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Database: UniProt
Entry: Q16539
LinkDB: Q16539
Original site: Q16539 
ID   MK14_HUMAN              Reviewed;         360 AA.
AC   Q16539; A6ZJ92; A8K6P4; B0LPH0; B5TY32; O60776; Q13083; Q14084;
AC   Q8TDX0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   31-JUL-2019, entry version 233.
DE   RecName: Full=Mitogen-activated protein kinase 14;
DE            Short=MAP kinase 14;
DE            Short=MAPK 14;
DE            EC=2.7.11.24 {ECO:0000269|PubMed:11010976, ECO:0000269|PubMed:15284239, ECO:0000269|PubMed:7493921};
DE   AltName: Full=Cytokine suppressive anti-inflammatory drug-binding protein;
DE            Short=CSAID-binding protein;
DE            Short=CSBP;
DE   AltName: Full=MAP kinase MXI2;
DE   AltName: Full=MAX-interacting protein 2;
DE   AltName: Full=Mitogen-activated protein kinase p38 alpha;
DE            Short=MAP kinase p38 alpha;
DE   AltName: Full=Stress-activated protein kinase 2a;
DE            Short=SAPK2a;
GN   Name=MAPK14; Synonyms=CSBP, CSBP1, CSBP2, CSPB1, MXI2, SAPK2A;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CSBP1 AND CSBP2), AND PARTIAL
RP   PROTEIN SEQUENCE.
RC   TISSUE=Peripheral blood;
RX   PubMed=7997261; DOI=10.1038/372739a0;
RA   Lee J.C., Laydon J.T., McDonnell P.C., Gallagher T.F., Kumar S.,
RA   Green D., McNulty D., Blumenthal M.J., Heys R.J., Landvatter S.W.,
RA   Strickler J.E., McLaughlin M.M., Siemens I.R., Fisher S.M., Livi G.P.,
RA   White J.R., Adams J.L., Young P.R.;
RT   "A protein kinase involved in the regulation of inflammatory cytokine
RT   biosynthesis.";
RL   Nature 372:739-746(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CSBP2).
RC   TISSUE=Liver;
RX   PubMed=7696354; DOI=10.1016/0167-4889(95)00002-A;
RA   Han J., Richter B., Li Z., Kravchenko V.V., Ulevitch R.J.;
RT   "Molecular cloning of human p38 MAP kinase.";
RL   Biochim. Biophys. Acta 1265:224-227(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MXI2).
RX   PubMed=7479834; DOI=10.1073/pnas.92.23.10531;
RA   Zervos A.S., Faccio L., Gatto J.P., Kyriakis J.M., Brent R.;
RT   "Mxi2, a mitogen-activated protein kinase that recognizes and
RT   phosphorylates Max protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:10531-10534(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CSBP2).
RC   TISSUE=B-cell;
RX   PubMed=10727080; DOI=10.3109/10425179909033952;
RA   Herbison C.E., Sayer D.C., Bellgard M., Allcock R.J.N.,
RA   Christiansen F.T., Price P.;
RT   "Structure and polymorphism of two stress-activated protein kinase
RT   genes centromeric of the MHC: SAPK2a and SAPK4.";
RL   DNA Seq. 10:229-243(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM EXIP), AND ACTIVITY REGULATION.
RC   TISSUE=Renal cell carcinoma;
RX   PubMed=11866441; DOI=10.1006/bbrc.2002.6529;
RA   Sudo T., Yagasaki Y., Hama H., Watanabe N., Osada H.;
RT   "Exip, a new alternative splicing variant of p38 alpha, can induce an
RT   earlier onset of apoptosis in HeLa cells.";
RL   Biochem. Biophys. Res. Commun. 291:838-843(2002).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RX   PubMed=19906316; DOI=10.1186/1471-2164-10-518;
RA   Wang P., Yu P., Gao P., Shi T., Ma D.;
RT   "Discovery of novel human transcript variants by analysis of intronic
RT   single-block EST with polyadenylation site.";
RL   BMC Genomics 10:518-518(2009).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CSBP2).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CSBP2).
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA   Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA   Korn B., Zuo D., Hu Y., LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   NHLBI resequencing and genotyping service (RS&G);
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [13]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CSBP2).
RC   TISSUE=Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [14]
RP   PROTEIN SEQUENCE OF 2-10.
RC   TISSUE=Platelet;
RX   PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA   Thomas G.R., Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass
RT   spectrometric identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [15]
RP   PROTEIN SEQUENCE OF 174-186.
RX   PubMed=7923354; DOI=10.1016/0092-8674(94)90278-X;
RA   Freshney N.W., Rawlinson L., Guesdon F., Jones E., Cowley S.,
RA   Hsuan J., Saklatvala J.;
RT   "Interleukin-1 activates a novel protein kinase cascade that results
RT   in the phosphorylation of Hsp27.";
RL   Cell 78:1039-1049(1994).
RN   [16]
RP   PHOSPHORYLATION AT THR-180 AND TYR-182, ACTIVITY REGULATION, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=7535770; DOI=10.1074/jbc.270.13.7420;
RA   Raingeaud J., Gupta S., Rogers J.S., Dickens M., Han J.,
RA   Ulevitch R.J., Davis R.J.;
RT   "Pro-inflammatory cytokines and environmental stress cause p38
RT   mitogen-activated protein kinase activation by dual phosphorylation on
RT   tyrosine and threonine.";
RL   J. Biol. Chem. 270:7420-7426(1995).
RN   [17]
RP   MUTAGENESIS OF ALA-34; LYS-53; ASP-168; THR-175; THR-180 AND TYR-182,
RP   AND CATALYTIC ACTIVITY.
RX   PubMed=7493921; DOI=10.1074/jbc.270.49.29043;
RA   Kumar S., McLaughlin M.M., McDonnell P.C., Lee J.C., Livi G.P.,
RA   Young P.R.;
RT   "Human mitogen-activated protein kinase CSBP1, but not CSBP2,
RT   complements a hog1 deletion in yeast.";
RL   J. Biol. Chem. 270:29043-29046(1995).
RN   [18]
RP   PHOSPHORYLATION BY MAP2K3/MKK3 AND MAP2K6/MKK6, AND ACTIVITY
RP   REGULATION.
RX   PubMed=8622669; DOI=10.1128/MCB.16.3.1247;
RA   Raingeaud J., Whitmarsh A.J., Barrett T., Derijard B., Davis R.J.;
RT   "MKK3- and MKK6-regulated gene expression is mediated by the p38
RT   mitogen-activated protein kinase signal transduction pathway.";
RL   Mol. Cell. Biol. 16:1247-1255(1996).
RN   [19]
RP   FUNCTION IN ACTIVATION OF RPS6KA5/MSK1.
RX   PubMed=9687510; DOI=10.1093/emboj/17.15.4426;
RA   Deak M., Clifton A.D., Lucocq J.M., Alessi D.R.;
RT   "Mitogen- and stress-activated protein kinase-1 (MSK1) is directly
RT   activated by MAPK and SAPK2/p38, and may mediate activation of CREB.";
RL   EMBO J. 17:4426-4441(1998).
RN   [20]
RP   FUNCTION IN PHOSPHORYLATION OF ATF2; ELK1 AND MBP, AND ACTIVITY
RP   REGULATION.
RX   PubMed=9430721; DOI=10.1074/jbc.273.3.1741;
RA   Enslen H., Raingeaud J., Davis R.J.;
RT   "Selective activation of p38 mitogen-activated protein (MAP) kinase
RT   isoforms by the MAP kinase kinases MKK3 and MKK6.";
RL   J. Biol. Chem. 273:1741-1748(1998).
RN   [21]
RP   INTERACTION WITH RPS6KA4, FUNCTION IN PHOSPHORYLATION OF RPS6KA4, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=9792677; DOI=10.1074/jbc.273.45.29661;
RA   Pierrat B., Correia J.D.S., Mary J.L., Tomas-Zuber M., Lesslauer W.;
RT   "RSK-B, a novel ribosomal S6 kinase family member, is a CREB kinase
RT   under dominant control of p38alpha mitogen-activated protein kinase
RT   (p38alphaMAPK).";
RL   J. Biol. Chem. 273:29661-29671(1998).
RN   [22]
RP   INTERACTION WITH DUSP10, AND ACTIVITY REGULATION.
RX   PubMed=10391943; DOI=10.1074/jbc.274.28.19949;
RA   Tanoue T., Moriguchi T., Nishida E.;
RT   "Molecular cloning and characterization of a novel dual specificity
RT   phosphatase, MKP-5.";
RL   J. Biol. Chem. 274:19949-19956(1999).
RN   [23]
RP   FUNCTION IN PHOSPHORYLATION OF MEF2A.
RX   PubMed=9858528; DOI=10.1128/MCB.19.1.21;
RA   Zhao M., New L., Kravchenko V.V., Kato Y., Gram H., di Padova F.,
RA   Olson E.N., Ulevitch R.J., Han J.-D.;
RT   "Regulation of the MEF2 family of transcription factors by p38.";
RL   Mol. Cell. Biol. 19:21-30(1999).
RN   [24]
RP   FUNCTION IN PHOSPHORYLATION OF MEF2A AND MEF2C.
RX   PubMed=10330143; DOI=10.1128/MCB.19.6.4028;
RA   Yang S.-H., Galanis A., Sharrocks A.D.;
RT   "Targeting of p38 mitogen-activated protein kinases to MEF2
RT   transcription factors.";
RL   Mol. Cell. Biol. 19:4028-4038(1999).
RN   [25]
RP   FUNCTION.
RC   TISSUE=Hepatoma;
RX   PubMed=10943842; DOI=10.1016/S0092-8674(00)00027-1;
RA   Tamura K., Sudo T., Senftleben U., Dadak A.M., Johnson R., Karin M.;
RT   "Requirement for p38alpha in erythropoietin expression: a role for
RT   stress kinases in erythropoiesis.";
RL   Cell 102:221-231(2000).
RN   [26]
RP   FUNCTION (ISOFORM MXI2), COFACTOR, AND ACTIVITY REGULATION.
RX   PubMed=10838079; DOI=10.1016/S0014-5793(00)01598-2;
RA   Sanz V., Arozarena I., Crespo P.;
RT   "Distinct carboxy-termini confer divergent characteristics to the
RT   mitogen-activated protein kinase p38alpha and its splice isoform
RT   Mxi2.";
RL   FEBS Lett. 474:169-174(2000).
RN   [27]
RP   INTERACTION WITH CSNK2A1 AND CSNK2B, AND FUNCTION IN ACTIVATION OF
RP   CASEIN KINASE II.
RX   PubMed=10747897; DOI=10.1074/jbc.M000312200;
RA   Sayed M., Kim S.O., Salh B.S., Issinger O.G., Pelech S.L.;
RT   "Stress-induced activation of protein kinase CK2 by direct interaction
RT   with p38 mitogen-activated protein kinase.";
RL   J. Biol. Chem. 275:16569-16573(2000).
RN   [28]
RP   INTERACTION WITH MA2PK6/MKK6, PHOSPHORYLATION BY MAP2K6/MKK6,
RP   AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-54, AND CATALYTIC ACTIVITY.
RX   PubMed=11010976; DOI=10.1074/jbc.M007835200;
RA   Alonso G., Ambrosino C., Jones M., Nebreda A.R.;
RT   "Differential activation of p38 mitogen-activated protein kinase
RT   isoforms depending on signal strength.";
RL   J. Biol. Chem. 275:40641-40648(2000).
RN   [29]
RP   INTERACTION WITH DUSP1, AND ACTIVITY REGULATION.
RX   PubMed=11278799; DOI=10.1074/jbc.M010966200;
RA   Slack D.N., Seternes O.M., Gabrielsen M., Keyse S.M.;
RT   "Distinct binding determinants for ERK2/p38alpha and JNK map kinases
RT   mediate catalytic activation and substrate selectivity of map kinase
RT   phosphatase-1.";
RL   J. Biol. Chem. 276:16491-16500(2001).
RN   [30]
RP   INTERACTION WITH DUSP16, AND ACTIVITY REGULATION.
RX   PubMed=11359773; DOI=10.1074/jbc.M101981200;
RA   Tanoue T., Yamamoto T., Maeda R., Nishida E.;
RT   "A Novel MAPK phosphatase MKP-7 acts preferentially on JNK/SAPK and
RT   p38 alpha and beta MAPKs.";
RL   J. Biol. Chem. 276:26629-26639(2001).
RN   [31]
RP   FUNCTION AS MKNK2 KINASE.
RX   PubMed=11154262; DOI=10.1128/MCB.21.3.743-754.2001;
RA   Scheper G.C., Morrice N.A., Kleijn M., Proud C.G.;
RT   "The mitogen-activated protein kinase signal-integrating kinase Mnk2
RT   is a eukaryotic initiation factor 4E kinase with high levels of basal
RT   activity in mammalian cells.";
RL   Mol. Cell. Biol. 21:743-754(2001).
RN   [32]
RP   INTERACTION WITH CDC25B AND CDC25C, AND FUNCTION IN PHOSPHORYLATION OF
RP   CDC25B AND CDC25C.
RX   PubMed=11333986; DOI=10.1038/35075107;
RA   Bulavin D.V., Higashimoto Y., Popoff I.J., Gaarde W.A., Basrur V.,
RA   Potapova O., Appella E., Fornace A.J. Jr.;
RT   "Initiation of a G2/M checkpoint after ultraviolet radiation requires
RT   p38 kinase.";
RL   Nature 411:102-107(2001).
RN   [33]
RP   INTERACTION WITH TAB1, AUTOPHOSPHORYLATION, ACTIVITY REGULATION, AND
RP   CATALYTIC ACTIVITY.
RX   PubMed=11847341; DOI=10.1126/science.1067289;
RA   Ge B., Gram H., Di Padova F., Huang B., New L., Ulevitch R.J., Luo Y.,
RA   Han J.;
RT   "MAPKK-independent activation of p38alpha mediated by TAB1-dependent
RT   autophosphorylation of p38alpha.";
RL   Science 295:1291-1294(2002).
RN   [34]
RP   MUTAGENESIS OF TYR-69; ASP-176; ASP-177; ALA-320; PHE-327 AND TRP-337.
RX   PubMed=15284239; DOI=10.1074/jbc.M404595200;
RA   Diskin R., Askari N., Capone R., Engelberg D., Livnah O.;
RT   "Active mutants of the human p38alpha mitogen-activated protein
RT   kinase.";
RL   J. Biol. Chem. 279:47040-47049(2004).
RN   [35]
RP   FUNCTION IN PHOSPHORYLATION OF S100A9.
RX   PubMed=15905572; DOI=10.4049/jimmunol.174.11.7257;
RA   Lominadze G., Rane M.J., Merchant M., Cai J., Ward R.A., McLeish K.R.;
RT   "Myeloid-related protein-14 is a p38 MAPK substrate in human
RT   neutrophils.";
RL   J. Immunol. 174:7257-7267(2005).
RN   [36]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT   cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [37]
RP   PHOSPHORYLATION AT TYR-323, AND ACTIVITY REGULATION.
RX   PubMed=15735648; DOI=10.1038/ni1177;
RA   Salvador J.M., Mittelstadt P.R., Guszczynski T., Copeland T.D.,
RA   Yamaguchi H., Appella E., Fornace A.J. Jr., Ashwell J.D.;
RT   "Alternative p38 activation pathway mediated by T cell receptor-
RT   proximal tyrosine kinases.";
RL   Nat. Immunol. 6:390-395(2005).
RN   [38]
RP   INTERACTION WITH TAB1, AUTOPHOSPHORYLATION, AND ACTIVITY REGULATION.
RX   PubMed=15735649; DOI=10.1038/ni1176;
RA   Salvador J.M., Mittelstadt P.R., Belova G.I., Fornace A.J. Jr.,
RA   Ashwell J.D.;
RT   "The autoimmune suppressor Gadd45alpha inhibits the T cell alternative
RT   p38 activation pathway.";
RL   Nat. Immunol. 6:396-402(2005).
RN   [39]
RP   INTERACTION WITH SUPT20H.
RX   PubMed=16751104; DOI=10.1016/j.cell.2006.03.048;
RA   Zohn I.E., Li Y., Skolnik E.Y., Anderson K.V., Han J., Niswander L.;
RT   "p38 and a p38-interacting protein are critical for downregulation of
RT   E-cadherin during mouse gastrulation.";
RL   Cell 125:957-969(2006).
RN   [40]
RP   FUNCTION IN STRESS-INDUCED INTERNALIZATION OF EGFR.
RX   PubMed=16932740; DOI=10.1038/sj.emboj.7601297;
RA   Zwang Y., Yarden Y.;
RT   "p38 MAP kinase mediates stress-induced internalization of EGFR:
RT   implications for cancer chemotherapy.";
RL   EMBO J. 25:4195-4206(2006).
RN   [41]
RP   FUNCTION IN PHOSPHORYLATION OF SIAH2, AND ACTIVITY REGULATION.
RX   PubMed=17003045; DOI=10.1074/jbc.M606568200;
RA   Khurana A., Nakayama K., Williams S., Davis R.J., Mustelin T.,
RA   Ronai Z.;
RT   "Regulation of the ring finger E3 ligase Siah2 by p38 MAPK.";
RL   J. Biol. Chem. 281:35316-35326(2006).
RN   [42]
RP   INTERACTION WITH NP60.
RX   PubMed=16352664; DOI=10.1242/jcs.02699;
RA   Fu J., Yang Z., Wei J., Han J., Gu J.;
RT   "Nuclear protein NP60 regulates p38 MAPK activity.";
RL   J. Cell Sci. 119:115-123(2006).
RN   [43]
RP   FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX   PubMed=17724032; DOI=10.1074/jbc.M703857200;
RA   Qi X., Pohl N.M., Loesch M., Hou S., Li R., Qin J.Z., Cuenda A.,
RA   Chen G.;
RT   "p38alpha antagonizes p38gamma activity through c-Jun-dependent
RT   ubiquitin-proteasome pathways in regulating Ras transformation and
RT   stress response.";
RL   J. Biol. Chem. 282:31398-31408(2007).
RN   [44]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-263, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [45]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Platelet;
RX   PubMed=18088087; DOI=10.1021/pr0704130;
RA   Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA   Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT   "Phosphoproteome of resting human platelets.";
RL   J. Proteome Res. 7:526-534(2008).
RN   [46]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-16, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [47]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180 AND TYR-182, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [48]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [49]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180 AND TYR-182, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [50]
RP   FUNCTION IN INHIBITION OF AUTOPHAGY.
RX   PubMed=19893488; DOI=10.1038/emboj.2009.321;
RA   Webber J.L., Tooze S.A.;
RT   "Coordinated regulation of autophagy by p38alpha MAPK through mAtg9
RT   and p38IP.";
RL   EMBO J. 29:27-40(2010).
RN   [51]
RP   FUNCTION IN PHOSPHORYLATION OF TIAR.
RX   PubMed=20932473; DOI=10.1016/j.molcel.2010.09.018;
RA   Reinhardt H.C., Hasskamp P., Schmedding I., Morandell S.,
RA   van Vugt M.A., Wang X., Linding R., Ong S.E., Weaver D., Carr S.A.,
RA   Yaffe M.B.;
RT   "DNA damage activates a spatially distinct late cytoplasmic cell-cycle
RT   checkpoint network controlled by MK2-mediated RNA stabilization.";
RL   Mol. Cell 40:34-49(2010).
RN   [52]
RP   INTERACTION WITH ADAM17, AND FUNCTION IN PHOSPHORYLATION OF ADAM17.
RX   PubMed=20188673; DOI=10.1016/j.molcel.2010.01.034;
RA   Xu P., Derynck R.;
RT   "Direct activation of TACE-mediated ectodomain shedding by p38 MAP
RT   kinase regulates EGF receptor-dependent cell proliferation.";
RL   Mol. Cell 37:551-566(2010).
RN   [53]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP   SCALE ANALYSIS] AT SER-2; THR-180 AND TYR-182, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [54]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [55]
RP   IDENTIFICATION IN A COMPLEX WITH AKAP13; PKN1; ZAK AND MAP2K3.
RX   PubMed=21224381; DOI=10.1074/jbc.M110.185645;
RA   Cariolato L., Cavin S., Diviani D.;
RT   "A-kinase anchoring protein (AKAP)-Lbc anchors a PKN-based signaling
RT   complex involved in alpha1-adrenergic receptor-induced p38
RT   activation.";
RL   J. Biol. Chem. 286:7925-7937(2011).
RN   [56]
RP   FUNCTION (MICROBIAL INFECTION).
RC   TISSUE=T-cell;
RX   PubMed=21586573; DOI=10.1074/jbc.M111.234062;
RA   Peng H., Wang X., Barnes P.F., Tang H., Townsend J.C., Samten B.;
RT   "The Mycobacterium tuberculosis early secreted antigenic target of 6
RT   kDa inhibits T cell interferon-gamma production through the p38
RT   mitogen-activated protein kinase pathway.";
RL   J. Biol. Chem. 286:24508-24518(2011).
RN   [57]
RP   ACETYLATION AT LYS-53 AND LYS-152 BY KAT2B/PCAF AND EP300, AND
RP   DEACETYLATION BY HDAC3.
RX   PubMed=21444723; DOI=10.1128/MCB.01205-10;
RA   Pillai V.B., Sundaresan N.R., Samant S.A., Wolfgeher D., Trivedi C.M.,
RA   Gupta M.P.;
RT   "Acetylation of a conserved lysine residue in the ATP binding pocket
RT   of p38 augments its kinase activity during hypertrophy of
RT   cardiomyocytes.";
RL   Mol. Cell. Biol. 31:2349-2363(2011).
RN   [58]
RP   INTERACTION WITH CDK5RAP3 AND PPM1D, AND DEPHOSPHORYLATION BY PPM1D.
RX   PubMed=21283629; DOI=10.1371/journal.pone.0016427;
RA   An H., Lu X., Liu D., Yarbrough W.G.;
RT   "LZAP inhibits p38 MAPK (p38) phosphorylation and activity by
RT   facilitating p38 association with the wild-type p53 induced
RT   phosphatase 1 (WIP1).";
RL   PLoS ONE 6:E16427-E16427(2011).
RN   [59]
RP   REVIEW ON FUNCTION.
RX   PubMed=12452429; DOI=10.1515/BC.2002.173;
RA   Shi Y., Gaestel M.;
RT   "In the cellular garden of forking paths: how p38 MAPKs signal for
RT   downstream assistance.";
RL   Biol. Chem. 383:1519-1536(2002).
RN   [60]
RP   REVIEW ON ACTIVITY REGULATION, AND REVIEW ON FUNCTION.
RX   PubMed=20626350; DOI=10.1042/BJ20100323;
RA   Cuadrado A., Nebreda A.R.;
RT   "Mechanisms and functions of p38 MAPK signalling.";
RL   Biochem. J. 429:403-417(2010).
RN   [61]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; THR-180 AND TYR-182,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [62]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [63]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA   Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [64]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX   PubMed=8910361; DOI=10.1074/jbc.271.44.27696;
RA   Wilson K.P., Fitzgibbon M.J., Caron P.R., Griffith J.P., Chen W.,
RA   McCaffrey P.G., Chambers S.P., Su M.S.-S.;
RT   "Crystal structure of p38 mitogen-activated protein kinase.";
RL   J. Biol. Chem. 271:27696-27700(1996).
RN   [65]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=9095200; DOI=10.1038/nsb0497-311;
RA   Tong L., Pav S., White D.M., Rogers S., Crane K.M., Cywin C.L.,
RA   Brown M.L., Pargellis C.A.;
RT   "A highly specific inhibitor of human p38 MAP kinase binds in the ATP
RT   pocket.";
RL   Nat. Struct. Biol. 4:311-316(1997).
RN   [66]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   PubMed=9753691; DOI=10.1016/S0969-2126(98)00113-0;
RA   Wang Z., Canagarajah B.J., Boehm J.C., Kassisa S., Cobb M.H.,
RA   Young P.R., Abdel-Meguid S., Adams J.L., Goldsmith E.J.;
RT   "Structural basis of inhibitor selectivity in MAP kinases.";
RL   Structure 6:1117-1128(1998).
RN   [67]
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS).
RX   PubMed=10633045; DOI=10.1021/jm990401t;
RA   Shewchuk L., Hassell A., Wisely B., Rocque W., Holmes W., Veal J.,
RA   Kuyper L.F.;
RT   "Binding mode of the 4-anilinoquinazoline class of protein kinase
RT   inhibitor: X-ray crystallographic studies of 4-anilinoquinazolines
RT   bound to cyclin-dependent kinase 2 and p38 kinase.";
RL   J. Med. Chem. 43:133-138(2000).
RN   [68]
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), AND ACTIVITY REGULATION.
RX   PubMed=11896401; DOI=10.1038/nsb770;
RA   Pargellis C., Tong L., Churchill L., Cirillo P.F., Gilmore T.,
RA   Graham A.G., Grob P.M., Hickey E.R., Moss N., Pav S., Regan J.;
RT   "Inhibition of p38 MAP kinase by utilizing a novel allosteric binding
RT   site.";
RL   Nat. Struct. Biol. 9:268-272(2002).
RN   [69]
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS), AND ACTIVITY REGULATION.
RX   PubMed=12482439; DOI=10.1016/S0960-894X(02)00752-7;
RA   Stelmach J.E., Liu L., Patel S.B., Pivnichny J.V., Scapin G.,
RA   Singh S., Hop C.E., Wang Z., Strauss J.R., Cameron P.M., Nichols E.A.,
RA   O'Keefe S.J., O'Neill E.A., Schmatz D.M., Schwartz C.D.,
RA   Thompson C.M., Zaller D.M., Doherty J.B.;
RT   "Design and synthesis of potent, orally bioavailable
RT   dihydroquinazolinone inhibitors of p38 MAP kinase.";
RL   Bioorg. Med. Chem. Lett. 13:277-280(2003).
RN   [70]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), AND ACTIVITY REGULATION.
RX   PubMed=14561090; DOI=10.1021/jm0301787;
RA   Trejo A., Arzeno H., Browner M., Chanda S., Cheng S., Comer D.D.,
RA   Dalrymple S.A., Dunten P., Lafargue J., Lovejoy B., Freire-Moar J.,
RA   Lim J., Mcintosh J., Miller J., Papp E., Reuter D., Roberts R.,
RA   Sanpablo F., Saunders J., Song K., Villasenor A., Warren S.D.,
RA   Welch M., Weller P., Whiteley P.E., Zeng L., Goldstein D.M.;
RT   "Design and synthesis of 4-azaindoles as inhibitors of p38 MAP
RT   kinase.";
RL   J. Med. Chem. 46:4702-4713(2003).
RN   [71]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
RX   PubMed=12897767; DOI=10.1038/nsb949;
RA   Fitzgerald C.E., Patel S.B., Becker J.W., Cameron P.M., Zaller D.,
RA   Pikounis V.B., O'Keefe S.J., Scapin G.;
RT   "Structural basis for p38alpha MAP kinase quinazolinone and pyridol-
RT   pyrimidine inhibitor specificity.";
RL   Nat. Struct. Biol. 10:764-769(2003).
RN   [72]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), AND ACTIVITY REGULATION.
RX   PubMed=14726206;
RA   Patel S.B., Cameron P.M., Frantz-Wattley B., O'Neill E., Becker J.W.,
RA   Scapin G.;
RT   "Lattice stabilization and enhanced diffraction in human p38 alpha
RT   crystals by protein engineering.";
RL   Biochim. Biophys. Acta 1696:67-73(2004).
RN   [73]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-359 IN COMPLEX WITH
RP   INHIBITOR.
RX   PubMed=16342939; DOI=10.1021/bi051714v;
RA   Sullivan J.E., Holdgate G.A., Campbell D., Timms D., Gerhardt S.,
RA   Breed J., Breeze A.L., Bermingham A., Pauptit R.A., Norman R.A.,
RA   Embrey K.J., Read J., VanScyoc W.S., Ward W.H.;
RT   "Prevention of MKK6-dependent activation by binding to p38alpha MAP
RT   kinase.";
RL   Biochemistry 44:16475-16490(2005).
RN   [74]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-359, AND ACTIVITY
RP   REGULATION.
RX   PubMed=15837335; DOI=10.1016/j.bmcl.2005.02.010;
RA   Tamayo N., Liao L., Goldberg M., Powers D., Tudor Y.Y., Yu V.,
RA   Wong L.M., Henkle B., Middleton S., Syed R., Harvey T., Jang G.,
RA   Hungate R., Dominguez C.;
RT   "Design and synthesis of potent pyridazine inhibitors of p38 MAP
RT   kinase.";
RL   Bioorg. Med. Chem. Lett. 15:2409-2413(2005).
RN   [75]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), AND ACTIVITY REGULATION.
RX   PubMed=16169718; DOI=10.1016/j.bmcl.2005.08.038;
RA   Michelotti E.L., Moffett K.K., Nguyen D., Kelly M.J., Shetty R.,
RA   Chai X., Northrop K., Namboodiri V., Campbell B., Flynn G.A.,
RA   Fujimoto T., Hollinger F.P., Bukhtiyarova M., Springman E.B.,
RA   Karpusas M.;
RT   "Two classes of p38alpha MAP kinase inhibitors having a common
RT   diphenylether core but exhibiting divergent binding modes.";
RL   Bioorg. Med. Chem. Lett. 15:5274-5279(2005).
RN   [76]
RP   X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 2-359 IN COMPLEX WITH
RP   INHIBITOR.
RX   PubMed=15658854; DOI=10.1021/jm0495778;
RA   Hartshorn M.J., Murray C.W., Cleasby A., Frederickson M., Tickle I.J.,
RA   Jhoti H.;
RT   "Fragment-based lead discovery using X-ray crystallography.";
RL   J. Med. Chem. 48:403-413(2005).
RN   [77]
RP   X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 2-359 IN COMPLEX WITH
RP   MAPKAPK2.
RX   PubMed=17255097; DOI=10.1074/jbc.M611165200;
RA   ter Haar E., Prabhakar P., Liu X., Lepre C.;
RT   "Crystal structure of the p38 alpha-MAPKAP kinase 2 heterodimer.";
RL   J. Biol. Chem. 282:9733-9739(2007).
RN   [78]
RP   ERRATUM.
RA   ter Haar E., Prabhakar P., Liu X., Lepre C.;
RL   J. Biol. Chem. 282:14684-14684(2007).
RN   [79]
RP   VARIANTS [LARGE SCALE ANALYSIS] VAL-51; ARG-322 AND GLY-343.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA   Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA   O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA   Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA   Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA   Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA   Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA   West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA   Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA   DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA   Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA   Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
CC   -!- FUNCTION: Serine/threonine kinase which acts as an essential
CC       component of the MAP kinase signal transduction pathway. MAPK14 is
CC       one of the four p38 MAPKs which play an important role in the
CC       cascades of cellular responses evoked by extracellular stimuli
CC       such as proinflammatory cytokines or physical stress leading to
CC       direct activation of transcription factors. Accordingly, p38 MAPKs
CC       phosphorylate a broad range of proteins and it has been estimated
CC       that they may have approximately 200 to 300 substrates each. Some
CC       of the targets are downstream kinases which are activated through
CC       phosphorylation and further phosphorylate additional targets.
CC       RPS6KA5/MSK1 and RPS6KA4/MSK2 can directly phosphorylate and
CC       activate transcription factors such as CREB1, ATF1, the NF-kappa-B
CC       isoform RELA/NFKB3, STAT1 and STAT3, but can also phosphorylate
CC       histone H3 and the nucleosomal protein HMGN1. RPS6KA5/MSK1 and
CC       RPS6KA4/MSK2 play important roles in the rapid induction of
CC       immediate-early genes in response to stress or mitogenic stimuli,
CC       either by inducing chromatin remodeling or by recruiting the
CC       transcription machinery. On the other hand, two other kinase
CC       targets, MAPKAPK2/MK2 and MAPKAPK3/MK3, participate in the control
CC       of gene expression mostly at the post-transcriptional level, by
CC       phosphorylating ZFP36 (tristetraprolin) and ELAVL1, and by
CC       regulating EEF2K, which is important for the elongation of mRNA
CC       during translation. MKNK1/MNK1 and MKNK2/MNK2, two other kinases
CC       activated by p38 MAPKs, regulate protein synthesis by
CC       phosphorylating the initiation factor EIF4E2. MAPK14 interacts
CC       also with casein kinase II, leading to its activation through
CC       autophosphorylation and further phosphorylation of TP53/p53. In
CC       the cytoplasm, the p38 MAPK pathway is an important regulator of
CC       protein turnover. For example, CFLAR is an inhibitor of TNF-
CC       induced apoptosis whose proteasome-mediated degradation is
CC       regulated by p38 MAPK phosphorylation. In a similar way, MAPK14
CC       phosphorylates the ubiquitin ligase SIAH2, regulating its activity
CC       towards EGLN3. MAPK14 may also inhibit the lysosomal degradation
CC       pathway of autophagy by interfering with the intracellular
CC       trafficking of the transmembrane protein ATG9. Another function of
CC       MAPK14 is to regulate the endocytosis of membrane receptors by
CC       different mechanisms that impinge on the small GTPase RAB5A. In
CC       addition, clathrin-mediated EGFR internalization induced by
CC       inflammatory cytokines and UV irradiation depends on MAPK14-
CC       mediated phosphorylation of EGFR itself as well as of RAB5A
CC       effectors. Ectodomain shedding of transmembrane proteins is
CC       regulated by p38 MAPKs as well. In response to inflammatory
CC       stimuli, p38 MAPKs phosphorylate the membrane-associated
CC       metalloprotease ADAM17. Such phosphorylation is required for
CC       ADAM17-mediated ectodomain shedding of TGF-alpha family ligands,
CC       which results in the activation of EGFR signaling and cell
CC       proliferation. Another p38 MAPK substrate is FGFR1. FGFR1 can be
CC       translocated from the extracellular space into the cytosol and
CC       nucleus of target cells, and regulates processes such as rRNA
CC       synthesis and cell growth. FGFR1 translocation requires p38 MAPK
CC       activation. In the nucleus, many transcription factors are
CC       phosphorylated and activated by p38 MAPKs in response to different
CC       stimuli. Classical examples include ATF1, ATF2, ATF6, ELK1, PTPRH,
CC       DDIT3, TP53/p53 and MEF2C and MEF2A. The p38 MAPKs are emerging as
CC       important modulators of gene expression by regulating chromatin
CC       modifiers and remodelers. The promoters of several genes involved
CC       in the inflammatory response, such as IL6, IL8 and IL12B, display
CC       a p38 MAPK-dependent enrichment of histone H3 phosphorylation on
CC       'Ser-10' (H3S10ph) in LPS-stimulated myeloid cells. This
CC       phosphorylation enhances the accessibility of the cryptic NF-
CC       kappa-B-binding sites marking promoters for increased NF-kappa-B
CC       recruitment. Phosphorylates CDC25B and CDC25C which is required
CC       for binding to 14-3-3 proteins and leads to initiation of a G2
CC       delay after ultraviolet radiation. Phosphorylates TIAR following
CC       DNA damage, releasing TIAR from GADD45A mRNA and preventing mRNA
CC       degradation. The p38 MAPKs may also have kinase-independent roles,
CC       which are thought to be due to the binding to targets in the
CC       absence of phosphorylation. Protein O-Glc-N-acylation catalyzed by
CC       the OGT is regulated by MAPK14, and, although OGT does not seem to
CC       be phosphorylated by MAPK14, their interaction increases upon
CC       MAPK14 activation induced by glucose deprivation. This interaction
CC       may regulate OGT activity by recruiting it to specific targets
CC       such as neurofilament H, stimulating its O-Glc-N-acylation.
CC       Required in mid-fetal development for the growth of embryo-derived
CC       blood vessels in the labyrinth layer of the placenta. Also plays
CC       an essential role in developmental and stress-induced
CC       erythropoiesis, through regulation of EPO gene expression. Isoform
CC       MXI2 activation is stimulated by mitogens and oxidative stress and
CC       only poorly phosphorylates ELK1 and ATF2. Isoform EXIP may play a
CC       role in the early onset of apoptosis. Phosphorylates S100A9 at
CC       'Thr-113'. {ECO:0000269|PubMed:10330143,
CC       ECO:0000269|PubMed:10747897, ECO:0000269|PubMed:10943842,
CC       ECO:0000269|PubMed:11154262, ECO:0000269|PubMed:11333986,
CC       ECO:0000269|PubMed:15905572, ECO:0000269|PubMed:16932740,
CC       ECO:0000269|PubMed:17003045, ECO:0000269|PubMed:17724032,
CC       ECO:0000269|PubMed:19893488, ECO:0000269|PubMed:20188673,
CC       ECO:0000269|PubMed:20932473, ECO:0000269|PubMed:9430721,
CC       ECO:0000269|PubMed:9687510, ECO:0000269|PubMed:9792677,
CC       ECO:0000269|PubMed:9858528}.
CC   -!- FUNCTION: (Microbial infection) Activated by phosphorylation by
CC       M.tuberculosis EsxA in T-cells leading to inhibition of IFN-gamma
CC       production; phosphorylation is apparent within 15 minute and is
CC       inhibited by kinase-specific inhibitors SB203580 and siRNA
CC       (PubMed:21586573). {ECO:0000269|PubMed:21586573}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC         EC=2.7.11.24; Evidence={ECO:0000269|PubMed:11010976};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.24; Evidence={ECO:0000269|PubMed:11010976};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:10838079};
CC   -!- ACTIVITY REGULATION: Activated by cell stresses such as DNA
CC       damage, heat shock, osmotic shock, anisomycin and sodium arsenite,
CC       as well as pro-inflammatory stimuli such as bacterial
CC       lipopolysaccharide (LPS) and interleukin-1. Activation occurs
CC       through dual phosphorylation of Thr-180 and Tyr-182 by either of
CC       two dual specificity kinases, MAP2K3/MKK3 or MAP2K6/MKK6, and
CC       potentially also MAP2K4/MKK4, as well as by TAB1-mediated
CC       autophosphorylation. MAPK14 phosphorylated on both Thr-180 and
CC       Tyr-182 is 10-20-fold more active than MAPK14 phosphorylated only
CC       on Thr-180, whereas MAPK14 phosphorylated on Tyr-182 alone is
CC       inactive. whereas Thr-180 is necessary for catalysis, Tyr-182 may
CC       be required for auto-activation and substrate recognition.
