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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.
17-JUN-2020, entry version 198.
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 ACTIVITY 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, ACTIVITY 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 ACTIVITY 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 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).
[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:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.24;
-!- 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.
{ECO:0000269|PubMed:11500363, ECO:0000269|PubMed:9218798,
ECO:0000269|PubMed:9374491}.
-!- SUBUNIT: Interacts with MAPK8IP2. {ECO:0000269|PubMed:11378392}.
-!- INTERACTION:
O15264; P21462: FPR1; NbExp=3; IntAct=EBI-2116951, EBI-2869495;
O15264; 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;
-!- 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; -; NOT_ANNOTATED_CDS; 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]
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; -.
SMR; O15264; -.
BioGRID; 111589; 18.
IntAct; O15264; 104.
MINT; O15264; -.
STRING; 9606.ENSP00000211287; -.
BindingDB; O15264; -.
ChEMBL; CHEMBL2939; -.
DrugBank; DB12010; Fostamatinib.
DrugBank; DB05157; KC706.
DrugCentral; O15264; -.
GuidetoPHARMACOLOGY; 1502; -.
iPTMnet; O15264; -.
PhosphoSitePlus; O15264; -.
BioMuta; MAPK13; -.
CPTAC; CPTAC-876; -.
CPTAC; CPTAC-877; -.
EPD; O15264; -.
jPOST; O15264; -.
MassIVE; O15264; -.
MaxQB; O15264; -.
PaxDb; O15264; -.
PeptideAtlas; O15264; -.
PRIDE; O15264; -.
ProteomicsDB; 48552; -. [O15264-1]
ProteomicsDB; 65225; -.
Antibodypedia; 2088; 829 antibodies.
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; ENSG00000156711; Low tissue specificity.
MIM; 602899; gene.
neXtProt; NX_O15264; -.
OpenTargets; ENSG00000156711; -.
PharmGKB; PA30620; -.
eggNOG; KOG0660; Eukaryota.
eggNOG; ENOG410XNY0; LUCA.
GeneTree; ENSGT00940000159584; -.
HOGENOM; CLU_000288_181_1_1; -.
InParanoid; O15264; -.
KO; K04441; -.
OMA; TMSSGAM; -.
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; -.
BioGRID-ORCS; 5603; 6 hits in 815 CRISPR screens.
ChiTaRS; MAPK13; human.
EvolutionaryTrace; O15264; -.
GeneWiki; MAPK13; -.
GenomeRNAi; 5603; -.
Pharos; O15264; Tchem.
PRO; PR:O15264; -.
Proteomes; UP000005640; Chromosome 6.
RNAct; O15264; protein.
Bgee; ENSG00000156711; Expressed in left adrenal gland and 186 other tissues.
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:0072740; P:cellular response to anisomycin; IDA:UniProtKB.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:UniProtKB.
GO; GO:0071347; P:cellular response to interleukin-1; IDA:UniProtKB.
GO; GO:1903936; P:cellular response to sodium arsenite; IDA:UniProtKB.
GO; GO:0072709; P:cellular response to sorbitol; IDA:UniProtKB.
GO; GO:0034644; P:cellular response to UV; IDA:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
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:0006970; P:response to osmotic stress; IDA:UniProtKB.
GO; GO:0051403; P:stress-activated MAPK cascade; IDA:UniProtKB.
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;
3D-structure; Alternative splicing; ATP-binding; Cell cycle; Kinase;
Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Stress response; Transcription;
Transcription regulation; Transferase.
CHAIN 1..365
/note="Mitogen-activated protein kinase 13"
/id="PRO_0000186286"
DOMAIN 25..308
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 31..39
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
MOTIF 180..182
/note="TXY"
ACT_SITE 150
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
BINDING 54
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
MOD_RES 47
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18088087"
MOD_RES 180
/note="Phosphothreonine; by MAP2K3, MAP2K4, MAP2K6 and
MAP2K7"
/evidence="ECO:0000269|PubMed:9374491"
MOD_RES 182
/note="Phosphotyrosine; by MAP2K3, MAP2K4, MAP2K6 and
MAP2K7"
/evidence="ECO:0000269|PubMed:9374491"
MOD_RES 350
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19369195"
VAR_SEQ 204..256
/note="VDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKVTGVPGTEFVQKLNDKAA
K -> GQILHPVPATDPQEGFHSAVPTGQPPGCGPAGEDAGARRGQAPDGRAGPHPSL
(in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_056558"
VAR_SEQ 257..364
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_056559"
VARIANT 41
/note="S -> L (in dbSNP:rs55776345)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_042267"
VARIANT 282
/note="A -> V (in dbSNP:rs55990045)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_042268"
VARIANT 300
/note="A -> T (in dbSNP:rs41270090)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_042269"
MUTAGEN 180
/note="T->A: Loss of kinase activity."
/evidence="ECO:0000269|PubMed:9374491"
MUTAGEN 182
/note="Y->A: Loss of kinase activity."
/evidence="ECO:0000269|PubMed:9374491"
CONFLICT 13..14
/note="DV -> EL (in Ref. 4; AAC51374)"
/evidence="ECO:0000305"
CONFLICT 39
/note="V -> W (in Ref. 4; AAC51374)"
/evidence="ECO:0000305"
CONFLICT 56
/note="L -> P (in Ref. 3; AAC51758)"
/evidence="ECO:0000305"
CONFLICT 166
/note="I -> V (in Ref. 3; AAC51758)"
/evidence="ECO:0000305"
CONFLICT 224
/note="K -> R (in Ref. 3; AAC51758 and 5; AAD23377)"
/evidence="ECO:0000305"
HELIX 4..8
/evidence="ECO:0000244|PDB:3COI"
STRAND 9..14
/evidence="ECO:0000244|PDB:4YNO"
STRAND 17..22
/evidence="ECO:0000244|PDB:4YNO"
STRAND 25..33
/evidence="ECO:0000244|PDB:4YNO"
STRAND 35..44
/evidence="ECO:0000244|PDB:4YNO"
TURN 45..47
/evidence="ECO:0000244|PDB:4YNO"
STRAND 50..56
/evidence="ECO:0000244|PDB:4YNO"
HELIX 63..78
/evidence="ECO:0000244|PDB:4YNO"
STRAND 88..91
/evidence="ECO:0000244|PDB:4YNO"
STRAND 95..97
/evidence="ECO:0000244|PDB:4YNO"
STRAND 104..108
/evidence="ECO:0000244|PDB:4YNO"
STRAND 111..113
/evidence="ECO:0000244|PDB:3COI"
HELIX 114..117
/evidence="ECO:0000244|PDB:4YNO"
HELIX 124..143
/evidence="ECO:0000244|PDB:4YNO"
HELIX 153..155
/evidence="ECO:0000244|PDB:4YNO"
STRAND 156..158
/evidence="ECO:0000244|PDB:4YNO"
STRAND 164..166
/evidence="ECO:0000244|PDB:4YNO"
HELIX 186..188
/evidence="ECO:0000244|PDB:4MYG"
HELIX 191..195
/evidence="ECO:0000244|PDB:4YNO"
TURN 196..198
/evidence="ECO:0000244|PDB:4MYG"
HELIX 204..218
/evidence="ECO:0000244|PDB:4YNO"
STRAND 222..226
/evidence="ECO:0000244|PDB:3COI"
HELIX 228..239
/evidence="ECO:0000244|PDB:4YNO"
HELIX 244..247
/evidence="ECO:0000244|PDB:4YNO"
HELIX 253..261
/evidence="ECO:0000244|PDB:4YNO"
HELIX 270..273
/evidence="ECO:0000244|PDB:4YNO"
HELIX 279..288
/evidence="ECO:0000244|PDB:4YNO"
TURN 293..295
/evidence="ECO:0000244|PDB:4YNO"
HELIX 299..303
/evidence="ECO:0000244|PDB:4YNO"
HELIX 306..308
/evidence="ECO:0000244|PDB:4YNO"
TURN 309..311
/evidence="ECO:0000244|PDB:4YNO"
HELIX 314..316
/evidence="ECO:0000244|PDB:4YNO"
HELIX 327..329
/evidence="ECO:0000244|PDB:4YNO"
HELIX 335..347
/evidence="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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WP1493: Carbon assimilation C4 pathway
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WP1653: Galactose metabolism
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WP253: Glycolysis
WP1681: Pantothenate and CoA biosynthesis
WP1694: Pyrimidine metabolism
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP1703: Streptomycin biosynthesis
WP1663: Homologous recombination
WP1567: Glycolysis and Gluconeogenesis
WP1619: Amino sugar and nucleotide sugar metabolism
WP1644: DNA replication
WP1693: Purine metabolism
WP1701: Starch and sucrose metabolism
WP1672: Mismatch repair
WP2292: Chemokine signaling pathway
WP2199: Seed Development
WP1438: Influenza A virus infection
WP1692: Protein export
WP232: G Protein Signaling Pathways
WP525: Mitochondrial Unfolded-Protein Response
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Related Genes :
[MAPK13 PRKM13 SAPK4] 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)
[Mapk13] 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)
[Mapk13 Serk4] 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)
[MAPK14 CSBP CSBP1 CSBP2 CSPB1 MXI2 SAPK2A] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Cytokine suppressive anti-inflammatory drug-binding protein) (CSAID-binding protein) (CSBP) (MAP kinase MXI2) (MAX-interacting protein 2) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha) (Stress-activated protein kinase 2a) (SAPK2a)
[Mapk12 Sapk3] Mitogen-activated protein kinase 12 (MAP kinase 12) (MAPK 12) (EC 2.7.11.24) (Extracellular signal-regulated kinase 6) (ERK-6) (Mitogen-activated protein kinase p38 gamma) (MAP kinase p38 gamma) (Stress-activated protein kinase 3)
[MAPK12 ERK6 SAPK3] Mitogen-activated protein kinase 12 (MAP kinase 12) (MAPK 12) (EC 2.7.11.24) (Extracellular signal-regulated kinase 6) (ERK-6) (Mitogen-activated protein kinase p38 gamma) (MAP kinase p38 gamma) (Stress-activated protein kinase 3)
[MAPK11 PRKM11 SAPK2 SAPK2B] Mitogen-activated protein kinase 11 (MAP kinase 11) (MAPK 11) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 beta) (MAP kinase p38 beta) (p38b) (Stress-activated protein kinase 2b) (SAPK2b) (p38-2)
[Mapk12 Sapk3] Mitogen-activated protein kinase 12 (MAP kinase 12) (MAPK 12) (EC 2.7.11.24) (Extracellular signal-regulated kinase 6) (ERK-6) (Mitogen-activated protein kinase p38 gamma) (MAP kinase p38 gamma) (Stress-activated protein kinase 3)
[Mapk14 Crk1 Csbp1 Csbp2] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (CRK1) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha)
[Mapk14 Csbp1 Csbp2] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (CRK1) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha)
[Mapk11 Prkm11] Mitogen-activated protein kinase 11 (MAP kinase 11) (MAPK 11) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 beta) (MAP kinase p38 beta) (p38B)
[MAPK14 CSBP1 CSBP2] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha)
[mapk14a mapk14] Mitogen-activated protein kinase 14A (MAP kinase 14A) (MAPK 14A) (EC 2.7.11.24) (Mitogen-activated protein kinase p38a) (MAP kinase p38a) (zp38a)
