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Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (CRK1) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha)

 MK14_RAT                Reviewed;         360 AA.
P70618; O08594; Q99MG4;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 154.
RecName: Full=Mitogen-activated protein kinase 14;
Short=MAP kinase 14;
Short=MAPK 14;
EC=2.7.11.24;
AltName: Full=CRK1;
AltName: Full=Mitogen-activated protein kinase p38 alpha;
Short=MAP kinase p38 alpha;
Name=Mapk14; Synonyms=Csbp1, Csbp2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9513091; DOI=10.1677/jme.0.0200151;
Nemeth E., Bole-Feysot C., Tashima L.S.;
"Suppression subtractive hybridization (SSH) identifies prolactin
stimulation of p38 MAP kinase gene expression in Nb2 T lymphoma cells:
molecular cloning of rat p38 MAP kinase.";
J. Mol. Endocrinol. 20:151-156(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=Lewis; TISSUE=Kidney;
Garcia G.E., Han J., Feng L.;
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Reick M.E., Goldsmith E.J.;
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
[4]
REVIEW ON FUNCTION.
PubMed=12452429; DOI=10.1515/BC.2002.173;
Shi Y., Gaestel M.;
"In the cellular garden of forking paths: how p38 MAPKs signal for
downstream assistance.";
Biol. Chem. 383:1519-1536(2002).
[5]
REVIEW ON ENZYME REGULATION, AND REVIEW ON FUNCTION.
PubMed=20626350; DOI=10.1042/BJ20100323;
Cuadrado A., Nebreda A.R.;
"Mechanisms and functions of p38 MAPK signalling.";
Biochem. J. 429:403-417(2010).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; THR-180 AND TYR-182,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Serine/threonine kinase which acts as an essential
component of the MAP kinase signal transduction pathway. MAPK14 is
one of the four p38 MAPKs which play an important role in the
cascades of cellular responses evoked by extracellular stimuli
such as proinflammatory cytokines or physical stress leading to
direct activation of transcription factors. Accordingly, p38 MAPKs
phosphorylate a broad range of proteins and it has been estimated
that they may have approximately 200 to 300 substrates each. Some
of the targets are downstream kinases which are activated through
phosphorylation and further phosphorylate additional targets.
RPS6KA5/MSK1 and RPS6KA4/MSK2 can directly phosphorylate and
activate transcription factors such as CREB1, ATF1, the NF-kappa-B
isoform RELA/NFKB3, STAT1 and STAT3, but can also phosphorylate
histone H3 and the nucleosomal protein HMGN1. RPS6KA5/MSK1 and
RPS6KA4/MSK2 play important roles in the rapid induction of
immediate-early genes in response to stress or mitogenic stimuli,
either by inducing chromatin remodeling or by recruiting the
transcription machinery. On the other hand, two other kinase
targets, MAPKAPK2/MK2 and MAPKAPK3/MK3, participate in the control
of gene expression mostly at the post-transcriptional level, by
phosphorylating ZFP36 (tristetraprolin) and ELAVL1, and by
regulating EEF2K, which is important for the elongation of mRNA
during translation. MKNK1/MNK1 and MKNK2/MNK2, two other kinases
activated by p38 MAPKs, regulate protein synthesis by
phosphorylating the initiation factor EIF4E2. MAPK14 interacts
also with casein kinase II, leading to its activation through
autophosphorylation and further phosphorylation of TP53/p53. In
the cytoplasm, the p38 MAPK pathway is an important regulator of
protein turnover. For example, CFLAR is an inhibitor of TNF-
induced apoptosis whose proteasome-mediated degradation is
regulated by p38 MAPK phosphorylation. In a similar way, MAPK14
phosphorylates the ubiquitin ligase SIAH2, regulating its activity
towards EGLN3. MAPK14 may also inhibit the lysosomal degradation
pathway of autophagy by interfering with the intracellular
trafficking of the transmembrane protein ATG9. Another function of
MAPK14 is to regulate the endocytosis of membrane receptors by
different mechanisms that impinge on the small GTPase RAB5A. In
addition, clathrin-mediated EGFR internalization induced by
inflammatory cytokines and UV irradiation depends on MAPK14-
mediated phosphorylation of EGFR itself as well as of RAB5A
effectors. Ectodomain shedding of transmembrane proteins is
regulated by p38 MAPKs as well. In response to inflammatory
stimuli, p38 MAPKs phosphorylate the membrane-associated
metalloprotease ADAM17. Such phosphorylation is required for
ADAM17-mediated ectodomain shedding of TGF-alpha family ligands,
which results in the activation of EGFR signaling and cell
proliferation. Another p38 MAPK substrate is FGFR1. FGFR1 can be
translocated from the extracellular space into the cytosol and
nucleus of target cells, and regulates processes such as rRNA
synthesis and cell growth. FGFR1 translocation requires p38 MAPK
activation. In the nucleus, many transcription factors are
phosphorylated and activated by p38 MAPKs in response to different
stimuli. Classical examples include ATF1, ATF2, ATF6, ELK1, PTPRH,
DDIT3, TP53/p53 and MEF2C and MEF2A. The p38 MAPKs are emerging as
important modulators of gene expression by regulating chromatin
modifiers and remodelers. The promoters of several genes involved
in the inflammatory response, such as IL6, IL8 and IL12B, display
a p38 MAPK-dependent enrichment of histone H3 phosphorylation on
'Ser-10' (H3S10ph) in LPS-stimulated myeloid cells. This
phosphorylation enhances the accessibility of the cryptic NF-
kappa-B-binding sites marking promoters for increased NF-kappa-B
recruitment. Phosphorylates CDC25B and CDC25C which is required
for binding to 14-3-3 proteins and leads to initiation of a G2
delay after ultraviolet radiation. Phosphorylates TIAR following
DNA damage, releasing TIAR from GADD45A mRNA and preventing mRNA
degradation. The p38 MAPKs may also have kinase-independent roles,
which are thought to be due to the binding to targets in the
absence of phosphorylation. Protein O-Glc-N-acylation catalyzed by
the OGT is regulated by MAPK14, and, although OGT does not seem to
be phosphorylated by MAPK14, their interaction increases upon
MAPK14 activation induced by glucose deprivation. This interaction
may regulate OGT activity by recruiting it to specific targets
such as neurofilament H, stimulating its O-Glc-N-acylation.
Required in mid-fetal development for the growth of embryo-derived
blood vessels in the labyrinth layer of the placenta. Also plays
an essential role in developmental and stress-induced
erythropoiesis, through regulation of EPO gene expression.
Phosphorylates S100A9 at 'Thr-113' (By similarity).
{ECO:0000250|UniProtKB:Q16539}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000250|UniProtKB:Q16539}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q16539};
-!- ENZYME REGULATION: Activated by cell stresses such as DNA damage,
heat shock, osmotic shock, anisomycin and sodium arsenite, as well
as pro-inflammatory stimuli such as bacterial lipopolysaccharide
(LPS) and interleukin-1. Activation occurs through dual
phosphorylation of Thr-180 and Tyr-182 by either of two dual
specificity kinases, MAP2K3/MKK3 or MAP2K6/MKK6, and potentially
also MAP2K4/MKK4, as well as by TAB1-mediated autophosphorylation.
MAPK14 phosphorylated on both Thr-180 and Tyr-182 is 10-20-fold
more active than MAPK14 phosphorylated only on Thr-180, whereas
MAPK14 phosphorylated on Tyr-182 alone is inactive. whereas Thr-
180 is necessary for catalysis, Tyr-182 may be required for auto-
activation and substrate recognition. Phosphorylated at Tyr-323 by
ZAP70 in an alternative activation pathway in response to TCR
signaling in T-cells. This alternative pathway is inhibited by
GADD45A. Inhibited by dual specificity phosphatases, such as
DUSP1, DUSP10, and DUSP16. Specifically inhibited by the binding
of pyridinyl-imidazole compounds, which are cytokine-suppressive
anti-inflammatory drugs (CSAID). SB203580 is an inhibitor of
MAPK14 (By similarity). {ECO:0000250|UniProtKB:Q16539}.
-!- SUBUNIT: Component of a signaling complex containing at least
AKAP13, PKN1, MAPK14, ZAK and MAP2K3. Within this complex, AKAP13
interacts directly with PKN1, which in turn recruits MAPK14,
MAP2K3 and ZAK (By similarity). Binds to a kinase interaction
motif within the protein tyrosine phosphatase, PTPRR (By
similarity). This interaction retains MAPK14 in the cytoplasm and
prevents nuclear accumulation (By similarity). Interacts with
SPAG9 and GADD45A (By similarity). Interacts with CDC25B, CDC25C,
DUSP1, DUSP10, DUSP16, NP60, SUPT20H and TAB1. Interacts with
casein kinase II subunits CSNK2A1 and CSNK2B. Interacts with
PPM1D. Interacts with CDK5RAP3; recruits PPM1D to MAPK14 and may
regulate its dephosphorylation (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:Q16539}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16539}.
Nucleus {ECO:0000250|UniProtKB:Q16539}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P70618-1; Sequence=Displayed;
Name=2;
IsoId=P70618-2; Sequence=VSP_004847;
-!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
whose phosphorylation activates the MAP kinases.
-!- PTM: Dually phosphorylated on Thr-180 and Tyr-182 by the MAP2Ks
MAP2K3/MKK3, MAP2K4/MKK4 and MAP2K6/MKK6 in response to
inflammatory cytokines, environmental stress or growth factors,
which activates the enzyme. Dual phosphorylation can also be
mediated by TAB1-mediated autophosphorylation. TCR engagement in
T-cells also leads to Tyr-323 phosphorylation by ZAP70.
Dephosphorylated and inactivated by DUPS1, DUSP10 and DUSP16 (By
similarity). PPM1D also mediates dephosphorylation and
inactivation of MAPK14 (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:Q16539}.
-!- PTM: Acetylated at Lys-53 and Lys-152 by KAT2B and EP300.
Acetylation at Lys-53 increases the affinity for ATP and enhances
kinase activity. Lys-53 and Lys-152 are deacetylated by HDAC3 (By
similarity). {ECO:0000250|UniProtKB:Q16539}.
-!- PTM: Ubiquitinated. Ubiquitination leads to degradation by the
proteasome pathway (By similarity).
{ECO:0000250|UniProtKB:Q16539}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. MAP kinase subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U73142; AAC71059.1; -; mRNA.
EMBL; U91847; AAB51285.1; -; mRNA.
EMBL; AF346293; AAK15541.1; -; mRNA.
UniGene; Rn.88085; -.
ProteinModelPortal; P70618; -.
SMR; P70618; -.
DIP; DIP-29878N; -.
IntAct; P70618; 2.
MINT; MINT-4777441; -.
STRING; 10116.ENSRNOP00000000617; -.
BindingDB; P70618; -.
ChEMBL; CHEMBL4825; -.
iPTMnet; P70618; -.
PhosphoSitePlus; P70618; -.
PaxDb; P70618; -.
PRIDE; P70618; -.
UCSC; RGD:70496; rat. [P70618-1]
RGD; 70496; Mapk14.
eggNOG; KOG0660; Eukaryota.
eggNOG; ENOG410XNY0; LUCA.
HOGENOM; HOG000233024; -.
HOVERGEN; HBG014652; -.
InParanoid; P70618; -.
PhylomeDB; P70618; -.
BRENDA; 2.7.11.24; 5301.
Reactome; R-RNO-171007; p38MAPK events.
PRO; PR:P70618; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005524; F:ATP binding; IDA:RGD.
GO; GO:0004707; F:MAP kinase activity; IDA:RGD.
GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
GO; GO:0038066; P:p38MAPK cascade; ISS:UniProtKB.
GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:UniProtKB.
GO; GO:1901741; P:positive regulation of myoblast fusion; ISS:UniProtKB.
GO; GO:0010831; P:positive regulation of myotube differentiation; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:RGD.
GO; GO:0046777; P:protein autophosphorylation; IDA:RGD.
GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
GO; GO:0007265; P:Ras protein signal transduction; TAS:Reactome.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0009749; P:response to glucose; IEP:RGD.
GO; GO:0051403; P:stress-activated MAPK cascade; IDA:RGD.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR003527; MAP_kinase_CS.
InterPro; IPR008352; MAPK_p38.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
Pfam; PF00069; Pkinase; 1.
PRINTS; PR01773; P38MAPKINASE.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS01351; MAPK; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Apoptosis; ATP-binding;
Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
Stress response; Transcription; Transcription regulation; Transferase;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q16539}.
CHAIN 2 360 Mitogen-activated protein kinase 14.
/FTId=PRO_0000186294.
DOMAIN 24 308 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 30 38 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 180 182 TXY.
ACT_SITE 150 150 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 53 53 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:Q16539}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 16 16 Phosphothreonine.
{ECO:0000250|UniProtKB:Q16539}.
MOD_RES 53 53 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q16539}.
MOD_RES 152 152 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q16539}.
MOD_RES 180 180 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 182 182 Phosphotyrosine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 323 323 Phosphotyrosine; by ZAP70.
{ECO:0000250|UniProtKB:Q16539}.
VAR_SEQ 230 254 DQLKLILRLVGTPGAELLKKISSES -> NQLQQIMRLTGT
PPAYLINRMPSHE (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_004847.
CONFLICT 59 59 F -> V (in Ref. 2; AAB51285).
{ECO:0000305}.
CONFLICT 61 61 S -> P (in Ref. 2; AAB51285).
{ECO:0000305}.
CONFLICT 68 68 T -> S (in Ref. 2; AAB51285).
{ECO:0000305}.
CONFLICT 321 321 E -> D (in Ref. 2; AAB51285 and 3;
AAK15541). {ECO:0000305}.
CONFLICT 332 332 F -> L (in Ref. 2; AAB51285 and 3;
AAK15541). {ECO:0000305}.
CONFLICT 359 359 E -> D (in Ref. 2; AAB51285 and 3;
AAK15541). {ECO:0000305}.
SEQUENCE 360 AA; 41321 MW; 59FBF1FC3398C5CA CRC64;
MSQERPTFYR QELNKTVWEV PERYQNLSPV GSGAYGSVCA AFDTKTGHRV AVKKLSRPFQ
SIIHAKRTYR ELRLLKHMKH ENVIGLLDVF TPARSLEEFN DVYLVTHLMG ADLNNIVKCQ
KLTDDHVQFL IYQILRGLKY IHSADIIHRD LKPSNLAVNE DCELKILDFG LARHTDDEMT
GYVATRWYRA PEIMLNWMHY NQTVDIWSVG CIMAELLTGR TLFPGTDHID QLKLILRLVG
TPGAELLKKI SSESARNYIQ SLAQMPKMNF ANVFIGANPL AVDLLEKMLV LDSDKRITAA
QALAHAYFAQ YHDPDDEPVA EPYDQSFESR DFLIDEWKSL TYDEVISFVP PPLDQEEMES


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