| + |
FAM83C | up-regulates quantity 
binding
|
CSNK1A1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273752 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29789297 |
We identified members of the FAM83 family of proteins as partners of CK1 in cells. All eight members of the FAM83 family (FAM83A–H) interacted with the α and α-like isoforms of CK1; FAM83A, -B, -E, and -H also interacted with the δ and ε isoforms of CK1. The intrinsic catalytic activity of CK1 is not affected by or required for the association of CK1 with FAM83 proteins. Our findings imply that the DUF1669 domains of FAM83 proteins anchor CK1 α, α-like, δ, and ε isoforms in specific subcellular compartments and potentially mediate their association with substrates. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FAM83C | up-regulates quantity
binding
|
CSNK1A1L |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273760 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29789297 |
We identified members of the FAM83 family of proteins as partners of CK1 in cells. All eight members of the FAM83 family (FAM83A–H) interacted with the α and α-like isoforms of CK1; FAM83A, -B, -E, and -H also interacted with the δ and ε isoforms of CK1. The intrinsic catalytic activity of CK1 is not affected by or required for the association of CK1 with FAM83 proteins. Our findings imply that the DUF1669 domains of FAM83 proteins anchor CK1 α, α-like, δ, and ε isoforms in specific subcellular compartments and potentially mediate their association with substrates. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
FAM83C
- 
- 