Relation Results

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273673	Ser135	EGEKESVsPESLKSS	Rattus norvegicus	PC-12 Cell
pmid	sentence
18046461	JNK phosphorylates Syt 4 at Ser135 in vitro and in vivo.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-184146	Ser140	GKKATQAsQEY	Homo sapiens
pmid	sentence
19234442	The stress-response kinase jnk1, activated by dna damage and initiating a pro-apoptotic program, has been recently shown to translocate into the nucleus upon activation where it phosphorylates substrates including h2ax s139, an event critical for dna degradation mediated by caspase-activated dnase (cad) in apoptotic cells

Publications:

1

Organism:

Homo Sapiens

Tissue:

Kidney

Identifier	Residue	Sequence	Organism
SIGNOR-165763	Ser140	KKEKKQQsIAGSADS	Homo sapiens
pmid	sentence
20510162	We further demonstrated that serine-140 residue of aimp1 was phosphorylated by jnk and alanine mutation of serine-140 suppressed lps-induced cell surface altogether, these results suggest that aimp1 is phosphorylated by jnk through tlr-myd88 pathway and lose the regulatory activity for er retention of gp96expression of gp96.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250123	Ser15	GLGGGAAsPPAASPF	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
12756254	After mapping JNK-dependent JIP1 phosphorylation sites and testing their functional significance, it was observed that phosphorylation by JNK of JIP1 on Thr-103 and not other phosphorylated JIP1 residues is necessary for the regulation of DLK association with JIP1, DLK activation, and subsequent module activation. The data presented corroborates our previous observations using endogenous proteins, demonstrates that JNK binding to JIP1 is necessary for module activation, and shows that activation of JIP1-JNK module dynamics requires phosphorylation of JIP1 on Thr-103 by JNK. and Thr-205 are phosphorylated directly by JNK after JNK binds to JIP1.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250124	Ser197	DRVSRSSsPLKTGEQ	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
12756254	After mapping JNK-dependent JIP1 phosphorylation sites and testing their functional significance, it was observed that phosphorylation by JNK of JIP1 on Thr-103 and not other phosphorylated JIP1 residues is necessary for the regulation of DLK association with JIP1, DLK activation, and subsequent module activation. The data presented corroborates our previous observations using endogenous proteins, demonstrates that JNK binding to JIP1 is necessary for module activation, and shows that activation of JIP1-JNK module dynamics requires phosphorylation of JIP1 on Thr-103 by JNK. and Thr-205 are phosphorylated directly by JNK after JNK binds to JIP1.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250125	Ser29	FLGLHIAsPPNFRLT	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
12756254	After mapping JNK-dependent JIP1 phosphorylation sites and testing their functional significance, it was observed that phosphorylation by JNK of JIP1 on Thr-103 and not other phosphorylated JIP1 residues is necessary for the regulation of DLK association with JIP1, DLK activation, and subsequent module activation. The data presented corroborates our previous observations using endogenous proteins, demonstrates that JNK binding to JIP1 is necessary for module activation, and shows that activation of JIP1-JNK module dynamics requires phosphorylation of JIP1 on Thr-103 by JNK. and Thr-205 are phosphorylated directly by JNK after JNK binds to JIP1.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250126	Ser421	DNCASVSsPYESAIG	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
12756254	After mapping JNK-dependent JIP1 phosphorylation sites and testing their functional significance, it was observed that phosphorylation by JNK of JIP1 on Thr-103 and not other phosphorylated JIP1 residues is necessary for the regulation of DLK association with JIP1, DLK activation, and subsequent module activation. The data presented corroborates our previous observations using endogenous proteins, demonstrates that JNK binding to JIP1 is necessary for module activation, and shows that activation of JIP1-JNK module dynamics requires phosphorylation of JIP1 on Thr-103 by JNK. and Thr-205 are phosphorylated directly by JNK after JNK binds to JIP1.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250127	Thr205	PLKTGEQtPPHEHIC	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
12756254	After mapping JNK-dependent JIP1 phosphorylation sites and testing their functional significance, it was observed that phosphorylation by JNK of JIP1 on Thr-103 and not other phosphorylated JIP1 residues is necessary for the regulation of DLK association with JIP1, DLK activation, and subsequent module activation. The data presented corroborates our previous observations using endogenous proteins, demonstrates that JNK binding to JIP1 is necessary for module activation, and shows that activation of JIP1-JNK module dynamics requires phosphorylation of JIP1 on Thr-103 by JNK. and Thr-205 are phosphorylated directly by JNK after JNK binds to JIP1.

Publications:

5

Organism:

Chlorocebus Aethiops

Pathways:

COVID-19 Causal Network, SARS-CoV ATTACHMENT AND ENTRY, Toll like receptors

Identifier	Residue	Sequence
SIGNOR-275552	Ser157	LNYSDAEsLELEGTE
pmid	sentence
19966288	Through use of different approaches including nano-scale proteomics, we show that activated-JNK, or Phospho-JNK (P-JNK), physically interacts with p45/NF-E2 and phosphorylates its Ser157 residue. This reaction leads to the poly-ubiquitination of p45/NF-E2 at one or more of six Lys residues, one of which being also a sumoylation site, and its degradation through the proteasome pathway.

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-164089	Ser168	SEMKYLGsPITTVPK	Homo sapiens
pmid	sentence
20220133	Here we show that jnk directly phosphorylates cdc25c at serine 168 during g(2) phase of the cell cycle. Cdc25c phosphorylation by jnk negatively regulates its phosphatase activity and thereby cdk1 activation, enabling a timely control of mitosis onset.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-183489	Ser173	PCPQPLRsPSLDNPT	Homo sapiens
pmid	sentence
19153595	In this study, we show that another kinase, c-jun-nh(2)-terminal kinase (jnk), phosphorylates irf3 on its n-terminal serine 173 residuejnk1 can synergize the action of irf3(5d), but not the s173a-irf3(5d) mutant

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250129	Ser178	PPLPGALsPLYGVPE	Rattus norvegicus	NBT-II Cell
pmid	sentence
12853963	JNK1 phosphorylates serine 178 on paxillin, a focal adhesion adaptor, both in vitro and in intact cells. NBT-II cells expressing the Ser 178 --> Ala mutant of paxillin (Pax(S178A)) formed focal adhesions and exhibited the limited movement associated with such contacts in both single-cell-migration and wound-healing assays. In contrast, cells expressing wild-type paxillin moved rapidly and retained close contacts as the predominant adhesion.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-124020	Ser184	FYYEILNsPEKACSL	Homo sapiens
pmid	sentence
15071501	Jnk phosphorylated 14-3-3 at ser-184 and 14-3-3 at ser-186 both in vitro and in vivo, and such phosphorylation reduced the affinity of 14-3-3 proteins for bax

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-124016	Ser186	FHYEIANsPEEAISL	Homo sapiens
pmid	sentence
15071501	Jnk phosphorylates 14-3-3zeta_ at ser-184 and 14-3-3sigma_ at ser-187.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-133875	Ser186	FYYEILNsPEKACSL	Homo sapiens
pmid	sentence
15696159	The c-jun n-terminal kinase (jnk) protein is activated in the cellular response to dna damage and phosphorylates 14-3-3 on ser 184 these results support a role for 14-3-3 proteins in inhibiting c-abl-mediated apoptosis by sequestering c-abl into the cytoplasm. these findings support a model in which jnk phosphorylation of 14-3-3 proteins induces dissociation of the c-abl_14-3-3 complex and thereby targeting of c-abl to the nucleus.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277280	Ser194	KYELFKSsPHSLFPE	Homo sapiens	A-431 Cell
pmid	sentence
27658202	Our data show that phosphorylation of Grb7 protein on the Ser194-Pro motif by c-Jun N-terminal kinase facilitates its binding with the WW domain of Pin1. Subsequently, Grb7 is degraded by the ubiquitin- and proteasome-dependent proteolytic pathway. I

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-277324	Ser198	GKTKTCEsPVSPIKM	in vitro
pmid	sentence
28943315	JNK1-mediated NLRP3 S194 phosphorylation is critical for NLRP3 deubiquitination and facilitates its self-association and the subsequent inflammasome assembly.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-106538	Ser20	PLSQETFsDLWKLLP	Mus musculus	JB6 Cell
pmid	sentence
11896587	Serine 20 phosphorylation of p53 has been shown to be required for the activation of p53 following UV radiation. we determined the role of map kinases in uvb-induced phosphorylation and found that jnks are directly involved in the phosphorylation of p53 at serine 20

Publications:

1

Organism:

Mus Musculus

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-115831	Ser20	PLSQETFsDLWKLLP	Homo sapiens
pmid	sentence
11896587	These findings strongly suggest that jnks are the major direct signaling mediators of uvb-induced p53 phosphorylation at serine 20. furthermore, phosphorylation of p53 at serine 20 by uvb-activated jnks and uvb-induced p53-dependent transcriptional activity were suppressed in jnk1 or jnk2 knockout (jnk1(-/-) or jnk2(-/-)) cells.

Identifier	Residue	Sequence	Organism
SIGNOR-97405	Thr81	APAPAAPtPAAPAPA	Homo sapiens
pmid	sentence
12531896	Wr1065 activates the jnk (c-jun n-terminal kinase), decreases complex formation between p53 and inactive jnk, and phosphorylates p53 at thr-81, a known site of phosphorylation by jnk.

Identifier	Residue	Organism
SIGNOR-59812		Homo sapiens
pmid	sentence
9724739	Activated jnk phosphorylates p53

Publications:

3

Organism:

Homo Sapiens

Pathways:

Glucocorticoid receptor Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276491	Ser205	GDNMLEPsPNMPWFK	Homo sapiens	HEK-293T Cell
pmid	sentence
23608534	Ribosome-associated JNK phosphorylates the eukaryotic translation elongation factor 1A isoform 2 (eEF1A2) on serines 205 and 358 to promote degradation of NSPs by the proteasome.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276492	Ser358	GQISAGYsPVIDCHT	Homo sapiens	HEK-293T Cell
pmid	sentence
23608534	Ribosome-associated JNK phosphorylates the eukaryotic translation elongation factor 1A isoform 2 (eEF1A2) on serines 205 and 358 to promote degradation of NSPs by the proteasome.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-278316	Ser207	ALQQHRPsPELTLSQ	Homo sapiens
pmid	sentence
27518429	The JNK1 protein kinase phosphorylates NEIL1 at S207, S306, and S61.

Identifier	Residue	Sequence	Organism
SIGNOR-278315	Ser306	KSKATQLsPEDRVED	Homo sapiens
pmid	sentence
27518429	These data confirm that NEIL1 can be phosphorylated by JNK1 in vitro at S207, S306, and S61.

Identifier	Residue	Sequence	Organism
SIGNOR-278317	Ser61	KELRLILsPLPGAQP	Homo sapiens
pmid	sentence
27518429	These data confirm that NEIL1 can be phosphorylated by JNK1 in vitro at S207, S306, and S61.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-105247	Ser216	ILDLISEsPIKGRAQ	Homo sapiens
pmid	sentence
11259409	The current studies demonstrate the identification of hnrnp-k as a jnk and erk substrate. The phosphoacceptor sites for jnk and erk on the k protein are different, and indeed, erk phosphorylation results in biological consequences different from those of phosphorylation by jnk (49). Whereas erk phosphorylation on aa 284 and 353 contributes to k protein nuclear export and concomitant inhibition of rna translation (49), phosphorylation by k protein on aa 216 and 353 increases the transcriptional effects of the k protein.

Identifier	Residue	Sequence	Organism
SIGNOR-105251	Ser353	DSAIDTWsPSEWQMA	Homo sapiens
pmid	sentence
11259409	The current studies demonstrate the identification of hnrnp-k as a jnk and erk substrate. The phosphoacceptor sites for jnk and erk on the k protein are different, and indeed, erk phosphorylation results in biological consequences different from those of phosphorylation by jnk (49). Whereas erk phosphorylation on aa 284 and 353 contributes to k protein nuclear export and concomitant inhibition of rna translation (49), phosphorylation by k protein on aa 216 and 353 increases the transcriptional effects of the k protein.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-263087	Ser216	SKSKAPGsPLSSEGA	in vitro
pmid	sentence
15850461	CapZIP was also phosphorylated rapidly by SAPK3/p38γ and SAPK4/p38δ, and even faster and more extensively by JNK1α1, these protein kinases phosphorylating CapZIP in vitro to >3, approx. 2 and >5 mol of phosphate/mol of protein respectively within a few minutes. Following tryptic digestion and C18 chromatography, further sites phosphorylated by JNK1α1 were identified as Ser-68, Ser-83 and Ser-216 (results not shown), and are highlighted in Figure 3.Using this antibody, we showed by immunoblotting that bacterially expressed CapZIP was phosphorylated at Ser-108 by SAPK4/p38δ, JNK1α1 and ERK2 in vitro, as well as by SAPK3/p38γ (results not shown).An important clue to the function of CapZIP and its phosphorylation came from the finding that it binds to the actin-capping protein CapZ (Figure 7A), and that cellular stresses trigger the dissociation of these two proteins (Figure 7B).Such an effect is presumably lost when CapZIP is phosphorylated and dissociates from CapZ.

Identifier	Residue	Sequence	Organism
SIGNOR-263085	Ser68	GQNGEEKsPPNASHP	in vitro
pmid	sentence
15850461	CapZIP was also phosphorylated rapidly by SAPK3/p38γ and SAPK4/p38δ, and even faster and more extensively by JNK1α1, these protein kinases phosphorylating CapZIP in vitro to >3, approx. 2 and >5 mol of phosphate/mol of protein respectively within a few minutes. Following tryptic digestion and C18 chromatography, further sites phosphorylated by JNK1α1 were identified as Ser-68, Ser-83 and Ser-216 (results not shown), and are highlighted in Figure 3.Using this antibody, we showed by immunoblotting that bacterially expressed CapZIP was phosphorylated at Ser-108 by SAPK4/p38δ, JNK1α1 and ERK2 in vitro, as well as by SAPK3/p38γ (results not shown).An important clue to the function of CapZIP and its phosphorylation came from the finding that it binds to the actin-capping protein CapZ (Figure 7A), and that cellular stresses trigger the dissociation of these two proteins (Figure 7B).Such an effect is presumably lost when CapZIP is phosphorylated and dissociates from CapZ.

Identifier	Residue	Sequence	Organism
SIGNOR-263086	Ser83	PKFKVKSsPLIEKLQ	in vitro
pmid	sentence
15850461	CapZIP was also phosphorylated rapidly by SAPK3/p38γ and SAPK4/p38δ, and even faster and more extensively by JNK1α1, these protein kinases phosphorylating CapZIP in vitro to >3, approx. 2 and >5 mol of phosphate/mol of protein respectively within a few minutes. Following tryptic digestion and C18 chromatography, further sites phosphorylated by JNK1α1 were identified as Ser-68, Ser-83 and Ser-216 (results not shown), and are highlighted in Figure 3.Using this antibody, we showed by immunoblotting that bacterially expressed CapZIP was phosphorylated at Ser-108 by SAPK4/p38δ, JNK1α1 and ERK2 in vitro, as well as by SAPK3/p38γ (results not shown).An important clue to the function of CapZIP and its phosphorylation came from the finding that it binds to the actin-capping protein CapZ (Figure 7A), and that cellular stresses trigger the dissociation of these two proteins (Figure 7B).Such an effect is presumably lost when CapZIP is phosphorylated and dissociates from CapZ.

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-105766	Ser216	ILDLISEsPIKGRAQ	Homo sapiens
pmid	sentence
11259409	The current studies demonstrate the identification of hnrnp-k as a jnk and erk substrate. The phosphoacceptor sites for jnk and erk on the k protein are different, and indeed, erk phosphorylation results in biological consequences different from those of phosphorylation by jnk (49). Whereas erk phosphorylation on aa 284 and 353 contributes to k protein nuclear export and concomitant inhibition of rna translation (49), phosphorylation by k protein on aa 216 and 353 increases the transcriptional effects of the k protein.

Identifier	Residue	Sequence	Organism
SIGNOR-105770	Ser353	DSAIDTWsPSEWQMA	Homo sapiens
pmid	sentence
11259409	The current studies demonstrate the identification of hnrnp-k as a jnk and erk substrate. The phosphoacceptor sites for jnk and erk on the k protein are different, and indeed, erk phosphorylation results in biological consequences different from those of phosphorylation by jnk (49). Whereas erk phosphorylation on aa 284 and 353 contributes to k protein nuclear export and concomitant inhibition of rna translation (49), phosphorylation by k protein on aa 216 and 353 increases the transcriptional effects of the k protein.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-93558	Ser226	IDENCLLsPLAGEDD	Homo sapiens
pmid	sentence
12351702	Taken together, these findings suggest that jnk-mediated phosphorylation of the gr-ser226 enhances gr nuclear export and may contribute to termination of gr-mediated transcription.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-245323	Ser240	RRVSGNNsPSLSNGG	Homo sapiens	HEK-293 Cell
pmid	sentence
16446428	Itch undergoes JNK1-mediated phosphorylation that greatly enhances its enzymatic activity. To investigate how phosphorylation activates an E3 Ub ligase we have identified the JNK1 phosphorylation sites within Itch as S199, S232, and T222

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249580	Ser273	RPASVNGsPSATSES	Homo sapiens	HEK-293 Cell
pmid	sentence
16446428	Itch undergoes JNK1-mediated phosphorylation that greatly enhances its enzymatic activity. To investigate how phosphorylation activates an E3 Ub ligase we have identified the JNK1 phosphorylation sites within Itch as S199, S232, and T222

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249579	Thr263	PSRPPPPtPRRPASV	Homo sapiens	HEK-293 Cell
pmid	sentence
16446428	Itch undergoes JNK1-mediated phosphorylation that greatly enhances its enzymatic activity. To investigate how phosphorylation activates an E3 Ub ligase we have identified the JNK1 phosphorylation sites within Itch as S199, S232, and T222

Identifier	Residue	Organism	Cell Line
SIGNOR-245315		Mus musculus	Helper T-lymphocyte
pmid	sentence
15358865	Activation of the Jun amino-terminal kinase (JNK) mitogen-activated protein kinase cascade after T cell stimulation accelerated degradation of c-Jun and JunB through phosphorylation-dependent activation of the E3 ligase Itch.

Identifier	Residue	Organism	Cell Line
SIGNOR-245310		Mus musculus	Hepatocyte
pmid	sentence
16469705	This is not due to direct c-FLIP phosphorylation but depends on JNK-mediated phosphorylation and activation of the E3 ubiquitin ligase Itch,

Publications:

5

Organism:

Homo Sapiens, Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-145297	Ser260	NMGLNPSsPNDPVTN	Homo sapiens
pmid	sentence
16551633	Under stress conditions, hyperphosphorylated by activated jnk on ser-56, ser-70, thr-82 and ser-260. These findings indicate that inflammation-mediated cell signaling leads to rapid and profound reductions in nuclear rxralpha levels, via a multistep, jnk-dependent mechanism involving ser260, nuclear export, and proteasomal degradation.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-274138	Ser27	HMAEVNASPLKHFVT	Homo sapiens	U2-OS Cell
pmid	sentence
22748923	We demonstrate that a critical component of the mitochondrial fusion apparatus, the mitofusin Mfn2, is a target for phosphorylation in response to a variety of cellular stresses. We provide direct evidence that JNK mediates this phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-162314	Ser27	ADREAASsPAGEPLR	Homo sapiens
pmid	sentence
20027304	Human sirt1 was phosphorylated by jnk1 on three sites: ser27, ser47, and thr530 and this phosphorylation of sirt1 increased its nuclear localization and enzymatic activity. Surprisingly, jnk1 phosphorylation of sirt1 showed substrate specificity resulting in deacetylation of histone h3, but not p53.

Identifier	Residue	Sequence	Organism
SIGNOR-162318	Ser47	DGPGLERsPGEPGGA	Homo sapiens
pmid	sentence
20027304	Human sirt1 was phosphorylated by jnk1 on three sites: ser27, ser47, and thr530 and this phosphorylation of sirt1 increased its nuclear localization and enzymatic activity. Surprisingly, jnk1 phosphorylation of sirt1 showed substrate specificity resulting in deacetylation of histone h3, but not p53.

Identifier	Residue	Sequence	Organism
SIGNOR-162322	Thr530	YLSELPPtPLHVSED	Homo sapiens
pmid	sentence
20027304	Human sirt1 was phosphorylated by jnk1 on three sites: ser27, ser47, and thr530 and this phosphorylation of sirt1 increased its nuclear localization and enzymatic activity. Surprisingly, jnk1 phosphorylation of sirt1 showed substrate specificity resulting in deacetylation of histone h3, but not p53.

Publications:

3

Organism:

Homo Sapiens

Pathways:

EGFR Signaling, SAPK/JNK Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-198984	Ser301	DAVLPEQsPGDFDFN	Homo sapiens
pmid	sentence
22966201	Identification of 4e-t phosphorylation sites regulated by jnk. identification of these residues as phosphorylation sites (ser301, ser374, ser513, ser587, ser693, and ser752) was obtained by ms/ms sequencing, these results demonstrate that jnk activity is required to stimulate the assembly of pbs in response to oxidative stress.

Identifier	Residue	Sequence	Organism
SIGNOR-198988	Ser374	GLEQAILsPGQNSGN	Homo sapiens
pmid	sentence
22966201	Identification of 4e-t phosphorylation sites regulated by jnk. identification of these residues as phosphorylation sites (ser301, ser374, ser513, ser587, ser693, and ser752) was obtained by ms/ms sequencing, these results demonstrate that jnk activity is required to stimulate the assembly of pbs in response to oxidative stress.

Identifier	Residue	Sequence	Organism
SIGNOR-198992	Ser513	NLESHLMsPAEIPGQ	Homo sapiens
pmid	sentence
22966201	Identification of 4e-t phosphorylation sites regulated by jnk. identification of these residues as phosphorylation sites (ser301, ser374, ser513, ser587, ser693, and ser752) was obtained by ms/ms sequencing, these results demonstrate that jnk activity is required to stimulate the assembly of pbs in response to oxidative stress.

Identifier	Residue	Sequence	Organism
SIGNOR-198996	Ser587	YLRPRIPsPIGFTPG	Homo sapiens
pmid	sentence
22966201	Identification of 4e-t phosphorylation sites regulated by jnk. identification of these residues as phosphorylation sites (ser301, ser374, ser513, ser587, ser693, and ser752) was obtained by ms/ms sequencing, these results demonstrate that jnk activity is required to stimulate the assembly of pbs in response to oxidative stress.

Identifier	Residue	Sequence	Organism
SIGNOR-199000	Ser693	ASITSMLsPSFTPTS	Homo sapiens
pmid	sentence
22966201	Identification of 4e-t phosphorylation sites regulated by jnk. identification of these residues as phosphorylation sites (ser301, ser374, ser513, ser587, ser693, and ser752) was obtained by ms/ms sequencing, these results demonstrate that jnk activity is required to stimulate the assembly of pbs in response to oxidative stress.

Identifier	Residue	Sequence	Organism
SIGNOR-199004	Ser752	PSADRDSsPTTNSKL	Homo sapiens
pmid	sentence
22966201	Identification of 4e-t phosphorylation sites regulated by jnk. identification of these residues as phosphorylation sites (ser301, ser374, ser513, ser587, ser693, and ser752) was obtained by ms/ms sequencing, these results demonstrate that jnk activity is required to stimulate the assembly of pbs in response to oxidative stress.

Publications:

6

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-96936	Ser307	TRRSRTEsITATSPA	Homo sapiens
pmid	sentence
12510059	Insulin also activates jnk, erk, pkc and mtor, which induce the phosphorylation of irs1 on serine residues 307, 612 and 632 and inhibit its functions. Our results indicate that the insulin-stimulated degradation of irs-1 via the phosphatidylinositol 3-kinase pathway is in part dependent upon the ser(312) phosphorylation of irs-1.

Identifier	Residue	Sequence	Organism
SIGNOR-118857	Ser307	TRRSRTEsITATSPA	Homo sapiens
pmid	sentence
14579029	Insulin also activates jnk, erk, pkc and mtor, which induce the phosphorylation of irs1 on serine residues 307, 612 and 632 and inhibit its functions. Our results indicate that the insulin-stimulated degradation of irs-1 via the phosphatidylinositol 3-kinase pathway is in part dependent upon the ser(312) phosphorylation of irs-1.

Identifier	Residue	Sequence	Organism
SIGNOR-180532	Ser312	TESITATsPASMVGG	Homo sapiens
pmid	sentence
18728222	Insulin also activates jnk, erk, pkc and mtor, which induce the phosphorylation of irs1 on serine residues 307, 612 and 632 and inhibit its functions. Our results indicate that the insulin-stimulated degradation of irs-1 via the phosphatidylinositol 3-kinase pathway is in part dependent upon the ser(312) phosphorylation of irs-1.

Identifier	Residue	Sequence	Organism
SIGNOR-118861	Ser315	ITATSPAsMVGGKPG	Homo sapiens
pmid	sentence
14579029	Insulin also activates jnk, erk, pkc and mtor, which induce the phosphorylation of irs1 on serine residues 307, 612 and 632 and inhibit its functions. Our results indicate that the insulin-stimulated degradation of irs-1 via the phosphatidylinositol 3-kinase pathway is in part dependent upon the ser(312) phosphorylation of irs-1.

Identifier	Residue	Sequence	Organism
SIGNOR-96940	Ser315	ITATSPAsMVGGKPG	Homo sapiens
pmid	sentence
12510059	Insulin also activates jnk, erk, pkc and mtor, which induce the phosphorylation of irs1 on serine residues 307, 612 and 632 and inhibit its functions. Our results indicate that the insulin-stimulated degradation of irs-1 via the phosphatidylinositol 3-kinase pathway is in part dependent upon the ser(312) phosphorylation of irs-1.

Publications:

5

Organism:

Homo Sapiens

Tissue:

Muscle, Skeletal Muscle

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236591	Ser312	TESITATsPASMVGG	Rattus norvegicus	H4-II-E-C3 Cell
pmid	sentence
12510059	Modulation of insulin-stimulated degradation of human insulin receptor substrate-1 by Serine 312 phosphorylationOne of the specific Ser phosphorylation sites in IRS-1 that has been proposed to negatively modulate the insulin signal is Ser312 (numbered according to the human sequence). Prior studies have demonstrated that IRS-1 associates with and is phosphorylated by JNK in vitro on Ser312

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250119	Ser363	DTEGRPPsPPPTSTP	Homo sapiens	HeLa Cell
pmid	sentence
10747973	JNK is activated by heat shock and phosphorylates HSF-1 on serine 363. JNK Phosphorylation of HSF-1 Leads to Reduction in Its Transcriptional Activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-166694	Ser38	SVPEFPLsPPKKKDL	Homo sapiens
pmid	sentence
20630875	Involved in the regulation of the microtubule (mt) filament system by destabilizing microtubules. Prevents assembly and promotes disassembly of microtubules. Here we show that in response to hyperosmotic stress, jnk phosphorylates a key cytoplasmic microtubule regulatory protein, stathmin (stmn), on conserved ser-25 and ser-38 residues. In in vitro biochemical studies, we identified stmn ser-38 as the critical residue required for efficient phosphorylation by jnk and identified a novel kinase interaction domain in stmn required for recognition by jnk. We revealed that jnk was required for microtubule stabilization in response to hyperosmotic stress.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-44356	Ser383	IHFWSTLsPIAPRSP	Homo sapiens
pmid	sentence
8846788	However, both of these stimuli strongly activate two other mapks, jnk1 and jnk2, and stimulate elk-1 transcriptional activity and phosphorylation jnk phosphorylation sites include ser383 and ser389, the major residues whose phosphorylation is responsible for enhancement of elk-1 trascriptional activity.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236432	Ser389	LSPIAPRsPAKLSFQ	Homo sapiens	HeLa Cell
pmid	sentence
7651411	However, both of these stimuli strongly activate two other mapks, jnk1 and jnk2, and stimulate elk-1 transcriptional activity and phosphorylation jnk phosphorylation sites include ser383 and ser389, the major residues whose phosphorylation is responsible for enhancement of elk-1 trascriptional activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236455	Ser389	LSPIAPRsPAKLSFQ	Homo sapiens	HeLa Cell
pmid	sentence
8846788	We find that the JNKs are the predominant Elk-1 activation domain kinases in extracts of UV-irradiated cells and that immunopurified JNK1/2 phosphorylate Elk-1 on the same major sites recognized by ERK1/2, that potentiate its transcriptional activity.

Publications:

2

Organism:

Homo Sapiens

Pathways:

EGFR Signaling, SAPK/JNK Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276361	Ser391	LRSAAPSsPGSPRPA	Homo sapiens	HeLa Cell
pmid	sentence
21930785	We discovered that human Cdt1, an essential origin licensing protein whose activity must be restricted to G(1) phase, is a substrate of the stress-activated mitogen-activated protein (MAP) kinases p38 and c-Jun N-terminal kinase (JNK). These MAP kinases phosphorylate Cdt1 both during unperturbed G(2) phase and during an acute stress response. Phosphorylation renders Cdt1 resistant to ubiquitin-mediated degradation during S phase and after DNA damage by blocking Cdt1 binding to the Cul4 adaptor, Cdt2.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276360	Ser491	GSCCTIMsPGEMEKH	Homo sapiens	HeLa Cell
pmid	sentence
21930785	We discovered that human Cdt1, an essential origin licensing protein whose activity must be restricted to G(1) phase, is a substrate of the stress-activated mitogen-activated protein (MAP) kinases p38 and c-Jun N-terminal kinase (JNK). These MAP kinases phosphorylate Cdt1 both during unperturbed G(2) phase and during an acute stress response. Phosphorylation renders Cdt1 resistant to ubiquitin-mediated degradation during S phase and after DNA damage by blocking Cdt1 binding to the Cul4 adaptor, Cdt2.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-149721	Ser422	AHPPHAPsPGQTVKP	Homo sapiens	Lung Cancer Cell
pmid	sentence
16984892	In this study, we found that c-jun nh2-terminal kinase 1 activation triggered ctbp phosphorylation on ser-422 and subsequent degradation,

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, EGFR Signaling, FLT3-ITD in AML, WNT Signaling, WNT/FLT3

Identifier	Residue	Sequence
SIGNOR-275550	Ser455	TKPTLPPsPLMAARR
pmid	sentence
28092672	Furthermore, we identify that BPGAP1 (a BCH domain-containing, Cdc42GAP-like Rho GTPase-activating protein) promotes MEK partner 1 (MP1)-induced ERK activation on late endosome through scaffolding MP1/MEK1 complex. This regulatory function requires phosphorylation of BPGAP1 by JNK at its C terminal tail (Ser424) to unlock its autoinhibitory conformation.

Publications:

1

Identifier	Residue	Sequence
SIGNOR-275554	Ser548	AAREMLHsPLPCTGG
pmid	sentence
30333228	C-Jun N-terminal kinase (JNK)-mediated phosphorylation of SARM1 regulates NAD+ cleavage activity to inhibit mitochondrial respiration\|Here, we report that NAD+ cleavage activity of SARM1 is regulated by its own phosphorylation at serine 548. The phosphorylation of SARM1 was mediated by c-jun N-terminal kinase (JNK) under oxidative stress conditions, resulting in inhibition of mitochondrial respiration concomitant with enhanced activity of NAD+ cleavage. Nonphosphorylatable mutation of Ser-548 or treatment with a JNK inhibitor decreased SARM1 activity.

Publications:

1

Pathways:

Toll like receptors

Identifier	Residue	Sequence	Organism
SIGNOR-96944	Ser616	DDGYMPMsPGVAPVP	Homo sapiens
pmid	sentence
12510059	Insulin also activates jnk, erk, pkc and mtor, which induce the phosphorylation of irs1 on serine residues 307, 612 and 632 and inhibit its functions. Our results indicate that the insulin-stimulated degradation of irs-1 via the phosphatidylinositol 3-kinase pathway is in part dependent upon the ser(312) phosphorylation of irs-1.

Identifier	Residue	Sequence	Organism
SIGNOR-96948	Ser636	SGDYMPMsPKSVSAP	Homo sapiens
pmid	sentence
12510059	Insulin also activates jnk, erk, pkc and mtor, which induce the phosphorylation of irs1 on serine residues 307, 612 and 632 and inhibit its functions. Our results indicate that the insulin-stimulated degradation of irs-1 via the phosphatidylinositol 3-kinase pathway is in part dependent upon the ser(312) phosphorylation of irs-1.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236018	Ser62	LLPTPPLsPSRRSGL	Homo sapiens	HEK-293 Cell, HeLa Cell
pmid	sentence
10551811	The jnk pathway is selectively involved in the c-myc-mediated apoptosis and that the apoptotic function of c-myc is directly regulated by jnk pathway through phosphorylation at ser-62 and ser-71.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236384	Ser71	SRRSGLCsPSYVAVT	Homo sapiens	HEK-293 Cell, HeLa Cell
pmid	sentence
10551811	The jnk pathway is selectively involved in the c-myc-mediated apoptosis and that the apoptotic function of c-myc is directly regulated by jnk pathway through phosphorylation at ser-62 and ser-71.

Publications:

2

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-99219	Ser62	PSWHLADsPAVNGAT	Homo sapiens	Prostate Gland Cancer Cell
pmid	sentence
12633850	By site-directed mutagenesis studies, we have identified that serine 62 is the necessary site for taxol- or 2-me-induced bcl-xl phosphorylation in prostate cancer cells. Further studies with the inhibitor of jun kinase (jnk) and phosphorylation mutant of bcl-xl reveal the augmentative role of jnk-mediated bcl-xl phosphorylation in apoptosis of prostate cancer cells. In summary, our studies suggest that the phosphorylation of bcl-xl by stress response kinase signaling might oppose the anti-apoptotic function of bcl-xl to permit prostate cancer cells to die by apoptosis

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, COVID-19 Causal Network, FLT3-ITD in AML

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252354	Ser63	KNSDLLTsPDVGLLK	Chlorocebus aethiops	COS Cell
pmid	sentence
8137421	The jnk-mediated phosphorylation of both ser63 and ser73 within the transactivation domain of c-jun potentiates its transcriptional activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252355	Ser73	VGLLKLAsPELERLI	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
8137421	JNK1 binds to the c-Jun transactivation domain and phosphorylates it on Ser-63 and Ser-73. The effect on AP-1 transcriptional activity results, in part, from enhanced phosphorylation of the c-Jun NH2-terminal activation domain.

Publications:

2

Organism:

Chlorocebus Aethiops

Pathways:

Acute Myeloid Leukemia, COVID-19 Causal Network, Toll like receptors

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235766	Ser63	KNSDLLTsPDVGLLK	Chlorocebus aethiops	COS Cell
pmid	sentence
8137421	The jnk-mediated phosphorylation of both ser63 and ser73 within the transactivation domain of c-jun potentiates its transcriptional activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250122	Ser73	VGLLKLAsPELERLI	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
8137421	JNK1 binds to the c-Jun transactivation domain and phosphorylates it on Ser-63 and Ser-73. The effect on AP-1 transcriptional activity results, in part, from enhanced phosphorylation of the c-Jun NH2-terminal activation domain.

Publications:

2

Organism:

Chlorocebus Aethiops

Pathways:

Acute Myeloid Leukemia, EGFR Signaling, Glucocorticoid receptor Signaling, SAPK/JNK Signaling, TNF-alpha Signaling, WNT Signaling, WNT/FLT3, WNT Signaling and Myogenesis

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-173417	Ser68	GGGDEPGsPAQGKRG	Homo sapiens	Breast Cancer Cell
pmid	sentence
21502402	Phosphorylation of serine 68 of twist1 by mapks stabilizes twist1 protein and promotes breast cancer cell invasiveness.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-250132	Ser69	GPLAPPAsPGPFATR	Mus musculus
pmid	sentence
15486195	Ser69 can also be phosphorylated by JNK and p38MAPK at least in vitro. Phosphorylation of BimEL on Ser69 promotes its ubiquitination.

Identifier	Residue	Sequence	Organism
SIGNOR-160323	Ser69	GPLAPPAsPGPFATR	Homo sapiens
pmid	sentence
18174237	Constitutive activation of the c-jun n-terminal kinase (jnk) pathway in sup-t1 cells promoted phosphorylation and degradation of bimel via the proteosome.

Publications:

2

Organism:

Mus Musculus, Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-72125	Ser70	RDPVARTsPLQTPAA	Homo sapiens
pmid	sentence
10567572	G(2)/m-phase cells proved more susceptible to death signals, and phosphorylation of bcl-2 appeared to be responsible, as a ser70ala substitution restored resistance to apoptosis. We noted that ask1 and jnk1 were normally activated at g(2)/m phase, and jnk was capable of phosphorylating bcl-2..

Identifier	Residue	Sequence	Organism
SIGNOR-179088	Ser70	RDPVARTsPLQTPAA	Homo sapiens
pmid	sentence
18570871	Together, our findings demonstrate that jnk1-mediated multisite phosphorylation of bcl-2 stimulates starvation-induced autophagy by disrupting the bcl-2/beclin 1 complex.

Publications:

2

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, EGFR Signaling, Macrophage polarization

Identifier	Residue	Sequence	Organism
SIGNOR-170153	Ser707	IPPYQGLsPEESVNV	Homo sapiens
pmid	sentence
21123173	Deactivation of stat6 through serine 707 phosphorylation by jnk.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Macrophage polarization

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235704	Ser727	NTIDLPMsPRTLDSL	Homo sapiens	BEAS-2B Cell
pmid	sentence
23255093	Transfection of the cells with sirna specific for jnk1 revealed that jnk silencing reduced serine727 phosphorylation of stat3,

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-102398	Ser739	EEYETPEsPVPPARS	Homo sapiens
pmid	sentence
12812981	Dentatorubral-pallidoluysian atrophy protein is phosphorylated by c-jun nh2-terminal kinase. serine 734 of the drpla protein is a phospho-acceptor site by jnk. The phosphorylation may be coupled to the activation of a protease. The molecular size of drpla protein detected in the rat brain with the specific phosphopeptide antibody was 150_kda, which was slightly smaller than that expected from the sequence and the results with the human protein. The phosphorylated forms of ha-tagged human drpla gradually disappeared after osmotic treatment,

Publications:

1

Organism:

Homo Sapiens

Tissue:

Brain

Identifier	Residue	Sequence	Organism
SIGNOR-114083	Ser74	TVNQSLLsPLVLEVD	Homo sapiens
pmid	sentence
11788583	Kinase assays showed that c-jun n-terminal kinase (jnk) was also activated with activation kinetics corresponding to that of k8 phosphorylation. Furthermore, k8 was also phosphorylated on ser-73 by jnk in vitro. The ser-73 --> ala-associated filament reorganization defect is rescued by a ser-73 --> asp mutation. Also, disease-causing keratin mutations can modulate keratin phosphorylation and organization, which may affect disease pathogenesis.

Identifier	Residue	Sequence	Organism
SIGNOR-113645	Ser74	TVNQSLLsPLVLEVD	Homo sapiens
pmid	sentence
11781324	Kinase assays showed that c-jun n-terminal kinase (jnk) was also activated with activation kinetics corresponding to that of k8 phosphorylation. Furthermore, k8 was also phosphorylated on ser-73 by jnk in vitro. The ser-73 --> ala-associated filament reorganization defect is rescued by a ser-73 --> asp mutation. Also, disease-causing keratin mutations can modulate keratin phosphorylation and organization, which may affect disease pathogenesis.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250133	Ser77	PGPFATRsPLFIFMR	Mus musculus
pmid	sentence
12818176	Mitochondrially localized JNKs but not their upstream activators MLKs or MKKs phosphorylated BIMEL at Ser65, potentiating its cytotoxicity without altering its subcellular distribution or integration into mitochondrial membranes. JNKs specifically phosphorylate BIMEL at Ser55, 65, and/or 73

Publications:

1

Organism:

Mus Musculus

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-162327	Ser82	SIMQQCDsPHVVKYY	Homo sapiens
pmid	sentence
20028971	C-jun n-terminal kinase enhances mst1-mediated pro-apoptotic signaling through phosphorylation at serine 82.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-179092	Ser87	AAAGPALsPVPPVVH	Homo sapiens
pmid	sentence
18570871	Jnk1-mediated phosphorylation of bcl-2 regulates starvation-induced autophagy.

Identifier	Residue	Sequence	Organism
SIGNOR-48038	Ser87	AAAGPALsPVPPVVH	Homo sapiens
pmid	sentence
10567572	Jnk1-mediated phosphorylation of bcl-2 regulates starvation-induced autophagy.

Publications:

2

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-178930	Ser93	HAGRAVQsPPDTGRR	Homo sapiens
pmid	sentence
18553930	Specific phosphorylation of pp2czeta at ser (92) by stress-activated jnk attenuates its phosphatase activity in cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-149998	Ser95	TSSSSATsPASASFK	Homo sapiens
pmid	sentence
17023523	We also identified the exact phosphorylation site of jnk to be serine 95 at the n terminus of tr3, around which a classical jnk phosphorylation motif exists. Furthermore, we demonstrated that tr3 phosphorylation by jnk coincided with its ubiquitination and degradation, resulting in the loss of its mitogenic activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250120	Thr102	SNGVITTtPTPPGQY	Mus musculus
pmid	sentence
9889198	JunB-control of IL-4 expression is mediated by the phosphorylation of JunB at Thr102 and -104 by JNK MAP kinase. The synergy between c-Maf and JunB can be attributed to cooperative DNA binding, which is facilitated by JunB phosphorylation.

Identifier	Residue	Sequence	Organism
SIGNOR-250121	Thr104	GVITTTPtPPGQYFY	Mus musculus
pmid	sentence
9889198	JunB-control of IL-4 expression is mediated by the phosphorylation of JunB at Thr102 and -104 by JNK MAP kinase. The synergy between c-Maf and JunB can be attributed to cooperative DNA binding, which is facilitated by JunB phosphorylation.

Publications:

2

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250128	Thr103	LIDATGDtPGAEDDE	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
12756254	After mapping JNK-dependent JIP1 phosphorylation sites and testing their functional significance, it was observed that phosphorylation by JNK of JIP1 on Thr-103 and not other phosphorylated JIP1 residues is necessary for the regulation of DLK association with JIP1, DLK activation, and subsequent module activation. The data presented corroborates our previous observations using endogenous proteins, demonstrates that JNK binding to JIP1 is necessary for module activation, and shows that activation of JIP1-JNK module dynamics requires phosphorylation of JIP1 on Thr-103 by JNK. and Thr-205 are phosphorylated directly by JNK after JNK binds to JIP1.

Publications:

1

Organism:

Chlorocebus Aethiops

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-271710	Thr1053	PSSSLPQtPEQEKFL	Homo sapiens	HEK-293 Cell
pmid	sentence
30566428	WDR62 is also negatively regulated by T1053 phosphorylation, leading to the recruitment of F-box and WD repeat domain-containing protein 7 (FBW7) and proteasomal degradation. \|JNK1 can induce the phosphorylation of WDR62 T1053

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-98396	Thr116	SCDKSTQtPSPPCQA	Homo sapiens
pmid	sentence
12591950	Here, we demonstrate that jnk phosphorylates two members of the bh3-only subgroup of bcl2-related proteins (bim and bmf) that are normally sequestered by binding to dynein and myosin v motor complexes. Phosphorylation by jnk causes release from the motor complexes

Identifier	Residue	Organism
SIGNOR-178686		Homo sapiens
pmid	sentence
18498746	Jnk phosphorylates two members of the bh3-only sub of bcl2-related proteins (bim and bmf).

Identifier	Residue	Organism
SIGNOR-98399		Homo sapiens
pmid	sentence
12591950	Jnk phosphorylates two members of the bh3-only sub of bcl2-related proteins (bim and bmf).

Publications:

3

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-179816	Thr163	TDGSLPStPPPAEEE	Homo sapiens	Breast Cancer Cell
pmid	sentence
18676833	Mcl-1 can be rapidly degraded by certain death-inducing signals, but it is able to be readily induced by diverse survival cytokines such as epidermal growth factor, vascular endothelial growth factor, granulocyt-macrophage colony-stimulating factor, and interleukin 3 through phosphatidy-linositol-3-oh kinase/akt, mek/mapk, or janus-activated kinase/stat signaling cascades

Identifier	Residue	Sequence	Organism
SIGNOR-92597	Thr163	TDGSLPStPPPAEEE	Homo sapiens
pmid	sentence
12223490	We found that jnk phosphorylated ser-121 and thr-163 of mcl-1 in response to stimulation with h(2)o(2) and that transfection of unphosphorylatable mcl-1 resulted in an enhanced anti-apoptotic activity in response to stimulation with h(2)o(2). Jnk-dependent phosphorylation and thus inactivation of mcl-1 may be one of the mechanisms through which oxidative stress induces cellular damage.

Publications:

2

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network, SARS-CoV ATTACHMENT AND ENTRY, TNF-alpha Signaling, Toll like receptors

Identifier	Residue	Sequence	Organism
SIGNOR-51199	Thr183	AGTSFMMtPYVVTRY	Homo sapiens
pmid	sentence
9312068	Jnk is activated by jnk-activating kinase 1 (jnkk1), a dual specificity protein kinase that phosphorylates jnk on threonine 183 and tyrosine 185 residues.

Identifier	Residue	Sequence	Organism
SIGNOR-83736	Thr183	AGTSFMMtPYVVTRY	Homo sapiens
pmid	sentence
11062067	Jnk full activation requires the phosphorylation of a threonine and a tyrosine residue in a thr-pro-tyr motif, which can be catalysed by the protein kinases mitogen-activated protein kinase kinase (mkk)4 and mkk7. Mkk7 shows a striking preference for the threonine residue (thr-183).

Identifier	Residue	Sequence	Organism
SIGNOR-51203	Tyr185	TSFMMTPyVVTRYYR	Homo sapiens
pmid	sentence
9312068	Jnk is activated by jnk-activating kinase 1 (jnkk1), a dual specificity protein kinase that phosphorylates jnk on threonine 183 and tyrosine 185 residues.

