GenomeNet

Database: UniProt
Entry: P53779
LinkDB: P53779
Original site: P53779 
ID   MK10_HUMAN              Reviewed;         464 AA.
AC   P53779; A6NFS3; A6NG28; B3KQ94; Q15707; Q49AP1;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   09-JUL-2014, entry version 165.
DE   RecName: Full=Mitogen-activated protein kinase 10;
DE            Short=MAP kinase 10;
DE            Short=MAPK 10;
DE            EC=2.7.11.24;
DE   AltName: Full=MAP kinase p49 3F12;
DE   AltName: Full=Stress-activated protein kinase 1b;
DE            Short=SAPK1b;
DE   AltName: Full=Stress-activated protein kinase JNK3;
DE   AltName: Full=c-Jun N-terminal kinase 3;
GN   Name=MAPK10; Synonyms=JNK3, JNK3A, PRKM10, SAPK1B;
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] (ISOFORM ALPHA-1).
RC   TISSUE=Hippocampus;
RX   PubMed=7826642; DOI=10.1016/0896-6273(95)90241-4;
RA   Mohit A.A., Martin J.H., Miller C.A.;
RT   "p493F12 kinase: a novel MAP kinase expressed in a subset of neurons
RT   in the human nervous system.";
RL   Neuron 14:67-78(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-1 AND ALPHA-2).
RC   TISSUE=Brain;
RX   PubMed=8654373;
RA   Gupta S., Barrett T., Whitmarsh A.J., Cavanagh J., Sluss H.K.,
RA   Derijard B., Davis R.J.;
RT   "Selective interaction of JNK protein kinase isoforms with
RT   transcription factors.";
RL   EMBO J. 15:2760-2770(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC   TISSUE=Caudate nucleus;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-2).
RC   TISSUE=Brain;
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   [7]
RP   PARTIAL PROTEIN SEQUENCE, REGULATION BY MAP2K4 AND MAP2K7,
RP   PHOSPHORYLATION AT THR-221 AND TYR-223, COFACTOR, AND MASS
RP   SPECTROMETRY.
RX   PubMed=10715136; DOI=10.1021/bi992410+;
RA   Lisnock J., Griffin P., Calaycay J., Frantz B., Parsons J.,
RA   O'Keefe S.J., LoGrasso P.;
RT   "Activation of JNK3 alpha 1 requires both MKK4 and MKK7: kinetic
RT   characterization of in vitro phosphorylated JNK3 alpha 1.";
RL   Biochemistry 39:3141-3148(2000).
RN   [8]
RP   ENZYME REGULATION.
RX   PubMed=11062067; DOI=10.1042/0264-6021:3520145;
RA   Fleming Y., Armstrong C.G., Morrice N., Paterson A., Goedert M.,
RA   Cohen P.;
RT   "Synergistic activation of stress-activated protein kinase 1/c-Jun N-
RT   terminal kinase (SAPK1/JNK) isoforms by mitogen-activated protein
RT   kinase kinase 4 (MKK4) and MKK7.";
RL   Biochem. J. 352:145-154(2000).
RN   [9]
RP   FUNCTION IN PHOSPHORYLATION OF STMN2.
RX   PubMed=11718727; DOI=10.1016/S0014-5793(01)03090-3;
RA   Neidhart S., Antonsson B., Gillieron C., Vilbois F., Grenningloh G.,
RA   Arkinstall S.;
RT   "c-Jun N-terminal kinase-3 (JNK3)/stress-activated protein kinase-beta
RT   (SAPKbeta) binds and phosphorylates the neuronal microtubule regulator
RT   SCG10.";
RL   FEBS Lett. 508:259-264(2001).
RN   [10]
RP   INTERACTION WITH SPAG9.
RX   PubMed=15693750; DOI=10.1042/BJ20041577;
RA   Jagadish N., Rana R., Selvi R., Mishra D., Garg M., Yadav S.,
RA   Herr J.C., Okumura K., Hasegawa A., Koyama K., Suri A.;
RT   "Characterization of a novel human sperm-associated antigen 9 (SPAG9)
RT   having structural homology with c-Jun N-terminal kinase-interacting
RT   protein.";
RL   Biochem. J. 389:73-82(2005).
