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P45984

- MK09_HUMAN

UniProt

P45984 - MK09_HUMAN

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Protein

Mitogen-activated protein kinase 9

Gene
MAPK9, JNK2, PRKM9, SAPK1A
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 MAPK9/JNK2. In turn, MAPK9/JNK2 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional activity. In response to oxidative or ribotoxic stresses, inhibits rRNA synthesis by phosphorylating and inactivating the RNA polymerase 1-specific transcription initiation factor RRN3. Promotes stressed cell apoptosis by phosphorylating key regulatory factors including TP53 and YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized differentiation of T-helper cells into Th1 cells. Upon T-cell receptor (TCR) stimulation, is activated by CARMA1, BCL10, MAP2K7 and MAP3K7/TAK1 to regulate JUN protein levels. Plays an important role in the osmotic stress-induced epithelial tight-junctions disruption. When activated, promotes beta-catenin/CTNNB1 degradation and inhibits the canonical Wnt signaling pathway. Participates also in neurite growth in spiral ganglion neurons.6 Publications
MAPK9 isoforms display different binding patterns: alpha-1 and alpha-2 preferentially bind to JUN, whereas beta-1 and beta-2 bind to ATF2. However, there is no correlation between binding and phosphorylation, which is achieved at about the same efficiency by all isoforms. JUNB is not a substrate for JNK2 alpha-2, and JUND binds only weakly to it.6 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.

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. cysteine-type endopeptidase activator activity involved in apoptotic process Source: Ensembl
  3. JUN kinase activity Source: UniProtKB
  4. protein binding Source: IntAct
  5. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. cellular response to growth factor stimulus Source: Ensembl
  2. cellular response to interleukin-1 Source: Ensembl
  3. cellular response to lipopolysaccharide Source: Ensembl
  4. cellular response to tumor necrosis factor Source: Ensembl
  5. cellular response to UV Source: Ensembl
  6. central nervous system development Source: Ensembl
  7. Fc-epsilon receptor signaling pathway Source: Reactome
  8. innate immune response Source: Reactome
  9. JNK cascade Source: UniProtKB
  10. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  11. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  12. neuron projection development Source: Ensembl
  13. positive regulation of apoptotic process Source: Ensembl
  14. positive regulation of apoptotic signaling pathway Source: Ensembl
  15. positive regulation of cell morphogenesis involved in differentiation Source: Ensembl
  16. positive regulation of chemokine production Source: Ensembl
  17. positive regulation of gene expression Source: BHF-UCL
  18. positive regulation of macrophage derived foam cell differentiation Source: BHF-UCL
  19. positive regulation of nitric oxide biosynthetic process Source: Ensembl
  20. positive regulation of nitric-oxide synthase biosynthetic process Source: Ensembl
  21. positive regulation of prostaglandin biosynthetic process Source: Ensembl
  22. positive regulation of prostaglandin secretion Source: Ensembl
  23. positive regulation of protein phosphorylation Source: Ensembl
  24. positive regulation of transcription, DNA-templated Source: Ensembl
  25. protein targeting to mitochondrion Source: Ensembl
  26. regulation of JNK cascade Source: Ensembl
  27. regulation of protein ubiquitination Source: Ensembl
  28. regulation of sequence-specific DNA binding transcription factor activity Source: Reactome
  29. release of cytochrome c from mitochondria Source: Ensembl
  30. response to amine Source: Ensembl
  31. response to cadmium ion Source: Ensembl
  32. response to drug Source: Ensembl
  33. response to mechanical stimulus Source: Ensembl
  34. response to stress Source: ProtInc
  35. response to toxic substance Source: Ensembl
  36. stress-activated MAPK cascade Source: Reactome
  37. toll-like receptor 10 signaling pathway Source: Reactome
  38. toll-like receptor 2 signaling pathway Source: Reactome
  39. toll-like receptor 3 signaling pathway Source: Reactome
  40. toll-like receptor 4 signaling pathway Source: Reactome
  41. toll-like receptor 5 signaling pathway Source: Reactome
  42. toll-like receptor 9 signaling pathway Source: Reactome
  43. toll-like receptor signaling pathway Source: Reactome
  44. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  45. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  46. 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.
SignaLinkiP45984.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase 9 (EC:2.7.11.24)
Short name:
MAP kinase 9
Short name:
MAPK 9
Alternative name(s):
JNK-55
Stress-activated protein kinase 1a
Short name:
SAPK1a
Stress-activated protein kinase JNK2
c-Jun N-terminal kinase 2
Gene namesi
Name:MAPK9
Synonyms:JNK2, PRKM9, SAPK1A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:6886. MAPK9.

Subcellular locationi

Cytoplasm. Nucleus 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. mitochondrion Source: Ensembl
  3. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30630.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 424424Mitogen-activated protein kinase 9PRO_0000186273Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei183 – 1831Phosphothreonine; by MAP2K71 Publication
Modified residuei185 – 1851Phosphotyrosine; by MAP2K41 Publication

Post-translational modificationi

Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K7 and MAP2K4, which activates the enzyme. Autophosphorylated in vitro.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP45984.
PaxDbiP45984.
PRIDEiP45984.

2D gel databases

REPRODUCTION-2DPAGEP45984.

PTM databases

PhosphoSiteiP45984.

Expressioni

Gene expression databases

ArrayExpressiP45984.
BgeeiP45984.
CleanExiHS_MAPK9.
GenevestigatoriP45984.

Organism-specific databases

HPAiCAB008910.
HPA055483.

Interactioni

Subunit structurei

Interacts with MECOM and DCLK2 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 NFATC4. Interacts with ATF7; the interaction does not phosphorylate ATF7 but acts as a docking site for ATF7-associated partners such as JUN. Interacts with BCL10. Interacts with CTNNB1 and GSK3B.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
STAT3P407633EBI-713586,EBI-518675

Protein-protein interaction databases

BioGridi111587. 71 interactions.
DIPiDIP-270N.
DIP-281N.
IntActiP45984. 36 interactions.
MINTiMINT-1400230.
STRINGi9606.ENSP00000321410.

Structurei

Secondary structure

1
424
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 156
Beta strandi18 – 236
Beta strandi26 – 338
Beta strandi38 – 458
Turni46 – 494
Beta strandi50 – 589
Helixi64 – 7916
Beta strandi88 – 925
Turni98 – 1003
Beta strandi105 – 1095
Beta strandi112 – 1143
Helixi115 – 1184
Helixi125 – 14420
Helixi154 – 1563
Beta strandi157 – 1593
Beta strandi165 – 1673
Turni176 – 1783
Beta strandi180 – 1834
Helixi189 – 1913
Helixi194 – 1974
Helixi206 – 22015
Helixi232 – 24110
Helixi246 – 2505
Helixi254 – 2618
Helixi271 – 2744
Helixi277 – 2793
Helixi286 – 30116
Turni306 – 3083
Helixi312 – 3165
Helixi319 – 3224
Helixi327 – 3304
Turni341 – 3433
Helixi349 – 36012

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3E7OX-ray2.14A/B7-362[»]
3NPCX-ray2.35A/B1-364[»]
ProteinModelPortaliP45984.
SMRiP45984. Positions 7-363.

Miscellaneous databases

EvolutionaryTraceiP45984.

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.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
KOiK04440.
OMAiSSMSTEH.
OrthoDBiEOG7PCJGV.
PhylomeDBiP45984.
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 Alpha-2 (identifier: P45984-1) [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

MSDSKCDSQF YSVQVADSTF TVLKRYQQLK PIGSGAQGIV CAAFDTVLGI    50
NVAVKKLSRP FQNQTHAKRA YRELVLLKCV NHKNIISLLN VFTPQKTLEE 100
FQDVYLVMEL MDANLCQVIH MELDHERMSY LLYQMLCGIK HLHSAGIIHR 150
DLKPSNIVVK SDCTLKILDF GLARTACTNF MMTPYVVTRY YRAPEVILGM 200
GYKENVDIWS VGCIMGELVK GCVIFQGTDH IDQWNKVIEQ LGTPSAEFMK 250
KLQPTVRNYV ENRPKYPGIK FEELFPDWIF PSESERDKIK TSQARDLLSK 300
MLVIDPDKRI SVDEALRHPY ITVWYDPAEA EAPPPQIYDA QLEEREHAIE 350
EWKELIYKEV MDWEERSKNG VVKDQPSDAA VSSNATPSQS SSINDISSMS 400
TEQTLASDTD SSLDASTGPL EGCR 424
Length:424
Mass (Da):48,139
Last modified:January 24, 2006 - v2
Checksum:i9C15DA79981290AF
GO
Isoform Alpha-1 (identifier: P45984-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     378-424: DAAVSSNATPSQSSSINDISSMSTEQTLASDTDSSLDASTGPLEGCR → AQMQQ

Show »
Length:382
Mass (Da):44,051
Checksum:iA1963C01247BDFF4
GO
Isoform Beta-1 (identifier: P45984-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     216-230: GELVKGCVIFQGTDH → AEMVLHKVLFPGRDY
     378-424: DAAVSSNATPSQSSSINDISSMSTEQTLASDTDSSLDASTGPLEGCR → AQMQQ

Show »
Length:382
Mass (Da):44,223
Checksum:i808ED1F85085CB4E
GO
Isoform Beta-2 (identifier: P45984-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     216-230: GELVKGCVIFQGTDH → AEMVLHKVLFPGRDY

Show »
Length:424
Mass (Da):48,311
Checksum:iA1B5FB794F373EB9
GO
Isoform 5 (identifier: P45984-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     230-242: HIDQWNKVIEQLG → RILPRDLGPAMLS
     243-424: Missing.

Show »
Length:242
Mass (Da):27,334
Checksum:iB37D5C58904AE9F1
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti13 – 131V → M in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
VAR_042260
Natural varianti56 – 561K → N in a head & Neck squamous cell carcinoma sample; somatic mutation. 1 Publication
VAR_042261
Natural varianti246 – 2461A → T.1 Publication
Corresponds to variant rs35421153 [ dbSNP | Ensembl ].
VAR_042262
Natural varianti268 – 2681G → A.1 Publication
Corresponds to variant rs35693958 [ dbSNP | Ensembl ].
VAR_025175
Natural varianti366 – 3661R → I.1 Publication
Corresponds to variant rs55736180 [ dbSNP | Ensembl ].
VAR_042263

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei216 – 23015GELVK…QGTDH → AEMVLHKVLFPGRDY in isoform Beta-1 and isoform Beta-2. VSP_004834Add
BLAST
Alternative sequencei230 – 24213HIDQW…IEQLG → RILPRDLGPAMLS in isoform 5. VSP_041908Add
BLAST
Alternative sequencei243 – 424182Missing in isoform 5. VSP_041909Add
BLAST
Alternative sequencei378 – 42447DAAVS…LEGCR → AQMQQ in isoform Alpha-1 and isoform Beta-1. VSP_004835Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti51 – 511N → S in AAA56831. 1 Publication
Sequence conflicti51 – 511N → S in AAC50606. 1 Publication
Sequence conflicti51 – 511N → S in AAC50608. 1 Publication
Sequence conflicti51 – 511N → S in AAC50609. 1 Publication
Sequence conflicti377 – 3771S → P in AAA74740. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L31951 mRNA. Translation: AAA56831.1.
U09759 mRNA. Translation: AAA74740.1.
U34821 mRNA. Translation: AAC50606.1.
U35002 mRNA. Translation: AAC50608.1.
U35003 mRNA. Translation: AAC50609.1.
EU927388 mRNA. Translation: ACH57450.1.
CR536580 mRNA. Translation: CAG38817.1.
AK289638 mRNA. Translation: BAF82327.1.
DQ066599 Genomic DNA. Translation: AAY46156.1.
AB451302 mRNA. Translation: BAG70116.1.
AB451355 mRNA. Translation: BAG70169.1.
AC008610 Genomic DNA. No translation available.
AC104115 Genomic DNA. No translation available.
CH471165 Genomic DNA. Translation: EAW53759.1.
CH471165 Genomic DNA. Translation: EAW53757.1.
CH471165 Genomic DNA. Translation: EAW53758.1.
CH471165 Genomic DNA. Translation: EAW53762.1.
BC032539 mRNA. Translation: AAH32539.1.
CCDSiCCDS43409.1. [P45984-2]
CCDS43410.1. [P45984-3]
CCDS4453.1. [P45984-1]
CCDS4454.1. [P45984-4]
CCDS47356.1. [P45984-5]
PIRiA55480.
S71102.
RefSeqiNP_001128516.1. NM_001135044.1. [P45984-5]
NP_002743.3. NM_002752.4. [P45984-1]
NP_620707.1. NM_139068.2. [P45984-2]
NP_620708.1. NM_139069.2. [P45984-3]
NP_620709.1. NM_139070.2. [P45984-4]
XP_006714954.1. XM_006714891.1. [P45984-1]
UniGeneiHs.484371.

