+ |
ROCK1 | up-regulates
phosphorylation
|
FHOD1 |
0.315 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-160544 |
Ser1131 |
AARERKRsRGNRKSL |
Homo sapiens |
|
pmid |
sentence |
18239683 |
Rock phosphorylates the c-terminal residues ser1131, ser1137, and thr1141 of formin homology domain protein 1 (fhod1). Phosphorylation of fhod1 at the three residues fully disrupts the autoinhibitory interaction, which culminates in formation of stress fibres. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-160548 |
Ser1137 |
RSRGNRKsLRRTLKS |
Homo sapiens |
|
pmid |
sentence |
18239683 |
Rock phosphorylates the c-terminal residues ser1131, ser1137, and thr1141 of formin homology domain protein 1 (fhod1). Phosphorylation of fhod1 at the three residues fully disrupts the autoinhibitory interaction, which culminates in formation of stress fibres. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-160552 |
Thr1141 |
NRKSLRRtLKSGLGD |
Homo sapiens |
|
pmid |
sentence |
18239683 |
Rock phosphorylates the c-terminal residues ser1131, ser1137, and thr1141 of formin homology domain protein 1 (fhod1). Phosphorylation of fhod1 at the three residues fully disrupts the autoinhibitory interaction, which culminates in formation of stress fibres. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
PRKG1 | up-regulates
phosphorylation
|
FHOD1 |
0.361 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-123646 |
Ser1131 |
AARERKRsRGNRKSL |
Homo sapiens |
|
pmid |
sentence |
15051728 |
Pkgi also directly phosphorylates fhod1, and studies with wild-type and mutant fhod1-derived peptides identify ser-1131 in the fhod1 c terminus as the unique pkgi phosphorylation site in fhod1. phosphorylation of three conserved residues within the dad domain activates fhod1 while binding to rac regulates fhod1 subcellular localization |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-170094 |
Ser1131 |
AARERKRsRGNRKSL |
Homo sapiens |
|
pmid |
sentence |
21106951 |
Pkgi also directly phosphorylates fhod1, and studies with wild-type and mutant fhod1-derived peptides identify ser-1131 in the fhod1 c terminus as the unique pkgi phosphorylation site in fhod1. phosphorylation of three conserved residues within the dad domain activates fhod1 while binding to rac regulates fhod1 subcellular localization |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Tissue: |
Muscle, Smooth Muscle |
+ |
SRC | up-regulates activity
phosphorylation
|
FHOD1 |
0.312 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276612 |
Tyr99 |
REMLEGFyEEISKGR |
Mus musculus |
|
pmid |
sentence |
24331927 |
Our results show that only Src can efficiently phosphorylate FHOD1 at Y99 to enable the downstream activation by ROCK. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
FHOD1 | up-regulates quantity by stabilization
binding
|
ACTB |
0.35 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276613 |
|
|
Homo sapiens |
|
pmid |
sentence |
14576350 |
Fhos, a mammalian formin, directly binds to F-actin via a region N-terminal to the FH1 domain and forms a homotypic complex via the FH2 domain to promote actin fiber formation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |