| + |
MAPK8 | up-regulates 
phosphorylation
|
HNRNPK |
0.38 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| 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 |
Cell Line |
| 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 |
| + |
MAPK8 | up-regulates activity
phosphorylation
|
HNRNPK |
0.38 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| 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 |
Cell Line |
| 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 |
| + |
MAPK10 | up-regulates activity
phosphorylation
|
HNRNPK |
0.345 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250081 |
Ser216 |
ILDLISEsPIKGRAQ |
Homo sapiens |
|
| pmid |
sentence |
| 11259409 |
JNK Phosphorylation of HnRNP K Increases Its Transcriptional Activity. the primary site for JNK phosphorylation consists of serines 216 and 353 on the K protein. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250083 |
Ser353 |
DSAIDTWsPSEWQMA |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11259409 |
JNK Phosphorylation of HnRNP K Increases Its Transcriptional Activity. the primary site for JNK phosphorylation consists of serines 216 and 353 on the K protein. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
JNK | up-regulates
phosphorylation
|
HNRNPK |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-105758 |
Ser216 |
ILDLISEsPIKGRAQ |
Homo sapiens |
|
| pmid |
sentence |
| 11259409 |
Using modified jnk and its atp analogue enables the detection of novel jnk substrates. Among substrates identified using this approach is heterogeneous nuclear ribonucleoprotein k, which is involved in transcription and post-transcriptional mrna metabolism. The newly identified substrate can be phosphorylated by jnk on amino acids 216 and 353, which contribute to heterogeneous nuclear ribonucleoprotein k mediated transcriptional activities. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-105762 |
Ser353 |
DSAIDTWsPSEWQMA |
Homo sapiens |
|
| pmid |
sentence |
| 11259409 |
Using modified jnk and its atp analogue enables the detection of novel jnk substrates. Among substrates identified using this approach is heterogeneous nuclear ribonucleoprotein k, which is involved in transcription and post-transcriptional mrna metabolism. The newly identified substrate can be phosphorylated by jnk on amino acids 216 and 353, which contribute to heterogeneous nuclear ribonucleoprotein k mediated transcriptional activities. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
MAPK3 | down-regulates 
phosphorylation
|
HNRNPK |
0.351 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-145375 |
Ser284 |
RRDYDDMsPRRGPPP |
Homo sapiens |
|
| pmid |
sentence |
| 16564677 |
Erk phosphorylation drives cytoplasmic accumulation of hnrnp-k and inhibition of mrna translation mitogen-activated protein kinase/extracellular-signal-regulated kinase (mapk/erk) efficiently phosphorylates hnrnp-k both in vitro and in vivo at serines 284 and 353. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK3 | down-regulates activity
phosphorylation
|
HNRNPK |
0.351 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-105238 |
Ser284 |
RRDYDDMsPRRGPPP |
Homo sapiens |
|
| pmid |
sentence |
| 11231586 |
Erk phosphorylation drives cytoplasmic accumulation of hnrnp-k and inhibition of mrna translation mitogen-activated protein kinase/extracellular-signal-regulated kinase (mapk/erk) efficiently phosphorylates hnrnp-k both in vitro and in vivo at serines 284 and 353. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK10 | down-regulates activity
phosphorylation
|
HNRNPK |
0.345 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250082 |
Ser284 |
RRDYDDMsPRRGPPP |
|
|
| pmid |
sentence |
| 11231586 |
Mitogen-activated protein kinase/extracellular-signal-regulated kinase (MAPK/ERK) efficiently phosphorylates hnRNP-K both in vitro and in vivo at serines 284 and 353. Our results establish the role of MAPK/ERK in phosphorylation-dependent cellular localization of hnRNP-K, which is required for its ability to silence mRNA translation. |
|
| Publications: |
1 |
| + |
PRKCD |
phosphorylation
|
HNRNPK |
0.35 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260877 |
Ser302 |
GRGGRGGsRARNLPL |
Homo sapiens |
|
| pmid |
sentence |
| 10329716 |
We have shown that PKCδ binds and phosphorylates K protein. These observations broaden the range of K protein interactions. PKCδ targets Ser302, which is located in the middle of what appears to be a highly interactive KI domain |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCD | down-regulates
phosphorylation
|
HNRNPK |
0.35 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-67515 |
Ser302 |
GRGGRGGsRARNLPL |
Homo sapiens |
|
| pmid |
sentence |
| 10329716 |
Ser302 is a major k protein site phosphorylated by pkcdelta in vitrothe ability of pkc_ to inducibly bind and phosphorylate k protein may serve not only to alter the activity of k protein itself, but k protein may also provide an avenue for pkc_ to engage in a cross-talk with other k protein molecular partners in response to specific changes in the extracellular environment |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERK1/2 | up-regulates
