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P45983

- MK08_HUMAN

UniProt

P45983 - MK08_HUMAN

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Protein

Mitogen-activated protein kinase 8

Gene
MAPK8, JNK1, PRKM8, SAPK1, SAPK1C
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 cell proliferation, differentiation, migration, transformation 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 MAPK8/JNK1. In turn, MAPK8/JNK1 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN, JDP2 and ATF2 and thus regulates AP-1 transcriptional activity. Phosphorylates the replication licensing factor CDT1, inhibiting the interaction between CDT1 and the histone H4 acetylase HBO1 to replication origins. Loss of this interaction abrogates the acetylation required for replication initiation. Promotes stressed cell apoptosis by phosphorylating key regulatory factors including p53/TP53 and Yes-associates protein YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized differentiation of T-helper cells into Th1 cells. Contributes to the survival of erythroid cells by phosphorylating the antagonist of cell death BAD upon EPO stimulation. Mediates starvation-induced BCL2 phosphorylation, BCL2 dissociation from BECN1, and thus activation of autophagy. Phosphorylates STMN2 and hence regulates microtubule dynamics, controlling neurite elongation in cortical neurons. In the developing brain, through its cytoplasmic activity on STMN2, negatively regulates the rate of exit from multipolar stage and of radial migration from the ventricular zone. Phosphorylates several other substrates including heat shock factor protein 4 (HSF4), the deacetylase SIRT1, ELK1, or the E3 ligase ITCH.8 Publications
JNK1 isoforms display different binding patterns: beta-1 preferentially binds to c-Jun, whereas alpha-1, alpha-2, and beta-2 have a similar low level of binding to both c-Jun or ATF2. However, there is no correlation between binding and phosphorylation, which is achieved at about the same efficiency by all isoforms.8 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium.1 Publication

Enzyme regulationi

Activated by threonine and tyrosine phosphorylation by either of two dual specificity kinases, MAP2K4 and MAP2K7. MAP2K4 shows a strong preference for Tyr-185 while MAP2K7 phosphorylates Tyr-183 preferentially. Inhibited by dual specificity phosphatases, such as DUSP1. Inhibited by SERPINB3.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei55 – 551ATP By similarity
Active sitei151 – 1511Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi32 – 409ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. histone deacetylase binding Source: BHF-UCL
  3. histone deacetylase regulator activity Source: BHF-UCL
  4. JUN kinase activity Source: UniProtKB
  5. protein binding Source: IntAct
  6. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: Reactome
  2. apoptotic signaling pathway Source: Reactome
  3. cellular response to lipopolysaccharide Source: MGI
  4. cellular response to mechanical stimulus Source: UniProtKB
  5. Fc-epsilon receptor signaling pathway Source: Reactome
  6. innate immune response Source: Reactome
  7. intrinsic apoptotic signaling pathway Source: Reactome
  8. JNK cascade Source: UniProtKB
  9. JUN phosphorylation Source: UniProtKB
  10. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  11. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  12. negative regulation of apoptotic process Source: UniProtKB
  13. negative regulation of protein binding Source: UniProtKB
  14. neurotrophin TRK receptor signaling pathway Source: Reactome
  15. ossification Source: Ensembl
  16. peptidyl-serine phosphorylation Source: UniProtKB
  17. peptidyl-threonine phosphorylation Source: UniProtKB
  18. positive regulation of apoptotic process Source: Reactome
  19. positive regulation of apoptotic signaling pathway Source: Ensembl
  20. positive regulation of deacetylase activity Source: BHF-UCL
  21. positive regulation of determination of dorsal identity Source: Ensembl
  22. positive regulation of gene expression Source: BHF-UCL
  23. positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
  24. regulation of histone deacetylation Source: GOC
  25. regulation of protein localization Source: BHF-UCL
  26. regulation of sequence-specific DNA binding transcription factor activity Source: Reactome
  27. response to cadmium ion Source: Ensembl
  28. response to stress Source: ProtInc
  29. response to UV Source: MGI
  30. stress-activated MAPK cascade Source: Reactome
  31. toll-like receptor 10 signaling pathway Source: Reactome
  32. toll-like receptor 2 signaling pathway Source: Reactome
  33. toll-like receptor 3 signaling pathway Source: Reactome
  34. toll-like receptor 4 signaling pathway Source: Reactome
  35. toll-like receptor 5 signaling pathway Source: Reactome
  36. toll-like receptor 9 signaling pathway Source: Reactome
  37. toll-like receptor signaling pathway Source: Reactome
  38. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  39. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  40. 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_13638. NRAGE signals death through JNK.
REACT_13643. NRIF signals cell death from the nucleus.
REACT_163701. FCERI mediated MAPK activation.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_2100. Activation of BMF and translocation to mitochondria.
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.
REACT_25299. DSCAM interactions.
SignaLinkiP45983.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase 8 (EC:2.7.11.24)
Short name:
MAP kinase 8
Short name:
MAPK 8
Alternative name(s):
JNK-46
Stress-activated protein kinase 1c
Short name:
SAPK1c
Stress-activated protein kinase JNK1
c-Jun N-terminal kinase 1
Gene namesi
Name:MAPK8
Synonyms:JNK1, PRKM8, SAPK1, SAPK1C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:6881. MAPK8.

