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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.
12-AUG-2020, entry version 218.
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; DOI=10.1002/j.1460-2075.1996.tb00636.x;
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]
ACTIVITY 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 ACTIVITY 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]
FUNCTION, AND INTERACTION WITH JUND.
PubMed=22327296; DOI=10.1038/nature10806;
Huang J., Gurung B., Wan B., Matkar S., Veniaminova N.A., Wan K.,
Merchant J.L., Hua X., Lei M.;
"The same pocket in menin binds both MLL and JUND but has opposite effects
on transcription.";
Nature 482:542-546(2012).
[18]
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).
Phosphorylates JUND and this phosphorylation is inhibited in the
presence of MEN1 (PubMed:22327296). {ECO:0000269|PubMed:11718727,
ECO:0000269|PubMed:22327296, ECO:0000269|PubMed:22441692}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.24;
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:10715136};
-!- ACTIVITY 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). Interacts with
MAPK8IP1/JIP-1 and MAPK8IP3/JIP-3/JSAP1 (By similarity). Interacts with
SPAG9/MAPK8IP4/JIP4 (PubMed:15693750). Interacts with HDAC9
(PubMed:16611996). Interacts with ARRB2; the interaction enhances
MAPK10 activation by MAP3K5 (PubMed:18435604). Interacts with SARM1 (By
similarity). Interacts with JUND; interaction is inhibited in the
presence of MEN1 (PubMed:22327296). {ECO:0000250|UniProtKB:P49187,
ECO:0000250|UniProtKB:Q61831, ECO:0000269|PubMed:15693750,
ECO:0000269|PubMed:16611996, ECO:0000269|PubMed:18435604,
ECO:0000269|PubMed:22327296}.
-!- INTERACTION:
P53779; P49407: ARRB1; NbExp=2; IntAct=EBI-713543, EBI-743313;
P53779; P05412: JUN; NbExp=4; IntAct=EBI-713543, EBI-852823;
P53779; P17535: JUND; NbExp=2; IntAct=EBI-713543, EBI-2682803;
P53779; 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;
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=Truncated N-terminus.; 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.
RefSeq; XP_016863909.1; XM_017008420.1. [P53779-1]
RefSeq; XP_016863910.1; XM_017008421.1.
RefSeq; XP_016863912.1; XM_017008423.1. [P53779-3]
RefSeq; XP_016863913.1; XM_017008424.1.
RefSeq; XP_016863914.1; XM_017008425.1.
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.
RefSeq; XP_016863921.1; XM_017008432.1. [P53779-2]
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.
PDB; 6EKD; X-ray; 2.10 A; A=39-402.
PDB; 6EMH; X-ray; 1.76 A; A/B/C/D=39-402.
PDB; 6EQ9; X-ray; 1.83 A; A/B=39-402.
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; -.
PDBsum; 6EKD; -.
PDBsum; 6EMH; -.
PDBsum; 6EQ9; -.
SMR; P53779; -.
BioGRID; 111588; 53.
CORUM; P53779; -.
DIP; DIP-1015N; -.
ELM; P53779; -.
IntAct; P53779; 24.
MINT; P53779; -.
STRING; 9606.ENSP00000352157; -.
BindingDB; P53779; -.
ChEMBL; CHEMBL2637; -.
DrugBank; DB08011; (3E)-5-fluoro-1-[(6-fluoro-4H-1,3-benzodioxin-8-yl)methyl]-1H-indole-2,3-dione 3-oxime.
DrugBank; DB08010; (3Z)-1-[(6-fluoro-4H-1,3-benzodioxin-8-yl)methyl]-4-[(E)-2-phenylethenyl]-1H-indole-2,3-dione 3-oxime.
DrugBank; DB08015; (3Z)-1-[(6-fluoro-4H-1,3-benzodioxin-8-yl)methyl]-4-phenyl-1H-indole-2,3-dione 3-oxime.
DrugBank; DB08555; 1-(3-bromophenyl)-7-chloro-6-methoxy-3,4-dihydroisoquinoline.
DrugBank; DB08026; 2-{4-[(4-imidazo[1,2-a]pyridin-3-ylpyrimidin-2-yl)amino]piperidin-1-yl}-N-methylacetamide.
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; DB03623; 9-(4-Hydroxyphenyl)-2,7-Phenanthroline.
DrugBank; DB02388; Cyclohexyl-{4-[5-(3,4-Dichlorophenyl)-2-Piperidin-4-Yl-3-Propyl-3h-Imidazol-4-Yl]-Pyrimidin-2-Yl}Amine.
DrugBank; DB03084; Cyclopropyl-{4-[5-(3,4-Dichlorophenyl)-2-[(1-Methyl)-Piperidin]-4-Yl-3-Propyl-3h-Imidazol-4-Yl]-Pyrimidin-2-Yl}Amine.
DrugBank; DB12010; Fostamatinib.
DrugBank; DB15624; Halicin.
DrugBank; DB01017; Minocycline.
DrugBank; DB07217; N-(3-cyano-4,5,6,7-tetrahydro-1-benzothien-2-yl)-2-fluorobenzamide.
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; DB08023; N-cyclohexyl-4-imidazo[1,2-a]pyridin-3-yl-N-methylpyrimidin-2-amine.
DrugBank; DB08025; N-{2'-[(4-FLUOROPHENYL)AMINO]-4,4'-BIPYRIDIN-2-YL}-4-METHOXYCYCLOHEXANECARBOXAMIDE.
DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DrugBank; DB01782; Pyrazolanthrone.
DrugCentral; P53779; -.
GuidetoPHARMACOLOGY; 1498; -.
iPTMnet; P53779; -.
PhosphoSitePlus; P53779; -.
SwissPalm; P53779; -.
BioMuta; MAPK10; -.
DMDM; 2507196; -.
EPD; P53779; -.
jPOST; P53779; -.
MassIVE; P53779; -.
MaxQB; P53779; -.
PaxDb; P53779; -.
PeptideAtlas; P53779; -.
PRIDE; P53779; -.
ProteomicsDB; 56616; -. [P53779-1]
ProteomicsDB; 56617; -. [P53779-2]
ProteomicsDB; 56618; -. [P53779-3]
Antibodypedia; 14345; 532 antibodies.
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; -.
HGNC; HGNC:6872; MAPK10.
HPA; ENSG00000109339; Tissue enhanced (brain).
MalaCards; MAPK10; -.
MIM; 602897; gene.
neXtProt; NX_P53779; -.
OpenTargets; ENSG00000109339; -.
Orphanet; 2382; Lennox-Gastaut syndrome.
PharmGKB; PA30617; -.
eggNOG; KOG0665; Eukaryota.
GeneTree; ENSGT00940000153692; -.
HOGENOM; CLU_000288_181_1_1; -.
InParanoid; P53779; -.
KO; K04440; -.
OMA; REFKLMN; -.
OrthoDB; 741207at2759; -.
PhylomeDB; P53779; -.
TreeFam; TF105100; -.
BRENDA; 2.7.11.24; 2681.
PathwayCommons; P53779; -.
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; -.
BioGRID-ORCS; 5602; 5 hits in 903 CRISPR screens.
ChiTaRS; MAPK10; human.
EvolutionaryTrace; P53779; -.
GeneWiki; MAPK10; -.
GenomeRNAi; 5602; -.
Pharos; P53779; Tchem.
PRO; PR:P53779; -.
Proteomes; UP000005640; Chromosome 4.
RNAct; P53779; protein.
Bgee; ENSG00000109339; Expressed in frontal cortex and 198 other tissues.
ExpressionAtlas; P53779; baseline and differential.
Genevisible; P53779; HS.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0043204; C:perikaryon; IEA:Ensembl.
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:0004707; F:MAP kinase activity; IBA:GO_Central.
GO; GO:0004708; F:MAP kinase kinase activity; TAS:ProtInc.
GO; GO:0071474; P:cellular hyperosmotic response; IEA:Ensembl.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0007254; P:JNK cascade; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0098969; P:neurotransmitter receptor transport to postsynaptic membrane; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IMP:UniProtKB.
GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:0051090; P:regulation of DNA-binding transcription factor activity; TAS:Reactome.
GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
GO; GO:0009416; P:response to light stimulus; ISS:UniProtKB.
GO; GO:0009414; P:response to water deprivation; IEA:Ensembl.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0099003; P:vesicle-mediated transport in synapse; IEA:Ensembl.
DisProt; DP02328; -.
IDEAL; IID00456; -.
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; 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
/note="Mitogen-activated protein kinase 10"
/id="PRO_0000186277"
DOMAIN 64..359
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 70..78
/note="ATP"
MOTIF 221..223
/note="TXY"
ACT_SITE 189
/note="Proton acceptor"
BINDING 93
/note="ATP"
MOD_RES 221
/note="Phosphothreonine; by MAP2K7"
/evidence="ECO:0000269|PubMed:10715136"
MOD_RES 223
/note="Phosphotyrosine; by MAP2K4"
/evidence="ECO:0000269|PubMed:10715136"
LIPID 462
/note="S-palmitoyl cysteine"
/evidence="ECO:0000305|PubMed:21941371"
LIPID 463
/note="S-palmitoyl cysteine"
/evidence="ECO:0000305|PubMed:21941371"
VAR_SEQ 1..38
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_041911"
VAR_SEQ 418..464
/note="GAAVNSSESLPPSSSVNDISSMSTDQTLASDTDSSLEASAGPLGCCR -> A
QVQQ (in isoform Alpha-1)"
/evidence="ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:7826642, ECO:0000303|PubMed:8654373"
/id="VSP_004839"
MUTAGEN 462
/note="C->S: Loss of palmitoylation."
/evidence="ECO:0000269|PubMed:21941371"
MUTAGEN 463
/note="C->S: Loss of palmitoylation."
/evidence="ECO:0000269|PubMed:21941371"
CONFLICT 162
/note="D -> G (in Ref. 3; BAG51956)"
/evidence="ECO:0000305"
STRAND 48..53
/evidence="ECO:0000244|PDB:3OY1"
STRAND 56..61
/evidence="ECO:0000244|PDB:3OY1"
STRAND 64..69
/evidence="ECO:0000244|PDB:3OY1"
STRAND 77..83
/evidence="ECO:0000244|PDB:3OY1"
TURN 84..87
/evidence="ECO:0000244|PDB:3OY1"
STRAND 88..97
/evidence="ECO:0000244|PDB:3OY1"
HELIX 98..100
/evidence="ECO:0000244|PDB:3OY1"
HELIX 102..114
/evidence="ECO:0000244|PDB:3OY1"
TURN 115..117
/evidence="ECO:0000244|PDB:3OY1"
STRAND 121..123
/evidence="ECO:0000244|PDB:3KVX"
STRAND 127..130
/evidence="ECO:0000244|PDB:3OY1"
TURN 136..138
/evidence="ECO:0000244|PDB:3OY1"
STRAND 142..147
/evidence="ECO:0000244|PDB:3OY1"
STRAND 150..152
/evidence="ECO:0000244|PDB:3OY1"
HELIX 153..157
/evidence="ECO:0000244|PDB:3OY1"
HELIX 163..182
/evidence="ECO:0000244|PDB:3OY1"
HELIX 192..194
/evidence="ECO:0000244|PDB:3OY1"
STRAND 195..197
/evidence="ECO:0000244|PDB:3OY1"
STRAND 199..201
/evidence="ECO:0000244|PDB:3RTP"
STRAND 203..205
/evidence="ECO:0000244|PDB:3OY1"
STRAND 207..209
/evidence="ECO:0000244|PDB:3PTG"
HELIX 212..214
/evidence="ECO:0000244|PDB:6EMH"
HELIX 216..219
/evidence="ECO:0000244|PDB:4H3B"
STRAND 220..222
/evidence="ECO:0000244|PDB:4H3B"
HELIX 227..229
/evidence="ECO:0000244|PDB:4H3B"
HELIX 232..235
/evidence="ECO:0000244|PDB:3OY1"
HELIX 244..258
/evidence="ECO:0000244|PDB:3OY1"
HELIX 268..279
/evidence="ECO:0000244|PDB:3OY1"
HELIX 284..287
/evidence="ECO:0000244|PDB:3OY1"
HELIX 292..299
/evidence="ECO:0000244|PDB:3OY1"
HELIX 309..312
/evidence="ECO:0000244|PDB:3OY1"
HELIX 315..317
/evidence="ECO:0000244|PDB:3OY1"
HELIX 323..339
/evidence="ECO:0000244|PDB:3OY1"
TURN 344..346
/evidence="ECO:0000244|PDB:3OY1"
HELIX 350..355
/evidence="ECO:0000244|PDB:3OY1"
TURN 357..361
/evidence="ECO:0000244|PDB:3OY1"
HELIX 365..368
/evidence="ECO:0000244|PDB:3OY1"
TURN 378..382
/evidence="ECO:0000244|PDB:6EMH"
HELIX 387..399
/evidence="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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EIAAB24856 c-Jun N-terminal kinase 1,Jnk1,MAP kinase 8,MAPK 8,Mapk8,Mitogen-activated protein kinase 8,Mouse,Mus musculus,Prkm8,Stress-activated protein kinase JNK1
EIAAB24872 MAP kinase 13,MAP kinase p38 delta,MAPK 13,Mapk13,Mitogen-activated protein kinase 13,Mitogen-activated protein kinase p38 delta,Mouse,Mus musculus,Serk4,Stress-activated protein kinase 4
EIAAB24869 MAP kinase 13,MAP kinase p38 delta,MAPK 13,Mapk13,Mitogen-activated protein kinase 13,Mitogen-activated protein kinase p38 delta,Rat,Rattus norvegicus,Stress-activated protein kinase 4
EIAAB24854 c-Jun N-terminal kinase 1,Jnk1,MAP kinase 8,MAPK 8,Mapk8,Mitogen-activated protein kinase 8,p54 gamma,Prkm8,Rat,Rattus norvegicus,SAPK gamma,Stress-activated protein kinase JNK1
EIAAB24858 c-Jun N-terminal kinase 2,Jnk2,MAP kinase 9,MAPK 9,Mapk9,Mitogen-activated protein kinase 9,p54-alpha,Prkm9,Rat,Rattus norvegicus,SAPK-alpha,Stress-activated protein kinase JNK2
10-782-55059 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.001 mg
10-782-55060 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.05 mg
10-782-55060 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.02 mg
10-782-55059 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.02 mg
10-782-55059 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.01 mg
10-782-55059 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.005 mg
EIAAB24859 Chicken,c-Jun N-terminal kinase 2,Gallus gallus,JNK2,MAP kinase 9,MAPK 9,MAPK9,Mitogen-activated protein kinase 9,Stress-activated protein kinase JNK2
U1206b CLIA Bos taurus,Bovine,ERK2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAPK 1,MAPK 2,MAPK1,Mitogen-activated protein kinase 1,Mitogen-activated protein kinase 2,PRKM1 96T
E1206b ELISA Bos taurus,Bovine,ERK2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAPK 1,MAPK 2,MAPK1,Mitogen-activated protein kinase 1,Mitogen-activated protein kinase 2,PRKM 96T
E1206m ELISA kit Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protei 96T
E1206r ELISA kit Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protei 96T
U1206r CLIA Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protein kina 96T