phosphorylation
|
HNRNPK |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-105754 |
Ser353 |
DSAIDTWsPSEWQMA |
Homo sapiens |
|
| pmid |
sentence |
| 11259409 |
When subjected to phosphorylation by erk, the most efficient decrease in erk phosphorylation was observed with the s353a mutantamong the mechanisms underlying k protein ability to confer increased transcriptional output are interconversion of duplex and single-stranded dna (59) and association with the c/ebp_ (60), each of which could be better affected by the phosphorylated form of the k protein, which may increase affinity to associated proteins or dna. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SRC | down-regulates
phosphorylation
|
HNRNPK |
0.608 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-88899 |
Tyr225 |
IKGRAQPyDPNFYDE |
Homo sapiens |
|
| pmid |
sentence |
| 12052863 |
We show that hnrnp k and the c-src kinase specifically interact with each other, leading to c-src activation and tyrosine phosphorylation of hnrnp k in vivo and in vitro. c-src-mediated phosphorylation reversibly inhibits the binding of hnrnp k to the differentiation control element (dice) of the lox mrna 3' untranslated region in vitro and specifically derepresses the translation of dice-bearing mrnas in vivo.We confirmed that tyr 230, 234, 236, and 380 are phosphorylated and identified two additional targets of c-src, tyr 72 and tyr 225 (data not shown). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-88903 |
Tyr230 |
QPYDPNFyDETYDYG |
Homo sapiens |
|
| pmid |
sentence |
| 12052863 |
We show that hnrnp k and the c-src kinase specifically interact with each other, leading to c-src activation and tyrosine phosphorylation of hnrnp k in vivo and in vitro. c-src-mediated phosphorylation reversibly inhibits the binding of hnrnp k to the differentiation control element (dice) of the lox mrna 3' untranslated region in vitro and specifically derepresses the translation of dice-bearing mrnas in vivo.We confirmed that tyr 230, 234, 236, and 380 are phosphorylated and identified two additional targets of c-src, tyr 72 and tyr 225 (data not shown). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-88907 |
Tyr234 |
PNFYDETyDYGGFTM |
Homo sapiens |
|
| pmid |
sentence |
| 12052863 |
We show that hnrnp k and the c-src kinase specifically interact with each other, leading to c-src activation and tyrosine phosphorylation of hnrnp k in vivo and in vitro. c-src-mediated phosphorylation reversibly inhibits the binding of hnrnp k to the differentiation control element (dice) of the lox mrna 3' untranslated region in vitro and specifically derepresses the translation of dice-bearing mrnas in vivo.We confirmed that tyr 230, 234, 236, and 380 are phosphorylated and identified two additional targets of c-src, tyr 72 and tyr 225 (data not shown). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-88911 |
Tyr236 |
FYDETYDyGGFTMMF |
Homo sapiens |
|
| pmid |
sentence |
| 12052863 |
We show that hnrnp k and the c-src kinase specifically interact with each other, leading to c-src activation and tyrosine phosphorylation of hnrnp k in vivo and in vitro. c-src-mediated phosphorylation reversibly inhibits the binding of hnrnp k to the differentiation control element (dice) of the lox mrna 3' untranslated region in vitro and specifically derepresses the translation of dice-bearing mrnas in vivo.We confirmed that tyr 230, 234, 236, and 380 are phosphorylated and identified two additional targets of c-src, tyr 72 and tyr 225 (data not shown). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-88915 |
Tyr380 |
YAGGRGSyGDLGGPI |
Homo sapiens |
|
| pmid |
sentence |
| 12052863 |
We show that hnrnp k and the c-src kinase specifically interact with each other, leading to c-src activation and tyrosine phosphorylation of hnrnp k in vivo and in vitro. c-src-mediated phosphorylation reversibly inhibits the binding of hnrnp k to the differentiation control element (dice) of the lox mrna 3' untranslated region in vitro and specifically derepresses the translation of dice-bearing mrnas in vivo.We confirmed that tyr 230, 234, 236, and 380 are phosphorylated and identified two additional targets of c-src, tyr 72 and tyr 225 (data not shown). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-88919 |
Tyr72 |
IKALRTDyNASVSVP |
Homo sapiens |
|
| pmid |
sentence |
| 12052863 |
We show that hnrnp k and the c-src kinase specifically interact with each other, leading to c-src activation and tyrosine phosphorylation of hnrnp k in vivo and in vitro. c-src-mediated phosphorylation reversibly inhibits the binding of hnrnp k to the differentiation control element (dice) of the lox mrna 3' untranslated region in vitro and specifically derepresses the translation of dice-bearing mrnas in vivo.We confirmed that tyr 230, 234, 236, and 380 are phosphorylated and identified two additional targets of c-src, tyr 72 and tyr 225 (data not shown). |
|
| Publications: |
6 |
Organism: |
Homo Sapiens |
3.0
HNRNPK
- 
- 