted, and therefore ERK5 enters the nucleus (Kondoh et al., 2006).
Function Genetic studies have shown that ERK5 (MAPK7) is essential for cardiovascular development and neuronal differentiation. ERK5 knock-out mice die at midgestation due to developmental failures in structures as placenta, heart and vascular system (Regan et al., 2002; Sohn et al., 2002; Yan et al., 2003; Hayashi et al., 2004; Wang et al., 2005). ERK5 also regulates cell survival in a variety of tissues. At nervous system, ERK5 acts as a neuroprotector from neurotrophic factor withdrawal and toxic insults (Cavanaugh, 2004). Also, ERK5 is required to mediate the survival response of neurons to nerve growth factor (Finegan et al., 2009). In the immune system, the ERK5 pathway regulates apoptosis of developing thymocytes (Sohn et al., 2008) and protects B cells from proapoptotic stimuli (Carvajal-Vergara et al., 2005). ERK5 is also required for cell cycle progression. It regulates cyclin D1 expression (Mulloy et al., 2003) and is necessary for EGF-induced cell proliferation and progression through the cell cycle (Kato et al., 1998). Moreover, it has been suggested that the ERK5-NFKappaB pathway may be required for a timely mitotic entry (Cude et al., 2007). Additionally, ERK5, along with other MAPK pathways can play an indirect role in cytoskeleton rearrangement (Barros and Marshall, 2005), in promoting SRC-induced podosome formation (Schramp et al., 2008), and in cell attachment to the extracellular matrix and in endothelial cell migration (Spiering et al., 2009; Sawhney et al., 2009).
ERK5 (MAPK7) is a protein with kinase activity (in its N-terminal region) and also transcriptional activation activity (in the C-terminal half). Downstream targets of ERK5 include the transcription factors MEF2A, MEF2C and MEF2D, SAP1a, c-Myc and CREB. For example, ERK5 phosphorylates SAP1, which enhances its transcriptional activity promoting c-FOS expression (Terasawa et al., 2003), and activates the serum- and glucocorticoid-inducible kinase1 (SGK1) by phosphorylating Ser78 in response to growth factors (Hayashi et al., 2001). In cardiac tissue, ERK5 may couple cells electrically and metabolically by phosphorylating the gap-junction protein Cx43 at a key residue for gap junction communication (Cameron et al., 2003). Also, phosphorylated ERK5 regulates gene expression through its C-terminal transcriptional activation domain (Morimoto et al., 2007).
Homology ERK5 (MAPK7) N-terminal half shares a 50% sequence identity with ERK1/2. The homology of the C-terminal part of ERK5 with other protein has not been reported. ERK5 possesses ortholog in the majority of mammals (sharing 80-98% homology). In C. elegans, the SMA-5 protein is a 60% similar to human ERK5 (Watanabe et al., 2005). In Saccharomyces cerevisiae, Slt2p (Mpk1p) is an ERK5 ortholog (Truman et al., 2006).

Mutations

Note Not identified.

Implicated in

Note
  
Entity Breast cancer
Note ERK5 (MAPK7) expression and activity is increased in breast cancer tumours. ERK5 overexpression has been established as an independent predictor of disease-free survival in breast cancer (Montero et al., 2009). In cell models, ERK5 has been linked to the regulation of breast cancer cells proliferation (Esparís-Ogando et al., 2002).
  
  
Entity Prostatic cancer
Note ERK5 (MAPK7) immunoreactivity is significantly up-regulated in high-grade prostate cancer. Increased ERK5 cytoplasmic signals correlated with metastases and locally advanced disease at diagnosis. Strong nuclear ERK5 localization in prostatic tumours correlates with poor disease-specific survival (McCracken et al., 2008).
  
  
Entity Hepatic carcinoma
Note An increase in ERK5 (MAPK7) copy number was detected in primary HCC tumours. It has been suggested that MAPK7 is likely the target of 17p11 amplification and that the ERK5 protein promotes the growth of hepatic carcinoma cells by regulating mitotic entry (Zen et al., 2009).
  

Bibliography

Activation of either ERK1/2 or ERK5 MAP kinase pathways can lead to disruption of the actin cytoskeleton.
Barros JC, Marshall CJ.
J Cell Sci. 2005 Apr 15;118(Pt 8):1663-71. Epub 2005 Mar 29.
PMID 15797923
 
Regulation of epidermal growth factor-induced connexin 43 gap junction communication by big mitogen-activated protein kinase1/ERK5 but not ERK1/2 kinase activation.
Cameron SJ, Malik S, Akaike M, Lerner-Marmarosh N, Yan C, Lee JD, Abe J, Yang J.
J Biol Chem. 2003 May 16;278(20):18682-8. Epub 2003 Mar 12.
PMID 12637502
 
Multifunctional role of Erk5 in multiple myeloma.
Carvajal-Vergara X, Tabera S, Montero JC, Esparis-Ogando A, Lopez-Perez R, Mateo G, Gutierrez N, Parmo-Cabanas M, Teixido J, San Miguel JF, Pandiella A.
Blood. 2005 Jun 1;105(11):4492-9. Epub 2005 Feb 3.
PMID 15692064
 
Role of extracellular signal regulated kinase 5 in neuronal survival.
Cavanaugh JE.
Eur J Biochem. 2004 Jun;271(11):2056-9. (REVIEW)
PMID 15153094
 
Regulation of the G2-M cell cycle progression by the ERK5-NFkappaB signaling pathway.
Cude K, Wang Y, Choi HJ, Hsuan SL, Zhang H, Wang CY, Xia Z.
J Cell Biol. 2007 Apr 23;177(2):253-64.
PMID 17452529
 
Erk5 participates in neuregulin signal transduction and is constitutively active in breast cancer cells overexpressing ErbB2.
Esparis-Ogando A, Diaz-Rodriguez E, Montero JC, Yuste L, Crespo P, Pandiella A.
Mol Cell Biol. 2002 Jan;22(1):270-85.
PMID 11739740
 
Regulation of neuronal survival by the extracellular signal-regulated protein kinase 5.
Finegan KG, Wang X, Lee EJ, Robinson AC, Tournier C.
Cell Death Differ. 2009 May;16(5):674-83. Epub 2009 Jan 16.
PMID 19148185
 
Targeted deletion of BMK1/ERK5 in adult mice perturbs vascular integrity and leads to endothelial failure.
Hayashi M, Kim SW, Imanaka-Yoshida K, Yoshida T, Abel ED, Eliceiri B, Yang Y, Ulevitch RJ, Lee JD.
J Clin Invest. 2004 Apr;113(8):1138-48.
PMID 15085193
 
BMK1 mediates growth factor-induced cell proliferation through direct cellular activation of serum and glucocorticoid-inducible kinase.
Hayashi M, Tapping RI, Chao TH, Lo JF, King CC, Yang Y, Lee JD.
J Biol Chem. 2001 Mar 23;276(12):8631-4. Epub 2001 Jan 31.
PMID 11254654
 
Bmk1/Erk5 is required for cell proliferation induced by epidermal growth factor.
Kato Y, Tapping RI, Huang S, Watson MH, Ulevitch RJ, Lee JD.
Nature. 1998 Oct 15;395(6703):713-6.
PMID 9790194
 
Regulation of nuclear translocation of extracellular signal-regulated kinase 5 by active nuclear import and export mechanisms.
Kondoh K, Terasawa K, Morimoto H, Nishida E.
Mol Cell Biol. 2006 Mar;26(5):1679-90.
PMID 16478989
 
The protein kinase complement of the human genome.
Manning G, Whyte DB, Martinez R, Hunter T, Sudarsanam S.
Science. 2002 Dec 6;298(5600):1912-34. (REVIEW)
PMID 12471243
 
Aberrant expression of extracellular signal-regulated kinase 5 in human prostate cancer.
McCracken SR, Ramsay A, Heer R, Mathers ME, Jenkins BL, Edwards J, Robson CN, Marquez R, Cohen P, Leung HY.
Oncogene. 2008 May 8;27(21):2978-88. Epub 2007 Dec 10.
PMID 18071319
 
An analysis of the phosphorylation and activation of extracellular-signal-regulated protein kinase 5 (ERK5) by mitogen-activated protein kinase kinase 5 (MKK5) in vitro.
Mody N, Campbell DG, Morrice N, Peggie M, Cohen P.
Biochem J. 2003 Jun 1;372(Pt 2):567-75.
PMID 12628002
 
Expression of Erk5 in early stage breast cancer and association with disease free survival identifies this kinase as a potential therapeutic target.
Montero JC, Ocana A, Abad M, Ortiz-Ruiz MJ, Pandiella A, Esparis-Ogando A.
PLoS One. 2009;4(5):e5565. Epub 2009 May 15.
PMID 19440538
 
Activation of a C-terminal transcriptional activation domain of ERK5 by autophosphorylation.
Morimoto H, Kondoh K, Nishimoto S, Terasawa K, Nishida E.
J Biol Chem. 2007 Dec 7;282(49):35449-56. Epub 2007 Oct 10.
PMID 17928297
 
Activation of cyclin D1 expression by the ERK5 cascade.
Mulloy R, Salinas S, Philips A, Hipskind RA.
Oncogene. 2003 Aug 21;22(35):5387-98.
PMID 12934098
 
Erk5 null mice display multiple extraembryonic vascular and embryonic cardiovascular defects.
Regan CP, Li W, Boucher DM, Spatz S, Su MS, Kuida K.
Proc Natl Acad Sci U S A. 2002 Jul 9;99(14):9248-53. Epub 2002 Jul 1.
PMID 12093914
 
A novel role of ERK5 in integrin-mediated cell adhesion and motility in cancer cells via Fak signaling.
Sawhney RS, Liu W, Brattain MG.
J Cell Physiol. 2009 Apr;219(1):152-61.
PMID 19089993
 
ERK5 promotes Src-induced podosome formation by limiting Rho activation.
Schramp M, Ying O, Kim TY, Martin GS.
J Cell Biol. 2008 Jun 30;181(7):1195-210. Epub 2008 Jun 23.
PMID 18573916
 
Non-redundant function of the MEK5-ERK5 pathway in thymocyte apoptosis.
Sohn SJ, Lewis GM, Winoto A.
EMBO J. 2008 Jul 9;27(13):1896-906. Epub 2008 Jun 12.
PMID 18548009
 
ERK5 MAPK regulates embryonic angiogenesis and acts as a hypoxia-sensitive repressor of vascular endothelial growth factor expression.
Sohn SJ, Sarvis BK, Cado D, Winoto A.
J Biol Chem. 2002 Nov 8;277(45):43344-51. Epub 2002 Sep 6.
PMID 12221099
 
MEK5/ERK5 signaling modulates endothelial cell migration and focal contact turnover.
Spiering D, Schmolke M, Ohnesorge N, Schmidt M, Goebeler M, Wegener J, Wixler V, Ludwig S.
J Biol Chem. 2009 Sep 11;284(37):24972-80. Epub 2009 Jul 15.
PMID 19605361
 
Regulation of c-Fos and Fra-1 by the MEK5-ERK5 pathway.
Terasawa K, Okazaki K, Nishida E.
Genes Cells. 2003 Mar;8(3):263-73.
PMID 12622723
 
Expressed in the yeast Saccharomyces cerevisiae, human ERK5 is a client of the Hsp90 chaperone that complements loss of the Slt2p (Mpk1p) cell integrity stress-activated protein kinase.
Truman AW, Millson SH, Nuttall JM, King V, Mollapour M, Prodromou C, Pearl LH, Piper PW.
Eukaryot Cell. 2006 Nov;5(11):1914-24. Epub 2006 Sep 1.
PMID 16950928
 
Targeted deletion of mek5 causes early embryonic death and defects in the extracellular signal-regulated kinase 5/myocyte enhancer factor 2 cell survival pathway.
Wang X, Merritt AJ, Seyfried J, Guo C, Papadakis ES, Finegan KG, Kayahara M, Dixon J, Boot-Handford RP, Cartwright EJ, Mayer U, Tournier C.
Mol Cell Biol. 2005 Jan;25(1):336-45.
PMID 15601854
 
Control of body size by SMA-5, a homolog of MAP kinase BMK1/ERK5, in C. elegans.
Watanabe N, Nagamatsu Y, Gengyo-Ando K, Mitani S, Ohshima Y.
Development. 2005 Jul;132(14):3175-84. Epub 2005 Jun 8.
PMID 15944183
 
Molecular cloning of mouse ERK5/BMK1 splice variants and characterization of ERK5 functional domains.
Yan C, Luo H, Lee JD, Abe J, Berk BC.
J Biol Chem. 2001 Apr 6;276(14):10870-8. Epub 2001 Jan 3.
PMID 11139578
 
Knockout of ERK5 causes multiple defects in placental and embryonic development.
Yan L, Carr J, Ashby PR, Murry-Tait V, Thompson C, Arthur JS.
BMC Dev Biol. 2003 Dec 16;3:11.
PMID 14675480
 
ERK5 is a target for gene amplification at 17p11 and promotes cell growth in hepatocellular carcinoma by regulating mitotic entry.
Zen K, Yasui K, Nakajima T, Zen Y, Zen K, Gen Y, Mitsuyoshi H, Minami M, Mitsufuji S, Tanaka S, Itoh Y, Nakanuma Y, Taniwaki M, Arii S, Okanoue T, Yoshikawa T.
Genes Chromosomes Cancer. 2009 Feb;48(2):109-20.
PMID 18973138
 

Citation

This paper should be referenced as such :
Iesta-Vaquera, FdA ; Cuenda, A
MAPK7 (mitogen-activated protein kinase 7)
Atlas Genet Cytogenet Oncol Haematol. 2010;14(12):1111-1114.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/MAPK7ID41294ch17p11.html


External links

Nomenclature
HGNC (Hugo)MAPK7   6880
Cards
AtlasMAPK7ID41294ch17p11
Entrez_Gene (NCBI)MAPK7  5598  mitogen-activated protein kinase 7
AliasesBMK1; ERK4; ERK5; PRKM7
GeneCards (Weizmann)MAPK7
Ensembl hg19 (Hinxton)ENSG00000166484 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000166484 [Gene_View]  chr17:19378461-19383544 [Contig_View]  MAPK7 [Vega]
ICGC DataPortalENSG00000166484
TCGA cBioPortalMAPK7
AceView (NCBI)MAPK7
Genatlas (Paris)MAPK7
WikiGenes5598
SOURCE (Princeton)MAPK7
Genetics Home Reference (NIH)MAPK7
Genomic and cartography
GoldenPath hg38 (UCSC)MAPK7  -     chr17:19378461-19383544 +  17p11.2   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)MAPK7  -     17p11.2   [Description]    (hg19-Feb_2009)
EnsemblMAPK7 - 17p11.2 [CytoView hg19]  MAPK7 - 17p11.2 [CytoView hg38]
Mapping of homologs : NCBIMAPK7 [Mapview hg19]  MAPK7 [Mapview hg38]
OMIM602521   
Gene and transcription
Genbank (Entrez)AB209611 AK295376 AY534741 BC007404 BC007992
RefSeq transcript (Entrez)NM_002749 NM_139032 NM_139033 NM_139034
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)MAPK7
Cluster EST : UnigeneHs.150136 [ NCBI ]
CGAP (NCI)Hs.150136
Alternative Splicing GalleryENSG00000166484
Gene ExpressionMAPK7 [ NCBI-GEO ]   MAPK7 [ EBI - ARRAY_EXPRESS ]   MAPK7 [ SEEK ]   MAPK7 [ MEM ]
Gene Expression Viewer (FireBrowse)MAPK7 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevestigatorExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)5598
GTEX Portal (Tissue expression)MAPK7
Human Protein AtlasENSG00000166484-MAPK7 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ13164   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ13164  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ13164
Splice isoforms : SwissVarQ13164
Catalytic activity : Enzyme2.7.11.24 [ Enzyme-Expasy ]   2.7.11.242.7.11.24 [ IntEnz-EBI ]   2.7.11.24 [ BRENDA ]   2.7.11.24 [ KEGG ]   
PhosPhoSitePlusQ13164
Domaine pattern : Prosite (Expaxy)MAPK (PS01351)    PROTEIN_KINASE_ATP (PS00107)    PROTEIN_KINASE_DOM (PS50011)    PROTEIN_KINASE_ST (PS00108)   
Domains : Interpro (EBI)Kinase-like_dom    MAP_kinase_CS    Prot_kinase_dom    Protein_kinase_ATP_BS    Ser/Thr_kinase_AS   
Domain families : Pfam (Sanger)Pkinase (PF00069)   
Domain families : Pfam (NCBI)pfam00069   
Domain families : Smart (EMBL)S_TKc (SM00220)  
Conserved Domain (NCBI)MAPK7
DMDM Disease mutations5598
Blocks (Seattle)MAPK7
PDB (SRS)2Q8Y    4B99    4IC7    4IC8    4ZSG    4ZSJ    4ZSL    5BYY    5BYZ   
PDB (PDBSum)2Q8Y    4B99    4IC7    4IC8    4ZSG    4ZSJ    4ZSL    5BYY    5BYZ   
PDB (IMB)2Q8Y    4B99    4IC7    4IC8    4ZSG    4ZSJ    4ZSL    5BYY    5BYZ   
PDB (RSDB)2Q8Y    4B99    4IC7    4IC8    4ZSG    4ZSJ    4ZSL    5BYY    5BYZ   
Structural Biology KnowledgeBase2Q8Y    4B99    4IC7    4IC8    4ZSG    4ZSJ    4ZSL    5BYY    5BYZ   
SCOP (Structural Classification of Proteins)2Q8Y    4B99    4IC7    4IC8    4ZSG    4ZSJ    4ZSL    5BYY    5BYZ   
CATH (Classification of proteins structures)2Q8Y    4B99    4IC7    4IC8    4ZSG    4ZSJ    4ZSL    5BYY    5BYZ   
SuperfamilyQ13164
Human Protein Atlas [tissue]ENSG00000166484-MAPK7 [tissue]
Peptide AtlasQ13164
HPRD03952
IPIIPI00219601   IPI00149048   IPI00426283   IPI00555640   IPI00910923   IPI00376860   
Protein Interaction databases
DIP (DOE-UCLA)Q13164
IntAct (EBI)Q13164
FunCoupENSG00000166484
BioGRIDMAPK7
STRING (EMBL)MAPK7
ZODIACMAPK7
Ontologies - Pathways
QuickGOQ13164
Ontology : AmiGOMAPK cascade  protein serine/threonine kinase activity  MAP kinase activity  protein binding  ATP binding  nucleus  nucleoplasm  nucleoplasm  cytoplasm  cytosol  cytosol  cell cycle  signal transduction  axon guidance  PML body  peptidyl-serine phosphorylation  cAMP-mediated signaling  negative regulation of cAMP catabolic process  negative regulation of heterotypic cell-cell adhesion  positive regulation of transcription from RNA polymerase II promoter in response to stress  negative regulation of MAP kinase activity  regulation of angiogenesis  positive regulation of transcription from RNA polymerase II promoter  negative regulation of inflammatory response  mitogen-activated protein kinase binding  positive regulation of protein metabolic process  negative regulation of cyclic-nucleotide phosphodiesterase activity  negative regulation of NFAT protein import into nucleus  negative regulation of response to cytokine stimulus  cellular response to hydrogen peroxide  negative regulation of ERK5 cascade  cellular response to growth factor stimulus  cellular response to laminar fluid shear stress  cellular response to laminar fluid shear stress  cellular response to transforming growth factor beta stimulus  negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway  negative regulation of endothelial cell apoptotic process  negative regulation of extrinsic apoptotic signaling pathway in absence of ligand  
Ontology : EGO-EBIMAPK cascade  protein serine/threonine kinase activity  MAP kinase activity  protein binding  ATP binding  nucleus  nucleoplasm  nucleoplasm  cytoplasm  cytosol  cytosol  cell cycle  signal transduction  axon guidance  PML body  peptidyl-serine phosphorylation  cAMP-mediated signaling  negative regulation of cAMP catabolic process  negative regulation of heterotypic cell-cell adhesion  positive regulation of transcription from RNA polymerase II promoter in response to stress  negative regulation of MAP kinase activity  regulation of angiogenesis  positive regulation of transcription from RNA polymerase II promoter  negative regulation of inflammatory response  mitogen-activated protein kinase binding  positive regulation of protein metabolic process  negative regulation of cyclic-nucleotide phosphodiesterase activity  negative regulation of NFAT protein import into nucleus  negative regulation of response to cytokine stimulus  cellular response to hydrogen peroxide  negative regulation of ERK5 cascade  cellular response to growth factor stimulus  cellular response to laminar fluid shear stress  cellular response to laminar fluid shear stress  cellular response to transforming growth factor beta stimulus  negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway  negative regulation of endothelial cell apoptotic process  negative regulation of extrinsic apoptotic signaling pathway in absence of ligand  
Pathways : BIOCARTARole of Erk5 in Neuronal Survival [Genes]    Control of skeletal myogenesis by HDAC & calcium/calmodulin-dependent kinase (CaMK) [Genes]    MAPKinase Signaling Pathway [Genes]   
Pathways : KEGGMAPK signaling pathway    Gap junction    Neurotrophin signaling pathway    GnRH signaling pathway    MicroRNAs in cancer   
REACTOMEQ13164 [protein]
REACTOME PathwaysR-HSA-8853659 [pathway]   
NDEx NetworkMAPK7
Atlas of Cancer Signalling NetworkMAPK7
Wikipedia pathwaysMAPK7
Orthology - Evolution
OrthoDB5598
GeneTree (enSembl)ENSG00000166484
Phylogenetic Trees/Animal Genes : TreeFamMAPK7
HOVERGENQ13164
HOGENOMQ13164
Homologs : HomoloGeneMAPK7
Homology/Alignments : Family Browser (UCSC)MAPK7
Gene fusions - Rearrangements
Tumor Fusion PortalMAPK7
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerMAPK7 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)MAPK7
dbVarMAPK7
ClinVarMAPK7
1000_GenomesMAPK7 
Exome Variant ServerMAPK7
ExAC (Exome Aggregation Consortium)ENSG00000166484
GNOMAD BrowserENSG00000166484
Genetic variants : HAPMAP5598
Genomic Variants (DGV)MAPK7 [DGVbeta]
DECIPHERMAPK7 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisMAPK7 
Mutations
ICGC Data PortalMAPK7 
TCGA Data PortalMAPK7 
Broad Tumor PortalMAPK7
OASIS PortalMAPK7 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICMAPK7  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDMAPK7
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch MAPK7
DgiDB (Drug Gene Interaction Database)MAPK7
DoCM (Curated mutations)MAPK7 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)MAPK7 (select a term)
intoGenMAPK7
NCG5 (London)MAPK7
Cancer3DMAPK7(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM602521   
Orphanet
DisGeNETMAPK7
MedgenMAPK7
Genetic Testing Registry MAPK7
NextProtQ13164 [Medical]
TSGene5598
GENETestsMAPK7
Target ValidationMAPK7
Huge Navigator MAPK7 [HugePedia]
snp3D : Map Gene to Disease5598
BioCentury BCIQMAPK7
ClinGenMAPK7
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD5598
Chemical/Pharm GKB GenePA30625
Clinical trialMAPK7
Miscellaneous
canSAR (ICR)MAPK7 (select the gene name)
Probes
Litterature
PubMed155 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineMAPK7
EVEXMAPK7
GoPubMedMAPK7
iHOPMAPK7
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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