RN   [11]
RP   CHROMOSOMAL REARRANGEMENT, AND DISEASE.
RX   PubMed=16249883; DOI=10.1007/s00439-005-0084-y;
RA   Shoichet S.A., Duprez L., Hagens O., Waetzig V., Menzel C.,
RA   Herdegen T., Schweiger S., Dan B., Vamos E., Ropers H.-H.,
RA   Kalscheuer V.M.;
RT   "Truncation of the CNS-expressed JNK3 in a patient with a severe
RT   developmental epileptic encephalopathy.";
RL   Hum. Genet. 118:559-567(2006).
RN   [12]
RP   SUBCELLULAR LOCATION.
RX   PubMed=16737965; DOI=10.1074/jbc.M603659200;
RA   Song X., Raman D., Gurevich E.V., Vishnivetskiy S.A., Gurevich V.V.;
RT   "Visual and both non-visual arrestins in their 'inactive' conformation
RT   bind JNK3 and Mdm2 and relocalize them from the nucleus to the
RT   cytoplasm.";
RL   J. Biol. Chem. 281:21491-21499(2006).
RN   [13]
RP   INTERACTION WITH HDAC9, AND ENZYME REGULATION.
RX   PubMed=16611996; DOI=10.1128/MCB.26.9.3550-3564.2006;
RA   Morrison B.E., Majdzadeh N., Zhang X., Lyles A., Bassel-Duby R.,
RA   Olson E.N., D'Mello S.R.;
RT   "Neuroprotection by histone deacetylase-related protein.";
RL   Mol. Cell. Biol. 26:3550-3564(2006).
RN   [14]
RP   INTERACTION WITH ARRB2.
RX   PubMed=18435604; DOI=10.1042/BJ20080685;
RA   Xu T.-R., Baillie G.S., Bhari N., Houslay T.M., Pitt A.M., Adams D.R.,
RA   Kolch W., Houslay M.D., Milligan G.;
RT   "Mutations of beta-arrestin 2 that limit self-association also
RT   interfere with interactions with the beta2-adrenoceptor and the ERK1/2
RT   MAPKs: implications for beta2-adrenoceptor signalling via the ERK1/2
RT   MAPKs.";
RL   Biochem. J. 413:51-60(2008).
RN   [15]
RP   PALMITOYLATION AT CYS-462 AND CYS-463, AND MUTAGENESIS OF CYS-462 AND
RP   CYS-463.
RX   PubMed=21941371; DOI=10.1038/cdd.2011.124;
RA   Yang G., Liu Y., Yang K., Liu R., Zhu S., Coquinco A., Wen W.,
RA   Kojic L., Jia W., Cynader M.;
RT   "Isoform-specific palmitoylation of JNK regulates axonal
RT   development.";
RL   Cell Death Differ. 19:553-561(2012).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 40-402.
RX   PubMed=9739089; DOI=10.1016/S0969-2126(98)00100-2;
RA   Xie X., Gu Y., Fox T., Coll J.T., Fleming M.A., Markland W.,
RA   Caron P.R., Wilson K.P., Su M.S.-S.;
RT   "Crystal structure of JNK3: a kinase implicated in neuronal
RT   apoptosis.";
RL   Structure 6:983-991(1998).
CC   -!- FUNCTION: Serine/threonine-protein kinase involved in various
CC       processes such as neuronal proliferation, differentiation,
CC       migration and programmed cell death. Extracellular stimuli such as
CC       proinflammatory cytokines or physical stress stimulate the stress-
CC       activated protein kinase/c-Jun N-terminal kinase (SAP/JNK)
CC       signaling pathway. In this cascade, two dual specificity kinases
CC       MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate
CC       MAPK10/JNK3. In turn, MAPK10/JNK3 phosphorylates a number of
CC       transcription factors, primarily components of AP-1 such as JUN
CC       and ATF2 and thus regulates AP-1 transcriptional activity. Plays
CC       regulatory roles in the signaling pathways during neuronal
CC       apoptosis. Phosphorylates the neuronal microtubule regulator
CC       STMN2. Acts in the regulation of the beta-amyloid precursor
CC       protein/APP signaling during neuronal differentiation by
CC       phosphorylating APP. Participates also in neurite growth in spiral
CC       ganglion neurons.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium.
CC   -!- ENZYME REGULATION: Activated by threonine and tyrosine
CC       phosphorylation by two dual specificity kinases, MAP2K4 and
CC       MAP2K7. MAP2K7 phosphorylates MAPK10 on Thr-221 causing a
CC       conformational change and a large increase in Vmax. MAP2K4 then
CC       phosphorylates Tyr-223 resulting in a further increase in Vmax.
CC       Inhibited by dual specificity phosphatases, such as DUSP1.
CC       Inhibited by HDAC9.
CC   -!- SUBUNIT: Interacts with MAPKBP1 (By similarity). Binds to at least
CC       four scaffolding proteins, MAPK8IP1/JIP-1, MAPK8IP2/JIP-2,
CC       MAPK8IP3/JIP-3/JSAP1 and SPAG9/MAPK8IP4/JIP-4. These proteins also
CC       bind other components of the JNK signaling pathway. Interacts with
CC       HDAC9. Interacts with ARRB2; the interaction enhances MAPK10
CC       activation by MAP3K5. Interacts with SARM1 (By similarity).
CC   -!- INTERACTION:
CC       P49407:ARRB1; NbExp=2; IntAct=EBI-713543, EBI-743313;
CC       P05412:JUN; NbExp=2; IntAct=EBI-713543, EBI-852823;
CC       Q04206:RELA; NbExp=2; IntAct=EBI-713543, EBI-73886;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Lipid-anchor. Nucleus.
CC       Mitochondrion. Note=Palmitoylation regulates MAPK10 trafficking to
CC       cytoskeleton. Recruited to the mitochondria in the presence of
CC       SARM1 (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC         Comment=A similar low level of binding to substrates is observed
CC         for isoform alpha-1 and isoform alpha-2. However, there is no
CC         correlation between binding and phosphorylation, which is
CC         achieved about at the same efficiency by all isoforms;
CC       Name=Alpha-2;
CC         IsoId=P53779-1; Sequence=Displayed;
CC       Name=Alpha-1;
CC         IsoId=P53779-2; Sequence=VSP_004839;
CC       Name=3;
CC         IsoId=P53779-3; Sequence=VSP_041911;
CC       Name=4;
CC         IsoId=P53779-4; Sequence=VSP_041910, VSP_004839;
CC   -!- TISSUE SPECIFICITY: Specific to a subset of neurons in the nervous
CC       system. Present in the hippocampus and areas, cerebellum,
CC       striatum, brain stem, and weakly in the spinal cord. Very weak
CC       expression in testis 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-221 and Tyr-223 by MAP2K4 and
CC       MAP2K7, which activates the enzyme. MAP2K7 shows a strong
CC       preference for Thr-221 while MAP2K4 phosphorylates Tyr-223
CC       preferentially. Weakly autophosphorylated on threonine and
CC       tyrosine residues in vitro.
CC   -!- PTM: Palmitoylation regulates subcellular location and axonal
CC       development.
CC   -!- MASS SPECTROMETRY: Mass=44070; Method=Electrospray; Range=1-464;
CC       Source=PubMed:10715136;
CC   -!- DISEASE: Note=A chromosomal aberration involving MAPK10 has been
CC       found in a single patient with pharmacoresistant epileptic
CC       encephalopathy. Translocation t(Y;4)(q11.2;q21) which causes
CC       MAPK10 truncation.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. MAP kinase subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/JNK3ID427.html";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U07620; AAC50101.1; -; mRNA.
DR   EMBL; U34819; AAC50604.1; -; mRNA.
DR   EMBL; U34820; AAC50605.1; -; mRNA.
DR   EMBL; AK057723; BAG51956.1; -; mRNA.
DR   EMBL; AK124791; BAG54096.1; -; mRNA.
DR   EMBL; AC096953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC104059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC104827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC108054; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC110076; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471057; EAX05963.1; -; Genomic_DNA.
DR   EMBL; BC035057; AAH35057.1; -; mRNA.
DR   CCDS; CCDS34026.1; -. [P53779-1]
DR   CCDS; CCDS3612.1; -. [P53779-3]
DR   CCDS; CCDS3613.1; -. [P53779-4]
DR   CCDS; CCDS43247.1; -. [P53779-2]
DR   PIR; S71104; S71104.
DR   RefSeq; NP_002744.1; NM_002753.3. [P53779-2]
DR   RefSeq; NP_620446.1; NM_138980.2. [P53779-3]
DR   RefSeq; NP_620447.1; NM_138981.2. [P53779-4]
DR   RefSeq; NP_620448.1; NM_138982.2. [P53779-1]
DR   RefSeq; XP_005263186.1; XM_005263129.1. [P53779-1]
DR   RefSeq; XP_005263187.1; XM_005263130.1. [P53779-1]
DR   RefSeq; XP_005263192.1; XM_005263135.2. [P53779-2]
DR   RefSeq; XP_006714330.1; XM_006714267.1. [P53779-1]
DR   RefSeq; XP_006714331.1; XM_006714268.1. [P53779-3]
DR   UniGene; Hs.125503; -.
DR   UniGene; Hs.13438; -.
DR   PDB; 1JNK; X-ray; 2.30 A; A=1-423.
DR   PDB; 1PMN; X-ray; 2.20 A; A=40-401.
DR   PDB; 1PMQ; X-ray; 2.20 A; A=40-401.
DR   PDB; 1PMU; X-ray; 2.70 A; A=40-401.
DR   PDB; 1PMV; X-ray; 2.50 A; A=40-401.
DR   PDB; 2B1P; X-ray; 1.90 A; A=46-400.
DR   PDB; 2EXC; X-ray; 2.75 A; X=45-400.
DR   PDB; 2O0U; X-ray; 2.10 A; A=39-402.
DR   PDB; 2O2U; X-ray; 2.45 A; A=39-402.
DR   PDB; 2OK1; X-ray; 2.40 A; A=40-402.
DR   PDB; 2P33; X-ray; 2.40 A; A=40-402.
DR   PDB; 2R9S; X-ray; 2.40 A; A/B=46-401.
DR   PDB; 2WAJ; X-ray; 2.40 A; A=39-402.
DR   PDB; 2ZDT; X-ray; 2.00 A; A=39-402.
DR   PDB; 2ZDU; X-ray; 2.50 A; A=39-402.
DR   PDB; 3CGF; X-ray; 3.00 A; A=40-402.
DR   PDB; 3CGO; X-ray; 3.00 A; A=40-402.
DR   PDB; 3DA6; X-ray; 2.00 A; A=39-402.
DR   PDB; 3FI2; X-ray; 2.28 A; A=39-402.
DR   PDB; 3FI3; X-ray; 2.20 A; A=39-402.
DR   PDB; 3FV8; X-ray; 2.28 A; A=39-402.
DR   PDB; 3G90; X-ray; 2.40 A; X=40-402.
DR   PDB; 3G9L; X-ray; 2.20 A; X=40-402.
DR   PDB; 3G9N; X-ray; 2.80 A; A=40-402.
DR   PDB; 3KVX; X-ray; 2.40 A; A=39-402.
DR   PDB; 3OXI; X-ray; 2.20 A; A=40-401.
DR   PDB; 3OY1; X-ray; 1.70 A; A=40-401.
DR   PDB; 3PTG; X-ray; 2.43 A; A=40-401.
DR   PDB; 3RTP; X-ray; 2.40 A; A=40-401.
DR   PDB; 3TTI; X-ray; 2.20 A; A=1-464.
DR   PDB; 3TTJ; X-ray; 2.10 A; A=1-464.
DR   PDB; 3V6R; X-ray; 2.60 A; A/B=39-402.
DR   PDB; 3V6S; X-ray; 2.97 A; A/B=39-402.
DR   PDB; 4H36; X-ray; 3.00 A; A=46-400.
DR   PDB; 4H39; X-ray; 1.99 A; A=46-400.
DR   PDB; 4H3B; X-ray; 2.08 A; A/C=46-400.
DR   PDB; 4KKE; X-ray; 2.20 A; A=40-402.
DR   PDB; 4KKG; X-ray; 2.40 A; A=40-402.
DR   PDB; 4KKH; X-ray; 2.00 A; A=40-402.
DR   PDBsum; 1JNK; -.
DR   PDBsum; 1PMN; -.
DR   PDBsum; 1PMQ; -.
DR   PDBsum; 1PMU; -.
DR   PDBsum; 1PMV; -.
DR   PDBsum; 2B1P; -.
DR   PDBsum; 2EXC; -.
DR   PDBsum; 2O0U; -.
DR   PDBsum; 2O2U; -.
DR   PDBsum; 2OK1; -.
DR   PDBsum; 2P33; -.
DR   PDBsum; 2R9S; -.
DR   PDBsum; 2WAJ; -.
DR   PDBsum; 2ZDT; -.
DR   PDBsum; 2ZDU; -.
DR   PDBsum; 3CGF; -.
DR   PDBsum; 3CGO; -.
DR   PDBsum; 3DA6; -.
DR   PDBsum; 3FI2; -.
DR   PDBsum; 3FI3; -.
DR   PDBsum; 3FV8; -.
DR   PDBsum; 3G90; -.
DR   PDBsum; 3G9L; -.
DR   PDBsum; 3G9N; -.
DR   PDBsum; 3KVX; -.
DR   PDBsum; 3OXI; -.
DR   PDBsum; 3OY1; -.
DR   PDBsum; 3PTG; -.
DR   PDBsum; 3RTP; -.
DR   PDBsum; 3TTI; -.
DR   PDBsum; 3TTJ; -.
DR   PDBsum; 3V6R; -.
DR   PDBsum; 3V6S; -.
DR   PDBsum; 4H36; -.
DR   PDBsum; 4H39; -.
DR   PDBsum; 4H3B; -.
DR   PDBsum; 4KKE; -.
DR   PDBsum; 4KKG; -.
DR   PDBsum; 4KKH; -.
DR   ProteinModelPortal; P53779; -.
DR   SMR; P53779; 11-429.
DR   BioGrid; 111588; 42.
DR   DIP; DIP-1015N; -.
DR   IntAct; P53779; 18.
DR   MINT; MINT-1373516; -.
DR   STRING; 9606.ENSP00000352157; -.
DR   BindingDB; P53779; -.
DR   ChEMBL; CHEMBL3038502; -.
DR   GuidetoPHARMACOLOGY; 1498; -.
DR   PhosphoSite; P53779; -.
DR   DMDM; 2507196; -.
DR   MaxQB; P53779; -.
DR   PaxDb; P53779; -.
DR   PRIDE; P53779; -.
DR   DNASU; 5602; -.
DR   Ensembl; ENST00000359221; ENSP00000352157; ENSG00000109339. [P53779-1]
DR   Ensembl; ENST00000361569; ENSP00000355297; ENSG00000109339. [P53779-2]
DR   Ensembl; ENST00000395160; ENSP00000378589; ENSG00000109339. [P53779-4]
DR   Ensembl; ENST00000395161; ENSP00000378590; ENSG00000109339. [P53779-2]
DR   Ensembl; ENST00000395166; ENSP00000378595; ENSG00000109339. [P53779-3]
DR   Ensembl; ENST00000395169; ENSP00000378598; ENSG00000109339. [P53779-3]
DR   GeneID; 5602; -.
DR   KEGG; hsa:5602; -.
DR   UCSC; uc003hpo.3; human. [P53779-1]
DR   UCSC; uc003hpp.3; human. [P53779-4]
DR   UCSC; uc003hpt.3; human. [P53779-2]
DR   CTD; 5602; -.
DR   GeneCards; GC04M086878; -.
DR   H-InvDB; HIX0163985; -.
DR   HGNC; HGNC:6872; MAPK10.
DR   HPA; CAB022625; -.
DR   MIM; 602897; gene.
DR   neXtProt; NX_P53779; -.
DR   Orphanet; 2382; Lennox-Gastaut syndrome.
DR   PharmGKB; PA30617; -.
DR   eggNOG; COG0515; -.
DR   HOGENOM; HOG000233024; -.
DR   HOVERGEN; HBG014652; -.
DR   InParanoid; P53779; -.
DR   KO; K04440; -.
DR   OMA; EVMNFEE; -.
DR   OrthoDB; EOG7PCJGV; -.
DR   PhylomeDB; P53779; -.
DR   TreeFam; TF105100; -.
DR   BRENDA; 2.7.11.24; 2681.
DR   Reactome; REACT_120956; Cellular responses to stress.
DR   Reactome; REACT_6782; TRAF6 Mediated Induction of proinflammatory cytokines.
DR   Reactome; REACT_6900; Immune System.
DR   SignaLink; P53779; -.
DR   ChiTaRS; MAPK10; human.
DR   EvolutionaryTrace; P53779; -.
DR   GeneWiki; MAPK10; -.
DR   GenomeRNAi; 5602; -.
DR   NextBio; 21762; -.
DR   PRO; PR:P53779; -.
DR   ArrayExpress; P53779; -.
DR   Bgee; P53779; -.
DR   CleanEx; HS_MAPK10; -.
DR   Genevestigator; P53779; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004705; F:JUN kinase activity; ISS:UniProtKB.
DR   GO; GO:0004708; F:MAP kinase kinase activity; TAS:ProtInc.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0000187; P:activation of MAPK activity; TAS:GOC.
DR   GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR   GO; GO:0007254; P:JNK cascade; ISS:UniProtKB.
DR   GO; GO:0007258; P:JUN phosphorylation; ISS:GOC.
DR   GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0002756; P:MyD88-independent toll-like receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0051090; P:regulation of sequence-specific DNA binding transcription factor activity; TAS:Reactome.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   GO; GO:0051403; P:stress-activated MAPK cascade; TAS:Reactome.
DR   GO; GO:0034166; P:toll-like receptor 10 signaling pathway; TAS:Reactome.
DR   GO; GO:0034134; P:toll-like receptor 2 signaling pathway; TAS:Reactome.
DR   GO; GO:0034138; P:toll-like receptor 3 signaling pathway; TAS:Reactome.
DR   GO; GO:0034142; P:toll-like receptor 4 signaling pathway; TAS:Reactome.
DR   GO; GO:0034146; P:toll-like receptor 5 signaling pathway; TAS:Reactome.
DR   GO; GO:0034162; P:toll-like receptor 9 signaling pathway; TAS:Reactome.
DR   GO; GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0038123; P:toll-like receptor TLR1:TLR2 signaling pathway; TAS:Reactome.
DR   GO; GO:0038124; P:toll-like receptor TLR6:TLR2 signaling pathway; TAS:Reactome.
DR   GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR003527; MAP_kinase_CS.
DR   InterPro; IPR008351; MAPK_JNK.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR002290; Ser/Thr_dual-sp_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR01772; JNKMAPKINASE.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS01351; MAPK; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding;
KW   Chromosomal rearrangement; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Epilepsy; Kinase; Lipoprotein; Membrane;
KW   Mental retardation; Mitochondrion; Nucleotide-binding; Nucleus;
KW   Palmitate; Phosphoprotein; Reference proteome; S-nitrosylation;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    464       Mitogen-activated protein kinase 10.
