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Mitogen-activated protein kinase 10 (MAP kinase 10) (MAPK 10) (EC 2.7.11.24) (MAP kinase p49 3F12) (Stress-activated protein kinase 1b) (SAPK1b) (Stress-activated protein kinase JNK3) (c-Jun N-terminal kinase 3)

 MK10_HUMAN              Reviewed;         464 AA.
P53779; A6NFS3; A6NG28; B3KQ94; Q15707; Q49AP1;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
22-NOV-2017, entry version 196.
RecName: Full=Mitogen-activated protein kinase 10;
Short=MAP kinase 10;
Short=MAPK 10;
EC=2.7.11.24;
AltName: Full=MAP kinase p49 3F12;
AltName: Full=Stress-activated protein kinase 1b;
Short=SAPK1b;
AltName: Full=Stress-activated protein kinase JNK3;
AltName: Full=c-Jun N-terminal kinase 3;
Name=MAPK10; Synonyms=JNK3, JNK3A, PRKM10, SAPK1B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1).
TISSUE=Hippocampus;
PubMed=7826642; DOI=10.1016/0896-6273(95)90241-4;
Mohit A.A., Martin J.H., Miller C.A.;
"p493F12 kinase: a novel MAP kinase expressed in a subset of neurons
in the human nervous system.";
Neuron 14:67-78(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-1 AND ALPHA-2).
TISSUE=Brain;
PubMed=8654373;
Gupta S., Barrett T., Whitmarsh A.J., Cavanagh J., Sluss H.K.,
Derijard B., Davis R.J.;
"Selective interaction of JNK protein kinase isoforms with
transcription factors.";
EMBO J. 15:2760-2770(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 143-464 (ISOFORM ALPHA-1).
TISSUE=Caudate nucleus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-2).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PARTIAL PROTEIN SEQUENCE, REGULATION BY MAP2K4 AND MAP2K7,
PHOSPHORYLATION AT THR-221 AND TYR-223, COFACTOR, AND MASS
SPECTROMETRY.
PubMed=10715136; DOI=10.1021/bi992410+;
Lisnock J., Griffin P., Calaycay J., Frantz B., Parsons J.,
O'Keefe S.J., LoGrasso P.;
"Activation of JNK3 alpha 1 requires both MKK4 and MKK7: kinetic
characterization of in vitro phosphorylated JNK3 alpha 1.";
Biochemistry 39:3141-3148(2000).
[8]
ENZYME REGULATION.
PubMed=11062067; DOI=10.1042/bj3520145;
Fleming Y., Armstrong C.G., Morrice N., Paterson A., Goedert M.,
Cohen P.;
"Synergistic activation of stress-activated protein kinase 1/c-Jun N-
terminal kinase (SAPK1/JNK) isoforms by mitogen-activated protein
kinase kinase 4 (MKK4) and MKK7.";
Biochem. J. 352:145-154(2000).
[9]
FUNCTION IN PHOSPHORYLATION OF STMN2.
PubMed=11718727; DOI=10.1016/S0014-5793(01)03090-3;
Neidhart S., Antonsson B., Gillieron C., Vilbois F., Grenningloh G.,
Arkinstall S.;
"c-Jun N-terminal kinase-3 (JNK3)/stress-activated protein kinase-beta
(SAPKbeta) binds and phosphorylates the neuronal microtubule regulator
SCG10.";
FEBS Lett. 508:259-264(2001).
[10]
INTERACTION WITH SPAG9.
PubMed=15693750; DOI=10.1042/BJ20041577;
Jagadish N., Rana R., Selvi R., Mishra D., Garg M., Yadav S.,
Herr J.C., Okumura K., Hasegawa A., Koyama K., Suri A.;
"Characterization of a novel human sperm-associated antigen 9 (SPAG9)
having structural homology with c-Jun N-terminal kinase-interacting
protein.";
Biochem. J. 389:73-82(2005).
[11]
CHROMOSOMAL REARRANGEMENT, AND DISEASE.
PubMed=16249883; DOI=10.1007/s00439-005-0084-y;
Shoichet S.A., Duprez L., Hagens O., Waetzig V., Menzel C.,
Herdegen T., Schweiger S., Dan B., Vamos E., Ropers H.-H.,
Kalscheuer V.M.;
"Truncation of the CNS-expressed JNK3 in a patient with a severe
developmental epileptic encephalopathy.";
Hum. Genet. 118:559-567(2006).
[12]
SUBCELLULAR LOCATION.
PubMed=16737965; DOI=10.1074/jbc.M603659200;
Song X., Raman D., Gurevich E.V., Vishnivetskiy S.A., Gurevich V.V.;
"Visual and both non-visual arrestins in their 'inactive' conformation
bind JNK3 and Mdm2 and relocalize them from the nucleus to the
cytoplasm.";
J. Biol. Chem. 281:21491-21499(2006).
[13]
INTERACTION WITH HDAC9, AND ENZYME REGULATION.
PubMed=16611996; DOI=10.1128/MCB.26.9.3550-3564.2006;
Morrison B.E., Majdzadeh N., Zhang X., Lyles A., Bassel-Duby R.,
Olson E.N., D'Mello S.R.;
"Neuroprotection by histone deacetylase-related protein.";
Mol. Cell. Biol. 26:3550-3564(2006).
[14]
INTERACTION WITH ARRB2.
PubMed=18435604; DOI=10.1042/BJ20080685;
Xu T.-R., Baillie G.S., Bhari N., Houslay T.M., Pitt A.M., Adams D.R.,
Kolch W., Houslay M.D., Milligan G.;
"Mutations of beta-arrestin 2 that limit self-association also
interfere with interactions with the beta2-adrenoceptor and the ERK1/2
MAPKs: implications for beta2-adrenoceptor signalling via the ERK1/2
MAPKs.";
Biochem. J. 413:51-60(2008).
[15]
PALMITOYLATION AT CYS-462 AND CYS-463, AND MUTAGENESIS OF CYS-462 AND
CYS-463.
PubMed=21941371; DOI=10.1038/cdd.2011.124;
Yang G., Liu Y., Yang K., Liu R., Zhu S., Coquinco A., Wen W.,
Kojic L., Jia W., Cynader M.;
"Isoform-specific palmitoylation of JNK regulates axonal
development.";
Cell Death Differ. 19:553-561(2012).
[16]
FUNCTION.
PubMed=22441692; DOI=10.1038/embor.2012.37;
Yoshitane H., Honma S., Imamura K., Nakajima H., Nishide S.Y., Ono D.,
Kiyota H., Shinozaki N., Matsuki H., Wada N., Doi H., Hamada T.,
Honma K., Fukada Y.;
"JNK regulates the photic response of the mammalian circadian clock.";
EMBO Rep. 13:455-461(2012).
[17]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 40-402.
PubMed=9739089; DOI=10.1016/S0969-2126(98)00100-2;
Xie X., Gu Y., Fox T., Coll J.T., Fleming M.A., Markland W.,
Caron P.R., Wilson K.P., Su M.S.-S.;
"Crystal structure of JNK3: a kinase implicated in neuronal
apoptosis.";
Structure 6:983-991(1998).
-!- FUNCTION: Serine/threonine-protein kinase involved in various
processes such as neuronal proliferation, differentiation,
migration and programmed cell death. Extracellular stimuli such as
proinflammatory cytokines or physical stress stimulate the stress-
activated protein kinase/c-Jun N-terminal kinase (SAP/JNK)
signaling pathway. In this cascade, two dual specificity kinases
MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate
MAPK10/JNK3. In turn, MAPK10/JNK3 phosphorylates a number of
transcription factors, primarily components of AP-1 such as JUN
and ATF2 and thus regulates AP-1 transcriptional activity. Plays
regulatory roles in the signaling pathways during neuronal
apoptosis. Phosphorylates the neuronal microtubule regulator
STMN2. Acts in the regulation of the amyloid-beta precursor
protein/APP signaling during neuronal differentiation by
phosphorylating APP. Participates also in neurite growth in spiral
ganglion neurons. Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer
and plays a role in the photic regulation of the circadian clock
(PubMed:22441692). {ECO:0000269|PubMed:11718727,
ECO:0000269|PubMed:22441692}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:10715136};
-!- ENZYME REGULATION: Activated by threonine and tyrosine
phosphorylation by two dual specificity kinases, MAP2K4 and
MAP2K7. MAP2K7 phosphorylates MAPK10 on Thr-221 causing a
conformational change and a large increase in Vmax. MAP2K4 then
phosphorylates Tyr-223 resulting in a further increase in Vmax.
Inhibited by dual specificity phosphatases, such as DUSP1.
Inhibited by HDAC9. {ECO:0000269|PubMed:11062067,
ECO:0000269|PubMed:16611996}.
-!- SUBUNIT: Interacts with MAPKBP1 (By similarity). Binds to at least
four scaffolding proteins, MAPK8IP1/JIP-1, MAPK8IP2/JIP-2,
MAPK8IP3/JIP-3/JSAP1 and SPAG9/MAPK8IP4/JIP-4. These proteins also
bind other components of the JNK signaling pathway. Interacts with
HDAC9. Interacts with ARRB2; the interaction enhances MAPK10
activation by MAP3K5. Interacts with SARM1 (By similarity).
{ECO:0000250}.
-!- INTERACTION:
P49407:ARRB1; NbExp=2; IntAct=EBI-713543, EBI-743313;
P05412:JUN; NbExp=4; IntAct=EBI-713543, EBI-852823;
P17535:JUND; NbExp=2; IntAct=EBI-713543, EBI-2682803;
Q04206:RELA; NbExp=2; IntAct=EBI-713543, EBI-73886;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16737965}.
Membrane {ECO:0000269|PubMed:16737965}; Lipid-anchor
{ECO:0000269|PubMed:16737965}. Nucleus
{ECO:0000269|PubMed:16737965}. Mitochondrion
{ECO:0000269|PubMed:16737965}. Note=Palmitoylation regulates
MAPK10 trafficking to cytoskeleton. Recruited to the mitochondria
in the presence of SARM1 (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=A similar low level of binding to substrates is observed
for isoform alpha-1 and isoform alpha-2. However, there is no
correlation between binding and phosphorylation, which is
achieved about at the same efficiency by all isoforms.;
Name=Alpha-2;
IsoId=P53779-1; Sequence=Displayed;
Name=Alpha-1;
IsoId=P53779-2; Sequence=VSP_004839;
Name=3;
IsoId=P53779-3; Sequence=VSP_041911;
-!- TISSUE SPECIFICITY: Specific to a subset of neurons in the nervous
system. Present in the hippocampus and areas, cerebellum,
striatum, brain stem, and weakly in the spinal cord. Very weak
expression in testis and kidney.
-!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
whose phosphorylation activates the MAP kinases.
-!- PTM: Dually phosphorylated on Thr-221 and Tyr-223 by MAP2K4 and
MAP2K7, which activates the enzyme. MAP2K7 shows a strong
preference for Thr-221 while MAP2K4 phosphorylates Tyr-223
preferentially. Weakly autophosphorylated on threonine and
tyrosine residues in vitro. {ECO:0000269|PubMed:10715136}.
-!- PTM: Palmitoylation regulates subcellular location and axonal
development. {ECO:0000269|PubMed:21941371}.
-!- MASS SPECTROMETRY: Mass=44070; Method=Electrospray; Range=1-464;
Evidence={ECO:0000269|PubMed:10715136};
-!- DISEASE: Note=A chromosomal aberration involving MAPK10 has been
found in a single patient with pharmacoresistant epileptic
encephalopathy. Translocation t(Y;4)(q11.2;q21) which causes
MAPK10 truncation. {ECO:0000269|PubMed:16249883}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. MAP kinase subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAG51956.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/JNK3ID427.html";
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EMBL; U07620; AAC50101.1; -; mRNA.
EMBL; U34819; AAC50604.1; -; mRNA.
EMBL; U34820; AAC50605.1; -; mRNA.
EMBL; AK057723; BAG51956.1; ALT_INIT; mRNA.
EMBL; AK124791; BAG54096.1; -; mRNA.
EMBL; AC096953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC104059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC104827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC108054; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC110076; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471057; EAX05963.1; -; Genomic_DNA.
EMBL; BC035057; AAH35057.1; -; mRNA.
CCDS; CCDS34026.1; -. [P53779-1]
CCDS; CCDS3612.1; -. [P53779-3]
CCDS; CCDS43247.1; -. [P53779-2]
PIR; S71104; S71104.
RefSeq; NP_001304996.1; NM_001318067.1.
RefSeq; NP_001304997.1; NM_001318068.1.
RefSeq; NP_001304998.1; NM_001318069.1.
RefSeq; NP_002744.1; NM_002753.4. [P53779-2]
RefSeq; NP_620446.1; NM_138980.3. [P53779-3]
RefSeq; NP_620448.1; NM_138982.3. [P53779-1]
RefSeq; XP_005263186.1; XM_005263129.2. [P53779-1]
RefSeq; XP_005263187.1; XM_005263130.2. [P53779-1]
RefSeq; XP_005263192.1; XM_005263135.3. [P53779-2]
RefSeq; XP_006714331.1; XM_006714268.2. [P53779-3]
RefSeq; XP_011530419.1; XM_011532117.2. [P53779-1]
RefSeq; XP_011530420.1; XM_011532118.2. [P53779-1]
RefSeq; XP_011530422.1; XM_011532120.2. [P53779-3]
RefSeq; XP_011530423.1; XM_011532121.2. [P53779-3]
RefSeq; XP_016863908.1; XM_017008419.1. [P53779-1]
RefSeq; XP_016863909.1; XM_017008420.1. [P53779-1]
RefSeq; XP_016863910.1; XM_017008421.1. [P53779-1]
RefSeq; XP_016863912.1; XM_017008423.1. [P53779-3]
RefSeq; XP_016863913.1; XM_017008424.1. [P53779-3]
RefSeq; XP_016863914.1; XM_017008425.1. [P53779-3]
RefSeq; XP_016863915.1; XM_017008426.1.
RefSeq; XP_016863918.1; XM_017008429.1. [P53779-2]
RefSeq; XP_016863919.1; XM_017008430.1. [P53779-2]
RefSeq; XP_016863920.1; XM_017008431.1. [P53779-2]
RefSeq; XP_016863921.1; XM_017008432.1. [P53779-2]
UniGene; Hs.125503; -.
UniGene; Hs.13438; -.
PDB; 1JNK; X-ray; 2.30 A; A=1-423.
PDB; 1PMN; X-ray; 2.20 A; A=40-401.
PDB; 1PMU; X-ray; 2.70 A; A=40-401.
PDB; 1PMV; X-ray; 2.50 A; A=40-401.
PDB; 2B1P; X-ray; 1.90 A; A=46-400.
PDB; 2EXC; X-ray; 2.75 A; X=45-400.
PDB; 2O0U; X-ray; 2.10 A; A=39-402.
PDB; 2O2U; X-ray; 2.45 A; A=39-402.
PDB; 2OK1; X-ray; 2.40 A; A=40-402.
PDB; 2P33; X-ray; 2.40 A; A=40-402.
PDB; 2R9S; X-ray; 2.40 A; A/B=46-401.
PDB; 2WAJ; X-ray; 2.40 A; A=39-402.
PDB; 2ZDT; X-ray; 2.00 A; A=39-402.
PDB; 2ZDU; X-ray; 2.50 A; A=39-402.
PDB; 3CGF; X-ray; 3.00 A; A=40-402.
PDB; 3CGO; X-ray; 3.00 A; A=40-402.
PDB; 3DA6; X-ray; 2.00 A; A=39-402.
PDB; 3FI2; X-ray; 2.28 A; A=39-402.
PDB; 3FI3; X-ray; 2.20 A; A=39-402.
PDB; 3FV8; X-ray; 2.28 A; A=39-402.
PDB; 3G90; X-ray; 2.40 A; X=40-402.
PDB; 3G9L; X-ray; 2.20 A; X=40-402.
PDB; 3G9N; X-ray; 2.80 A; A=40-402.
PDB; 3KVX; X-ray; 2.40 A; A=39-402.
PDB; 3OXI; X-ray; 2.20 A; A=40-401.
PDB; 3OY1; X-ray; 1.70 A; A=40-401.
PDB; 3PTG; X-ray; 2.43 A; A=40-401.
PDB; 3RTP; X-ray; 2.40 A; A=40-401.
PDB; 3TTI; X-ray; 2.20 A; A=1-464.
PDB; 3TTJ; X-ray; 2.10 A; A=1-464.
PDB; 3V6R; X-ray; 2.60 A; A/B=39-402.
PDB; 3V6S; X-ray; 2.97 A; A/B=39-402.
PDB; 4H36; X-ray; 3.00 A; A=45-400.
PDB; 4H39; X-ray; 1.99 A; A=45-400.
PDB; 4H3B; X-ray; 2.08 A; A/C=45-400.
PDB; 4KKE; X-ray; 2.20 A; A=40-402.
PDB; 4KKG; X-ray; 2.40 A; A=40-402.
PDB; 4KKH; X-ray; 2.00 A; A=40-402.
PDB; 4U79; X-ray; 2.23 A; A=39-402.
PDB; 4W4V; X-ray; 2.01 A; A=39-402.
PDB; 4W4W; X-ray; 1.90 A; A=39-402.
PDB; 4W4X; X-ray; 2.65 A; A=39-402.
PDB; 4W4Y; X-ray; 2.30 A; A=39-402.
PDB; 4WHZ; X-ray; 1.79 A; A=39-423.
PDB; 4X21; X-ray; 1.95 A; A/B=39-402.
PDB; 4Y46; X-ray; 2.04 A; A=39-402.
PDB; 4Y5H; X-ray; 2.06 A; A=39-402.
PDB; 4Z9L; X-ray; 2.10 A; A=40-401.
PDBsum; 1JNK; -.
PDBsum; 1PMN; -.
PDBsum; 1PMU; -.
PDBsum; 1PMV; -.
PDBsum; 2B1P; -.
PDBsum; 2EXC; -.
PDBsum; 2O0U; -.
PDBsum; 2O2U; -.
PDBsum; 2OK1; -.
PDBsum; 2P33; -.
PDBsum; 2R9S; -.
PDBsum; 2WAJ; -.
PDBsum; 2ZDT; -.
PDBsum; 2ZDU; -.
PDBsum; 3CGF; -.
PDBsum; 3CGO; -.
PDBsum; 3DA6; -.
PDBsum; 3FI2; -.
PDBsum; 3FI3; -.
PDBsum; 3FV8; -.
PDBsum; 3G90; -.
PDBsum; 3G9L; -.
PDBsum; 3G9N; -.
PDBsum; 3KVX; -.
PDBsum; 3OXI; -.
PDBsum; 3OY1; -.
PDBsum; 3PTG; -.
PDBsum; 3RTP; -.
PDBsum; 3TTI; -.
PDBsum; 3TTJ; -.
PDBsum; 3V6R; -.
PDBsum; 3V6S; -.
PDBsum; 4H36; -.
PDBsum; 4H39; -.
PDBsum; 4H3B; -.
PDBsum; 4KKE; -.
PDBsum; 4KKG; -.
PDBsum; 4KKH; -.
PDBsum; 4U79; -.
PDBsum; 4W4V; -.
PDBsum; 4W4W; -.
PDBsum; 4W4X; -.
PDBsum; 4W4Y; -.
PDBsum; 4WHZ; -.
PDBsum; 4X21; -.
PDBsum; 4Y46; -.
PDBsum; 4Y5H; -.
PDBsum; 4Z9L; -.
ProteinModelPortal; P53779; -.
SMR; P53779; -.
BioGrid; 111588; 48.
CORUM; P53779; -.
DIP; DIP-1015N; -.
ELM; P53779; -.
IntAct; P53779; 19.
MINT; MINT-1373516; -.
STRING; 9606.ENSP00000352157; -.
BindingDB; P53779; -.
ChEMBL; CHEMBL2637; -.
DrugBank; DB08005; 4-{[5-chloro-4-(1H-indol-3-yl)pyrimidin-2-yl]amino}-N-ethylpiperidine-1-carboxamide.
DrugBank; DB08021; 5-bromo-N-(3-chloro-2-(4-(prop-2-ynyl)piperazin-1-yl)phenyl)furan-2-carboxamide.
DrugBank; DB06933; N-(tert-butyl)-4-[5-(pyridin-2-ylamino)quinolin-3-yl]benzenesulfonamide.
DrugBank; DB07010; N-BENZYL-4-[4-(3-CHLOROPHENYL)-1H-PYRAZOL-3-YL]-1H-PYRROLE-2-CARBOXAMIDE.
DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
GuidetoPHARMACOLOGY; 1498; -.
iPTMnet; P53779; -.
PhosphoSitePlus; P53779; -.
SwissPalm; P53779; -.
BioMuta; MAPK10; -.
DMDM; 2507196; -.
EPD; P53779; -.
MaxQB; P53779; -.
PaxDb; P53779; -.
PeptideAtlas; P53779; -.
PRIDE; P53779; -.
DNASU; 5602; -.
Ensembl; ENST00000395157; ENSP00000378586; ENSG00000109339. [P53779-2]
Ensembl; ENST00000395166; ENSP00000378595; ENSG00000109339. [P53779-3]
Ensembl; ENST00000515400; ENSP00000424154; ENSG00000109339. [P53779-1]
Ensembl; ENST00000515650; ENSP00000492204; ENSG00000109339. [P53779-1]
Ensembl; ENST00000638225; ENSP00000491866; ENSG00000109339. [P53779-3]
Ensembl; ENST00000638313; ENSP00000492292; ENSG00000109339. [P53779-1]
Ensembl; ENST00000639175; ENSP00000491160; ENSG00000109339. [P53779-3]
Ensembl; ENST00000639234; ENSP00000491306; ENSG00000109339. [P53779-2]
Ensembl; ENST00000639242; ENSP00000491089; ENSG00000109339. [P53779-3]
Ensembl; ENST00000640858; ENSP00000491122; ENSG00000109339. [P53779-2]
Ensembl; ENST00000640970; ENSP00000492231; ENSG00000109339. [P53779-2]
Ensembl; ENST00000641050; ENSP00000493270; ENSG00000109339. [P53779-2]
Ensembl; ENST00000641051; ENSP00000493275; ENSG00000109339. [P53779-1]
Ensembl; ENST00000641066; ENSP00000493072; ENSG00000109339. [P53779-1]
Ensembl; ENST00000641110; ENSP00000493163; ENSG00000109339. [P53779-3]
Ensembl; ENST00000641157; ENSP00000493363; ENSG00000109339. [P53779-1]
Ensembl; ENST00000641170; ENSP00000493237; ENSG00000109339. [P53779-2]
Ensembl; ENST00000641207; ENSP00000493450; ENSG00000109339. [P53779-1]
Ensembl; ENST00000641274; ENSP00000492929; ENSG00000109339. [P53779-2]
Ensembl; ENST00000641283; ENSP00000493444; ENSG00000109339. [P53779-3]
Ensembl; ENST00000641287; ENSP00000493100; ENSG00000109339. [P53779-3]
Ensembl; ENST00000641297; ENSP00000493092; ENSG00000109339. [P53779-3]
Ensembl; ENST00000641341; ENSP00000493290; ENSG00000109339. [P53779-1]
Ensembl; ENST00000641391; ENSP00000493008; ENSG00000109339. [P53779-3]
Ensembl; ENST00000641410; ENSP00000493208; ENSG00000109339. [P53779-2]
Ensembl; ENST00000641462; ENSP00000493435; ENSG00000109339. [P53779-1]
Ensembl; ENST00000641647; ENSP00000493375; ENSG00000109339. [P53779-1]
Ensembl; ENST00000641657; ENSP00000493105; ENSG00000109339. [P53779-3]
Ensembl; ENST00000641724; ENSP00000493038; ENSG00000109339. [P53779-3]
Ensembl; ENST00000641737; ENSP00000493177; ENSG00000109339. [P53779-3]
Ensembl; ENST00000641803; ENSP00000493049; ENSG00000109339. [P53779-3]
Ensembl; ENST00000641823; ENSP00000493408; ENSG00000109339. [P53779-1]
Ensembl; ENST00000641862; ENSP00000493396; ENSG00000109339. [P53779-2]
Ensembl; ENST00000641902; ENSP00000492903; ENSG00000109339. [P53779-1]
Ensembl; ENST00000641911; ENSP00000493374; ENSG00000109339. [P53779-3]
Ensembl; ENST00000641943; ENSP00000492941; ENSG00000109339. [P53779-3]
Ensembl; ENST00000641952; ENSP00000493013; ENSG00000109339. [P53779-1]
Ensembl; ENST00000641983; ENSP00000493045; ENSG00000109339. [P53779-1]
Ensembl; ENST00000642009; ENSP00000493168; ENSG00000109339. [P53779-3]
Ensembl; ENST00000642015; ENSP00000493040; ENSG00000109339. [P53779-3]
Ensembl; ENST00000642038; ENSP00000492942; ENSG00000109339. [P53779-2]
Ensembl; ENST00000642103; ENSP00000493001; ENSG00000109339. [P53779-3]
GeneID; 5602; -.
KEGG; hsa:5602; -.
UCSC; uc003hpp.4; human. [P53779-1]
CTD; 5602; -.
DisGeNET; 5602; -.
EuPathDB; HostDB:ENSG00000109339.18; -.
GeneCards; MAPK10; -.
H-InvDB; HIX0163985; -.
HGNC; HGNC:6872; MAPK10.
HPA; CAB022625; -.
HPA; HPA060304; -.
MalaCards; MAPK10; -.
MIM; 602897; gene.
neXtProt; NX_P53779; -.
OpenTargets; ENSG00000109339; -.
Orphanet; 2382; Lennox-Gastaut syndrome.
PharmGKB; PA30617; -.
eggNOG; KOG0665; Eukaryota.
eggNOG; ENOG410XSHI; LUCA.
GeneTree; ENSGT00550000074271; -.
HOGENOM; HOG000233024; -.
HOVERGEN; HBG014652; -.
InParanoid; P53779; -.
KO; K04440; -.
OMA; DCLFPAD; -.
OrthoDB; EOG091G09G2; -.
PhylomeDB; P53779; -.
TreeFam; TF105100; -.
BRENDA; 2.7.11.24; 2681.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
Reactome; R-HSA-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
Reactome; R-HSA-450341; Activation of the AP-1 family of transcription factors.
SignaLink; P53779; -.
SIGNOR; P53779; -.
ChiTaRS; MAPK10; human.
EvolutionaryTrace; P53779; -.
GeneWiki; MAPK10; -.
GenomeRNAi; 5602; -.
PRO; PR:P53779; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000109339; -.
CleanEx; HS_MAPK10; -.
ExpressionAtlas; P53779; baseline and differential.
Genevisible; P53779; HS.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0043005; C:neuron projection; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004705; F:JUN kinase activity; ISS:UniProtKB.
GO; GO:0004708; F:MAP kinase kinase activity; TAS:ProtInc.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0007254; P:JNK cascade; ISS:UniProtKB.
GO; GO:0048666; P:neuron development; IBA:GO_Central.
GO; GO:0006468; P:protein phosphorylation; IMP:UniProtKB.
GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
GO; GO:0051090; P:regulation of sequence-specific DNA binding transcription factor activity; TAS:Reactome.
GO; GO:0009416; P:response to light stimulus; ISS:UniProtKB.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR003527; MAP_kinase_CS.
InterPro; IPR008351; MAPK_JNK.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
PRINTS; PR01772; JNKMAPKINASE.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS01351; MAPK; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Biological rhythms;
Chromosomal rearrangement; Complete proteome; Cytoplasm;
Direct protein sequencing; Epilepsy; Kinase; Lipoprotein; Membrane;
Mental retardation; Mitochondrion; Nucleotide-binding; Nucleus;
Palmitate; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 464 Mitogen-activated protein kinase 10.
/FTId=PRO_0000186277.
DOMAIN 64 359 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 70 78 ATP.
MOTIF 221 223 TXY.
ACT_SITE 189 189 Proton acceptor.
BINDING 93 93 ATP.
MOD_RES 221 221 Phosphothreonine; by MAP2K7.
{ECO:0000269|PubMed:10715136}.
MOD_RES 223 223 Phosphotyrosine; by MAP2K4.
{ECO:0000269|PubMed:10715136}.
LIPID 462 462 S-palmitoyl cysteine.
{ECO:0000305|PubMed:21941371}.
LIPID 463 463 S-palmitoyl cysteine.
{ECO:0000305|PubMed:21941371}.
VAR_SEQ 1 38 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041911.
VAR_SEQ 418 464 GAAVNSSESLPPSSSVNDISSMSTDQTLASDTDSSLEASAG
PLGCCR -> AQVQQ (in isoform Alpha-1).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:7826642,
ECO:0000303|PubMed:8654373}.
/FTId=VSP_004839.
MUTAGEN 462 462 C->S: Loss of palmitoylation.
{ECO:0000269|PubMed:21941371}.
MUTAGEN 463 463 C->S: Loss of palmitoylation.
{ECO:0000269|PubMed:21941371}.
CONFLICT 162 162 D -> G (in Ref. 3; BAG51956).
{ECO:0000305}.
STRAND 48 53 {ECO:0000244|PDB:3OY1}.
STRAND 56 61 {ECO:0000244|PDB:3OY1}.
STRAND 64 69 {ECO:0000244|PDB:3OY1}.
STRAND 77 83 {ECO:0000244|PDB:3OY1}.
TURN 84 87 {ECO:0000244|PDB:3OY1}.
STRAND 88 97 {ECO:0000244|PDB:3OY1}.
HELIX 98 100 {ECO:0000244|PDB:3OY1}.
HELIX 102 114 {ECO:0000244|PDB:3OY1}.
TURN 115 117 {ECO:0000244|PDB:3OY1}.
STRAND 121 123 {ECO:0000244|PDB:3KVX}.
STRAND 127 130 {ECO:0000244|PDB:3OY1}.
TURN 136 138 {ECO:0000244|PDB:3OY1}.
STRAND 142 147 {ECO:0000244|PDB:3OY1}.
STRAND 150 152 {ECO:0000244|PDB:3OY1}.
HELIX 153 157 {ECO:0000244|PDB:3OY1}.
HELIX 163 182 {ECO:0000244|PDB:3OY1}.
HELIX 192 194 {ECO:0000244|PDB:3OY1}.
STRAND 195 197 {ECO:0000244|PDB:3OY1}.
STRAND 199 201 {ECO:0000244|PDB:3RTP}.
STRAND 203 205 {ECO:0000244|PDB:3OY1}.
STRAND 207 209 {ECO:0000244|PDB:3PTG}.
TURN 212 214 {ECO:0000244|PDB:4H36}.
HELIX 216 219 {ECO:0000244|PDB:4H3B}.
STRAND 220 222 {ECO:0000244|PDB:4H3B}.
HELIX 227 229 {ECO:0000244|PDB:4H3B}.
HELIX 232 235 {ECO:0000244|PDB:3OY1}.
HELIX 244 258 {ECO:0000244|PDB:3OY1}.
HELIX 268 279 {ECO:0000244|PDB:3OY1}.
HELIX 284 287 {ECO:0000244|PDB:3OY1}.
HELIX 292 299 {ECO:0000244|PDB:3OY1}.
HELIX 309 312 {ECO:0000244|PDB:3OY1}.
HELIX 315 317 {ECO:0000244|PDB:3OY1}.
HELIX 323 339 {ECO:0000244|PDB:3OY1}.
TURN 344 346 {ECO:0000244|PDB:3OY1}.
HELIX 350 355 {ECO:0000244|PDB:3OY1}.
TURN 357 361 {ECO:0000244|PDB:3OY1}.
HELIX 365 368 {ECO:0000244|PDB:3OY1}.
HELIX 378 382 {ECO:0000244|PDB:4H39}.
HELIX 387 399 {ECO:0000244|PDB:3OY1}.
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


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