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MAP kinase-activated protein kinase 3 (MAPK-activated protein kinase 3) (MAPKAP kinase 3) (MAPKAP-K3) (MAPKAPK-3) (MK-3) (EC 2.7.11.1) (Chromosome 3p kinase) (3pK)

 MAPK3_HUMAN             Reviewed;         382 AA.
Q16644; B5BU67;
06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
23-MAY-2018, entry version 164.
RecName: Full=MAP kinase-activated protein kinase 3;
Short=MAPK-activated protein kinase 3;
Short=MAPKAP kinase 3;
Short=MAPKAP-K3;
Short=MAPKAPK-3;
Short=MK-3;
EC=2.7.11.1;
AltName: Full=Chromosome 3p kinase;
Short=3pK;
Name=MAPKAPK3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
PHOSPHORYLATION.
PubMed=8626550; DOI=10.1074/jbc.271.14.8488;
McLaughlin M.M., Kumar S., McDonnell P.C., Van Horn S., Lee J.C.,
Livi G.P., Young P.R.;
"Identification of mitogen-activated protein (MAP) kinase-activated
protein kinase-3, a novel substrate of CSBP p38 MAP kinase.";
J. Biol. Chem. 271:8488-8492(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND PHOSPHORYLATION BY
MAPK1/ERK2 AND MAPK3/ERK1.
TISSUE=Heart;
PubMed=8622688; DOI=10.1128/MCB.16.3.868;
Sithanandam G., Latif F., Duh F.-M., Bernal R., Smola U., Li H.,
Kuzmin I., Wixler V., Geil L., Shrestha S., Lloyd P.A., Bader S.,
Sekido Y., Tartof K.D., Kashuba V.I., Zabarovsky E.R., Dean M.,
Klein G., Lerman M.I., Minna J.D., Rapp U.R., Allikmets R.;
"3pK, a new mitogen-activated protein kinase-activated protein kinase
located in the small cell lung cancer tumor suppressor gene region.";
Mol. Cell. Biol. 16:868-876(1996).
[3]
ERRATUM.
Sithanandam G., Latif F., Duh F.-M., Bernal R., Smola U., Li H.,
Kuzmin I., Wixler V., Geil L., Shrestha S., Lloyd P.A., Bader S.,
Sekido Y., Tartof K.D., Kashuba V.I., Zabarovsky E.R., Dean M.,
Klein G., Lerman M.I., Minna J.D., Rapp U.R., Allikmets R.;
Mol. Cell. Biol. 16:1880-1880(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon, and Skin;
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).
[7]
CATALYTIC ACTIVITY, AND FUNCTION IN PHOSPHORYLATION OF HSPB1.
PubMed=8774846; DOI=10.1016/0014-5793(96)00816-2;
Clifton A.D., Young P.R., Cohen P.;
"A comparison of the substrate specificity of MAPKAP kinase-2 and
MAPKAP kinase-3 and their activation by cytokines and cellular
stress.";
FEBS Lett. 392:209-214(1996).
[8]
FUNCTION IN PHOSPHORYLATION OF HSPB1.
PubMed=10383393; DOI=10.1074/jbc.274.27.18947;
Rogalla T., Ehrnsperger M., Preville X., Kotlyarov A., Lutsch G.,
Ducasse C., Paul C., Wieske M., Arrigo A.P., Buchner J., Gaestel M.;
"Regulation of Hsp27 oligomerization, chaperone function, and
protective activity against oxidative stress/tumor necrosis factor
alpha by phosphorylation.";
J. Biol. Chem. 274:18947-18956(1999).
[9]
INTERACTION WITH TCF3.
PubMed=10781029; DOI=10.1074/jbc.C901040199;
Neufeld B., Grosse-Wilde A., Hoffmeyer A., Jordan B.W., Chen P.,
Dinev D., Ludwig S., Rapp U.R.;
"Serine/Threonine kinases 3pK and MAPK-activated protein kinase 2
interact with the basic helix-loop-helix transcription factor E47 and
repress its transcriptional activity.";
J. Biol. Chem. 275:20239-20242(2000).
[10]
SUBCELLULAR LOCATION.
PubMed=15302577; DOI=10.1016/j.yexcr.2004.05.027;
Zakowski V., Keramas G., Kilian K., Rapp U.R., Ludwig S.;
"Mitogen-activated 3p kinase is active in the nucleus.";
Exp. Cell Res. 299:101-109(2004).
[11]
FUNCTION, MUTAGENESIS OF LYS-73, AND INTERACTION WITH PHC2 AND BMI1.
PubMed=15563468; DOI=10.1074/jbc.M407155200;
Voncken J.W., Niessen H., Neufeld B., Rennefahrt U., Dahlmans V.,
Kubben N., Holzer B., Ludwig S., Rapp U.R.;
"MAPKAP kinase 3pK phosphorylates and regulates chromatin association
of the polycomb group protein Bmi1.";
J. Biol. Chem. 280:5178-5187(2005).
[12]
FUNCTION IN PHOSPHORYLATION OF TAB3.
PubMed=18021073; DOI=10.1042/BJ20071149;
Mendoza H., Campbell D.G., Burness K., Hastie J., Ronkina N.,
Shim J.H., Arthur J.S., Davis R.J., Gaestel M., Johnson G.L.,
Ghosh S., Cohen P.;
"Roles for TAB1 in regulating the IL-1-dependent phosphorylation of
the TAB3 regulatory subunit and activity of the TAK1 complex.";
Biochem. J. 409:711-722(2008).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
FUNCTION.
PubMed=20599781; DOI=10.1016/j.bcp.2010.06.021;
Ronkina N., Menon M.B., Schwermann J., Tiedje C., Hitti E.,
Kotlyarov A., Gaestel M.;
"MAPKAP kinases MK2 and MK3 in inflammation: complex regulation of TNF
biosynthesis via expression and phosphorylation of tristetraprolin.";
Biochem. Pharmacol. 80:1915-1920(2010).
[15]
REVIEW.
PubMed=18508601; DOI=10.2741/3095;
Ronkina N., Kotlyarov A., Gaestel M.;
"MK2 and MK3--a pair of isoenzymes?";
Front. Biosci. 13:5511-5521(2008).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[18]
TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INVOLVEMENT IN MDPT3,
VARIANT MDPT3 PRO-173, AND CHARACTERIZATION OF VARIANT MDPT3 PRO-173.
PubMed=26744326; DOI=10.1093/hmg/ddv624;
Meunier I., Lenaers G., Bocquet B., Baudoin C., Piro-Megy C.,
Cubizolle A., Quiles M., Jean-Charles A., Cohen S.Y., Merle H.,
Gaudric A., Labesse G., Manes G., Pequignot M., Cazevieille C.,
Dhaenens C.M., Fichard A., Ronkina N., Arthur S.J., Gaestel M.,
Hamel C.P.;
"A dominant mutation in MAPKAPK3, an actor of p38 signaling pathway,
causes a new retinal dystrophy involving Bruch's membrane and retinal
pigment epithelium.";
Hum. Mol. Genet. 25:916-926(2016).
[19]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 33-349 IN COMPLEX WITH
INHIBITOR P4O.
PubMed=19937655; DOI=10.1002/pro.294;
Cheng R., Felicetti B., Palan S., Toogood-Johnson I., Scheich C.,
Barker J., Whittaker M., Hesterkamp T.;
"High-resolution crystal structure of human Mapkap kinase 3 in complex
with a high affinity ligand.";
Protein Sci. 19:168-173(2010).
[20]
X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 33-349 IN COMPLEX WITH
INHIBITOR 5B.
PubMed=21565500; DOI=10.1016/j.bmcl.2011.04.018;
Barf T., Kaptein A., de Wilde S., van der Heijden R., van Someren R.,
Demont D., Schultz-Fademrecht C., Versteegh J., van Zeeland M.,
Seegers N., Kazemier B., van de Kar B., van Hoek M., de Roos J.,
Klop H., Smeets R., Hofstra C., Hornberg J., Oubrie A.;
"Structure-based lead identification of ATP-competitive MK2
inhibitors.";
Bioorg. Med. Chem. Lett. 21:3818-3822(2011).
[21]
VARIANTS [LARGE SCALE ANALYSIS] SER-28; ALA-105 AND TYR-276.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Stress-activated serine/threonine-protein kinase
involved in cytokines production, endocytosis, cell migration,
chromatin remodeling and transcriptional regulation. Following
stress, it is phosphorylated and activated by MAP kinase p38-
alpha/MAPK14, leading to phosphorylation of substrates.
Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S,
where Hyd is a large hydrophobic residue. MAPKAPK2 and MAPKAPK3,
share the same function and substrate specificity, but MAPKAPK3
kinase activity and level in protein expression are lower compared
to MAPKAPK2. Phosphorylates HSP27/HSPB1, KRT18, KRT20, RCSD1,
RPS6KA3, TAB3 and TTP/ZFP36. Mediates phosphorylation of
HSP27/HSPB1 in response to stress, leading to dissociate
HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers
and impair their chaperone activities and ability to protect
against oxidative stress effectively. Involved in inflammatory
response by regulating tumor necrosis factor (TNF) and IL6
production post-transcriptionally: acts by phosphorylating AU-rich
elements (AREs)-binding proteins, such as TTP/ZFP36, leading to
regulate the stability and translation of TNF and IL6 mRNAs.
Phosphorylation of TTP/ZFP36, a major post-transcriptional
regulator of TNF, promotes its binding to 14-3-3 proteins and
reduces its ARE mRNA affinity leading to inhibition of dependent
degradation of ARE-containing transcript. Involved in toll-like
receptor signaling pathway (TLR) in dendritic cells: required for
acute TLR-induced macropinocytosis by phosphorylating and
activating RPS6KA3. Also acts as a modulator of Polycomb-mediated
repression. {ECO:0000269|PubMed:10383393,
ECO:0000269|PubMed:15563468, ECO:0000269|PubMed:18021073,
ECO:0000269|PubMed:20599781, ECO:0000269|PubMed:8626550,
ECO:0000269|PubMed:8774846}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:8774846}.
-!- ENZYME REGULATION: Activated following phosphorylation by p38-
alpha/MAPK14 following various stresses. Inhibited by ligand 5B
(2'-[2-(1,3-benzodioxol-5-yl)pyrimidin-4-yl]-5',6'-
dihydrospiro[piperidine-4,7'-pyrrolo[3,2-c]pyridin]- 4'(1'h)-one)
and ligand P4O (2-[2-(2-fluorophenyl)pyridin-4-yl]-1,5,6,7-
tetrahydro- 4h-pyrrolo[3,2-c]pyridin-4-one), 2 ATP-competitive
inhibitors.
-!- SUBUNIT: Heterodimer with p38-alpha/MAPK14. The heterodimer with
p38-alpha/MAPK14 forms a stable complex: molecules are positioned
'face to face' so that the ATP-binding sites of both kinases are
at the heterodimer interface (By similarity). Interacts with TCF3
and with polycomb proteins, such as PCH2 and BMI1/PCGF4.
{ECO:0000250, ECO:0000269|PubMed:10781029,
ECO:0000269|PubMed:15563468, ECO:0000269|PubMed:19937655,
ECO:0000269|PubMed:21565500}.
-!- INTERACTION:
P27958:- (xeno); NbExp=5; IntAct=EBI-1384657, EBI-6377335;
P04792:HSPB1; NbExp=3; IntAct=EBI-1384657, EBI-352682;
Q16539:MAPK14; NbExp=5; IntAct=EBI-1384657, EBI-73946;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15302577,
ECO:0000269|PubMed:26744326}. Cytoplasm
{ECO:0000269|PubMed:15302577, ECO:0000269|PubMed:26744326}.
Note=Predominantly located in the nucleus, when activated it
translocates to the cytoplasm.
-!- TISSUE SPECIFICITY: Widely expressed, with a higher expression
level observed in heart and skeletal muscle. No expression in
brain. Expressed in the retinal pigment epithelium
(PubMed:26744326). {ECO:0000269|PubMed:26744326,
ECO:0000269|PubMed:8622688, ECO:0000269|PubMed:8626550}.
-!- PTM: Phosphorylated and activated by MAPK1/ERK2 and MAPK3/ERK1.
Phosphorylated and activated by MAP kinase p38-alpha/MAPK14 at
Thr-201, Ser-251 and Thr-313 (By similarity). {ECO:0000250}.
-!- DISEASE: Macular dystrophy, patterned, 3 (MDPT3) [MIM:617111]: A
form of retinal patterned dystrophy, characterized by retinal
pigment epithelium and Bruch's membrane changes resembling a 'dry
desert land'. It begins around the age of 30 and progresses to
retinitis pigmentosa. MDPT3 inheritance is autosomal dominant.
{ECO:0000269|PubMed:26744326}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. {ECO:0000305}.
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EMBL; U43784; AAC50428.1; -; mRNA.
EMBL; U09578; AAD09136.1; -; mRNA.
EMBL; AB451303; BAG70117.1; -; mRNA.
EMBL; CH471055; EAW65131.1; -; Genomic_DNA.
