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MAP kinase-activated protein kinase 2 (MAPK-activated protein kinase 2) (MAPKAP kinase 2) (MAPKAP-K2) (MAPKAPK-2) (MK-2) (MK2) (EC 2.7.11.1) (Fragment)

 MAPK2_RABIT             Reviewed;         366 AA.
P49139; G1T708;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
25-JAN-2012, sequence version 2.
30-AUG-2017, entry version 106.
RecName: Full=MAP kinase-activated protein kinase 2;
Short=MAPK-activated protein kinase 2;
Short=MAPKAP kinase 2;
Short=MAPKAP-K2;
Short=MAPKAPK-2;
Short=MK-2;
Short=MK2;
EC=2.7.11.1;
Flags: Fragment;
Name=MAPKAPK2;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Thorbecke;
The Genome Sequencing Platform;
Di Palma F., Heiman D., Young S., Gnerre S., Johnson J., Lander E.S.,
Lindblad-Toh K.;
"Genome Sequence of Oryctolagus cuniculus (European rabbit).";
Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-256.
STRAIN=New Zealand white; TISSUE=Skeletal muscle;
PubMed=8280084; DOI=10.1042/bj2960843;
Stokoe D., Caudwell B., Cohen P.T.W., Cohen P.;
"The substrate specificity and structure of mitogen-activated protein
(MAP) kinase-activated protein kinase-2.";
Biochem. J. 296:843-849(1993).
[3]
FUNCTION IN PHOSPHORYLATION OF HSPB1.
PubMed=1332886; DOI=10.1016/0014-5793(92)81216-9;
Stokoe D., Engel K., Campbell D.G., Cohen P., Gaestel M.;
"Identification of MAPKAP kinase 2 as a major enzyme responsible for
the phosphorylation of the small mammalian heat shock proteins.";
FEBS Lett. 313:307-313(1992).
[4]
PARTIAL PROTEIN SEQUENCE, FUNCTION, AND PHOSPHORYLATION AT THR-300.
STRAIN=New Zealand white;
PubMed=1327754;
Stokoe D., Campbell D.G., Nakielny S., Hidaka H., Leevers S.J.,
Marshall C., Cohen P.;
"MAPKAP kinase-2; a novel protein kinase activated by mitogen-
activated protein kinase.";
EMBO J. 11:3985-3994(1992).
-!- FUNCTION: Stress-activated serine/threonine-protein kinase
involved in cytokine production, endocytosis, reorganization of
the cytoskeleton, cell migration, cell cycle control, chromatin
remodeling, DNA damage response 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. Phosphorylates ALOX5,
CDC25B, CDC25C, CEP131, ELAVL1, HNRNPA0, HSP27/HSPB1, KRT18,
KRT20, LIMK1, LSP1, PABPC1, PARN, PDE4A, RCSD1, RPS6KA3, TAB3 and
TTP/ZFP36. Phosphorylates HSF1; leading to the interaction with
HSP90 proteins and inhibiting HSF1 homotrimerization, DNA-binding
and transactivation activities (By similarity). Mediates
phosphorylation of HSP27/HSPB1 in response to stress, leading to
dissociation of HSP27/HSPB1 from large small heat-shock protein
(sHsps) oligomers and impairment of 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 ELAVL1, HNRNPA0, PABPC1
and 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 transcripts.
Phosphorylates CEP131 in response to cellular stress following
ultraviolet irradiation which promotes binding of CEP131 to 14-3-3
proteins and inhibits formation of novel centriolar satellites (By
similarity). Also involved in late G2/M checkpoint following DNA
damage through a process of post-transcriptional mRNA
stabilization: following DNA damage, relocalizes from nucleus to
cytoplasm and phosphorylates HNRNPA0 and PARN, leading to
stabilization of GADD45A mRNA. Involved in toll-like receptor
signaling pathway (TLR) in dendritic cells: required for acute
TLR-induced macropinocytosis by phosphorylating and activating
RPS6KA3. {ECO:0000250|UniProtKB:P49137,
ECO:0000269|PubMed:1327754, ECO:0000269|PubMed:1332886}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Activated following phosphorylation by p38-
alpha/MAPK14 following various stresses. Inhibited following
sumoylation. Specifically inhibited by pyrrolopyridine inhibitors
(By similarity). {ECO:0000250}.
-!- SUBUNIT: Heterodimer with p38-alpha/MAPK14; this heterodimer forms
a stable complex: molecules are positioned 'face to face' so that
the ATP-binding sites of both kinases are at the heterodimer
interface. Interacts with PHC2. Interacts with HSF1.
