GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

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)

 MK14_HUMAN              Reviewed;         360 AA.
Q16539; A6ZJ92; A8K6P4; B0LPH0; B5TY32; O60776; Q13083; Q14084; Q8TDX0;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
12-AUG-2020, entry version 241.
RecName: Full=Mitogen-activated protein kinase 14;
Short=MAP kinase 14;
Short=MAPK 14;
EC=2.7.11.24 {ECO:0000269|PubMed:11010976, ECO:0000269|PubMed:15284239, ECO:0000269|PubMed:7493921};
AltName: Full=Cytokine suppressive anti-inflammatory drug-binding protein;
Short=CSAID-binding protein;
Short=CSBP;
AltName: Full=MAP kinase MXI2;
AltName: Full=MAX-interacting protein 2;
AltName: Full=Mitogen-activated protein kinase p38 alpha;
Short=MAP kinase p38 alpha;
AltName: Full=Stress-activated protein kinase 2a;
Short=SAPK2a;
Name=MAPK14; Synonyms=CSBP, CSBP1, CSBP2, CSPB1, MXI2, SAPK2A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CSBP1 AND CSBP2), AND PARTIAL PROTEIN
SEQUENCE.
TISSUE=Peripheral blood;
PubMed=7997261; DOI=10.1038/372739a0;
Lee J.C., Laydon J.T., McDonnell P.C., Gallagher T.F., Kumar S., Green D.,
McNulty D., Blumenthal M.J., Heys R.J., Landvatter S.W., Strickler J.E.,
McLaughlin M.M., Siemens I.R., Fisher S.M., Livi G.P., White J.R.,
Adams J.L., Young P.R.;
"A protein kinase involved in the regulation of inflammatory cytokine
biosynthesis.";
Nature 372:739-746(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CSBP2).
TISSUE=Liver;
PubMed=7696354; DOI=10.1016/0167-4889(95)00002-a;
Han J., Richter B., Li Z., Kravchenko V.V., Ulevitch R.J.;
"Molecular cloning of human p38 MAP kinase.";
Biochim. Biophys. Acta 1265:224-227(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MXI2).
PubMed=7479834; DOI=10.1073/pnas.92.23.10531;
Zervos A.S., Faccio L., Gatto J.P., Kyriakis J.M., Brent R.;
"Mxi2, a mitogen-activated protein kinase that recognizes and
phosphorylates Max protein.";
Proc. Natl. Acad. Sci. U.S.A. 92:10531-10534(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CSBP2).
TISSUE=B-cell;
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM EXIP), AND ACTIVITY REGULATION.
TISSUE=Renal cell carcinoma;
PubMed=11866441; DOI=10.1006/bbrc.2002.6529;
Sudo T., Yagasaki Y., Hama H., Watanabe N., Osada H.;
"Exip, a new alternative splicing variant of p38 alpha, can induce an
earlier onset of apoptosis in HeLa cells.";
Biochem. Biophys. Res. Commun. 291:838-843(2002).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
PubMed=19906316; DOI=10.1186/1471-2164-10-518;
Wang P., Yu P., Gao P., Shi T., Ma D.;
"Discovery of novel human transcript variants by analysis of intronic
single-block EST with polyadenylation site.";
BMC Genomics 10:518-518(2009).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CSBP2).
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.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CSBP2).
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
[11]
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).
[12]
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.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CSBP2).
TISSUE=Placenta;
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).
[14]
PROTEIN SEQUENCE OF 2-10.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass spectrometric
identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[15]
PROTEIN SEQUENCE OF 174-186.
PubMed=7923354; DOI=10.1016/0092-8674(94)90278-x;
Freshney N.W., Rawlinson L., Guesdon F., Jones E., Cowley S., Hsuan J.,
Saklatvala J.;
"Interleukin-1 activates a novel protein kinase cascade that results in the
phosphorylation of Hsp27.";
Cell 78:1039-1049(1994).
[16]
PHOSPHORYLATION AT THR-180 AND TYR-182, ACTIVITY REGULATION, AND
SUBCELLULAR LOCATION.
PubMed=7535770; DOI=10.1074/jbc.270.13.7420;
Raingeaud J., Gupta S., Rogers J.S., Dickens M., Han J., Ulevitch R.J.,
Davis R.J.;
"Pro-inflammatory cytokines and environmental stress cause p38 mitogen-
activated protein kinase activation by dual phosphorylation on tyrosine and
threonine.";
J. Biol. Chem. 270:7420-7426(1995).
[17]
MUTAGENESIS OF ALA-34; LYS-53; ASP-168; THR-175; THR-180 AND TYR-182, AND
CATALYTIC ACTIVITY.
PubMed=7493921; DOI=10.1074/jbc.270.49.29043;
Kumar S., McLaughlin M.M., McDonnell P.C., Lee J.C., Livi G.P., Young P.R.;
"Human mitogen-activated protein kinase CSBP1, but not CSBP2, complements a
hog1 deletion in yeast.";
J. Biol. Chem. 270:29043-29046(1995).
[18]
PHOSPHORYLATION BY MAP2K3/MKK3 AND MAP2K6/MKK6, AND ACTIVITY REGULATION.
PubMed=8622669; DOI=10.1128/mcb.16.3.1247;
Raingeaud J., Whitmarsh A.J., Barrett T., Derijard B., Davis R.J.;
"MKK3- and MKK6-regulated gene expression is mediated by the p38 mitogen-
activated protein kinase signal transduction pathway.";
Mol. Cell. Biol. 16:1247-1255(1996).
[19]
FUNCTION IN ACTIVATION OF RPS6KA5/MSK1.
PubMed=9687510; DOI=10.1093/emboj/17.15.4426;
Deak M., Clifton A.D., Lucocq J.M., Alessi D.R.;
"Mitogen- and stress-activated protein kinase-1 (MSK1) is directly
activated by MAPK and SAPK2/p38, and may mediate activation of CREB.";
EMBO J. 17:4426-4441(1998).
[20]
FUNCTION IN PHOSPHORYLATION OF ATF2; ELK1 AND MBP, AND ACTIVITY REGULATION.
PubMed=9430721; DOI=10.1074/jbc.273.3.1741;
Enslen H., Raingeaud J., Davis R.J.;
"Selective activation of p38 mitogen-activated protein (MAP) kinase
isoforms by the MAP kinase kinases MKK3 and MKK6.";
J. Biol. Chem. 273:1741-1748(1998).
[21]
INTERACTION WITH RPS6KA4, FUNCTION IN PHOSPHORYLATION OF RPS6KA4, AND
SUBCELLULAR LOCATION.
PubMed=9792677; DOI=10.1074/jbc.273.45.29661;
Pierrat B., Correia J.D.S., Mary J.L., Tomas-Zuber M., Lesslauer W.;
"RSK-B, a novel ribosomal S6 kinase family member, is a CREB kinase under
dominant control of p38alpha mitogen-activated protein kinase
(p38alphaMAPK).";
J. Biol. Chem. 273:29661-29671(1998).
[22]
INTERACTION WITH DUSP10, AND ACTIVITY REGULATION.
PubMed=10391943; DOI=10.1074/jbc.274.28.19949;
Tanoue T., Moriguchi T., Nishida E.;
"Molecular cloning and characterization of a novel dual specificity
phosphatase, MKP-5.";
J. Biol. Chem. 274:19949-19956(1999).
[23]
FUNCTION IN PHOSPHORYLATION OF MEF2A.
PubMed=9858528; DOI=10.1128/mcb.19.1.21;
Zhao M., New L., Kravchenko V.V., Kato Y., Gram H., di Padova F.,
Olson E.N., Ulevitch R.J., Han J.-D.;
"Regulation of the MEF2 family of transcription factors by p38.";
Mol. Cell. Biol. 19:21-30(1999).
[24]
FUNCTION IN PHOSPHORYLATION OF MEF2A AND MEF2C.
PubMed=10330143; DOI=10.1128/mcb.19.6.4028;
Yang S.-H., Galanis A., Sharrocks A.D.;
"Targeting of p38 mitogen-activated protein kinases to MEF2 transcription
factors.";
Mol. Cell. Biol. 19:4028-4038(1999).
[25]
FUNCTION.
TISSUE=Hepatoma;
PubMed=10943842; DOI=10.1016/s0092-8674(00)00027-1;
Tamura K., Sudo T., Senftleben U., Dadak A.M., Johnson R., Karin M.;
"Requirement for p38alpha in erythropoietin expression: a role for stress
kinases in erythropoiesis.";
Cell 102:221-231(2000).
[26]
FUNCTION (ISOFORM MXI2), COFACTOR, AND ACTIVITY REGULATION.
PubMed=10838079; DOI=10.1016/s0014-5793(00)01598-2;
Sanz V., Arozarena I., Crespo P.;
"Distinct carboxy-termini confer divergent characteristics to the mitogen-
activated protein kinase p38alpha and its splice isoform Mxi2.";
FEBS Lett. 474:169-174(2000).
[27]
INTERACTION WITH CSNK2A1 AND CSNK2B, AND FUNCTION IN ACTIVATION OF CASEIN
KINASE II.
PubMed=10747897; DOI=10.1074/jbc.m000312200;
Sayed M., Kim S.O., Salh B.S., Issinger O.G., Pelech S.L.;
"Stress-induced activation of protein kinase CK2 by direct interaction with
p38 mitogen-activated protein kinase.";
J. Biol. Chem. 275:16569-16573(2000).
[28]
INTERACTION WITH MA2PK6/MKK6, PHOSPHORYLATION BY MAP2K6/MKK6,
AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-54, AND CATALYTIC ACTIVITY.
PubMed=11010976; DOI=10.1074/jbc.m007835200;
Alonso G., Ambrosino C., Jones M., Nebreda A.R.;
"Differential activation of p38 mitogen-activated protein kinase isoforms
depending on signal strength.";
J. Biol. Chem. 275:40641-40648(2000).
[29]
INTERACTION WITH DUSP1, AND ACTIVITY REGULATION.
PubMed=11278799; DOI=10.1074/jbc.m010966200;
Slack D.N., Seternes O.M., Gabrielsen M., Keyse S.M.;
"Distinct binding determinants for ERK2/p38alpha and JNK map kinases
mediate catalytic activation and substrate selectivity of map kinase
phosphatase-1.";
J. Biol. Chem. 276:16491-16500(2001).
[30]
INTERACTION WITH DUSP16, AND ACTIVITY REGULATION.
PubMed=11359773; DOI=10.1074/jbc.m101981200;
Tanoue T., Yamamoto T., Maeda R., Nishida E.;
"A Novel MAPK phosphatase MKP-7 acts preferentially on JNK/SAPK and p38
alpha and beta MAPKs.";
J. Biol. Chem. 276:26629-26639(2001).
[31]
FUNCTION AS MKNK2 KINASE.
PubMed=11154262; DOI=10.1128/mcb.21.3.743-754.2001;
Scheper G.C., Morrice N.A., Kleijn M., Proud C.G.;
"The mitogen-activated protein kinase signal-integrating kinase Mnk2 is a
eukaryotic initiation factor 4E kinase with high levels of basal activity
in mammalian cells.";
Mol. Cell. Biol. 21:743-754(2001).
[32]
INTERACTION WITH CDC25B AND CDC25C, AND FUNCTION IN PHOSPHORYLATION OF
CDC25B AND CDC25C.
PubMed=11333986; DOI=10.1038/35075107;
Bulavin D.V., Higashimoto Y., Popoff I.J., Gaarde W.A., Basrur V.,
Potapova O., Appella E., Fornace A.J. Jr.;
"Initiation of a G2/M checkpoint after ultraviolet radiation requires p38
kinase.";
Nature 411:102-107(2001).
[33]
INTERACTION WITH TAB1, AUTOPHOSPHORYLATION, ACTIVITY REGULATION, AND
CATALYTIC ACTIVITY.
PubMed=11847341; DOI=10.1126/science.1067289;
Ge B., Gram H., Di Padova F., Huang B., New L., Ulevitch R.J., Luo Y.,
Han J.;
"MAPKK-independent activation of p38alpha mediated by TAB1-dependent
autophosphorylation of p38alpha.";
Science 295:1291-1294(2002).
[34]
MUTAGENESIS OF TYR-69; ASP-176; ASP-177; ALA-320; PHE-327 AND TRP-337.
PubMed=15284239; DOI=10.1074/jbc.m404595200;
Diskin R., Askari N., Capone R., Engelberg D., Livnah O.;
"Active mutants of the human p38alpha mitogen-activated protein kinase.";
J. Biol. Chem. 279:47040-47049(2004).
[35]
FUNCTION IN PHOSPHORYLATION OF S100A9.
PubMed=15905572; DOI=10.4049/jimmunol.174.11.7257;
Lominadze G., Rane M.J., Merchant M., Cai J., Ward R.A., McLeish K.R.;
"Myeloid-related protein-14 is a p38 MAPK substrate in human neutrophils.";
J. Immunol. 174:7257-7267(2005).
[36]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[37]
PHOSPHORYLATION AT TYR-323, AND ACTIVITY REGULATION.
PubMed=15735648; DOI=10.1038/ni1177;
Salvador J.M., Mittelstadt P.R., Guszczynski T., Copeland T.D.,
Yamaguchi H., Appella E., Fornace A.J. Jr., Ashwell J.D.;
"Alternative p38 activation pathway mediated by T cell receptor-proximal
tyrosine kinases.";
Nat. Immunol. 6:390-395(2005).
[38]
INTERACTION WITH TAB1, AUTOPHOSPHORYLATION, AND ACTIVITY REGULATION.
PubMed=15735649; DOI=10.1038/ni1176;
Salvador J.M., Mittelstadt P.R., Belova G.I., Fornace A.J. Jr.,
Ashwell J.D.;
"The autoimmune suppressor Gadd45alpha inhibits the T cell alternative p38
activation pathway.";
Nat. Immunol. 6:396-402(2005).
[39]
INTERACTION WITH SUPT20H.
PubMed=16751104; DOI=10.1016/j.cell.2006.03.048;
Zohn I.E., Li Y., Skolnik E.Y., Anderson K.V., Han J., Niswander L.;
"p38 and a p38-interacting protein are critical for downregulation of E-
cadherin during mouse gastrulation.";
Cell 125:957-969(2006).
[40]
FUNCTION IN STRESS-INDUCED INTERNALIZATION OF EGFR.
PubMed=16932740; DOI=10.1038/sj.emboj.7601297;
Zwang Y., Yarden Y.;
"p38 MAP kinase mediates stress-induced internalization of EGFR:
implications for cancer chemotherapy.";
EMBO J. 25:4195-4206(2006).
[41]
FUNCTION IN PHOSPHORYLATION OF SIAH2, AND ACTIVITY REGULATION.
PubMed=17003045; DOI=10.1074/jbc.m606568200;
Khurana A., Nakayama K., Williams S., Davis R.J., Mustelin T., Ronai Z.;
"Regulation of the ring finger E3 ligase Siah2 by p38 MAPK.";
J. Biol. Chem. 281:35316-35326(2006).
[42]
INTERACTION WITH NP60.
PubMed=16352664; DOI=10.1242/jcs.02699;
Fu J., Yang Z., Wei J., Han J., Gu J.;
"Nuclear protein NP60 regulates p38 MAPK activity.";
J. Cell Sci. 119:115-123(2006).
[43]
FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND UBIQUITINATION.
PubMed=17724032; DOI=10.1074/jbc.m703857200;
Qi X., Pohl N.M., Loesch M., Hou S., Li R., Qin J.Z., Cuenda A., Chen G.;
"p38alpha antagonizes p38gamma activity through c-Jun-dependent ubiquitin-
proteasome pathways in regulating Ras transformation and stress response.";
J. Biol. Chem. 282:31398-31408(2007).
[44]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-263, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[45]
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).
[46]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-16, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the
kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[47]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180 AND TYR-182, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[48]
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).
[49]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180 AND TYR-182, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[50]
FUNCTION IN INHIBITION OF AUTOPHAGY.
PubMed=19893488; DOI=10.1038/emboj.2009.321;
Webber J.L., Tooze S.A.;
"Coordinated regulation of autophagy by p38alpha MAPK through mAtg9 and
p38IP.";
EMBO J. 29:27-40(2010).
[51]
FUNCTION IN PHOSPHORYLATION OF TIAR.
PubMed=20932473; DOI=10.1016/j.molcel.2010.09.018;
Reinhardt H.C., Hasskamp P., Schmedding I., Morandell S., van Vugt M.A.,
Wang X., Linding R., Ong S.E., Weaver D., Carr S.A., Yaffe M.B.;
"DNA damage activates a spatially distinct late cytoplasmic cell-cycle
checkpoint network controlled by MK2-mediated RNA stabilization.";
Mol. Cell 40:34-49(2010).
[52]
INTERACTION WITH ADAM17, AND FUNCTION IN PHOSPHORYLATION OF ADAM17.
PubMed=20188673; DOI=10.1016/j.molcel.2010.01.034;
Xu P., Derynck R.;
"Direct activation of TACE-mediated ectodomain shedding by p38 MAP kinase
regulates EGF receptor-dependent cell proliferation.";
Mol. Cell 37:551-566(2010).
[53]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
ANALYSIS] AT SER-2; THR-180 AND TYR-182, CLEAVAGE OF INITIATOR METHIONINE
[LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[54]
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).
[55]
IDENTIFICATION IN A COMPLEX WITH AKAP13; PKN1; ZAK AND MAP2K3.
PubMed=21224381; DOI=10.1074/jbc.m110.185645;
Cariolato L., Cavin S., Diviani D.;
"A-kinase anchoring protein (AKAP)-Lbc anchors a PKN-based signaling
complex involved in alpha1-adrenergic receptor-induced p38 activation.";
J. Biol. Chem. 286:7925-7937(2011).
[56]
FUNCTION (MICROBIAL INFECTION).
TISSUE=T-cell;
PubMed=21586573; DOI=10.1074/jbc.m111.234062;
Peng H., Wang X., Barnes P.F., Tang H., Townsend J.C., Samten B.;
"The Mycobacterium tuberculosis early secreted antigenic target of 6 kDa
inhibits T cell interferon-gamma production through the p38 mitogen-
activated protein kinase pathway.";
J. Biol. Chem. 286:24508-24518(2011).
[57]
ACETYLATION AT LYS-53 AND LYS-152 BY KAT2B/PCAF AND EP300, AND
DEACETYLATION BY HDAC3.
PubMed=21444723; DOI=10.1128/mcb.01205-10;
Pillai V.B., Sundaresan N.R., Samant S.A., Wolfgeher D., Trivedi C.M.,
Gupta M.P.;
"Acetylation of a conserved lysine residue in the ATP binding pocket of p38
augments its kinase activity during hypertrophy of cardiomyocytes.";
Mol. Cell. Biol. 31:2349-2363(2011).
[58]
INTERACTION WITH CDK5RAP3 AND PPM1D, AND DEPHOSPHORYLATION BY PPM1D.
PubMed=21283629; DOI=10.1371/journal.pone.0016427;
An H., Lu X., Liu D., Yarbrough W.G.;
"LZAP inhibits p38 MAPK (p38) phosphorylation and activity by facilitating
p38 association with the wild-type p53 induced phosphatase 1 (WIP1).";
PLoS ONE 6:E16427-E16427(2011).
[59]
REVIEW ON FUNCTION.
PubMed=12452429; DOI=10.1515/bc.2002.173;
Shi Y., Gaestel M.;
"In the cellular garden of forking paths: how p38 MAPKs signal for
downstream assistance.";
Biol. Chem. 383:1519-1536(2002).
[60]
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).
[61]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; THR-180 AND TYR-182, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[62]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[63]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[64]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
PubMed=8910361; DOI=10.1074/jbc.271.44.27696;
Wilson K.P., Fitzgibbon M.J., Caron P.R., Griffith J.P., Chen W.,
McCaffrey P.G., Chambers S.P., Su M.S.-S.;
"Crystal structure of p38 mitogen-activated protein kinase.";
J. Biol. Chem. 271:27696-27700(1996).
[65]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=9095200; DOI=10.1038/nsb0497-311;
Tong L., Pav S., White D.M., Rogers S., Crane K.M., Cywin C.L., Brown M.L.,
Pargellis C.A.;
"A highly specific inhibitor of human p38 MAP kinase binds in the ATP
pocket.";
Nat. Struct. Biol. 4:311-316(1997).
[66]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=9753691; DOI=10.1016/s0969-2126(98)00113-0;
Wang Z., Canagarajah B.J., Boehm J.C., Kassisa S., Cobb M.H., Young P.R.,
Abdel-Meguid S., Adams J.L., Goldsmith E.J.;
"Structural basis of inhibitor selectivity in MAP kinases.";
Structure 6:1117-1128(1998).
[67]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS).
PubMed=10633045; DOI=10.1021/jm990401t;
Shewchuk L., Hassell A., Wisely B., Rocque W., Holmes W., Veal J.,
Kuyper L.F.;
"Binding mode of the 4-anilinoquinazoline class of protein kinase
inhibitor: X-ray crystallographic studies of 4-anilinoquinazolines bound to
cyclin-dependent kinase 2 and p38 kinase.";
J. Med. Chem. 43:133-138(2000).
[68]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), AND ACTIVITY REGULATION.
PubMed=11896401; DOI=10.1038/nsb770;
Pargellis C., Tong L., Churchill L., Cirillo P.F., Gilmore T., Graham A.G.,
Grob P.M., Hickey E.R., Moss N., Pav S., Regan J.;
"Inhibition of p38 MAP kinase by utilizing a novel allosteric binding
site.";
Nat. Struct. Biol. 9:268-272(2002).
[69]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS), AND ACTIVITY REGULATION.
PubMed=12482439; DOI=10.1016/s0960-894x(02)00752-7;
Stelmach J.E., Liu L., Patel S.B., Pivnichny J.V., Scapin G., Singh S.,
Hop C.E., Wang Z., Strauss J.R., Cameron P.M., Nichols E.A., O'Keefe S.J.,
O'Neill E.A., Schmatz D.M., Schwartz C.D., Thompson C.M., Zaller D.M.,
Doherty J.B.;
"Design and synthesis of potent, orally bioavailable dihydroquinazolinone
inhibitors of p38 MAP kinase.";
Bioorg. Med. Chem. Lett. 13:277-280(2003).
[70]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), AND ACTIVITY REGULATION.
PubMed=14561090; DOI=10.1021/jm0301787;
Trejo A., Arzeno H., Browner M., Chanda S., Cheng S., Comer D.D.,
Dalrymple S.A., Dunten P., Lafargue J., Lovejoy B., Freire-Moar J., Lim J.,
Mcintosh J., Miller J., Papp E., Reuter D., Roberts R., Sanpablo F.,
Saunders J., Song K., Villasenor A., Warren S.D., Welch M., Weller P.,
Whiteley P.E., Zeng L., Goldstein D.M.;
"Design and synthesis of 4-azaindoles as inhibitors of p38 MAP kinase.";
J. Med. Chem. 46:4702-4713(2003).
[71]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
PubMed=12897767; DOI=10.1038/nsb949;
Fitzgerald C.E., Patel S.B., Becker J.W., Cameron P.M., Zaller D.,
Pikounis V.B., O'Keefe S.J., Scapin G.;
"Structural basis for p38alpha MAP kinase quinazolinone and pyridol-
pyrimidine inhibitor specificity.";
Nat. Struct. Biol. 10:764-769(2003).
[72]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), AND ACTIVITY REGULATION.
PubMed=14726206; DOI=10.1016/j.bbapap.2003.09.009;
Patel S.B., Cameron P.M., Frantz-Wattley B., O'Neill E., Becker J.W.,
Scapin G.;
"Lattice stabilization and enhanced diffraction in human p38 alpha crystals
by protein engineering.";
Biochim. Biophys. Acta 1696:67-73(2004).
[73]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-359 IN COMPLEX WITH INHIBITOR.
PubMed=16342939; DOI=10.1021/bi051714v;
Sullivan J.E., Holdgate G.A., Campbell D., Timms D., Gerhardt S., Breed J.,
Breeze A.L., Bermingham A., Pauptit R.A., Norman R.A., Embrey K.J.,
Read J., VanScyoc W.S., Ward W.H.;
"Prevention of MKK6-dependent activation by binding to p38alpha MAP
kinase.";
Biochemistry 44:16475-16490(2005).
[74]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-359, AND ACTIVITY REGULATION.
PubMed=15837335; DOI=10.1016/j.bmcl.2005.02.010;
Tamayo N., Liao L., Goldberg M., Powers D., Tudor Y.Y., Yu V., Wong L.M.,
Henkle B., Middleton S., Syed R., Harvey T., Jang G., Hungate R.,
Dominguez C.;
"Design and synthesis of potent pyridazine inhibitors of p38 MAP kinase.";
Bioorg. Med. Chem. Lett. 15:2409-2413(2005).
[75]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), AND ACTIVITY REGULATION.
PubMed=16169718; DOI=10.1016/j.bmcl.2005.08.038;
Michelotti E.L., Moffett K.K., Nguyen D., Kelly M.J., Shetty R., Chai X.,
Northrop K., Namboodiri V., Campbell B., Flynn G.A., Fujimoto T.,
Hollinger F.P., Bukhtiyarova M., Springman E.B., Karpusas M.;
"Two classes of p38alpha MAP kinase inhibitors having a common
diphenylether core but exhibiting divergent binding modes.";
Bioorg. Med. Chem. Lett. 15:5274-5279(2005).
[76]
X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 2-359 IN COMPLEX WITH INHIBITOR.
PubMed=15658854; DOI=10.1021/jm0495778;
Hartshorn M.J., Murray C.W., Cleasby A., Frederickson M., Tickle I.J.,
Jhoti H.;
"Fragment-based lead discovery using X-ray crystallography.";
J. Med. Chem. 48:403-413(2005).
[77]
X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 2-359 IN COMPLEX WITH MAPKAPK2.
PubMed=17255097; DOI=10.1074/jbc.m611165200;
ter Haar E., Prabhakar P., Liu X., Lepre C.;
"Crystal structure of the p38 alpha-MAPKAP kinase 2 heterodimer.";
J. Biol. Chem. 282:9733-9739(2007).
[78]
ERRATUM OF PUBMED:17255097.
ter Haar E., Prabhakar P., Liu X., Lepre C.;
J. Biol. Chem. 282:14684-14684(2007).
[79]
VARIANTS [LARGE SCALE ANALYSIS] VAL-51; ARG-322 AND GLY-343.
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. MAPK14 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. Accordingly, p38 MAPKs phosphorylate a broad
range of proteins and it has been estimated that they may have
approximately 200 to 300 substrates each. Some of the targets are
downstream kinases which are activated through phosphorylation and
further phosphorylate additional targets. RPS6KA5/MSK1 and RPS6KA4/MSK2
can directly phosphorylate and activate transcription factors such as
CREB1, ATF1, the NF-kappa-B isoform RELA/NFKB3, STAT1 and STAT3, but
can also phosphorylate histone H3 and the nucleosomal protein HMGN1.
RPS6KA5/MSK1 and RPS6KA4/MSK2 play important roles in the rapid
induction of immediate-early genes in response to stress or mitogenic
stimuli, either by inducing chromatin remodeling or by recruiting the
transcription machinery. On the other hand, two other kinase targets,
MAPKAPK2/MK2 and MAPKAPK3/MK3, participate in the control of gene
expression mostly at the post-transcriptional level, by phosphorylating
ZFP36 (tristetraprolin) and ELAVL1, and by regulating EEF2K, which is
important for the elongation of mRNA during translation. MKNK1/MNK1 and
MKNK2/MNK2, two other kinases activated by p38 MAPKs, regulate protein
synthesis by phosphorylating the initiation factor EIF4E2. MAPK14
interacts also with casein kinase II, leading to its activation through
autophosphorylation and further phosphorylation of TP53/p53. In the
cytoplasm, the p38 MAPK pathway is an important regulator of protein
turnover. For example, CFLAR is an inhibitor of TNF-induced apoptosis
whose proteasome-mediated degradation is regulated by p38 MAPK
phosphorylation. In a similar way, MAPK14 phosphorylates the ubiquitin
ligase SIAH2, regulating its activity towards EGLN3. MAPK14 may also
inhibit the lysosomal degradation pathway of autophagy by interfering
with the intracellular trafficking of the transmembrane protein ATG9.
Another function of MAPK14 is to regulate the endocytosis of membrane
receptors by different mechanisms that impinge on the small GTPase
RAB5A. In addition, clathrin-mediated EGFR internalization induced by
inflammatory cytokines and UV irradiation depends on MAPK14-mediated
phosphorylation of EGFR itself as well as of RAB5A effectors.
Ectodomain shedding of transmembrane proteins is regulated by p38 MAPKs
as well. In response to inflammatory stimuli, p38 MAPKs phosphorylate
the membrane-associated metalloprotease ADAM17. Such phosphorylation is
required for ADAM17-mediated ectodomain shedding of TGF-alpha family
ligands, which results in the activation of EGFR signaling and cell
proliferation. Another p38 MAPK substrate is FGFR1. FGFR1 can be
translocated from the extracellular space into the cytosol and nucleus
of target cells, and regulates processes such as rRNA synthesis and
cell growth. FGFR1 translocation requires p38 MAPK activation. In the
nucleus, many transcription factors are phosphorylated and activated by
p38 MAPKs in response to different stimuli. Classical examples include
ATF1, ATF2, ATF6, ELK1, PTPRH, DDIT3, TP53/p53 and MEF2C and MEF2A. The
p38 MAPKs are emerging as important modulators of gene expression by
regulating chromatin modifiers and remodelers. The promoters of several
genes involved in the inflammatory response, such as IL6, IL8 and
IL12B, display a p38 MAPK-dependent enrichment of histone H3
phosphorylation on 'Ser-10' (H3S10ph) in LPS-stimulated myeloid cells.
This phosphorylation enhances the accessibility of the cryptic NF-
kappa-B-binding sites marking promoters for increased NF-kappa-B
recruitment. Phosphorylates CDC25B and CDC25C which is required for
binding to 14-3-3 proteins and leads to initiation of a G2 delay after
ultraviolet radiation. Phosphorylates TIAR following DNA damage,
releasing TIAR from GADD45A mRNA and preventing mRNA degradation. The
p38 MAPKs may also have kinase-independent roles, which are thought to
be due to the binding to targets in the absence of phosphorylation.
Protein O-Glc-N-acylation catalyzed by the OGT is regulated by MAPK14,
and, although OGT does not seem to be phosphorylated by MAPK14, their
interaction increases upon MAPK14 activation induced by glucose
deprivation. This interaction may regulate OGT activity by recruiting
it to specific targets such as neurofilament H, stimulating its O-Glc-
N-acylation. Required in mid-fetal development for the growth of
embryo-derived blood vessels in the labyrinth layer of the placenta.
Also plays an essential role in developmental and stress-induced
erythropoiesis, through regulation of EPO gene expression. Isoform MXI2
activation is stimulated by mitogens and oxidative stress and only
poorly phosphorylates ELK1 and ATF2. Isoform EXIP may play a role in
the early onset of apoptosis. Phosphorylates S100A9 at 'Thr-113'.
{ECO:0000269|PubMed:10330143, ECO:0000269|PubMed:10747897,
ECO:0000269|PubMed:10943842, ECO:0000269|PubMed:11154262,
ECO:0000269|PubMed:11333986, ECO:0000269|PubMed:15905572,
ECO:0000269|PubMed:16932740, ECO:0000269|PubMed:17003045,
ECO:0000269|PubMed:17724032, ECO:0000269|PubMed:19893488,
ECO:0000269|PubMed:20188673, ECO:0000269|PubMed:20932473,
ECO:0000269|PubMed:9430721, ECO:0000269|PubMed:9687510,
ECO:0000269|PubMed:9792677, ECO:0000269|PubMed:9858528}.
-!- FUNCTION: (Microbial infection) Activated by phosphorylation by
M.tuberculosis EsxA in T-cells leading to inhibition of IFN-gamma
production; phosphorylation is apparent within 15 minute and is
inhibited by kinase-specific inhibitors SB203580 and siRNA
(PubMed:21586573). {ECO:0000269|PubMed:21586573}.
-!- 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;
Evidence={ECO:0000269|PubMed:11010976};
-!- 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; Evidence={ECO:0000269|PubMed:11010976};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:10838079};
-!- ACTIVITY REGULATION: Activated by cell stresses such as DNA damage,
heat shock, osmotic shock, anisomycin and sodium arsenite, as well as
pro-inflammatory stimuli such as bacterial lipopolysaccharide (LPS) and
interleukin-1. Activation occurs through dual phosphorylation of Thr-
180 and Tyr-182 by either of two dual specificity kinases, MAP2K3/MKK3
or MAP2K6/MKK6, and potentially also MAP2K4/MKK4, as well as by TAB1-
mediated autophosphorylation. MAPK14 phosphorylated on both Thr-180 and
Tyr-182 is 10-20-fold more active than MAPK14 phosphorylated only on
Thr-180, whereas MAPK14 phosphorylated on Tyr-182 alone is inactive.
whereas Thr-180 is necessary for catalysis, Tyr-182 may be required for
auto-activation and substrate recognition. Phosphorylated at Tyr-323 by
ZAP70 in an alternative activation pathway in response to TCR signaling
in T-cells. This alternative pathway is inhibited by GADD45A. Inhibited
by dual specificity phosphatases, such as DUSP1, DUSP10, and DUSP16.
Specifically inhibited by the binding of pyridinyl-imidazole compounds,
which are cytokine-suppressive anti-inflammatory drugs (CSAID). Isoform
Mxi2 is 100-fold less sensitive to these agents than the other isoforms
and is not inhibited by DUSP1. Isoform Exip is not activated by MAP2K6.
SB203580 is an inhibitor of MAPK14. {ECO:0000269|PubMed:10391943,
ECO:0000269|PubMed:10838079, ECO:0000269|PubMed:11278799,
ECO:0000269|PubMed:11359773, ECO:0000269|PubMed:11847341,
ECO:0000269|PubMed:11866441, ECO:0000269|PubMed:11896401,
ECO:0000269|PubMed:12482439, ECO:0000269|PubMed:14561090,
ECO:0000269|PubMed:14726206, ECO:0000269|PubMed:15735648,
ECO:0000269|PubMed:15735649, ECO:0000269|PubMed:15837335,
ECO:0000269|PubMed:16169718, ECO:0000269|PubMed:17003045,
ECO:0000269|PubMed:7535770, ECO:0000269|PubMed:8622669,
ECO:0000269|PubMed:9430721}.
-!- SUBUNIT: Component of a signaling complex containing at least AKAP13,
PKN1, MAPK14, ZAK and MAP2K3. Within this complex, AKAP13 interacts
directly with PKN1, which in turn recruits MAPK14, MAP2K3 and ZAK
(PubMed:21224381). Binds to a kinase interaction motif within the
protein tyrosine phosphatase, PTPRR (By similarity). This interaction
retains MAPK14 in the cytoplasm and prevents nuclear accumulation (By
similarity). Interacts with SPAG9 and GADD45A (By similarity).
Interacts with CDC25B, CDC25C, DUSP1, DUSP10, DUSP16, NP60, SUPT20H and
TAB1. Interacts with casein kinase II subunits CSNK2A1 and CSNK2B.
Interacts with PPM1D. Interacts with CDK5RAP3; recruits PPM1D to MAPK14
and may regulate its dephosphorylation (PubMed:21283629).
{ECO:0000250|UniProtKB:P47811, ECO:0000269|PubMed:10391943,
ECO:0000269|PubMed:10747897, ECO:0000269|PubMed:11010976,
ECO:0000269|PubMed:11278799, ECO:0000269|PubMed:11333986,
ECO:0000269|PubMed:11359773, ECO:0000269|PubMed:11847341,
ECO:0000269|PubMed:12897767, ECO:0000269|PubMed:15658854,
ECO:0000269|PubMed:15735649, ECO:0000269|PubMed:16342939,
ECO:0000269|PubMed:16352664, ECO:0000269|PubMed:16751104,
ECO:0000269|PubMed:17255097, ECO:0000269|PubMed:20188673,
ECO:0000269|PubMed:21224381, ECO:0000269|PubMed:21283629,
ECO:0000269|PubMed:9792677}.
-!- INTERACTION:
Q16539; P31749: AKT1; NbExp=2; IntAct=EBI-73946, EBI-296087;
Q16539; P28562: DUSP1; NbExp=3; IntAct=EBI-73946, EBI-975493;
Q16539; Q99956: DUSP9; NbExp=2; IntAct=EBI-73946, EBI-3906678;
Q16539; P68104: EEF1A1; NbExp=3; IntAct=EBI-73946, EBI-352162;
Q16539; P46734: MAP2K3; NbExp=4; IntAct=EBI-73946, EBI-602462;
Q16539; P27361: MAPK3; NbExp=5; IntAct=EBI-73946, EBI-73995;
Q16539; P49137: MAPKAPK2; NbExp=9; IntAct=EBI-73946, EBI-993299;
Q16539; Q16644: MAPKAPK3; NbExp=8; IntAct=EBI-73946, EBI-1384657;
Q16539; Q9BUB5: MKNK1; NbExp=3; IntAct=EBI-73946, EBI-73837;
Q16539; Q9HBH9: MKNK2; NbExp=3; IntAct=EBI-73946, EBI-2864341;
Q16539; P35813: PPM1A; NbExp=2; IntAct=EBI-73946, EBI-989143;
Q16539; Q15256: PTPRR; NbExp=3; IntAct=EBI-73946, EBI-2265659;
Q16539; P06400: RB1; NbExp=4; IntAct=EBI-73946, EBI-491274;
Q16539; O75676: RPS6KA4; NbExp=6; IntAct=EBI-73946, EBI-73933;
Q16539; Q8NEM7: SUPT20H; NbExp=5; IntAct=EBI-73946, EBI-946984;
Q16539; Q15750: TAB1; NbExp=2; IntAct=EBI-73946, EBI-358643;
Q16539; Q92574: TSC1; NbExp=2; IntAct=EBI-73946, EBI-1047085;
Q16539; Q07352: ZFP36L1; NbExp=2; IntAct=EBI-73946, EBI-721823;
Q16539; O43257: ZNHIT1; NbExp=7; IntAct=EBI-73946, EBI-347522;
Q16539-1; P22736-1: NR4A1; NbExp=5; IntAct=EBI-15834191, EBI-16085263;
Q16539-1; Q15256-1: PTPRR; NbExp=6; IntAct=EBI-15834191, EBI-16067395;
Q16539-1; P54830-1: Ptpn5; Xeno; NbExp=6; IntAct=EBI-15834191, EBI-16067443;
Q16539-3; P28482: MAPK1; NbExp=5; IntAct=EBI-6932370, EBI-959949;
Q16539-3; P49790: NUP153; NbExp=2; IntAct=EBI-6932370, EBI-286779;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7535770}. Nucleus
{ECO:0000269|PubMed:7535770}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=CSBP2;
IsoId=Q16539-1; Sequence=Displayed;
Name=CSBP1;
IsoId=Q16539-2; Sequence=VSP_004842;
Name=Mxi2;
IsoId=Q16539-3; Sequence=VSP_004844;
Name=Exip; Synonyms=Exon skip;
IsoId=Q16539-4; Sequence=VSP_004843, VSP_004845;
Name=5;
IsoId=Q16539-5; Sequence=VSP_057194;
-!- TISSUE SPECIFICITY: Brain, heart, placenta, pancreas and skeletal
muscle. Expressed to a lesser extent in lung, liver and kidney.
-!- 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 the MAP2Ks
MAP2K3/MKK3, MAP2K4/MKK4 and MAP2K6/MKK6 in response to inflammatory
citokines, environmental stress or growth factors, which activates the
enzyme. Dual phosphorylation can also be mediated by TAB1-mediated
autophosphorylation. TCR engagement in T-cells also leads to Tyr-323
phosphorylation by ZAP70. Dephosphorylated and inactivated by DUPS1,
DUSP10 and DUSP16. PPM1D also mediates dephosphorylation and
inactivation of MAPK14 (PubMed:21283629). {ECO:0000269|PubMed:11010976,
ECO:0000269|PubMed:15735648, ECO:0000269|PubMed:17724032,
ECO:0000269|PubMed:21283629, ECO:0000269|PubMed:7535770,
ECO:0000269|PubMed:8622669}.
-!- PTM: Acetylated at Lys-53 and Lys-152 by KAT2B and EP300. Acetylation
at Lys-53 increases the affinity for ATP and enhances kinase activity.
Lys-53 and Lys-152 are deacetylated by HDAC3.
{ECO:0000269|PubMed:21444723}.
-!- PTM: Ubiquitinated. Ubiquitination leads to degradation by the
proteasome pathway. {ECO:0000269|PubMed:17724032}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
protein kinase family. MAP kinase subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=P38 mitogen-activated protein
kinases entry;
URL="https://en.wikipedia.org/wiki/P38_mitogen-activated_protein_kinases";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MAPK14ID41292ch6p21.html";
---------------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
EMBL; L35263; AAA57455.1; -; mRNA.
EMBL; L35264; AAA57456.1; -; mRNA.
EMBL; L35253; AAA74301.1; -; mRNA.
EMBL; U19775; AAC50329.1; -; mRNA.
EMBL; AF100544; AAF36770.1; -; mRNA.
EMBL; AB074150; BAB85654.1; -; mRNA.
EMBL; FJ032367; ACI00233.1; -; mRNA.
EMBL; AK291709; BAF84398.1; -; mRNA.
EMBL; BT006933; AAP35579.1; -; mRNA.
EMBL; CR536505; CAG38743.1; -; mRNA.
EMBL; EU332860; ABY87549.1; -; Genomic_DNA.
EMBL; Z95152; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471081; EAX03869.1; -; Genomic_DNA.
EMBL; BC000092; AAH00092.1; -; mRNA.
EMBL; BC031574; AAH31574.1; -; mRNA.
CCDS; CCDS4815.1; -. [Q16539-2]
CCDS; CCDS4816.1; -. [Q16539-1]
CCDS; CCDS4817.1; -. [Q16539-4]
PIR; S53536; S53536.
RefSeq; NP_001306.1; NM_001315.2. [Q16539-2]
RefSeq; NP_620581.1; NM_139012.2. [Q16539-1]
RefSeq; NP_620582.1; NM_139013.2. [Q16539-3]
RefSeq; NP_620583.1; NM_139014.2. [Q16539-4]
PDB; 1A9U; X-ray; 2.50 A; A=1-360.
PDB; 1BL6; X-ray; 2.50 A; A=1-360.
PDB; 1BL7; X-ray; 2.50 A; A=1-360.
PDB; 1BMK; X-ray; 2.40 A; A=1-360.
PDB; 1DI9; X-ray; 2.60 A; A=1-360.
PDB; 1IAN; X-ray; 2.00 A; A=2-360.
PDB; 1KV1; X-ray; 2.50 A; A=1-360.
PDB; 1KV2; X-ray; 2.80 A; A=1-360.
PDB; 1M7Q; X-ray; 2.40 A; A=1-360.
PDB; 1OUK; X-ray; 2.50 A; A=1-360.
PDB; 1OUY; X-ray; 2.50 A; A=1-360.
PDB; 1OVE; X-ray; 2.10 A; A=1-360.
PDB; 1OZ1; X-ray; 2.10 A; A=1-360.
PDB; 1R39; X-ray; 2.30 A; A=1-360.
PDB; 1R3C; X-ray; 2.00 A; A=1-360.
PDB; 1W7H; X-ray; 2.21 A; A=2-360.
PDB; 1W82; X-ray; 2.20 A; A=2-360.
PDB; 1W83; X-ray; 2.50 A; A=2-360.
PDB; 1W84; X-ray; 2.20 A; A=2-360.
PDB; 1WBN; X-ray; 2.40 A; A=2-360.
PDB; 1WBO; X-ray; 2.16 A; A=2-360.
PDB; 1WBS; X-ray; 1.80 A; A=2-360.
PDB; 1WBT; X-ray; 2.00 A; A=2-360.
PDB; 1WBV; X-ray; 2.00 A; A=2-360.
PDB; 1WBW; X-ray; 2.41 A; A=2-360.
PDB; 1WFC; X-ray; 2.30 A; A=1-360.
PDB; 1YQJ; X-ray; 2.00 A; A=2-360.
PDB; 1ZYJ; X-ray; 2.00 A; A=1-360.
PDB; 1ZZ2; X-ray; 2.00 A; A=1-360.
PDB; 1ZZL; X-ray; 2.00 A; A=4-354.
PDB; 2BAJ; X-ray; 2.25 A; A=2-360.
PDB; 2BAK; X-ray; 2.20 A; A=2-360.
PDB; 2BAL; X-ray; 2.10 A; A=2-360.
PDB; 2BAQ; X-ray; 2.80 A; A=2-360.
PDB; 2FSL; X-ray; 1.70 A; X=2-360.
PDB; 2FSM; X-ray; 1.86 A; X=2-360.
PDB; 2FSO; X-ray; 1.83 A; X=2-360.
PDB; 2FST; X-ray; 1.45 A; X=2-360.
PDB; 2GFS; X-ray; 1.75 A; A=2-360.
PDB; 2I0H; X-ray; 2.00 A; A=1-360.
PDB; 2LGC; NMR; -; A=2-354.
PDB; 2NPQ; X-ray; 1.80 A; A=2-360.
PDB; 2OKR; X-ray; 2.00 A; A/D=2-360.
PDB; 2ONL; X-ray; 4.00 A; A/B=2-360.
PDB; 2QD9; X-ray; 1.70 A; A=2-360.
PDB; 2RG5; X-ray; 2.40 A; A=2-360.
PDB; 2RG6; X-ray; 1.72 A; A=2-360.
PDB; 2Y8O; X-ray; 1.95 A; A=1-360.
PDB; 2YIS; X-ray; 2.00 A; A=2-360.
PDB; 2YIW; X-ray; 2.00 A; A=2-360.
PDB; 2YIX; X-ray; 2.30 A; A=4-354.
PDB; 2ZAZ; X-ray; 1.80 A; A=1-360.
PDB; 2ZB0; X-ray; 2.10 A; A=1-360.
PDB; 2ZB1; X-ray; 2.50 A; A=1-360.
PDB; 3BV2; X-ray; 2.40 A; A=2-360.
PDB; 3BV3; X-ray; 2.59 A; A=2-360.
PDB; 3BX5; X-ray; 2.40 A; A=2-360.
PDB; 3C5U; X-ray; 2.80 A; A=2-360.
PDB; 3CTQ; X-ray; 1.95 A; A=5-352.
PDB; 3D7Z; X-ray; 2.10 A; A=1-360.
PDB; 3D83; X-ray; 1.90 A; A=1-360.
PDB; 3DS6; X-ray; 2.90 A; A/B/C/D=1-360.
PDB; 3DT1; X-ray; 2.80 A; A=1-360.
PDB; 3E92; X-ray; 2.00 A; A=1-360.
PDB; 3E93; X-ray; 2.00 A; A=1-360.
PDB; 3FC1; X-ray; 2.40 A; X=1-360.
PDB; 3FI4; X-ray; 2.20 A; A=1-360.
PDB; 3FKL; X-ray; 2.00 A; A=1-360.
PDB; 3FKN; X-ray; 2.00 A; A=1-360.
PDB; 3FKO; X-ray; 2.00 A; A=1-360.
PDB; 3FL4; X-ray; 1.80 A; A=1-360.
PDB; 3FLN; X-ray; 1.90 A; C=1-360.
PDB; 3FLQ; X-ray; 1.90 A; A=1-360.
PDB; 3FLS; X-ray; 2.30 A; A=1-360.
PDB; 3FLW; X-ray; 2.10 A; A=1-360.
PDB; 3FLY; X-ray; 1.80 A; A=1-360.
PDB; 3FLZ; X-ray; 2.23 A; A=1-360.
PDB; 3FMH; X-ray; 1.90 A; A=1-360.
PDB; 3FMJ; X-ray; 2.00 A; A=1-360.
PDB; 3FMK; X-ray; 1.70 A; A=1-360.
PDB; 3FML; X-ray; 2.10 A; A=1-360.
PDB; 3FMM; X-ray; 2.00 A; A=1-360.
PDB; 3FMN; X-ray; 1.90 A; A=1-360.
PDB; 3FSF; X-ray; 2.10 A; A=1-360.
PDB; 3FSK; X-ray; 2.00 A; A=1-360.
PDB; 3GC7; X-ray; 1.80 A; A=1-360.
PDB; 3GCP; X-ray; 2.25 A; A=2-360.
PDB; 3GCQ; X-ray; 2.00 A; A=2-360.
PDB; 3GCS; X-ray; 2.10 A; A=2-360.
PDB; 3GCU; X-ray; 2.10 A; A/B=2-360.
PDB; 3GCV; X-ray; 2.30 A; A=2-360.
PDB; 3GFE; X-ray; 2.10 A; A=1-360.
PDB; 3GI3; X-ray; 2.40 A; A=1-360.
PDB; 3HA8; X-ray; 2.48 A; A=1-360.
PDB; 3HEC; X-ray; 2.50 A; A=5-352.
PDB; 3HEG; X-ray; 2.20 A; A=5-352.
PDB; 3HL7; X-ray; 1.88 A; A=1-360.
PDB; 3HLL; X-ray; 1.95 A; A=1-360.
PDB; 3HP2; X-ray; 2.15 A; A=1-360.
PDB; 3HP5; X-ray; 2.30 A; A=1-360.
PDB; 3HRB; X-ray; 2.20 A; A=2-360.
PDB; 3HUB; X-ray; 2.25 A; A=2-360.
PDB; 3HUC; X-ray; 1.80 A; A=2-360.
PDB; 3HV3; X-ray; 2.00 A; A=2-360.
PDB; 3HV4; X-ray; 2.60 A; A/B=2-360.
PDB; 3HV5; X-ray; 2.25 A; A/B=2-360.
PDB; 3HV6; X-ray; 1.95 A; A=2-360.
PDB; 3HV7; X-ray; 2.40 A; A=2-360.
PDB; 3HVC; X-ray; 2.10 A; A=1-360.
PDB; 3IPH; X-ray; 2.10 A; A=1-360.
PDB; 3ITZ; X-ray; 2.25 A; A=1-360.
PDB; 3IW5; X-ray; 2.50 A; A=2-360.
PDB; 3IW6; X-ray; 2.10 A; A=2-360.
PDB; 3IW7; X-ray; 2.40 A; A=2-360.
PDB; 3IW8; X-ray; 2.00 A; A=2-360.
PDB; 3K3I; X-ray; 1.70 A; A=5-352.
PDB; 3K3J; X-ray; 2.00 A; A=1-360.
PDB; 3KF7; X-ray; 2.00 A; A=1-360.
PDB; 3KQ7; X-ray; 1.80 A; A=1-360.
PDB; 3L8S; X-ray; 2.35 A; A=2-360.
PDB; 3L8X; X-ray; 2.15 A; A=2-360.
PDB; 3LFA; X-ray; 2.10 A; A=2-360.
PDB; 3LFB; X-ray; 2.60 A; A=2-360.
PDB; 3LFC; X-ray; 2.80 A; A=2-360.
PDB; 3LFD; X-ray; 3.40 A; A=2-360.
PDB; 3LFE; X-ray; 2.30 A; A=2-360.
PDB; 3LFF; X-ray; 1.50 A; A=2-360.
PDB; 3LHJ; X-ray; 3.31 A; A=1-360.
PDB; 3MGY; X-ray; 2.10 A; A=1-360.
PDB; 3MH0; X-ray; 2.00 A; A=1-360.
PDB; 3MH1; X-ray; 2.20 A; A=1-360.
PDB; 3MH2; X-ray; 2.30 A; A=1-360.
PDB; 3MH3; X-ray; 2.20 A; A=1-360.
PDB; 3MPA; X-ray; 2.10 A; A=1-360.
PDB; 3MPT; X-ray; 1.89 A; A=1-360.
PDB; 3MVL; X-ray; 2.80 A; A/B=2-360.
PDB; 3MVM; X-ray; 2.00 A; A/B=2-360.
PDB; 3MW1; X-ray; 2.80 A; A=2-360.
PDB; 3NEW; X-ray; 2.51 A; A=1-360.
PDB; 3NNU; X-ray; 2.40 A; A=1-354.
PDB; 3NNV; X-ray; 2.10 A; A=1-354.
PDB; 3NNW; X-ray; 1.89 A; A=1-354.
PDB; 3NNX; X-ray; 2.28 A; A=1-354.
PDB; 3NWW; X-ray; 2.09 A; A=2-360.
PDB; 3O8P; X-ray; 2.10 A; A=1-360.
PDB; 3O8T; X-ray; 2.00 A; A=1-360.
PDB; 3O8U; X-ray; 2.10 A; A=1-360.
PDB; 3OBG; X-ray; 2.80 A; A=1-360.
PDB; 3OBJ; X-ray; 2.40 A; A=1-360.
PDB; 3OC1; X-ray; 2.59 A; A=1-360.
PDB; 3OCG; X-ray; 2.21 A; A=2-360.
PDB; 3OD6; X-ray; 2.68 A; X=1-360.
PDB; 3ODY; X-ray; 2.20 A; X=1-360.
PDB; 3ODZ; X-ray; 2.30 A; X=1-360.
PDB; 3OEF; X-ray; 1.60 A; X=1-360.
PDB; 3PG3; X-ray; 2.00 A; A=2-360.
PDB; 3QUD; X-ray; 2.00 A; A=2-360.
PDB; 3QUE; X-ray; 2.70 A; A=2-360.
PDB; 3RIN; X-ray; 2.20 A; A=1-360.
PDB; 3ROC; X-ray; 1.70 A; A=1-360.
PDB; 3S3I; X-ray; 1.80 A; A=4-352.
PDB; 3S4Q; X-ray; 2.27 A; A=2-360.
PDB; 3U8W; X-ray; 2.15 A; A=1-360.
PDB; 3UVP; X-ray; 2.40 A; A=2-360.
PDB; 3UVQ; X-ray; 2.20 A; A=2-360.
PDB; 3UVR; X-ray; 2.10 A; A=2-360.
PDB; 3ZS5; X-ray; 1.60 A; A=2-360.
PDB; 3ZSG; X-ray; 1.89 A; A=2-360.
PDB; 3ZSH; X-ray; 2.05 A; A=2-360.
PDB; 3ZSI; X-ray; 2.40 A; A=2-360.
PDB; 3ZYA; X-ray; 1.90 A; A=1-360.
PDB; 4A9Y; X-ray; 2.20 A; A=2-360.
PDB; 4AA0; X-ray; 1.80 A; A=2-360.
PDB; 4AA4; X-ray; 2.30 A; A=2-360.
PDB; 4AA5; X-ray; 2.38 A; A=2-360.
PDB; 4AAC; X-ray; 2.50 A; A=2-360.
PDB; 4DLI; X-ray; 1.91 A; A=2-360.
PDB; 4DLJ; X-ray; 2.60 A; A=2-360.
PDB; 4E5A; X-ray; 1.87 A; X=1-360.
PDB; 4E5B; X-ray; 2.00 A; A=1-360.
PDB; 4E6A; X-ray; 2.09 A; A=1-360.
PDB; 4E6C; X-ray; 2.39 A; A=1-360.
PDB; 4E8A; X-ray; 2.70 A; A=1-360.
PDB; 4EH2; X-ray; 2.00 A; A=2-360.
PDB; 4EH3; X-ray; 2.40 A; A=2-360.
PDB; 4EH4; X-ray; 2.50 A; A=2-360.
PDB; 4EH5; X-ray; 2.00 A; A=2-360.
PDB; 4EH6; X-ray; 2.10 A; A=2-360.
PDB; 4EH7; X-ray; 2.10 A; A=2-360.
PDB; 4EH8; X-ray; 2.20 A; A=2-360.
PDB; 4EH9; X-ray; 2.10 A; A=2-360.
PDB; 4EHV; X-ray; 1.60 A; A=2-360.
PDB; 4EWQ; X-ray; 2.10 A; A=2-360.
PDB; 4F9W; X-ray; 2.00 A; A=2-360.
PDB; 4F9Y; X-ray; 1.85 A; A=2-360.
PDB; 4FA2; X-ray; 2.00 A; A=2-360.
PDB; 4GEO; X-ray; 1.66 A; A=2-360.
PDB; 4KIN; X-ray; 1.97 A; A/B/C/D=2-360.
PDB; 4KIP; X-ray; 2.27 A; A/B=2-360.
PDB; 4KIQ; X-ray; 2.50 A; A/B/C/D=2-360.
PDB; 4L8M; X-ray; 2.10 A; A=2-360.
PDB; 4R3C; X-ray; 2.06 A; A=2-360.
PDB; 4ZTH; X-ray; 2.15 A; A=2-360.
PDB; 5ETA; X-ray; 2.80 A; A/B=1-360.
PDB; 5ETC; X-ray; 2.42 A; A=1-360.
PDB; 5ETF; X-ray; 2.40 A; A=1-360.
PDB; 5ETI; X-ray; 2.80 A; A=1-360.
PDB; 5ML5; X-ray; 1.90 A; A=1-360.
PDB; 5MTX; X-ray; 1.80 A; A=1-360.
PDB; 5MTY; X-ray; 2.31 A; A=1-360.
PDB; 5MZ3; X-ray; 2.15 A; A=1-360.
PDB; 5N63; X-ray; 2.40 A; A=1-360.
PDB; 5N64; X-ray; 2.40 A; A=1-360.
PDB; 5N65; X-ray; 2.00 A; A=1-360.
PDB; 5N66; X-ray; 2.40 A; A=1-360.
PDB; 5N67; X-ray; 1.90 A; A=1-360.
PDB; 5N68; X-ray; 1.85 A; A=1-360.
PDB; 5O8U; X-ray; 2.00 A; A=1-360.
PDB; 5O8V; X-ray; 2.00 A; A=1-360.
PDB; 5OMG; X-ray; 2.00 A; A=1-360.
PDB; 5OMH; X-ray; 2.50 A; A=1-360.
PDB; 5TBE; X-ray; 2.44 A; A=1-360.
PDB; 5TCO; X-ray; 2.10 A; A=2-360.
PDB; 5WJJ; X-ray; 1.60 A; A=1-360.
PDB; 5XYX; X-ray; 2.61 A; A=1-360.
PDB; 5XYY; X-ray; 1.70 A; A=1-360.
PDB; 6ANL; X-ray; 2.00 A; A=1-360.
PDB; 6HWT; X-ray; 1.70 A; A=2-360.
PDB; 6HWU; X-ray; 2.30 A; A=2-360.
PDB; 6HWV; X-ray; 1.70 A; A=2-360.
PDB; 6M95; X-ray; 1.80 A; A=1-360.
PDB; 6M9L; X-ray; 2.45 A; A=1-360.
PDB; 6OHD; X-ray; 2.50 A; A=1-360.
PDB; 6QDZ; X-ray; 1.73 A; A=1-360.
PDB; 6QE1; X-ray; 1.85 A; A=1-360.
PDB; 6QYX; X-ray; 1.66 A; A=1-166, A=197-360.
PDB; 6SFI; X-ray; 1.60 A; A=1-360.
PDB; 6SFJ; X-ray; 1.95 A; A=1-360.
PDB; 6SFK; X-ray; 1.80 A; A=1-360.
PDB; 6SFO; X-ray; 1.75 A; A=1-360.
PDBsum; 1A9U; -.
PDBsum; 1BL6; -.
PDBsum; 1BL7; -.
PDBsum; 1BMK; -.
PDBsum; 1DI9; -.
PDBsum; 1IAN; -.
PDBsum; 1KV1; -.
PDBsum; 1KV2; -.
PDBsum; 1M7Q; -.
PDBsum; 1OUK; -.
PDBsum; 1OUY; -.
PDBsum; 1OVE; -.
PDBsum; 1OZ1; -.
PDBsum; 1R39; -.
PDBsum; 1R3C; -.
PDBsum; 1W7H; -.
PDBsum; 1W82; -.
PDBsum; 1W83; -.
PDBsum; 1W84; -.
PDBsum; 1WBN; -.
PDBsum; 1WBO; -.
PDBsum; 1WBS; -.
PDBsum; 1WBT; -.
PDBsum; 1WBV; -.
PDBsum; 1WBW; -.
PDBsum; 1WFC; -.
PDBsum; 1YQJ; -.
PDBsum; 1ZYJ; -.
PDBsum; 1ZZ2; -.
PDBsum; 1ZZL; -.
PDBsum; 2BAJ; -.
PDBsum; 2BAK; -.
PDBsum; 2BAL; -.
PDBsum; 2BAQ; -.
PDBsum; 2FSL; -.
PDBsum; 2FSM; -.
PDBsum; 2FSO; -.
PDBsum; 2FST; -.
PDBsum; 2GFS; -.
PDBsum; 2I0H; -.
PDBsum; 2LGC; -.
PDBsum; 2NPQ; -.
PDBsum; 2OKR; -.
PDBsum; 2ONL; -.
PDBsum; 2QD9; -.
PDBsum; 2RG5; -.
PDBsum; 2RG6; -.
PDBsum; 2Y8O; -.
PDBsum; 2YIS; -.
PDBsum; 2YIW; -.
PDBsum; 2YIX; -.
PDBsum; 2ZAZ; -.
PDBsum; 2ZB0; -.
PDBsum; 2ZB1; -.
PDBsum; 3BV2; -.
PDBsum; 3BV3; -.
PDBsum; 3BX5; -.
PDBsum; 3C5U; -.
PDBsum; 3CTQ; -.
PDBsum; 3D7Z; -.
PDBsum; 3D83; -.
PDBsum; 3DS6; -.
PDBsum; 3DT1; -.
PDBsum; 3E92; -.
PDBsum; 3E93; -.
PDBsum; 3FC1; -.
PDBsum; 3FI4; -.
PDBsum; 3FKL; -.
PDBsum; 3FKN; -.
PDBsum; 3FKO; -.
PDBsum; 3FL4; -.
PDBsum; 3FLN; -.
PDBsum; 3FLQ; -.
PDBsum; 3FLS; -.
PDBsum; 3FLW; -.
PDBsum; 3FLY; -.
PDBsum; 3FLZ; -.
PDBsum; 3FMH; -.
PDBsum; 3FMJ; -.
PDBsum; 3FMK; -.
PDBsum; 3FML; -.
PDBsum; 3FMM; -.
PDBsum; 3FMN; -.
PDBsum; 3FSF; -.
PDBsum; 3FSK; -.
PDBsum; 3GC7; -.
PDBsum; 3GCP; -.
PDBsum; 3GCQ; -.
PDBsum; 3GCS; -.
PDBsum; 3GCU; -.
PDBsum; 3GCV; -.
PDBsum; 3GFE; -.
PDBsum; 3GI3; -.
PDBsum; 3HA8; -.
PDBsum; 3HEC; -.
PDBsum; 3HEG; -.
PDBsum; 3HL7; -.
PDBsum; 3HLL; -.
PDBsum; 3HP2; -.
PDBsum; 3HP5; -.
PDBsum; 3HRB; -.
PDBsum; 3HUB; -.
PDBsum; 3HUC; -.
PDBsum; 3HV3; -.
PDBsum; 3HV4; -.
PDBsum; 3HV5; -.
PDBsum; 3HV6; -.
PDBsum; 3HV7; -.
PDBsum; 3HVC; -.
PDBsum; 3IPH; -.
PDBsum; 3ITZ; -.
PDBsum; 3IW5; -.
PDBsum; 3IW6; -.
PDBsum; 3IW7; -.
PDBsum; 3IW8; -.
PDBsum; 3K3I; -.
PDBsum; 3K3J; -.
PDBsum; 3KF7; -.
PDBsum; 3KQ7; -.
PDBsum; 3L8S; -.
PDBsum; 3L8X; -.
PDBsum; 3LFA; -.
PDBsum; 3LFB; -.
PDBsum; 3LFC; -.
PDBsum; 3LFD; -.
PDBsum; 3LFE; -.
PDBsum; 3LFF; -.