[mapk14b mapk14] Mitogen-activated protein kinase 14B (MAP kinase 14B) (MAPK 14B) (EC 2.7.11.24) (Mitogen-activated protein kinase p38b) (MAP kinase p38b) (zp38b)
[pmk-1 B0218.3] Mitogen-activated protein kinase pmk-1 (EC 2.7.11.24) (Stress-activated protein kinase pmk-1) (p38 MAP kinase 1)
[mapk14b] Mitogen-activated protein kinase 14B (MAP kinase 14B) (MAPK 14B) (EC 2.7.11.24) (Mitogen-activated protein kinase p38b) (MAP kinase p38b) (cp38b)
[pmk-3 F42G8.4] Mitogen-activated protein kinase pmk-3 (EC 2.7.11.24) (Stress-activated protein kinase pmk-3) (p38 MAP kinase 3)
[mapk14a] Mitogen-activated protein kinase 14A (MAP kinase 14A) (MAPK 14A) (EC 2.7.11.24) (Mitogen-activated protein kinase p38a) (MAP kinase p38a) (cp38a)
[p38b CG7393] Mitogen-activated protein kinase p38b (MAP kinase p38b) (MAPK p38b) (EC 2.7.11.24)
[MAPK14 CSBP1] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha) (Stress-activated protein kinase 2a)
[MAPKAPK5 PRAK] MAP kinase-activated protein kinase 5 (MAPK-activated protein kinase 5) (MAPKAP kinase 5) (MAPKAP-K5) (MAPKAPK-5) (MK-5) (MK5) (EC 2.7.11.1) (p38-regulated/activated protein kinase) (PRAK)
[MAPK1 ERK2 PRKM1 PRKM2] Mitogen-activated protein kinase 1 (MAP kinase 1) (MAPK 1) (EC 2.7.11.24) (ERT1) (Extracellular signal-regulated kinase 2) (ERK-2) (MAP kinase isoform p42) (p42-MAPK) (Mitogen-activated protein kinase 2) (MAP kinase 2) (MAPK 2)
[Mapk8 Jnk1 Prkm8] Mitogen-activated protein kinase 8 (MAP kinase 8) (MAPK 8) (EC 2.7.11.24) (Stress-activated protein kinase JNK1) (c-Jun N-terminal kinase 1)
[MAPK3 ERK1 PRKM3] Mitogen-activated protein kinase 3 (MAP kinase 3) (MAPK 3) (EC 2.7.11.24) (ERT2) (Extracellular signal-regulated kinase 1) (ERK-1) (Insulin-stimulated MAP2 kinase) (MAP kinase isoform p44) (p44-MAPK) (Microtubule-associated protein 2 kinase) (p44-ERK1)
[MAP2K6 MEK6 MKK6 PRKMK6 SKK3] Dual specificity mitogen-activated protein kinase kinase 6 (MAP kinase kinase 6) (MAPKK 6) (EC 2.7.12.2) (MAPK/ERK kinase 6) (MEK 6) (Stress-activated protein kinase kinase 3) (SAPK kinase 3) (SAPKK-3) (SAPKK3)
[Mapk8 Jnk1 Prkm8] Mitogen-activated protein kinase 8 (MAP kinase 8) (MAPK 8) (EC 2.7.11.24) (SAPK gamma) (Stress-activated protein kinase JNK1) (c-Jun N-terminal kinase 1) (p54 gamma)
[MAP3K5 ASK1 MAPKKK5 MEKK5] Mitogen-activated protein kinase kinase kinase 5 (EC 2.7.11.25) (Apoptosis signal-regulating kinase 1) (ASK-1) (MAPK/ERK kinase kinase 5) (MEK kinase 5) (MEKK 5)
[MAP3K20 MLTK ZAK HCCS4] Mitogen-activated protein kinase kinase kinase 20 (EC 2.7.11.25) (Human cervical cancer suppressor gene 4 protein) (HCCS-4) (Leucine zipper- and sterile alpha motif-containing kinase) (MLK-like mitogen-activated protein triple kinase) (Mitogen-activated protein kinase kinase kinase MLT) (Mixed lineage kinase-related kinase) (MLK-related kinase) (MRK) (Sterile alpha motif- and leucine zipper-containing kinase AZK)
[MAP4K2 GCK RAB8IP] Mitogen-activated protein kinase kinase kinase kinase 2 (EC 2.7.11.1) (B lymphocyte serine/threonine-protein kinase) (Germinal center kinase) (GC kinase) (MAPK/ERK kinase kinase kinase 2) (MEK kinase kinase 2) (MEKKK 2) (Rab8-interacting protein)
[MAPK10 JNK3 JNK3A PRKM10 SAPK1B] Mitogen-activated protein kinase 10 (MAP kinase 10) (MAPK 10) (EC 2.7.11.24) (MAP kinase p49 3F12) (Stress-activated protein kinase 1b) (SAPK1b) (Stress-activated protein kinase JNK3) (c-Jun N-terminal kinase 3)

Bibliography :
No related Items