EC Number   |
Posttranslational Modification |
Reference |
|---|
    2.7.7.15 | lipoprotein |
H-form appears to be a lipoprotein consisting of an apoprotein i.e. L-form dimer of 45000 MW subunits complexed with lipids |
642902 |
| 2.7.7.15 | lipoprotein |
H-form of enzyme |
642902, 642905 |
| 2.7.7.15 | lipoprotein |
phosphatidylinositol is present in the H-form isolated from Hep G2 cells |
642902 |
| 2.7.7.15 | phosphoprotein |
- |
642920, 662364 |
| 2.7.7.15 | phosphoprotein |
16 serine and 2 tyrosine residues available for phosphorylation, phosphorylation is associated with decreased membrane binding and therefore, decreased activity |
662320 |
| 2.7.7.15 | phosphoprotein |
C-terminal region is highly phosphorylated, phosphorylation decreases membrane affinity and is therefore involved in regulation of enzyme activity |
661213 |
| 2.7.7.15 | phosphoprotein |
enzyme phosphorylation is involved in regulation of activity |
660981 |
| 2.7.7.15 | phosphoprotein |
oleate treatment of cultured cells triggers CCTalpha translocation to the nuclear envelope and nuclear lipid droplets and rapid dephosphorylation of pS319. Removal of oleate leads to dissociation of CCTalpha from the nuclear envelope and increased phosphorylation of S319. Choline depletion of cells causes CCTalpha translocation to the nuclear envelope and S319 dephosphorylation. Y359 and S362 are constitutively phosphorylated during oleate addition and removal. The P-domain undergoes negative charge polarization due to dephosphorylation of S319 and possibly other proline-directed sites and retention of Y359 and S362 phosphorylation. Dephosphorylation of S319 and S315 is involved in CCTalpha recruitment to nuclear membranes |
761872 |
| 2.7.7.15 | phosphoprotein |
phosphorylated on serine and threonine but not on tyrosine residues |
661238 |
| 2.7.7.15 | phosphoprotein |
phosphorylation is confined to 15-16 serine residues near the C-terminus |
642929 |
