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 29-MAY-2013, entry version 152.
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 INVOLVEMENT IN EPILEPTIC ENCEPHALOPATHY
RP LENNOX-GASTAUT TYPE.
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 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: Epileptic encephalopathy, Lennox-Gastaut type (EELG)
CC [MIM:606369]: A childhhod disorder characterized by a combination
CC of seizures, usually including atypical absence seizures, tonic
CC seizures, atonic or astatic seizures, and mental retardation.
CC Note=The disease is caused by mutations affecting the gene
CC represented in this entry. A chromosomal aberration involving
CC MAPK10 has been found in a single patient. Translocation
CC t(Y;4)(q11.2;q21) which causes 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 -----------------------------------------------------------------------
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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 IPI; IPI00003148; -.
DR IPI; IPI00023547; -.
DR PIR; S71104; S71104.
DR RefSeq; NP_002744.1; NM_002753.3.
DR RefSeq; NP_620446.1; NM_138980.2.
DR RefSeq; NP_620447.1; NM_138981.2.
DR RefSeq; NP_620448.1; NM_138982.2.
DR UniGene; Hs.125503; -.
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; 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 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; 3TTI; -.
DR PDBsum; 3TTJ; -.
DR PDBsum; 3V6R; -.
DR PDBsum; 3V6S; -.
DR PDBsum; 4H36; -.
DR PDBsum; 4H39; -.
DR PDBsum; 4H3B; -.
DR ProteinModelPortal; P53779; -.
DR DIP; DIP-1015N; -.
DR IntAct; P53779; 11.
DR MINT; MINT-1373516; -.
DR STRING; 9606.ENSP00000352157; -.
DR PhosphoSite; P53779; -.
DR DMDM; 2507196; -.
DR PaxDb; P53779; -.
DR PRIDE; P53779; -.
DR DNASU; 5602; -.
DR Ensembl; ENST00000359221; ENSP00000352157; ENSG00000109339.
DR Ensembl; ENST00000361569; ENSP00000355297; ENSG00000109339.
DR Ensembl; ENST00000395160; ENSP00000378589; ENSG00000109339.
DR Ensembl; ENST00000395161; ENSP00000378590; ENSG00000109339.
DR Ensembl; ENST00000395166; ENSP00000378595; ENSG00000109339.
DR Ensembl; ENST00000395169; ENSP00000378598; ENSG00000109339.
DR GeneID; 5602; -.
DR KEGG; hsa:5602; -.
DR UCSC; uc003hpo.3; human.
DR UCSC; uc003hpt.3; human.
DR CTD; 5602; -.
DR GeneCards; GC04M086878; -.
DR H-InvDB; HIX0163985; -.
DR HGNC; HGNC:6872; MAPK10.
DR HPA; CAB022625; -.
DR MIM; 602897; gene.
DR MIM; 606369; phenotype.
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; KEVMNFE; -.
DR OrthoDB; EOG48SGT3; -.
DR BRENDA; 2.7.11.24; 2681.
DR Pathway_Interaction_DB; foxopathway; FoxO family signaling.
DR Pathway_Interaction_DB; p75ntrpathway; p75(NTR)-mediated signaling.
DR Reactome; REACT_6782; TRAF6 Mediated Induction of proinflammatory cytokines.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P53779; -.
DR BindingDB; P53779; -.
DR ChEMBL; CHEMBL2637; -.
DR ChiTaRS; MAPK10; human.
DR EvolutionaryTrace; P53779; -.
DR GenomeRNAi; 5602; -.
DR NextBio; 21762; -.
DR ArrayExpress; P53779; -.
DR Bgee; P53779; -.
DR CleanEx; HS_MAPK10; -.
DR Genevestigator; P53779; -.
DR GermOnline; ENSG00000109339; Homo sapiens.
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:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0002755; P:MyD88-dependent 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: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: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_cat_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; Kinase_like; 1.
DR PROSITE; PS01351; MAPK; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
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;
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 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 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
//
