P53779 (MK10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mitogen-activated protein kinase 10
Short name=MAP kinase 10
Short name=MAPK 10
EC=2.7.11.24

Alternative name(s):
MAP kinase p49 3F12
Stress-activated protein kinase 1b
Short name=SAPK1b
Stress-activated protein kinase JNK3
c-Jun N-terminal kinase 3

Gene names

Name:	MAPK10
Synonyms:	JNK3, JNK3A, PRKM10, SAPK1B

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	464 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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 beta-amyloid precursor protein/APP signaling during neuronal differentiation by phosphorylating APP. Participates also in neurite growth in spiral ganglion neurons. Ref.9
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium. Ref.7
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. Ref.8 Ref.13
Subunit structure	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. Ref.10 Ref.13 Ref.14
Subcellular location	Cytoplasm. Membrane; Lipid-anchor. Nucleus. Mitochondrion. Note: Palmitoylation regulates MAPK10 trafficking to cytoskeleton. Recruited to the mitochondria in the presence of SARM1 By similarity. Ref.12
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.
Post-translational modification	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. Ref.7 Palmitoylation regulates subcellular location and axonal development. Ref.15
Involvement in disease	Epileptic encephalopathy, Lennox-Gastaut type (EELG) [MIM:606369]: A childhhod disorder characterized by a combination of seizures, usually including atypical absence seizures, tonic seizures, atonic or astatic seizures, and mental retardation. Note: The disease is caused by mutations affecting the gene represented in this entry. A chromosomal aberration involving MAPK10 has been found in a single patient. Translocation t(Y;4)(q11.2;q21) which causes MAPK10 truncation.
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily. Contains 1 protein kinase domain.
Mass spectrometry	Molecular mass is 44070 Da from positions 1 - 464. Determined by ESI. Ref.7

Ontologies

Keywords
Cellular component	Cytoplasm Membrane Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement
Disease	Epilepsy Mental retardation
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	MyD88-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome TRIF-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome innate immune response Traceable author statement. Source: Reactome regulation of sequence-specific DNA binding transcription factor activity Traceable author statement. Source: Reactome toll-like receptor 10 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 2 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 3 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 4 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 5 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 9 signaling pathway Traceable author statement. Source: Reactome toll-like receptor TLR1:TLR2 signaling pathway Traceable author statement. Source: Reactome toll-like receptor TLR6:TLR2 signaling pathway Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome mitochondrion Inferred from sequence or structural similarity. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW JUN kinase activity Inferred from sequence or structural similarity Ref.2. Source: UniProtKB MAP kinase kinase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RELA	Q04206	2	EBI-713543,EBI-73886

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: 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.

Isoform Alpha-2 (identifier: P53779-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Alpha-1 (identifier: P53779-2)

The sequence of this isoform differs from the canonical sequence as follows:
     418-464: GAAVNSSESLPPSSSVNDISSMSTDQTLASDTDSSLEASAGPLGCCR → AQVQQ

Isoform 3 (identifier: P53779-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: Missing.

Isoform 4 (identifier: P53779-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-145: Missing.
     418-464: GAAVNSSESLPPSSSVNDISSMSTDQTLASDTDSSLEASAGPLGCCR → AQVQQ

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 464

464

Mitogen-activated protein kinase 10

PRO_0000186277

Regions

Domain

64 – 359

296

Protein kinase

Nucleotide binding

70 – 78

9

ATP

Motif

221 – 223

3

TXY

Sites

Active site

189

1

Proton acceptor

Binding site

93

1

ATP

Amino acid modifications

Modified residue

221

1

Phosphothreonine; by MAP2K7 Ref.7

Modified residue

223

1

Phosphotyrosine; by MAP2K4 Ref.7

Lipidation

462

1

S-palmitoyl cysteine Probable

Lipidation

463

1

S-palmitoyl cysteine Probable

Natural variations

Alternative sequence

1 – 145

145

Missing in isoform 4.

VSP_041910

Alternative sequence

1 – 38

38

Missing in isoform 3.

VSP_041911

Alternative sequence

418 – 464

47

GAAVN…LGCCR → AQVQQ in isoform Alpha-1 and isoform 4.

VSP_004839

Experimental info

Mutagenesis

462

1

C → S: Loss of palmitoylation. Ref.15

Mutagenesis

463

1

C → S: Loss of palmitoylation. Ref.15

Sequence conflict

162

1

D → G in BAG51956. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

464

Helix Strand Turn

Details...

Beta strand

48 – 53

6

Beta strand

56 – 61

6

Beta strand

64 – 69

6

Beta strand

77 – 83

7

Turn

84 – 87

4

Beta strand

88 – 97

10

Helix

98 – 100

3

Helix

102 – 114

13

Turn

115 – 117

3

Beta strand

121 – 123

3

Beta strand

127 – 130

4

Turn

136 – 138

3

Beta strand

142 – 147

6

Beta strand

150 – 152

3

Helix

153 – 157

5

Helix

163 – 182

20

Helix

192 – 194

3

Beta strand

195 – 197

3

Beta strand

203 – 205

3

Beta strand

207 – 209

3

Turn

212 – 214

3

Helix

216 – 219

4

Beta strand

220 – 222

3

Helix

227 – 229

3

Helix

232 – 235

4

Helix

244 – 258

15

Helix

268 – 279

12

Helix

284 – 287

4

Helix

292 – 299

8

Helix

309 – 312

4

Helix

315 – 317

3

Helix

323 – 339

17

Turn

344 – 346

3

Helix

350 – 355

6

Turn

357 – 361

5

Helix

365 – 368

4

Helix

378 – 382

5

Helix

387 – 399

13

Sequences

	Sequence		Length	Mass (Da)
	Isoform Alpha-2 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 2E20C05EB89CDA66	FASTA	464	52,585
	10 20 30 40 50 60 MSLHFLYYCS EPTLDVKIAF CQGFDKQVDV SYIAKHYNMS KSKVDNQFYS VEVGDSTFTV 70 80 90 100 110 120 LKRYQNLKPI GSGAQGIVCA AYDAVLDRNV AIKKLSRPFQ NQTHAKRAYR ELVLMKCVNH 130 140 150 160 170 180 KNIISLLNVF TPQKTLEEFQ DVYLVMELMD ANLCQVIQME LDHERMSYLL YQMLCGIKHL 190 200 210 220 230 240 HSAGIIHRDL KPSNIVVKSD CTLKILDFGL ARTAGTSFMM TPYVVTRYYR APEVILGMGY 250 260 270 280 290 300 KENVDIWSVG CIMGEMVRHK ILFPGRDYID QWNKVIEQLG TPCPEFMKKL QPTVRNYVEN 310 320 330 340 350 360 RPKYAGLTFP KLFPDSLFPA DSEHNKLKAS QARDLLSKML VIDPAKRISV DDALQHPYIN 370 380 390 400 410 420 VWYDPAEVEA PPPQIYDKQL DEREHTIEEW KELIYKEVMN SEEKTKNGVV KGQPSPSGAA 430 440 450 460 VNSSESLPPS SSVNDISSMS TDQTLASDTD SSLEASAGPL GCCR
	Isoform Alpha-1 [UniParc]. Checksum: FCC8C11954481C04	FASTA	422	48,554
	10 20 30 40 50 60 MSLHFLYYCS EPTLDVKIAF CQGFDKQVDV SYIAKHYNMS KSKVDNQFYS VEVGDSTFTV 70 80 90 100 110 120 LKRYQNLKPI GSGAQGIVCA AYDAVLDRNV AIKKLSRPFQ NQTHAKRAYR ELVLMKCVNH 130 140 150 160 170 180 KNIISLLNVF TPQKTLEEFQ DVYLVMELMD ANLCQVIQME LDHERMSYLL YQMLCGIKHL 190 200 210 220 230 240 HSAGIIHRDL KPSNIVVKSD CTLKILDFGL ARTAGTSFMM TPYVVTRYYR APEVILGMGY 250 260 270 280 290 300 KENVDIWSVG CIMGEMVRHK ILFPGRDYID QWNKVIEQLG TPCPEFMKKL QPTVRNYVEN 310 320 330 340 350 360 RPKYAGLTFP KLFPDSLFPA DSEHNKLKAS QARDLLSKML VIDPAKRISV DDALQHPYIN 370 380 390 400 410 420 VWYDPAEVEA PPPQIYDKQL DEREHTIEEW KELIYKEVMN SEEKTKNGVV KGQPSPSAQV QQ
	Isoform 3 [UniParc]. Checksum: 1022B6AC7774A666	FASTA	426	48,128
	10 20 30 40 50 60 MSKSKVDNQF YSVEVGDSTF TVLKRYQNLK PIGSGAQGIV CAAYDAVLDR NVAIKKLSRP 70 80 90 100 110 120 FQNQTHAKRA YRELVLMKCV NHKNIISLLN VFTPQKTLEE FQDVYLVMEL MDANLCQVIQ 130 140 150 160 170 180 MELDHERMSY LLYQMLCGIK HLHSAGIIHR DLKPSNIVVK SDCTLKILDF GLARTAGTSF 190 200 210 220 230 240 MMTPYVVTRY YRAPEVILGM GYKENVDIWS VGCIMGEMVR HKILFPGRDY IDQWNKVIEQ 250 260 270 280 290 300 LGTPCPEFMK KLQPTVRNYV ENRPKYAGLT FPKLFPDSLF PADSEHNKLK ASQARDLLSK 310 320 330 340 350 360 MLVIDPAKRI SVDDALQHPY INVWYDPAEV EAPPPQIYDK QLDEREHTIE EWKELIYKEV 370 380 390 400 410 420 MNSEEKTKNG VVKGQPSPSG AAVNSSESLP PSSSVNDISS MSTDQTLASD TDSSLEASAG PLGCCR
	Isoform 4 [UniParc]. Checksum: 5C2FA3CFC85C1FF8	FASTA	277	31,933
	10 20 30 40 50 60 MELMDANLCQ VIQMELDHER MSYLLYQMLC GIKHLHSAGI IHRDLKPSNI VVKSDCTLKI 70 80 90 100 110 120 LDFGLARTAG TSFMMTPYVV TRYYRAPEVI LGMGYKENVD IWSVGCIMGE MVRHKILFPG 130 140 150 160 170 180 RDYIDQWNKV IEQLGTPCPE FMKKLQPTVR NYVENRPKYA GLTFPKLFPD SLFPADSEHN 190 200 210 220 230 240 KLKASQARDL LSKMLVIDPA KRISVDDALQ HPYINVWYDP AEVEAPPPQI YDKQLDEREH 250 260 270 TIEEWKELIY KEVMNSEEKT KNGVVKGQPS PSAQVQQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"p493F12 kinase: a novel MAP kinase expressed in a subset of neurons in the human nervous system." Mohit A.A., Martin J.H., Miller C.A. Neuron 14:67-78(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1). Tissue: Hippocampus.
[2]	"Selective interaction of JNK protein kinase isoforms with transcription factors." Gupta S., Barrett T., Whitmarsh A.J., Cavanagh J., Sluss H.K., Derijard B., Davis R.J. EMBO J. 15:2760-2770(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-1 AND ALPHA-2). Tissue: Brain.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4). Tissue: Caudate nucleus.
[4]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." 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. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-2). Tissue: Brain.
[7]	"Activation of JNK3 alpha 1 requires both MKK4 and MKK7: kinetic characterization of in vitro phosphorylated JNK3 alpha 1." Lisnock J., Griffin P., Calaycay J., Frantz B., Parsons J., O'Keefe S.J., LoGrasso P. Biochemistry 39:3141-3148(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, REGULATION BY MAP2K4 AND MAP2K7, PHOSPHORYLATION AT THR-221 AND TYR-223, COFACTOR, MASS SPECTROMETRY.
[8]	"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." Fleming Y., Armstrong C.G., Morrice N., Paterson A., Goedert M., Cohen P. Biochem. J. 352:145-154(2000) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[9]	"c-Jun N-terminal kinase-3 (JNK3)/stress-activated protein kinase-beta (SAPKbeta) binds and phosphorylates the neuronal microtubule regulator SCG10." Neidhart S., Antonsson B., Gillieron C., Vilbois F., Grenningloh G., Arkinstall S. FEBS Lett. 508:259-264(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF STMN2.
[10]	"Characterization of a novel human sperm-associated antigen 9 (SPAG9) having structural homology with c-Jun N-terminal kinase-interacting protein." Jagadish N., Rana R., Selvi R., Mishra D., Garg M., Yadav S., Herr J.C., Okumura K., Hasegawa A., Koyama K., Suri A. Biochem. J. 389:73-82(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SPAG9.
[11]	"Truncation of the CNS-expressed JNK3 in a patient with a severe developmental epileptic encephalopathy." 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. Hum. Genet. 118:559-567(2006) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL REARRANGEMENT, INVOLVEMENT IN EPILEPTIC ENCEPHALOPATHY LENNOX-GASTAUT TYPE.
[12]	"Visual and both non-visual arrestins in their 'inactive' conformation bind JNK3 and Mdm2 and relocalize them from the nucleus to the cytoplasm." Song X., Raman D., Gurevich E.V., Vishnivetskiy S.A., Gurevich V.V. J. Biol. Chem. 281:21491-21499(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[13]	"Neuroprotection by histone deacetylase-related protein." Morrison B.E., Majdzadeh N., Zhang X., Lyles A., Bassel-Duby R., Olson E.N., D'Mello S.R. Mol. Cell. Biol. 26:3550-3564(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HDAC9, ENZYME REGULATION.
[14]	"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." Xu T.-R., Baillie G.S., Bhari N., Houslay T.M., Pitt A.M., Adams D.R., Kolch W., Houslay M.D., Milligan G. Biochem. J. 413:51-60(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ARRB2.
[15]	"Isoform-specific palmitoylation of JNK regulates axonal development." Yang G., Liu Y., Yang K., Liu R., Zhu S., Coquinco A., Wen W., Kojic L., Jia W., Cynader M. Cell Death Differ. 19:553-561(2012) [PubMed] [Europe PMC] [Abstract] Cited for: PALMITOYLATION AT CYS-462 AND CYS-463, MUTAGENESIS OF CYS-462 AND CYS-463.
[16]	"Crystal structure of JNK3: a kinase implicated in neuronal apoptosis." Xie X., Gu Y., Fox T., Coll J.T., Fleming M.A., Markland W., Caron P.R., Wilson K.P., Su M.S.-S. Structure 6:983-991(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 40-402.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U07620 mRNA. Translation: AAC50101.1.
U34819 mRNA. Translation: AAC50604.1.
U34820 mRNA. Translation: AAC50605.1.
AK057723 mRNA. Translation: BAG51956.1.
AK124791 mRNA. Translation: BAG54096.1.
AC096953 Genomic DNA. No translation available.
AC104059 Genomic DNA. No translation available.
AC104827 Genomic DNA. No translation available.
AC108054 Genomic DNA. No translation available.
AC110076 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX05963.1.
BC035057 mRNA. Translation: AAH35057.1.

IPI

IPI00003148.
IPI00023547.

PIR

S71104.

RefSeq

NP_002744.1. NM_002753.3.
NP_620446.1. NM_138980.2.
NP_620447.1. NM_138981.2.
NP_620448.1. NM_138982.2.

UniGene

Hs.125503.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JNK	X-ray	2.30	A	1-423	[»]
1PMN	X-ray	2.20	A	40-401	[»]
1PMQ	X-ray	2.20	A	40-401	[»]
1PMU	X-ray	2.70	A	40-401	[»]
1PMV	X-ray	2.50	A	40-401	[»]
2B1P	X-ray	1.90	A	46-400	[»]
2EXC	X-ray	2.75	X	45-400	[»]
2O0U	X-ray	2.10	A	39-402	[»]
2O2U	X-ray	2.45	A	39-402	[»]
2OK1	X-ray	2.40	A	40-402	[»]
2P33	X-ray	2.40	A	40-402	[»]
2R9S	X-ray	2.40	A/B	46-401	[»]
2WAJ	X-ray	2.40	A	39-402	[»]
2ZDT	X-ray	2.00	A	39-402	[»]
2ZDU	X-ray	2.50	A	39-402	[»]
3CGF	X-ray	3.00	A	40-402	[»]
3CGO	X-ray	3.00	A	40-402	[»]
3DA6	X-ray	2.00	A	39-402	[»]
3FI2	X-ray	2.28	A	39-402	[»]
3FI3	X-ray	2.20	A	39-402	[»]
3FV8	X-ray	2.28	A	39-402	[»]
3G90	X-ray	2.40	X	40-402	[»]
3G9L	X-ray	2.20	X	40-402	[»]
3G9N	X-ray	2.80	A	40-402	[»]
3KVX	X-ray	2.40	A	39-402	[»]
3OXI	X-ray	2.20	A	40-401	[»]
3OY1	X-ray	1.70	A	40-401	[»]
3PTG	X-ray	2.43	A	40-401	[»]
3TTI	X-ray	2.20	A	1-464	[»]
3TTJ	X-ray	2.10	A	1-464	[»]
3V6R	X-ray	2.60	A/B	39-402	[»]
3V6S	X-ray	2.97	A/B	39-402	[»]
4H36	X-ray	3.00	A	46-400	[»]
4H39	X-ray	1.99	A	46-400	[»]
4H3B	X-ray	2.08	A/C	46-400	[»]

ProteinModelPortal

P53779.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1015N.

IntAct

P53779. 11 interactions.

MINT

MINT-1373516.

STRING

9606.ENSP00000352157.

PTM databases

PhosphoSite

P53779.

Polymorphism databases

DMDM

2507196.

Proteomic databases

PaxDb

P53779.

PRIDE

P53779.

Protocols and materials databases

DNASU

5602.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000359221; ENSP00000352157; ENSG00000109339.
ENST00000361569; ENSP00000355297; ENSG00000109339.
ENST00000395160; ENSP00000378589; ENSG00000109339.
ENST00000395161; ENSP00000378590; ENSG00000109339.
ENST00000395166; ENSP00000378595; ENSG00000109339.
ENST00000395169; ENSP00000378598; ENSG00000109339.

GeneID

5602.

KEGG

hsa:5602.

UCSC

uc003hpo.3. human.
uc003hpt.3. human.

Organism-specific databases

CTD

5602.

GeneCards

GC04M086878.

H-InvDB

HIX0163985.

HGNC

HGNC:6872. MAPK10.

HPA

CAB022625.

MIM

602897. gene.
606369. phenotype.

neXtProt

NX_P53779.

Orphanet

2382. Lennox-Gastaut syndrome.

PharmGKB

PA30617.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233024.

HOVERGEN

HBG014652.

InParanoid

P53779.

KO

K04440.

OMA

KEVMNFE.

OrthoDB

EOG48SGT3.

Enzyme and pathway databases

BRENDA

2.7.11.24. 2681.

Pathway_Interaction_DB

foxopathway. FoxO family signaling.
p75ntrpathway. p75(NTR)-mediated signaling.

Reactome

REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.

SignaLink

P53779.

Gene expression databases

ArrayExpress

P53779.

Bgee

P53779.

CleanEx

HS_MAPK10.

Genevestigator

P53779.

GermOnline

ENSG00000109339. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008351. MAPK_JNK.
IPR000719. Prot_kinase_cat_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

PRINTS

PR01772. JNKMAPKINASE.

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P53779.

ChEMBL

CHEMBL2637.

ChiTaRS

MAPK10. human.

EvolutionaryTrace

P53779.

GenomeRNAi

5602.

NextBio

21762.

SOURCE

Search...

Entry information

Entry name

MK10_HUMAN

Accession

Primary (citable) accession number: P53779
Secondary accession number(s): A6NFS3 , A6NG28, B3KQ94, Q15707, Q49AP1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	November 1, 1997
Last modified:	May 29, 2013
This is version 152 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.