MAPK14 information

MAPK14
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1A9U, 1BL6, 1BL7, 1BMK, 1DI9, 1IAN, 1KV1, 1KV2, 1M7Q, 1OUK, 1OUY, 1OVE, 1OZ1, 1R39, 1R3C, 1W7H, 1W82, 1W83, 1W84, 1WBN, 1WBO, 1WBS, 1WBT, 1WBV, 1WBW, 1WFC, 1YQJ, 1ZYJ, 1ZZ2, 1ZZL, 2BAJ, 2BAK, 2BAL, 2BAQ, 2FSL, 2FSM, 2FSO, 2FST, 2GFS, 2I0H, 2LGC, 2NPQ, 2OKR, 2ONL, 2QD9, 2RG5, 2RG6, 2Y8O, 2YIS, 2YIW, 2YIX, 2ZAZ, 2ZB0, 2ZB1, 3BV2, 3BV3, 3BX5, 3C5U, 3CTQ, 3D7Z, 3D83, 3DS6, 3DT1, 3E92, 3E93, 3FI4, 3FKL, 3FKN, 3FKO, 3FL4, 3FLN, 3FLQ, 3FLS, 3FLW, 3FLY, 3FLZ, 3FMH, 3FMJ, 3FMK, 3FML, 3FMM, 3FMN, 3FSF, 3FSK, 3GC7, 3GCP, 3GCQ, 3GCS, 3GCU, 3GCV, 3GFE, 3GI3, 3HA8, 3HEC, 3HEG, 3HL7, 3HLL, 3HP2, 3HP5, 3HRB, 3HUB, 3HUC, 3HV3, 3HV4, 3HV5, 3HV6, 3HV7, 3HVC, 3IPH, 3ITZ, 3IW5, 3IW6, 3IW7, 3IW8, 3K3I, 3K3J, 3KF7, 3KQ7, 3L8S, 3L8X, 3LFA, 3LFB, 3LFC, 3LFD, 3LFE, 3LFF, 3LHJ, 3MGY, 3MH0, 3MH1, 3MH2, 3MH3, 3MPA, 3MPT, 3MVL, 3MVM, 3MW1, 3NEW, 3NNU, 3NNV, 3NNW, 3NNX, 3NWW, 3O8P, 3O8T, 3O8U, 3OBG, 3OBJ, 3OC1, 3OCG, 3OD6, 3ODY, 3ODZ, 3OEF, 3PG3, 3QUD, 3QUE, 3RIN, 3ROC, 3S3I, 3S4Q, 3U8W, 3UVP, 3UVQ, 3UVR, 3ZS5, 3ZSG, 3ZSH, 3ZSI, 3ZYA, 4A9Y, 4AA0, 4AA4, 4AA5, 4AAC, 4DLI, 4DLJ, 4E5A, 4E5B, 4E6A, 4E6C, 4E8A, 4EH2, 4EH3, 4EH4, 4EH5, 4EH6, 4EH7, 4EH8, 4EH9, 4EHV, 4EWQ, 4F9W, 4F9Y, 4FA2, 4GEO, 4KIN, 4KIP, 4KIQ, 4L8M, 3FC1, 4R3C, 5ETC, 5ETI, 4ZTH
Identifiers
Aliases	MAPK14, CSBP, CSBP1, CSBP2, CSPB1, EXIP, Mxi2, PRKM14, PRKM15, RK, SAPK2A, p38, p38ALPHA, mitogen-activated protein kinase 14
External IDs	OMIM: 600289; MGI: 1346865; HomoloGene: 31777; GeneCards: MAPK14; OMA:MAPK14 - orthologs
Gene location (Human)
Chr.	Chromosome 6 (human)
End	36,111,236 bp
Gene location (Mouse)
Chr.	Chromosome 17 (mouse)
End	28,967,380 bp
RNA expression pattern
	Top expressed in
	blood; ; bone marrow; ; bone marrow cells; ; monocyte; ; trabecular bone; ; Achilles tendon; ; endothelial cell; ; stromal cell of endometrium; ; myometrium; ; smooth muscle tissue;
	Top expressed in
	renal corpuscle; ; medullary collecting duct; ; blood; ; conjunctival fornix; ; knee joint; ; triceps brachii muscle; ; primitive streak; ; masseter muscle; ; vastus lateralis muscle; ; submandibular gland;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	kinase activity; protein phosphatase binding; ATP binding; protein kinase activity; MAP kinase activity; protein serine/threonine kinase activity; enzyme binding; NFAT protein binding; transferase activity; protein binding; nucleotide binding; MAP kinase kinase activity; mitogen-activated protein kinase p38 binding;
Cellular component	cytosol; mitochondrion; spindle pole; extracellular region; nucleoplasm; nuclear speck; secretory granule lumen; ficolin-1-rich granule lumen; nucleus; cytoplasm; glutamatergic synapse;
Biological process	positive regulation of glucose import; positive regulation of muscle cell differentiation; placenta development; regulation of transcription by RNA polymerase II; cellular response to DNA damage stimulus; protein phosphorylation; cell surface receptor signaling pathway; positive regulation of reactive oxygen species metabolic process; positive regulation of cardiac muscle cell proliferation; fatty acid oxidation; angiogenesis; positive regulation of blood vessel endothelial cell migration; glucose metabolic process; cellular response to ionizing radiation; negative regulation of canonical Wnt signaling pathway; apoptotic process; response to muscle stretch; regulation of transcription, DNA-templated; positive regulation of erythrocyte differentiation; stress-induced premature senescence; osteoclast differentiation; response to muramyl dipeptide; transcription, DNA-templated; p38MAPK cascade; positive regulation of protein import into nucleus; 3'-UTR-mediated mRNA stabilization; myoblast differentiation involved in skeletal muscle regeneration; chondrocyte differentiation; phosphorylation; signal transduction in response to DNA damage; chemotaxis; positive regulation of myoblast fusion; response to lipopolysaccharide; positive regulation of cyclase activity; cartilage condensation; lipopolysaccharide-mediated signaling pathway; positive regulation of myotube differentiation; intracellular signal transduction; regulation of cytokine production involved in inflammatory response; DNA damage checkpoint signaling; positive regulation of gene expression; transmembrane receptor protein serine/threonine kinase signaling pathway; positive regulation of myoblast differentiation; peptidyl-serine phosphorylation; cell morphogenesis; striated muscle cell differentiation; cellular response to vascular endothelial growth factor stimulus; cellular response to lipopolysaccharide; positive regulation of brown fat cell differentiation; skeletal muscle tissue development; positive regulation of transcription by RNA polymerase II; signal transduction; regulation of signal transduction by p53 class mediator; regulation of ossification; neutrophil degranulation; positive regulation of macrophage chemotaxis; positive regulation of metallopeptidase activity; cellular response to lipoteichoic acid; cellular response to tumor necrosis factor; vascular endothelial growth factor receptor signaling pathway; regulation of synaptic membrane adhesion; regulation of gene expression; cellular response to organic substance; Ras protein signal transduction; regulation of DNA-binding transcription factor activity;
	Sources:Amigo / QuickGO
Orthologs
	1432
	26416
	ENSG00000112062
	ENSMUSG00000053436
	Q16539
	P47811
	NM_001315; NM_139012; NM_139013; NM_139014
	NM_001168508; NM_001168513; NM_001168514; NM_011951; NM_001357724
	NP_001306; NP_620581; NP_620582; NP_620583
	NP_001161980; NP_001161985; NP_001161986; NP_036081; NP_001344653
	Wikidata
View/Edit Human	View/Edit Mouse

Mitogen-activated protein kinase 14, also called p38-α, is an enzyme that in humans is encoded by the MAPK14 gene.^[5]

MAPK14 encodes p38α mitogen-activated protein kinase (MAPK) which is the prototypic member of the p38 MAPK family. p38 MAPKs are also known as stress-activated serine/threonine-specific kinases (SAPKs). In addition to MAPK14 for p38α MAPK, the p38 MAPK family has three additional members, including MAPK11, MAPK12 and MAPK13 which encodes p38β MAPK, p38γ MAPK and p38δ MAPK isoforms, respectively. p38α MAPK was originally identified as a tyrosine phosphorylated protein detected in activated immune cell macrophages with an essential role in inflammatory cytokine induction, such as Tumor Necrotic Factor α (TNFα).^[6]^[7] However, p38α MAPK mediated kinase activity has been implicated in many tissues beyond immune systems. p38α MAPK is mainly activated through MAPK kinase kinase cascades and exerts its biological function via downstream substrate phosphorylation. p38α MAPK is implicated in diverse cellular functions, from gene expression to programmed cell death through a network of signaling molecules and transcription factors. Pharmacological and genetic inhibition of p38α MAPK not only revealed its biological significance in physiological function but also the potential of targeting p38α MAPK in human disease such as immune disorders and heart failure.

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000112062 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000053436 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Lee JC, Laydon JT, McDonnell PC, Gallagher TF, Kumar S, Green D, McNulty D, Blumenthal MJ, Heys JR, Landvatter SW (January 1995). "A protein kinase involved in the regulation of inflammatory cytokine biosynthesis". Nature. 372 (6508): 739–46. doi:10.1038/372739a0. PMID 7997261. S2CID 4306822.
^ Han J, Lee JD, Bibbs L, Ulevitch RJ (Aug 1994). "A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells". Science. 265 (5173): 808–11. Bibcode:1994Sci...265..808H. doi:10.1126/science.7914033. PMID 7914033.
^ Han J, Lee JD, Tobias PS, Ulevitch RJ (Nov 1993). "Endotoxin induces rapid protein tyrosine phosphorylation in 70Z/3 cells expressing CD14". The Journal of Biological Chemistry. 268 (33): 25009–14. doi:10.1016/S0021-9258(19)74564-5. PMID 7693711.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000112062 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000053436 – 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.

[pmid7997261-5] Lee JC, Laydon JT, McDonnell PC, Gallagher TF, Kumar S, Green D, McNulty D, Blumenthal MJ, Heys JR, Landvatter SW (January 1995). "A protein kinase involved in the regulation of inflammatory cytokine biosynthesis". Nature. 372 (6508): 739–46. doi:10.1038/372739a0. PMID 7997261. S2CID 4306822.

[6] Han J, Lee JD, Bibbs L, Ulevitch RJ (Aug 1994). "A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells". Science. 265 (5173): 808–11. Bibcode:1994Sci...265..808H. doi:10.1126/science.7914033. PMID 7914033.

[7] Han J, Lee JD, Tobias PS, Ulevitch RJ (Nov 1993). "Endotoxin induces rapid protein tyrosine phosphorylation in 70Z/3 cells expressing CD14". The Journal of Biological Chemistry. 268 (33): 25009–14. doi:10.1016/S0021-9258(19)74564-5. PMID 7693711.

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