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P53779

- MK10_HUMAN

UniProt

P53779 - MK10_HUMAN

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Protein

Mitogen-activated protein kinase 10

Gene

MAPK10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium.1 Publication

Enzyme regulationi

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 HDAC9.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei93 – 931ATP
Active sitei189 – 1891Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi70 – 789ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. JUN kinase activity Source: UniProtKB
  3. MAP kinase kinase activity Source: ProtInc

GO - Biological processi

  1. activation of MAPK activity Source: GOC
  2. Fc-epsilon receptor signaling pathway Source: Reactome
  3. innate immune response Source: Reactome
  4. JNK cascade Source: UniProtKB
  5. JUN phosphorylation Source: GOC
  6. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  7. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  8. regulation of sequence-specific DNA binding transcription factor activity Source: Reactome
  9. signal transduction Source: ProtInc
  10. stress-activated MAPK cascade Source: Reactome
  11. toll-like receptor 10 signaling pathway Source: Reactome
  12. toll-like receptor 2 signaling pathway Source: Reactome
  13. toll-like receptor 3 signaling pathway Source: Reactome
  14. toll-like receptor 4 signaling pathway Source: Reactome
  15. toll-like receptor 5 signaling pathway Source: Reactome
  16. toll-like receptor 9 signaling pathway Source: Reactome
  17. toll-like receptor signaling pathway Source: Reactome
  18. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  19. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  20. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.24. 2681.
ReactomeiREACT_163701. FCERI mediated MAPK activation.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_21326. Activation of the AP-1 family of transcription factors.
REACT_21368. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
SignaLinkiP53779.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase 10 (EC:2.7.11.24)
Short name:
MAP kinase 10
Short name:
MAPK 10
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 namesi
Name:MAPK10
Synonyms:JNK3, JNK3A, PRKM10, SAPK1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:6872. MAPK10.

Subcellular locationi

Cytoplasm 1 Publication. Membrane 1 Publication; Lipid-anchor 1 Publication. Nucleus 1 Publication. Mitochondrion 1 Publication
Note: Palmitoylation regulates MAPK10 trafficking to cytoskeleton. Recruited to the mitochondria in the presence of SARM1 By similarity.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. mitochondrion Source: UniProtKB
  4. nucleoplasm Source: Reactome
  5. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi462 – 4621C → S: Loss of palmitoylation. 1 Publication
Mutagenesisi463 – 4631C → S: Loss of palmitoylation. 1 Publication

Keywords - Diseasei

Epilepsy, Mental retardation

Organism-specific databases

Orphaneti2382. Lennox-Gastaut syndrome.
PharmGKBiPA30617.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 464464Mitogen-activated protein kinase 10PRO_0000186277Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei154 – 1541S-nitrosocysteineBy similarity
Modified residuei221 – 2211Phosphothreonine; by MAP2K71 Publication
Modified residuei223 – 2231Phosphotyrosine; by MAP2K41 Publication
Lipidationi462 – 4621S-palmitoyl cysteine1 Publication
Lipidationi463 – 4631S-palmitoyl cysteine1 Publication

Post-translational modificationi

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.1 Publication
Palmitoylation regulates subcellular location and axonal development.1 Publication

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein, S-nitrosylation

Proteomic databases

MaxQBiP53779.
PaxDbiP53779.
PRIDEiP53779.

PTM databases

PhosphoSiteiP53779.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiP53779.
CleanExiHS_MAPK10.
ExpressionAtlasiP53779. baseline and differential.
GenevestigatoriP53779.

Organism-specific databases

HPAiCAB022625.

Interactioni

Subunit structurei

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.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ARRB1P494072EBI-713543,EBI-743313
JUNP054122EBI-713543,EBI-852823
RELAQ042062EBI-713543,EBI-73886

Protein-protein interaction databases

BioGridi111588. 45 interactions.
DIPiDIP-1015N.
IntActiP53779. 18 interactions.
MINTiMINT-1373516.
STRINGi9606.ENSP00000352157.

Structurei

Secondary structure

1
464
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi48 – 536Combined sources
Beta strandi56 – 616Combined sources
Beta strandi64 – 696Combined sources
Beta strandi77 – 837Combined sources
Turni84 – 874Combined sources
Beta strandi88 – 9710Combined sources
Helixi98 – 1003Combined sources
Helixi102 – 11413Combined sources
Turni115 – 1173Combined sources
Beta strandi121 – 1233Combined sources
Beta strandi127 – 1304Combined sources
Turni136 – 1383Combined sources
Beta strandi142 – 1476Combined sources
Beta strandi150 – 1523Combined sources
Helixi153 – 1575Combined sources
Helixi163 – 18220Combined sources
Helixi192 – 1943Combined sources
Beta strandi195 – 1973Combined sources
Beta strandi199 – 2013Combined sources
Beta strandi203 – 2053Combined sources
Beta strandi207 – 2093Combined sources
Turni212 – 2143Combined sources
Helixi216 – 2194Combined sources
Beta strandi220 – 2223Combined sources
Helixi227 – 2293Combined sources
Helixi232 – 2354Combined sources
Helixi244 – 25815Combined sources
Helixi268 – 27912Combined sources
Helixi284 – 2874Combined sources
Helixi292 – 2998Combined sources
Helixi309 – 3124Combined sources
Helixi315 – 3173Combined sources
Helixi323 – 33917Combined sources
Turni344 – 3463Combined sources
Helixi350 – 3556Combined sources
Turni357 – 3615Combined sources
Helixi365 – 3684Combined sources
Helixi378 – 3825Combined sources
Helixi387 – 39913Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JNKX-ray2.30A1-423[»]
1PMNX-ray2.20A40-401[»]
1PMQX-ray2.20A40-401[»]
1PMUX-ray2.70A40-401[»]
1PMVX-ray2.50A40-401[»]
2B1PX-ray1.90A46-400[»]
2EXCX-ray2.75X45-400[»]
2O0UX-ray2.10A39-402[»]
2O2UX-ray2.45A39-402[»]
2OK1X-ray2.40A40-402[»]
2P33X-ray2.40A40-402[»]
2R9SX-ray2.40A/B46-401[»]
2WAJX-ray2.40A39-402[»]
2ZDTX-ray2.00A39-402[»]
2ZDUX-ray2.50A39-402[»]
3CGFX-ray3.00A40-402[»]
3CGOX-ray3.00A40-402[»]
3DA6X-ray2.00A39-402[»]
3FI2X-ray2.28A39-402[»]
3FI3X-ray2.20A39-402[»]
3FV8X-ray2.28A39-402[»]
3G90X-ray2.40X40-402[»]
3G9LX-ray2.20X40-402[»]
3G9NX-ray2.80A40-402[»]
3KVXX-ray2.40A39-402[»]
3OXIX-ray2.20A40-401[»]
3OY1X-ray1.70A40-401[»]
3PTGX-ray2.43A40-401[»]
3RTPX-ray2.40A40-401[»]
3TTIX-ray2.20A1-464[»]
3TTJX-ray2.10A1-464[»]
3V6RX-ray2.60A/B39-402[»]
3V6SX-ray2.97A/B39-402[»]
4H36X-ray3.00A46-400[»]
4H39X-ray1.99A46-400[»]
4H3BX-ray2.08A/C46-400[»]
4KKEX-ray2.20A40-402[»]
4KKGX-ray2.40A40-402[»]
4KKHX-ray2.00A40-402[»]
ProteinModelPortaliP53779.
SMRiP53779. Positions 11-429.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53779.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini64 – 359296Protein kinasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi221 – 2233TXY

Domaini

The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00550000074271.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiP53779.
KOiK04440.
OMAiEVMNFEE.
OrthoDBiEOG7PCJGV.
PhylomeDBiP53779.
TreeFamiTF105100.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008351. MAPK_JNK.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01772. JNKMAPKINASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01351. MAPK. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

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) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSLHFLYYCS EPTLDVKIAF CQGFDKQVDV SYIAKHYNMS KSKVDNQFYS
60 70 80 90 100
VEVGDSTFTV LKRYQNLKPI GSGAQGIVCA AYDAVLDRNV AIKKLSRPFQ
110 120 130 140 150
NQTHAKRAYR ELVLMKCVNH KNIISLLNVF TPQKTLEEFQ DVYLVMELMD
160 170 180 190 200
ANLCQVIQME LDHERMSYLL YQMLCGIKHL HSAGIIHRDL KPSNIVVKSD
210 220 230 240 250
CTLKILDFGL ARTAGTSFMM TPYVVTRYYR APEVILGMGY KENVDIWSVG
260 270 280 290 300
CIMGEMVRHK ILFPGRDYID QWNKVIEQLG TPCPEFMKKL QPTVRNYVEN
310 320 330 340 350
RPKYAGLTFP KLFPDSLFPA DSEHNKLKAS QARDLLSKML VIDPAKRISV
360 370 380 390 400
DDALQHPYIN VWYDPAEVEA PPPQIYDKQL DEREHTIEEW KELIYKEVMN
410 420 430 440 450
SEEKTKNGVV KGQPSPSGAA VNSSESLPPS SSVNDISSMS TDQTLASDTD
460
SSLEASAGPL GCCR
Length:464
Mass (Da):52,585
Last modified:November 1, 1997 - v2
Checksum:i2E20C05EB89CDA66
GO
Isoform Alpha-1 (identifier: P53779-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:422
Mass (Da):48,554
Checksum:iFCC8C11954481C04
GO
Isoform 3 (identifier: P53779-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:426
Mass (Da):48,128
Checksum:i1022B6AC7774A666
GO
Isoform 4 (identifier: P53779-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:277
Mass (Da):31,933
Checksum:i5C2FA3CFC85C1FF8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti162 – 1621D → G in BAG51956. (PubMed:14702039)Curated

Mass spectrometryi

Molecular mass is 44070 Da from positions 1 - 464. Determined by ESI. 1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 145145Missing in isoform 4. 1 PublicationVSP_041910Add
BLAST
Alternative sequencei1 – 3838Missing in isoform 3. 1 PublicationVSP_041911Add
BLAST
Alternative sequencei418 – 46447GAAVN…LGCCR → AQVQQ in isoform Alpha-1 and isoform 4. 3 PublicationsVSP_004839Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS34026.1. [P53779-1]
CCDS3612.1. [P53779-3]
CCDS3613.1. [P53779-4]
CCDS43247.1. [P53779-2]
PIRiS71104.
RefSeqiNP_002744.1. NM_002753.3. [P53779-2]
NP_620446.1. NM_138980.2. [P53779-3]
NP_620447.1. NM_138981.2. [P53779-4]
NP_620448.1. NM_138982.2. [P53779-1]
XP_005263186.1. XM_005263129.1. [P53779-1]
XP_005263187.1. XM_005263130.1. [P53779-1]
XP_005263192.1. XM_005263135.2. [P53779-2]
XP_006714330.1. XM_006714267.1. [P53779-1]
XP_006714331.1. XM_006714268.1. [P53779-3]
UniGeneiHs.125503.
Hs.13438.

Genome annotation databases

EnsembliENST00000359221; ENSP00000352157; ENSG00000109339. [P53779-1]
ENST00000361569; ENSP00000355297; ENSG00000109339. [P53779-2]
ENST00000395160; ENSP00000378589; ENSG00000109339. [P53779-4]
ENST00000395166; ENSP00000378595; ENSG00000109339. [P53779-3]
ENST00000395169; ENSP00000378598; ENSG00000109339. [P53779-3]
GeneIDi5602.
KEGGihsa:5602.
UCSCiuc003hpo.3. human. [P53779-1]
uc003hpp.3. human. [P53779-4]
uc003hpt.3. human. [P53779-2]

Polymorphism databases

DMDMi2507196.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS34026.1. [P53779-1 ]
CCDS3612.1. [P53779-3 ]
CCDS3613.1. [P53779-4 ]
CCDS43247.1. [P53779-2 ]
PIRi S71104.
RefSeqi NP_002744.1. NM_002753.3. [P53779-2 ]
NP_620446.1. NM_138980.2. [P53779-3 ]
NP_620447.1. NM_138981.2. [P53779-4 ]
NP_620448.1. NM_138982.2. [P53779-1 ]
XP_005263186.1. XM_005263129.1. [P53779-1 ]
XP_005263187.1. XM_005263130.1. [P53779-1 ]
XP_005263192.1. XM_005263135.2. [P53779-2 ]
XP_006714330.1. XM_006714267.1. [P53779-1 ]
XP_006714331.1. XM_006714268.1. [P53779-3 ]
UniGenei Hs.125503.
Hs.13438.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
3RTP X-ray 2.40 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 [» ]
4KKE X-ray 2.20 A 40-402 [» ]
4KKG X-ray 2.40 A 40-402 [» ]
4KKH X-ray 2.00 A 40-402 [» ]
ProteinModelPortali P53779.
SMRi P53779. Positions 11-429.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111588. 45 interactions.
DIPi DIP-1015N.
IntActi P53779. 18 interactions.
MINTi MINT-1373516.
STRINGi 9606.ENSP00000352157.

Chemistry

BindingDBi P53779.
ChEMBLi CHEMBL3038502.
GuidetoPHARMACOLOGYi 1498.

PTM databases

PhosphoSitei P53779.

Polymorphism databases

DMDMi 2507196.

Proteomic databases

MaxQBi P53779.
PaxDbi P53779.
PRIDEi P53779.

Protocols and materials databases

DNASUi 5602.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000359221 ; ENSP00000352157 ; ENSG00000109339 . [P53779-1 ]
ENST00000361569 ; ENSP00000355297 ; ENSG00000109339 . [P53779-2 ]
ENST00000395160 ; ENSP00000378589 ; ENSG00000109339 . [P53779-4 ]
ENST00000395166 ; ENSP00000378595 ; ENSG00000109339 . [P53779-3 ]
ENST00000395169 ; ENSP00000378598 ; ENSG00000109339 . [P53779-3 ]
GeneIDi 5602.
KEGGi hsa:5602.
UCSCi uc003hpo.3. human. [P53779-1 ]
uc003hpp.3. human. [P53779-4 ]
uc003hpt.3. human. [P53779-2 ]

Organism-specific databases

CTDi 5602.
GeneCardsi GC04M086936.
H-InvDB HIX0163985.
HGNCi HGNC:6872. MAPK10.
HPAi CAB022625.
MIMi 602897. gene.
neXtProti NX_P53779.
Orphaneti 2382. Lennox-Gastaut syndrome.
PharmGKBi PA30617.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00550000074271.
HOGENOMi HOG000233024.
HOVERGENi HBG014652.
InParanoidi P53779.
KOi K04440.
OMAi EVMNFEE.
OrthoDBi EOG7PCJGV.
PhylomeDBi P53779.
TreeFami TF105100.

Enzyme and pathway databases

BRENDAi 2.7.11.24. 2681.
Reactomei REACT_163701. FCERI mediated MAPK activation.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_21326. Activation of the AP-1 family of transcription factors.
REACT_21368. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
SignaLinki P53779.

Miscellaneous databases

ChiTaRSi MAPK10. human.
EvolutionaryTracei P53779.
GeneWikii MAPK10.
GenomeRNAii 5602.
NextBioi 21762.
PROi P53779.
SOURCEi Search...

Gene expression databases

Bgeei P53779.
CleanExi HS_MAPK10.
ExpressionAtlasi P53779. baseline and differential.
Genevestigatori P53779.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008351. MAPK_JNK.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
PRINTSi PR01772. JNKMAPKINASE.
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS01351. MAPK. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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, DISEASE.
  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. 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.

Entry informationi

Entry nameiMK10_HUMAN
AccessioniPrimary (citable) accession number: P53779
Secondary accession number(s): A6NFS3
, A6NG28, B3KQ94, Q15707, Q49AP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: October 29, 2014
This is version 168 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3