Genome annotation databases

EnsembliENST00000343111; ENSP00000345524; ENSG00000050748. [P45984-3]
ENST00000393360; ENSP00000377028; ENSG00000050748. [P45984-2]
ENST00000425491; ENSP00000397422; ENSG00000050748. [P45984-5]
ENST00000452135; ENSP00000394560; ENSG00000050748. [P45984-1]
ENST00000455781; ENSP00000389338; ENSG00000050748. [P45984-4]
GeneIDi5601.
KEGGihsa:5601.
UCSCiuc003mls.4. human. [P45984-1]
uc003mlt.4. human. [P45984-2]
uc003mlv.4. human. [P45984-3]
uc010jlc.3. human. [P45984-4]
uc011dgx.2. human. [P45984-5]

Polymorphism databases

DMDMi85700366.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L31951 mRNA. Translation: AAA56831.1 .
U09759 mRNA. Translation: AAA74740.1 .
U34821 mRNA. Translation: AAC50606.1 .
U35002 mRNA. Translation: AAC50608.1 .
U35003 mRNA. Translation: AAC50609.1 .
EU927388 mRNA. Translation: ACH57450.1 .
CR536580 mRNA. Translation: CAG38817.1 .
AK289638 mRNA. Translation: BAF82327.1 .
DQ066599 Genomic DNA. Translation: AAY46156.1 .
AB451302 mRNA. Translation: BAG70116.1 .
AB451355 mRNA. Translation: BAG70169.1 .
AC008610 Genomic DNA. No translation available.
AC104115 Genomic DNA. No translation available.
CH471165 Genomic DNA. Translation: EAW53759.1 .
CH471165 Genomic DNA. Translation: EAW53757.1 .
CH471165 Genomic DNA. Translation: EAW53758.1 .
CH471165 Genomic DNA. Translation: EAW53762.1 .
BC032539 mRNA. Translation: AAH32539.1 .
CCDSi CCDS43409.1. [P45984-2 ]
CCDS43410.1. [P45984-3 ]
CCDS4453.1. [P45984-1 ]
CCDS4454.1. [P45984-4 ]
CCDS47356.1. [P45984-5 ]
PIRi A55480.
S71102.
RefSeqi NP_001128516.1. NM_001135044.1. [P45984-5 ]
NP_002743.3. NM_002752.4. [P45984-1 ]
NP_620707.1. NM_139068.2. [P45984-2 ]
NP_620708.1. NM_139069.2. [P45984-3 ]
NP_620709.1. NM_139070.2. [P45984-4 ]
XP_006714954.1. XM_006714891.1. [P45984-1 ]
UniGenei Hs.484371.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3E7O X-ray 2.14 A/B 7-362 [» ]
3NPC X-ray 2.35 A/B 1-364 [» ]
ProteinModelPortali P45984.
SMRi P45984. Positions 7-363.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111587. 71 interactions.
DIPi DIP-270N.
DIP-281N.
IntActi P45984. 36 interactions.
MINTi MINT-1400230.
STRINGi 9606.ENSP00000321410.

Chemistry

BindingDBi P45984.
ChEMBLi CHEMBL4179.
GuidetoPHARMACOLOGYi 1497.

PTM databases

PhosphoSitei P45984.

Polymorphism databases

DMDMi 85700366.

2D gel databases

REPRODUCTION-2DPAGE P45984.

Proteomic databases

MaxQBi P45984.
PaxDbi P45984.
PRIDEi P45984.

Protocols and materials databases

DNASUi 5601.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000343111 ; ENSP00000345524 ; ENSG00000050748 . [P45984-3 ]
ENST00000393360 ; ENSP00000377028 ; ENSG00000050748 . [P45984-2 ]
ENST00000425491 ; ENSP00000397422 ; ENSG00000050748 . [P45984-5 ]
ENST00000452135 ; ENSP00000394560 ; ENSG00000050748 . [P45984-1 ]
ENST00000455781 ; ENSP00000389338 ; ENSG00000050748 . [P45984-4 ]
GeneIDi 5601.
KEGGi hsa:5601.
UCSCi uc003mls.4. human. [P45984-1 ]
uc003mlt.4. human. [P45984-2 ]
uc003mlv.4. human. [P45984-3 ]
uc010jlc.3. human. [P45984-4 ]
uc011dgx.2. human. [P45984-5 ]

Organism-specific databases

CTDi 5601.
GeneCardsi GC05M179595.
HGNCi HGNC:6886. MAPK9.
HPAi CAB008910.
HPA055483.
MIMi 602896. gene.
neXtProti NX_P45984.
PharmGKBi PA30630.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233024.
HOVERGENi HBG014652.
KOi K04440.
OMAi SSMSTEH.
OrthoDBi EOG7PCJGV.
PhylomeDBi P45984.
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 P45984.

Miscellaneous databases

ChiTaRSi MAPK9. human.
EvolutionaryTracei P45984.
GeneWikii Mitogen-activated_protein_kinase_9.
GenomeRNAii 5601.
NextBioi 21752.
PROi P45984.
SOURCEi Search...

Gene expression databases

ArrayExpressi P45984.
Bgeei P45984.
CleanExi HS_MAPK9.
Genevestigatori P45984.

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. "Signal transduction by tumor necrosis factor mediated by JNK protein kinases."
    Sluss H.K., Barrett T., Derijard B., Davis R.J.
    Mol. Cell. Biol. 14:8376-8384(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation."
    Kallunki T., Su B., Tsigelny I., Sluss H.K., Derijard B., Moore G., Davis R., Karin M.
    Genes Dev. 8:2996-3007(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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.
  4. "Molecular cloning and characterization of novel human JNK2 (MAPK9) transcript variants that show different stimulation activities on AP-1."
    Wang P., Xiong Y., Ma C., Shi T., Ma D.
    BMB Rep. 43:738-743(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "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] (ISOFORM BETA-2).
    Tissue: Amygdala.
  7. NIEHS SNPs program
    Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-268.
  8. "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 ALPHA-2).
  9. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "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].
    Tissue: Skin.
  12. Cited for: INTERACTION WITH ATF7, FUNCTION.
  13. "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.
  14. "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.
  15. "The nucleolus as a stress sensor: JNK2 inactivates the transcription factor TIF-IA and down-regulates rRNA synthesis."
    Mayer C., Bierhoff H., Grummt I.
    Genes Dev. 19:933-941(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF RRN3.
  16. "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.
  17. "The CARMA1-Bcl10 signaling complex selectively regulates JNK2 kinase in the T cell receptor-signaling pathway."
    Blonska M., Pappu B.P., Matsumoto R., Li H., Su B., Wang D., Lin X.
    Immunity 26:55-66(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BCL10.
  18. "Cooperation between JNK1 and JNK2 in activation of p53 apoptotic pathway."
    Oleinik N.V., Krupenko N.I., Krupenko S.A.
    Oncogene 26:7222-7230(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF TP53.
  19. "CARMA1-mediated NF-kappaB and JNK activation in lymphocytes."
    Blonska M., Lin X.
    Immunol. Rev. 228:199-211(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "GSK3beta is involved in JNK2-mediated beta-catenin inhibition."
    Hu D., Bi X., Fang W., Han A., Yang W.
    PLoS ONE 4:E6640-E6640(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CTNNB1.
  22. "c-Jun NH2-terminal kinase-2 mediates osmotic stress-induced tight junction disruption in the intestinal epithelium."
    Samak G., Suzuki T., Bhargava A., Rao R.K.
    Am. J. Physiol. 299:G572-G584(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  23. "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.
  24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "The crystal structure of JNK2 reveals conformational flexibility in the MAP kinase insert and indicates its involvement in the regulation of catalytic activity."
    Shaw D., Wang S.M., Villasenor A.G., Tsing S., Walter D., Browner M.F., Barnett J., Kuglstatter A.
    J. Mol. Biol. 383:885-893(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) OF 7-362.
  26. "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] MET-13; ASN-56; THR-246 AND ILE-366.

Entry informationi

Entry nameiMK09_HUMAN
AccessioniPrimary (citable) accession number: P45984
Secondary accession number(s): A8K0S3
, B5BU66, B5M0B4, D3DWQ8, D3DWQ9, Q15708, Q15710, Q15711, Q8N5C5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 24, 2006
Last modified: September 3, 2014
This is version 160 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 5
    Human chromosome 5: 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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