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Protein Page:
JNK2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
JNK2 a protein kinase of the MAPK family that is potently activated by a variety of environmental stresses including UV radiation. Phosphorylates specific transcription factors such as c-Jun and ATF2, mediating immediate-early gene expression. Closely related to JNK1. Both are involved in UV radiation induced apoptosis. Blocks the ubiquitination of tumor suppressor p53, and thus it increases the stability of p53 in nonstressed cells. JNK1 and JNK2 are required for polarized differentiation of T-helper cells into Th1 cells in the mouse. Four alternatively-spliced isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: Kinase, protein; Protein kinase, CMGC; EC 2.7.11.24; Protein kinase, Ser/Thr (non-receptor); CMGC group; MAPK family; MAPK/JNK subfamily; JNK subfamily
Chromosomal Location of Human Ortholog: 5q35
Cellular Component: cytosol; mitochondrion; nucleoplasm
Molecular Function: ATP binding; caspase activator activity; JUN kinase activity; mitogen-activated protein kinase kinase kinase binding; protein binding; transcription factor binding
Biological Process: caspase activation; central nervous system development; JNK cascade; JUN phosphorylation; neurite development; positive regulation of chemokine production; positive regulation of nitric oxide biosynthetic process; positive regulation of nitric-oxide synthase biosynthetic process; positive regulation of prostaglandin biosynthetic process; positive regulation of prostaglandin secretion; positive regulation of protein amino acid phosphorylation; positive regulation of transcription, DNA-dependent; protein amino acid phosphorylation; protein targeting to mitochondrion; regulation of circadian rhythm; regulation of JNK cascade; regulation of protein ubiquitination; regulation of transcription factor activity; release of cytochrome c from mitochondria; response to amine stimulus; response to cadmium ion; response to drug; response to mechanical stimulus; response to stress; response to toxin; rhythmic process
Reference #:  P45984 (UniProtKB)
Gene Symbols: MAPK9
Molecular weight: 48,139 Da
Basal Isoelectric point: 5.41  Predict pI for various phosphorylation states
CST Pathways:  Apoptosis Regulation  |  B Cell Receptor Signaling  |  Death Receptor Signaling  |  ErbB/HER Signaling  |  Inhibition of Apoptosis  |  Insulin Receptor Signaling  |  Mitochondrial Control of Apoptosis  |  NF-kB Signaling  |  Parkinson's Disease  |  SAPK/JNK Signaling Cascades  |  T Cell Receptor Signaling  |  TGF-ß Signaling  |  Toll-Like Receptor Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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JNK2

Protein Structure Not Found.
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Substrate Sequence Logo
Sequence Logo

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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
1 0 S129 ELDHERMSYLLYQML
0 1 S144‑p CGIKHLHsAGIIHRD
0 2 K153‑ub GIIHRDLkPSNIVVK
0 4 K166‑ub VKSDCTLkILDFGLA
0 2 T178‑p GLARTACtNFMMtPy
69 441 T183‑p ACtNFMMtPyVVtRY
70 1450 Y185‑p tNFMMtPyVVtRYYR
0 29 T188‑p MMtPyVVtRYYRAPE
0 1 K236 DHIDQWNKVIEQLGT
0 1 K250‑ac TPSAEFMkKLQPTVR
0 2 K250‑ub TPSAEFMkKLQPTVR
0 1 S292‑p ERDKIKTsQARDLLS
0 1 K353‑ub EHAIEEWkELIyKEV
0 1 Y357‑p EEWkELIyKEVMDWE
1 0 T404‑p SSMSTEQtLAsDTDS
1 0 S407‑p STEQtLAsDTDSSLD
  JNK2 iso2  
S129 ELDHERMSYLLYQML
S144 CGIKHLHSAGIIHRD
K153 GIIHRDLKPSNIVVK
K166 VKSDCTLKILDFGLA
T178 GLARTACTNFMMTPy
T183 ACTNFMMTPyVVTRY
Y185‑p TNFMMTPyVVTRYYR
T188 MMTPyVVTRYYRAPE
K236 DHIDQWNKVIEQLGT
K250 TPSAEFMKKLQPTVR
K250 TPSAEFMKKLQPTVR
S292 ERDKIKTSQARDLLS
K353 EHAIEEWKELIYKEV
Y357 EEWKELIYKEVMDWE
- gap
- gap
  JNK2 iso3  
S129 ELDHERMSYLLYQML
S144 CGIKHLHSAGIIHRD
K153 GIIHRDLKPSNIVVK
K166 VKSDCTLKILDFGLA
T178 GLARTACTNFMMTPY
T183 ACTNFMMTPYVVTRY
Y185 TNFMMTPYVVTRYYR
T188 MMTPYVVTRYYRAPE
K236‑ub DYIDQWNkVIEQLGT
K250 TPSAEFMKKLQPTVR
K250 TPSAEFMKKLQPTVR
S292 ERDKIKTSQARDLLS
K353 EHAIEEWKELIYKEV
Y357 EEWKELIYKEVMDWE
- gap
- gap
  mouse

 
S129‑p ELDHERMsYLLYQML
S144 CGIKHLHSAGIIHRD
K153‑ub GIIHRDLkPSNIVVK
K166‑ub VKSDCTLkILDFGLA
T178 GLARTACTNFMMtPy
T183‑p ACTNFMMtPyVVtRY
Y185‑p TNFMMtPyVVtRYYR
T188‑p MMtPyVVtRYYRAPE
K236 DYIDQWNKVIEQLGT
K250 TPSAEFMKKLQPTVR
K250‑ub TPSAEFMkKLQPTVR
S292 ERDKIKTSQARDLLS
K353 EHAIEEWKELIYKEV
Y357 EEWKELIYKEVMDWE
T403 SSMSTEHTLASDTDS
S406 STEHTLASDTDSSLD
  rat

 
S129 ELDHERMSYLLYQML
S144 CGIKHLHSAGIIHRD
K153 GIIHRDLKPSNIVVK
K166 VKSDCTLKILDFGLA
T178 GLARTACTNFMMtPy
T183‑p ACTNFMMtPyVVTRY
Y185‑p TNFMMtPyVVTRYYR
T188 MMtPyVVTRYYRAPE
K236 DHIDQWNKVIEQLGT
K250 TPSAEFMKKLQPTVR
K250 TPSAEFMKKLQPTVR
S292 ERDKIKTSQARDLLS
K353 EHAIEEWKELIYKEV
Y357 EEWKELIYKEVMDWE
T403 SSMSTEHTLASDTDS
S406 STEHTLASDTDSSLD
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