| + |
UBE2I | up-regulates 
sumoylation
|
SMAD4 |
0.609 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-98993 |
Lys113 |
KNELKHVkYCQYAFD |
Homo sapiens |
|
| pmid |
sentence |
| 12621041 |
The mh1 domain of smad4 was shown to associate physically with ubc9, the ubiquitin carrier protein (e2) conjugating enzyme in sumoylation. In cultured cells, smad4 is modified by sumo-1 at the endogenous level. The sumoylation sites were identified as two evolutionarily conserved lysine residues, lys-113 and lys-159, in the mh1 domain. We found that the mutations at lys-113 and lys-159 did not alter the ability of smad4 to form a complex with smad2 and fast on the mix.2 promoter. Importantly, sumo-1 overexpression enhanced tgf-beta-induced transcriptional responses. These findings identify sumoylation as a unique mechanism to modulate smad4-dependent cellular responses |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-98997 |
Lys159 |
APSSMMVkDEYVHDF |
Homo sapiens |
|
| pmid |
sentence |
| 12621041 |
The mh1 domain of smad4 was shown to associate physically with ubc9, the ubiquitin carrier protein (e2) conjugating enzyme in sumoylation. In cultured cells, smad4 is modified by sumo-1 at the endogenous level. The sumoylation sites were identified as two evolutionarily conserved lysine residues, lys-113 and lys-159, in the mh1 domain. We found that the mutations at lys-113 and lys-159 did not alter the ability of smad4 to form a complex with smad2 and fast on the mix.2 promoter. Importantly, sumo-1 overexpression enhanced tgf-beta-induced transcriptional responses. These findings identify sumoylation as a unique mechanism to modulate smad4-dependent cellular responses |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
UBE2I | up-regulates activity
sumoylation
|
MBD4 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275676 |
Lys137 |
KNGETSLkPEDFDFT |
|
|
| pmid |
sentence |
| 31476572 |
MBD4 is sumoylated at three main sites: K137, K215 and K377.|Sumoylation increases the G:T repair activity of MBD4 in cell extracts.|we conducted an in vitrosumoylation assay, employing recombinant activating E1 (Aos1-Uba2) and conjugating E2 (Ubc9) enzymes, along with recombinant YFP-SUMO1 and MBD4 or, as positive control for sumoylation, TDG (Fig. 2D). These results indicate that MBD4 is sumoylated in vivo and in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275677 |
Lys215 |
TSTHLLLkEDEGVDD |
|
|
| pmid |
sentence |
| 31476572 |
MBD4 is sumoylated at three main sites: K137, K215 and K377.|Sumoylation increases the G:T repair activity of MBD4 in cell extracts.|we conducted an in vitrosumoylation assay, employing recombinant activating E1 (Aos1-Uba2) and conjugating E2 (Ubc9) enzymes, along with recombinant YFP-SUMO1 and MBD4 or, as positive control for sumoylation, TDG (Fig. 2D). These results indicate that MBD4 is sumoylated in vivo and in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275678 |
Lys377 |
HLHTDILkRGSEMDN |
|
|
| pmid |
sentence |
| 31476572 |
MBD4 is sumoylated at three main sites: K137, K215 and K377.|Sumoylation increases the G:T repair activity of MBD4 in cell extracts.|we conducted an in vitrosumoylation assay, employing recombinant activating E1 (Aos1-Uba2) and conjugating E2 (Ubc9) enzymes, along with recombinant YFP-SUMO1 and MBD4 or, as positive control for sumoylation, TDG (Fig. 2D). These results indicate that MBD4 is sumoylated in vivo and in vitro. |
|
| Publications: |
3 |
| + |
UBE2I | up-regulates quantity by stabilization
sumoylation
|
ZHX1 |
0.465 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263899 |
Lys159 |
TFDGSFVkEENAEQA |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23686912 |
Here, we report that the SUMO-E2 conjugating enzyme Ubc9 was identified to interact with ZHX1 by an interaction screen using a yeast two-hybrid system. This interaction was confirmed by co-immunoprecipitation and co-localization assays. Further study showed that ZHX1 is SUMOylated by Ubc9 with SUMO1 at the sites K159, K454, and K626. Furthermore, we demonstrated that the SUMOylation of ZHX1 regulated the stability, ubiquitination and transcriptional activity of ZHX1. The sumoylation of zinc‐fingers and homeoboxes 1 (ZHX1) by ubc9 regulates its stability and transcriptional repression activity. However, in the current work, we demonstrated that ZHX1 was only SUMOylated by SUMO1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263900 |
Lys454 |
VPTSQSVkHETALVN |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23686912 |
Here, we report that the SUMO-E2 conjugating enzyme Ubc9 was identified to interact with ZHX1 by an interaction screen using a yeast two-hybrid system. This interaction was confirmed by co-immunoprecipitation and co-localization assays. Further study showed that ZHX1 is SUMOylated by Ubc9 with SUMO1 at the sites K159, K454, and K626. Furthermore, we demonstrated that the SUMOylation of ZHX1 regulated the stability, ubiquitination and transcriptional activity of ZHX1. The sumoylation of zinc‐fingers and homeoboxes 1 (ZHX1) by ubc9 regulates its stability and transcriptional repression activity. However, in the current work, we demonstrated that ZHX1 was only SUMOylated by SUMO1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263901 |
Lys626 |
KKKSKALkEEKMEID |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23686912 |
Here, we report that the SUMO-E2 conjugating enzyme Ubc9 was identified to interact with ZHX1 by an interaction screen using a yeast two-hybrid system. This interaction was confirmed by co-immunoprecipitation and co-localization assays. Further study showed that ZHX1 is SUMOylated by Ubc9 with SUMO1 at the sites K159, K454, and K626. Furthermore, we demonstrated that the SUMOylation of ZHX1 regulated the stability, ubiquitination and transcriptional activity of ZHX1. The sumoylation of zinc‐fingers and homeoboxes 1 (ZHX1) by ubc9 regulates its stability and transcriptional repression activity. However, in the current work, we demonstrated that ZHX1 was only SUMOylated by SUMO1. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
UBE2I | down-regulates activity 
sumoylation
|
CEBPA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256334 |
Lys161 |
ALRPLVIkQEPREED |
in vitro |
|
| pmid |
sentence |
| 12511558 |
C/EBPalpha interacts directly with the E2 SUMO-conjugating enzyme Ubc9 and can be SUMOylated in vitro using purified recombinant components. Our results indicate that SUMO modification of SC motifs provides a means to rapidly control higher order interactions among transcription factors and suggests that SUMOylation may be a general mechanism to limit transcriptional synergy. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
UBE2I | down-regulates activity
sumoylation
|
JUN |
0.43 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263002 |
Lys226 |
HPRLQALkEEPQTVP |
Homo sapiens |
|
| pmid |
sentence |
| 16055711 |
We report here that lysine 265 of c-Fos is conjugated by the peptidic posttranslational modifiers SUMO-1, SUMO-2, and SUMO-3 and that c-Jun can be sumoylated on lysine 257 as well as on the previously described lysine 229. Sumoylation of c-Fos preferentially occurs in the context of c-Jun/c-Fos heterodimers.|Inhibition of c-Fos and c-Jun sumoylation stimulates AP-1-dependent transcription activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263001 |
Lys254 |
MESQERIkAERKRMR |
Homo sapiens |
|
| pmid |
sentence |
| 16055711 |
We report here that lysine 265 of c-Fos is conjugated by the peptidic posttranslational modifiers SUMO-1, SUMO-2, and SUMO-3 and that c-Jun can be sumoylated on lysine 257 as well as on the previously described lysine 229. Sumoylation of c-Fos preferentially occurs in the context of c-Jun/c-Fos heterodimers.|Inhibition of c-Fos and c-Jun sumoylation stimulates AP-1-dependent transcription activity. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
UBE2I | down-regulates
sumoylation
|
PLAG1 |
0.281 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126044 |
Lys244 |
NQELLKVkTEPVDFL |
Homo sapiens |
|
| pmid |
sentence |
| 15208321 |
Sumoylation decreases the transcriptional activity of plag1 / plag1 is sumoylated at 2 specific lysine residues (lys-244 and lys-263) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126048 |
Lys263 |
CNVSVPIkDELLPVM |
Homo sapiens |
|
| pmid |
sentence |
| 15208321 |
Sumoylation decreases the transcriptional activity of plag1 / plag1 is sumoylated at 2 specific lysine residues (lys-244 and lys-263) |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
UBE2I | up-regulates
sumoylation
|
FOXL2 |
0.686 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187901 |
Lys25 |
PETGRTVkEPEGPPP |
Homo sapiens |
|
| pmid |
sentence |
| 19744555 |
Foxl2 is sumoylated by ubc9, and this ubc9-mediated sumoylation is essential to the transcriptional activity of foxl2 on the star promoter. / the sumoylation site was identified at lysine 25 of foxl2 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UBE2I | down-regulates activity
sumoylation
|
FOS |
0.373 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263013 |
Lys265 |
SISSMELkTEPFDDF |
Homo sapiens |
|
| pmid |
sentence |
| 16055711 |
We report here that lysine 265 of c-Fos is conjugated by the peptidic posttranslational modifiers SUMO-1, SUMO-2, and SUMO-3 and that c-Jun can be sumoylated on lysine 257 as well as on the previously described lysine 229. Sumoylation of c-Fos preferentially occurs in the context of c-Jun/c-Fos heterodimers.|Inhibition of c-Fos and c-Jun sumoylation stimulates AP-1-dependent transcription activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UBE2I | down-regulates
ubiquitination
|
MITF |
0.546 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-75117 |
Lys308 |
SEARALAkERQKKDN |
Homo sapiens |
|
| pmid |
sentence |
| 10673502 |
Furthermore, we identified lysine 201 as a potential ubiquitination site. A lysine to arginine mutation abolished mitf (k201r) degradation by hubc9 in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UBE2I | down-regulates activity
sumoylation
|
SOX6 |
0.374 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256129 |
Lys404 |
VSPTGIkNEKRGTS |
Homo sapiens |
|
| pmid |
sentence |
| 16442531 |
We show that SOX6 is modified in vitro and in vivo by small ubiquitin‐related modifier (SUMO) on two distinct sites. Mutation of both sites abolished SOX6 sumoylation and increased SOX6 transcriptional activity. SUMO dependent repression of SOX6 transcription was promoted by UBC9 whereas siRNA to UBC9, cotransfection of inactive UBC9 or a SUMO protease increased SOX6 transcriptional activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256130 |
