MAPK2_MOUSE
ID MAPK2_MOUSE Reviewed; 386 AA.
AC P49138; Q6P561;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=MAP kinase-activated protein kinase 2;
DE Short=MAPK-activated protein kinase 2;
DE Short=MAPKAP kinase 2;
DE Short=MAPKAP-K2;
DE Short=MAPKAPK-2;
DE Short=MK-2;
DE Short=MK2;
DE EC=2.7.11.1;
GN Name=Mapkapk2; Synonyms=Rps6kc1;
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 [MRNA] OF 2-386.
RC TISSUE=Lung;
RX PubMed=8262198; DOI=10.1016/0014-5793(93)81628-d;
RA Engel K., Plath K., Gaestel M.;
RT "The MAP kinase-activated protein kinase 2 contains a proline-rich SH3-
RT binding domain.";
RL FEBS Lett. 336:143-147(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP FUNCTION IN PHOSPHORYLATION OF HSPB1.
RX PubMed=8093612; DOI=10.1016/s0021-9258(18)53882-5;
RA Jakob U., Gaestel M., Engel K., Buchner J.;
RT "Small heat shock proteins are molecular chaperones.";
RL J. Biol. Chem. 268:1517-1520(1993).
RN [4]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-208 AND THR-320, AND
RP MUTAGENESIS OF THR-208; THR-320; LYS-329 AND TRP-335.
RX PubMed=7592979; DOI=10.1074/jbc.270.45.27213;
RA Engel K., Schultz H., Martin F., Kotlyarov A., Plath K., Hahn M.,
RA Heinemann U., Gaestel M.;
RT "Constitutive activation of mitogen-activated protein kinase-activated
RT protein kinase 2 by mutation of phosphorylation sites and an A-helix
RT motif.";
RL J. Biol. Chem. 270:27213-27221(1995).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10559880; DOI=10.1038/10061;
RA Kotlyarov A., Neininger A., Schubert C., Eckert R., Birchmeier C.,
RA Volk H.D., Gaestel M.;
RT "MAPKAP kinase 2 is essential for LPS-induced TNF-alpha biosynthesis.";
RL Nat. Cell Biol. 1:94-97(1999).
RN [6]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-208 AND THR-320, AND NUCLEAR
RP EXPORT SIGNAL (NES).
RX PubMed=9628873; DOI=10.1093/emboj/17.12.3363;
RA Engel K., Kotlyarov A., Gaestel M.;
RT "Leptomycin B-sensitive nuclear export of MAPKAP kinase 2 is regulated by
RT phosphorylation.";
RL EMBO J. 17:3363-3371(1998).
RN [7]
RP FUNCTION IN PHOSPHORYLATION OF HNRNPA0.
RX PubMed=12456657; DOI=10.1093/emboj/cdf639;
RA Rousseau S., Morrice N., Peggie M., Campbell D.G., Gaestel M., Cohen P.;
RT "Inhibition of SAPK2a/p38 prevents hnRNP A0 phosphorylation by MAPKAP-K2
RT and its interaction with cytokine mRNAs.";
RL EMBO J. 21:6505-6514(2002).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=12052889; DOI=10.1128/mcb.22.13.4827-4835.2002;
RA Kotlyarov A., Yannoni Y., Fritz S., Laass K., Telliez J.B., Pitman D.,
RA Lin L.L., Gaestel M.;
RT "Distinct cellular functions of MK2.";
RL Mol. Cell. Biol. 22:4827-4835(2002).
RN [9]
RP FUNCTION IN PHOSPHORYLATION OF ZFP36.
RX PubMed=14688255; DOI=10.1074/jbc.m310486200;
RA Chrestensen C.A., Schroeder M.J., Shabanowitz J., Hunt D.F., Pelo J.W.,
RA Worthington M.T., Sturgill T.W.;
RT "MAPKAP kinase 2 phosphorylates tristetraprolin on in vivo sites including
RT Ser178, a site required for 14-3-3 binding.";
RL J. Biol. Chem. 279:10176-10184(2004).
RN [10]
RP FUNCTION IN PHOSPHORYLATION OF RCSD1.
RX PubMed=15850461; DOI=10.1042/bj20050387;
RA Eyers C.E., McNeill H., Knebel A., Morrice N., Arthur S.J.C., Cuenda A.,
RA Cohen P.;
RT "The phosphorylation of CapZ-interacting protein (CapZIP) by stress-
RT activated protein kinases triggers its dissociation from CapZ.";
RL Biochem. J. 389:127-135(2005).
RN [11]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
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 [12]
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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [15]
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 [16]
RP FUNCTION IN PHOSPHORYLATION OF PDE4A.
RX PubMed=21323643; DOI=10.1042/bj20101184;
RA MacKenzie K.F., Wallace D.A., Hill E.V., Anthony D.F., Henderson D.J.,
RA Houslay D.M., Arthur J.S., Baillie G.S., Houslay M.D.;
RT "Phosphorylation of cAMP-specific PDE4A5 (phosphodiesterase-4A5) by MK2
RT (MAPKAPK2) attenuates its activation through protein kinase A
RT phosphorylation.";
RL Biochem. J. 435:755-769(2011).
CC -!- FUNCTION: Stress-activated serine/threonine-protein kinase involved in
CC cytokine production, endocytosis, reorganization of the cytoskeleton,
CC cell migration, cell cycle control, chromatin remodeling, DNA damage
CC response and transcriptional regulation. Following stress, it is
CC phosphorylated 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 Phosphorylates ALOX5, CDC25B, CDC25C, CEP131, ELAVL1, HNRNPA0,
CC HSP27/HSPB1, KRT18, KRT20, LIMK1, LSP1, PABPC1, PARN, PDE4A, RCSD1,
CC RPS6KA3, TAB3 and TTP/ZFP36. Phosphorylates HSF1; leading to the
CC interaction with HSP90 proteins and inhibiting HSF1 homotrimerization,
CC DNA-binding and transactivation activities (By similarity). Mediates
CC phosphorylation of HSP27/HSPB1 in response to stress, leading to
CC dissociation of HSP27/HSPB1 from large small heat-shock protein (sHsps)
CC oligomers and impairment of their chaperone activities and ability to
CC protect against oxidative stress effectively. Involved in inflammatory
CC response by regulating tumor necrosis factor (TNF) and IL6 production
CC post-transcriptionally: acts by phosphorylating AU-rich elements
CC (AREs)-binding proteins ELAVL1, HNRNPA0, PABPC1 and TTP/ZFP36, leading
CC to regulation of the stability and translation of TNF and IL6 mRNAs.
CC Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of
CC TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA
CC affinity leading to inhibition of dependent degradation of ARE-
CC containing transcripts. Phosphorylates CEP131 in response to cellular
CC stress following ultraviolet irradiation which promotes binding of
CC CEP131 to 14-3-3 proteins and inhibits formation of novel centriolar
CC satellites (By similarity). Also involved in late G2/M checkpoint
CC following DNA damage through a process of post-transcriptional mRNA
CC stabilization: following DNA damage, relocalizes from nucleus to
CC cytoplasm and phosphorylates HNRNPA0 and PARN, leading to stabilization
CC of GADD45A mRNA. Involved in toll-like receptor signaling pathway (TLR)
CC in dendritic cells: required for acute TLR-induced macropinocytosis by
CC phosphorylating and activating RPS6KA3. {ECO:0000250|UniProtKB:P49137,
CC ECO:0000269|PubMed:10559880, ECO:0000269|PubMed:12456657,
CC ECO:0000269|PubMed:14688255, ECO:0000269|PubMed:15850461,
CC ECO:0000269|PubMed:17906627, ECO:0000269|PubMed:20724476,
CC ECO:0000269|PubMed:21323643, ECO:0000269|PubMed:8093612}.
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 following
CC sumoylation. Specifically inhibited by pyrrolopyridine inhibitors (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer with p38-alpha/MAPK14; this heterodimer forms a
CC stable complex: molecules are positioned 'face to face' so that the
CC ATP-binding sites of both kinases are at the heterodimer interface.
CC Interacts with PHC2. Interacts with HSF1.
CC {ECO:0000250|UniProtKB:P49137}.
CC -!- INTERACTION:
CC P49138; P47811: Mapk14; NbExp=2; IntAct=EBI-298776, EBI-298727;
CC P49138; Q64028: Phc1; NbExp=2; IntAct=EBI-298776, EBI-927346;
CC P49138; Q9QWH1: Phc2; NbExp=5; IntAct=EBI-298776, EBI-642357;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Phosphorylation and
CC subsequent activation releases the autoinhibitory helix, resulting in
CC the export from the nucleus into the cytoplasm.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed (at protein level).
CC {ECO:0000269|PubMed:17030606}.
CC -!- PTM: Sumoylation inhibits the protein kinase activity. {ECO:0000250}.
CC -!- PTM: Phosphorylated and activated by MAP kinase p38-alpha/MAPK14 at
CC Thr-208; Ser-258 and Thr-320. {ECO:0000269|PubMed:7592979,
CC ECO:0000269|PubMed:9628873}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice are fertile and do not
CC exhibit behavioral phenotype. Mice show decreased production of
CC inflammatory cytokines such as TNF and IL6 upon LPS-stimulation.
CC Impaired cytokine production make mice less sensitive to LPS-induced
CC endotoxic shock, but more susceptible to bacterial infection. Moreover,
CC the amount of MAP kinase p38 is significantly reduced in cells and
CC tissues. Mice lacking both Mapkapk2 and Mapkapk3 show further reduction
CC of TNF production. {ECO:0000269|PubMed:10559880,
CC ECO:0000269|PubMed:12052889, ECO:0000269|PubMed:17030606}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; X76850; CAA54183.1; -; mRNA.
DR EMBL; BC063064; AAH63064.1; -; mRNA.
DR CCDS; CCDS15266.1; -.
DR PIR; S78100; S78100.
DR RefSeq; NP_032577.1; NM_008551.2.
DR AlphaFoldDB; P49138; -.
DR BMRB; P49138; -.
DR SMR; P49138; -.
DR BioGRID; 201308; 12.
DR IntAct; P49138; 6.
DR MINT; P49138; -.
DR STRING; 10090.ENSMUSP00000016672; -.
DR BindingDB; P49138; -.
DR ChEMBL; CHEMBL4990; -.
DR iPTMnet; P49138; -.
DR PhosphoSitePlus; P49138; -.
DR EPD; P49138; -.
DR jPOST; P49138; -.
DR PaxDb; P49138; -.
DR PeptideAtlas; P49138; -.
DR PRIDE; P49138; -.
DR ProteomicsDB; 295824; -.
DR Antibodypedia; 4144; 963 antibodies from 47 providers.
DR DNASU; 17164; -.
DR Ensembl; ENSMUST00000016672; ENSMUSP00000016672; ENSMUSG00000016528.
DR GeneID; 17164; -.
DR KEGG; mmu:17164; -.
DR UCSC; uc007cmv.1; mouse.
DR CTD; 9261; -.
DR MGI; MGI:109298; Mapkapk2.
DR VEuPathDB; HostDB:ENSMUSG00000016528; -.
DR eggNOG; KOG0604; Eukaryota.
DR GeneTree; ENSGT00940000157261; -.
DR InParanoid; P49138; -.
DR OMA; CPHIVKI; -.
DR OrthoDB; 843707at2759; -.
DR PhylomeDB; P49138; -.
DR TreeFam; TF312891; -.
DR Reactome; R-MMU-171007; p38MAPK events.
DR Reactome; R-MMU-199920; CREB phosphorylation.
DR Reactome; R-MMU-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-MMU-450302; activated TAK1 mediates p38 MAPK activation.
DR Reactome; R-MMU-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR Reactome; R-MMU-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
DR BioGRID-ORCS; 17164; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Mapkapk2; mouse.
DR PRO; PR:P49138; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P49138; protein.
DR Bgee; ENSMUSG00000016528; Expressed in plantaris and 241 other tissues.
DR ExpressionAtlas; P49138; baseline and differential.
DR Genevisible; P49138; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:UniProtKB.
DR GO; GO:0048839; P:inner ear development; IDA:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0044351; P:macropinocytosis; IMP:UniProtKB.
DR GO; GO:0048255; P:mRNA stabilization; IMP:MGI.
DR GO; GO:0038066; P:p38MAPK cascade; IMP:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; IMP:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0032675; P:regulation of interleukin-6 production; IMP:UniProtKB.
DR GO; GO:0032680; P:regulation of tumor necrosis factor production; IMP:UniProtKB.
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 GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; ISO:MGI.
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 ATP-binding; Cytoplasm; DNA damage; Isopeptide bond; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT CHAIN 1..386
FT /note="MAP kinase-activated protein kinase 2"
FT /id="PRO_0000086289"
FT DOMAIN 50..311
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..350
FT /note="Autoinhibitory helix"
FT REGION 352..376
FT /note="p38 MAPK-binding site"
FT /evidence="ECO:0000250"
FT MOTIF 331..354
FT /note="Nuclear export signal (NES)"
FT MOTIF 342..351
FT /note="Nuclear export signal (NES)"
FT /evidence="ECO:0000250"
FT MOTIF 357..360
FT /note="Bipartite nuclear localization signal 1"
FT MOTIF 371..375
FT /note="Bipartite nuclear localization signal 2"
FT COMPBIAS 8..29
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 56..64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 125..127
FT /ligand="staurosporine"
FT /ligand_id="ChEBI:CHEBI:57491"
FT /evidence="ECO:0000250"
FT MOD_RES 208
FT /note="Phosphothreonine; by MAPK14"
FT /evidence="ECO:0000269|PubMed:7592979,
FT ECO:0000269|PubMed:9628873"
FT MOD_RES 258
FT /note="Phosphoserine; by MAPK14"
FT /evidence="ECO:0000250|UniProtKB:P49137"
FT MOD_RES 314
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 320
FT /note="Phosphothreonine; by MAPK14"
FT /evidence="ECO:0000269|PubMed:7592979,
FT ECO:0000269|PubMed:9628873"
FT CROSSLNK 339
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT MUTAGEN 208
FT /note="T->A: Strong decrease in kinase activity; when
FT associated with A-320."
FT /evidence="ECO:0000269|PubMed:7592979"
FT MUTAGEN 208
FT /note="T->E: Mimicks phosphorylation state and constitutive
FT protein kinase activity; when associated with E-320."
FT /evidence="ECO:0000269|PubMed:7592979"
FT MUTAGEN 320
FT /note="T->A: Strong decrease in kinase activity; when
FT associated with A-208."
FT /evidence="ECO:0000269|PubMed:7592979"
FT MUTAGEN 320
FT /note="T->E: Mimicks phosphorylation state and constitutive
FT protein kinase activity; when associated with E-208."
FT /evidence="ECO:0000269|PubMed:7592979"
FT MUTAGEN 329
FT /note="K->R: Leads to constitutive protein kinase
FT activity."
FT /evidence="ECO:0000269|PubMed:7592979"
FT MUTAGEN 335
FT /note="W->A: Leads to constitutive protein kinase
FT activity."
FT /evidence="ECO:0000269|PubMed:7592979"
FT CONFLICT 2..3
FT /note="LS -> IR (in Ref. 1; CAA54183)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 386 AA; 44050 MW; ED7827641A826BF3 CRC64;
MLSGSPGQTP PAPFPSPPPP APAQPPPPFP QFHVKSGLQI RKNAITDDYK VTSQVLGLGI
NGKVLRIFDK RTQQKFALKM LQDCPKARRE VELHWRASQC PHIVHIVDVY ENLYAGRKCL
LIVMECLDGG ELFSRIQDRG DQAFTEREAS EIMKSIGEAI QYLHSINIAH RDVKPENLLY
TSKRPNAILK LTDFGFAKET TSHNSLTTPC YTPYYVAPEV LGPEKYDKSC DMWSLGVIMY
ILLCGYPPFY SNHGLAISPG MKTRIRMGQY EFPNPEWSEV SEEVKMLIRN LLKTEPTQRM
TITEFMNHPW IMQSTKVPQT PLHTSRVLKE DKERWEDVKE EMTSALATMR VDYEQIKIKK
IEDASNPLLL KRRKKARAVE DAALAH