Publications:

3

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-244982	Thr183	AGTSFMMtPYVVTRY	Homo sapiens	HEK-293 Cell
pmid	sentence
9724739	MKK4/7, in turn, phosphorylates JNK on residues 183 and 185 (1720). Activated JNK phosphorylates its substrates, c-Jun, ATF2, ELK1, and p53

Identifier	Residue	Sequence	Organism
SIGNOR-251419	Tyr185	TSFMMTPyVVTRYYR	in vitro
pmid	sentence
11062067	Stress-activated protein kinase 1 (SAPK1), also called c-Jun N-terminal kinase (JNK), becomes activated in vivo in response to pro-inflammatory cytokines or cellular stresses. Its full activation requires the phosphorylation of a threonine and a tyrosine residue in a Thr-Pro-Tyr motif, which can be catalysed by the protein kinases mitogen-activated protein kinase kinase (MKK)4 and MKK7. Here we report that MKK4 shows a striking preference for the tyrosine residue (Tyr-185), and MKK7 a striking preference for the threonine residue (Thr-183) in three SAPK1/JNK1 isoforms tested (JNK1 alpha 1, JNK2 alpha 2 and JNK3 alpha 1).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249654	Tyr185	TSFMMTPyVVTRYYR	Homo sapiens	HEK-293 Cell
pmid	sentence
9724739	MKK4/7, in turn, phosphorylates JNK on residues 183 and 185 (1720). Activated JNK phosphorylates its substrates, c-Jun, ATF2, ELK1, and p53

Publications:

3

Organism:

Homo Sapiens, In Vitro

Pathways:

COVID-19 Causal Network, EGFR Signaling, Macrophage polarization, SAPK/JNK Signaling, SARS-CoV ATTACHMENT AND ENTRY, TNF-alpha Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-125774	Thr184	PSAPALStPGIRDSA	Homo sapiens
pmid	sentence
15192708	Lat, an adapter protein essential for t-cell signaling, is phosphorylated at its thr 155 by erk in response to t-cell receptor stimulation. Thr 155 phosphorylation reduces the ability of lat to recruit plcgamma1 and slp76, leading to attenuation of subsequent downstream events such as [ca2+]i mobilization and activation of the erk pathway.Mutational analysis revealed that t155 but not t94 or t140 is the site of jnk-mediated phosphorylation (figure 2b). Erk also phosphorylated lat at t155 (figure 2c), whereas p38, which was able to phosphorylate atf2, failed to induce threonine phosphorylation of lat (figure 2d). These results indicate that lat is directly phosphorylated by erk and jnk at the same site, t155.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-134541	Thr265	GQSSAAAtPSTTGTK	Homo sapiens
pmid	sentence
15767678	Phosphoamino acid analysis confirmed that jnk caused thr phosphorylation of jip3 (fig. _(fig.3c).3c). This phosphorylation on thr was markedly decreased when thr266, thr276, and thr287 were replaced with ala. These data indicate that jnk phosphorylated jip3 on thr266, thr276, and thr287 in vitro.

Identifier	Residue	Sequence	Organism
SIGNOR-134545	Thr275	TTGTKSNtPTSSVPS	Homo sapiens
pmid	sentence
15767678	Phosphoamino acid analysis confirmed that jnk caused thr phosphorylation of jip3 (fig. _(fig.3c).3c). This phosphorylation on thr was markedly decreased when thr266, thr276, and thr287 were replaced with ala. These data indicate that jnk phosphorylated jip3 on thr266, thr276, and thr287 in vitro.

Identifier	Residue	Sequence	Organism
SIGNOR-134549	Thr286	SVPSAAVtPLNESLQ	Homo sapiens
pmid	sentence
15767678	Phosphoamino acid analysis confirmed that jnk caused thr phosphorylation of jip3 (fig. _(fig.3c).3c). This phosphorylation on thr was markedly decreased when thr266, thr276, and thr287 were replaced with ala. These data indicate that jnk phosphorylated jip3 on thr266, thr276, and thr287 in vitro.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-184190	Thr278	SVSAATLtPSSQAVT	Homo sapiens
pmid	sentence
19245816	In addition, for mutation of the jnk-1 phosphorylated residues of sp1, namely, sp1(t278/739a) and sp1(t278/739d), the effect of ga on sp1 stability was reversed.

Identifier	Residue	Sequence	Organism
SIGNOR-184194	Thr739	SEGSGTAtPSALITT	Homo sapiens
pmid	sentence
19245816	In addition, for mutation of the jnk-1 phosphorylated residues of sp1, namely, sp1(t278/739a) and sp1(t278/739d), the effect of ga on sp1 stability was reversed.

Publications:

2

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-278445	Thr29	PPKLACRtPSPARPA	Homo sapiens
pmid	sentence
21856198	In this pathway, stress activates JNK1, which phosphorylates Cdt1 on T29, thereby inhibiting the interaction with HBO1, a co-activator of Cdt1 necessary for licensing.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276933	Thr365	CIMLSGEtAKGDYPL	Homo sapiens	HEK-293T Cell
pmid	sentence
26258887	Active JNK1 specifically activates PKM2 but not PKM1. Mechanistically, PARP14 inhibits the pro-apoptotic kinase JNK1, which results in the activation of PKM2 through phosphorylation of Thr365.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252426	Thr450	TAQMITItPPDQDDS	Rattus norvegicus	Cardiomyocyte Cell Line
pmid	sentence
16306447	We report that JNKs are necessary for the reactivation of Akt after ischemic injury. We identified Thr450 of Akt as a residue that is phosphorylated by JNKs, and the phosphorylation status of Thr450 regulates reactivation of Akt after hypoxia, apparently by priming Akt for subsequent phosphorylation by 3-phosphoinositide-dependent protein kinase.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-130381	Thr451	PIPKALGtPVLTPPT	Homo sapiens
pmid	sentence
15538382	Upon treatment of cells with h2o2, the small gtpase ral is activated and this results in a jnk-dependent phosphorylation of foxo4 on threonine 447 and threonine 451. This ral-mediated, jnk-dependent phosphorylation is involved in the nuclear translocation and transcriptional activation of foxo4 after h2o2 treatment.

Identifier	Residue	Sequence	Organism
SIGNOR-130385	Thr455	ALGTPVLtPPTEAAS	Homo sapiens
pmid	sentence
15538382	Upon treatment of cells with h2o2, the small gtpase ral is activated and this results in a jnk-dependent phosphorylation of foxo4 on threonine 447 and threonine 451. This ral-mediated, jnk-dependent phosphorylation is involved in the nuclear translocation and transcriptional activation of foxo4 after h2o2 treatment.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252964	Thr451	PIPKALGtPVLTPPT	Homo sapiens
pmid	sentence
15538382	Upon treatment of cells with h2o2, the small gtpase ral is activated and this results in a jnk-dependent phosphorylation of foxo4 on threonine 447 and threonine 451. This ral-mediated, jnk-dependent phosphorylation is involved in the nuclear translocation and transcriptional activation of foxo4 after h2o2 treatment.

Identifier	Residue	Sequence	Organism
SIGNOR-252965	Thr455	ALGTPVLtPPTEAAS	Homo sapiens
pmid	sentence
15538382	Upon treatment of cells with h2o2, the small gtpase ral is activated and this results in a jnk-dependent phosphorylation of foxo4 on threonine 447 and threonine 451. This ral-mediated, jnk-dependent phosphorylation is involved in the nuclear translocation and transcriptional activation of foxo4 after h2o2 treatment.

Publications:

2

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network, TNF-alpha Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-279076	Thr59	EGYDELQtDGNRSSH	Homo sapiens
pmid	sentence
25077544	(b) Phosphorylation of Bid at Thr59 by JNK1 and JNK2 (in vitro kinase assay).

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-33914	Thr69	SVIVADQtPTPTRFL	Homo sapiens
pmid	sentence
7824938	Activating transcription factor-2 (atf2) was found to be a target of the jnk signal transduction pathway. Atf2 was phosphorylated by jnk on two closely spaced threonine residues within the nh2-terminal activation domain.

Identifier	Residue	Sequence	Organism
SIGNOR-32421	Thr69	SVIVADQtPTPTRFL	Homo sapiens
pmid	sentence
7737130	Stimulation of atf-2-dependent transactivation by genotoxic agents requires the presence of threonines 69 and 71 located in the n-terminal transactivation domain. These sites are the target of p54 and p46 stress-activated protein kinases (sapks) which bind to, and phosphorylate atf-2 in vitro.

Identifier	Residue	Sequence	Organism
SIGNOR-32425	Thr71	IVADQTPtPTRFLKN	Homo sapiens
pmid	sentence
7737130	Stimulation of atf-2-dependent transactivation by genotoxic agents requires the presence of threonines 69 and 71 located in the n-terminal transactivation domain. These sites are the target of p54 and p46 stress-activated protein kinases (sapks) which bind to, and phosphorylate atf-2 in vitro.

Identifier	Residue	Sequence	Organism
SIGNOR-33918	Thr71	IVADQTPtPTRFLKN	Homo sapiens
pmid	sentence
7824938	Activating transcription factor-2 (atf2) was found to be a target of the jnk signal transduction pathway. Atf2 was phosphorylated by jnk on two closely spaced threonine residues within the nh2-terminal activation domain.

Publications:

4

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-72361	Thr69	SRDPVARtSPLQTPA	Homo sapiens
pmid	sentence
10567572	G(2)/m-phase cells proved more susceptible to death signals, and phosphorylation of bcl-2 appeared to be responsible, as a ser70ala substitution restored resistance to apoptosis. We noted that ask1 and jnk1 were normally activated at g(2)/m phase, and jnk was capable of phosphorylating bcl-2..

Identifier	Residue	Sequence	Organism
SIGNOR-179096	Thr69	SRDPVARtSPLQTPA	Homo sapiens
pmid	sentence
18570871	Together, our findings demonstrate that jnk1-mediated multisite phosphorylation of bcl-2 stimulates starvation-induced autophagy by disrupting the bcl-2/beclin 1 complex.

