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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_HUMAN              Reviewed;         365 AA.
O15264; O14739; O15124; Q5U4A5; Q6FI46; Q9UNU0;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
27-SEP-2017, entry version 180.
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; Synonyms=PRKM13, SAPK4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ENZYME REGULATION.
TISSUE=Pituitary;
PubMed=9218798; DOI=10.1093/emboj/16.12.3563;
Goedert M., Cuenda A., Craxton M., Jakes R., Cohen P.;
"Activation of the novel stress-activated protein kinase SAPK4 by
cytokines and cellular stresses is mediated by SKK3 (MKK6); comparison
of its substrate specificity with that of other SAP kinases.";
EMBO J. 16:3563-3571(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION AT THR-180 AND
TYR-182, MUTAGENESIS OF THR-180 AND TYR-182, ENZYME REGULATION, AND
TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=9374491; DOI=10.1074/jbc.272.48.30122;
Jiang Y., Gram H., Zhao M., New L., Gu J., Feng L., Di Padova F.,
Ulevitch R.J., Han J.;
"Characterization of the structure and function of the fourth member
of p38 group mitogen-activated protein kinases, p38delta.";
J. Biol. Chem. 272:30122-30128(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9295308; DOI=10.1074/jbc.272.38.23668;
Wang X.S., Diener K., Manthey C.L., Wang S.-W., Rosenzweig B.,
Bray J., Delaney J., Cole C., Zukowski M., Yao Z.;
"Molecular cloning and characterization of a novel p38 mitogen-
activated protein kinase.";
J. Biol. Chem. 272:23668-23674(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9207191; DOI=10.1006/bbrc.1997.6849;
Kumar S., McDonnell P.C., Gum R.J., Hand A.T., Lee J.C., Young P.R.;
"Novel homologues of CSBP/p38 MAP kinase: activation, substrate
specificity and sensitivity to inhibition by pyridinyl imidazoles.";
Biochem. Biophys. Res. Commun. 235:533-538(1997).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10727080; DOI=10.3109/10425179909033952;
Herbison C.E., Sayer D.C., Bellgard M., Allcock R.J.N.,
Christiansen F.T., Price P.;
"Structure and polymorphism of two stress-activated protein kinase
genes centromeric of the MHC: SAPK2a and SAPK4.";
DNA Seq. 10:229-243(1999).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[10]
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.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Lung, and Pancreas;
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).
[12]
FUNCTION IN PHOSPHORYLATION OF STMN1.
PubMed=9731215; DOI=10.1006/bbrc.1998.9250;
Parker C.G., Hunt J., Diener K., McGinley M., Soriano B.,
Keesler G.A., Bray J., Yao Z., Wang X.S., Kohno T., Lichenstein H.S.;
"Identification of stathmin as a novel substrate for p38 delta.";
Biochem. Biophys. Res. Commun. 249:791-796(1998).
[13]
TISSUE SPECIFICITY.
PubMed=10201954;
Hale K.K., Trollinger D., Rihanek M., Manthey C.L.;
"Differential expression and activation of p38 mitogen-activated
protein kinase alpha, beta, gamma, and delta in inflammatory cell
lineages.";
J. Immunol. 162:4246-4252(1999).
[14]
INTERACTION WITH MAPK8IP2.
PubMed=11378392; DOI=10.1016/S0960-9822(01)00232-9;
Schoorlemmer J., Goldfarb M.;
"Fibroblast growth factor homologous factors are intracellular
signaling proteins.";
Curr. Biol. 11:793-797(2001).
[15]
FUNCTION, AND ENZYME REGULATION.
PubMed=11500363; DOI=10.1093/emboj/20.16.4360;
Knebel A., Morrice N., Cohen P.;
"A novel method to identify protein kinase substrates: eEF2 kinase is
phosphorylated and inhibited by SAPK4/p38delta.";
EMBO J. 20:4360-4369(2001).
[16]
FUNCTION IN PHOSPHORYLATION OF MAPT.
PubMed=11943212; DOI=10.1016/S0014-5793(02)02460-2;
Buee-Scherrer V., Goedert M.;
"Phosphorylation of microtubule-associated protein tau by stress-
activated protein kinases in intact cells.";
FEBS Lett. 515:151-154(2002).
[17]
FUNCTION IN PHOSPHORYLATION OF MAPT.
PubMed=15632108; DOI=10.1242/jcs.01655;
Feijoo C., Campbell D.G., Jakes R., Goedert M., Cuenda A.;
"Evidence that phosphorylation of the microtubule-associated protein
Tau by SAPK4/p38delta at Thr50 promotes microtubule assembly.";
J. Cell Sci. 118:397-408(2005).
[18]
FUNCTION IN KERATINOCYTE APOPTOSIS.
PubMed=17256148; DOI=10.1007/s00403-006-0727-4;
Kraft C.A., Efimova T., Eckert R.L.;
"Activation of PKCdelta and p38delta MAPK during okadaic acid
dependent keratinocyte apoptosis.";
Arch. Dermatol. Res. 299:71-83(2007).
[19]
FUNCTION IN PHOSPHORYLATION OF MYB.
PubMed=18006338; DOI=10.1016/j.bcmd.2007.09.010;
Pani E., Ferrari S.;
"p38MAPK delta controls c-Myb degradation in response to stress.";
Blood Cells Mol. Dis. 40:388-394(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[21]
DEPHOSPHORYLATION BY DUSP1, AND FUNCTION.
PubMed=18367666; DOI=10.1073/pnas.0801453105;
Zhou X., Ferraris J.D., Dmitrieva N.I., Liu Y., Burg M.B.;
"MKP-1 inhibits high NaCl-induced activation of p38 but does not
inhibit the activation of TonEBP/OREBP: opposite roles of p38alpha and
p38delta.";
Proc. Natl. Acad. Sci. U.S.A. 105:5620-5625(2008).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[23]
FUNCTION.
PubMed=20478268; DOI=10.1016/j.bbrc.2010.05.072;
Ozawa S., Ito S., Kato Y., Kubota E., Hata R.;
"Human p38 delta MAP kinase mediates UV irradiation induced up-
regulation of the gene expression of chemokine BRAK/CXCL14.";
Biochem. Biophys. Res. Commun. 396:1060-1064(2010).
[24]
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).
[25]
REVIEW ON ENZYME 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).
[26]
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).
[27]
X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 2-352.
New York structural genomix research consortium (NYSGXRC);
"Crystal structure of p38delta kinase.";
Submitted (JUN-2009) to the PDB data bank.
[28]
VARIANTS [LARGE SCALE ANALYSIS] LEU-41; VAL-282 AND THR-300.
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: 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:11500363, ECO:0000269|PubMed:11943212,
ECO:0000269|PubMed:15632108, ECO:0000269|PubMed:17256148,
ECO:0000269|PubMed:18006338, ECO:0000269|PubMed:18367666,
ECO:0000269|PubMed:20478268, ECO:0000269|PubMed:9731215}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ENZYME 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.
{ECO:0000269|PubMed:11500363, ECO:0000269|PubMed:9218798,
ECO:0000269|PubMed:9374491}.
-!- SUBUNIT: Interacts with MAPK8IP2. {ECO:0000269|PubMed:11378392}.
-!- INTERACTION:
P21462:FPR1; NbExp=3; IntAct=EBI-2116951, EBI-2869495;
Q15139:PRKD1; NbExp=6; IntAct=EBI-2116951, EBI-1181072;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O15264-1; Sequence=Displayed;
Name=2;
IsoId=O15264-2; Sequence=VSP_056558, VSP_056559;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in testes, pancreas, small
intestine, lung and kidney. Abundant in macrophages, also present
in neutrophils, CD4+ T-cells, and endothelial cells.
{ECO:0000269|PubMed:10201954, ECO:0000269|PubMed:9374491}.
-!- 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.
{ECO:0000269|PubMed:9374491}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. MAP kinase subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MAPK13ID41291ch6p21.html";
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EMBL; Y10488; CAA71512.1; -; mRNA.
EMBL; U93232; AAB87639.1; -; mRNA.
EMBL; AF015256; AAC51758.1; -; mRNA.
EMBL; AF004709; AAC51374.1; -; mRNA.
EMBL; AF092535; AAD23377.1; -; mRNA.
EMBL; AF100546; AAF36772.1; -; mRNA.
EMBL; BT007221; AAP35885.1; -; mRNA.
EMBL; CR536490; CAG38729.1; -; mRNA.
EMBL; Z95152; CAB08438.1; -; Genomic_DNA.
EMBL; CH471081; EAX03874.1; -; Genomic_DNA.
EMBL; CH471081; EAX03875.1; -; Genomic_DNA.
EMBL; BC000433; AAH00433.1; -; mRNA.
EMBL; BC001641; AAH01641.1; -; mRNA.
EMBL; BC004428; AAH04428.1; -; mRNA.
EMBL; BC085196; AAH85196.1; -; mRNA.
CCDS; CCDS4818.1; -. [O15264-1]
PIR; JC5528; JC5528.
RefSeq; NP_002745.1; NM_002754.4. [O15264-1]
UniGene; Hs.178695; -.
PDB; 3COI; X-ray; 2.09 A; A=2-352.
PDB; 4EYJ; X-ray; 2.10 A; A=1-352.
PDB; 4EYM; X-ray; 2.35 A; A=1-352.
PDB; 4MYG; X-ray; 2.59 A; A/B=1-352.
PDB; 4YNO; X-ray; 1.70 A; A=1-352.
PDB; 5EKN; X-ray; 2.59 A; A=1-352.
PDB; 5EKO; X-ray; 2.00 A; A=1-352.
PDBsum; 3COI; -.
PDBsum; 4EYJ; -.
PDBsum; 4EYM; -.
PDBsum; 4MYG; -.
PDBsum; 4YNO; -.
PDBsum; 5EKN; -.
PDBsum; 5EKO; -.
ProteinModelPortal; O15264; -.
SMR; O15264; -.
BioGrid; 111589; 17.
IntAct; O15264; 90.
MINT; MINT-1183220; -.
STRING; 9606.ENSP00000211287; -.
BindingDB; O15264; -.
ChEMBL; CHEMBL2939; -.
DrugBank; DB05157; KC706.
GuidetoPHARMACOLOGY; 1502; -.
iPTMnet; O15264; -.
PhosphoSitePlus; O15264; -.
BioMuta; MAPK13; -.
EPD; O15264; -.
MaxQB; O15264; -.
PaxDb; O15264; -.
PeptideAtlas; O15264; -.
PRIDE; O15264; -.
DNASU; 5603; -.
Ensembl; ENST00000211287; ENSP00000211287; ENSG00000156711. [O15264-1]
Ensembl; ENST00000373766; ENSP00000362871; ENSG00000156711. [O15264-2]
GeneID; 5603; -.
KEGG; hsa:5603; -.
UCSC; uc003ols.5; human. [O15264-1]
CTD; 5603; -.
DisGeNET; 5603; -.
EuPathDB; HostDB:ENSG00000156711.16; -.
GeneCards; MAPK13; -.
HGNC; HGNC:6875; MAPK13.
HPA; CAB025854; -.
HPA; HPA007667; -.
MIM; 602899; gene.
neXtProt; NX_O15264; -.
OpenTargets; ENSG00000156711; -.
PharmGKB; PA30620; -.
eggNOG; KOG0660; Eukaryota.
eggNOG; ENOG410XNY0; LUCA.
GeneTree; ENSGT00550000074271; -.
HOGENOM; HOG000233024; -.
HOVERGEN; HBG014652; -.
InParanoid; O15264; -.
KO; K04441; -.
OMA; EWKQHIY; -.
OrthoDB; EOG091G08QL; -.
PhylomeDB; O15264; -.
TreeFam; TF105100; -.
BRENDA; 2.7.11.24; 2681.
Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
Reactome; R-HSA-171007; p38MAPK events.
Reactome; R-HSA-376172; DSCAM interactions.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
SignaLink; O15264; -.
SIGNOR; O15264; -.
EvolutionaryTrace; O15264; -.
GeneWiki; MAPK13; -.
GenomeRNAi; 5603; -.
PRO; PR:O15264; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000156711; -.
CleanEx; HS_MAPK13; -.
ExpressionAtlas; O15264; baseline and differential.
Genevisible; O15264; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004707; F:MAP kinase activity; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:BHF-UCL.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:BHF-UCL.
GO; GO:0050729; P:positive regulation of inflammatory response; IC:BHF-UCL.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:BHF-UCL.
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:0006970; P:response to osmotic stress; IDA:UniProtKB.
GO; GO:0006950; P:response to stress; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR003527; MAP_kinase_CS.
InterPro; IPR008352; MAPK_p38.
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;
3D-structure; Alternative splicing; ATP-binding; Cell cycle;
Complete proteome; Kinase; Nucleotide-binding; Phosphoprotein;
Polymorphism; Reference proteome; Serine/threonine-protein kinase;
Stress response; Transcription; Transcription regulation; Transferase.
CHAIN 1 365 Mitogen-activated protein kinase 13.
/FTId=PRO_0000186286.
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 47 47 Phosphoserine.
{ECO:0000244|PubMed:18088087}.
MOD_RES 180 180 Phosphothreonine; by MAP2K3, MAP2K4,
MAP2K6 and MAP2K7.
{ECO:0000269|PubMed:9374491}.
MOD_RES 182 182 Phosphotyrosine; by MAP2K3, MAP2K4,
MAP2K6 and MAP2K7.
{ECO:0000269|PubMed:9374491}.
MOD_RES 350 350 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
VAR_SEQ 204 256 VDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKVTGVPGT
EFVQKLNDKAAK -> GQILHPVPATDPQEGFHSAVPTGQP
PGCGPAGEDAGARRGQAPDGRAGPHPSL (in isoform
2). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_056558.
VAR_SEQ 257 364 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_056559.
VARIANT 41 41 S -> L (in dbSNP:rs55776345).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042267.
VARIANT 282 282 A -> V (in dbSNP:rs55990045).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042268.
VARIANT 300 300 A -> T (in dbSNP:rs41270090).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042269.
MUTAGEN 180 180 T->A: Loss of kinase activity.
{ECO:0000269|PubMed:9374491}.
MUTAGEN 182 182 Y->A: Loss of kinase activity.
{ECO:0000269|PubMed:9374491}.
CONFLICT 13 14 DV -> EL (in Ref. 4; AAC51374).
{ECO:0000305}.
CONFLICT 39 39 V -> W (in Ref. 4; AAC51374).
{ECO:0000305}.
CONFLICT 56 56 L -> P (in Ref. 3; AAC51758).
{ECO:0000305}.
CONFLICT 166 166 I -> V (in Ref. 3; AAC51758).
{ECO:0000305}.
CONFLICT 224 224 K -> R (in Ref. 3; AAC51758 and 5;
AAD23377). {ECO:0000305}.
HELIX 4 8 {ECO:0000244|PDB:3COI}.
STRAND 9 14 {ECO:0000244|PDB:4YNO}.
STRAND 17 22 {ECO:0000244|PDB:4YNO}.
STRAND 25 33 {ECO:0000244|PDB:4YNO}.
STRAND 35 44 {ECO:0000244|PDB:4YNO}.
TURN 45 47 {ECO:0000244|PDB:4YNO}.
STRAND 50 56 {ECO:0000244|PDB:4YNO}.
HELIX 63 78 {ECO:0000244|PDB:4YNO}.
STRAND 88 91 {ECO:0000244|PDB:4YNO}.
STRAND 95 97 {ECO:0000244|PDB:4YNO}.
STRAND 104 108 {ECO:0000244|PDB:4YNO}.
STRAND 111 113 {ECO:0000244|PDB:3COI}.
HELIX 114 117 {ECO:0000244|PDB:4YNO}.
HELIX 124 143 {ECO:0000244|PDB:4YNO}.
HELIX 153 155 {ECO:0000244|PDB:4YNO}.
STRAND 156 158 {ECO:0000244|PDB:4YNO}.
STRAND 164 166 {ECO:0000244|PDB:4YNO}.
HELIX 186 188 {ECO:0000244|PDB:4MYG}.
HELIX 191 195 {ECO:0000244|PDB:4YNO}.
TURN 196 198 {ECO:0000244|PDB:4MYG}.
HELIX 204 218 {ECO:0000244|PDB:4YNO}.
STRAND 222 226 {ECO:0000244|PDB:3COI}.
HELIX 228 239 {ECO:0000244|PDB:4YNO}.
HELIX 244 247 {ECO:0000244|PDB:4YNO}.
HELIX 253 261 {ECO:0000244|PDB:4YNO}.
HELIX 270 273 {ECO:0000244|PDB:4YNO}.
HELIX 279 288 {ECO:0000244|PDB:4YNO}.
TURN 293 295 {ECO:0000244|PDB:4YNO}.
HELIX 299 303 {ECO:0000244|PDB:4YNO}.
HELIX 306 308 {ECO:0000244|PDB:4YNO}.
TURN 309 311 {ECO:0000244|PDB:4YNO}.
HELIX 314 316 {ECO:0000244|PDB:4YNO}.
HELIX 327 329 {ECO:0000244|PDB:4YNO}.
HELIX 335 347 {ECO:0000244|PDB:4YNO}.
SEQUENCE 365 AA; 42090 MW; 52E749EDB2973DDF CRC64;
MSLIRKKGFY KQDVNKTAWE LPKTYVSPTH VGSGAYGSVC SAIDKRSGEK VAIKKLSRPF
QSEIFAKRAY RELLLLKHMQ HENVIGLLDV FTPASSLRNF YDFYLVMPFM QTDLQKIMGM
EFSEEKIQYL VYQMLKGLKY IHSAGVVHRD LKPGNLAVNE DCELKILDFG LARHADAEMT
GYVVTRWYRA PEVILSWMHY NQTVDIWSVG CIMAEMLTGK TLFKGKDYLD QLTQILKVTG
VPGTEFVQKL NDKAAKSYIQ SLPQTPRKDF TQLFPRASPQ AADLLEKMLE LDVDKRLTAA
QALTHPFFEP FRDPEEETEA QQPFDDSLEH EKLTVDEWKQ HIYKEIVNFS PIARKDSRRR
SGMKL


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