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MAP kinase-activated protein kinase 5 (MAPK-activated protein kinase 5) (MAPKAP kinase 5) (MAPKAPK-5) (EC 2.7.11.1)

 MAPK5_MOUSE             Reviewed;         473 AA.
O54992; E9QQ45; Q6QME4; Q6QME5; Q6QME6; Q6QME7;
13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
12-SEP-2018, entry version 156.
RecName: Full=MAP kinase-activated protein kinase 5;
Short=MAPK-activated protein kinase 5;
Short=MAPKAP kinase 5;
Short=MAPKAPK-5;
EC=2.7.11.1;
Name=Mapkapk5;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
MUTAGENESIS OF LYS-51, ACTIVITY REGULATION, AND PHOSPHORYLATION BY
ERK2/MAPK1 AND MAPK14.
TISSUE=Spleen;
PubMed=9480836; DOI=10.1006/bbrc.1998.8135;
Ni H., Wang X.S., Diener K., Yao Z.;
"MAPKAPK5, a novel mitogen-activated protein kinase (MAPK)-activated
protein kinase, is a substrate of the extracellular-regulated kinase
(ERK) and p38 kinase.";
Biochem. Biophys. Res. Commun. 243:492-496(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5).
Benoit M.-J., Moise N., Mamarbachi A.M., Allen B.G.;
"Novel splice variants of MK5 from mouse heart.";
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N-3; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
DISRUPTION PHENOTYPE.
PubMed=14560018; DOI=10.1128/MCB.23.21.7732-7741.2003;
Shi Y., Kotlyarov A., Laabeta K., Gruber A.D., Butt E., Marcus K.,
Meyer H.E., Friedrich A., Volk H.D., Gaestel M.;
"Elimination of protein kinase MK5/PRAK activity by targeted
homologous recombination.";
Mol. Cell. Biol. 23:7732-7741(2003).
[6]
FUNCTION IN PHOSPHORYLATION OF MAPK6, SUBCELLULAR LOCATION,
INTERACTION WITH MAPK6, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT
THR-182, MUTAGENESIS OF LYS-51 AND THR-182, AND DISRUPTION PHENOTYPE.
PubMed=15538386; DOI=10.1038/sj.emboj.7600467;
Schumacher S., Laass K., Kant S., Shi Y., Visel A., Gruber A.D.,
Kotlyarov A., Gaestel M.;
"Scaffolding by ERK3 regulates MK5 in development.";
EMBO J. 23:4770-4779(2004).
[7]
FUNCTION IN PHOSPHORYLATION OF MAPK6, SUBCELLULAR LOCATION,
INTERACTION WITH MAPK6, PHOSPHORYLATION AT THR-182, AND MUTAGENESIS OF
THR-182.
PubMed=15577943; DOI=10.1038/sj.emboj.7600489;
Seternes O.M., Mikalsen T., Johansen B., Michaelsen E.,
Armstrong C.G., Morrice N.A., Turgeon B., Meloche S., Moens U.,
Keyse S.M.;
"Activation of MK5/PRAK by the atypical MAP kinase ERK3 defines a
novel signal transduction pathway.";
EMBO J. 23:4780-4791(2004).
[8]
FUNCTION IN PHOSPHORYLATION OF MAPK4, SUBCELLULAR LOCATION, AND
INTERACTION WITH MAPK4.
PubMed=16973613; DOI=10.1074/jbc.M606693200;
Kant S., Schumacher S., Singh M.K., Kispert A., Kotlyarov A.,
Gaestel M.;
"Characterization of the atypical MAPK ERK4 and its activation of the
MAPK-activated protein kinase MK5.";
J. Biol. Chem. 281:35511-35519(2006).
[9]
MUTAGENESIS OF LEU-337.
PubMed=17997833; DOI=10.1186/1744-9081-3-58;
Gerits N., Van Belle W., Moens U.;
"Transgenic mice expressing constitutive active MAPKAPK5 display
gender-dependent differences in exploration and activity.";
Behav. Brain Funct. 3:58-58(2007).
[10]
FUNCTION IN PHOSPHORYLATION OF TP53, DISRUPTION PHENOTYPE, AND
MUTAGENESIS OF LYS-51 AND THR-182.
PubMed=17254968; DOI=10.1016/j.cell.2006.11.050;
Sun P., Yoshizuka N., New L., Moser B.A., Li Y., Liao R., Xie C.,
Chen J., Deng Q., Yamout M., Dong M.Q., Frangou C.G., Yates J.R. III,
Wright P.E., Han J.;
"PRAK is essential for ras-induced senescence and tumor suppression.";
Cell 128:295-308(2007).
[11]
SUBCELLULAR LOCATION.
PubMed=17947239; DOI=10.1074/jbc.M704873200;
Gerits N., Mikalsen T., Kostenko S., Shiryaev A., Johannessen M.,
Moens U.;
"Modulation of F-actin rearrangement by the cyclic AMP/cAMP-dependent
protein kinase (PKA) pathway is mediated by MAPK-activated protein
kinase 5 and requires PKA-induced nuclear export of MK5.";
J. Biol. Chem. 282:37232-37243(2007).
[12]
INTERACTION WITH MAPK4.
PubMed=18248330; DOI=10.1042/BJ20071369;
Perander M., Aberg E., Johansen B., Dreyer B., Guldvik I.J.,
Outzen H., Keyse S.M., Seternes O.M.;
"The Ser(186) phospho-acceptor site within ERK4 is essential for its
ability to interact with and activate PRAK/MK5.";
Biochem. J. 411:613-622(2008).
[13]
SUBCELLULAR LOCATION.
PubMed=18268017; DOI=10.1074/jbc.M709682200;
Li Q., Zhang N., Zhang D., Wang Y., Lin T., Wang Y., Zhou H., Ye Z.,
Zhang F., Lin S.C., Han J.;
"Determinants that control the distinct subcellular localization of
p38alpha-PRAK and p38beta-PRAK complexes.";
J. Biol. Chem. 283:11014-11023(2008).
[14]
INTERACTION WITH MAPK4 AND MAPK6.
PubMed=18720373; DOI=10.1002/jcp.21560;
Deleris P., Rousseau J., Coulombe P., Rodier G., Tanguay P.L.,
Meloche S.;
"Activation loop phosphorylation of the atypical MAP kinases ERK3 and
ERK4 is required for binding, activation and cytoplasmic
relocalization of MK5.";
J. Cell. Physiol. 217:778-788(2008).
[15]
INTERACTION WITH MAPK4 AND MAPK6.
PubMed=19473979; DOI=10.1074/jbc.M109.023283;
Aberg E., Torgersen K.M., Johansen B., Keyse S.M., Perander M.,
Seternes O.M.;
"Docking of PRAK/MK5 to the atypical MAPKs ERK3 and ERK4 defines a
novel MAPK interaction motif.";
J. Biol. Chem. 284:19392-19401(2009).
[16]
CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND
MUTAGENESIS OF THR-182.
PubMed=20640477; DOI=10.1007/s00018-010-0452-1;
Kostenko S., Khan M.T., Sylte I., Moens U.;
"The diterpenoid alkaloid noroxoaconitine is a Mapkap kinase 5
(MK5/PRAK) inhibitor.";
Cell. Mol. Life Sci. 68:289-301(2011).
[17]
PHOSPHORYLATION AT SER-115, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
SER-115.
PubMed=20734105; DOI=10.1007/s00018-010-0496-2;
Kostenko S., Shiryaev A., Gerits N., Dumitriu G., Klenow H.,
Johannessen M., Moens U.;
"Serine residue 115 of MAPK-activated protein kinase MK5 is crucial
for its PKA-regulated nuclear export and biological function.";
Cell. Mol. Life Sci. 68:847-862(2011).
[18]
FUNCTION IN PHOSPHORYLATION OF HSPB1.
PubMed=21575178; DOI=10.1186/1750-2187-6-4;
Shiryaev A., Dumitriu G., Moens U.;
"Distinct roles of MK2 and MK5 in cAMP/PKA- and stress/p38MAPK-induced
heat shock protein 27 phosphorylation.";
J. Mol. Signal. 6:4-4(2011).
[19]
FUNCTION IN PHOSPHORYLATION OF RHEB, AND MUTAGENESIS OF LYS-51.
PubMed=21336308; DOI=10.1038/ncb2168;
Zheng M., Wang Y.H., Wu X.N., Wu S.Q., Lu B.J., Dong M.Q., Zhang H.,
Sun P., Lin S.C., Guan K.L., Han J.;
"Inactivation of Rheb by PRAK-mediated phosphorylation is essential
for energy-depletion-induced suppression of mTORC1.";
Nat. Cell Biol. 13:263-272(2011).
-!- FUNCTION: Tumor suppressor serine/threonine-protein kinase
involved in mTORC1 signaling and post-transcriptional regulation.
Phosphorylates FOXO3, ERK3/MAPK6, ERK4/MAPK4, HSP27/HSPB1,
p53/TP53 and RHEB. Acts as a tumor suppressor by mediating Ras-
induced senescence and phosphorylating p53/TP53. Involved in post-
transcriptional regulation of MYC by mediating phosphorylation of
FOXO3: phosphorylation of FOXO3 leads to promote nuclear
localization of FOXO3, enabling expression of miR-34b and miR-34c,
2 post-transcriptional regulators of MYC that bind to the 3'UTR of
MYC transcript and prevent MYC translation. Acts as a negative
regulator of mTORC1 signaling by mediating phosphorylation and
inhibition of RHEB. Part of the atypical MAPK signaling via its
interaction with ERK3/MAPK6 or ERK4/MAPK4: the precise role of the
complex formed with ERK3/MAPK6 or ERK4/MAPK4 is still unclear, but
the complex follows a complex set of phosphorylation events: upon
interaction with atypical MAPK (ERK3/MAPK6 or ERK4/MAPK4),
ERK3/MAPK6 (or ERK4/MAPK4) is phosphorylated and then mediates
phosphorylation and activation of MAPKAPK5, which in turn
phosphorylates ERK3/MAPK6 (or ERK4/MAPK4). Mediates
phosphorylation of HSP27/HSPB1 in response to PKA/PRKACA
stimulation, inducing F-actin rearrangement.
{ECO:0000269|PubMed:15538386, ECO:0000269|PubMed:15577943,
ECO:0000269|PubMed:16973613, ECO:0000269|PubMed:17254968,
ECO:0000269|PubMed:21336308, ECO:0000269|PubMed:21575178}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:20640477}.
-!- ACTIVITY REGULATION: Activated following phosphorylation at Thr-
182 by p38-alpha/MAPK14, p38-beta/MAPK11, ERK2/MAPK1, ERK3/MAPK6,
and ERK4/MAPK4. Activated by stress-related extracellular stimuli;
such as H(2)O(2), arsenite, anisomycin TNF alpha and also PMA and
the calcium ionophore A23187; but to a lesser extent. In vitro,
activated by SQSTM1. Inhibited by diterpenoid alkaloid
noroxoaconitine. {ECO:0000269|PubMed:20640477,
ECO:0000269|PubMed:9480836}.
-!- SUBUNIT: Interacts with SQSTM1 (By similarity). Interacts with
ERK3/MAPK6 and ERK4/MAPK4 (via FRIEDE motif); the interaction is
direct. Interacts with YWHAE; the interaction prevents
phosphorylation of HSP27/HSPB1 leading to disrupt F-actin
polymerization. {ECO:0000250, ECO:0000269|PubMed:15538386,
ECO:0000269|PubMed:15577943, ECO:0000269|PubMed:16973613,
ECO:0000269|PubMed:18248330, ECO:0000269|PubMed:18720373,
ECO:0000269|PubMed:19473979}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocates to the
cytoplasm following phosphorylation and activation. Interaction
with ERK3/MAPK6 or ERK4/MAPK4 and phosphorylation at Thr-182,
activates the protein kinase activity, followed by translocation
to the cytoplasm. Phosphorylation by PKA/PRKACA at Ser-115 also
induces nuclear export.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=MK-5 type 1;
IsoId=O54992-1; Sequence=Displayed;
Name=2; Synonyms=MK-5 type 3;
IsoId=O54992-2; Sequence=VSP_011600;
Name=3; Synonyms=MK-5 type 4;
IsoId=O54992-3; Sequence=VSP_011599;
Name=4; Synonyms=MK-5 type 5;
IsoId=O54992-4; Sequence=VSP_011599, VSP_011598;
Name=5; Synonyms=MK-5 type 2;
IsoId=O54992-5; Sequence=VSP_011598;
-!- TISSUE SPECIFICITY: Expressed ubiquitously.
{ECO:0000269|PubMed:9480836}.
-!- PTM: Phosphorylated on Thr-182 ERK3/MAPK6 or ERK4/MAPK4; which is
the regulatory phosphorylation site and is located on the T-
loop/loop 12, leading to activation. Phosphorylation at Thr-182 by
p38-alpha/MAPK14, p38-beta/MAPK11 is subject to debate.
Phosphorylated at Ser-115 by PKA/PRKACA, leading to localization
to the cytoplasm. Autophosphorylated.
{ECO:0000269|PubMed:15538386, ECO:0000269|PubMed:15577943,
ECO:0000269|PubMed:20734105, ECO:0000269|PubMed:9480836}.
-!- DISRUPTION PHENOTYPE: Phenotypes are different depending on
reports. According to a first report, mice are viable and fertile
and do not show changes in tissue morphology and behavior: they
exhibit the same susceptibility to LPS-induced endotoxic shock as
wild-type animals and do not show the defects in LPS-induced
biosynthesis of inflammatory cytokines known to occur with
Mapkapk2-deficient animals (PubMed:14560018). According to another
report, both homozygous and heterozygous mutant mice are highly
susceptible to skin carcinogenesis induced by DMBA
(PubMed:17254968). According to a third report, mutant show
embryonic lethality around E11 in a C57BL/6 background
(PubMed:15538386). {ECO:0000269|PubMed:14560018,
ECO:0000269|PubMed:15538386, ECO:0000269|PubMed:17254968}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. {ECO:0000305}.
-!- CAUTION: The role of p38 MAPK kinases is unclear in
phosphorylation and activation of Mapkapk5. According to some
reports, it interacts and is phosphorylated by p38-alpha/MAPK14
and p38-beta/MAPK11 (PubMed:9480836). According to other reports,
it is not activated by p38-alpha/MAPK14 and p38-beta/MAPK11
(PubMed:14560018). An explanation for these discrepancies, might
be that the interaction with p38 MAPK kinases is weak and occurs
only under specific conditions. {ECO:0000305|PubMed:14560018,
ECO:0000305|PubMed:9480836}.
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EMBL; AF039840; AAC40047.1; -; mRNA.
EMBL; AY533679; AAS22330.1; -; mRNA.
EMBL; AY533680; AAS22331.2; -; mRNA.
EMBL; AY533681; AAS22332.1; -; mRNA.
EMBL; AY533682; AAS22333.1; -; mRNA.
EMBL; AC155316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC019184; AAH19184.1; -; mRNA.
CCDS; CCDS39248.1; -. [O54992-1]
PIR; JC5952; JC5952.
RefSeq; NP_034895.1; NM_010765.2. [O54992-1]
UniGene; Mm.272206; -.
ProteinModelPortal; O54992; -.
SMR; O54992; -.
BioGrid; 201309; 2.
IntAct; O54992; 2.
STRING; 10090.ENSMUSP00000031410; -.
iPTMnet; O54992; -.
PhosphoSitePlus; O54992; -.
MaxQB; O54992; -.
PaxDb; O54992; -.
PeptideAtlas; O54992; -.
PRIDE; O54992; -.
Ensembl; ENSMUST00000031410; ENSMUSP00000031410; ENSMUSG00000029454. [O54992-1]
Ensembl; ENSMUST00000111782; ENSMUSP00000107412; ENSMUSG00000029454. [O54992-4]
Ensembl; ENSMUST00000111783; ENSMUSP00000107413; ENSMUSG00000029454. [O54992-5]
Ensembl; ENSMUST00000111786; ENSMUSP00000107416; ENSMUSG00000029454. [O54992-3]
Ensembl; ENSMUST00000200170; ENSMUSP00000143668; ENSMUSG00000072647. [O54992-5]
GeneID; 17165; -.
KEGG; mmu:17165; -.
UCSC; uc008zjq.1; mouse. [O54992-1]
UCSC; uc008zjr.1; mouse. [O54992-3]
UCSC; uc008zjs.1; mouse. [O54992-4]
CTD; 8550; -.
MGI; MGI:1333110; Mapkapk5.
eggNOG; KOG0604; Eukaryota.
eggNOG; ENOG410XP8F; LUCA.
GeneTree; ENSGT00900000140876; -.
GeneTree; ENSGT00910000144019; -.
HOGENOM; HOG000233031; -.
HOVERGEN; HBG106948; -.
InParanoid; O54992; -.
KO; K04442; -.
OMA; IHDRENG; -.
OrthoDB; EOG091G14PL; -.
PhylomeDB; O54992; -.
TreeFam; TF312891; -.
Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
ChiTaRS; Mapkapk5; mouse.
PRO; PR:O54992; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000029454; Expressed in 29 organ(s), highest expression level in embryo.
CleanEx; MM_MAPKAPK5; -.
ExpressionAtlas; O54992; baseline and differential.
Genevisible; O54992; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:MGI.
GO; GO:0032156; C:septin cytoskeleton; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
GO; GO:0051019; F:mitogen-activated protein kinase binding; IPI:UniProtKB.
GO; GO:0002039; F:p53 binding; IDA:UniProtKB.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
GO; GO:0032007; P:negative regulation of TOR signaling; IDA:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0060999; P:positive regulation of dendritic spine development; IMP:MGI.
GO; GO:0051973; P:positive regulation of telomerase activity; ISO:MGI.
GO; GO:1904355; P:positive regulation of telomere capping; ISO:MGI.
GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:MGI.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0007265; P:Ras protein signal transduction; IMP:UniProtKB.
GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
GO; GO:0090400; P:stress-induced premature senescence; IMP:UniProtKB.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Coiled coil; Complete proteome;
Cytoplasm; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Transferase;
Tumor suppressor.
CHAIN 1 473 MAP kinase-activated protein kinase 5.
/FTId=PRO_0000086297.
DOMAIN 22 304 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 28 36 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COILED 409 440 {ECO:0000255}.
ACT_SITE 148 148 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 51 51 ATP. {ECO:0000305}.
MOD_RES 115 115 Phosphoserine; by PKA.
{ECO:0000269|PubMed:20734105}.
MOD_RES 182 182 Phosphothreonine; by MAPK11, MAPK14,
MAPK4, MAPK6 and PKA.
{ECO:0000269|PubMed:15538386,
ECO:0000269|PubMed:15577943}.
MOD_RES 212 212 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IW41}.
MOD_RES 354 354 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IW41}.
VAR_SEQ 13 161 Missing (in isoform 3 and isoform 4).
{ECO:0000303|Ref.2}.
/FTId=VSP_011599.
VAR_SEQ 344 408 DLKVSLKPLHSVNNPILRKRKLLGTKPKDGIYIHDHENGTE
DSNVALEKLRDVIAQCILPQAGKG -> E (in isoform
2). {ECO:0000303|Ref.2}.
/FTId=VSP_011600.
VAR_SEQ 407 408 Missing (in isoform 4 and isoform 5).
{ECO:0000303|Ref.2}.
/FTId=VSP_011598.
MUTAGEN 51 51 K->E: No p38-alpha/MAPK14-, p38-
beta/MAPK11-, ERK3/MAPK6-, ERK4/MAPK4-
induced activation.
{ECO:0000269|PubMed:15538386,
ECO:0000269|PubMed:17254968,
ECO:0000269|PubMed:21336308,
ECO:0000269|PubMed:9480836}.
MUTAGEN 51 51 K->R,M: Kinase defective mutant,
abolishes activity.
{ECO:0000269|PubMed:15538386,
ECO:0000269|PubMed:17254968,
ECO:0000269|PubMed:21336308,
ECO:0000269|PubMed:9480836}.
MUTAGEN 115 115 S->A: Impairs shuttling to the cytoplasm.
{ECO:0000269|PubMed:20734105}.
MUTAGEN 115 115 S->D: Mimicks phosphorylation state,
lesding to localization to the cytoplasm.
{ECO:0000269|PubMed:20734105}.
MUTAGEN 182 182 T->A: Impairs protein kinase activity and
shuttling to the cytoplasm.
{ECO:0000269|PubMed:15538386,
ECO:0000269|PubMed:15577943,
ECO:0000269|PubMed:17254968,
ECO:0000269|PubMed:20640477}.
MUTAGEN 337 337 L->A: Constitutive active mutant. In a
knockin model, mouse display increased
amounts of head dips and open arm time on
the maze, compared to littermate
controls. In addition, they also explore
further into the open arm on the elevated
plus maze and are less active in the
closed arm compared to littermate
controls. Male knockin mice display no
differences in anxiety, but their
locomotor activity increases compared to
non-transgenic littermates.
{ECO:0000269|PubMed:17997833}.
SEQUENCE 473 AA; 54152 MW; 45441A735075B247 CRC64;
MSEDSDMEKA IKETSILEEY SINWTQKLGA GISGPVRVCV KKSTQERFAL KILLDRPKAR
NEVRLHMMCA THPNIVQIIE VFANSVQFPH ESSPRARLLI VMEMMEGGEL FHRISQHRHF
TEKQASQVTK QIALALQHCH LLNIAHRDLK PENLLFKDNS LDAPVKLCDF GFAKVDQGDL
MTPQFTPYYV APQVLEAQRR HQKEKSGIIP TSPTPYTYNK SCDLWSLGVI IYVMLCGYPP
FYSKHHSRTI PKDMRKKIMT GSFEFPEEEW SQISEMAKDV VRKLLKVKPE ERLTIEGVLD
HPWLNSTEAL DNVLPSAQLM MDKAVVAGIQ QAHAEQLANM RIQDLKVSLK PLHSVNNPIL
RKRKLLGTKP KDGIYIHDHE NGTEDSNVAL EKLRDVIAQC ILPQAGKGEN EDEKLNEVMQ
EAWKYNRECK LLRDALQSFS WNGRGFTDKV DRLKLAEVVK QVIEEQTLPH EPQ


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