CC       Phosphorylated at Tyr-323 by ZAP70 in an alternative activation
CC       pathway in response to TCR signaling in T-cells. This alternative
CC       pathway is inhibited by GADD45A. Inhibited by dual specificity
CC       phosphatases, such as DUSP1, DUSP10, and DUSP16. Specifically
CC       inhibited by the binding of pyridinyl-imidazole compounds, which
CC       are cytokine-suppressive anti-inflammatory drugs (CSAID). Isoform
CC       Mxi2 is 100-fold less sensitive to these agents than the other
CC       isoforms and is not inhibited by DUSP1. Isoform Exip is not
CC       activated by MAP2K6. SB203580 is an inhibitor of MAPK14.
CC       {ECO:0000269|PubMed:10391943, ECO:0000269|PubMed:10838079,
CC       ECO:0000269|PubMed:11278799, ECO:0000269|PubMed:11359773,
CC       ECO:0000269|PubMed:11847341, ECO:0000269|PubMed:11866441,
CC       ECO:0000269|PubMed:11896401, ECO:0000269|PubMed:12482439,
CC       ECO:0000269|PubMed:14561090, ECO:0000269|PubMed:14726206,
CC       ECO:0000269|PubMed:15735648, ECO:0000269|PubMed:15735649,
CC       ECO:0000269|PubMed:15837335, ECO:0000269|PubMed:16169718,
CC       ECO:0000269|PubMed:17003045, ECO:0000269|PubMed:7535770,
CC       ECO:0000269|PubMed:8622669, ECO:0000269|PubMed:9430721}.
CC   -!- SUBUNIT: Component of a signaling complex containing at least
CC       AKAP13, PKN1, MAPK14, ZAK and MAP2K3. Within this complex, AKAP13
CC       interacts directly with PKN1, which in turn recruits MAPK14,
CC       MAP2K3 and ZAK (PubMed:21224381). Binds to a kinase interaction
CC       motif within the protein tyrosine phosphatase, PTPRR (By
CC       similarity). This interaction retains MAPK14 in the cytoplasm and
CC       prevents nuclear accumulation (By similarity). Interacts with
CC       SPAG9 and GADD45A (By similarity). Interacts with CDC25B, CDC25C,
CC       DUSP1, DUSP10, DUSP16, NP60, SUPT20H and TAB1. Interacts with
CC       casein kinase II subunits CSNK2A1 and CSNK2B. Interacts with
CC       PPM1D. Interacts with CDK5RAP3; recruits PPM1D to MAPK14 and may
CC       regulate its dephosphorylation (PubMed:21283629).
CC       {ECO:0000250|UniProtKB:P47811, ECO:0000269|PubMed:10391943,
CC       ECO:0000269|PubMed:10747897, ECO:0000269|PubMed:11010976,
CC       ECO:0000269|PubMed:11278799, ECO:0000269|PubMed:11333986,
CC       ECO:0000269|PubMed:11359773, ECO:0000269|PubMed:11847341,
CC       ECO:0000269|PubMed:12897767, ECO:0000269|PubMed:15658854,
CC       ECO:0000269|PubMed:15735649, ECO:0000269|PubMed:16342939,
CC       ECO:0000269|PubMed:16352664, ECO:0000269|PubMed:16751104,
CC       ECO:0000269|PubMed:17255097, ECO:0000269|PubMed:20188673,
CC       ECO:0000269|PubMed:21224381, ECO:0000269|PubMed:21283629,
CC       ECO:0000269|PubMed:9792677}.
CC   -!- INTERACTION:
CC       P31749:AKT1; NbExp=2; IntAct=EBI-73946, EBI-296087;
CC       P28562:DUSP1; NbExp=3; IntAct=EBI-73946, EBI-975493;
CC       Q99956:DUSP9; NbExp=2; IntAct=EBI-73946, EBI-3906678;
CC       P46734:MAP2K3; NbExp=2; IntAct=EBI-73946, EBI-602462;
CC       P28482:MAPK1; NbExp=5; IntAct=EBI-6932370, EBI-959949;
CC       P27361:MAPK3; NbExp=5; IntAct=EBI-73946, EBI-73995;
CC       P49137:MAPKAPK2; NbExp=7; IntAct=EBI-73946, EBI-993299;
CC       Q16644:MAPKAPK3; NbExp=5; IntAct=EBI-73946, EBI-1384657;
CC       Q9BUB5:MKNK1; NbExp=3; IntAct=EBI-73946, EBI-73837;
CC       Q9HBH9:MKNK2; NbExp=3; IntAct=EBI-73946, EBI-2864341;
CC       P22736-1:NR4A1; NbExp=5; IntAct=EBI-15834191, EBI-16085263;
CC       P49790:NUP153; NbExp=2; IntAct=EBI-6932370, EBI-286779;
CC       P35813:PPM1A; NbExp=2; IntAct=EBI-73946, EBI-989143;
CC       P54830-1:Ptpn5 (xeno); NbExp=6; IntAct=EBI-15834191, EBI-16067443;
CC       Q15256:PTPRR; NbExp=3; IntAct=EBI-73946, EBI-2265659;
CC       Q15256-1:PTPRR; NbExp=6; IntAct=EBI-15834191, EBI-16067395;
CC       P06400:RB1; NbExp=4; IntAct=EBI-73946, EBI-491274;
CC       O75676:RPS6KA4; NbExp=4; IntAct=EBI-73946, EBI-73933;
CC       Q8NEM7:SUPT20H; NbExp=5; IntAct=EBI-73946, EBI-946984;
CC       Q15750:TAB1; NbExp=2; IntAct=EBI-73946, EBI-358643;
CC       Q92574:TSC1; NbExp=2; IntAct=EBI-73946, EBI-1047085;
CC       Q07352:ZFP36L1; NbExp=2; IntAct=EBI-73946, EBI-721823;
CC       O43257:ZNHIT1; NbExp=7; IntAct=EBI-73946, EBI-347522;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7535770}.
CC       Nucleus {ECO:0000269|PubMed:7535770}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=CSBP2;
CC         IsoId=Q16539-1; Sequence=Displayed;
CC       Name=CSBP1;
CC         IsoId=Q16539-2; Sequence=VSP_004842;
CC       Name=Mxi2;
CC         IsoId=Q16539-3; Sequence=VSP_004844;
CC       Name=Exip; Synonyms=Exon skip;
CC         IsoId=Q16539-4; Sequence=VSP_004843, VSP_004845;
CC       Name=5;
CC         IsoId=Q16539-5; Sequence=VSP_057194;
CC   -!- TISSUE SPECIFICITY: Brain, heart, placenta, pancreas and skeletal
CC       muscle. Expressed to a lesser extent in lung, liver and kidney.
CC   -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC       whose phosphorylation activates the MAP kinases.
CC   -!- PTM: Dually phosphorylated on Thr-180 and Tyr-182 by the MAP2Ks
CC       MAP2K3/MKK3, MAP2K4/MKK4 and MAP2K6/MKK6 in response to
CC       inflammatory citokines, environmental stress or growth factors,
CC       which activates the enzyme. Dual phosphorylation can also be
CC       mediated by TAB1-mediated autophosphorylation. TCR engagement in
CC       T-cells also leads to Tyr-323 phosphorylation by ZAP70.
CC       Dephosphorylated and inactivated by DUPS1, DUSP10 and DUSP16.
CC       PPM1D also mediates dephosphorylation and inactivation of MAPK14
CC       (PubMed:21283629). {ECO:0000269|PubMed:11010976,
CC       ECO:0000269|PubMed:15735648, ECO:0000269|PubMed:17724032,
CC       ECO:0000269|PubMed:21283629, ECO:0000269|PubMed:7535770,
CC       ECO:0000269|PubMed:8622669}.
CC   -!- PTM: Acetylated at Lys-53 and Lys-152 by KAT2B and EP300.
CC       Acetylation at Lys-53 increases the affinity for ATP and enhances
CC       kinase activity. Lys-53 and Lys-152 are deacetylated by HDAC3.
CC       {ECO:0000269|PubMed:21444723}.
CC   -!- PTM: Ubiquitinated. Ubiquitination leads to degradation by the
CC       proteasome pathway. {ECO:0000269|PubMed:17724032}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. MAP kinase subfamily.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=P38 mitogen-activated protein
CC       kinases entry;
CC       URL="https://en.wikipedia.org/wiki/P38_mitogen-activated_protein_kinases";
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/MAPK14ID41292ch6p21.html";
DR   EMBL; L35263; AAA57455.1; -; mRNA.
DR   EMBL; L35264; AAA57456.1; -; mRNA.
DR   EMBL; L35253; AAA74301.1; -; mRNA.
DR   EMBL; U19775; AAC50329.1; -; mRNA.
DR   EMBL; AF100544; AAF36770.1; -; mRNA.
DR   EMBL; AB074150; BAB85654.1; -; mRNA.
DR   EMBL; FJ032367; ACI00233.1; -; mRNA.
DR   EMBL; AK291709; BAF84398.1; -; mRNA.
DR   EMBL; BT006933; AAP35579.1; -; mRNA.
DR   EMBL; CR536505; CAG38743.1; -; mRNA.
DR   EMBL; EU332860; ABY87549.1; -; Genomic_DNA.
DR   EMBL; Z95152; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471081; EAX03869.1; -; Genomic_DNA.
DR   EMBL; BC000092; AAH00092.1; -; mRNA.
DR   EMBL; BC031574; AAH31574.1; -; mRNA.
DR   CCDS; CCDS4815.1; -. [Q16539-2]
DR   CCDS; CCDS4816.1; -. [Q16539-1]
DR   CCDS; CCDS4817.1; -. [Q16539-4]
DR   PIR; S53536; S53536.
DR   RefSeq; NP_001306.1; NM_001315.2. [Q16539-2]
DR   RefSeq; NP_620581.1; NM_139012.2. [Q16539-1]
DR   RefSeq; NP_620582.1; NM_139013.2. [Q16539-3]
DR   RefSeq; NP_620583.1; NM_139014.2. [Q16539-4]
DR   PDB; 1A9U; X-ray; 2.50 A; A=1-360.
DR   PDB; 1BL6; X-ray; 2.50 A; A=1-360.
DR   PDB; 1BL7; X-ray; 2.50 A; A=1-360.
DR   PDB; 1BMK; X-ray; 2.40 A; A=1-360.
DR   PDB; 1DI9; X-ray; 2.60 A; A=1-360.
DR   PDB; 1IAN; X-ray; 2.00 A; A=2-360.
DR   PDB; 1KV1; X-ray; 2.50 A; A=1-360.
DR   PDB; 1KV2; X-ray; 2.80 A; A=1-360.
DR   PDB; 1M7Q; X-ray; 2.40 A; A=1-360.
DR   PDB; 1OUK; X-ray; 2.50 A; A=1-360.
DR   PDB; 1OUY; X-ray; 2.50 A; A=1-360.
DR   PDB; 1OVE; X-ray; 2.10 A; A=1-360.
DR   PDB; 1OZ1; X-ray; 2.10 A; A=1-360.
DR   PDB; 1R39; X-ray; 2.30 A; A=1-360.
DR   PDB; 1R3C; X-ray; 2.00 A; A=1-360.
DR   PDB; 1W7H; X-ray; 2.21 A; A=2-360.
DR   PDB; 1W82; X-ray; 2.20 A; A=2-360.
DR   PDB; 1W83; X-ray; 2.50 A; A=2-360.
DR   PDB; 1W84; X-ray; 2.20 A; A=2-360.
DR   PDB; 1WBN; X-ray; 2.40 A; A=2-360.
DR   PDB; 1WBO; X-ray; 2.16 A; A=2-360.
DR   PDB; 1WBS; X-ray; 1.80 A; A=2-360.
DR   PDB; 1WBT; X-ray; 2.00 A; A=2-360.
DR   PDB; 1WBV; X-ray; 2.00 A; A=2-360.
DR   PDB; 1WBW; X-ray; 2.41 A; A=2-360.
DR   PDB; 1WFC; X-ray; 2.30 A; A=1-360.
DR   PDB; 1YQJ; X-ray; 2.00 A; A=2-360.
DR   PDB; 1ZYJ; X-ray; 2.00 A; A=1-360.
DR   PDB; 1ZZ2; X-ray; 2.00 A; A=1-360.
