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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 JNK3) (c-Jun N-terminal kinase 3)

 MK10_MOUSE              Reviewed;         464 AA.
Q61831; Q9R0U6;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
25-OCT-2017, entry version 164.
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 JNK3;
AltName: Full=c-Jun N-terminal kinase 3;
Name=Mapk10; Synonyms=Jnk3, Prkm10, Serk2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=8717339; DOI=10.1016/0169-328X(95)00181-Q;
Martin J.H., Mohit A.A., Miller C.A.;
"Developmental expression in the mouse nervous system of the p493F12
SAP kinase.";
Brain Res. Mol. Brain Res. 35:47-57(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 39-464.
TISSUE=Brain;
PubMed=10523642; DOI=10.1128/MCB.19.11.7539;
Ito M., Yoshioka K., Akechi M., Yamashita S., Takamatsu N.,
Sugiyama K., Hibi M., Nakabeppu Y., Shiba T., Yamamoto K.;
"JSAP1, a novel jun N-terminal protein kinase (JNK)-binding protein
that functions as a scaffold factor in the JNK signaling pathway.";
Mol. Cell. Biol. 19:7539-7548(1999).
[3]
IDENTIFICATION OF LONG FORM (ALPHA-2).
Hulo-Demole C., Braconi-Quintaje S.;
Unpublished observations (MAR-1997).
[4]
FUNCTION, AND COFACTOR.
TISSUE=Hippocampus;
PubMed=9349820; DOI=10.1038/39899;
Yang D.D., Kuan C.-Y., Whitmarsh A.J., Rincon M., Zheng T.S.,
Davis R.J., Rakic P., Flavell R.A.;
"Absence of excitotoxicity-induced apoptosis in the hippocampus of
mice lacking the Jnk3 gene.";
Nature 389:865-870(1997).
[5]
INTERACTION WITH MAPKBP1.
PubMed=10471813; DOI=10.1016/S0014-5793(99)01084-4;
Koyano S., Ito M., Takamatsu N., Shiba T., Yamamoto K., Yoshioka K.;
"A novel Jun N-terminal kinase (JNK)-binding protein that enhances the
activation of JNK by MEK kinase 1 and TGF-beta-activated kinase 1.";
FEBS Lett. 457:385-388(1999).
[6]
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).
[7]
SUBCELLULAR LOCATION, AND INTERACTION WITH SARM1.
PubMed=17724133; DOI=10.1084/jem.20070868;
Kim Y., Zhou P., Qian L., Chuang J.Z., Lee J., Li C., Iadecola C.,
Nathan C., Ding A.;
"MyD88-5 links mitochondria, microtubules, and JNK3 in neurons and
regulates neuronal survival.";
J. Exp. Med. 204:2063-2074(2007).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
FUNCTION IN NEURONAL APOPTOSIS.
PubMed=20418776; DOI=10.1097/NEN.0b013e3181db8100;
Choi W.S., Abel G., Klintworth H., Flavell R.A., Xia Z.;
"JNK3 mediates paraquat- and rotenone-induced dopaminergic neuron
death.";
J. Neuropathol. Exp. Neurol. 69:511-520(2010).
[10]
FUNCTION IN NEURITE GROWTH.
PubMed=21554942; DOI=10.1016/j.heares.2011.04.011;
Atkinson P.J., Cho C.H., Hansen M.R., Green S.H.;
"Activity of all JNK isoforms contributes to neurite growth in spiral
ganglion neurons.";
Hear. Res. 278:77-85(2011).
[11]
FUNCTION, AND TISSUE SPECIFICITY.
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).
-!- 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:20418776,
ECO:0000269|PubMed:21554942, ECO:0000269|PubMed:22441692,
ECO:0000269|PubMed:9349820}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:9349820};
-!- 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 for the enzyme.
MAP2K4 then phosphorylates Tyr-223 resulting in a further increase
in Vmax. Inhibited by dual specificity phosphatases, such as DUSP1
(By similarity). Inhibited by HDAC9. {ECO:0000250,
ECO:0000269|PubMed:16611996}.
-!- SUBUNIT: 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 (By similarity). Interacts with HDAC9
and MAPKBP1. Interacts with ARRB2; the interaction enhances MAPK10
activation by MAP3K5 (By similarity). Interacts with SARM1.
{ECO:0000250, ECO:0000269|PubMed:10471813,
ECO:0000269|PubMed:16611996, ECO:0000269|PubMed:17724133}.
-!- INTERACTION:
Q9ESN9-2:Mapk8ip3; NbExp=4; IntAct=EBI-400741, EBI-9549291;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17724133}.
Membrane {ECO:0000269|PubMed:17724133}; Lipid-anchor
{ECO:0000269|PubMed:17724133}. Nucleus
{ECO:0000269|PubMed:17724133}. Mitochondrion
{ECO:0000269|PubMed:17724133}. Note=Palmitoylation regulates
MAPK10 trafficking to cytoskeleton (By similarity). Recruited to
the mitochondria in the presence of SARM1. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Alpha-2;
IsoId=Q61831-1; Sequence=Displayed;
Name=Alpha-1;
IsoId=Q61831-2; Sequence=VSP_004840;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Brain (at protein level). Expressed
specifically in neurons of the hippocampus, cortex, cerebellum,
brainstem, and spinal cord. Seems to be also found in testis, and
very weakly in the heart. {ECO:0000269|PubMed:22441692}.
-!- DEVELOPMENTAL STAGE: Expression begins in day E11.5 embryos, and
is localized in both the rostral spinal cord and rhombencephalon.
In day E12.5-13 embryos, it is found throughout the telencephalon.
By day 17.5, JNK3 is also expressed in neurons of dorsal root and
sensory ganglia and at lower levels in neurons of the myenteric
plexus and the developing heart.
-!- 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 (By similarity). {ECO:0000250}.
-!- PTM: Palmitoylation regulates subcellular location and axonal
development. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. MAP kinase subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L35236; AAB37741.1; -; mRNA.
EMBL; AB005665; BAA85877.1; -; mRNA.
RefSeq; NP_001297615.1; NM_001310686.2.
RefSeq; XP_017176379.1; XM_017320890.1.
RefSeq; XP_017176380.1; XM_017320891.1.
UniGene; Mm.39253; -.
UniGene; Mm.472459; -.
ProteinModelPortal; Q61831; -.
SMR; Q61831; -.
BioGrid; 204967; 4.
ELM; Q61831; -.
IntAct; Q61831; 3.
MINT; MINT-1487701; -.
STRING; 10090.ENSMUSP00000108468; -.
iPTMnet; Q61831; -.
PhosphoSitePlus; Q61831; -.
PaxDb; Q61831; -.
PeptideAtlas; Q61831; -.
PRIDE; Q61831; -.
GeneID; 26414; -.
KEGG; mmu:26414; -.
UCSC; uc008yjg.1; mouse. [Q61831-1]
CTD; 5602; -.
MGI; MGI:1346863; Mapk10.
eggNOG; KOG0665; Eukaryota.
eggNOG; ENOG410XSHI; LUCA.
HOGENOM; HOG000233024; -.
HOVERGEN; HBG014652; -.
InParanoid; Q61831; -.
KO; K04440; -.
PhylomeDB; Q61831; -.
BRENDA; 2.7.11.24; 3474.
ChiTaRS; Mapk10; mouse.
PRO; PR:Q61831; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_MAPK10; -.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0043005; C:neuron projection; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0014069; C:postsynaptic density; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004705; F:JUN kinase activity; IDA:UniProtKB.
GO; GO:0007254; P:JNK cascade; IDA:UniProtKB.
GO; GO:0045475; P:locomotor rhythm; IMP: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; IMP:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
GO; GO:0009416; P:response to light stimulus; IMP:UniProtKB.
InterPro; IPR011009; Kinase-like_dom.
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;
Alternative splicing; ATP-binding; Biological rhythms;
Complete proteome; Cytoplasm; Kinase; Lipoprotein; Membrane;
Mitochondrion; Nucleotide-binding; Nucleus; Palmitate; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Transferase.
CHAIN 1 464 Mitogen-activated protein kinase 10.
/FTId=PRO_0000186278.
DOMAIN 64 359 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 70 78 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 221 223 TXY.
ACT_SITE 189 189 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 93 93 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 221 221 Phosphothreonine; by MAP2K7.
{ECO:0000250|UniProtKB:P53779}.
MOD_RES 223 223 Phosphotyrosine; by MAP2K4.
{ECO:0000250|UniProtKB:P53779}.
LIPID 462 462 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 463 463 S-palmitoyl cysteine. {ECO:0000250}.
VAR_SEQ 418 464 GAAVNSSESLPPSSAVNDISSMSTDQTLASDTDSSLEASAG
PLGCCR -> AQVQQ (in isoform Alpha-1).
{ECO:0000305}.
/FTId=VSP_004840.
CONFLICT 267 267 S -> D (in Ref. 2; BAA85877).
{ECO:0000305}.
CONFLICT 345 345 V -> A (in Ref. 2; BAA85877).
{ECO:0000305}.
CONFLICT 412 412 S -> G (in Ref. 2; BAA85877).
{ECO:0000305}.
CONFLICT 418 423 GAAVNS -> AQVQQ (in Ref. 2).
{ECO:0000305}.
SEQUENCE 464 AA; 52532 MW; 4313335AC2E9D2E6 CRC64;
MSLHFLYYCS EPTLDVKIAF CQGFDKHVDV SSIAKHYNMS KSKVDNQFYS VEVGDSTFTV
LKRYQNLKPI GSGAQGIVCA AYDAVLDRNV AIKKLSRPFQ NQTHAKRAYR ELVLMKCVNH
KNIISLLNVF TPQKTLEEFQ DVYLVMELMD ANLCQVIQME LDHERMSYLL YQMLCGIKHL
HSAGIIHRDL KPSNIVVKSD CTLKILDFGL ARTAGTSFMM TPYVVTRYYR APEVILGMGY
KENVDIWSVG CIMGEMVRHK ILFPGRSYID QWNKVIEQLG TPCPEFMKKL QPTVRNYVEN
RPKYAGLTFP KLFPDSLFPA DSEHNKLKAS QARDLLSKML VIDPVKRISV DDALQHPYIN
VWYDPAEVEA PPPQIYDKQL DEREHTIEEW KELIYKEVMN SEEKTKNGVV KSQPSPSGAA
VNSSESLPPS SAVNDISSMS TDQTLASDTD SSLEASAGPL GCCR


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