| + |
CSNK2A2 |
phosphorylation
|
SLC18A2 |
0.31 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251038 |
Ser511 |
PIGEDEEsESD |
in vitro |
|
| pmid |
sentence |
| 9045708 |
Purified CKI and CKII phosphorylate the wild-type carboxyl terminus of VMAT2, but not a double mutant with both serines 512 and 514 replaced by alanine. The protein kinase inhibitor CKI-7 and unlabeled GTP both block in vitro phosphorylation by cell homogenates, indicating a role for CKII and possibly CKI in vivo. Both kinases phosphorylate the VMAT2 fusion protein to a much greater extent than a similar fusion protein containing the carboxyl terminus of VMAT1, consistent with differential phosphorylation of the two transporters observed in intact cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251037 |
Ser513 |
GEDEESEsD |
in vitro |
|
| pmid |
sentence |
| 9045708 |
Purified CKI and CKII phosphorylate the wild-type carboxyl terminus of VMAT2, but not a double mutant with both serines 512 and 514 replaced by alanine. The protein kinase inhibitor CKI-7 and unlabeled GTP both block in vitro phosphorylation by cell homogenates, indicating a role for CKII and possibly CKI in vivo. Both kinases phosphorylate the VMAT2 fusion protein to a much greater extent than a similar fusion protein containing the carboxyl terminus of VMAT1, consistent with differential phosphorylation of the two transporters observed in intact cells. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
CSNK2A1 |
phosphorylation
|
SLC18A2 |
0.351 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250953 |
Ser511 |
PIGEDEEsESD |
in vitro |
|
| pmid |
sentence |
| 9045708 |
Purified CKI and CKII phosphorylate the wild-type carboxyl terminus of VMAT2, but not a double mutant with both serines 512 and 514 replaced by alanine. The protein kinase inhibitor CKI-7 and unlabeled GTP both block in vitro phosphorylation by cell homogenates, indicating a role for CKII and possibly CKI in vivo. Both kinases phosphorylate the VMAT2 fusion protein to a much greater extent than a similar fusion protein containing the carboxyl terminus of VMAT1, consistent with differential phosphorylation of the two transporters observed in intact cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250952 |
Ser513 |
GEDEESEsD |
in vitro |
|
| pmid |
sentence |
| 9045708 |
Purified CKI and CKII phosphorylate the wild-type carboxyl terminus of VMAT2, but not a double mutant with both serines 512 and 514 replaced by alanine. The protein kinase inhibitor CKI-7 and unlabeled GTP both block in vitro phosphorylation by cell homogenates, indicating a role for CKII and possibly CKI in vivo. Both kinases phosphorylate the VMAT2 fusion protein to a much greater extent than a similar fusion protein containing the carboxyl terminus of VMAT1, consistent with differential phosphorylation of the two transporters observed in intact cells. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
CSNK1A1 |
phosphorylation
|
SLC18A2 |
0.327 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250794 |
Ser511 |
PIGEDEEsESD |
in vitro |
|
| pmid |
sentence |
| 9045708 |
Purified CKI and CKII phosphorylate the wild-type carboxyl terminus of VMAT2, but not a double mutant with both serines 512 and 514 replaced by alanine. The protein kinase inhibitor CKI-7 and unlabeled GTP both block in vitro phosphorylation by cell homogenates, indicating a role for CKII and possibly CKI in vivo. Both kinases phosphorylate the VMAT2 fusion protein to a much greater extent than a similar fusion protein containing the carboxyl terminus of VMAT1, consistent with differential phosphorylation of the two transporters observed in intact cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250793 |
Ser513 |
GEDEESEsD |
in vitro |
|
| pmid |
sentence |
| 9045708 |
Purified CKI and CKII phosphorylate the wild-type carboxyl terminus of VMAT2, but not a double mutant with both serines 512 and 514 replaced by alanine. The protein kinase inhibitor CKI-7 and unlabeled GTP both block in vitro phosphorylation by cell homogenates, indicating a role for CKII and possibly CKI in vivo. Both kinases phosphorylate the VMAT2 fusion protein to a much greater extent than a similar fusion protein containing the carboxyl terminus of VMAT1, consistent with differential phosphorylation of the two transporters observed in intact cells. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
SLC18A2 | up-regulates activity 
binding
|
BLOC-1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265997 |
|
|
Homo sapiens |
Blood Platelet |
| pmid |
sentence |
| 23805129 |
The multidrug transporter MRP4, a multidrug resistance protein, is found on platelet dense granules and is proposed to transport adenine nucleotides into these granules (Jedlitschky et al., 2004). Uptake of serotonin from platelet cytosol into dense granules is mediated by vesicular monoamine transporter 2 (VMAT2). |VMAT2 also appears to mediate histamine transport into dense granules |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SLC18A2 | up-regulates quantity
relocalization
|
dopamine |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269197 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 30465801 |
Key regulators of transmitter release and the signaling dynamics of dopamine are the plasma membrane reuptake transporter (DAT) and the vesicular monoamine transporter (VMAT2). These proteins serve to remove dopamine molecules from the extracellular and cytosolic space, respectively and both determine the amount of transmitter released from synaptic vesicles. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269190 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 30465801 |
Key regulators of transmitter release and the signaling dynamics of dopamine are the plasma membrane reuptake transporter (DAT) and the vesicular monoamine transporter (VMAT2). These proteins serve to remove dopamine molecules from the extracellular and cytosolic space, respectively and both determine the amount of transmitter released from synaptic vesicles. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ketanserin | down-regulates activity 
chemical inhibition
|
SLC18A2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258494 |
|
|
Homo sapiens |
CV-1 Cell |
| pmid |
sentence |
| 8643547 |
Reserpine and ketanserin are slightly more potent inhibitors of VMAT2-mediated transport than of VMAT1-mediated transport, whereas tetrabenazine binds to and inhibits only VMAT2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
reserpine | down-regulates activity
chemical inhibition
|
SLC18A2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258490 |
|
|
Homo sapiens |
CV-1 Cell |
| pmid |
sentence |
| 8643547 |
Reserpine and ketanserin are slightly more potent inhibitors of VMAT2-mediated transport than of VMAT1-mediated transport, whereas tetrabenazine binds to and inhibits only VMAT2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
tetrabenazine | down-regulates activity
chemical inhibition
|
SLC18A2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258491 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8643547 |
Reserpine and ketanserin are slightly more potent inhibitors of VMAT2-mediated transport than of VMAT1-mediated transport, whereas tetrabenazine binds to and inhibits only VMAT2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
SLC18A2
- 
- 