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Mitogen-activated protein kinase 13 (MAP kinase 13) (MAPK 13) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 delta) (MAP kinase p38 delta) (Stress-activated protein kinase 4)

 MK13_RAT                Reviewed;         366 AA.
Q9WTY9;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
12-SEP-2018, entry version 132.
RecName: Full=Mitogen-activated protein kinase 13;
Short=MAP kinase 13;
Short=MAPK 13;
EC=2.7.11.24;
AltName: Full=Mitogen-activated protein kinase p38 delta;
Short=MAP kinase p38 delta;
AltName: Full=Stress-activated protein kinase 4;
Name=Mapk13;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10066767; DOI=10.1074/jbc.274.11.7095;
Hu M.C.-T., Wang Y.-P., Mikhail A., Qiu W.R., Tan T.-H.;
"Murine p38-delta mitogen-activated protein kinase, a developmentally
regulated protein kinase that is activated by stress and
proinflammatory cytokines.";
J. Biol. Chem. 274:7095-7102(1999).
[2]
PHOSPHORYLATION, AND FUNCTION.
PubMed=20826544; DOI=10.1096/fj.10-164277;
Leong D.J., Li Y.H., Gu X.I., Sun L., Zhou Z., Nasser P.,
Laudier D.M., Iqbal J., Majeska R.J., Schaffler M.B., Goldring M.B.,
Cardoso L., Zaidi M., Sun H.B.;
"Physiological loading of joints prevents cartilage degradation
through CITED2.";
FASEB J. 25:182-191(2011).
[3]
REVIEW ON FUNCTION.
PubMed=20090411; DOI=10.4161/cc.9.3.10541;
Efimova T.;
"p38delta mitogen-activated protein kinase regulates skin homeostasis
and tumorigenesis.";
Cell Cycle 9:498-505(2010).
[4]
REVIEW ON ACTIVITY REGULATION, AND REVIEW ON FUNCTION.
PubMed=20626350; DOI=10.1042/BJ20100323;
Cuadrado A., Nebreda A.R.;
"Mechanisms and functions of p38 MAPK signalling.";
Biochem. J. 429:403-417(2010).
-!- FUNCTION: Serine/threonine kinase which acts as an essential
component of the MAP kinase signal transduction pathway. MAPK13 is
one of the four p38 MAPKs which play an important role in the
cascades of cellular responses evoked by extracellular stimuli
such as proinflammatory cytokines or physical stress leading to
direct activation of transcription factors such as ELK1 and ATF2.
Accordingly, p38 MAPKs phosphorylate a broad range of proteins and
it has been estimated that they may have approximately 200 to 300
substrates each. MAPK13 is one of the less studied p38 MAPK
isoforms. Some of the targets are downstream kinases such as
MAPKAPK2, which are activated through phosphorylation and further
phosphorylate additional targets. Plays a role in the regulation
of protein translation by phosphorylating and inactivating EEF2K.
Involved in cytoskeletal remodeling through phosphorylation of
MAPT and STMN1. Mediates UV irradiation induced up-regulation of
the gene expression of CXCL14. Plays an important role in the
regulation of epidermal keratinocyte differentiation, apoptosis
and skin tumor development. Phosphorylates the transcriptional
activator MYB in response to stress which leads to rapid MYB
degradation via a proteasome-dependent pathway. MAPK13 also
phosphorylates and down-regulates PRKD1 during regulation of
insulin secretion in pancreatic beta cells.
{ECO:0000269|PubMed:20826544}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ACTIVITY REGULATION: Activated by phosphorylation on threonine and
tyrosine by dual specificity kinases, MAP2K3/MKK3, MAP2K6/MKK6,
MAP2K4/MKK4 and MAP2K7/MKK7. Activation by ultraviolet radiation,
hyperosmotic shock, anisomycin or by TNF-alpha is mediated by
MAP2K3/MKK3. Inhibited by dual specificity phosphatase DUSP1.
-!- SUBUNIT: Interacts with MAPK8IP2. {ECO:0000250}.
-!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
whose phosphorylation activates the MAP kinases.
-!- PTM: Dually phosphorylated on Thr-180 and Tyr-182 by MAP2K3/MKK3,
MAP2K4/MKK4, MAP2K6/MKK6 and MAP2K7/MKK7, which activates the
enzyme. Dephosphorylated by dual specificity phosphatase DUSP1 (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. MAP kinase subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF092534; AAD23376.1; -; mRNA.
UniGene; Rn.207195; -.
ProteinModelPortal; Q9WTY9; -.
SMR; Q9WTY9; -.
STRING; 10116.ENSRNOP00000000621; -.
iPTMnet; Q9WTY9; -.
PhosphoSitePlus; Q9WTY9; -.
PaxDb; Q9WTY9; -.
PRIDE; Q9WTY9; -.
UCSC; RGD:3045; rat.
RGD; 3045; Mapk13.
eggNOG; KOG0660; Eukaryota.
eggNOG; ENOG410XNY0; LUCA.
HOGENOM; HOG000233024; -.
HOVERGEN; HBG014652; -.
InParanoid; Q9WTY9; -.
PhylomeDB; Q9WTY9; -.
BRENDA; 2.7.11.24; 5301.
PRO; PR:Q9WTY9; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IDA:RGD.
GO; GO:0004707; F:MAP kinase activity; IDA:RGD.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0051403; P:stress-activated MAPK cascade; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd07879; STKc_p38delta; 1.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR003527; MAP_kinase_CS.
InterPro; IPR008352; MAPK_p38-like.
InterPro; IPR038785; p38delta.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
Pfam; PF00069; Pkinase; 1.
PRINTS; PR01773; P38MAPKINASE.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS01351; MAPK; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
1: Evidence at protein level;
ATP-binding; Cell cycle; Complete proteome; Kinase;
Nucleotide-binding; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Stress response; Transcription;
Transcription regulation; Transferase.
CHAIN 1 366 Mitogen-activated protein kinase 13.
/FTId=PRO_0000186289.
DOMAIN 25 308 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 31 39 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 180 182 TXY.
ACT_SITE 150 150 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 54 54 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 180 180 Phosphothreonine; by MAP2K3, MAP2K4,
MAP2K6 and MAP2K7.
{ECO:0000250|UniProtKB:O15264}.
MOD_RES 182 182 Phosphotyrosine; by MAP2K3, MAP2K4,
MAP2K6 and MAP2K7.
{ECO:0000250|UniProtKB:O15264}.
MOD_RES 350 350 Phosphoserine.
{ECO:0000250|UniProtKB:O15264}.
SEQUENCE 366 AA; 42051 MW; 09F6E65092F2E8D8 CRC64;
MSLIRKRGFY KQDINKTAWE LPKTYLAPAH VGSGAYGAVC SAIDKRTGEK VAIKKLSRPF
QSEIFAKRAY RELLLLKHMH HENVIGLLDV YTPATSVRNF QDFYLVMPFM QTDLQKIMGM
EFSEEKVQYL VYQMLKGLKY IHSAGIVHRD LKPGNLAVNE DCELKILDFG LARHTDAEMT
GYVVTRWYRA PEVILSWMHY NQTVDIWSVG CIMAEMLTGK TLFKGKDYLD QLTQILKVTG
VPGAEFVQKL KDKAAKSYIQ SLPQSPKKDF TQLFPRASPQ AVDLLDKMLE LDVDKRLTAA
QALAHPLFEP LRDPEEETEA QQPFDDALER ENLSVDEWKQ HIYKEIANFS PIARKDSRRR
SGMKLQ


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