{ECO:0000250|UniProtKB:P49137}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P49137}.
Nucleus {ECO:0000250|UniProtKB:P49137}. Note=Phosphorylation and
subsequent activation releases the autoinhibitory helix, resulting
in the export from the nucleus into the cytoplasm.
{ECO:0000250|UniProtKB:P49137}.
-!- PTM: Sumoylation inhibits the protein kinase activity.
{ECO:0000250|UniProtKB:P49137}.
-!- PTM: Phosphorylated and activated by MAP kinase p38-alpha/MAPK14
at Thr-188, Ser-238 and Thr-300. {ECO:0000305|PubMed:1327754}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; X75345; CAA53093.1; -; mRNA.
EMBL; AAGW02025411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; S39794; S39794.
UniGene; Ocu.3281; -.
SMR; P49139; -.
STRING; 9986.ENSOCUP00000012250; -.
iPTMnet; P49139; -.
eggNOG; KOG0604; Eukaryota.
eggNOG; ENOG410XP8F; LUCA.
HOVERGEN; HBG106948; -.
InParanoid; P49139; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; ISS:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0031572; P:G2 DNA damage checkpoint; ISS:UniProtKB.
GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
GO; GO:0044351; P:macropinocytosis; ISS:UniProtKB.
GO; GO:0032675; P:regulation of interleukin-6 production; ISS:UniProtKB.
GO; GO:0032680; P:regulation of tumor necrosis factor production; ISS:UniProtKB.
GO; GO:0034097; P:response to cytokine; ISS:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; ISS:UniProtKB.
GO; GO:0002224; P:toll-like receptor signaling pathway; ISS:UniProtKB.
Gene3D; 4.10.1170.10; -; 1.
InterPro; IPR011009; Kinase-like_dom.
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;
ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing;
DNA damage; Isopeptide bond; Kinase; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
Transferase; Ubl conjugation.
CHAIN <1 366 MAP kinase-activated protein kinase 2.
/FTId=PRO_0000086290.
DOMAIN 30 291 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 36 44 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 105 107 Staurosporine binding. {ECO:0000250}.
REGION 294 330 Autoinhibitory helix. {ECO:0000250}.
REGION 332 356 p38 MAPK-binding site. {ECO:0000250}.
MOTIF 322 331 Nuclear export signal (NES).
{ECO:0000250}.
MOTIF 337 340 Bipartite nuclear localization signal 1.
{ECO:0000250}.
MOTIF 351 355 Bipartite nuclear localization signal 2.
{ECO:0000250}.
COMPBIAS 1 6 Poly-Pro.
ACT_SITE 152 152 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 59 59 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 188 188 Phosphothreonine; by MAPK14.
{ECO:0000250|UniProtKB:P49137}.
MOD_RES 238 238 Phosphoserine; by MAPK14.
{ECO:0000250|UniProtKB:P49137}.
MOD_RES 294 294 Phosphoserine; by autocatalysis.
{ECO:0000250}.
MOD_RES 300 300 Phosphothreonine; by MAPK14.
{ECO:0000269|PubMed:1327754}.
CROSSLNK 319 319 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CONFLICT 111 111 E -> L (in Ref. 2; CAA53093).
{ECO:0000305}.
CONFLICT 315 315 W -> G (in Ref. 4; AA sequence).
{ECO:0000305}.
NON_TER 1 1
SEQUENCE 366 AA; 42124 MW; F1F86EDE08C42C34 CRC64;
PPPPPPQQFP QFHVRSGLQI KKNAIIDDYK VTSQVLGLGI NGKVLQIFSK KTQEKFALKM
LQDCPKARRE VELHWRASQC PHIVRIVDVY ENLYAGRKCL LIVMECLDGG ELFSRIQDRG
DQAFTEREAS EIMKSIGEAI QYLHSINIAH RDVKPENLLY TSKRPKAILK LTDFGFAKET
TSHNSLTTPC YTPYYVAPEV LGPEKYDKSC DMWSLGVIMY ILLCGYPPFY SNHGLAISPG
MKTRIRMGQY EFPNPEWSEV SEEVKMLIRN LLKTEPTQRM TITEFMNHPW IMQSTKVPQT
PLHTSRVLKE DKERWEDVKE EMTSALATMR VDYEQIKIKK IEDASNPLLL KRRKKARALE
AAALAH


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