FT                                /FTId=PRO_0000186277.
FT   DOMAIN       64    359       Protein kinase.
FT   NP_BIND      70     78       ATP.
FT   MOTIF       221    223       TXY.
FT   ACT_SITE    189    189       Proton acceptor.
FT   BINDING      93     93       ATP.
FT   MOD_RES     154    154       S-nitrosocysteine (By similarity).
FT   MOD_RES     221    221       Phosphothreonine; by MAP2K7.
FT   MOD_RES     223    223       Phosphotyrosine; by MAP2K4.
FT   LIPID       462    462       S-palmitoyl cysteine (Probable).
FT   LIPID       463    463       S-palmitoyl cysteine (Probable).
FT   VAR_SEQ       1    145       Missing (in isoform 4).
FT                                /FTId=VSP_041910.
FT   VAR_SEQ       1     38       Missing (in isoform 3).
FT                                /FTId=VSP_041911.
FT   VAR_SEQ     418    464       GAAVNSSESLPPSSSVNDISSMSTDQTLASDTDSSLEASAG
FT                                PLGCCR -> AQVQQ (in isoform Alpha-1 and
FT                                isoform 4).
FT                                /FTId=VSP_004839.
FT   MUTAGEN     462    462       C->S: Loss of palmitoylation.
FT   MUTAGEN     463    463       C->S: Loss of palmitoylation.
FT   CONFLICT    162    162       D -> G (in Ref. 3; BAG51956).
FT   STRAND       48     53
FT   STRAND       56     61
FT   STRAND       64     69
FT   STRAND       77     83
FT   TURN         84     87
FT   STRAND       88     97
FT   HELIX        98    100
FT   HELIX       102    114
FT   TURN        115    117
FT   STRAND      121    123
FT   STRAND      127    130
FT   TURN        136    138
FT   STRAND      142    147
FT   STRAND      150    152
FT   HELIX       153    157
FT   HELIX       163    182
FT   HELIX       192    194
FT   STRAND      195    197
FT   STRAND      199    201
FT   STRAND      203    205
FT   STRAND      207    209
FT   TURN        212    214
FT   HELIX       216    219
FT   STRAND      220    222
FT   HELIX       227    229
FT   HELIX       232    235
FT   HELIX       244    258
FT   HELIX       268    279
FT   HELIX       284    287
FT   HELIX       292    299
FT   HELIX       309    312
FT   HELIX       315    317
FT   HELIX       323    339
FT   TURN        344    346
FT   HELIX       350    355
FT   TURN        357    361
FT   HELIX       365    368
FT   HELIX       378    382
FT   HELIX       387    399
SQ   SEQUENCE   464 AA;  52585 MW;  2E20C05EB89CDA66 CRC64;
     MSLHFLYYCS EPTLDVKIAF CQGFDKQVDV SYIAKHYNMS KSKVDNQFYS VEVGDSTFTV
     LKRYQNLKPI GSGAQGIVCA AYDAVLDRNV AIKKLSRPFQ NQTHAKRAYR ELVLMKCVNH
     KNIISLLNVF TPQKTLEEFQ DVYLVMELMD ANLCQVIQME LDHERMSYLL YQMLCGIKHL
     HSAGIIHRDL KPSNIVVKSD CTLKILDFGL ARTAGTSFMM TPYVVTRYYR APEVILGMGY
     KENVDIWSVG CIMGEMVRHK ILFPGRDYID QWNKVIEQLG TPCPEFMKKL QPTVRNYVEN
     RPKYAGLTFP KLFPDSLFPA DSEHNKLKAS QARDLLSKML VIDPAKRISV DDALQHPYIN
     VWYDPAEVEA PPPQIYDKQL DEREHTIEEW KELIYKEVMN SEEKTKNGVV KGQPSPSGAA
     VNSSESLPPS SSVNDISSMS TDQTLASDTD SSLEASAGPL GCCR
//
DBGET integrated database retrieval system