+ |
GRK2 | down-regulates activity
phosphorylation
|
SLC9A5 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275503 |
Ser702 |
AVILTVEsEEEEEES |
|
|
pmid |
sentence |
21296876 |
Simultaneous mutation of five Ser/Thr residues within 702-714 to Ala ((702)ST/AA(714)) abolished phosphorylation and binding of beta-arrestin2. In transfected cells, the CK2 catalytic alpha subunit formed a complex with NHE5 and decreased wild-type but not (702)ST/AA(714) NHE5 activity, further supporting a regulatory role for this kinase. The rate of internalization of (702)ST/AA(714) was also diminished and relatively insensitive to overexpression of beta-arrestin2. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275504 |
Ser709 |
SEEEEEEsDSSETEK |
|
|
pmid |
sentence |
21296876 |
Simultaneous mutation of five Ser/Thr residues within 702-714 to Ala ((702)ST/AA(714)) abolished phosphorylation and binding of beta-arrestin2. In transfected cells, the CK2 catalytic alpha subunit formed a complex with NHE5 and decreased wild-type but not (702)ST/AA(714) NHE5 activity, further supporting a regulatory role for this kinase. The rate of internalization of (702)ST/AA(714) was also diminished and relatively insensitive to overexpression of beta-arrestin2. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275501 |
Ser711 |
EEEEESDsSETEKED |
|
|
pmid |
sentence |
21296876 |
Simultaneous mutation of five Ser/Thr residues within 702-714 to Ala ((702)ST/AA(714)) abolished phosphorylation and binding of beta-arrestin2. In transfected cells, the CK2 catalytic alpha subunit formed a complex with NHE5 and decreased wild-type but not (702)ST/AA(714) NHE5 activity, further supporting a regulatory role for this kinase. The rate of internalization of (702)ST/AA(714) was also diminished and relatively insensitive to overexpression of beta-arrestin2. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275500 |
Ser712 |
EEEESDSsETEKEDD |
|
|
pmid |
sentence |
21296876 |
Simultaneous mutation of five Ser/Thr residues within 702-714 to Ala ((702)ST/AA(714)) abolished phosphorylation and binding of beta-arrestin2. In transfected cells, the CK2 catalytic alpha subunit formed a complex with NHE5 and decreased wild-type but not (702)ST/AA(714) NHE5 activity, further supporting a regulatory role for this kinase. The rate of internalization of (702)ST/AA(714) was also diminished and relatively insensitive to overexpression of beta-arrestin2. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275502 |
Thr714 |
EESDSSEtEKEDDEG |
|
|
pmid |
sentence |
21296876 |
Simultaneous mutation of five Ser/Thr residues within 702-714 to Ala ((702)ST/AA(714)) abolished phosphorylation and binding of beta-arrestin2. In transfected cells, the CK2 catalytic alpha subunit formed a complex with NHE5 and decreased wild-type but not (702)ST/AA(714) NHE5 activity, further supporting a regulatory role for this kinase. The rate of internalization of (702)ST/AA(714) was also diminished and relatively insensitive to overexpression of beta-arrestin2. |
|
Publications: |
5 |
+ |
CSNK2A1 | down-regulates activity
phosphorylation
|
SLC9A5 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276253 |
Ser702 |
AVILTVEsEEEEEES |
in vitro |
|
pmid |
sentence |
21296876 |
CK2 phosphorylation of an acidic Ser/Thr di-isoleucine motif in the Na+/H+ exchanger NHE5 isoform promotes association with beta-arrestin2 and endocytosis |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276252 |
Ser709 |
SEEEEEEsDSSETEK |
in vitro |
|
pmid |
sentence |
21296876 |
CK2 phosphorylation of an acidic Ser/Thr di-isoleucine motif in the Na+/H+ exchanger NHE5 isoform promotes association with beta-arrestin2 and endocytosis |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276251 |
Ser711 |
EEEEESDsSETEKED |
in vitro |
|
pmid |
sentence |
21296876 |
CK2 phosphorylation of an acidic Ser/Thr di-isoleucine motif in the Na+/H+ exchanger NHE5 isoform promotes association with beta-arrestin2 and endocytosis |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276249 |
Ser712 |
EEEESDSsETEKEDD |
in vitro |
|
pmid |
sentence |
21296876 |
CK2 phosphorylation of an acidic Ser/Thr di-isoleucine motif in the Na+/H+ exchanger NHE5 isoform promotes association with beta-arrestin2 and endocytosis |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276250 |
Thr714 |
EESDSSEtEKEDDEG |
in vitro |
|
pmid |
sentence |
21296876 |
CK2 phosphorylation of an acidic Ser/Thr di-isoleucine motif in the Na+/H+ exchanger NHE5 isoform promotes association with beta-arrestin2 and endocytosis |
|
Publications: |
5 |
Organism: |
In Vitro |
+ |
ARRB2 | down-regulates activity
relocalization
|
SLC9A5 |
0.406 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275506 |
|
|
|
|
pmid |
sentence |
21296876 |
Internalization of the Na(+)/H(+) exchanger NHE5 into recycling endosomes is enhanced by the endocytic adaptor proteins beta-arrestin1 and -2, best known for their preferential recognition of ligand-activated G protein-coupled receptors (GPCRs) |
|
Publications: |
1 |
+ |
ARRB1 | down-regulates activity
relocalization
|
SLC9A5 |
0.41 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275505 |
|
|
|
|
pmid |
sentence |
21296876 |
Internalization of the Na(+)/H(+) exchanger NHE5 into recycling endosomes is enhanced by the endocytic adaptor proteins beta-arrestin1 and -2, best known for their preferential recognition of ligand-activated G protein-coupled receptors (GPCRs) |
|
Publications: |
1 |
+ |
SLC9A5 | up-regulates quantity
relocalization
|
sodium(1+) |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265604 |
|
|
Homo sapiens |
Neuron |
pmid |
sentence |
31507243 |
Na+/H+ exchangers play pivotal roles in the control of cell and tissue pH by mediating the electroneutral exchange of Na+ and H+ across cellular membranes. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SLC9A5 | down-regulates quantity
relocalization
|
hydron |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265595 |
|
|
Homo sapiens |
Neuron |
pmid |
sentence |
31507243 |
Na+/H+ exchangers play pivotal roles in the control of cell and tissue pH by mediating the electroneutral exchange of Na+ and H+ across cellular membranes. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |