| + |
SUMO1 | up-regulates 
sumoylation
|
PML |
0.771 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261786 |
Lys160 |
EAHQWFLkHEARPLA |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 9756909 |
We have shown previously that wild type PML, but not PML-RARalpha, is covalently modified by the sentrin family of ubiquitin-like proteins|We show that Lys65 in the RING finger domain, Lys160 in the B1 Box, and Lys490 in the nuclear localization signal contributes three major sentrinization sites| Furthermore, the triple substitution mutant is localized predominantly to the nucleoplasm, in contrast to wild type PML, which is localized to the nuclear bodies. Thus, sentrinization of PML, in the context of the RING finger and the B1 box, regulates nuclear body formation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261787 |
Lys490 |
QCPRKVIkMESEEGK |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 9756909 |
We have shown previously that wild type PML, but not PML-RARalpha, is covalently modified by the sentrin family of ubiquitin-like proteins|We show that Lys65 in the RING finger domain, Lys160 in the B1 Box, and Lys490 in the nuclear localization signal contributes three major sentrinization sites| Furthermore, the triple substitution mutant is localized predominantly to the nucleoplasm, in contrast to wild type PML, which is localized to the nuclear bodies. Thus, sentrinization of PML, in the context of the RING finger and the B1 box, regulates nuclear body formation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261788 |
Lys65 |
QQCQAEAkCPKLLPC |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 9756909 |
We have shown previously that wild type PML, but not PML-RARalpha, is covalently modified by the sentrin family of ubiquitin-like proteins|We show that Lys65 in the RING finger domain, Lys160 in the B1 Box, and Lys490 in the nuclear localization signal contributes three major sentrinization sites| Furthermore, the triple substitution mutant is localized predominantly to the nucleoplasm, in contrast to wild type PML, which is localized to the nuclear bodies. Thus, sentrinization of PML, in the context of the RING finger and the B1 box, regulates nuclear body formation. |
|
| Publications: |
3 |
Organism: |
Chlorocebus Aethiops |
| + |
SUMO1 | up-regulates activity
sumoylation
|
PML |
0.771 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270540 |
Lys160 |
EAHQWFLkHEARPLA |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 9756909 |
We have shown previously that wild type PML, but not PML-RARalpha, is covalently modified by the sentrin family of ubiquitin-like proteins |We show that Lys65 in the RING finger domain, Lys160 in the B1 Box, and Lys490 in the nuclear localization signal contributes three major sentrinization sites. The PML mutant with Lys to Arg substitutions in all three sites is expressed normally, but cannot be sentrinized|Furthermore, the triple substitution mutant is localized predominantly to the nucleoplasm, in contrast to wild type PML, which is localized to the nuclear bodies. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270541 |
Lys490 |
QCPRKVIkMESEEGK |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 9756909 |
We have shown previously that wild type PML, but not PML-RARalpha, is covalently modified by the sentrin family of ubiquitin-like proteins |We show that Lys65 in the RING finger domain, Lys160 in the B1 Box, and Lys490 in the nuclear localization signal contributes three major sentrinization sites. The PML mutant with Lys to Arg substitutions in all three sites is expressed normally, but cannot be sentrinized|Furthermore, the triple substitution mutant is localized predominantly to the nucleoplasm, in contrast to wild type PML, which is localized to the nuclear bodies. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270542 |
Lys65 |
QQCQAEAkCPKLLPC |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 9756909 |
We have shown previously that wild type PML, but not PML-RARalpha, is covalently modified by the sentrin family of ubiquitin-like proteins |We show that Lys65 in the RING finger domain, Lys160 in the B1 Box, and Lys490 in the nuclear localization signal contributes three major sentrinization sites. The PML mutant with Lys to Arg substitutions in all three sites is expressed normally, but cannot be sentrinized|Furthermore, the triple substitution mutant is localized predominantly to the nucleoplasm, in contrast to wild type PML, which is localized to the nuclear bodies. |
|
| Publications: |
3 |
Organism: |
Chlorocebus Aethiops |
| + |
CHEK2 |
phosphorylation
|
PML |
0.407 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-94872 |
Ser117 |
ESLQRRLsVYRQIVD |
Homo sapiens |
|
| pmid |
sentence |
| 12402044 |
Hcds1/chk2 phosphorylates pml at ser 117 in vitro. hcds1/chk2 phosphorylates pml in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK1 | up-regulates
phosphorylation
|
PML |
0.366 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124240 |
Ser36 |
PSEGRQPsPSPSPTE |
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 15093545 |
