| Sr.No. | Uniprot ID | Organism | Uniprot ID Isoforms | PTM | Domain | Source | Modifier | Nuclear Receptor | Site of PTM (Uniprot) | Effect |
| 1 |
P10275 |
Human |
P10275-1 |
Phosphorylation |
N-terminal Domain |
Curated |
Src Protooncogene tyrosine-protein kinase |
AR |
Y225 |
Increase in AR tyrosine phosphorylation and Src kinase activity is associated with prostate cancer progression. |
| 2 |
P10275 |
Human |
P10275-1 |
Phosphorylation |
N-terminal Domain |
Curated |
Src Protooncogene tyrosine-protein kinase |
AR |
Y309 |
Increase in AR tyrosine phosphorylation and Src kinase activity is associated with prostate cancer progression. |
| 3 |
P10275 |
Human |
P10275-1 |
Phosphorylation |
N-terminal Domain |
Curated |
Src Protooncogene tyrosine-protein kinase |
AR |
Y348 |
Increase in AR tyrosine phosphorylation and Src kinase activity is associated with prostate cancer progression. |
| 4 |
P10275 |
Human |
P10275-1 |
Phosphorylation |
N-terminal Domain |
Curated |
Src Protooncogene tyrosine-protein kinase |
AR |
Y364 |
Increase in AR tyrosine phosphorylation and Src kinase activity is associated with prostate cancer progression. |
| 5 |
P10275 |
Human |
P10275-1 |
Phosphorylation |
N-terminal Domain |
Curated |
Src Protooncogene tyrosine-protein kinase |
AR |
Y395 |
Increase in AR tyrosine phosphorylation and Src kinase activity is associated with prostate cancer progression. |
| 6 |
P10275 |
Human |
P10275-1 |
Phosphorylation |
N-terminal Domain |
Curated |
Src Protooncogene tyrosine-protein kinase |
AR |
Y552 |
Increase in AR tyrosine phosphorylation and Src kinase activity is associated with prostate cancer progression. |
| 7 |
P10275 |
Human |
P10275-1 |
Phosphorylation |
N-terminal Domain |
Curated |
Src Protooncogene tyrosine-protein kinase |
AR |
Y535 |
Phosphorylation of Y534 may be required for the Src-promoted nuclear translocation of AR under androgen-depleted conditions and Src-induced ARY534 phosphorylation is important for prostate tumor growth under androgen-depleted conditions. |
| 8 |
P41235 |
Human |
P41235-2 |
Phosphorylation |
N-terminal Domain |
Curated |
Src Protooncogene tyrosine-protein kinase |
HNF4ɑ |
Y23 |
pY14 binds the SH2 domain of Src and the proline-rich F domain of HNF4α binds the Src SH3 domain, thereby facilitating the phosphorylation of first Y277 and then Y279 in the HNF4α LBD. The net result is a triply phosphorylated HNF4α in which pY277 and pY279 evidently disrupt the coactivator binding site, resulting in a loss of transactivation, nuclear localization, and protein stability. |
| 9 |
Q96RI1 |
Human |
Q96RI1-1 |
Phosphorylation |
N-terminal Domain |
Curated |
Src Protooncogene tyrosine-protein kinase |
FXR |
Y67 |
FXR is phosphorylated at Y67 by non-receptor tyrosine kinase; Src; in response to postprandial FGF19; which is critical for its nuclear localization and transcriptional regulation of BA levels. |