+ |
CAMK2B | down-regulates quantity by destabilization
phosphorylation
|
GABBR1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277851 |
Ser868 |
ITRGEWQsEAQDTMK |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
37686242 |
ERK1/2 and CaMKIIβ mediated phosphorylation of GABAB1 at serine 867 (S867) and threonine 872 (T872). We found that, in addition to CaMKIIβ, also ERK1/2 is involved in the degradation pathway of GABAB receptors under physiological and ischemic conditions. In contrast to our previous view, CaMKIIβ does not appear to directly phosphorylate S867. Instead, the data support a mechanism in which CaMKIIβ activates ERK1/2, which then phosphorylates S867 and T872 in GABAB1. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277850 |
Thr873 |
WQSEAQDtMKTGSST |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
37686242 |
ERK1/2 and CaMKIIβ mediated phosphorylation of GABAB1 at serine 867 (S867) and threonine 872 (T872). We found that, in addition to CaMKIIβ, also ERK1/2 is involved in the degradation pathway of GABAB receptors under physiological and ischemic conditions. In contrast to our previous view, CaMKIIβ does not appear to directly phosphorylate S867. Instead, the data support a mechanism in which CaMKIIβ activates ERK1/2, which then phosphorylates S867 and T872 in GABAB1. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
ERK1/2 | down-regulates quantity by destabilization
phosphorylation
|
GABBR1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277853 |
Ser868 |
ITRGEWQsEAQDTMK |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
37686242 |
We found that, in addition to CaMKIIβ, also ERK1/2 is involved in the degradation pathway of GABAB receptors under physiological and ischemic conditions. In contrast to our previous view, CaMKIIβ does not appear to directly phosphorylate S867. Instead, the data support a mechanism in which CaMKIIβ activates ERK1/2, which then phosphorylates S867 and T872 in GABAB1. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277852 |
Thr873 |
WQSEAQDtMKTGSST |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
37686242 |
We found that, in addition to CaMKIIβ, also ERK1/2 is involved in the degradation pathway of GABAB receptors under physiological and ischemic conditions. In contrast to our previous view, CaMKIIβ does not appear to directly phosphorylate S867. Instead, the data support a mechanism in which CaMKIIβ activates ERK1/2, which then phosphorylates S867 and T872 in GABAB1. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CAMK2A | down-regulates
phosphorylation
|
GABBR1 |
0.238 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-166846 |
Ser868 |
ITRGEWQsEAQDTMK |
Homo sapiens |
Neuron |
pmid |
sentence |
20643921 |
Nmda-dependent internalization of gabab receptors requires activation of ca2+/calmodulin-dependent protein kinase ii (camkii), which associates with gabab receptors in vivo and phosphorylates serine 867 (s867) in the intracellular c terminus of the gabab1 subunit. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Brain |
+ |
MAPK3 | down-regulates quantity by destabilization
phosphorylation
|
GABBR1 |
0.279 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277854 |
Ser868 |
ITRGEWQsEAQDTMK |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
37686242 |
We found that, in addition to CaMKIIβ, also ERK1/2 is involved in the degradation pathway of GABAB receptors under physiological and ischemic conditions. In contrast to our previous view, CaMKIIβ does not appear to directly phosphorylate S867. Instead, the data support a mechanism in which CaMKIIβ activates ERK1/2, which then phosphorylates S867 and T872 in GABAB1. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277855 |
Thr873 |
WQSEAQDtMKTGSST |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
37686242 |
We found that, in addition to CaMKIIβ, also ERK1/2 is involved in the degradation pathway of GABAB receptors under physiological and ischemic conditions. In contrast to our previous view, CaMKIIβ does not appear to directly phosphorylate S867. Instead, the data support a mechanism in which CaMKIIβ activates ERK1/2, which then phosphorylates S867 and T872 in GABAB1. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
MAPK1 | down-regulates quantity by destabilization
phosphorylation
|
GABBR1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277856 |
Ser868 |
ITRGEWQsEAQDTMK |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
37686242 |
We found that, in addition to CaMKIIβ, also ERK1/2 is involved in the degradation pathway of GABAB receptors under physiological and ischemic conditions. In contrast to our previous view, CaMKIIβ does not appear to directly phosphorylate S867. Instead, the data support a mechanism in which CaMKIIβ activates ERK1/2, which then phosphorylates S867 and T872 in GABAB1. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277857 |
Thr873 |
WQSEAQDtMKTGSST |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
37686242 |
We found that, in addition to CaMKIIβ, also ERK1/2 is involved in the degradation pathway of GABAB receptors under physiological and ischemic conditions. In contrast to our previous view, CaMKIIβ does not appear to directly phosphorylate S867. Instead, the data support a mechanism in which CaMKIIβ activates ERK1/2, which then phosphorylates S867 and T872 in GABAB1. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
GABBR1 | form complex
binding
|
GABA-B receptor |
0.681 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263742 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
9872316 |
Heterodimerization is required for the formation of a functional GABA(B) receptor.|These results indicate that, in vivo, functional brain GABA(B) receptors may be heterodimers composed of GABA(B)R1 and GABA(B)R2. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
JAKMIP1 | up-regulates quantity
|
GABBR1 |
0.535 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260988 |
|
|
Chlorocebus aethiops |
COS Cell |
pmid |
sentence |
14718537 |
Reduction in the Marlin-1 protein levels interferes with the translation, assembly, or stability of GABAB receptors during the maturation of cortical neurons. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
KIF5B | up-regulates activity
relocalization
|
GABBR1 |
0.257 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260990 |
|
|
Mus musculus |
|
pmid |
sentence |
17532644 |
GABABR1 co-immunoprecipitated with Marlin-1 and kinesin-I, providing evidence for the existence of a complex between these proteins. Kinesin-I modulates GABAB receptor transport. |
|
Publications: |
1 |
Organism: |
Mus Musculus |