We conclude that phosphorylation by map kinase cascades potentiates the antiproliferative functions of pml and helps mediate the proapoptotic effects of as(2)o(3). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124244 |
Ser38 |
EGRQPSPsPSPTERA |
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 15093545 |
We conclude that phosphorylation by map kinase cascades potentiates the antiproliferative functions of pml and helps mediate the proapoptotic effects of as(2)o(3). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124248 |
Ser40 |
RQPSPSPsPTERAPA |
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 15093545 |
We report here that as(2)o(3) treatment induces phosphorylation of the pml protein through a mitogen-activated protein (map) kinase pathway. Increased pml phosphorylation is associated with increased sumoylation of pml and increased pml-mediated apoptosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124252 |
Ser527 |
PHLDGPPsPRSPVIG |
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 15093545 |
We conclude that phosphorylation by map kinase cascades potentiates the antiproliferative functions of pml and helps mediate the proapoptotic effects of as(2)o(3). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124056 |
Ser530 |
DGPPSPRsPVIGSEV |
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 15093545 |
We conclude that phosphorylation by map kinase cascades potentiates the antiproliferative functions of pml and helps mediate the proapoptotic effects of as(2)o(3). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124313 |
Thr28 |
PTMPPPEtPSEGRQP |
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 15093545 |
We conclude that phosphorylation by map kinase cascades potentiates the antiproliferative functions of pml and helps mediate the proapoptotic effects of as(2)o(3). |
|
| Publications: |
6 |
Organism: |
Homo Sapiens |
| + |
HIPK2 | up-regulates
phosphorylation
|
PML |
0.449 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182428 |
Ser38 |
EGRQPSPsPSPTERA |
Homo sapiens |
|
| pmid |
sentence |
| 19015637 |
In response to dna damage, hipk2 phosphorylates pml at serines 8 and 38. he n-terminal phosphorylation sites contribute to the dna damage-induced pml sumoylation and are required for the ability of pml to cooperate with hipk2 for the induction of cell death. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182432 |
Ser8 |
MEPAPARsPRPQQDP |
Homo sapiens |
|
| pmid |
sentence |
| 19015637 |
In response to dna damage, hipk2 phosphorylates pml at serines 8 and 38. he n-terminal phosphorylation sites contribute to the dna damage-induced pml sumoylation and are required for the ability of pml to cooperate with hipk2 for the induction of cell death. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CSNK2A1 | down-regulates 
phosphorylation
|
PML |
0.348 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-148306 |
Ser518 |
PSTSKAVsPPHLDGP |
Homo sapiens |
Lung Cancer Cell |
| pmid |
sentence |
| 16873060 |
Here we show that ck2 regulates pml protein levels by promoting its ubiquitin-mediated degradation dependent on direct phosphorylation at ser517. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-148310 |
Ser565 |
VISSSEDsDAENSSS |
Homo sapiens |
Lung Cancer Cell |
| pmid |
sentence |
| 16873060 |
Here we show that ck2 regulates pml protein levels by promoting its ubiquitin-mediated degradation dependent on direct phosphorylation at ser517. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
MAPK3 | up-regulates
phosphorylation
|
PML |
0.345 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124317 |
Ser530 |
DGPPSPRsPVIGSEV |
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 15093545 |
Phosphorylation of pml by mitogen-activated protein kinases plays a key role in arsenic trioxide-mediated apoptosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PML | up-regulates activity
binding
|
SMAD2 |
0.531 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-128738 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15356634 |
Cytoplasmic pml physically interacts with smad2/3 and sara (smad anchor for receptor activation) and is required for association of smad2/3 with sara and for the accumulation of sara and tgf-beta receptor in the early endosome. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Gbeta | up-regulates
phosphorylation
|
PML |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270034 |
|
|
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 15093545 |
Phosphorylation of pml by mitogen-activated protein kinases plays a key role in arsenic trioxide-mediated apoptosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PML | up-regulates 
|
Apoptosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124320 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15093545 |
The promyelocytic leukemia (pml) protein is a potent growth suppressor and proapototic factor |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RNF111 | down-regulates quantity by destabilization
polyubiquitination
|
PML |
0.362 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272883 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23530056 |
Upon TGF-β induction, interaction of Arkadia with phosphorylated Smad2 triggers degradation of SnoN, whereas upon arsenic treatment, interaction of Arkadia with poly-SUMO in PML nuclear bodies induces degradation of polysumoylated PML together with RNF4. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RNF4 | down-regulates quantity by destabilization
polyubiquitination
|
PML |
0.5 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272884 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23530056 |
Upon TGF-β induction, interaction of Arkadia with phosphorylated Smad2 triggers degradation of SnoN, whereas upon arsenic treatment, interaction of Arkadia with poly-SUMO in PML nuclear bodies induces degradation of polysumoylated PML together with RNF4. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Ub:E2 | up-regulates activity
ubiquitination
|
PML |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270992 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 34199813 |
The ubiquitination process is mediated sequentially by three classes of enzymes consisting of a Ub-activating enzyme E1, a Ub-conjugating enzyme E2, and a Ub ligase E3. Ub is first activated by E1 in an adenosine 5′-triphosphate (ATP)-dependent manner t |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PML | form complex 
binding
|
KAT6A/PML |
0.504 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-201489 |
|
|
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 23431171 |
We show here that moz is an acetyltransferase of p53 at k120 and k382 and colocalizes with p53 in promyelocytic leukemia (pml) nuclear bodies following cellular stress. The moz-pml-p53 interaction enhances moz-mediated acetylation of p53, and this ternary complex enhances p53-dependent p21 expression |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PML | up-regulates
|
Cell_death |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256659 |
|
|
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 15093545 |
The promyelocytic leukemia (pml) protein is a potent growth suppressor and proapototic factor |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PML | up-regulates
binding
|
SMAD3 |
0.529 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-128741 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15356634 |
Cytoplasmic pml physically interacts with smad2/3 and sara (smad anchor for receptor activation) and is required for association of smad2/3 with sara and for the accumulation of sara and tgf-beta receptor in the early endosome. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK1 | down-regulates
phosphorylation
|
PML |
0.351 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176033 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21840486 |
Here, we show that klhl20, a cullin3 (cul3) substrate adaptor induced by hif-1, coordinates with the actions of cdk1/2 and pin1 to mediate hypoxia-induced pml proteasomal degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PML | up-regulates activity
binding
|
SMAD3 |
0.529 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-232090 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15356634 |
Cytoplasmic pml physically interacts with smad2/3 and sara (smad anchor for receptor activation) and is required for association of smad2/3 with sara and for the accumulation of sara and tgf-beta receptor in the early endosome. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PML | up-regulates
binding
|
ZFYVE9 |
0.557 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-128744 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15356634 |
Cytoplasmic pml physically interacts with smad2/3 and sara (smad anchor for receptor activation) and is required for association of smad2/3 with sara and for the accumulation of sara and tgf-beta receptor in the early endosome. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERK1/2 | up-regulates
phosphorylation
|
PML |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270153 |
|
|
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 15093545 |
Phosphorylation of pml by mitogen-activated protein kinases plays a key role in arsenic trioxide-mediated apoptosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK7 | down-regulates
phosphorylation
|
PML |
0.486 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167947 |
|
|
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 20832753 |
We found that bmk1 interacted with promyelocytic leukemia protein (pml), and inhibited its tumor-suppressor function through phosphorylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PML | up-regulates
binding
|
SMAD2 |
0.531 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-128735 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15356634 |
Cytoplasmic pml physically interacts with smad2/3 and sara (smad anchor for receptor activation) and is required for association of smad2/3 with sara and for the accumulation of sara and tgf-beta receptor in the early endosome. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PML
- 
- 