Subcellular locationi

Cytoplasm. Nucleus 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. mitochondrion Source: Ensembl
  3. nucleoplasm Source: Reactome
  4. nucleus Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi183 – 1831T → A: Phosphorylation blocked.
Mutagenesisi185 – 1851Y → F: Phosphorylation blocked.

Organism-specific databases

PharmGKBiPA283.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 427427Mitogen-activated protein kinase 8PRO_0000186262Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei116 – 1161S-nitrosocysteine By similarity
Modified residuei183 – 1831Phosphothreonine; by MAP2K71 Publication
Modified residuei185 – 1851Phosphotyrosine; by MAP2K41 Publication
Modified residuei377 – 3771Phosphoserine By similarity

Post-translational modificationi

Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K7 and MAP2K4, which activates the enzyme. Phosphorylated by TAOK2.2 Publications

Keywords - PTMi

Phosphoprotein, S-nitrosylation

Proteomic databases

MaxQBiP45983.
PaxDbiP45983.
PRIDEiP45983.

PTM databases

PhosphoSiteiP45983.

Expressioni

Gene expression databases

ArrayExpressiP45983.
BgeeiP45983.
CleanExiHS_MAPK8.
GenevestigatoriP45983.

Organism-specific databases

HPAiCAB004463.

Interactioni

Subunit structurei

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 TP53 and WWOX. Interacts with JAMP. Forms a complex with MAPK8IP1 and ARHGEF28 By similarity. Interacts (phosphorylated form) with NFE2; the interaction phosphorylates NFE2 in undifferentiated cells By similarity. Interacts with NFATC4. Interacts with MECOM; regulates JNK signaling. Interacts with PIN1; this interaction mediates MAPK8 conformational changes leading to the binding of MAPK8 to its substrates.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BADQ929342EBI-286483,EBI-700771
CBLP226812EBI-286483,EBI-518228
JUNP054124EBI-286483,EBI-852823
MAP2K7O14733-23EBI-286483,EBI-492627
MAPK8IP1Q9UQF27EBI-286483,EBI-78404
Mapk8ip1Q9WVI9-12EBI-286483,EBI-288461From a different organism.
PIK3R1P279862EBI-286483,EBI-79464

Protein-protein interaction databases

BioGridi111585. 143 interactions.
DIPiDIP-249N.
IntActiP45983. 46 interactions.
MINTiMINT-1211982.
STRINGi9606.ENSP00000353483.

Structurei

Secondary structure

1
427
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 96
Beta strandi10 – 156
Beta strandi18 – 236
Beta strandi26 – 349
Beta strandi36 – 4510
Turni46 – 494
Beta strandi50 – 589
Helixi60 – 623
Helixi64 – 7916
Beta strandi83 – 853
Beta strandi88 – 925
Beta strandi94 – 974
Turni98 – 1003
Beta strandi103 – 1097
Beta strandi112 – 1143
Helixi115 – 1206
Helixi125 – 14420
Helixi154 – 1563
Beta strandi157 – 1593
Turni161 – 1633
Beta strandi165 – 1673
Beta strandi174 – 1774
Beta strandi178 – 1803
Beta strandi182 – 1843
Beta strandi185 – 1873
Helixi189 – 1913
Helixi194 – 1974
Helixi206 – 22015
Helixi230 – 24112
Helixi246 – 2494
Helixi254 – 2618
Helixi271 – 2744
Helixi277 – 2793
Helixi285 – 30117
Helixi306 – 3083
Helixi312 – 3176
Helixi319 – 3224
Helixi327 – 3304
Turni339 – 3424
Helixi349 – 36315