PDBsum; 3LHJ; -.
PDBsum; 3MGY; -.
PDBsum; 3MH0; -.
PDBsum; 3MH1; -.
PDBsum; 3MH2; -.
PDBsum; 3MH3; -.
PDBsum; 3MPA; -.
PDBsum; 3MPT; -.
PDBsum; 3MVL; -.
PDBsum; 3MVM; -.
PDBsum; 3MW1; -.
PDBsum; 3NEW; -.
PDBsum; 3NNU; -.
PDBsum; 3NNV; -.
PDBsum; 3NNW; -.
PDBsum; 3NNX; -.
PDBsum; 3NWW; -.
PDBsum; 3O8P; -.
PDBsum; 3O8T; -.
PDBsum; 3O8U; -.
PDBsum; 3OBG; -.
PDBsum; 3OBJ; -.
PDBsum; 3OC1; -.
PDBsum; 3OCG; -.
PDBsum; 3OD6; -.
PDBsum; 3ODY; -.
PDBsum; 3ODZ; -.
PDBsum; 3OEF; -.
PDBsum; 3PG3; -.
PDBsum; 3QUD; -.
PDBsum; 3QUE; -.
PDBsum; 3RIN; -.
PDBsum; 3ROC; -.
PDBsum; 3S3I; -.
PDBsum; 3S4Q; -.
PDBsum; 3U8W; -.
PDBsum; 3UVP; -.
PDBsum; 3UVQ; -.
PDBsum; 3UVR; -.
PDBsum; 3ZS5; -.
PDBsum; 3ZSG; -.
PDBsum; 3ZSH; -.
PDBsum; 3ZSI; -.
PDBsum; 3ZYA; -.
PDBsum; 4A9Y; -.
PDBsum; 4AA0; -.
PDBsum; 4AA4; -.
PDBsum; 4AA5; -.
PDBsum; 4AAC; -.
PDBsum; 4DLI; -.
PDBsum; 4DLJ; -.
PDBsum; 4E5A; -.
PDBsum; 4E5B; -.
PDBsum; 4E6A; -.
PDBsum; 4E6C; -.
PDBsum; 4E8A; -.
PDBsum; 4EH2; -.
PDBsum; 4EH3; -.
PDBsum; 4EH4; -.
PDBsum; 4EH5; -.
PDBsum; 4EH6; -.
PDBsum; 4EH7; -.
PDBsum; 4EH8; -.
PDBsum; 4EH9; -.
PDBsum; 4EHV; -.
PDBsum; 4EWQ; -.
PDBsum; 4F9W; -.
PDBsum; 4F9Y; -.
PDBsum; 4FA2; -.
PDBsum; 4GEO; -.
PDBsum; 4KIN; -.
PDBsum; 4KIP; -.
PDBsum; 4KIQ; -.
PDBsum; 4L8M; -.
PDBsum; 4R3C; -.
PDBsum; 4ZTH; -.
PDBsum; 5ETA; -.
PDBsum; 5ETC; -.
PDBsum; 5ETF; -.
PDBsum; 5ETI; -.
PDBsum; 5ML5; -.
PDBsum; 5MTX; -.
PDBsum; 5MTY; -.
PDBsum; 5MZ3; -.
PDBsum; 5N63; -.
PDBsum; 5N64; -.
PDBsum; 5N65; -.
PDBsum; 5N66; -.
PDBsum; 5N67; -.
PDBsum; 5N68; -.
PDBsum; 5O8U; -.
PDBsum; 5O8V; -.
PDBsum; 5OMG; -.
PDBsum; 5OMH; -.
PDBsum; 5TBE; -.
PDBsum; 5TCO; -.
PDBsum; 5WJJ; -.
PDBsum; 5XYX; -.
PDBsum; 5XYY; -.
PDBsum; 6ANL; -.
PDBsum; 6HWT; -.
PDBsum; 6HWU; -.
PDBsum; 6HWV; -.
PDBsum; 6M95; -.
PDBsum; 6M9L; -.
PDBsum; 6OHD; -.
PDBsum; 6QDZ; -.
PDBsum; 6QE1; -.
PDBsum; 6QYX; -.
PDBsum; 6SFI; -.
PDBsum; 6SFJ; -.
PDBsum; 6SFK; -.
PDBsum; 6SFO; -.
SMR; Q16539; -.
BioGRID; 107819; 242.
CORUM; Q16539; -.
DIP; DIP-30987N; -.
ELM; Q16539; -.
IntAct; Q16539; 153.
MINT; Q16539; -.
STRING; 9606.ENSP00000229795; -.
ChEMBL; CHEMBL260; -.
DrugBank; DB02873; 1-(2,6-Dichlorophenyl)-5-(2,4-Difluorophenyl)-7-Piperazin-1-Yl-3,4-Dihydroquinazolin-2(1h)-One.
DrugBank; DB01948; 1-(2,6-Dichlorophenyl)-5-(2,4-Difluorophenyl)-7-Piperidin-4-Yl-3,4-Dihydroquinolin-2(1h)-One.
DrugBank; DB02277; 1-(5-Tert-Butyl-2-Methyl-2h-Pyrazol-3-Yl)-3-(4-Chloro-Phenyl)-Urea.
DrugBank; DB06882; 1-[1-(3-aminophenyl)-3-tert-butyl-1H-pyrazol-5-yl]-3-naphthalen-1-ylurea.
DrugBank; DB08097; 2-(2,6-DIFLUOROPHENOXY)-N-(2-FLUOROPHENYL)-9-ISOPROPYL-9H-PURIN-8-AMINE.
DrugBank; DB08395; 2-(ETHOXYMETHYL)-4-(4-FLUOROPHENYL)-3-[2-(2-HYDROXYPHENOXY)PYRIMIDIN-4-YL]ISOXAZOL-5(2H)-ONE.
DrugBank; DB03110; 2-Chlorophenol.
DrugBank; DB07942; 2-fluoro-4-[4-(4-fluorophenyl)-1H-pyrazol-3-yl]pyridine.
DrugBank; DB08093; 3-(1-NAPHTHYLMETHOXY)PYRIDIN-2-AMINE.
DrugBank; DB08095; 3-(2-CHLOROPHENYL)-1-(2-{[(1S)-2-HYDROXY-1,2-DIMETHYLPROPYL]AMINO}PYRIMIDIN-4-YL)-1-(4-METHOXYPHENYL)UREA.
DrugBank; DB02195; 3-(4-Fluorophenyl)-1-Hydroxy-2-(Pyridin-4-Yl)-1h-Pyrrolo[3,2-B]Pyridine.
DrugBank; DB02352; 3-(Benzyloxy)Pyridin-2-Amine.
DrugBank; DB08730; 3-FLUORO-5-MORPHOLIN-4-YL-N-[1-(2-PYRIDIN-4-YLETHYL)-1H-INDOL-6-YL]BENZAMIDE.
DrugBank; DB08091; 3-FLUORO-5-MORPHOLIN-4-YL-N-[3-(2-PYRIDIN-4-YLETHYL)-1H-INDOL-5-YL]BENZAMIDE.
DrugBank; DB08092; 3-fluoro-N-1H-indol-5-yl-5-morpholin-4-ylbenzamide.
DrugBank; DB04632; 4-(2-HYDROXYBENZYLAMINO)-N-(3-(4-FLUOROPHENOXY)PHENYL)PIPERIDINE-1-SULFONAMIDE.
DrugBank; DB08522; 4-(4-FLUOROPHENYL)-1-CYCLOROPROPYLMETHYL-5-(4-PYRIDYL)-IMIDAZOLE.
DrugBank; DB03980; 4-(Fluorophenyl)-1-Cyclopropylmethyl-5-(2-Amino-4-Pyrimidinyl)Imidazole.
DrugBank; DB07829; 4-[3-(4-FLUOROPHENYL)-1H-PYRAZOL-4-YL]PYRIDINE.
DrugBank; DB02984; 4-[3-Methylsulfanylanilino]-6,7-Dimethoxyquinazoline.
DrugBank; DB08521; 4-[4-(4-Fluorophenyl)-2-[4-[(R)-methylsulfinyl]phenyl]-1H-imidazol-5-yl]pyridine.
DrugBank; DB07607; 4-[5-(3-IODO-PHENYL)-2-(4-METHANESULFINYL-PHENYL)-1H-IMIDAZOL-4-YL]-PYRIDINE.
DrugBank; DB01761; 4-[5-[2-(1-Phenyl-Ethylamino)-Pyrimidin-4-Yl]-1-Methyl-4-(3-Trifluoromethylphenyl)-1h-Imidazol-2-Yl]-Piperidine.
DrugBank; DB07459; 4-PHENOXY-N-(PYRIDIN-2-YLMETHYL)BENZAMIDE.
DrugBank; DB07832; 4-{4-[(5-hydroxy-2-methylphenyl)amino]quinolin-7-yl}-1,3-thiazole-2-carbaldehyde.
DrugBank; DB01988; 6((S)-3-Benzylpiperazin-1-Yl)-3-(Naphthalen-2-Yl)-4-(Pyridin-4-Yl)Pyrazine.
DrugBank; DB08352; 6-[4-(2-fluorophenyl)-1,3-oxazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine.
DrugBank; DB08096; 8-(2-CHLOROPHENYLAMINO)-2-(2,6-DIFLUOROPHENYLAMINO)-9-ETHYL-9H-PURINE-1,7-DIIUM.
DrugBank; DB08424; [5-AMINO-1-(4-FLUOROPHENYL)-1H-PYRAZOL-4-YL](3-{[(2R)-2,3-DIHYDROXYPROPYL]OXY}PHENYL)METHANONE.
DrugBank; DB08423; [5-AMINO-1-(4-FLUOROPHENYL)-1H-PYRAZOL-4-YL][3-(PIPERIDIN-4-YLOXY)PHENYL]METHANONE.
DrugBank; DB01254; Dasatinib.
DrugBank; DB03044; Doramapimod.
DrugBank; DB12010; Fostamatinib.
DrugBank; DB01953; Inhibitor of P38 Kinase.
DrugBank; DB05157; KC706.
DrugBank; DB01017; Minocycline.
DrugBank; DB08242; N,4-dimethyl-3-[(1-phenyl-1H-pyrazolo[3,4-d]pyrimidin-4-yl)amino]benzamide.
DrugBank; DB07833; N-(3-cyanophenyl)-2'-methyl-5'-(5-methyl-1,3,4-oxadiazol-2-yl)-4-biphenylcarboxamide.
DrugBank; DB08064; N-(3-TERT-BUTYL-1H-PYRAZOL-5-YL)-N'-{4-CHLORO-3-[(PYRIDIN-3-YLOXY)METHYL]PHENYL}UREA.
DrugBank; DB07834; N-(cyclopropylmethyl)-2'-methyl-5'-(5-methyl-1,3,4-oxadiazol-2-yl)biphenyl-4-carboxamide.
DrugBank; DB01807; N-[(3Z)-5-Tert-butyl-2-phenyl-1,2-dihydro-3H-pyrazol-3-ylidene]-N'-(4-chlorophenyl)urea.
DrugBank; DB06991; N-[2-methyl-5-(methylcarbamoyl)phenyl]-2-{[(1R)-1-methylpropyl]amino}-1,3-thiazole-5-carboxamide.
DrugBank; DB08068; N-[4-CHLORO-3-(PYRIDIN-3-YLOXYMETHYL)-PHENYL]-3-FLUORO.
DrugBank; DB07811; N-cyclopropyl-2',6-dimethyl-4'-(5-methyl-1,3,4-oxadiazol-2-yl)biphenyl-3-carboxamide.
DrugBank; DB08349; N-cyclopropyl-3-{[1-(2,4-difluorophenyl)-7-methyl-6-oxo-6,7-dihydro-1H-pyrazolo[3,4-b]pyridin-4-yl]amino}-4-methylbenzamide.
DrugBank; DB07307; N-cyclopropyl-4-methyl-3-[1-(2-methylphenyl)phthalazin-6-yl]benzamide.
DrugBank; DB08351; N-cyclopropyl-4-methyl-3-{2-[(2-morpholin-4-ylethyl)amino]quinazolin-6-yl}benzamide.
DrugBank; DB06940; N-ethyl-4-{[5-(methoxycarbamoyl)-2-methylphenyl]amino}-5-methylpyrrolo[2,1-f][1,2,4]triazine-6-carboxamide.
DrugBank; DB07138; Neflamapimod.
DrugBank; DB07835; N~3~-cyclopropyl-N~4~'-(cyclopropylmethyl)-6-methylbiphenyl-3,4'-dicarboxamide.
DrugBank; DB07941; PH-797804.
DrugBank; DB06518; R-1487.
DrugBank; DB04338; SB220025.
DrugBank; DB07943; SD-0006.
DrugBank; DB05412; Talmapimod.
DrugBank; DB04797; Triazolopyridine.
DrugBank; DB05470; VX-702.
DrugCentral; Q16539; -.
GuidetoPHARMACOLOGY; 1499; -.
iPTMnet; Q16539; -.
MetOSite; Q16539; -.
PhosphoSitePlus; Q16539; -.
BioMuta; MAPK14; -.
OGP; Q16539; -.
CPTAC; CPTAC-1325; -.
CPTAC; CPTAC-1355; -.
CPTAC; CPTAC-1356; -.
CPTAC; CPTAC-878; -.
CPTAC; CPTAC-879; -.
EPD; Q16539; -.
jPOST; Q16539; -.
MassIVE; Q16539; -.
MaxQB; Q16539; -.
PaxDb; Q16539; -.
PeptideAtlas; Q16539; -.
PRIDE; Q16539; -.
ProteomicsDB; 60901; -. [Q16539-1]
ProteomicsDB; 60902; -. [Q16539-2]
ProteomicsDB; 60903; -. [Q16539-3]
ProteomicsDB; 60904; -. [Q16539-4]
Antibodypedia; 4142; 2134 antibodies.
DNASU; 1432; -.
Ensembl; ENST00000229794; ENSP00000229794; ENSG00000112062. [Q16539-1]
Ensembl; ENST00000229795; ENSP00000229795; ENSG00000112062. [Q16539-2]
Ensembl; ENST00000310795; ENSP00000308669; ENSG00000112062. [Q16539-4]
GeneID; 1432; -.
KEGG; hsa:1432; -.
UCSC; uc003olp.4; human. [Q16539-1]
CTD; 1432; -.
DisGeNET; 1432; -.
EuPathDB; HostDB:ENSG00000112062.10; -.
GeneCards; MAPK14; -.
HGNC; HGNC:6876; MAPK14.
HPA; ENSG00000112062; Low tissue specificity.
MIM; 600289; gene.
neXtProt; NX_Q16539; -.
OpenTargets; ENSG00000112062; -.
PharmGKB; PA30621; -.
eggNOG; KOG0660; Eukaryota.
GeneTree; ENSGT00940000155325; -.
InParanoid; Q16539; -.
KO; K04441; -.
OMA; EITNRYT; -.
OrthoDB; 683132at2759; -.
PhylomeDB; Q16539; -.
TreeFam; TF105100; -.
BioCyc; MetaCyc:HS03507-MONOMER; -.
BRENDA; 2.7.11.24; 2681.
PathwayCommons; Q16539; -.
Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
Reactome; R-HSA-171007; p38MAPK events.
Reactome; R-HSA-198753; ERK/MAPK targets.
Reactome; R-HSA-2151209; Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-376172; DSCAM interactions.
Reactome; R-HSA-418592; ADP signalling through P2Y purinoceptor 1.
Reactome; R-HSA-432142; Platelet sensitization by LDL.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-450302; activated TAK1 mediates p38 MAPK activation.
Reactome; R-HSA-450341; Activation of the AP-1 family of transcription factors.
Reactome; R-HSA-450604; KSRP (KHSRP) binds and destabilizes mRNA.
Reactome; R-HSA-525793; Myogenesis.
Reactome; R-HSA-5668599; RHO GTPases Activate NADPH Oxidases.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-9662834; CD163 mediating an anti-inflammatory response.
SignaLink; Q16539; -.
SIGNOR; Q16539; -.
BioGRID-ORCS; 1432; 46 hits in 911 CRISPR screens.
ChiTaRS; MAPK14; human.
EvolutionaryTrace; Q16539; -.
GeneWiki; MAPK14; -.
GenomeRNAi; 1432; -.
Pharos; Q16539; Tchem.
PRO; PR:Q16539; -.
Proteomes; UP000005640; Chromosome 6.
RNAct; Q16539; protein.
Bgee; ENSG00000112062; Expressed in blood and 236 other tissues.
ExpressionAtlas; Q16539; baseline and differential.
Genevisible; Q16539; HS.
GO; GO:0005623; C:cell; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0000922; C:spindle pole; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0004707; F:MAP kinase activity; IDA:UniProtKB.
GO; GO:0004708; F:MAP kinase kinase activity; TAS:ProtInc.
GO; GO:0048273; F:mitogen-activated protein kinase p38 binding; IPI:UniProtKB.
GO; GO:0051525; F:NFAT protein binding; ISS:BHF-UCL.
GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:Reactome.
GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; TAS:UniProtKB.
GO; GO:0000187; P:activation of MAPK activity; TAS:Reactome.
GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0001502; P:cartilage condensation; IEA:Ensembl.
GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:0071479; P:cellular response to ionizing radiation; IMP:BHF-UCL.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
GO; GO:0071223; P:cellular response to lipoteichoic acid; IMP:UniProtKB.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IMP:BHF-UCL.
GO; GO:0098586; P:cellular response to virus; IMP:UniProtKB.
GO; GO:0006935; P:chemotaxis; TAS:ProtInc.
GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
GO; GO:0000077; P:DNA damage checkpoint; IEA:Ensembl.
GO; GO:0019395; P:fatty acid oxidation; IEA:Ensembl.
GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IEA:Ensembl.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:0035331; P:negative regulation of hippo signaling; IMP:FlyBase.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0030316; P:osteoclast differentiation; ISS:BHF-UCL.
GO; GO:0038066; P:p38MAPK cascade; ISS:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:BHF-UCL.
GO; GO:0001890; P:placenta development; IEA:Ensembl.
GO; GO:0090336; P:positive regulation of brown fat cell differentiation; IEA:Ensembl.
GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IEA:Ensembl.
GO; GO:0031281; P:positive regulation of cyclase activity; IMP:CACAO.
GO; GO:0002741; P:positive regulation of cytokine secretion involved in immune response; IEA:Ensembl.
GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IMP:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0046326; P:positive regulation of glucose import; IEA:Ensembl.
GO; GO:2001184; P:positive regulation of interleukin-12 secretion; IMP:UniProtKB.
GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IEA:Ensembl.
GO; GO:1905050; P:positive regulation of metallopeptidase activity; IEA:Ensembl.
GO; GO:0051149; P:positive regulation of muscle cell differentiation; TAS:Reactome.
GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:UniProtKB.
GO; GO:1901741; P:positive regulation of myoblast fusion; ISS:UniProtKB.
GO; GO:0010831; P:positive regulation of myotube differentiation; ISS:UniProtKB.
GO; GO:0042307; P:positive regulation of protein import into nucleus; IEA:Ensembl.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0007265; P:Ras protein signal transduction; TAS:Reactome.
GO; GO:1900015; P:regulation of cytokine production involved in inflammatory response; IDA:CACAO.
GO; GO:0051090; P:regulation of DNA-binding transcription factor activity; TAS:Reactome.
GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
GO; GO:0030278; P:regulation of ossification; IEA:Ensembl.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0099179; P:regulation of synaptic membrane adhesion; IEA:Ensembl.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0032495; P:response to muramyl dipeptide; IEA:Ensembl.
GO; GO:0035994; P:response to muscle stretch; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0042770; P:signal transduction in response to DNA damage; IMP:BHF-UCL.
GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
GO; GO:0090400; P:stress-induced premature senescence; IMP:BHF-UCL.
GO; GO:0051146; P:striated muscle cell differentiation; IEA:Ensembl.
GO; GO:0007178; P:transmembrane receptor protein serine/threonine kinase signaling pathway; IEA:Ensembl.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IMP:BHF-UCL.
CDD; cd07877; STKc_p38alpha; 1.
IDEAL; IID00280; -.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR003527; MAP_kinase_CS.
InterPro; IPR008352; MAPK_p38-like.
InterPro; IPR038784; p38alpha.
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; Acetylation; Alternative splicing; Apoptosis; ATP-binding;
Cytoplasm; Direct protein sequencing; Kinase; Nucleotide-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Stress response; Transcription;
Transcription regulation; Transferase; Ubl conjugation.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:12665801"
CHAIN 2..360
/note="Mitogen-activated protein kinase 14"
/id="PRO_0000186291"
DOMAIN 24..308
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 30..38
/note="ATP"
REGION 70..71
/note="Inhibitor-binding"
REGION 106..110
/note="Inhibitor-binding"
REGION 168..169
/note="Inhibitor-binding"
MOTIF 180..182
/note="TXY"
ACT_SITE 168
/note="Proton acceptor"
BINDING 35
/note="Inhibitor"
/evidence="ECO:0000269|PubMed:12897767,
ECO:0000269|PubMed:15658854, ECO:0000269|PubMed:16342939"
BINDING 53
/note="ATP"
BINDING 53
/note="Inhibitor"
/evidence="ECO:0000269|PubMed:12897767,
ECO:0000269|PubMed:15658854, ECO:0000269|PubMed:16342939"
BINDING 71
/note="Inhibitor"
/evidence="ECO:0000269|PubMed:12897767,
ECO:0000269|PubMed:15658854, ECO:0000269|PubMed:16342939"
BINDING 109
/note="Inhibitor; via amide nitrogen and carbonyl oxygen"
/evidence="ECO:0000269|PubMed:12897767,
ECO:0000269|PubMed:15658854, ECO:0000269|PubMed:16342939"
BINDING 154
/note="Inhibitor; via carbonyl oxygen"
/evidence="ECO:0000269|PubMed:12897767,
ECO:0000269|PubMed:15658854, ECO:0000269|PubMed:16342939"
BINDING 168
/note="Inhibitor; via amide nitrogen and carbonyl oxygen"
/evidence="ECO:0000269|PubMed:12897767,
ECO:0000269|PubMed:15658854, ECO:0000269|PubMed:16342939"
BINDING 197
/note="Inhibitor"
/evidence="ECO:0000269|PubMed:12897767,
ECO:0000269|PubMed:15658854, ECO:0000269|PubMed:16342939"
BINDING 252
/note="Inhibitor; via amide nitrogen"
/evidence="ECO:0000269|PubMed:12897767,
ECO:0000269|PubMed:15658854, ECO:0000269|PubMed:16342939"
MOD_RES 2
/note="N-acetylserine"
/evidence="ECO:0000244|PubMed:20068231"
MOD_RES 2
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163"
MOD_RES 16
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:18691976"
MOD_RES 53
/note="N6-acetyllysine"
/evidence="ECO:0000269|PubMed:21444723"
MOD_RES 152
/note="N6-acetyllysine"
/evidence="ECO:0000269|PubMed:21444723"
MOD_RES 180
/note="Phosphothreonine; by MAP2K3, MAP2K4, MAP2K6 and
autocatalysis"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163, ECO:0000269|PubMed:7535770"
MOD_RES 182
/note="Phosphotyrosine; by MAP2K3, MAP2K4, MAP2K6 and
autocatalysis"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163, ECO:0000269|PubMed:7535770"
MOD_RES 263
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:17525332"
MOD_RES 323
/note="Phosphotyrosine; by ZAP70"
/evidence="ECO:0000269|PubMed:15735648"
VAR_SEQ 230..254
/note="DQLKLILRLVGTPGAELLKKISSES -> NQLQQIMRLTGTPPAYLINRMPS
HE (in isoform CSBP1)"
/evidence="ECO:0000303|PubMed:7997261"
/id="VSP_004842"
VAR_SEQ 255..360
/note="ARNYIQSLTQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHA
YFAQYHDPDDEPVADPYDQSFESRDLLIDEWKSLTYDEVISFVPPPLDQEEMES -> V
S (in isoform 5)"
/evidence="ECO:0000303|PubMed:19906316"
/id="VSP_057194"
VAR_SEQ 255..307
/note="ARNYIQSLTQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHA
Y -> LSTCWRRCLYWTQIRELQRPKPLHMPTLLSTTILMMNQWPILMISPLKAGTSL
(in isoform Exip)"
/evidence="ECO:0000303|PubMed:11866441"
/id="VSP_004843"
VAR_SEQ 281..360
/note="AVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPDDEPVADPYDQSFESRDL
LIDEWKSLTYDEVISFVPPPLDQEEMES -> GKLTIYPHLMDIELVMI (in
isoform Mxi2)"
/evidence="ECO:0000303|PubMed:7479834"
/id="VSP_004844"
VAR_SEQ 308..360
/note="Missing (in isoform Exip)"
/evidence="ECO:0000303|PubMed:11866441"
/id="VSP_004845"
VARIANT 51
/note="A -> V (in a gastric adenocarcinoma sample; somatic
mutation)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_042270"
VARIANT 322
/note="P -> R (in a lung adenocarcinoma sample; somatic
mutation)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_042271"
VARIANT 343
/note="D -> G (in dbSNP:rs45496794)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_042272"
MUTAGEN 34
/note="A->V: Lowered kinase activity."
/evidence="ECO:0000269|PubMed:7493921"
MUTAGEN 53
/note="K->R: Loss of kinase activity."
/evidence="ECO:0000269|PubMed:7493921"
MUTAGEN 54
/note="K->R: Impairs MAP2K6/MKK6-dependent
autophosphorylation."
/evidence="ECO:0000269|PubMed:11010976"
MUTAGEN 69
/note="Y->H: Lowered kinase activity."
/evidence="ECO:0000269|PubMed:15284239"
MUTAGEN 168
/note="D->A: Loss of kinase activity."
/evidence="ECO:0000269|PubMed:7493921"
MUTAGEN 175
/note="T->A: No effect on either the kinase activity or
tyrosine phosphorylation."
/evidence="ECO:0000269|PubMed:7493921"
MUTAGEN 176
/note="D->A: Emulation of the active state. Increase in
activity; when associated with S-327 or L-327."
/evidence="ECO:0000269|PubMed:15284239"
MUTAGEN 177
/note="D->A: Loss of kinase activity."
/evidence="ECO:0000269|PubMed:15284239"
MUTAGEN 180
/note="T->E: Loss of kinase activity."
/evidence="ECO:0000269|PubMed:7493921"
MUTAGEN 182
/note="Y->F: Loss of kinase activity."
/evidence="ECO:0000269|PubMed:7493921"
MUTAGEN 320
/note="A->T: Lowered kinase activity."
/evidence="ECO:0000269|PubMed:15284239"
MUTAGEN 327
/note="F->L: Emulation of the active state. Increase in
activity; when associated with A-176."
/evidence="ECO:0000269|PubMed:15284239"
MUTAGEN 327
/note="F->S: Emulation of the active state. Increase in
activity; when associated with A-176."
/evidence="ECO:0000269|PubMed:15284239"
MUTAGEN 337
/note="W->R: Loss of kinase activity."
/evidence="ECO:0000269|PubMed:15284239"
CONFLICT 67
/note="R -> G (in Ref. 7; BAF84398)"
/evidence="ECO:0000305"
STRAND 8..13
/evidence="ECO:0000244|PDB:2FST"
STRAND 16..21
/evidence="ECO:0000244|PDB:2FST"
STRAND 24..29
/evidence="ECO:0000244|PDB:2FST"
HELIX 31..33
/evidence="ECO:0000244|PDB:6SFI"
TURN 34..36
/evidence="ECO:0000244|PDB:3BV2"
STRAND 38..43
/evidence="ECO:0000244|PDB:2FST"
TURN 44..47
/evidence="ECO:0000244|PDB:2FST"
STRAND 48..54
/evidence="ECO:0000244|PDB:2FST"
HELIX 62..77
/evidence="ECO:0000244|PDB:2FST"
STRAND 87..90
/evidence="ECO:0000244|PDB:2FST"
HELIX 96..98
/evidence="ECO:0000244|PDB:2FST"
STRAND 103..107
/evidence="ECO:0000244|PDB:2FST"
STRAND 110..112
/evidence="ECO:0000244|PDB:3LFF"
TURN 113..115
/evidence="ECO:0000244|PDB:4GEO"
TURN 116..119
/evidence="ECO:0000244|PDB:3LFF"
HELIX 124..143
/evidence="ECO:0000244|PDB:2FST"
HELIX 153..155
/evidence="ECO:0000244|PDB:2FST"
STRAND 156..158
/evidence="ECO:0000244|PDB:2FST"
TURN 160..162
/evidence="ECO:0000244|PDB:2RG6"
STRAND 164..166
/evidence="ECO:0000244|PDB:2FST"
STRAND 168..170
/evidence="ECO:0000244|PDB:4GEO"
HELIX 173..175
/evidence="ECO:0000244|PDB:1ZZL"
TURN 176..179
/evidence="ECO:0000244|PDB:5XYY"
STRAND 180..182
/evidence="ECO:0000244|PDB:3FMK"
TURN 185..188
/evidence="ECO:0000244|PDB:3LFF"
HELIX 191..194
/evidence="ECO:0000244|PDB:2FST"
STRAND 197..199
/evidence="ECO:0000244|PDB:4EHV"
HELIX 204..218
/evidence="ECO:0000244|PDB:2FST"
HELIX 228..239
/evidence="ECO:0000244|PDB:2FST"
HELIX 244..247
/evidence="ECO:0000244|PDB:2FST"
HELIX 253..260
/evidence="ECO:0000244|PDB:2FST"
HELIX 270..273
/evidence="ECO:0000244|PDB:2FST"
TURN 274..276
/evidence="ECO:0000244|PDB:2FST"
HELIX 279..288
/evidence="ECO:0000244|PDB:2FST"
HELIX 293..295
/evidence="ECO:0000244|PDB:2FST"
HELIX 299..303
/evidence="ECO:0000244|PDB:2FST"
HELIX 306..308
/evidence="ECO:0000244|PDB:2FST"
TURN 309..311
/evidence="ECO:0000244|PDB:2FST"
HELIX 314..316
/evidence="ECO:0000244|PDB:2FST"
HELIX 325..327
/evidence="ECO:0000244|PDB:2FST"
HELIX 334..347
/evidence="ECO:0000244|PDB:2FST"
SEQUENCE 360 AA; 41293 MW; 286C81D0487618B3 CRC64;
MSQERPTFYR QELNKTIWEV PERYQNLSPV GSGAYGSVCA AFDTKTGLRV AVKKLSRPFQ
SIIHAKRTYR ELRLLKHMKH ENVIGLLDVF TPARSLEEFN DVYLVTHLMG ADLNNIVKCQ
KLTDDHVQFL IYQILRGLKY IHSADIIHRD LKPSNLAVNE DCELKILDFG LARHTDDEMT
GYVATRWYRA PEIMLNWMHY NQTVDIWSVG CIMAELLTGR TLFPGTDHID QLKLILRLVG
TPGAELLKKI SSESARNYIQ SLTQMPKMNF ANVFIGANPL AVDLLEKMLV LDSDKRITAA
QALAHAYFAQ YHDPDDEPVA DPYDQSFESR DLLIDEWKSL TYDEVISFVP PPLDQEEMES


Related products :

Catalog number Product name Quantity
18-785-210329 P38 MAPK (Phospho-Tyr182) - EC 2.7.11.24; Mitogen-activated protein kinase p38 alpha; MAP kinase p38 alpha; Cytokine suppressive anti-inflammatory drug-binding protein; CSAID-binding protein; CSBP; MA 0.1 mg
18-785-210329 P38 MAPK (Phospho-Tyr182) - EC 2.7.11.24; Mitogen-activated protein kinase p38 alpha; MAP kinase p38 alpha; Cytokine suppressive anti-inflammatory drug-binding protein; CSAID-binding protein; CSBP; MA 0.05 mg
18-785-210328 P38 MAPK (Phospho-Thr180) - EC 2.7.11.24; Mitogen-activated protein kinase p38 alpha; MAP kinase p38 alpha; Cytokine suppressive anti-inflammatory drug-binding protein; CSAID-binding protein; CSBP; MA 0.1 mg
18-785-210328 P38 MAPK (Phospho-Thr180) - EC 2.7.11.24; Mitogen-activated protein kinase p38 alpha; MAP kinase p38 alpha; Cytokine suppressive anti-inflammatory drug-binding protein; CSAID-binding protein; CSBP; MA 0.05 mg
18-785-210330 P38 MAPK (Ab-182) - EC 2.7.11.24; Mitogen-activated protein kinase p38 alpha; MAP kinase p38 alpha; Cytokine suppressive anti-inflammatory drug-binding protein; CSAID-binding protein; CSBP; MAX-intera 0.1 mg
18-785-210330 P38 MAPK (Ab-182) - EC 2.7.11.24; Mitogen-activated protein kinase p38 alpha; MAP kinase p38 alpha; Cytokine suppressive anti-inflammatory drug-binding protein; CSAID-binding protein; CSBP; MAX-intera 0.05 mg
EIAAB24876 CSAID-binding protein,CSBP,CSBP,CSBP1,CSBP2,CSPB1,Cytokine suppressive anti-inflammatory drug-binding protein,Homo sapiens,Human,MAP kinase 14,MAP kinase MXI2,MAP kinase p38 alpha,MAPK 14,MAPK14,MAX-i
EIAAB24870 Homo sapiens,Human,MAP kinase 13,MAP kinase p38 delta,MAPK 13,MAPK13,Mitogen-activated protein kinase 13,Mitogen-activated protein kinase p38 delta,PRKM13,SAPK4,Stress-activated protein kinase 4
EIAAB24864 Homo sapiens,Human,MAP kinase 11,MAP kinase p38 beta,MAPK 11,MAPK11,Mitogen-activated protein kinase 11,Mitogen-activated protein kinase p38 beta,p38-2,p38b,PRKM11,SAPK2,Stress-activated protein kinas
EIAAB24855 c-Jun N-terminal kinase 1,Homo sapiens,Human,JNK1,JNK-46,MAP kinase 8,MAPK 8,MAPK8,Mitogen-activated protein kinase 8,PRKM8,SAPK1,Stress-activated protein kinase 1,Stress-activated protein kinase JNK1
EIAAB24872 MAP kinase 13,MAP kinase p38 delta,MAPK 13,Mapk13,Mitogen-activated protein kinase 13,Mitogen-activated protein kinase p38 delta,Mouse,Mus musculus,Serk4,Stress-activated protein kinase 4
EIAAB41230 Homo sapiens,Human,KIAA0733,MAP3K7IP2,Mitogen-activated protein kinase kinase kinase 7-interacting protein 2,TAB2,TAB-2,TAK1-binding protein 2,TGF-beta-activated kinase 1 and MAP3K7-binding protein 2,
EIAAB41234 Homo sapiens,Human,MAP3K7IP3,Mitogen-activated protein kinase kinase kinase 7-interacting protein 3,NF-kappa-B-activating protein 1,TAB3,TAB-3,TAK1-binding protein 3,TGF-beta-activated kinase 1 and MA
EIAAB41233 Kiaa4135,Map3k7ip3,Mitogen-activated protein kinase kinase kinase 7-interacting protein 3,Mouse,Mus musculus,Tab3,TAB-3,TAK1-binding protein 3,TGF-beta-activated kinase 1 and MAP3K7-binding protein 3,
EIAAB41231 Kiaa0733,Map3k7ip2,Mitogen-activated protein kinase kinase kinase 7-interacting protein 2,Mouse,Mus musculus,Tab2,TAB-2,TAK1-binding protein 2,TGF-beta-activated kinase 1 and MAP3K7-binding protein 2,
EIAAB24858 c-Jun N-terminal kinase 2,Jnk2,MAP kinase 9,MAPK 9,Mapk9,Mitogen-activated protein kinase 9,p54-alpha,Prkm9,Rat,Rattus norvegicus,SAPK-alpha,Stress-activated protein kinase JNK2
EIAAB24874 CRK1,Csbp1,Csbp2,MAP kinase 14,MAP kinase p38 alpha,MAPK 14,Mapk14,Mitogen-activated protein kinase 14,Mitogen-activated protein kinase p38 alpha,Rat,Rattus norvegicus
EIAAB24869 MAP kinase 13,MAP kinase p38 delta,MAPK 13,Mapk13,Mitogen-activated protein kinase 13,Mitogen-activated protein kinase p38 delta,Rat,Rattus norvegicus,Stress-activated protein kinase 4
E1206b ELISA Bos taurus,Bovine,ERK2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAPK 1,MAPK 2,MAPK1,Mitogen-activated protein kinase 1,Mitogen-activated protein kinase 2,PRKM 96T
U1206b CLIA Bos taurus,Bovine,ERK2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAPK 1,MAPK 2,MAPK1,Mitogen-activated protein kinase 1,Mitogen-activated protein kinase 2,PRKM1 96T
10-782-55059 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.005 mg
10-782-55060 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.05 mg
10-782-55060 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.02 mg
10-782-55059 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.02 mg
10-782-55059 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.01 mg
Pathways :
WP1493: Carbon assimilation C4 pathway
WP1531: Vitamin D synthesis
WP2292: Chemokine signaling pathway
WP2199: Seed Development
WP731: Sterol regulatory element binding protein related
WP32: Translation Factors
WP1566: Citrate cycle (TCA cycle)
WP1616: ABC transporters
WP210: Cytoplasmic Ribosomal Proteins
WP1502: Mitochondrial biogenesis
WP1689: Porphyrin and chlorophyll metabolism
WP1650: Fluorobenzoate degradation
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP1892: Protein folding
WP1693: Purine metabolism
WP346: Protein Modifications
WP1701: Starch and sucrose metabolism
WP2203: TSLP Signaling Pathway
WP1661: Glyoxylate and dicarboxylate metabolism
WP1909: Signal regulatory protein (SIRP) family interactions
WP1946: Cori Cycle
WP1714: Tyrosine metabolism
WP2272: Pathogenic Escherichia coli infection
WP1672: Mismatch repair
WP1438: Influenza A virus infection

Related Genes :
[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)
[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)
[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)
[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)
[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)
[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 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)
[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)
[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 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)
[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)
[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)
[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)
[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)
[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)
[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)
[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)
[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)
[p38b CG7393] Mitogen-activated protein kinase p38b (MAP kinase p38b) (MAPK p38b) (EC 2.7.11.24)
[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)
[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) (Stress-activated protein kinase JNK1) (c-Jun N-terminal kinase 1)
[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)
[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)
[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)

Bibliography :