Literature summary for 2.7.11.24 extracted from

Beenstock, J.; Ben-Yehuda, S.; Melamed, D.; Admon, A.; Livnah, O.; Ahn, N.; Engelberg, D.
The p38beta mitogen-activated protein kinase possesses an intrinsic autophosphorylation activity, generated by a short region composed of the alpha-G helix and MAPK insert (2014), J. Biol. Chem., 289, 23546-23556.

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Cloned(Commentary)

Cloned (Comment)	Organism
transient expression of wild-type and mutant p38alpha in HEK-293 cells	Homo sapiens
transient expression of wild-type and mutant p38beta in HEK-293 cells	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
D176A	site-directed mutagenesis of p38beta, the intrinsically active variant is spontaneously phosphorylated and active toward MK2, the mutant manifests elevated catalytic activity when immunoprecipitated from cells not exposed to any activating signal	Homo sapiens
D176A/F327S	site-directed mutagenesis of p38alpha, the intrinsically active variant is spontaneously phosphorylated and active toward MK2, the mutant manifests elevated catalytic activity when immunoprecipitated from cells not exposed to any activating signal	Homo sapiens
additional information	elevating expression levels of p38alpha wild-type results in only a slight increase in their apparent phosphorylation that is not sufficient to induce phosphorylation of the p38 substrate MAPKAPK2. Expression of the chimera containing Gln218-Val246, which possesses the highest intrinsic activity as a recombinant purified protein, leads to its spontaneously phosphorylation at high levels in HEK-293 cells and to a spontaneous, signal-independent phosphorylation of MK2. Generation of a p38alpha/beta/alpha/beta chimera that has, in addition to the G-helix-MKI (Gln218-Val246) region from p38beta, also the C-terminus of p38beta, Leu334-Gln364. The p38alpha/beta/alpha/beta chimera shows lose spontaneous activity and is more active than the parental chimera. p38alpha/beta/alpha/beta is phosphorylated at higher levels and shows higher phosphorylation of MK2 in HEK-293 cells than p38alpha/beta/alpha	Homo sapiens
additional information	elevating expression levels of p38beta wild-type results in only a slight increase in their apparent phosphorylation that is not sufficient to induce phosphorylation of the p38 substrate MAPKAPK2. Expression of the chimera containing Gln218-Val246, which possesses the highest intrinsic activity as a recombinant purified protein, leads to its spontaneously phosphorylation at high levels in HEK-293 cells and to a spontaneous, signal-independent phosphorylation of MK2. Construction of enzyme mutants by insertion of premature stop codons p38beta generating p38beta C-terminal truncation mutants p38betaT341, p38betaV345, p38betaF348, and p38betaK355, the mutants lacking the C-terminus show elevated spontaneous MKK6-independent autophosphorylation activities. Generation of a p38alpha/beta/alpha/beta chimera that has, in addition to the G-helix-MKI (Gln218-Val246) region from p38beta, also the C-terminus of p38beta, Leu334-Gln364. The p38alpha/beta/alpha/beta chimera shows lose spontaneous activity and is more active than the parental chimera. p38alpha/beta/alpha/beta is phosphorylated at higher levels and shows higher phosphorylation of MK2 in HEK-293 cells than p38alpha/beta/alpha	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + MAPKAPK2	Homo sapiens	-	ADP + phosphorylated MAPKAPK2	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q15759	-	-
Homo sapiens	Q16539	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	p38beta can autophosphorylate and thus autoactivate itself, the C tail of p38beta inhibits autophosphorylation	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + MAPKAPK2	-	Homo sapiens	ADP + phosphorylated MAPKAPK2	-	?
additional information	p38beta can autophosphorylate and thus autoactivate itself, the C tail of p38beta inhibits autophosphorylation	Homo sapiens	?	-	?

Synonyms

Synonyms	Comment	Organism
MAPK11	-	Homo sapiens
MAPK14	-	Homo sapiens
p38alpha	-	Homo sapiens
p38beta	-	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	the intrinsic activity of wild-type p38beta is regulated in mammalian cells	Homo sapiens

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Release 2023.1 (January 2023)