Identifier	Residue	Organism
SIGNOR-72364		Homo sapiens
pmid	sentence
10567572	Jnk was capable of phosphorylating bcl-2. Phosphorylation of bcl-2 inactivates the molecule

Publications:

3

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-122196	Thr736	VEVDPMLtPEERHLN	Homo sapiens
pmid	sentence
14970211	Phosphorylation at the thr(668) residue of app (with respect to the numbering conversion for the app 695 isoform) and the thr(736) residue of aplp2 (with respect to the numbering conversion for the aplp2 763 isoform) in their cytoplasmic domains acts as a molecular switch for their protein-protein interaction and is implicated in neural function(s) and/or alzheimer's disease pathogenesis. Here we demonstrate that both app and aplp2 can be phosphorylated by jnk at the thr(668) and thr(736) residues, respectively, in response to cellular stress.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-117852	Thr743	VEVDAAVtPEERHLS	Homo sapiens	SH-SY5Y Cell
pmid	sentence
12917434	Phosphorylation of amyloid precursor protein at threonine 668 is essential for its copper-responsive trafficking in sh-sy5y neuroblastoma cells. We found that the threonine 668 within the abetapp intracellular domain (aid or elsewhere aicd) is indeed phosphorylated by jnk1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-204679	Thr743	VEVDAAVtPEERHLS	Homo sapiens	SH-SY5Y Cell
pmid	sentence
24610780	Phosphorylation of amyloid precursor protein at threonine 668 is essential for its copper-responsive trafficking in sh-sy5y neuroblastoma cells. We found that the threonine 668 within the abetapp intracellular domain (aid or elsewhere aicd) is indeed phosphorylated by jnk1

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-106542	Thr81	APAPAAPtPAAPAPA	Homo sapiens	HEK-293 Cell
pmid	sentence
11283254	Jnk phosphorylated p53 at t81 in response to dna damage and stress-inducing agents, as determined by phospho-specific antibodies to t81 . Jun NH2-terminal kinase phosphorylation of p53 on Thr-81 is important for p53 stabilization and transcriptional activities in response to stress.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251101	Tyr701	DGPKGTGyIKTELIS	Mus musculus	Embryonic Stem Cell
pmid	sentence
24913968	SP600125 prevented phosphorylation of STAT1 at Tyr701 site [..] Western blot analysis confirmed that blocking p-JNK using SP600125 markedly reduced STAT3 localization in the nucleus and STAT1 phosphorylation

Publications:

1

Organism:

Mus Musculus

Pathways:

EGFR Signaling

Identifier	Residue	Organism
SIGNOR-45791		Homo sapiens
pmid	sentence
9003778	The kinase-inactive mlk-3 failed to activate sapk, demonstraiting that mlk-3 catalytic activity is necessary for the induction of the sapk pathway.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-271718		Mus musculus
pmid	sentence
30566428	In the WT brain, the WDR62 scaffold organizes a protein complex including MEKK3, MKK4/7, and JNK1 to control NPC development during corticogenesis

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Organism	Cell Line
SIGNOR-160326		Homo sapiens	T-lymphocyte, Leukemia Cell
pmid	sentence
18174237	Constitutive activation of the c-jun n-terminal kinase (jnk) pathway in sup-t1 cells promoted phosphorylation and degradation of bimel via the proteosome.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, FLT3-ITD in AML, WNT Signaling, WNT/FLT3, WNT Signaling and Myogenesis

Identifier	Residue	Organism
SIGNOR-199539		Homo sapiens
pmid	sentence
23151663	Planar cell polarity (pcp) signalling triggers activation of the small gtpases rhoa and rac1, which in turn activate rho kinase (rock) and jun-n-terminal kinase (jnk), respectively, leading to actin polymerization and microtubule stabilization.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Organism
SIGNOR-102034		Homo sapiens
pmid	sentence
12807881	Rfp expression in hek 293 cells activated jnk1

Publications:

1

Organism:

Homo Sapiens

Tissue:

Kidney

Identifier	Residue	Organism
SIGNOR-279218		Homo sapiens
pmid	sentence
10075927	JNK1 phosphorylates E2F1 in vitro, and co-transfection of JNK1 reduces the DNA binding activity of E2F1

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279219		Homo sapiens
pmid	sentence
23516355	Therefore, it is likely that p73 recruitment to the \u0394Np73 promoter is mediated by its JNK-1-dependent phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279228		Homo sapiens
pmid	sentence
28701917	In addition, DCX can be phosphorylated by mitogen activated protein kinase 8 (MAPK8 and JNK1) at Thr321, Thr331, and Ser334 sites in humans with corresponding sites at Thr326, Thr336, and Ser339 in mouse.

Identifier	Residue	Organism
SIGNOR-279217		Homo sapiens
pmid	sentence
21477071	DCX phosphorylation by JNK1 is required for glioma suppression.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-260639		Homo sapiens	HEK-293T Cell, Brain
pmid	sentence
17761173	To examine whether GRASP‐1 interacts with MEKK1 and JNK1 in neurons, co‐immunoprecipitation experiments were performed with detergent‐solubilized extracts from cultured cortical neurons. Both antiJNK1 and anti‐MEKK1 antibodies immunoprecipitated GRASP‐1 from neuronal lysates. These results suggest that GRASP‐1 interacts with MEKK1 and JNK1 in neurons. GRASP-1 potently activates JNK pathway signaling, with no effect on ERK signaling. Such JNK pathway activating activity requires binding of GRASP-1 to both JNK and the upstream JNK pathway activator MEKK-1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-118217		Homo sapiens	T-lymphocyte
pmid	sentence
14517246	Jnks directly phosphorylate nuclear factor of activated t-cell (nfat) transcription factors, thus antagonizing the effects of calcium-regulated signaling through the protein phosphatase calcineurin jnk directly regulated nuclear factor of activated t-cell (nfat) activation in culture and in transgenic mice containing an nfat-dependent luciferase reporter.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, FLT3-ITD in AML, WNT Signaling, WNT/FLT3, WNT Signaling and Myogenesis

Identifier	Residue	Organism
SIGNOR-140553		Homo sapiens
pmid	sentence
16172114	Hsp70 inhibited stress-induced jnk activation and jnk with sp600125 or by expression of a dominant negative mutant of jnk-blocked bax translocation as effectively as hsp70 overexpression

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250139
pmid	sentence
11042694	JNK binds to the J box in the middle of the protein, and binding is required for phosphorylation of the adjacent EXport motif. Both the binding and phosphorylation sites (the JEX element) are important for Net export.

Publications:

1

Identifier	Residue	Organism
SIGNOR-70860		Homo sapiens
pmid	sentence
10490659	These experiments demonstrated that 10 different jnk isoforms bound to both jip proteins.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-151428		Homo sapiens
pmid	sentence
17183360	By contrast, after uv stimulation, rela directly induces the expression of pkcdelta, which in turn activates jnk.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-168998		Homo sapiens
pmid	sentence
20974802	We show that several proline-directed mitogen-activated protein kinases (mapks), such as p38, erk1/2, and jnk1 are sufficient and required for the phosphorylation of ppps/tp motifs of lrp6. External stimuli, which control the activity of mapks, such as phorbol esters and fibroblast growth factor 2 (fgf2) control the choice of the lrp6-ppps/tp kinase and regulate the amplitude of lrp6 phosphorylation and wnt/beta-catenin-dependent transcription

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-195414		Homo sapiens
pmid	sentence
22252525	The mechanism by which pak1 induced cancer growth might involve activation of jnk in the non-canonical wnt pathway, frizzled uses galfaq or galfai and gbetagamma dimers to activate phospholipase c (plc), resulting in protein kinase c (pkc) activation and calcium mobilization that regulates the transcription factor nfat, and frizzled also signals through the small gtpases rho and rac to c-jun n-terminal kinase (jnk), which activates the ap1 transcription factor.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Organism
SIGNOR-178655		Homo sapiens
pmid	sentence
18486448	The jip proteins function by aggregating components of a map kinase module (including mlk, mkk7, and jnk) and facilitate signal transmission by the protein kinase cascade. Overexpression of jip1 deactivates the jnk pathway selectively by cytoplasmic retention of jnk and thereby inhibits gene expression mediated by jnk, which occurs in the nucleus

Identifier	Residue	Organism
SIGNOR-70851		Homo sapiens
pmid	sentence
10490659	These experiments demonstrated that 10 different jnk isoforms bound to both jip proteins.