Lys417 |
TSPVTQkVkDEAAAQP |
Homo sapiens |
|
| pmid |
sentence |
| 16442531 |
We show that SOX6 is modified in vitro and in vivo by small ubiquitin‐related modifier (SUMO) on two distinct sites. Mutation of both sites abolished SOX6 sumoylation and increased SOX6 transcriptional activity. SUMO dependent repression of SOX6 transcription was promoted by UBC9 whereas siRNA to UBC9, cotransfection of inactive UBC9 or a SUMO protease increased SOX6 transcriptional activity. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
UBE2I | down-regulates activity
sumoylation
|
IRF7 |
0.292 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266837 |
Lys452 |
EKSLVLVkLEPWLCR |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 22951831 |
One mechanism by which LMP1 regulates cellular activation is through the induction of protein posttranslational modifications. We have now identified a specific target of LMP1-induced sumoylation, interferon regulatory factor 7 (IRF7). We hypothesize that during EBV latency, LMP1 induces the sumoylation of IRF7, limiting its transcriptional activity and modulating the activation of innate immune responses. We recently documented that LMP1 induces a third major protein modification by physically interacting with the SUMO-conjugating enzyme Ubc9 through CTAR3 and inducing the sumoylation of cellular proteins in latently infected cells. we identified that IRF7 is sumoylated at lysine 452. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EBV infection |
| + |
UBE2I | up-regulates activity
sumoylation
|
N |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260263 |
Lys62 |
TALTQHGkEELRFPR |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 17037517 |
In this study, we identified Ubc9 as a host protein that interacts specifically with SARS-CoV N protein. This interaction was verified both in vivo and in vitro. Furthermore, we showed that, in addition to phosphorylation, the N protein was modified by covalent attachment of SUMO to its lysine 62 residue. Evidence provided demonstrated that sumoylation may promote homo-oligomerization of the protein. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UBE2I | down-regulates
sumoylation
|
ETV5 |
0.269 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-135850 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15857832 |
Here we show that erm interacts with the sumo-conjugating enzyme ubc9 and is modified by sumo. We further show that sumo modification of this ets transcription factor affects its ability to activate transcription. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LMP1 | up-regulates activity
binding
|
UBE2I |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266838 |
|
|
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 22951831 |
One mechanism by which LMP1 regulates cellular activation is through the induction of protein posttranslational modifications. We have now identified a specific target of LMP1-induced sumoylation, interferon regulatory factor 7 (IRF7). We hypothesize that during EBV latency, LMP1 induces the sumoylation of IRF7, limiting its transcriptional activity and modulating the activation of innate immune responses. We recently documented that LMP1 induces a third major protein modification by physically interacting with the SUMO-conjugating enzyme Ubc9 through CTAR3 and inducing the sumoylation of cellular proteins in latently infected cells. we identified that IRF7 is sumoylated at lysine 452. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EBV infection |
| + |
UBE2I | down-regulates quantity by destabilization
polyubiquitination
|
BHLHE40 |
0.331 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272579 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11278694 |
Co-expression of STRA13 and UBC9 led to an increase of the pSTRA13 ubiquitination and subsequent degradation. These data established that UBC9/STRA13 association in cells is of physiological importance, presenting direct proof of UBC9 involvement in the ubiquitin-dependent degradation of pSTRA13. We also checked whether UBC9 is directly involved in pSTRA13 ubiquitination. Taken together, these results strongly suggest that pSTRA13 is targeted for proteolysis by the ubiquitin-dependent proteasome pathway through association with UBC9. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PCGF2 | down-regulates activity
binding
|
UBE2I |
0.591 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-226248 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18211895 |
Based on this finding of interaction between MEL-18 and UBC9, we envisioned a mechanism in which MEL-18 bound to HSF2 inhibits its sumoylation by binding to and inhibiting the activity of UBC9 enzymes that approach HSF2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Ub:E1 (UBA1 substrate) | up-regulates activity
ubiquitination
|
UBE2I |
0.547 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271312 |
|
|
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 |
| + |
Ub:E1 (UBA6 substrate) | up-regulates activity
ubiquitination
|
UBE2I |
0.451 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271346 |
|
|
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 |
3.0
UBE2I
- 
- 