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UKHX-ray2.35A1-363[»]
1UKIX-ray2.70A1-363[»]
2G01X-ray3.50A/B1-364[»]
2GMXX-ray3.50A/B1-364[»]
2H96X-ray3.00A/B1-364[»]
2NO3X-ray3.20A/B1-364[»]
2XRWX-ray1.33A2-364[»]
2XS0X-ray2.60A1-379[»]
3ELJX-ray1.80A1-364[»]
3O17X-ray3.00A/B1-364[»]
3O2MX-ray2.70A/B1-364[»]
3PZEX-ray2.00A7-364[»]
3V3VX-ray2.70A1-366[»]
3VUDX-ray3.50A1-364[»]
3VUGX-ray3.24A1-364[»]
3VUHX-ray2.70A1-364[»]
3VUIX-ray2.80A1-364[»]
3VUKX-ray2.95A1-364[»]
3VULX-ray2.81A1-364[»]
3VUMX-ray2.69A1-364[»]
4AWIX-ray1.91A1-364[»]
4E73X-ray2.27A1-363[»]
4G1WX-ray2.45A1-363[»]
4HYSX-ray2.42A1-363[»]
4HYUX-ray2.15A1-363[»]
4IZYX-ray2.30A1-363[»]
4L7FX-ray1.95A7-362[»]
ProteinModelPortaliP45983.
SMRiP45983. Positions 7-364.

Miscellaneous databases

EvolutionaryTraceiP45983.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 321296Protein kinaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi183 – 1853TXY

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
HOVERGENiHBG014652.
InParanoidiP45983.
KOiK04440.
OMAiREHTLEQ.
OrthoDBiEOG7PCJGV.
PhylomeDBiP45983.
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_dom.
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 (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 2 (identifier: P45983-1) [UniParc]FASTAAdd to Basket

Also known as: JNK1-alpha-2

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

MSRSKRDNNF YSVEIGDSTF TVLKRYQNLK PIGSGAQGIV CAAYDAILER    50
NVAIKKLSRP FQNQTHAKRA YRELVLMKCV NHKNIIGLLN VFTPQKSLEE 100
FQDVYIVMEL MDANLCQVIQ MELDHERMSY LLYQMLCGIK HLHSAGIIHR 150
DLKPSNIVVK SDCTLKILDF GLARTAGTSF MMTPYVVTRY YRAPEVILGM 200
GYKENVDLWS VGCIMGEMVC HKILFPGRDY IDQWNKVIEQ LGTPCPEFMK 250
KLQPTVRTYV ENRPKYAGYS FEKLFPDVLF PADSEHNKLK ASQARDLLSK 300
MLVIDASKRI SVDEALQHPY INVWYDPSEA EAPPPKIPDK QLDEREHTIE 350
EWKELIYKEV MDLEERTKNG VIRGQPSPLG AAVINGSQHP SSSSSVNDVS 400
SMSTDPTLAS DTDSSLEAAA GPLGCCR 427
Length:427
Mass (Da):48,296
Last modified:November 1, 1997 - v2
Checksum:i94FB6BE0358B9B60
GO
Isoform 1 (identifier: P45983-2) [UniParc]FASTAAdd to Basket

Also known as: JNK1-alpha-1

The sequence of this isoform differs from the canonical sequence as follows:
     380-427: GAAVINGSQHPSSSSSVNDVSSMSTDPTLASDTDSSLEAAAGPLGCCR → AQVQQ

Note: Contains a phosphoserine at position 377.

Show »
Length:384
Mass (Da):44,229
Checksum:iA7320EF933E9CF85
GO
Isoform 3 (identifier: P45983-3) [UniParc]FASTAAdd to Basket

Also known as: JNK1-beta-1

The sequence of this isoform differs from the canonical sequence as follows:
     208-208: L → I
     219-230: VCHKILFPGRDY → IKGGVLFPGTDH
     380-427: GAAVINGSQHPSSSSSVNDVSSMSTDPTLASDTDSSLEAAAGPLGCCR → AQVQQ

Note: Contains a phosphoserine at position 377.

Show »
Length:384
Mass (Da):44,022
Checksum:i76E49A950E64C1A1
GO
Isoform 4 (identifier: P45983-4) [UniParc]FASTAAdd to Basket

Also known as: JNK1-beta-2

The sequence of this isoform differs from the canonical sequence as follows:
     208-208: L → I
     219-230: VCHKILFPGRDY → IKGGVLFPGTDH

Show »
Length:427
Mass (Da):48,088
Checksum:i3F5CC3F6A4F3EF2D
GO
Isoform 5 (identifier: P45983-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     206-281: Missing.
     380-427: GAAVINGSQHPSSSSSVNDVSSMSTDPTLASDTDSSLEAAAGPLGCCR → AQVQQ

Show »
Length:308
Mass (Da):35,333
Checksum:i914B803A1223601D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti171 – 1711G → S in a renal clear cell carcinoma sample; somatic mutation. 1 Publication
VAR_042258
Natural varianti177 – 1771G → R in a glioblastoma multiforme sample; somatic mutation. 1 Publication
VAR_042259
Natural varianti365 – 3651E → K.
Corresponds to variant rs45483593 [ dbSNP | Ensembl ].
VAR_050592

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei206 – 28176Missing in isoform 5. VSP_054554Add
BLAST
Alternative sequencei208 – 2081L → I in isoform 3 and isoform 4. VSP_004831
Alternative sequencei219 – 23012VCHKI…PGRDY → IKGGVLFPGTDH in isoform 3 and isoform 4. VSP_004832Add
BLAST
Alternative sequencei380 – 42748GAAVI…LGCCR → AQVQQ in isoform 1, isoform 3 and isoform 5. VSP_004833Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L26318 mRNA. Translation: AAA36131.1.
U34822 mRNA. Translation: AAC50607.1.
U35004 mRNA. Translation: AAC50610.1.
U35005 mRNA. Translation: AAC50611.1.
DQ234352 mRNA. Translation: ABB29981.1.
AC016397 Genomic DNA. No translation available.
AC074325 Genomic DNA. No translation available.
AB451231 mRNA. Translation: BAG70045.1.
CH471187 Genomic DNA. Translation: EAW93132.1.
CH471187 Genomic DNA. Translation: EAW93129.1.
CH471187 Genomic DNA. Translation: EAW93130.1.
CH471187 Genomic DNA. Translation: EAW93133.1.
CH471187 Genomic DNA. Translation: EAW93134.1.
CH471187 Genomic DNA. Translation: EAW93136.1.
BC144063 mRNA. Translation: AAI44064.1.
CCDSiCCDS60527.1. [P45983-5]
CCDS7223.1. [P45983-4]
CCDS7224.1. [P45983-1]
CCDS7225.1. [P45983-2]
CCDS7226.1. [P45983-3]
PIRiS71097.
S71099.
RefSeqiNP_001265476.1. NM_001278547.1. [P45983-4]
NP_001265477.1. NM_001278548.1. [P45983-5]
NP_002741.1. NM_002750.3. [P45983-2]
NP_620634.1. NM_139046.2. [P45983-3]
NP_620637.1. NM_139049.2. [P45983-1]
XP_006717980.1. XM_006717917.1. [P45983-1]
XP_006717981.1. XM_006717918.1. [P45983-3]
XP_006717982.1. XM_006717919.1. [P45983-2]
UniGeneiHs.138211.
Hs.522924.

Genome annotation databases

EnsembliENST00000360332; ENSP00000353483; ENSG00000107643. [P45983-1]
ENST00000374176; ENSP00000363291; ENSG00000107643. [P45983-4]
ENST00000374179; ENSP00000363294; ENSG00000107643. [P45983-3]
ENST00000374182; ENSP00000363297; ENSG00000107643. [P45983-2]
ENST00000374189; ENSP00000363304; ENSG00000107643. [P45983-1]
ENST00000395611; ENSP00000378974; ENSG00000107643.
GeneIDi5599.
KEGGihsa:5599.
UCSCiuc001jgo.3. human. [P45983-3]
uc001jgp.3. human. [P45983-1]
uc001jgq.3. human. [P45983-2]

Polymorphism databases

DMDMi2507195.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Wikipedia

C-Jun N-terminal kinases entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L26318 mRNA. Translation: AAA36131.1 .
U34822 mRNA. Translation: AAC50607.1 .
U35004 mRNA. Translation: AAC50610.1 .
U35005 mRNA. Translation: AAC50611.1 .
DQ234352 mRNA. Translation: ABB29981.1 .
AC016397 Genomic DNA. No translation available.
AC074325 Genomic DNA. No translation available.
AB451231 mRNA. Translation: BAG70045.1 .
CH471187 Genomic DNA. Translation: EAW93132.1 .
CH471187 Genomic DNA. Translation: EAW93129.1 .
CH471187 Genomic DNA. Translation: EAW93130.1 .
CH471187 Genomic DNA. Translation: EAW93133.1 .
CH471187 Genomic DNA. Translation: EAW93134.1 .
CH471187 Genomic DNA. Translation: EAW93136.1 .
BC144063 mRNA. Translation: AAI44064.1 .
CCDSi CCDS60527.1. [P45983-5 ]
CCDS7223.1. [P45983-4 ]
CCDS7224.1. [P45983-1 ]
CCDS7225.1. [P45983-2 ]
CCDS7226.1. [P45983-3 ]
PIRi S71097.
S71099.
RefSeqi NP_001265476.1. NM_001278547.1. [P45983-4 ]
NP_001265477.1. NM_001278548.1. [P45983-5 ]
NP_002741.1. NM_002750.3. [P45983-2 ]
NP_620634.1. NM_139046.2. [P45983-3 ]
NP_620637.1. NM_139049.2. [P45983-1 ]
XP_006717980.1. XM_006717917.1. [P45983-1 ]
XP_006717981.1. XM_006717918.1. [P45983-3 ]
XP_006717982.1. XM_006717919.1. [P45983-2 ]
UniGenei Hs.138211.
Hs.522924.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1UKH X-ray 2.35 A 1-363 [» ]
1UKI X-ray 2.70 A 1-363 [» ]
2G01 X-ray 3.50 A/B 1-364 [» ]
2GMX X-ray 3.50 A/B 1-364 [» ]
2H96 X-ray 3.00 A/B 1-364 [» ]
2NO3 X-ray 3.20 A/B 1-364 [» ]
2XRW X-ray 1.33 A 2-364 [» ]
2XS0 X-ray 2.60 A 1-379 [» ]
3ELJ X-ray 1.80 A 1-364 [» ]
3O17 X-ray 3.00 A/B 1-364 [» ]
3O2M X-ray 2.70 A/B 1-364 [» ]
3PZE X-ray 2.00 A 7-364 [» ]
3V3V X-ray 2.70 A 1-366 [» ]
3VUD X-ray 3.50 A 1-364 [» ]
3VUG X-ray 3.24 A 1-364 [» ]
3VUH X-ray 2.70 A 1-364 [» ]
3VUI X-ray 2.80 A 1-364 [» ]
3VUK X-ray 2.95 A 1-364 [» ]
3VUL X-ray 2.81 A 1-364 [» ]
3VUM X-ray 2.69 A 1-364 [» ]
4AWI X-ray 1.91 A 1-364 [» ]
4E73 X-ray 2.27 A 1-363 [» ]
4G1W X-ray 2.45 A 1-363 [» ]
4HYS X-ray 2.42 A 1-363 [» ]
4HYU X-ray 2.15 A 1-363 [» ]
4IZY X-ray 2.30 A 1-363 [» ]
4L7F X-ray 1.95 A 7-362 [» ]
ProteinModelPortali P45983.
SMRi P45983. Positions 7-364.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111585. 143 interactions.
DIPi DIP-249N.
IntActi P45983. 46 interactions.
MINTi MINT-1211982.
STRINGi 9606.ENSP00000353483.

Chemistry

BindingDBi P45983.
ChEMBLi CHEMBL2096667.
GuidetoPHARMACOLOGYi 1496.

PTM databases

PhosphoSitei P45983.

Polymorphism databases

DMDMi 2507195.

Proteomic databases

MaxQBi P45983.
PaxDbi P45983.
PRIDEi P45983.

Protocols and materials databases

DNASUi 5599.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000360332 ; ENSP00000353483 ; ENSG00000107643 . [P45983-1 ]
ENST00000374176 ; ENSP00000363291 ; ENSG00000107643 . [P45983-4 ]
ENST00000374179 ; ENSP00000363294 ; ENSG00000107643 . [P45983-3 ]
ENST00000374182 ; ENSP00000363297 ; ENSG00000107643 . [P45983-2 ]
ENST00000374189 ; ENSP00000363304 ; ENSG00000107643 . [P45983-1 ]
ENST00000395611 ; ENSP00000378974 ; ENSG00000107643 .
GeneIDi 5599.
KEGGi hsa:5599.
UCSCi uc001jgo.3. human. [P45983-3 ]
uc001jgp.3. human. [P45983-1 ]
uc001jgq.3. human. [P45983-2 ]

Organism-specific databases

CTDi 5599.
GeneCardsi GC10P049514.
HGNCi HGNC:6881. MAPK8.
HPAi CAB004463.
MIMi 601158. gene.
neXtProti NX_P45983.
PharmGKBi PA283.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOVERGENi HBG014652.
InParanoidi P45983.
KOi K04440.
OMAi REHTLEQ.
OrthoDBi EOG7PCJGV.
PhylomeDBi P45983.
TreeFami TF105100.

Enzyme and pathway databases

BRENDAi 2.7.11.24. 2681.
Reactomei REACT_13638. NRAGE signals death through JNK.
REACT_13643. NRIF signals cell death from the nucleus.
REACT_163701. FCERI mediated MAPK activation.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_2100. Activation of BMF and translocation to mitochondria.
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.
REACT_25299. DSCAM interactions.
SignaLinki P45983.

Miscellaneous databases

EvolutionaryTracei P45983.
GeneWikii MAPK8.
GenomeRNAii 5599.
NextBioi 21738.
PROi P45983.
SOURCEi Search...

Gene expression databases

ArrayExpressi P45983.
Bgeei P45983.
CleanExi HS_MAPK8.
Genevestigatori P45983.

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_dom.
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. "JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain."
    Derijard B., Hibi M., Wu I.-H., Barrett T., Su B., Deng T., Karin M., Davis R.J.
    Cell 76:1025-1037(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetal brain.
  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], ALTERNATIVE SPLICING.
    Tissue: Brain.
  3. Lin L., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M., Tang Z., Huang B., Li H., Yang S.
    Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
  4. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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 3).
  8. "Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms."
    Derijard B., Raingeaud J., Barrett T., Wu I.-H., Han J., Ulevitch R.J., Davis R.J.
    Science 267:682-685(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  9. "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: PHOSPHORYLATION AT THR-183 AND TYR-185, REGULATION BY MAP2K4 AND MAP2K7, COFACTOR.
  10. "The evi-1 oncoprotein inhibits c-Jun N-terminal kinase and prevents stress-induced cell death."
    Kurokawa M., Mitani K., Yamagata T., Takahashi T., Izutsu K., Ogawa S., Moriguchi T., Nishida E., Yazaki Y., Hirai H.
    EMBO J. 19:2958-2968(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MECOM.
  11. "JNK1 physically interacts with WW domain-containing oxidoreductase (WOX1) and inhibits WOX1-mediated apoptosis."
    Chang N.-S., Doherty J., Ensign A.
    J. Biol. Chem. 278:9195-9202(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WWOX AND TP53.
  12. "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.
  13. "Association and regulation of heat shock transcription factor 4b with both extracellular signal-regulated kinase mitogen-activated protein kinase and dual-specificity tyrosine phosphatase DUSP26."
    Hu Y., Mivechi N.F.
    Mol. Cell. Biol. 26:3282-3294(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HSF4.
  14. "Nuclear factor of activated T3 is a negative regulator of Ras-JNK1/2-AP-1 induced cell transformation."
    Yao K., Cho Y.-Y., Bergen H.R. III, Madden B.J., Choi B.Y., Ma W.-Y., Bode A.M., Dong Z.
    Cancer Res. 67:8725-8735(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NFATC4.
  15. "Prostate-derived sterile 20-like kinase 1-alpha induces apoptosis. JNK-and caspase-dependent nuclear localization is a requirement for membrane blebbing."
    Zihni C., Mitsopoulos C., Tavares I.A., Baum B., Ridley A.J., Morris J.D.
    J. Biol. Chem. 282:6484-6493(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY TAOK2.
  16. "Rev7/MAD2B links c-Jun N-terminal protein kinase pathway signaling to activation of the transcription factor Elk-1."
    Zhang L., Yang S.H., Sharrocks A.D.
    Mol. Cell. Biol. 27:2861-2869(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF ELK1.
  17. "Phosphorylation of two eukaryotic transcription factors, Jun dimerization protein 2 and activation transcription factor 2, in Escherichia coli by Jun N-terminal kinase 1."
    Murata T., Shinozuka Y., Obata Y., Yokoyama K.K.
    Anal. Biochem. 376:115-121(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF JDP2.
  18. "JNK1-mediated phosphorylation of Bcl-2 regulates starvation-induced autophagy."
    Wei Y., Pattingre S., Sinha S., Bassik M., Levine B.
    Mol. Cell 30:678-688(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF BCL2.
  19. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377 (ISOFORMS 1 AND 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. "Crystal structure of SCCA1 and insight about the interaction with JNK1."
    Zheng B., Matoba Y., Kumagai T., Katagiri C., Hibino T., Sugiyama M.
    Biochem. Biophys. Res. Commun. 380:143-147(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SERPINB3, ENZYME REGULATION.
  22. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377 (ISOFORMS 1 AND 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "JNK1 phosphorylates SIRT1 and promotes its enzymatic activity."
    Nasrin N., Kaushik V.K., Fortier E., Wall D., Pearson K.J., de Cabo R., Bordone L.
    PLoS ONE 4:E8414-E8414(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF SIRT1.
  24. "JNK phosphorylates Yes-associated protein (YAP) to regulate apoptosis."
    Tomlinson V., Gudmundsdottir K., Luong P., Leung K.Y., Knebel A., Basu S.
    Cell Death Dis. 1:E29-E29(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF YAP1.
  25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "A critical step for JNK activation: isomerization by the prolyl isomerase Pin1."
    Park J.E., Lee J.A., Park S.G., Lee D.H., Kim S.J., Kim H.J., Uchida C., Uchida T., Park B.C., Cho S.
    Cell Death Differ. 19:153-161(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIN1.
  27. "Phosphorylation of Bcl-associated death protein (Bad) by erythropoietin-activated c-Jun N-terminal protein kinase 1 contributes to survival of erythropoietin-dependent cells."
    Deng H., Zhang J., Yoon T., Song D., Li D., Lin A.
    Int. J. Biochem. Cell Biol. 43:409-415(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF BAD.
  28. "Defective anchoring of JNK1 in the cytoplasm by MKK7 in Jurkat cells is associated with resistance to Fas-mediated apoptosis."
    Wang J., Tang R., Lv M., Wang Q., Zhang X., Guo Y., Chang H., Qiao C., Xiao H., Li X., Li Y., Shen B., Zhang J.
    Mol. Biol. Cell 22:117-127(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  29. "JNK1 phosphorylation of Cdt1 inhibits recruitment of HBO1 histone acetylase and blocks replication licensing in response to stress."
    Miotto B., Struhl K.
    Mol. Cell 44:62-71(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF CDT1.
  30. "Structural basis for the selective inhibition of JNK1 by the scaffolding protein JIP1 and SP600125."
    Heo Y.S., Kim S.K., Seo C.I., Kim Y.K., Sung B.J., Lee H.S., Lee J.I., Park S.Y., Kim J.H., Hwang K.Y., Hyun Y.L., Jeon Y.H., Ro S., Cho J.M., Lee T.G., Yang C.H.
    EMBO J. 23:2185-2195(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-363.
  31. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-171 AND ARG-177.

Entry informationi

Entry nameiMK08_HUMAN
AccessioniPrimary (citable) accession number: P45983
Secondary accession number(s): B5BTZ5
, B7ZLV4, D3DX88, D3DX92, Q15709, Q15712, Q15713, Q308M2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: September 3, 2014
This is version 165 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, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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