| + |
CAMK2G | up-regulates activity 
phosphorylation
|
TH |
0.331 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250709 |
Ser19 |
KGFRRAVsELDAKQA |
|
|
| pmid |
sentence |
| 1680128 |
In both isoforms, Ser-40 was found to be phosphorylated by PKA, and Ser-19 and Ser-40 were found to be phosphorylated by CaM-PK II. The putative phosphorylation site generated by alternative splicing (Ser-31) was phosphorylated specifically by CaM-PK II in TH-2 only. | Unlike TH-1, phosphorylation of TH-2 by CaM-PK II resulted in an increase of the Ki value for dopamine. |
|
| Publications: |
1 |
| + |
MAPKAPK2 | up-regulates activity
phosphorylation
|
TH |
0.508 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250149 |
Ser19 |
KGFRRAVsELDAKQA |
in vitro |
|
| pmid |
sentence |
| 11359875 |
MAPKAP-K2 phosphorylates both Ser19 and Ser40 of TH. Tyrosine hydroxylase (TH) has been reported to require binding of 14-3-3 proteins for optimal activation by phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250150 |
Ser40 |
GQGAPGPsLTGSPWP |
in vitro |
|
| pmid |
sentence |
| 11359875 |
MAPKAP-K2 phosphorylates both Ser19 and Ser40 of TH. Tyrosine hydroxylase (TH) has been reported to require binding of 14-3-3 proteins for optimal activation by phosphorylation. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
MAPKAPK5 | up-regulates
phosphorylation
|
TH |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-95479 |
Ser19 |
KGFRRAVsELDAKQA |
Homo sapiens |
|
| pmid |
sentence |
| 12421349 |
Recombinant human tyrosine hydroxylase (hth1) was found to be phosphorylated by mitogen and stress-activated protein kinase 1 (msk1) at ser40 and by p38 regulated/activated kinase (prak) on ser19. Phosphorylation of both ser40 and ser19 induced a high-affinity binding of 14-3-3 proteins, but only the interaction of 14-3-3 with ser19 increased the hth1 activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK2A | up-regulates
phosphorylation
|
TH |
0.259 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-20912 |
Ser19 |
KGFRRAVsELDAKQA |
Homo sapiens |
|
| pmid |
sentence |
| 1680128 |
This increase in ser19 phosphorylation was associated with enhanced th activity and was due, in part, to glutamate-receptor-mediated calcium influx and possibly calcium/calmodulin-dependent protein kinase ii (camkii) activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
RPS6KA3 | up-regulates
phosphorylation
|
TH |
0.271 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-34682 |
Ser40 |
GQGAPGPsLTGSPWP |
Homo sapiens |
|
| pmid |
sentence |
| 7901013 |
Mitogen-activated protein-kinase (map) kinase-activated protein kinases 1 and 2 (mapkap kinase-1, mapkap kinase-2), were found to phosphorylate bacterially expressed human tyrosine hydroxylaserecombinant human tyrosine hydroxylase (hth1) was found to be phosphorylated by mitogen and stress-activated protein kinase 1 (msk1) at ser40 and by p38 regulated/activated kinase (prak) on ser19. Phosphorylation by msk1 induced an increase in vmax |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-95483 |
Ser40 |
GQGAPGPsLTGSPWP |
Homo sapiens |
|
| pmid |
sentence |
| 12421349 |
Mitogen-activated protein-kinase (map) kinase-activated protein kinases 1 and 2 (mapkap kinase-1, mapkap kinase-2), were found to phosphorylate bacterially expressed human tyrosine hydroxylaserecombinant human tyrosine hydroxylase (hth1) was found to be phosphorylated by mitogen and stress-activated protein kinase 1 (msk1) at ser40 and by p38 regulated/activated kinase (prak) on ser19. Phosphorylation by msk1 induced an increase in vmax |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-95487 |
Ser71 |
RFIGRRQsLIEDARK |
Homo sapiens |
|
| pmid |
sentence |
| 12421349 |
Mitogen-activated protein-kinase (map) kinase-activated protein kinases 1 and 2 (mapkap kinase-1, mapkap kinase-2), were found to phosphorylate bacterially expressed human tyrosine hydroxylaserecombinant human tyrosine hydroxylase (hth1) was found to be phosphorylated by mitogen and stress-activated protein kinase 1 (msk1) at ser40 and by p38 regulated/activated kinase (prak) on ser19. Phosphorylation by msk1 induced an increase in vmax |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-34686 |
Ser71 |
RFIGRRQsLIEDARK |
Homo sapiens |
|
| pmid |
sentence |
| 7901013 |
Mitogen-activated protein-kinase (map) kinase-activated protein kinases 1 and 2 (mapkap kinase-1, mapkap kinase-2), were found to phosphorylate bacterially expressed human tyrosine hydroxylaserecombinant human tyrosine hydroxylase (hth1) was found to be phosphorylated by mitogen and stress-activated protein kinase 1 (msk1) at ser40 and by p38 regulated/activated kinase (prak) on ser19. Phosphorylation by msk1 induced an increase in vmax |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
PRKACA | up-regulates activity
phosphorylation
|
TH |
0.363 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250061 |
Ser40 |
GQGAPGPsLTGSPWP |
in vitro |
|
| pmid |
sentence |
| 11359875 |
HTH1 was phosphorylated at Ser40 by PKA. Tyrosine hydroxylase (TH) has been reported to require binding of 14-3-3 proteins for optimal activation by phosphorylation. phosphorylationof hTH1‚4 at Ser40, to a stoichiometry of up to 1.0 molphosphate per mol TH subunit, dramatically increases their binding to 14-3-3 proteins. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
RPS6KA5 | up-regulates
phosphorylation
|
TH |
0.336 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-95491 |
Ser40 |
GQGAPGPsLTGSPWP |
Homo sapiens |
|
| pmid |
sentence |
| 12421349 |
Recombinant human tyrosine hydroxylase (hth1) was found to be phosphorylated by mitogen and stress-activated protein kinase 1 (msk1) at ser40 and by p38 regulated/activated kinase (prak) on ser19. Phosphorylation by msk1 induced an increase in vmax. studies on th from several species suggest that ser40 is the main site involved in direct activation of th |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK3 | up-regulates
phosphorylation
|
TH |
0.488 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-34678 |
Ser62 |
SYTPTPRsPRFIGRR |
Homo sapiens |
|
| pmid |
sentence |
| 7901013 |
In this paper we have studied the phosphorylation and activation of alternatively spliced forms of human th by mapkap kinase-1 , mapkap kinase-2, map kinase, and cam kinase-11 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK1 | up-regulates
phosphorylation
|
TH |
0.445 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-34674 |
Ser62 |
SYTPTPRsPRFIGRR |
Homo sapiens |
|
| pmid |
sentence |
| 7901013 |
Mitogen-activated protein-kinase (map) kinase-activated protein kinases 1 and 2 (mapkap kinase-1, mapkap kinase-2), were found to phosphorylate bacterially expressed human tyrosine hydroxylase in vitro at comparable rates to other proteins thought to be physiological substrates of these protein kinases.The effect on activity of phosphorylating both ser31 and ser40 was not additive. The possible roles of mapkap kinase-1, mapkap kinase-2 and map kinase in the regulation of tyrosine hydroxylase in vivo are discussed. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ARNT | down-regulates quantity by repression 
transcriptional regulation
|
TH |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253701 |
|
|
Mus musculus |
MN-9D Cell |
| pmid |
sentence |
| 17457889 |
Overexpression and siRNA experiments revealed that NPAS1, in concert with ARNT, negatively regulates the expression of TH and that this regulation is mediated by a direct binding of NPAS1 on the TH promoter. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
NPAS1 | down-regulates quantity by repression 
transcriptional regulation
|
TH |
0.256 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253702 |
|
|
Mus musculus |
MN-9D Cell |
| pmid |
sentence |
| 17457889 |
Overexpression and siRNA experiments revealed that NPAS1, in concert with ARNT, negatively regulates the expression of TH and that this regulation is mediated by a direct binding of NPAS1 on the TH promoter. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
SFPQ | down-regulates quantity by repression
transcriptional regulation
|
TH |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271697 |
|
|
|
|
| pmid |
sentence |
| 20938049 |
It has been reported that DJ-1 is a neuroprotective transcriptional co-activator that sequesters a transcriptional co-repressor polypyrimidine tract-binding protein-associated splicing factor (PSF) from the TH gene promoter. |
|
| Publications: |
1 |
| + |
MTA1/DJ1 complex | up-regulates quantity by expression 
transcriptional regulation
|
TH |
0.469 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-239773 |
|
|
Homo sapiens |
SH-SY5Y Cell |
| pmid |
sentence |
| 21368136 |
we found that the MTA1/DJ1 complex is required for optimum stimulation of the TH expression by paired like homeodomain transcription factor (Pitx3) homeodomain transcription factor and that the MTA1/DJ1 complex is recruited to the TH gene chromatin via the direct interaction of MTA1 with Pitx3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Gbeta | up-regulates
phosphorylation
|
TH |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270055 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 7901013 |
In this paper we have studied the phosphorylation and activation of alternatively spliced forms of human th by mapkap kinase-1 , mapkap kinase-2, map kinase, and cam kinase-11 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CTF1 | down-regulates quantity by repression
transcriptional regulation
|
TH |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252219 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12859689 |
CT-1 exerted these effects by decreasing tyrosine hydroxylase, GTP cyclohydrolase (GCH) and NE transporter mRNAs, while IL-6 lowered only GCH mRNA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK5 | up-regulates activity
phosphorylation
|
TH |
0.42 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279022 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15471880 |
In addition, we demonstrate that co-expression of cdk5 and its regulatory activator p35 with TH increases the stability of TH.|We show that cdk5 phosphorylates TH at serine 31 and that this phosphorylation is associated with an increase in total TH activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERK1/2 | up-regulates
phosphorylation
|
TH |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270167 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 7901013 |
In this paper we have studied the phosphorylation and activation of alternatively spliced forms of human th by mapkap kinase-1 , mapkap kinase-2, map kinase, and cam kinase-11 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TH | down-regulates quantity
chemical modification
|
tyrosine |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263990 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| NBK536726 |
Tyrosine produced in the liver is then transported by an active transport mechanism into the dopaminergic neurons within the brain. This is followed by the conversion of L-tyrosine into L-DOPA through hydroxylation at the phenol ring by the enzyme tyrosine hydroxylase (TH). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Catecholamine metabolism |
| + |
TH | up-regulates quantity
chemical modification
|
L-dopa |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263991 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| NBK536726 |
Tyrosine produced in the liver is then transported by an active transport mechanism into the dopaminergic neurons within the brain. This is followed by the conversion of L-tyrosine into L-DOPA through hydroxylation at the phenol ring by the enzyme tyrosine hydroxylase (TH). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Catecholamine metabolism |
4.0
TH
- 
- 