MAPK13

Protein-coding gene in the species Homo sapiens
MAPK13
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

3COI, 4EYJ, 4EYM, 4MYG, 4YNO, 5EKO, 5EKN

Identifiers
AliasesMAPK13, MAPK 13, MAPK-13, PRKM13, SAPK4, p38delta, mitogen-activated protein kinase 13
External IDsOMIM: 602899 MGI: 1346864 HomoloGene: 48133 GeneCards: MAPK13
Gene location (Human)
Chromosome 6 (human)
Chr.Chromosome 6 (human)[1]
Chromosome 6 (human)
Genomic location for MAPK13
Genomic location for MAPK13
Band6p21.31Start36,127,809 bp[1]
End36,144,524 bp[1]
Gene location (Mouse)
Chromosome 17 (mouse)
Chr.Chromosome 17 (mouse)[2]
Chromosome 17 (mouse)
Genomic location for MAPK13
Genomic location for MAPK13
Band17|17 A3.3Start28,988,271 bp[2]
End28,999,207 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • gums

  • right adrenal gland

  • left adrenal gland

  • human penis

  • parotid gland

  • vulva

  • sperm

  • duodenum

  • oral cavity

  • skin of abdomen
Top expressed in
  • lip

  • crypt of lieberkuhn of small intestine

  • epithelium of stomach

  • duodenum

  • large intestine

  • ileum

  • colon

  • intestinal villus

  • jejunum

  • left colon
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • transferase activity
  • nucleotide binding
  • protein kinase activity
  • MAP kinase activity
  • kinase activity
  • protein serine/threonine kinase activity
  • protein binding
  • ATP binding
Cellular component
  • cytosol
  • nucleus
  • cytoplasm
Biological process
  • positive regulation of inflammatory response
  • regulation of transcription, DNA-templated
  • phosphorylation
  • transcription, DNA-templated
  • response to osmotic stress
  • protein phosphorylation
  • peptidyl-serine phosphorylation
  • positive regulation of interleukin-6 production
  • cell cycle
  • regulation of gene expression
  • cellular response to UV
  • stress-activated MAPK cascade
  • cellular response to hydrogen peroxide
  • cellular response to interleukin-1
  • cellular response to sorbitol
  • cellular response to anisomycin
  • cellular response to sodium arsenite
  • MAPK cascade
  • intracellular signal transduction
  • cellular response to organic substance
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5603

26415

Ensembl

ENSG00000156711

ENSMUSG00000004864

UniProt

O15264

Q9Z1B7

RefSeq (mRNA)

NM_002754

NM_011950

RefSeq (protein)

NP_002745

NP_036080

Location (UCSC)Chr 6: 36.13 – 36.14 MbChr 17: 28.99 – 29 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Mitogen-activated protein kinase 13 (MAPK 13), also known as stress-activated protein kinase 4 (SAPK4), is an enzyme that in humans is encoded by the MAPK13 gene.[5]

Function

The protein encoded by this gene is a member of the MAP kinase family. MAP kinases act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. This kinase is closely related to p38 MAP kinase, both of which can be activated by proinflammatory cytokines and cellular stress. MAP kinase kinases 3, and 6 can phosphorylate and activate this kinase. Transcription factor ATF2, and microtubule dynamics regulator stathmin have been shown to be the substrates of this kinase.[5]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000156711 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000004864 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b "Entrez Gene: mitogen-activated protein kinase 13".

Further reading

  • Efimova T, Broome AM, Eckert RL (2004). "Protein kinase Cdelta regulates keratinocyte death and survival by regulating activity and subcellular localization of a p38delta-extracellular signal-regulated kinase 1/2 complex". Mol. Cell. Biol. 24 (18): 8167–83. doi:10.1128/MCB.24.18.8167-8183.2004. PMC 515052. PMID 15340077.
  • Joneson T, Bar-Sagi D (1997). "Ras effectors and their role in mitogenesis and oncogenesis". J. Mol. Med. 75 (8): 587–93. doi:10.1007/s001090050143. PMID 9297626. S2CID 23541383.
  • Efimova T (2010). "p38delta mitogen-activated protein kinase regulates skin homeostasis and tumorigenesis". Cell Cycle. 9 (3): 498–05. doi:10.4161/cc.9.3.10541. PMID 20090411.
  • Gutierrez-Sanmartin D, Varela-Ledo E, Aguilera A, et al. (2008). "Implication of p38 mitogen-activated protein kinase isoforms (alpha, beta, gamma and delta) in CD4+ T-cell infection with human immunodeficiency virus type I." J. Gen. Virol. 89 (Pt 7): 1661–71. doi:10.1099/vir.0.82971-0. PMID 18559936.
  • Zhang J, Harrison JS, Studzinski GP (2011). "Isoforms of p38MAPK gamma and delta contribute to differentiation of human AML cells induced by 1,25-dihydroxyvitamin D₃". Exp. Cell Res. 317 (1): 117–30. doi:10.1016/j.yexcr.2010.08.010. PMC 2998239. PMID 20804750.
  • Segat L, Brandão LA, Guimarães RL, et al. (2010). "Polymorphisms in innate immunity genes and patients response to dendritic cell-based HIV immuno-treatment". Vaccine. 28 (10): 2201–6. doi:10.1016/j.vaccine.2009.12.056. PMID 20056178.
  • Zhou X, Ferraris JD, Dmitrieva NI, et al. (2008). "MKP-1 inhibits high NaCl-induced activation of p38 but does not inhibit the activation of TonEBP/OREBP: opposite roles of p38alpha and p38delta". Proc. Natl. Acad. Sci. U.S.A. 105 (14): 5620–5. Bibcode:2008PNAS..105.5620Z. doi:10.1073/pnas.0801453105. PMC 2291081. PMID 18367666.
  • Coulthard LR, Taylor JC, Eyre S, et al. (2011). "Genetic variants within the MAP kinase signalling network and anti-TNF treatment response in rheumatoid arthritis patients". Ann. Rheum. Dis. 70 (1): 98–103. doi:10.1136/ard.2010.133249. PMID 20805296. S2CID 37511360.
  • Efimova T, Broome AM, Eckert RL (2003). "A regulatory role for p38 delta MAPK in keratinocyte differentiation. Evidence for p38 delta-ERK1/2 complex formation". J. Biol. Chem. 278 (36): 34277–85. doi:10.1074/jbc.M302759200. PMID 12810719.
  • Kim SJ, Zhang Z, Hitomi E, et al. (2006). "Endoplasmic reticulum stress-induced caspase-4 activation mediates apoptosis and neurodegeneration in INCL". Hum. Mol. Genet. 15 (11): 1826–34. doi:10.1093/hmg/ddl105. PMID 16644870.
  • Talmud PJ, Drenos F, Shah S, et al. (2009). "Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip". Am. J. Hum. Genet. 85 (5): 628–42. doi:10.1016/j.ajhg.2009.10.014. PMC 2775832. PMID 19913121.
  • Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature. 425 (6960): 805–11. Bibcode:2003Natur.425..805M. doi:10.1038/nature02055. PMID 14574404.
  • Colland F, Jacq X, Trouplin V, et al. (2004). "Functional proteomics mapping of a human signaling pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
  • 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): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Ozawa S, Ito S, Kato Y, et al. (2010). "Human p38 delta MAP kinase mediates UV irradiation induced up-regulation of the gene expression of chemokine BRAK/CXCL14". Biochem. Biophys. Res. Commun. 396 (4): 1060–4. doi:10.1016/j.bbrc.2010.05.072. PMID 20478268.
  • Kitatani K, Sheldon K, Anelli V, et al. (2009). "Acid beta-glucosidase 1 counteracts p38delta-dependent induction of interleukin-6: possible role for ceramide as an anti-inflammatory lipid". J. Biol. Chem. 284 (19): 12979–88. doi:10.1074/jbc.M809500200. PMC 2676030. PMID 19279008.
  • Tan FL, Ooi A, Huang D, et al. (2010). "p38delta/MAPK13 as a diagnostic marker for cholangiocarcinoma and its involvement in cell motility and invasion". Int. J. Cancer. 126 (10): 2353–61. doi:10.1002/ijc.24944. PMID 19816939. S2CID 34276751.
  • Sofroniew MV, Howe CL, Mobley WC (2001). "Nerve growth factor signaling, neuroprotection, and neural repair". Annu. Rev. Neurosci. 24: 1217–81. doi:10.1146/annurev.neuro.24.1.1217. PMID 11520933.
  • Bailey SD, Xie C, Do R, et al. (2010). "Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study". Diabetes Care. 33 (10): 2250–3. doi:10.2337/dc10-0452. PMC 2945168. PMID 20628086.
  • Sumara G, Formentini I, Collins S, et al. (2009). "Regulation of PKD by the MAPK p38delta in insulin secretion and glucose homeostasis". Cell. 136 (2): 235–48. doi:10.1016/j.cell.2008.11.018. PMC 2638021. PMID 19135240.
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  • 3coi: Crystal structure of p38delta kinase
    3coi: Crystal structure of p38delta kinase
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Non-specific serine/threonine protein kinases (EC 2.7.11.1)
Pyruvate dehydrogenase kinase (EC 2.7.11.2)
Dephospho-(reductase kinase) kinase (EC 2.7.11.3)
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)
(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)
(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)
Myosin-heavy-chain kinase (EC 2.7.11.7)
Fas-activated serine/threonine kinase (EC 2.7.11.8)
Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)
  • -
IκB kinase (EC 2.7.11.10)
cAMP-dependent protein kinase (EC 2.7.11.11)
cGMP-dependent protein kinase (EC 2.7.11.12)
Protein kinase C (EC 2.7.11.13)
Rhodopsin kinase (EC 2.7.11.14)
Beta adrenergic receptor kinase (EC 2.7.11.15)
G-protein coupled receptor kinases (EC 2.7.11.16)
Ca2+/calmodulin-dependent (EC 2.7.11.17)
Myosin light-chain kinase (EC 2.7.11.18)
Phosphorylase kinase (EC 2.7.11.19)
Elongation factor 2 kinase (EC 2.7.11.20)
Polo kinase (EC 2.7.11.21)
Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)
Polo kinase (EC 2.7.11.21)
Cyclin-dependent kinase (EC 2.7.11.22)
(RNA-polymerase)-subunit kinase (EC 2.7.11.23)
Mitogen-activated protein kinase (EC 2.7.11.24)
MAP3K (EC 2.7.11.25)
Tau-protein kinase (EC 2.7.11.26)
(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)
  • -
Tropomyosin kinase (EC 2.7.11.28)
  • -
Low-density-lipoprotein receptor kinase (EC 2.7.11.29)
  • -
Receptor protein serine/threonine kinase (EC 2.7.11.30)
MAP2K
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