| + |
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 |
| + |
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 |
| + |
BCL6 | down-regulates quantity by repression 
transcriptional regulation
|
SUMO1 |
0.31 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253929 |
|
|
Homo sapiens |
HT-29 Cell |
| pmid |
sentence |
| 22723377 |
QPCR analysis of the resulting gene expression levels identified three genes that were affected in opposite sense by the downregulation of either BCL-6 or STAT5, namely cyclin D2 (CCND2), cyclin-dependent kinase inhibitor p15INK4B (CDKN2B), and SUMO1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
SUMO1
- 
- 