EMBL; BC001662; AAH01662.1; -; mRNA.
EMBL; BC007591; AAH07591.1; -; mRNA.
EMBL; BC010407; AAH10407.1; -; mRNA.
CCDS; CCDS2832.1; -.
PIR; JC6094; JC6094.
RefSeq; NP_001230854.1; NM_001243925.1.
RefSeq; NP_001230855.1; NM_001243926.1.
RefSeq; NP_004626.1; NM_004635.4.
UniGene; Hs.234521; -.
UniGene; Hs.735013; -.
PDB; 3FHR; X-ray; 1.90 A; A=33-349.
PDB; 3FXW; X-ray; 2.00 A; A=33-349.
PDB; 3R1N; X-ray; 2.09 A; A=33-349.
PDB; 3SHE; X-ray; 2.25 A; A=33-349.
PDBsum; 3FHR; -.
PDBsum; 3FXW; -.
PDBsum; 3R1N; -.
PDBsum; 3SHE; -.
ProteinModelPortal; Q16644; -.
SMR; Q16644; -.
BioGrid; 113617; 30.
ELM; Q16644; -.
IntAct; Q16644; 27.
MINT; Q16644; -.
STRING; 9606.ENSP00000350639; -.
BindingDB; Q16644; -.
ChEMBL; CHEMBL4670; -.
GuidetoPHARMACOLOGY; 2095; -.
iPTMnet; Q16644; -.
PhosphoSitePlus; Q16644; -.
BioMuta; MAPKAPK3; -.
DMDM; 74762148; -.
EPD; Q16644; -.
MaxQB; Q16644; -.
PaxDb; Q16644; -.
PeptideAtlas; Q16644; -.
PRIDE; Q16644; -.
DNASU; 7867; -.
Ensembl; ENST00000357955; ENSP00000350639; ENSG00000114738.
Ensembl; ENST00000446044; ENSP00000396467; ENSG00000114738.
Ensembl; ENST00000621469; ENSP00000478922; ENSG00000114738.
GeneID; 7867; -.
KEGG; hsa:7867; -.
UCSC; uc003day.3; human.
CTD; 7867; -.
DisGeNET; 7867; -.
EuPathDB; HostDB:ENSG00000114738.10; -.
GeneCards; MAPKAPK3; -.
HGNC; HGNC:6888; MAPKAPK3.
HPA; HPA058275; -.
MalaCards; MAPKAPK3; -.
MIM; 602130; gene.
MIM; 617111; phenotype.
neXtProt; NX_Q16644; -.
OpenTargets; ENSG00000114738; -.
PharmGKB; PA30632; -.
eggNOG; KOG0604; Eukaryota.
eggNOG; ENOG410XP8F; LUCA.
GeneTree; ENSGT00900000140876; -.
HOGENOM; HOG000233031; -.
HOVERGEN; HBG106948; -.
InParanoid; Q16644; -.
KO; K04444; -.
OMA; RMGQYGF; -.
OrthoDB; EOG091G14PL; -.
PhylomeDB; Q16644; -.
TreeFam; TF312891; -.
Reactome; R-HSA-171007; p38MAPK events.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-450302; activated TAK1 mediates p38 MAPK activation.
SignaLink; Q16644; -.
SIGNOR; Q16644; -.
ChiTaRS; MAPKAPK3; human.
EvolutionaryTrace; Q16644; -.
GeneWiki; MAPKAPK3; -.
GenomeRNAi; 7867; -.
PRO; PR:Q16644; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000114738; -.
CleanEx; HS_MAPKAPK3; -.
ExpressionAtlas; Q16644; baseline and differential.
Genevisible; Q16644; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
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:0004708; F:MAP kinase kinase activity; TAS:ProtInc.
GO; GO:0051019; F:mitogen-activated protein kinase binding; IBA:GO_Central.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0000187; P:activation of MAPK activity; TAS:Reactome.
GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
GO; GO:0044351; P:macropinocytosis; ISS:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:BHF-UCL.
GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
GO; GO:0034097; P:response to cytokine; IDA:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; ISS:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0002224; P:toll-like receptor signaling pathway; ISS:UniProtKB.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
Gene3D; 4.10.1170.10; -; 1.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR027442; MAPKAPK_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Complete proteome; Cytoplasm;
Disease mutation; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Serine/threonine-protein kinase;
Transferase.
CHAIN 1 382 MAP kinase-activated protein kinase 3.
/FTId=PRO_0000086293.
DOMAIN 44 304 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 50 58 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 307 343 Autoinhibitory helix. {ECO:0000250}.
REGION 345 369 p38 MAPK-binding site. {ECO:0000250}.
MOTIF 335 344 Nuclear export signal (NES).
{ECO:0000250}.
MOTIF 350 353 Bipartite nuclear localization signal 1.
{ECO:0000250}.
MOTIF 364 368 Bipartite nuclear localization signal 2.
{ECO:0000250}.
ACT_SITE 166 166 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 73 73 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
MOD_RES 201 201 Phosphothreonine; by MAPK14.
{ECO:0000250|UniProtKB:Q3UMW7}.
MOD_RES 251 251 Phosphoserine; by MAPK14. {ECO:0000250}.
MOD_RES 307 307 Phosphoserine; by autocatalysis.
{ECO:0000250}.
MOD_RES 313 313 Phosphothreonine; by MAPK14.
{ECO:0000250}.
VARIANT 28 28 P -> S (in a glioblastoma multiforme
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040755.
VARIANT 105 105 E -> A (in an ovarian endometrioid
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040756.
VARIANT 173 173 L -> P (in MDPT3; decreased localization
to the nucleus; dbSNP:rs886037913).
{ECO:0000269|PubMed:26744326}.
/FTId=VAR_077085.
VARIANT 276 276 D -> Y (in dbSNP:rs56107897).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040757.
MUTAGEN 73 73 K->M: Higher affinity toward PCH2.
{ECO:0000269|PubMed:15563468}.
HELIX 39 41 {ECO:0000244|PDB:3FHR}.
STRAND 43 53 {ECO:0000244|PDB:3FHR}.
STRAND 56 63 {ECO:0000244|PDB:3FHR}.
TURN 64 66 {ECO:0000244|PDB:3FHR}.
STRAND 69 78 {ECO:0000244|PDB:3FHR}.
HELIX 79 91 {ECO:0000244|PDB:3FHR}.
STRAND 100 108 {ECO:0000244|PDB:3FHR}.
STRAND 111 119 {ECO:0000244|PDB:3FHR}.
HELIX 126 131 {ECO:0000244|PDB:3FHR}.
HELIX 140 159 {ECO:0000244|PDB:3FHR}.
HELIX 169 171 {ECO:0000244|PDB:3FHR}.
STRAND 172 175 {ECO:0000244|PDB:3FHR}.
STRAND 183 185 {ECO:0000244|PDB:3FHR}.
HELIX 218 237 {ECO:0000244|PDB:3FHR}.
TURN 267 269 {ECO:0000244|PDB:3FHR}.
STRAND 271 273 {ECO:0000244|PDB:3R1N}.
HELIX 275 284 {ECO:0000244|PDB:3FHR}.
HELIX 289 291 {ECO:0000244|PDB:3FHR}.
HELIX 295 300 {ECO:0000244|PDB:3FHR}.
HELIX 302 305 {ECO:0000244|PDB:3FHR}.
HELIX 307 309 {ECO:0000244|PDB:3FHR}.
HELIX 317 323 {ECO:0000244|PDB:3FHR}.
HELIX 325 327 {ECO:0000244|PDB:3FHR}.
HELIX 328 343 {ECO:0000244|PDB:3FHR}.
STRAND 344 346 {ECO:0000244|PDB:3SHE}.
SEQUENCE 382 AA; 42987 MW; 405F958B7F54E6F3 CRC64;
MDGETAEEQG GPVPPPVAPG GPGLGGAPGG RREPKKYAVT DDYQLSKQVL GLGVNGKVLE
CFHRRTGQKC ALKLLYDSPK ARQEVDHHWQ ASGGPHIVCI LDVYENMHHG KRCLLIIMEC
MEGGELFSRI QERGDQAFTE REAAEIMRDI GTAIQFLHSH NIAHRDVKPE NLLYTSKEKD
AVLKLTDFGF AKETTQNALQ TPCYTPYYVA PEVLGPEKYD KSCDMWSLGV IMYILLCGFP
PFYSNTGQAI SPGMKRRIRL GQYGFPNPEW SEVSEDAKQL IRLLLKTDPT ERLTITQFMN
HPWINQSMVV PQTPLHTARV LQEDKDHWDE VKEEMTSALA TMRVDYDQVK IKDLKTSNNR
LLNKRRKKQA GSSSASQGCN NQ


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