+ |
PDPK1 | down-regulates activity
phosphorylation
|
AHCYL1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249174 |
Ser68 |
RSLSRSIsQSSTDSY |
Chlorocebus aethiops |
|
pmid |
sentence |
17635105 |
Residue 68 resides in a consensus phosphorylation site for PKD (Figure 1A) [22,23]. Interestingly, phosphorylation of Ser68 could allow for subsequent phosphorylation of Ser71, Ser74, Ser77 and Ser80 by CK1, for which the consensus phosphorylation site is pS/T-X-X-S/T| We found that phosphorylation of Ser71 and Ser74 were sufficient to enable inhibition of IP3 binding to the IP3R |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
PPP1CC |
dephosphorylation
|
AHCYL1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248498 |
Ser68 |
RSLSRSIsQSSTDSY |
Mus musculus |
|
pmid |
sentence |
17635105 |
Moreover, IRBIT-associated PP1 specifically dephosphorylated Ser68 of IRBIT. Phosphorylation of Ser68 was required for subsequent phosphorylation of Ser71 and Ser74, but the latter two sites were not targeted by PP1. We found that phosphorylation of Ser71 and Ser74 were sufficient to enable inhibition of IP3 binding to the IP3R|Given the importance of phosphorylation for the function of IRBIT in suppressing IP3R activity [7,10], in the present study, we searched for a protein phosphatase involved in the dephosphorylation and, hence, inactivation of IRBIT. We found that IRBIT contains a specific well-conserved binding site for PP1. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
PP1 |
dephosphorylation
|
AHCYL1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264657 |
Ser68 |
RSLSRSIsQSSTDSY |
Mus musculus |
|
pmid |
sentence |
17635105 |
Moreover, IRBIT-associated PP1 specifically dephosphorylated Ser68 of IRBIT. Phosphorylation of Ser68 was required for subsequent phosphorylation of Ser71 and Ser74, but the latter two sites were not targeted by PP1. We found that phosphorylation of Ser71 and Ser74 were sufficient to enable inhibition of IP3 binding to the IP3R|Given the importance of phosphorylation for the function of IRBIT in suppressing IP3R activity [7,10], in the present study, we searched for a protein phosphatase involved in the dephosphorylation and, hence, inactivation of IRBIT. We found that IRBIT contains a specific well-conserved binding site for PP1. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
PPP1CA |
dephosphorylation
|
AHCYL1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248555 |
Ser68 |
RSLSRSIsQSSTDSY |
Mus musculus |
|
pmid |
sentence |
17635105 |
Moreover, IRBIT-associated PP1 specifically dephosphorylated Ser68 of IRBIT. Phosphorylation of Ser68 was required for subsequent phosphorylation of Ser71 and Ser74, but the latter two sites were not targeted by PP1. We found that phosphorylation of Ser71 and Ser74 were sufficient to enable inhibition of IP3 binding to the IP3R|Given the importance of phosphorylation for the function of IRBIT in suppressing IP3R activity [7,10], in the present study, we searched for a protein phosphatase involved in the dephosphorylation and, hence, inactivation of IRBIT. We found that IRBIT contains a specific well-conserved binding site for PP1. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
PPP1CB |
dephosphorylation
|
AHCYL1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248571 |
Ser68 |
RSLSRSIsQSSTDSY |
Mus musculus |
|
pmid |
sentence |
17635105 |
Moreover, IRBIT-associated PP1 specifically dephosphorylated Ser68 of IRBIT. Phosphorylation of Ser68 was required for subsequent phosphorylation of Ser71 and Ser74, but the latter two sites were not targeted by PP1. We found that phosphorylation of Ser71 and Ser74 were sufficient to enable inhibition of IP3 binding to the IP3R|Given the importance of phosphorylation for the function of IRBIT in suppressing IP3R activity [7,10], in the present study, we searched for a protein phosphatase involved in the dephosphorylation and, hence, inactivation of IRBIT. We found that IRBIT contains a specific well-conserved binding site for PP1. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
CSNK1A1 |
phosphorylation
|
AHCYL1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249185 |
Ser77 |
SSTDSYSsAASYTDS |
Chlorocebus aethiops |
|
pmid |
sentence |
17635105 |
Residue 68 resides in a consensus phosphorylation site for PKD (Figure 1A) [22,23]. Interestingly, phosphorylation of Ser68 could allow for subsequent phosphorylation of Ser71, Ser74, Ser77 and Ser80 by CK1, for which the consensus phosphorylation site is pS/T-X-X-S/T |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
AHCYL1 | down-regulates activity
binding
|
PAPOLB |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-268331 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19224921 |
Inositol 1,4,5-triphosphate receptor-binding protein released with inositol 1,4,5-triphosphate (IRBIT) associates with components of the mRNA 3' processing machinery in a phosphorylation-dependent manner and inhibits polyadenylation|In addition to CPSF, IRBIT interacted in vitro with poly(A) polymerase (PAP), which is the enzyme recruited by CPSF to elongate the poly(A) tail, and inhibited PAP activity in a phosphorylation-dependent manner. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AHCYL1 | down-regulates activity
binding
|
PAPOLA |
0.248 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-268329 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19224921 |
Inositol 1,4,5-triphosphate receptor-binding protein released with inositol 1,4,5-triphosphate (IRBIT) associates with components of the mRNA 3' processing machinery in a phosphorylation-dependent manner and inhibits polyadenylation|In addition to CPSF, IRBIT interacted in vitro with poly(A) polymerase (PAP), which is the enzyme recruited by CPSF to elongate the poly(A) tail, and inhibited PAP activity in a phosphorylation-dependent manner. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AHCYL1 | up-regulates activity
relocalization
|
PP1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264645 |
|
|
Mus musculus |
|
pmid |
sentence |
21317537 |
WNK kinases acted as scaffolds to recruit SPAK, which phosphorylated CFTR and NBCe1-B, reducing their cell surface expression. IRBIT opposed the effects of WNKs and SPAK by recruiting PP1 to the complex to dephosphorylate CFTR and NBCe1-B, restoring their cell surface expression, |
|
Publications: |
1 |
Organism: |
Mus Musculus |
Tissue: |
Pancreas |
+ |
AHCYL1 | up-regulates activity
binding
|
SLC4A4 |
0.693 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263135 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21317537 |
IRBIT opposed the effects of WNKs and SPAK by recruiting PP1 to the complex to dephosphorylate CFTR and NBCe1-B, restoring their cell surface expression, in addition to stimulating their activities. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |