| + |
CSNK1A1 | down-regulates activity 
phosphorylation
|
SNCA |
0.38 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-73795 |
Ser129 |
NEAYEMPsEEGYQDY |
Homo sapiens |
|
| pmid |
sentence |
| 10617630 |
In vitro experiments and two-dimensional phosphopeptide mapping provided further evidence that serine 129 was phosphorylated by ck-1 and ck-2. Moreover, phosphorylation of serine 129 was reduced in vivo upon inhibition of ck-1 or ck-2.| together, these data may indicate that ck-1 and ck-2 are involved in the regulation of neuronal function and one may speculate that phosphorylation of alpha-synuclein could affect its binding to membranes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLK2 | down-regulates activity
phosphorylation
|
SNCA |
0.495 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182155 |
Ser129 |
NEAYEMPsEEGYQDY |
Homo sapiens |
|
| pmid |
sentence |
| 19889641 |
Polo-like kinase 2 (plk2) phosphorylates alpha-synuclein at serine 129 in central nervous system. The membrane association of pd-linked mutant alpha -synuclein, but not wild-type -synuclein, was increased by serine 129 phosphorylation. Pathological serine 129 phosphorylation regulates membrane accumulation of mutant alpha-synuclein. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GRK2 | down-regulates activity
phosphorylation
|
SNCA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-78333 |
Ser129 |
NEAYEMPsEEGYQDY |
Homo sapiens |
|
| pmid |
sentence |
| 10852916 |
We found that grk-mediated phosphorylation inhibits synuclein's interaction with both phospholipids and pld2. These findings suggest that gpcrs may be able to indirectly stimulate pld2 activity via their ability to regulate grk-promoted phosphorylation of synuclein. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GRK5 | down-regulates activity
phosphorylation
|
SNCA |
0.618 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149372 |
Ser129 |
NEAYEMPsEEGYQDY |
Homo sapiens |
|
| pmid |
sentence |
| 16957079 |
Grk5 phosphorylated ser-129 of alpha-synuclein at the plasma membrane and induced translocation of phosphorylated alpha-synuclein to the perikaryal area. Grk5-catalyzed phosphorylation also promoted the formation of soluble oligomers and aggregates of alpha-synuclein. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP2CB | down-regulates activity
dephosphorylation
|
SNCA |
0.278 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248592 |
Ser129 |
NEAYEMPsEEGYQDY |
Homo sapiens |
|
| pmid |
sentence |
| 21562258 |
α-Synuclein (α-Syn) is a key protein that accumulates as hyperphosphorylated aggregates in pathologic hallmark features of Parkinson's disease (PD) and other neurodegenerative disorders. Phosphorylation of this protein at serine 129 is believed to promote its aggregation and neurotoxicity, suggesting that this post-translational modification could be a therapeutic target. Here, we demonstrate that phosphoprotein phosphatase 2A (PP2A) dephosphorylates α-Syn at serine 129 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK2A1 | down-regulates activity
phosphorylation
|
SNCA |
0.486 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-73803 |
Ser129 |
NEAYEMPsEEGYQDY |
Homo sapiens |
|
| pmid |
sentence |
| 10617630 |
In vitro experiments and two-dimensional phosphopeptide mapping provided further evidence that serine 129 was phosphorylated by ck-1 and ck-2. Moreover, phosphorylation of serine 129 was reduced in vivo upon inhibition of ck-1 or ck-2.| together, these data may indicate that ck-1 and ck-2 are involved in the regulation of neuronal function and one may speculate that phosphorylation of alpha-synuclein could affect its binding to membranes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Neurotransmitters release |
| + |
LRRK2 | down-regulates activity
phosphorylation
|
SNCA |
0.651 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249690 |
Ser129 |
NEAYEMPsEEGYQDY |
Homo sapiens |
|
| pmid |
sentence |
| 19576176 |
Here we show that full-length Lrrk2 or fragments containing its kinase domain have a significant capacity to phosphorylate recombinant alpha synuclein (Asyn) at serine 129. Such phosphorylated Asyn is the major component of pathological deposits in PD. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Parkinson |
| + |
PLK3 | down-regulates activity
phosphorylation
|
SNCA |
0.324 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189053 |
Ser129 |
NEAYEMPsEEGYQDY |
Homo sapiens |
|
| pmid |
sentence |
| 19889641 |
Polo-like kinase (plk) family (plk1, plk2, and plk3) phosphorylate alpha-syn and beta-syn specifically at ser-129 and ser-118, respectively. Polo-like kinase 2 (plk2) phosphorylates alpha-synuclein at serine 129 in central nervous system. The membrane association of pd-linked mutant alpha -synuclein, but not wild-type -synuclein, was increased by serine 129 phosphorylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP2CA | down-regulates activity
dephosphorylation
|
SNCA |
0.339 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248635 |
Ser129 |
NEAYEMPsEEGYQDY |
Homo sapiens |
|
| pmid |
sentence |
| 21562258 |
α-Synuclein (α-Syn) is a key protein that accumulates as hyperphosphorylated aggregates in pathologic hallmark features of Parkinson's disease (PD) and other neurodegenerative disorders. Phosphorylation of this protein at serine 129 is believed to promote its aggregation and neurotoxicity, suggesting that this post-translational modification could be a therapeutic target. Here, we demonstrate that phosphoprotein phosphatase 2A (PP2A) dephosphorylates α-Syn at serine 129 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLK1 | down-regulates activity
phosphorylation
|
SNCA |
0.359 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189045 |
Ser129 |
NEAYEMPsEEGYQDY |
Homo sapiens |
|
| pmid |
sentence |
| 19889641 |
Polo-like kinase (plk) family (plk1, plk2, and plk3) phosphorylate alpha-syn and beta-syn specifically at ser-129 and ser-118, respectively. Polo-like kinase 2 (plk2) phosphorylates alpha-synuclein at serine 129 in central nervous system. The membrane association of pd-linked mutant alpha -synuclein, but not wild-type -synuclein, was increased by serine 129 phosphorylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DYRK1A | up-regulates 
phosphorylation
|
SNCA |
0.585 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149393 |
Ser87 |
KTVEGAGsIAAATGF |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 16959772 |
In vitro kinase assay of anti-dyrk1a immunocomplexes demonstrated that dyrk1a could phosphorylate alpha-synuclein at ser-87. Furthermore, aggregates formed by phosphorylated alpha-synuclein have a distinct morphology and are more neurotoxic compared with aggregates composed of unmodified wild type alpha-synuclein. These findings suggest alpha-synuclein inclusion formation regulated by dyrk1a, potentially affecting neuronal cell viability. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK1A1 | up-regulates
phosphorylation
|
SNCA |
0.38 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-73799 |
Ser87 |
KTVEGAGsIAAATGF |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 10617630 |
In vitro experiments and two-dimensional phosphopeptide mapping provided further evidence that serine 129 was phosphorylated by ck-1 and ck-2. Moreover, phosphorylation of serine 129 was reduced in vivo upon inhibition of ck-1 or ck-2. These data demonstrate that alpha-synuclein is constitutively phosphorylated within its c terminus and may indicate that the function of alpha-synuclein is regulated by phosphorylation/dephosphorylation.From these data we conclude that _-synuclein is predominantly phosphorylated at serine residue 129. However, a second serine at position 87 is also used for phosphorylation to some extent. together, these data may indicate that ck-1 and ck-2 are involved in the regulation of neuronal function and one may speculate that phosphorylation of _-synuclein could affect its binding to membranes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK2A1 | up-regulates
phosphorylation
|
SNCA |
0.486 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-73807 |
Ser87 |
KTVEGAGsIAAATGF |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 10617630 |
In vitro experiments and two-dimensional phosphopeptide mapping provided further evidence that serine 129 was phosphorylated by ck-1 and ck-2. Moreover, phosphorylation of serine 129 was reduced in vivo upon inhibition of ck-1 or ck-2. These data demonstrate that alpha-synuclein is constitutively phosphorylated within its c terminus and may indicate that the function of alpha-synuclein is regulated by phosphorylation/dephosphorylation.From these data we conclude that _-synuclein is predominantly phosphorylated at serine residue 129. However, a second serine at position 87 is also used for phosphorylation to some extent. together, these data may indicate that ck-1 and ck-2 are involved in the regulation of neuronal function and one may speculate that phosphorylation of _-synuclein could affect its binding to membranes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Neurotransmitters release |
| + |
SYK | down-regulates
phosphorylation
|
SNCA |
0.506 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-113061 |
Tyr125 |
VDPDNEAyEMPSEEG |
Homo sapiens |
|
| pmid |
sentence |
| 11744621 |
Here, we show that alpha-synuclein (alpha-syn) is an outstanding substrate for the protein tyrosine kinase p72syk (syk), which phosphorylates three tyrosyl residues in its c-terminal domain (y-125, y-133, and y-136), here, we show that _-syn is an outstanding substrate for syk and that once it is tyrosine phosphorylated, it loses the ability to form oligomers. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-113065 |
Tyr133 |
EMPSEEGyQDYEPEA |
Homo sapiens |
|
| pmid |
sentence |
| 11744621 |
Here, we show that alpha-synuclein (alpha-syn) is an outstanding substrate for the protein tyrosine kinase p72syk (syk), which phosphorylates three tyrosyl residues in its c-terminal domain (y-125, y-133, and y-136), here, we show that _-syn is an outstanding substrate for syk and that once it is tyrosine phosphorylated, it loses the ability to form oligomers. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-113069 |
Tyr136 |
SEEGYQDyEPEA |
Homo sapiens |
|
| pmid |
sentence |
| 11744621 |
Here, we show that alpha-synuclein (alpha-syn) is an outstanding substrate for the protein tyrosine kinase p72syk (syk), which phosphorylates three tyrosyl residues in its c-terminal domain (y-125, y-133, and y-136), here, we show that _-syn is an outstanding substrate for syk and that once it is tyrosine phosphorylated, it loses the ability to form oligomers. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Tissue: |
Ovary, Brain |
| + |
PTK2B |
phosphorylation
|
SNCA |
0.32 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249151 |
Tyr125 |
VDPDNEAyEMPSEEG |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 12096713 |
The present report demonstrates that the protein tyrosine kinase Pyk2/RAFTK is involved in cell stress-induced tyrosine phosphorylation of alpha S. Hyperosmotic stress induced tyrosine phosphorylation of alpha S via Pyk2/RAFTK at tyrosine residue 125. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
SNCA | up-regulates 
|
Lewy_body_formation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249700 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12666095 |
A key observation linking alpha-synuclein to PD was the demonstration that it is one of the principal components of Lewy bodies. Furthermore, mutant isoforms of alpha-synuclein more readily oligomerize, and it has been suggested that its tendency to aggregate into misfolded structures may confer toxic properties to the protein. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Parkinson |
| + |
SNCA | down-regulates quantity 
transcriptional regulation
|
CADPS2 |
0.281 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268929 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28647363 |
This approach enabled us to disclose a differential effect of high levels of LRRK2 and aSyn on CADPS2 promoter activity. Specifically, CADPS2 transcriptional activity was enhanced by high cellular levels of LRRK2 and reduced by overexpression of aSyn. Consistently, CADPS2 mRNA levels were diminished in aSyn overexpressing cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKN | down-regulates quantity by destabilization
ubiquitination
|
SNCA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249705 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 12666095 |
Parkin is a protein of 465 amino acids, and its structure includes a ubiquitin homologous domain in its N terminus and two RING finger domains in its C terminus. Molecular studies have determined that parkin is an E3 ubiquitin ligase function, implicating parkin in the ubiquitin-proteasome system, and raising the possibility that mutations in the gene lead to loss or diminished function. Three substrates for the ubiquitin-ligase function of parkin have been identified to date.1. A 22kDa glycosolated form of alpha-synuclei|2. Parkin-associated endothelin receptor-like receptor (Pael-R). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Parkinson |
| + |
SNCA | down-regulates quantity
binding
|
VAMP2 |
0.413 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264104 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 31110017 |
The normal function of the small presynaptic protein α-synuclein (α-syn) is of exceptional interest, not only in the context of neurodegeneration, but also as a cytosolic regulator of neurotransmission. we show that α-syn-VAMP2 interactions are necessary for α-syn-induced synaptic attenuation. Our data connect divergent views and suggest a unified model of α-syn function. the data indicate that α-syn–VAMP2 binding is essential for α-syn function and advocate an “interlocking model” where α-syn multimers on the SV surface interact with VAMP2 on adjacent SVs, helping to maintain physiologic SV clustering. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Neurotransmitters release |
| + |
SNCAIP | up-regulates activity
binding
|
SNCA |
0.794 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272597 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19224863 |
Synphilin-1 interacts in vivo with α-synuclein, and their coexpression promotes the formation of Lewy body-like inclusions |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ROS | up-regulates quantity
|
SNCA |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249699 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16000336 |
The increased concentration of neuronal alpha-synuclein and pigment in normal A9 neurons may already predispose these neurons to precipitate alpha-synuclein around pigment-associated lipid under oxidative conditions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Parkinson |
| + |
SNCA | up-regulates
|
ER stress |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249702 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12666095 |
Furthermore, mutant isoforms of alpha-synuclein more readily oligomerize, and it has been suggested that its tendency to aggregate into misfolded structures may confer toxic properties to the protein. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Parkinson |
3.0
SNCA
- 
- 