DR   PDB; 1ZZL; X-ray; 2.00 A; A=4-354.
DR   PDB; 2BAJ; X-ray; 2.25 A; A=2-360.
DR   PDB; 2BAK; X-ray; 2.20 A; A=2-360.
DR   PDB; 2BAL; X-ray; 2.10 A; A=2-360.
DR   PDB; 2BAQ; X-ray; 2.80 A; A=2-360.
DR   PDB; 2FSL; X-ray; 1.70 A; X=2-360.
DR   PDB; 2FSM; X-ray; 1.86 A; X=2-360.
DR   PDB; 2FSO; X-ray; 1.83 A; X=2-360.
DR   PDB; 2FST; X-ray; 1.45 A; X=2-360.
DR   PDB; 2GFS; X-ray; 1.75 A; A=2-360.
DR   PDB; 2I0H; X-ray; 2.00 A; A=1-360.
DR   PDB; 2LGC; NMR; -; A=2-354.
DR   PDB; 2NPQ; X-ray; 1.80 A; A=2-360.
DR   PDB; 2OKR; X-ray; 2.00 A; A/D=2-360.
DR   PDB; 2ONL; X-ray; 4.00 A; A/B=2-360.
DR   PDB; 2QD9; X-ray; 1.70 A; A=2-360.
DR   PDB; 2RG5; X-ray; 2.40 A; A=2-360.
DR   PDB; 2RG6; X-ray; 1.72 A; A=2-360.
DR   PDB; 2Y8O; X-ray; 1.95 A; A=1-360.
DR   PDB; 2YIS; X-ray; 2.00 A; A=2-360.
DR   PDB; 2YIW; X-ray; 2.00 A; A=2-360.
DR   PDB; 2YIX; X-ray; 2.30 A; A=4-354.
DR   PDB; 2ZAZ; X-ray; 1.80 A; A=1-360.
DR   PDB; 2ZB0; X-ray; 2.10 A; A=1-360.
DR   PDB; 2ZB1; X-ray; 2.50 A; A=1-360.
DR   PDB; 3BV2; X-ray; 2.40 A; A=2-360.
DR   PDB; 3BV3; X-ray; 2.59 A; A=2-360.
DR   PDB; 3BX5; X-ray; 2.40 A; A=2-360.
DR   PDB; 3C5U; X-ray; 2.80 A; A=2-360.
DR   PDB; 3CTQ; X-ray; 1.95 A; A=5-352.
DR   PDB; 3D7Z; X-ray; 2.10 A; A=1-360.
DR   PDB; 3D83; X-ray; 1.90 A; A=1-360.
DR   PDB; 3DS6; X-ray; 2.90 A; A/B/C/D=1-360.
DR   PDB; 3DT1; X-ray; 2.80 A; A=1-360.
DR   PDB; 3E92; X-ray; 2.00 A; A=1-360.
DR   PDB; 3E93; X-ray; 2.00 A; A=1-360.
DR   PDB; 3FC1; X-ray; 2.40 A; X=1-360.
DR   PDB; 3FI4; X-ray; 2.20 A; A=1-360.
DR   PDB; 3FKL; X-ray; 2.00 A; A=1-360.
DR   PDB; 3FKN; X-ray; 2.00 A; A=1-360.
DR   PDB; 3FKO; X-ray; 2.00 A; A=1-360.
DR   PDB; 3FL4; X-ray; 1.80 A; A=1-360.
DR   PDB; 3FLN; X-ray; 1.90 A; C=1-360.
DR   PDB; 3FLQ; X-ray; 1.90 A; A=1-360.
DR   PDB; 3FLS; X-ray; 2.30 A; A=1-360.
DR   PDB; 3FLW; X-ray; 2.10 A; A=1-360.
DR   PDB; 3FLY; X-ray; 1.80 A; A=1-360.
DR   PDB; 3FLZ; X-ray; 2.23 A; A=1-360.
DR   PDB; 3FMH; X-ray; 1.90 A; A=1-360.
DR   PDB; 3FMJ; X-ray; 2.00 A; A=1-360.
DR   PDB; 3FMK; X-ray; 1.70 A; A=1-360.
DR   PDB; 3FML; X-ray; 2.10 A; A=1-360.
DR   PDB; 3FMM; X-ray; 2.00 A; A=1-360.
DR   PDB; 3FMN; X-ray; 1.90 A; A=1-360.
DR   PDB; 3FSF; X-ray; 2.10 A; A=1-360.
DR   PDB; 3FSK; X-ray; 2.00 A; A=1-360.
DR   PDB; 3GC7; X-ray; 1.80 A; A=1-360.
DR   PDB; 3GCP; X-ray; 2.25 A; A=2-360.
DR   PDB; 3GCQ; X-ray; 2.00 A; A=2-360.
DR   PDB; 3GCS; X-ray; 2.10 A; A=2-360.
DR   PDB; 3GCU; X-ray; 2.10 A; A/B=2-360.
DR   PDB; 3GCV; X-ray; 2.30 A; A=2-360.
DR   PDB; 3GFE; X-ray; 2.10 A; A=1-360.
DR   PDB; 3GI3; X-ray; 2.40 A; A=1-360.
DR   PDB; 3HA8; X-ray; 2.48 A; A=1-360.
DR   PDB; 3HEC; X-ray; 2.50 A; A=5-352.
DR   PDB; 3HEG; X-ray; 2.20 A; A=5-352.
DR   PDB; 3HL7; X-ray; 1.88 A; A=1-360.
DR   PDB; 3HLL; X-ray; 1.95 A; A=1-360.
DR   PDB; 3HP2; X-ray; 2.15 A; A=1-360.
DR   PDB; 3HP5; X-ray; 2.30 A; A=1-360.
DR   PDB; 3HRB; X-ray; 2.20 A; A=2-360.
DR   PDB; 3HUB; X-ray; 2.25 A; A=2-360.
DR   PDB; 3HUC; X-ray; 1.80 A; A=2-360.
DR   PDB; 3HV3; X-ray; 2.00 A; A=2-360.
DR   PDB; 3HV4; X-ray; 2.60 A; A/B=2-360.
DR   PDB; 3HV5; X-ray; 2.25 A; A/B=2-360.
DR   PDB; 3HV6; X-ray; 1.95 A; A=2-360.
DR   PDB; 3HV7; X-ray; 2.40 A; A=2-360.
DR   PDB; 3HVC; X-ray; 2.10 A; A=1-360.
DR   PDB; 3IPH; X-ray; 2.10 A; A=1-360.
DR   PDB; 3ITZ; X-ray; 2.25 A; A=1-360.
DR   PDB; 3IW5; X-ray; 2.50 A; A=2-360.
DR   PDB; 3IW6; X-ray; 2.10 A; A=2-360.
DR   PDB; 3IW7; X-ray; 2.40 A; A=2-360.
DR   PDB; 3IW8; X-ray; 2.00 A; A=2-360.
DR   PDB; 3K3I; X-ray; 1.70 A; A=5-352.
DR   PDB; 3K3J; X-ray; 2.00 A; A=1-360.
DR   PDB; 3KF7; X-ray; 2.00 A; A=1-360.
DR   PDB; 3KQ7; X-ray; 1.80 A; A=1-360.
DR   PDB; 3L8S; X-ray; 2.35 A; A=2-360.
DR   PDB; 3L8X; X-ray; 2.15 A; A=2-360.
DR   PDB; 3LFA; X-ray; 2.10 A; A=2-360.
DR   PDB; 3LFB; X-ray; 2.60 A; A=2-360.
DR   PDB; 3LFC; X-ray; 2.80 A; A=2-360.
DR   PDB; 3LFD; X-ray; 3.40 A; A=2-360.
DR   PDB; 3LFE; X-ray; 2.30 A; A=2-360.
DR   PDB; 3LFF; X-ray; 1.50 A; A=2-360.
DR   PDB; 3LHJ; X-ray; 3.31 A; A=1-360.
DR   PDB; 3MGY; X-ray; 2.10 A; A=1-360.
DR   PDB; 3MH0; X-ray; 2.00 A; A=1-360.
DR   PDB; 3MH1; X-ray; 2.20 A; A=1-360.
DR   PDB; 3MH2; X-ray; 2.30 A; A=1-360.
DR   PDB; 3MH3; X-ray; 2.20 A; A=1-360.
DR   PDB; 3MPA; X-ray; 2.10 A; A=1-360.
DR   PDB; 3MPT; X-ray; 1.89 A; A=1-360.
DR   PDB; 3MVL; X-ray; 2.80 A; A/B=2-360.
DR   PDB; 3MVM; X-ray; 2.00 A; A/B=2-360.
DR   PDB; 3MW1; X-ray; 2.80 A; A=2-360.
DR   PDB; 3NEW; X-ray; 2.51 A; A=1-360.
DR   PDB; 3NNU; X-ray; 2.40 A; A=1-354.
DR   PDB; 3NNV; X-ray; 2.10 A; A=1-354.
DR   PDB; 3NNW; X-ray; 1.89 A; A=1-354.
DR   PDB; 3NNX; X-ray; 2.28 A; A=1-354.
DR   PDB; 3NWW; X-ray; 2.09 A; A=2-360.
DR   PDB; 3O8P; X-ray; 2.10 A; A=1-360.
DR   PDB; 3O8T; X-ray; 2.00 A; A=1-360.
DR   PDB; 3O8U; X-ray; 2.10 A; A=1-360.
DR   PDB; 3OBG; X-ray; 2.80 A; A=1-360.
DR   PDB; 3OBJ; X-ray; 2.40 A; A=1-360.
DR   PDB; 3OC1; X-ray; 2.59 A; A=1-360.
DR   PDB; 3OCG; X-ray; 2.21 A; A=2-360.
DR   PDB; 3OD6; X-ray; 2.68 A; X=1-360.
DR   PDB; 3ODY; X-ray; 2.20 A; X=1-360.
DR   PDB; 3ODZ; X-ray; 2.30 A; X=1-360.
DR   PDB; 3OEF; X-ray; 1.60 A; X=1-360.
DR   PDB; 3PG3; X-ray; 2.00 A; A=2-360.
DR   PDB; 3QUD; X-ray; 2.00 A; A=2-360.
DR   PDB; 3QUE; X-ray; 2.70 A; A=2-360.
DR   PDB; 3RIN; X-ray; 2.20 A; A=1-360.
DR   PDB; 3ROC; X-ray; 1.70 A; A=1-360.
DR   PDB; 3S3I; X-ray; 1.80 A; A=4-352.
DR   PDB; 3S4Q; X-ray; 2.27 A; A=2-360.
DR   PDB; 3U8W; X-ray; 2.15 A; A=1-360.
DR   PDB; 3UVP; X-ray; 2.40 A; A=2-360.
DR   PDB; 3UVQ; X-ray; 2.20 A; A=2-360.
DR   PDB; 3UVR; X-ray; 2.10 A; A=2-360.
DR   PDB; 3ZS5; X-ray; 1.60 A; A=2-360.
DR   PDB; 3ZSG; X-ray; 1.89 A; A=2-360.
DR   PDB; 3ZSH; X-ray; 2.05 A; A=2-360.
DR   PDB; 3ZSI; X-ray; 2.40 A; A=2-360.
DR   PDB; 3ZYA; X-ray; 1.90 A; A=1-360.
DR   PDB; 4A9Y; X-ray; 2.20 A; A=2-360.
DR   PDB; 4AA0; X-ray; 1.80 A; A=2-360.
DR   PDB; 4AA4; X-ray; 2.30 A; A=2-360.
DR   PDB; 4AA5; X-ray; 2.38 A; A=2-360.
DR   PDB; 4AAC; X-ray; 2.50 A; A=2-360.
DR   PDB; 4DLI; X-ray; 1.91 A; A=2-360.
DR   PDB; 4DLJ; X-ray; 2.60 A; A=2-360.
DR   PDB; 4E5A; X-ray; 1.87 A; X=1-360.
DR   PDB; 4E5B; X-ray; 2.00 A; A=1-360.
DR   PDB; 4E6A; X-ray; 2.09 A; A=1-360.
DR   PDB; 4E6C; X-ray; 2.39 A; A=1-360.
DR   PDB; 4E8A; X-ray; 2.70 A; A=1-360.
DR   PDB; 4EH2; X-ray; 2.00 A; A=2-360.
DR   PDB; 4EH3; X-ray; 2.40 A; A=2-360.
DR   PDB; 4EH4; X-ray; 2.50 A; A=2-360.
DR   PDB; 4EH5; X-ray; 2.00 A; A=2-360.
DR   PDB; 4EH6; X-ray; 2.10 A; A=2-360.
DR   PDB; 4EH7; X-ray; 2.10 A; A=2-360.
DR   PDB; 4EH8; X-ray; 2.20 A; A=2-360.
DR   PDB; 4EH9; X-ray; 2.10 A; A=2-360.
DR   PDB; 4EHV; X-ray; 1.60 A; A=2-360.
DR   PDB; 4EWQ; X-ray; 2.10 A; A=2-360.
DR   PDB; 4F9W; X-ray; 2.00 A; A=2-360.
DR   PDB; 4F9Y; X-ray; 1.85 A; A=2-360.
DR   PDB; 4FA2; X-ray; 2.00 A; A=2-360.
DR   PDB; 4GEO; X-ray; 1.66 A; A=2-360.
DR   PDB; 4KIN; X-ray; 1.97 A; A/B/C/D=2-360.
DR   PDB; 4KIP; X-ray; 2.27 A; A/B=2-360.
DR   PDB; 4KIQ; X-ray; 2.50 A; A/B/C/D=2-360.
DR   PDB; 4L8M; X-ray; 2.10 A; A=2-360.
DR   PDB; 4R3C; X-ray; 2.06 A; A=2-360.
DR   PDB; 4ZTH; X-ray; 2.15 A; A=2-360.
DR   PDB; 5ETA; X-ray; 2.80 A; A/B=1-360.
DR   PDB; 5ETC; X-ray; 2.42 A; A=1-360.
DR   PDB; 5ETF; X-ray; 2.40 A; A=1-360.
DR   PDB; 5ETI; X-ray; 2.80 A; A=1-360.
DR   PDB; 5ML5; X-ray; 1.90 A; A=1-360.
DR   PDB; 5MTX; X-ray; 1.80 A; A=1-360.
DR   PDB; 5MTY; X-ray; 2.31 A; A=1-360.
DR   PDB; 5MZ3; X-ray; 2.15 A; A=1-360.
DR   PDB; 5N63; X-ray; 2.40 A; A=1-360.
DR   PDB; 5N64; X-ray; 2.40 A; A=1-360.
DR   PDB; 5N65; X-ray; 2.00 A; A=1-360.
DR   PDB; 5N66; X-ray; 2.40 A; A=1-360.
DR   PDB; 5N67; X-ray; 1.90 A; A=1-360.
DR   PDB; 5N68; X-ray; 1.85 A; A=1-360.
DR   PDB; 5O8U; X-ray; 2.00 A; A=1-360.
DR   PDB; 5O8V; X-ray; 2.00 A; A=1-360.
DR   PDB; 5OMG; X-ray; 2.00 A; A=1-360.
DR   PDB; 5OMH; X-ray; 2.50 A; A=1-360.
DR   PDB; 5TBE; X-ray; 2.44 A; A=1-360.
DR   PDB; 5TCO; X-ray; 2.10 A; A=2-360.
DR   PDB; 5WJJ; X-ray; 1.60 A; A=1-360.
DR   PDB; 5XYX; X-ray; 2.61 A; A=1-360.
DR   PDB; 5XYY; X-ray; 1.70 A; A=1-360.
DR   PDB; 6ANL; X-ray; 2.00 A; A=1-360.
DR   PDB; 6HWT; X-ray; 1.70 A; A=2-360.
DR   PDB; 6HWU; X-ray; 2.30 A; A=2-360.
DR   PDB; 6HWV; X-ray; 1.70 A; A=2-360.
DR   PDB; 6M95; X-ray; 1.80 A; A=1-360.
DR   PDB; 6M9L; X-ray; 2.45 A; A=1-360.
DR   PDBsum; 1A9U; -.
DR   PDBsum; 1BL6; -.
DR   PDBsum; 1BL7; -.
DR   PDBsum; 1BMK; -.
DR   PDBsum; 1DI9; -.
DR   PDBsum; 1IAN; -.
DR   PDBsum; 1KV1; -.
DR   PDBsum; 1KV2; -.
DR   PDBsum; 1M7Q; -.
DR   PDBsum; 1OUK; -.
DR   PDBsum; 1OUY; -.
DR   PDBsum; 1OVE; -.
DR   PDBsum; 1OZ1; -.
DR   PDBsum; 1R39; -.
DR   PDBsum; 1R3C; -.
DR   PDBsum; 1W7H; -.
DR   PDBsum; 1W82; -.
DR   PDBsum; 1W83; -.
DR   PDBsum; 1W84; -.
DR   PDBsum; 1WBN; -.
DR   PDBsum; 1WBO; -.
DR   PDBsum; 1WBS; -.
DR   PDBsum; 1WBT; -.
DR   PDBsum; 1WBV; -.
DR   PDBsum; 1WBW; -.
DR   PDBsum; 1WFC; -.
DR   PDBsum; 1YQJ; -.
DR   PDBsum; 1ZYJ; -.
DR   PDBsum; 1ZZ2; -.
DR   PDBsum; 1ZZL; -.
DR   PDBsum; 2BAJ; -.
DR   PDBsum; 2BAK; -.
DR   PDBsum; 2BAL; -.
DR   PDBsum; 2BAQ; -.
DR   PDBsum; 2FSL; -.
DR   PDBsum; 2FSM; -.
DR   PDBsum; 2FSO; -.
DR   PDBsum; 2FST; -.
DR   PDBsum; 2GFS; -.
DR   PDBsum; 2I0H; -.
DR   PDBsum; 2LGC; -.
DR   PDBsum; 2NPQ; -.
DR   PDBsum; 2OKR; -.
DR   PDBsum; 2ONL; -.
DR   PDBsum; 2QD9; -.
DR   PDBsum; 2RG5; -.
DR   PDBsum; 2RG6; -.
DR   PDBsum; 2Y8O; -.
DR   PDBsum; 2YIS; -.
DR   PDBsum; 2YIW; -.
DR   PDBsum; 2YIX; -.
DR   PDBsum; 2ZAZ; -.
DR   PDBsum; 2ZB0; -.
DR   PDBsum; 2ZB1; -.
DR   PDBsum; 3BV2; -.
DR   PDBsum; 3BV3; -.
DR   PDBsum; 3BX5; -.
DR   PDBsum; 3C5U; -.
DR   PDBsum; 3CTQ; -.
DR   PDBsum; 3D7Z; -.
DR   PDBsum; 3D83; -.
DR   PDBsum; 3DS6; -.
DR   PDBsum; 3DT1; -.
DR   PDBsum; 3E92; -.
DR   PDBsum; 3E93; -.
DR   PDBsum; 3FC1; -.
DR   PDBsum; 3FI4; -.
DR   PDBsum; 3FKL; -.
DR   PDBsum; 3FKN; -.
DR   PDBsum; 3FKO; -.
DR   PDBsum; 3FL4; -.
DR   PDBsum; 3FLN; -.
DR   PDBsum; 3FLQ; -.
DR   PDBsum; 3FLS; -.
DR   PDBsum; 3FLW; -.
DR   PDBsum; 3FLY; -.
DR   PDBsum; 3FLZ; -.
DR   PDBsum; 3FMH; -.
DR   PDBsum; 3FMJ; -.
DR   PDBsum; 3FMK; -.
DR   PDBsum; 3FML; -.
DR   PDBsum; 3FMM; -.
DR   PDBsum; 3FMN; -.
DR   PDBsum; 3FSF; -.
DR   PDBsum; 3FSK; -.
DR   PDBsum; 3GC7; -.
DR   PDBsum; 3GCP; -.
DR   PDBsum; 3GCQ; -.
DR   PDBsum; 3GCS; -.
DR   PDBsum; 3GCU; -.
DR   PDBsum; 3GCV; -.
DR   PDBsum; 3GFE; -.
DR   PDBsum; 3GI3; -.
DR   PDBsum; 3HA8; -.
DR   PDBsum; 3HEC; -.
DR   PDBsum; 3HEG; -.
DR   PDBsum; 3HL7; -.
DR   PDBsum; 3HLL; -.
DR   PDBsum; 3HP2; -.
DR   PDBsum; 3HP5; -.
DR   PDBsum; 3HRB; -.
DR   PDBsum; 3HUB; -.
DR   PDBsum; 3HUC; -.
DR   PDBsum; 3HV3; -.
DR   PDBsum; 3HV4; -.
DR   PDBsum; 3HV5; -.
DR   PDBsum; 3HV6; -.
DR   PDBsum; 3HV7; -.
DR   PDBsum; 3HVC; -.
DR   PDBsum; 3IPH; -.
DR   PDBsum; 3ITZ; -.
DR   PDBsum; 3IW5; -.
DR   PDBsum; 3IW6; -.
DR   PDBsum; 3IW7; -.
DR   PDBsum; 3IW8; -.
DR   PDBsum; 3K3I; -.
DR   PDBsum; 3K3J; -.
DR   PDBsum; 3KF7; -.
DR   PDBsum; 3KQ7; -.
DR   PDBsum; 3L8S; -.
DR   PDBsum; 3L8X; -.
DR   PDBsum; 3LFA; -.
DR   PDBsum; 3LFB; -.
DR   PDBsum; 3LFC; -.
DR   PDBsum; 3LFD; -.
DR   PDBsum; 3LFE; -.
DR   PDBsum; 3LFF; -.
DR   PDBsum; 3LHJ; -.
DR   PDBsum; 3MGY; -.
DR   PDBsum; 3MH0; -.
DR   PDBsum; 3MH1; -.
DR   PDBsum; 3MH2; -.
DR   PDBsum; 3MH3; -.
DR   PDBsum; 3MPA; -.
DR   PDBsum; 3MPT; -.
DR   PDBsum; 3MVL; -.
DR   PDBsum; 3MVM; -.
DR   PDBsum; 3MW1; -.
DR   PDBsum; 3NEW; -.
DR   PDBsum; 3NNU; -.
DR   PDBsum; 3NNV; -.
DR   PDBsum; 3NNW; -.
DR   PDBsum; 3NNX; -.
DR   PDBsum; 3NWW; -.
DR   PDBsum; 3O8P; -.
DR   PDBsum; 3O8T; -.
DR   PDBsum; 3O8U; -.
DR   PDBsum; 3OBG; -.
DR   PDBsum; 3OBJ; -.
DR   PDBsum; 3OC1; -.
DR   PDBsum; 3OCG; -.
DR   PDBsum; 3OD6; -.
DR   PDBsum; 3ODY; -.
DR   PDBsum; 3ODZ; -.
DR   PDBsum; 3OEF; -.
DR   PDBsum; 3PG3; -.
DR   PDBsum; 3QUD; -.
DR   PDBsum; 3QUE; -.
DR   PDBsum; 3RIN; -.
DR   PDBsum; 3ROC; -.
DR   PDBsum; 3S3I; -.
DR   PDBsum; 3S4Q; -.
DR   PDBsum; 3U8W; -.
DR   PDBsum; 3UVP; -.
DR   PDBsum; 3UVQ; -.
DR   PDBsum; 3UVR; -.
DR   PDBsum; 3ZS5; -.
DR   PDBsum; 3ZSG; -.
DR   PDBsum; 3ZSH; -.
DR   PDBsum; 3ZSI; -.
DR   PDBsum; 3ZYA; -.
DR   PDBsum; 4A9Y; -.
DR   PDBsum; 4AA0; -.
DR   PDBsum; 4AA4; -.
DR   PDBsum; 4AA5; -.
DR   PDBsum; 4AAC; -.
DR   PDBsum; 4DLI; -.
DR   PDBsum; 4DLJ; -.
DR   PDBsum; 4E5A; -.
DR   PDBsum; 4E5B; -.
DR   PDBsum; 4E6A; -.
DR   PDBsum; 4E6C; -.
DR   PDBsum; 4E8A; -.
DR   PDBsum; 4EH2; -.
DR   PDBsum; 4EH3; -.
DR   PDBsum; 4EH4; -.
DR   PDBsum; 4EH5; -.
DR   PDBsum; 4EH6; -.
DR   PDBsum; 4EH7; -.
DR   PDBsum; 4EH8; -.
DR   PDBsum; 4EH9; -.
DR   PDBsum; 4EHV; -.
DR   PDBsum; 4EWQ; -.
DR   PDBsum; 4F9W; -.
DR   PDBsum; 4F9Y; -.
DR   PDBsum; 4FA2; -.
DR   PDBsum; 4GEO; -.
DR   PDBsum; 4KIN; -.
DR   PDBsum; 4KIP; -.
DR   PDBsum; 4KIQ; -.
DR   PDBsum; 4L8M; -.
DR   PDBsum; 4R3C; -.
DR   PDBsum; 4ZTH; -.
DR   PDBsum; 5ETA; -.
DR   PDBsum; 5ETC; -.
DR   PDBsum; 5ETF; -.
DR   PDBsum; 5ETI; -.
DR   PDBsum; 5ML5; -.
DR   PDBsum; 5MTX; -.
DR   PDBsum; 5MTY; -.
DR   PDBsum; 5MZ3; -.
DR   PDBsum; 5N63; -.
DR   PDBsum; 5N64; -.
DR   PDBsum; 5N65; -.
DR   PDBsum; 5N66; -.
DR   PDBsum; 5N67; -.
DR   PDBsum; 5N68; -.
DR   PDBsum; 5O8U; -.
DR   PDBsum; 5O8V; -.
DR   PDBsum; 5OMG; -.
DR   PDBsum; 5OMH; -.
DR   PDBsum; 5TBE; -.
DR   PDBsum; 5TCO; -.
DR   PDBsum; 5WJJ; -.
DR   PDBsum; 5XYX; -.
DR   PDBsum; 5XYY; -.
DR   PDBsum; 6ANL; -.
DR   PDBsum; 6HWT; -.
DR   PDBsum; 6HWU; -.
DR   PDBsum; 6HWV; -.
DR   PDBsum; 6M95; -.
DR   PDBsum; 6M9L; -.
DR   SMR; Q16539; -.
DR   BioGrid; 107819; 235.
DR   CORUM; Q16539; -.
DR   DIP; DIP-30987N; -.
DR   ELM; Q16539; -.
DR   IntAct; Q16539; 104.
DR   MINT; Q16539; -.
DR   STRING; 9606.ENSP00000229795; -.
DR   BindingDB; Q16539; -.
DR   ChEMBL; CHEMBL260; -.
DR   DrugBank; DB02277; 1-(5-Tert-Butyl-2-Methyl-2h-Pyrazol-3-Yl)-3-(4-Chloro-Phenyl)-Urea.
DR   DrugBank; DB03044; 1-(5-Tert-Butyl-2-P-Tolyl-2h-Pyrazol-3-Yl)-3-[4-(2-Morpholin-4-Yl-Ethoxy)-Naphthalen-1-Yl]-Urea.
DR   DrugBank; DB06882; 1-[1-(3-aminophenyl)-3-tert-butyl-1H-pyrazol-5-yl]-3-naphthalen-1-ylurea.
DR   DrugBank; DB08395; 2-(ETHOXYMETHYL)-4-(4-FLUOROPHENYL)-3-[2-(2-HYDROXYPHENOXY)PYRIMIDIN-4-YL]ISOXAZOL-5(2H)-ONE.
DR   DrugBank; DB03110; 2-Chlorophenol.
DR   DrugBank; DB07942; 2-fluoro-4-[4-(4-fluorophenyl)-1H-pyrazol-3-yl]pyridine.
DR   DrugBank; DB07943; 2-{4-[5-(4-chlorophenyl)-4-pyrimidin-4-yl-1H-pyrazol-3-yl]piperidin-1-yl}-2-oxoethanol.
DR   DrugBank; DB08093; 3-(1-NAPHTHYLMETHOXY)PYRIDIN-2-AMINE.
DR   DrugBank; DB02352; 3-(Benzyloxy)Pyridin-2-Amine.
DR   DrugBank; DB08730; 3-FLUORO-5-MORPHOLIN-4-YL-N-[1-(2-PYRIDIN-4-YLETHYL)-1H-INDOL-6-YL]BENZAMIDE.
DR   DrugBank; DB08091; 3-FLUORO-5-MORPHOLIN-4-YL-N-[3-(2-PYRIDIN-4-YLETHYL)-1H-INDOL-5-YL]BENZAMIDE.
DR   DrugBank; DB08092; 3-fluoro-N-1H-indol-5-yl-5-morpholin-4-ylbenzamide.
DR   DrugBank; DB04632; 4-(2-HYDROXYBENZYLAMINO)-N-(3-(4-FLUOROPHENOXY)PHENYL)PIPERIDINE-1-SULFONAMIDE.
DR   DrugBank; DB08522; 4-(4-FLUOROPHENYL)-1-CYCLOROPROPYLMETHYL-5-(4-PYRIDYL)-IMIDAZOLE.
DR   DrugBank; DB03980; 4-(Fluorophenyl)-1-Cyclopropylmethyl-5-(2-Amino-4-Pyrimidinyl)Imidazole.
DR   DrugBank; DB07829; 4-[3-(4-FLUOROPHENYL)-1H-PYRAZOL-4-YL]PYRIDINE.
DR   DrugBank; DB07607; 4-[5-(3-IODO-PHENYL)-2-(4-METHANESULFINYL-PHENYL)-1H-IMIDAZOL-4-YL]-PYRIDINE.
DR   DrugBank; DB08521; 4-[5-(4-FLUORO-PHENYL)-2-(4-METHANESULFINYL-PHENYL)-3H-IMIDAZOL-4-YL]-PYRIDINE.
DR   DrugBank; DB01761; 4-[5-[2-(1-Phenyl-Ethylamino)-Pyrimidin-4-Yl]-1-Methyl-4-(3-Trifluoromethylphenyl)-1h-Imidazol-2-Yl]-Piperidine.
DR   DrugBank; DB07459; 4-PHENOXY-N-(PYRIDIN-2-YLMETHYL)BENZAMIDE.
DR   DrugBank; DB01988; 6((S)-3-Benzylpiperazin-1-Yl)-3-(Naphthalen-2-Yl)-4-(Pyridin-4-Yl)Pyrazine.
DR   DrugBank; DB08423; [5-AMINO-1-(4-FLUOROPHENYL)-1H-PYRAZOL-4-YL][3-(PIPERIDIN-4-YLOXY)PHENYL]METHANONE.
DR   DrugBank; DB01953; Inhibitor of P38 Kinase.
DR   DrugBank; DB05157; KC706.
DR   DrugBank; DB08064; N-(3-TERT-BUTYL-1H-PYRAZOL-5-YL)-N'-{4-CHLORO-3-[(PYRIDIN-3-YLOXY)METHYL]PHENYL}UREA.
DR   DrugBank; DB08068; N-[4-CHLORO-3-(PYRIDIN-3-YLOXYMETHYL)-PHENYL]-3-FLUORO-.
DR   DrugBank; DB07307; N-cyclopropyl-4-methyl-3-[1-(2-methylphenyl)phthalazin-6-yl]benzamide.
DR   DrugBank; DB08351; N-cyclopropyl-4-methyl-3-{2-[(2-morpholin-4-ylethyl)amino]quinazolin-6-yl}benzamide.
DR   DrugBank; DB04338; SB220025.
DR   DrugBank; DB05412; SCIO-469.
DR   DrugBank; DB04797; Triazolopyridine.
DR   DrugBank; DB05470; VX-702.
DR   GuidetoPHARMACOLOGY; 1499; -.
DR   iPTMnet; Q16539; -.
DR   PhosphoSitePlus; Q16539; -.
DR   BioMuta; MAPK14; -.
DR   OGP; Q16539; -.
DR   CPTAC; CPTAC-1325; -.
DR   CPTAC; CPTAC-1355; -.
DR   CPTAC; CPTAC-1356; -.
DR   CPTAC; CPTAC-878; -.
DR   CPTAC; CPTAC-879; -.
DR   EPD; Q16539; -.
DR   jPOST; Q16539; -.
DR   MaxQB; Q16539; -.
DR   PaxDb; Q16539; -.
DR   PeptideAtlas; Q16539; -.
DR   PRIDE; Q16539; -.
DR   ProteomicsDB; 60901; -. [Q16539-1]
DR   ProteomicsDB; 60902; -. [Q16539-2]
DR   ProteomicsDB; 60903; -. [Q16539-3]
DR   ProteomicsDB; 60904; -. [Q16539-4]
DR   DNASU; 1432; -.
DR   Ensembl; ENST00000229794; ENSP00000229794; ENSG00000112062. [Q16539-1]
DR   Ensembl; ENST00000229795; ENSP00000229795; ENSG00000112062. [Q16539-2]
DR   Ensembl; ENST00000310795; ENSP00000308669; ENSG00000112062. [Q16539-4]
DR   GeneID; 1432; -.
DR   KEGG; hsa:1432; -.
DR   UCSC; uc003olp.4; human. [Q16539-1]
DR   CTD; 1432; -.
DR   DisGeNET; 1432; -.
DR   GeneCards; MAPK14; -.
DR   HGNC; HGNC:6876; MAPK14.
DR   HPA; CAB010285; -.
DR   HPA; CAB040578; -.
DR   HPA; HPA051825; -.
DR   MIM; 600289; gene.
DR   neXtProt; NX_Q16539; -.
DR   OpenTargets; ENSG00000112062; -.
DR   PharmGKB; PA30621; -.
DR   eggNOG; KOG0660; Eukaryota.
DR   eggNOG; ENOG410XNY0; LUCA.
DR   GeneTree; ENSGT00940000155325; -.
DR   HOGENOM; HOG000233024; -.
DR   InParanoid; Q16539; -.
DR   KO; K04441; -.
DR   OMA; EITNRYT; -.
DR   OrthoDB; 321213at2759; -.
DR   PhylomeDB; Q16539; -.
DR   TreeFam; TF105100; -.
DR   BioCyc; MetaCyc:HS03507-MONOMER; -.
DR   BRENDA; 2.7.11.24; 2681.
DR   Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
DR   Reactome; R-HSA-171007; p38MAPK events.
DR   Reactome; R-HSA-198753; ERK/MAPK targets.
DR   Reactome; R-HSA-2151209; Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
DR   Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
DR   Reactome; R-HSA-376172; DSCAM interactions.
DR   Reactome; R-HSA-418592; ADP signalling through P2Y purinoceptor 1.
DR   Reactome; R-HSA-432142; Platelet sensitization by LDL.
DR   Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
DR   Reactome; R-HSA-450302; activated TAK1 mediates p38 MAPK activation.
DR   Reactome; R-HSA-450341; Activation of the AP-1 family of transcription factors.
DR   Reactome; R-HSA-450604; KSRP (KHSRP) binds and destabilizes mRNA.
DR   Reactome; R-HSA-525793; Myogenesis.
DR   Reactome; R-HSA-5668599; RHO GTPases Activate NADPH Oxidases.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR   SignaLink; Q16539; -.
DR   SIGNOR; Q16539; -.
DR   ChiTaRS; MAPK14; human.
DR   EvolutionaryTrace; Q16539; -.
DR   GeneWiki; MAPK14; -.
DR   GenomeRNAi; 1432; -.
DR   PRO; PR:Q16539; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   Bgee; ENSG00000112062; Expressed in 228 organ(s), highest expression level in blood.
DR   ExpressionAtlas; Q16539; baseline and differential.
DR   Genevisible; Q16539; HS.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR   GO; GO:0000922; C:spindle pole; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR   GO; GO:0004707; F:MAP kinase activity; IDA:UniProtKB.
DR   GO; GO:0004708; F:MAP kinase kinase activity; TAS:ProtInc.
DR   GO; GO:0048273; F:mitogen-activated protein kinase p38 binding; IPI:UniProtKB.
DR   GO; GO:0051525; F:NFAT protein binding; ISS:BHF-UCL.
DR   GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:Reactome.
DR   GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; TAS:UniProtKB.
DR   GO; GO:0000187; P:activation of MAPK activity; TAS:Reactome.
DR   GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0001502; P:cartilage condensation; IEA:Ensembl.
DR   GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR   GO; GO:0071479; P:cellular response to ionizing radiation; IMP:BHF-UCL.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
DR   GO; GO:0071223; P:cellular response to lipoteichoic acid; IMP:UniProtKB.
DR   GO; GO:0071310; P:cellular response to organic substance; IBA:GO_Central.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR   GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IMP:BHF-UCL.
DR   GO; GO:0098586; P:cellular response to virus; IMP:UniProtKB.
DR   GO; GO:0006935; P:chemotaxis; TAS:ProtInc.
DR   GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0000077; P:DNA damage checkpoint; IEA:Ensembl.
DR   GO; GO:0019395; P:fatty acid oxidation; IEA:Ensembl.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl.
DR   GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
DR   GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
DR   GO; GO:0030316; P:osteoclast differentiation; ISS:BHF-UCL.
DR   GO; GO:0038066; P:p38MAPK cascade; ISS:UniProtKB.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:BHF-UCL.
DR   GO; GO:0001890; P:placenta development; IEA:Ensembl.
DR   GO; GO:0090336; P:positive regulation of brown fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IEA:Ensembl.
DR   GO; GO:0031281; P:positive regulation of cyclase activity; IMP:CACAO.
DR   GO; GO:0002741; P:positive regulation of cytokine secretion involved in immune response; IEA:Ensembl.
DR   GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IMP:BHF-UCL.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0046326; P:positive regulation of glucose import; IEA:Ensembl.
DR   GO; GO:2001184; P:positive regulation of interleukin-12 secretion; IMP:UniProtKB.
DR   GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IEA:Ensembl.
DR   GO; GO:1905050; P:positive regulation of metallopeptidase activity; IEA:Ensembl.
DR   GO; GO:0051149; P:positive regulation of muscle cell differentiation; TAS:Reactome.
DR   GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:UniProtKB.
DR   GO; GO:1901741; P:positive regulation of myoblast fusion; ISS:UniProtKB.
DR   GO; GO:0010831; P:positive regulation of myotube differentiation; ISS:UniProtKB.
DR   GO; GO:0042307; P:positive regulation of protein import into nucleus; IEA:Ensembl.
DR   GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IMP:BHF-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0007265; P:Ras protein signal transduction; TAS:Reactome.
DR   GO; GO:1900015; P:regulation of cytokine production involved in inflammatory response; IDA:CACAO.
DR   GO; GO:0051090; P:regulation of DNA-binding transcription factor activity; TAS:Reactome.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   GO; GO:0030278; P:regulation of ossification; IEA:Ensembl.
DR   GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
DR   GO; GO:0099179; P:regulation of synaptic membrane adhesion; IEA:Ensembl.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0032495; P:response to muramyl dipeptide; IEA:Ensembl.
DR   GO; GO:0035994; P:response to muscle stretch; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   GO; GO:0042770; P:signal transduction in response to DNA damage; IMP:BHF-UCL.
DR   GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
DR   GO; GO:0090400; P:stress-induced premature senescence; IMP:BHF-UCL.
DR   GO; GO:0051146; P:striated muscle cell differentiation; IEA:Ensembl.
DR   GO; GO:0007178; P:transmembrane receptor protein serine/threonine kinase signaling pathway; IEA:Ensembl.
DR   GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IMP:BHF-UCL.
DR   CDD; cd07877; STKc_p38alpha; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR003527; MAP_kinase_CS.
DR   InterPro; IPR008352; MAPK_p38-like.
DR   InterPro; IPR038784; p38alpha.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR01773; P38MAPKINASE.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS01351; MAPK; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Apoptosis;
KW   ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
KW   Reference proteome; Serine/threonine-protein kinase; Stress response;
KW   Transcription; Transcription regulation; Transferase; Ubl conjugation.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:20068231,
FT                                ECO:0000269|PubMed:12665801}.
FT   CHAIN         2    360       Mitogen-activated protein kinase 14.
FT                                /FTId=PRO_0000186291.
FT   DOMAIN       24    308       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND      30     38       ATP.
FT   REGION       70     71       Inhibitor-binding.
FT   REGION      106    110       Inhibitor-binding.
FT   REGION      168    169       Inhibitor-binding.
FT   MOTIF       180    182       TXY.
FT   ACT_SITE    168    168       Proton acceptor.
FT   BINDING      35     35       Inhibitor. {ECO:0000269|PubMed:12897767,
FT                                ECO:0000269|PubMed:15658854,
FT                                ECO:0000269|PubMed:16342939}.
FT   BINDING      53     53       ATP.
FT   BINDING      53     53       Inhibitor. {ECO:0000269|PubMed:12897767,
FT                                ECO:0000269|PubMed:15658854,
FT                                ECO:0000269|PubMed:16342939}.
FT   BINDING      71     71       Inhibitor. {ECO:0000269|PubMed:12897767,
FT                                ECO:0000269|PubMed:15658854,
FT                                ECO:0000269|PubMed:16342939}.
FT   BINDING     109    109       Inhibitor; via amide nitrogen and
FT                                carbonyl oxygen.
FT                                {ECO:0000269|PubMed:12897767,
FT                                ECO:0000269|PubMed:15658854,
FT                                ECO:0000269|PubMed:16342939}.
FT   BINDING     154    154       Inhibitor; via carbonyl oxygen.
FT                                {ECO:0000269|PubMed:12897767,
FT                                ECO:0000269|PubMed:15658854,
FT                                ECO:0000269|PubMed:16342939}.
FT   BINDING     168    168       Inhibitor; via amide nitrogen and
FT                                carbonyl oxygen.
FT                                {ECO:0000269|PubMed:12897767,
FT                                ECO:0000269|PubMed:15658854,
FT                                ECO:0000269|PubMed:16342939}.
FT   BINDING     197    197       Inhibitor. {ECO:0000269|PubMed:12897767,
FT                                ECO:0000269|PubMed:15658854,
FT                                ECO:0000269|PubMed:16342939}.
FT   BINDING     252    252       Inhibitor; via amide nitrogen.
FT                                {ECO:0000269|PubMed:12897767,
FT                                ECO:0000269|PubMed:15658854,
FT                                ECO:0000269|PubMed:16342939}.
FT   MOD_RES       2      2       N-acetylserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES       2      2       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES      16     16       Phosphothreonine.
FT                                {ECO:0000244|PubMed:18691976}.
FT   MOD_RES      53     53       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:21444723}.
FT   MOD_RES     152    152       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:21444723}.
FT   MOD_RES     180    180       Phosphothreonine; by MAP2K3, MAP2K4,
FT                                MAP2K6 and autocatalysis.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163,
FT                                ECO:0000269|PubMed:7535770}.
FT   MOD_RES     182    182       Phosphotyrosine; by MAP2K3, MAP2K4,
FT                                MAP2K6 and autocatalysis.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163,
FT                                ECO:0000269|PubMed:7535770}.
FT   MOD_RES     263    263       Phosphothreonine.
FT                                {ECO:0000244|PubMed:17525332}.
FT   MOD_RES     323    323       Phosphotyrosine; by ZAP70.
FT                                {ECO:0000269|PubMed:15735648}.
FT   VAR_SEQ     230    254       DQLKLILRLVGTPGAELLKKISSES -> NQLQQIMRLTGT
FT                                PPAYLINRMPSHE (in isoform CSBP1).
FT                                {ECO:0000303|PubMed:7997261}.
FT                                /FTId=VSP_004842.
FT   VAR_SEQ     255    360       ARNYIQSLTQMPKMNFANVFIGANPLAVDLLEKMLVLDSDK
FT                                RITAAQALAHAYFAQYHDPDDEPVADPYDQSFESRDLLIDE
FT                                WKSLTYDEVISFVPPPLDQEEMES -> VS (in
FT                                isoform 5).
FT                                {ECO:0000303|PubMed:19906316}.
FT                                /FTId=VSP_057194.
FT   VAR_SEQ     255    307       ARNYIQSLTQMPKMNFANVFIGANPLAVDLLEKMLVLDSDK
FT                                RITAAQALAHAY -> LSTCWRRCLYWTQIRELQRPKPLHM
FT                                PTLLSTTILMMNQWPILMISPLKAGTSL (in isoform
FT                                Exip). {ECO:0000303|PubMed:11866441}.
FT                                /FTId=VSP_004843.
FT   VAR_SEQ     281    360       AVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPDDEPVAD
FT                                PYDQSFESRDLLIDEWKSLTYDEVISFVPPPLDQEEMES
FT                                -> GKLTIYPHLMDIELVMI (in isoform Mxi2).
FT                                {ECO:0000303|PubMed:7479834}.
FT                                /FTId=VSP_004844.
FT   VAR_SEQ     308    360       Missing (in isoform Exip).
FT                                {ECO:0000303|PubMed:11866441}.
FT                                /FTId=VSP_004845.
FT   VARIANT      51     51       A -> V (in a gastric adenocarcinoma
FT                                sample; somatic mutation).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_042270.
FT   VARIANT     322    322       P -> R (in a lung adenocarcinoma sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_042271.
FT   VARIANT     343    343       D -> G (in dbSNP:rs45496794).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_042272.
FT   MUTAGEN      34     34       A->V: Lowered kinase activity.
FT                                {ECO:0000269|PubMed:7493921}.
FT   MUTAGEN      53     53       K->R: Loss of kinase activity.
FT                                {ECO:0000269|PubMed:7493921}.
FT   MUTAGEN      54     54       K->R: Impairs MAP2K6/MKK6-dependent
FT                                autophosphorylation.
FT                                {ECO:0000269|PubMed:11010976}.
FT   MUTAGEN      69     69       Y->H: Lowered kinase activity.
FT                                {ECO:0000269|PubMed:15284239}.
FT   MUTAGEN     168    168       D->A: Loss of kinase activity.
FT                                {ECO:0000269|PubMed:7493921}.
FT   MUTAGEN     175    175       T->A: No effect on either the kinase
FT                                activity or tyrosine phosphorylation.
FT                                {ECO:0000269|PubMed:7493921}.
FT   MUTAGEN     176    176       D->A: Emulation of the active state.
FT                                Increase in activity; when associated
FT                                with S-327 or L-327.
FT                                {ECO:0000269|PubMed:15284239}.
FT   MUTAGEN     177    177       D->A: Loss of kinase activity.
FT                                {ECO:0000269|PubMed:15284239}.
FT   MUTAGEN     180    180       T->E: Loss of kinase activity.
FT                                {ECO:0000269|PubMed:7493921}.
FT   MUTAGEN     182    182       Y->F: Loss of kinase activity.
FT                                {ECO:0000269|PubMed:7493921}.
FT   MUTAGEN     320    320       A->T: Lowered kinase activity.
FT                                {ECO:0000269|PubMed:15284239}.
FT   MUTAGEN     327    327       F->L: Emulation of the active state.
FT                                Increase in activity; when associated
FT                                with A-176.
FT                                {ECO:0000269|PubMed:15284239}.
FT   MUTAGEN     327    327       F->S: Emulation of the active state.
FT                                Increase in activity; when associated
FT                                with A-176.
FT                                {ECO:0000269|PubMed:15284239}.
FT   MUTAGEN     337    337       W->R: Loss of kinase activity.
FT                                {ECO:0000269|PubMed:15284239}.
FT   CONFLICT     67     67       R -> G (in Ref. 7; BAF84398).
FT                                {ECO:0000305}.
FT   STRAND        8     13       {ECO:0000244|PDB:2FST}.
FT   STRAND       16     21       {ECO:0000244|PDB:2FST}.
FT   STRAND       24     29       {ECO:0000244|PDB:2FST}.
FT   HELIX        31     33       {ECO:0000244|PDB:2GFS}.
FT   TURN         34     36       {ECO:0000244|PDB:3BV2}.
FT   STRAND       38     43       {ECO:0000244|PDB:2FST}.
FT   TURN         44     47       {ECO:0000244|PDB:2FST}.
FT   STRAND       48     54       {ECO:0000244|PDB:2FST}.
FT   HELIX        62     77       {ECO:0000244|PDB:2FST}.
FT   STRAND       87     90       {ECO:0000244|PDB:2FST}.
FT   HELIX        96     98       {ECO:0000244|PDB:2FST}.
FT   STRAND      103    107       {ECO:0000244|PDB:2FST}.
FT   STRAND      110    112       {ECO:0000244|PDB:3LFF}.
FT   TURN        113    115       {ECO:0000244|PDB:4GEO}.
FT   TURN        116    119       {ECO:0000244|PDB:3LFF}.
FT   HELIX       124    143       {ECO:0000244|PDB:2FST}.
FT   HELIX       153    155       {ECO:0000244|PDB:2FST}.
FT   STRAND      156    158       {ECO:0000244|PDB:2FST}.
FT   TURN        160    162       {ECO:0000244|PDB:2RG6}.
FT   STRAND      164    166       {ECO:0000244|PDB:2FST}.
FT   STRAND      168    170       {ECO:0000244|PDB:4GEO}.
FT   HELIX       173    175       {ECO:0000244|PDB:1ZZL}.
FT   TURN        176    179       {ECO:0000244|PDB:5XYY}.
FT   STRAND      180    182       {ECO:0000244|PDB:3FMK}.
FT   TURN        185    188       {ECO:0000244|PDB:3LFF}.
FT   HELIX       191    194       {ECO:0000244|PDB:2FST}.
FT   STRAND      197    199       {ECO:0000244|PDB:4EHV}.
FT   HELIX       204    218       {ECO:0000244|PDB:2FST}.
FT   HELIX       228    239       {ECO:0000244|PDB:2FST}.
FT   HELIX       244    247       {ECO:0000244|PDB:2FST}.
FT   HELIX       253    260       {ECO:0000244|PDB:2FST}.
FT   HELIX       270    273       {ECO:0000244|PDB:2FST}.
FT   TURN        274    276       {ECO:0000244|PDB:2FST}.
FT   HELIX       279    288       {ECO:0000244|PDB:2FST}.
FT   HELIX       293    295       {ECO:0000244|PDB:2FST}.
FT   HELIX       299    303       {ECO:0000244|PDB:2FST}.
FT   HELIX       306    308       {ECO:0000244|PDB:2FST}.
FT   TURN        309    311       {ECO:0000244|PDB:2FST}.
FT   HELIX       314    316       {ECO:0000244|PDB:2FST}.
FT   HELIX       325    327       {ECO:0000244|PDB:2FST}.
FT   HELIX       334    347       {ECO:0000244|PDB:2FST}.
SQ   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
//
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