Identifier	Residue	Organism
SIGNOR-64175		Homo sapiens
pmid	sentence
9922370	The jip proteins function by aggregating components of a map kinase module (including mlk, mkk7, and jnk) and facilitate signal transmission by the protein kinase cascade. Overexpression of jip1 deactivates the jnk pathway selectively by cytoplasmic retention of jnk and thereby inhibits gene expression mediated by jnk, which occurs in the nucleus

Identifier	Residue	Organism
SIGNOR-124727		Homo sapiens
pmid	sentence
15141161	The jip proteins function by aggregating components of a map kinase module (including mlk, mkk7, and jnk) and facilitate signal transmission by the protein kinase cascade. Overexpression of jip1 deactivates the jnk pathway selectively by cytoplasmic retention of jnk and thereby inhibits gene expression mediated by jnk, which occurs in the nucleus

Publications:

4

Organism:

Homo Sapiens

Pathways:

Glucocorticoid receptor Signaling

Identifier	Residue	Organism	Cell Line
SIGNOR-249513		Homo sapiens	Macrophage
pmid	sentence
9625767	Il-1 binding to its receptor triggers a cascade of signaling events, including activation of the stress-activated mitogen-activated protein (map) kinases, c-jun nh2-terminal kinase (jnk) and p38 map kinase, as well as transcription factor nuclear factor kappab (nf-kappab

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-251676		Mus musculus
pmid	sentence
11742987	GR-mediated inhibition of c-Jun N-terminal kinase (JNK) activity

Publications:

1

Organism:

Mus Musculus

Pathways:

Identifier	Residue	Organism
SIGNOR-181647		Homo sapiens
pmid	sentence
18922779	Bi-78d3, dose-dependently inhibits the phosphorylation of jnk substrates both in vitro and in cell.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-169007		Homo sapiens	HEK-293 Cell
pmid	sentence
20974802	We show that several proline-directed mitogen-activated protein kinases (mapks), such as p38, erk1/2, and jnk1 are sufficient and required for the phosphorylation of ppps/tp motifs of lrp6. External stimuli, which control the activity of mapks, such as phorbol esters and fibroblast growth factor 2 (fgf2) control the choice of the lrp6-ppps/tp kinase and regulate the amplitude of lrp6 phosphorylation and wnt/beta-catenin-dependent transcription.

Publications:

1

Organism:

Homo Sapiens

Pathways:

WNT Signaling, WNT/FLT3, WNT Signaling and Myogenesis

Identifier	Residue	Organism	Cell Line
SIGNOR-183899		Homo sapiens	Skin Cancer Cell
pmid	sentence
19204086	A kinase assay using gst-myt1 revealed that active jnk1 or jnk3, but not jnk2, phosphorylated myt1 in vitro.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264876
pmid	sentence
30925160	CK1a1, JNK1 and CDK1 had the highest site-specific activity for ORP4L, while CDK1, GSK3a, CK1a1 and GSK3b showed the highest specificity for the site when corrected for background activity with ORP4L-S4A. Because of the complexity of the serine/proline-rich site, we did not determine which serine(s) in ORP4L were phosphorylated by candidate kinases.\|We conclude that phosphorylation of a unique serine/proline motif in the ORD induces a conformation change in ORP4L that enhances interaction with vimentin and cholesterol extraction from membranes.

Publications:

1

Identifier	Residue	Organism
SIGNOR-155205		Homo sapiens
pmid	sentence
17525747	Our studies revealed a novel mechanism in which phosphorylation of jnk2 is mediated by jnk1 before phosphorylation of p53, and then p53 is directly phosphorylated by jnk2 at ser6.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-250116		Homo sapiens	HEK-293 Cell
pmid	sentence
12591950	Activated JNK causes BimL and Bmf phosphorylation in vivo. It is known that UV radiation causes the release of Bim and Bmf from dynein and myosin V motor complexes and that these proteins cause Bax/Bak-dependent apoptosis . The results of this study demonstrate that JNK can engage this apoptotic pathway by phosphorylation of BH3-only proteins, including Bim and Bmf.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-55759		Homo sapiens
pmid	sentence
9482736	Posh activates jnk1 in cos-1 cells.

Publications:

1

Organism:

Homo Sapiens

Pathways:

WNT Signaling, WNT/FLT3, WNT Signaling and Myogenesis

Identifier	Residue	Organism
SIGNOR-189702		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-27756		Homo sapiens
pmid	sentence
9020184	Jnk1 phosphorylation and activation was inhibited by expression of both mkp1 and mkp2

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-144456		Homo sapiens
pmid	sentence
16469705	Here we show that tnfalpha-mediated jnk activation accelerates turnover of the nf-kappab-induced antiapoptotic protein c-flip, an inhibitor of caspase-8. This is not due to direct c-flip phosphorylation but depends on jnk-mediated phosphorylation and activation of the e3 ubiquitin ligase itch, which specifically ubiquitinates c-flip and induces its proteasomal degradation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-190964		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-258974		Homo sapiens
pmid	sentence
8824197	We found that in the human kidney epithelial cell line, 293T, Cdc42 and all Rho proteins, RhoA, RhoB, and RhoC, but not Rac or Ras can induce activation of JNK.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Organism
SIGNOR-179671		Homo sapiens
pmid	sentence
18667433	Wnt5a stimulation induces activation of the c-jun n-terminal kinase jnk at the wound edge in a ror2-dependent manner, and inhibiting jnk activity abrogates wnt5a-induced lamellipodia formation and mtoc reorientation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-258973		Homo sapiens
pmid	sentence
18667433	Additionally, the association of Ror2 with the actin-binding protein filamin A is required for Wnt5a-induced JNK activation and polarized cell migration.

Publications:

1

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network, SARS-CoV ATTACHMENT AND ENTRY

Identifier	Residue	Organism
SIGNOR-118220		Homo sapiens
pmid	sentence
14517246	Jnks directly phosphorylate nuclear factor of activated t-cell (nfat) transcription factors, thus antagonizing the effects of calcium-regulated signaling through the protein phosphatase calcineurin

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-89334		Homo sapiens
pmid	sentence
12058026	Ikap efficiently and specifically enhanced jnk activation induced by ectopic expression of mekk1 and ask1, upstream activators of jnk

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-68986		Homo sapiens
pmid	sentence
10391943	Mkp-5 directly dephosphorylates sapk/jnk and p38 in vitromkp-5 binds to p38 and sapk/jnk, but not to mapk/erk, and inactivates p38 and sapk/jnk

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-152811		Homo sapiens
pmid	sentence
17251915	In the non-canonical wnt pathway, frizzled uses galfaq or galfai and gbetagamma dimers to activate phospholipase c (plc), resulting in protein kinase c (pkc) activation and calcium mobilization that regulates the transcription factor nfat, and frizzled also signals through the small gtpases rho and rac to c-jun n-terminal kinase (jnk), which activates the ap1 transcription factor

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-121940		Homo sapiens
pmid	sentence
14967141	Jnk phosphorylates bad at threonine 201, thereby inhibiting bad association with the antiapoptotic molecule bcl-x(l)

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, COVID-19 Causal Network, FLT3-ITD in AML

Identifier	Residue	Organism
SIGNOR-79489		Homo sapiens
pmid	sentence
10903733	Overexpression of bcma activates jnk

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-134558		Homo sapiens
pmid	sentence
15767678	The c-jun nh2-terminal kinase (jnk)-interacting protein (jip) group of scaffold proteins (jip1, jip2, and jip3) can interact with components of the jnk signaling pathway and potently activate jnk.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-46079		Homo sapiens
pmid	sentence
9020184	Jnk1 phosphorylation and activation was inhibited by expression of both mkp1 and mkp2.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-149367		Homo sapiens
pmid	sentence
17181399	Finally, downregulation of p70 s6 kinase by sirna significantly enhanced the fgf-2-stimulated vegf release and phosphorylation of sapk/jnk.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-258976		Homo sapiens
pmid	sentence
19279717	To date it is not clear whether any genes are transcribed downstream of these two GTPases for non-canonical signaling. The prevailing dogma remains that their primary roles are indeed solely for cytoskeletal modulation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-152808		Homo sapiens
pmid	sentence
17251915	The mechanism by which pak1 induced cancer growth might involve activation of jnk in the non-canonical wnt pathway, frizzled uses galfaq or galfai and gbetagamma dimers to activate phospholipase c (plc), resulting in protein kinase c (pkc) activation and calcium mobilization that regulates the transcription factor nfat, and frizzled also signals through the small gtpases rho and rac to c-jun n-terminal kinase (jnk), which activates the ap1 transcription factor.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, FLT3-ITD in AML, WNT Signaling, WNT/FLT3, WNT Signaling and Myogenesis

Identifier	Residue	Organism
SIGNOR-124012		Homo sapiens
pmid	sentence
15071501	We demonstrate that jnk-mediated phosphorylation of 14-3-3 induces the release of bax from 14-3-3 and triggers its translocation to the mitochondria here we demonstrate that activated jnk promotes bax translocation to mitochondria through phosphorylation of 14-3-3, a cytoplasmic anchor of bax. Phosphorylation of 14-3-3 led to dissociation of bax from this protein.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, COVID-19 Causal Network, SAPK/JNK Signaling, TNF-alpha Signaling

Identifier	Residue	Organism
SIGNOR-111983		Homo sapiens
pmid	sentence
11717429	We report the identification of an anthrapyrazolone series with significant jnk1, -2, and -3 (k(i) = 0.19 microm).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-277150		Homo sapiens
pmid	sentence
24861519	Our data demonstrate MKP-3 has differential substrate preference in astrocytes compared to other cells types, since it preferentially dephosphorylated p-JNK over p-ERK.\|The main findings of our studies are (1) MKP-3 preferentially reduces p-JNK over p-ERK and p-p38 in primary astrocytes; (2) This MAPK modulation pattern in primary astrocytes significantly reduced NO and completely abolished IL-6 and TNF accumulation; and (3) These effects are specifically induced by MKP-3 since block-age of MKP-3 mRNA expression reversed its action on MAPKs and pro-inflammatory mediators in BV-2 microglia cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-43999		Homo sapiens
pmid	sentence
8824585	These results demonstrated that the observed jnk1 activation was from hpk1 and not from other hpkl-associated kinases or from cross-reactive kinases precipitated by anti-hpk1 antibody.

Publications:

1

Organism:

Homo Sapiens

Pathways: