Relation Results

Summary

Name AHCYL1
Full Name S-adenosylhomocysteine hydrolase-like protein 1
Synonyms AdoHcyase 2, DC-expressed AHCY-like molecule, IP(3)Rs binding protein released with IP(3), IRBIT, S-adenosyl-L-homocysteine hydrolase 2, S-adenosylhomocysteine hydrolase-like protein 1 | DCAL, IRBIT, XPVKONA
Primary ID O43865
Links - -
Type protein
Relations 10
Function Multifaceted cellular regulator which coordinates several essential cellular functions including regulation of epithelial HCO3(-) and fluid secretion, ...
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Type: Score: Layout: SPV 
0.20.20.20.20.20.20.20.6920.20.248PP1AHCYL1PPP1CCPDPK1PPP1CAPPP1CBCSNK1A1SLC4A4PAPOLBPAPOLA

Modifications Tables

Relations

Regulator
Mechanism
target
score
+ img/unknown.png dephosphorylation AHCYL1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-264657 Ser68 RSLSRSIsQSSTDSY Mus musculus
pmid sentence
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
+ img/unknown.png dephosphorylation AHCYL1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-248498 Ser68 RSLSRSIsQSSTDSY Mus musculus
pmid sentence
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
+ down-regulates activity img/direct_inhibition.png phosphorylation AHCYL1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-249174 Ser68 RSLSRSIsQSSTDSY Chlorocebus aethiops
pmid sentence
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
+ img/unknown.png dephosphorylation AHCYL1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-248555 Ser68 RSLSRSIsQSSTDSY Mus musculus
pmid sentence
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
+ img/unknown.png dephosphorylation AHCYL1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-248571 Ser68 RSLSRSIsQSSTDSY Mus musculus
pmid sentence
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
+ img/unknown.png phosphorylation AHCYL1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-249185 Ser77 SSTDSYSsAASYTDS Chlorocebus aethiops
pmid sentence
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
+ up-regulates activity img/direct-activation.png relocalization PP1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-264645 Mus musculus
pmid sentence
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
+ up-regulates activity img/direct-activation.png binding SLC4A4 0.692
Identifier Residue Sequence Organism Cell Line
SIGNOR-263135 Homo sapiens HEK-293 Cell
pmid sentence
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
+ down-regulates activity img/direct_inhibition.png binding PAPOLB 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-268331 Homo sapiens HEK-293 Cell
pmid sentence
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
+ down-regulates activity img/direct_inhibition.png binding PAPOLA 0.248
Identifier Residue Sequence Organism Cell Line
SIGNOR-268329 Homo sapiens HEK-293 Cell
pmid sentence
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
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