MAPK3_MOUSE
ID MAPK3_MOUSE Reviewed; 384 AA.
AC Q3UMW7; B0QZU7; E9QNE1; Q3T9E6; Q8K0G3;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=MAP kinase-activated protein kinase 3;
DE Short=MAPK-activated protein kinase 3;
DE Short=MAPKAP kinase 3;
DE Short=MAPKAP-K3;
DE Short=MAPKAPK-3;
DE Short=MK-3;
DE EC=2.7.11.1;
GN Name=Mapkapk3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=NOD; TISSUE=Lung, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND PHOSPHORYLATION AT THR-203.
RX PubMed=17030606; DOI=10.1128/mcb.01456-06;
RA Ronkina N., Kotlyarov A., Dittrich-Breiholz O., Kracht M., Hitti E.,
RA Milarski K., Askew R., Marusic S., Lin L.L., Gaestel M., Telliez J.B.;
RT "The mitogen-activated protein kinase (MAPK)-activated protein kinases MK2
RT and MK3 cooperate in stimulation of tumor necrosis factor biosynthesis and
RT stabilization of p38 MAPK.";
RL Mol. Cell. Biol. 27:170-181(2007).
RN [6]
RP FUNCTION IN PHOSPHORYLATION OF RPS6KA3.
RX PubMed=17906627; DOI=10.1038/ni1517;
RA Zaru R., Ronkina N., Gaestel M., Arthur J.S., Watts C.;
RT "The MAPK-activated kinase Rsk controls an acute Toll-like receptor
RT signaling response in dendritic cells and is activated through two distinct
RT pathways.";
RL Nat. Immunol. 8:1227-1235(2007).
RN [7]
RP ALTERNATIVE SPLICING (ISOFORM 3), SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP THR-203, AND MUTAGENESIS OF THR-203.
RX PubMed=20570725; DOI=10.1016/j.cellsig.2010.05.019;
RA Moise N., Dingar D., Mamarbachi A.M., Villeneuve L.R., Farhat N.,
RA Gaestel M., Khairallah M., Allen B.G.;
RT "Characterization of a novel MK3 splice variant from murine ventricular
RT myocardium.";
RL Cell. Signal. 22:1502-1512(2010).
RN [8]
RP FUNCTION IN PHOSPHORYLATION OF KRT18 AND KRT20.
RX PubMed=20724476; DOI=10.1074/jbc.m110.132357;
RA Menon M.B., Schwermann J., Singh A.K., Franz-Wachtel M., Pabst O.,
RA Seidler U., Omary M.B., Kotlyarov A., Gaestel M.;
RT "p38 MAP kinase and MAPKAP kinases MK2/3 cooperatively phosphorylate
RT epithelial keratins.";
RL J. Biol. Chem. 285:33242-33251(2010).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=26744326; DOI=10.1093/hmg/ddv624;
RA Meunier I., Lenaers G., Bocquet B., Baudoin C., Piro-Megy C., Cubizolle A.,
RA Quiles M., Jean-Charles A., Cohen S.Y., Merle H., Gaudric A., Labesse G.,
RA Manes G., Pequignot M., Cazevieille C., Dhaenens C.M., Fichard A.,
RA Ronkina N., Arthur S.J., Gaestel M., Hamel C.P.;
RT "A dominant mutation in MAPKAPK3, an actor of p38 signaling pathway, causes
RT a new retinal dystrophy involving Bruch's membrane and retinal pigment
RT epithelium.";
RL Hum. Mol. Genet. 25:916-926(2016).
CC -!- FUNCTION: Stress-activated serine/threonine-protein kinase involved in
CC cytokines production, endocytosis, cell migration, chromatin remodeling
CC and transcriptional regulation. Following stress, it is phosphorylated
CC and activated by MAP kinase p38-alpha/MAPK14, leading to
CC phosphorylation of substrates. Phosphorylates serine in the peptide
CC sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue.
CC MAPKAPK2 and MAPKAPK3, share the same function and substrate
CC specificity, but MAPKAPK3 kinase activity and level in protein
CC expression are lower compared to MAPKAPK2. Phosphorylates HSP27/HSPB1,
CC KRT18, KRT20, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Mediates
CC phosphorylation of HSP27/HSPB1 in response to stress, leading to
CC dissociate HSP27/HSPB1 from large small heat-shock protein (sHsps)
CC oligomers and impair their chaperone activities and ability to protect
CC against oxidative stress effectively. Involved in inflammatory response
CC by regulating tumor necrosis factor (TNF) and IL6 production post-
CC transcriptionally: acts by phosphorylating AU-rich elements (AREs)-
CC binding proteins, such as TTP/ZFP36, leading to regulate the stability
CC and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a
CC major post-transcriptional regulator of TNF, promotes its binding to
CC 14-3-3 proteins and reduces its ARE mRNA affinity leading to inhibition
CC of dependent degradation of ARE-containing transcript. Involved in
CC toll-like receptor signaling pathway (TLR) in dendritic cells: required
CC for acute TLR-induced macropinocytosis by phosphorylating and
CC activating RPS6KA3. Also acts as a modulator of Polycomb-mediated
CC repression. {ECO:0000269|PubMed:17906627, ECO:0000269|PubMed:20724476}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- ACTIVITY REGULATION: Activated following phosphorylation by p38-
CC alpha/MAPK14 following various stresses. Inhibited by ligand 5B (2'-[2-
CC (1,3-benzodioxol-5-yl)pyrimidin-4-yl]-5',6'-dihydrospiro[piperidine-
CC 4,7'-pyrrolo[3,2-c]pyridin]- 4'(1'h)-one) and ligand P4O (2-[2-(2-
CC fluorophenyl)pyridin-4-yl]-1,5,6,7-tetrahydro- 4h-pyrrolo[3,2-
CC c]pyridin-4-one), 2 ATP-competitive inhibitors (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer with p38-alpha/MAPK14. The heterodimer with p38-
CC alpha/MAPK14 forms a stable complex: molecules are positioned 'face to
CC face' so that the ATP-binding sites of both kinases are at the
CC heterodimer interface. Interacts with TCF3 and with polycomb proteins,
CC such as PCH2 and BMI1/PCGF4 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus. Cytoplasm.
CC Note=Predominantly located in the nucleus, when activated it
CC translocates to the cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus. Cytoplasm. Note=Localizes
CC throughout the cell. Degraded in response to osmotic stress.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3UMW7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UMW7-2; Sequence=VSP_016386, VSP_016387;
CC Name=3; Synonyms=MK3.2;
CC IsoId=Q3UMW7-3; Sequence=VSP_042175, VSP_042176;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed (at protein level). Isoform
CC 3 is expressed in skeletal muscles and heart.
CC {ECO:0000269|PubMed:17030606}.
CC -!- PTM: Phosphorylated and activated by MAPK1/ERK2 and MAPK3/ERK1 (By
CC similarity). Phosphorylated and activated by MAP kinase p38-
CC alpha/MAPK14 at Thr-201, Ser-251 and Thr-313. Isoform 3 is degraded
CC following phosphorylation at Thr-203. {ECO:0000250,
CC ECO:0000269|PubMed:17030606, ECO:0000269|PubMed:20570725}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice are fertile and do not
CC exhibit behavioral phenotype. Mice do not show decreased production of
CC inflammatory cytokines such as TNF and IL6 upon LPS-stimulation. Mice
CC lacking both Mapkapk2 and Mapkapk3 show further reduction of TNF
CC production, compared to mice lacking only Mapkapk2. These data suggest
CC that Mapkapk3 may function additively in stress-induced cytokine
CC production. MAPKAPK3 knockdown homozygous mice develop Bruch's membrane
CC abnormal thickening and thinning progressing with age
CC (PubMed:26744326). {ECO:0000269|PubMed:17030606,
CC ECO:0000269|PubMed:26744326}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AK087496; BAC39897.1; -; mRNA.
DR EMBL; AK144637; BAE25981.1; -; mRNA.
DR EMBL; AK151881; BAE30767.1; -; mRNA.
DR EMBL; AK172344; BAE42958.1; -; mRNA.
DR EMBL; AK172578; BAE43076.1; -; mRNA.
DR EMBL; AL672070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466560; EDL21175.1; -; Genomic_DNA.
DR EMBL; BC031467; AAH31467.1; -; mRNA.
DR CCDS; CCDS23487.1; -. [Q3UMW7-1]
DR CCDS; CCDS85722.1; -. [Q3UMW7-3]
DR RefSeq; NP_001303620.1; NM_001316691.1. [Q3UMW7-3]
DR RefSeq; NP_849238.1; NM_178907.3. [Q3UMW7-1]
DR RefSeq; XP_006511679.1; XM_006511616.3. [Q3UMW7-1]
DR AlphaFoldDB; Q3UMW7; -.
DR SMR; Q3UMW7; -.
DR BioGRID; 221912; 2.
DR STRING; 10090.ENSMUSP00000035194; -.
DR iPTMnet; Q3UMW7; -.
DR PhosphoSitePlus; Q3UMW7; -.
DR EPD; Q3UMW7; -.
DR MaxQB; Q3UMW7; -.
DR PaxDb; Q3UMW7; -.
DR PeptideAtlas; Q3UMW7; -.
DR PRIDE; Q3UMW7; -.
DR ProteomicsDB; 292016; -. [Q3UMW7-1]
DR ProteomicsDB; 292017; -. [Q3UMW7-2]
DR ProteomicsDB; 292018; -. [Q3UMW7-3]
DR Antibodypedia; 30996; 337 antibodies from 33 providers.
DR DNASU; 102626; -.
DR Ensembl; ENSMUST00000035194; ENSMUSP00000035194; ENSMUSG00000032577. [Q3UMW7-1]
DR Ensembl; ENSMUST00000192054; ENSMUSP00000141342; ENSMUSG00000032577. [Q3UMW7-3]
DR GeneID; 102626; -.
DR KEGG; mmu:102626; -.
DR UCSC; uc009rkx.1; mouse. [Q3UMW7-1]
DR UCSC; uc009rla.1; mouse. [Q3UMW7-2]
DR UCSC; uc012hab.1; mouse. [Q3UMW7-3]
DR CTD; 7867; -.
DR MGI; MGI:2143163; Mapkapk3.
DR VEuPathDB; HostDB:ENSMUSG00000032577; -.
DR eggNOG; KOG0604; Eukaryota.
DR GeneTree; ENSGT00940000154089; -.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q3UMW7; -.
DR OMA; LTIMQFM; -.
DR OrthoDB; 843707at2759; -.
DR PhylomeDB; Q3UMW7; -.
DR TreeFam; TF312891; -.
DR Reactome; R-MMU-171007; p38MAPK events.
DR Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-MMU-450302; activated TAK1 mediates p38 MAPK activation.
DR BioGRID-ORCS; 102626; 2 hits in 76 CRISPR screens.
DR PRO; PR:Q3UMW7; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q3UMW7; protein.
DR Bgee; ENSMUSG00000032577; Expressed in hair follicle and 199 other tissues.
DR ExpressionAtlas; Q3UMW7; baseline and differential.
DR Genevisible; Q3UMW7; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0044351; P:macropinocytosis; IMP:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR GO; GO:0034097; P:response to cytokine; ISS:UniProtKB.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:UniProtKB.
DR GO; GO:0002224; P:toll-like receptor signaling pathway; IMP:UniProtKB.
DR Gene3D; 4.10.1170.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027442; MAPKAPK_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cytoplasm; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..384
FT /note="MAP kinase-activated protein kinase 3"
FT /id="PRO_0000086294"
FT DOMAIN 46..306
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..345
FT /note="Autoinhibitory helix"
FT /evidence="ECO:0000250"
FT REGION 347..371
FT /note="p38 MAPK-binding site"
FT /evidence="ECO:0000250"
FT REGION 359..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 337..346
FT /note="Nuclear export signal (NES)"
FT /evidence="ECO:0000250"
FT MOTIF 352..355
FT /note="Bipartite nuclear localization signal 1"
FT /evidence="ECO:0000250"
FT MOTIF 366..370
FT /note="Bipartite nuclear localization signal 2"
FT /evidence="ECO:0000250"
FT COMPBIAS 370..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 52..60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q16644"
FT MOD_RES 203
FT /note="Phosphothreonine; by MAPK14"
FT /evidence="ECO:0000269|PubMed:17030606,
FT ECO:0000269|PubMed:20570725"
FT MOD_RES 253
FT /note="Phosphoserine; by MAPK14"
FT /evidence="ECO:0000250"
FT MOD_RES 309
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 315
FT /note="Phosphothreonine; by MAPK14"
FT /evidence="ECO:0000250"
FT VAR_SEQ 212..249
FT /note="APEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTG -> GESFACGLHP
FT HCCRML (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016386"
FT VAR_SEQ 238..266
FT /note="LCGFPPFYSNTGQAISPGMKRRIRLGQYS -> NPWWSHRPHSTQPECSRKT
FT KITGMTSRKR (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_042175"
FT VAR_SEQ 250..384
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016387"
FT VAR_SEQ 267..384
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_042176"
FT MUTAGEN 203
FT /note="T->A: Prevents degradation of isoform 3."
FT /evidence="ECO:0000269|PubMed:20570725"
FT CONFLICT 216
FT /note="L -> P (in Ref. 1; BAE25981)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 384 AA; 43293 MW; 7DDE2C8E01BBD244 CRC64;
MDGETAGEKG SLVPPPGALG GSALGGAPAP GVRREPKKYA VTDDYQLSKQ VLGLGVNGKV
LECYHRRSGQ KCALKLLYDS PKARQEVDHH WQASGGPHIV RILDVYENMH HGKRCLLIVM
ECMEGGELFS RIQERGDQAF TEREAAEIMR DIGTAIQFLH SRNIAHRDVK PENLLYTSKE
KDAVLKLTDF GFAKETTQNA LQTPCYTPYY VAPEVLGPEK YDKSCDMWSL GVIMYILLCG
FPPFYSNTGQ AISPGMKRRI RLGQYSFPNP EWLDVSEDAK QLIRLLLKTD PTERLTIMQF
MNHPWINQSM VVPQTPLYTA RVLQEDKDHW DDVKEEMTSA LATMRVDYDQ VKIKDLKTSN
NRLLNKRRKK QAGSSSASQG CNNQ
