| + |
ATM | up-regulates activity 
phosphorylation
|
SMURF2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277534 |
Ser384 |
KILRQELsQQQPQAG |
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 33097595 |
Using biochemical approaches and MS analysis, we show that upon the onset of the DNA-damage response, SMURF2 becomes phosphorylated at Ser384 by ataxia telangiectasia mutated (ATM) serine/threonine kinase, and this phosphorylation is required for its interaction with RNF20. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
SMURF2 | down-regulates 
ubiquitination
|
SMAD1/5/8 |
0.778 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269845 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22298955 |
Smurf1 and smurf2 are e3 ubiquitin ligases known to suppress tgf-beta signaling through degra-dation of smads and receptors for tgf-beta and bmps |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMURF2 | down-regulates
ubiquitination
|
BMPR2 |
0.481 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-193119 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22298955 |
Smurf1 and smurf2 are e3 ubiquitin ligases known to suppress tgf-beta signaling through degra-dation of smads and receptors for tgf-beta and bmps. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RNF11 | up-regulates activity
binding
|
SMURF2 |
0.557 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272952 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 14755250 |
RNF11 recruits AMSH to Smurf2 E3 ligase. Smurf2 promotes ubiquitination of AMSH in the presence of wt RNF11. Previously, we have shown that RNF11 interacts with the HECT-type E3 ligases AIP4 and Smurf2. Here, we show that RNF11 binds to AMSH in mammalian cells and that this interaction is independent of the RNF11 RING-finger domain and the PY motif. Our results also demonstrate that AMSH is ubiquitinated by Smurf2 E3 ligase in the presence of RNF11 and that a consequent reduction in its steady-state level requires both RNF11 and Smurf2. RNF11 therefore recruits AMSH to Smurf2 for ubiquitination, leading to its degradation by the 26S proteasome. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMURF2 | down-regulates quantity by destabilization
polyubiquitination
|
TGFBR1 |
0.698 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272938 |
|
|
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 11163210 |
Smad7 Recruits Smurf2 to the TGFβ Receptor Complex. Here, we identify Smurf2, a C2-WW-HECT domain ubiquitin ligase and show that Smurf2 associates constitutively with Smad7. Smurf2 is nuclear, but binding to Smad7 induces export and recruitment to the activated TGF beta receptor, where it causes degradation of receptors and Smad7 via proteasomal and lysosomal pathways. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
SMAD7 | up-regulates activity
binding, relocalization
|
SMURF2 |
0.865 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272937 |
|
|
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 11163210 |
Smad7 Recruits Smurf2 to the TGFβ Receptor Complex. Here, we identify Smurf2, a C2-WW-HECT domain ubiquitin ligase and show that Smurf2 associates constitutively with Smad7. Smurf2 is nuclear, but binding to Smad7 induces export and recruitment to the activated TGF beta receptor, where it causes degradation of receptors and Smad7 via proteasomal and lysosomal pathways. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-168450 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19352540 |
Smad7 also recruits the HECT type of E3 ubiquitin ligases, Smurf1 and Smurf2. It binds to Smurfs in the nucleus and translocates into the cytoplasm in response to TGF-_ and recruits the ubiquitin ligases to the activated type I receptor ALK5/T_RI, leading to the degradation of the receptor through the proteasomal pathway. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-104996 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11163210 |
Smurf2 is nuclear, but binding to smad7 induces export and recruitment to the activated tgf beta receptor, where it causes degradation of receptors and smad7 via proteasomal and lysosomal pathways. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-227556 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21791611 |
One of the major mechanisms underlying the inhibitory effect of Smad7 on TGF-_ signaling operates through accelerating T_RI turnover by recruiting ubiquitin E3 ligases such as Smurf1 and Smurf2 |
|
| Publications: |
4 |
Organism: |
Chlorocebus Aethiops, Homo Sapiens |
| + |
SMURF2 | down-regulates
ubiquitination
|
SMAD1 |
0.713 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-153417 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22298955 |
Smurf1 and smurf2 are e3 ubiquitin ligases known to suppress tgf-beta signaling through degra-dation of smads and receptors for tgf-beta and bmps |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMURF2 | down-regulates
ubiquitination
|
SMAD9 |
0.63 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-193390 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22298955 |
Smurf1 and smurf2 are e3 ubiquitin ligases known to suppress tgf-beta signaling through degra-dation of smads and receptors for tgf-beta and bmps |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMURF2 | down-regulates quantity by destabilization
polyubiquitination
|
SMAD7 |
0.865 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272940 |
|
|
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 11163210 |
Smad7 Recruits Smurf2 to the TGFβ Receptor Complex. Here, we identify Smurf2, a C2-WW-HECT domain ubiquitin ligase and show that Smurf2 associates constitutively with Smad7. Smurf2 is nuclear, but binding to Smad7 induces export and recruitment to the activated TGF beta receptor, where it causes degradation of receptors and Smad7 via proteasomal and lysosomal pathways. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
SMURF2 | down-regulates quantity by destabilization
polyubiquitination, ubiquitination
|
SMAD1 |
0.713 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272936 |
|
|
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 11158580 |
Here, we report the identification of Smurf2, a new member of the Hect family of E3 ubiquitin ligases. Smurf2 selectively interacts with receptor-regulated Smads and preferentially targets Smad1 for ubiquitination and proteasome-mediated degradation. At higher expression levels, Smurf2 also decreases the protein levels of Smad2, but not Smad3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120647 |
|
|
Homo sapiens |
Osteoblast |
| pmid |
sentence |
| 22298955 |
Smurf1 and smurf2 are e3 ubiquitin ligases known to suppress tgf-beta signaling through degra-dation of smads and receptors for tgf-beta and bmps |
|
| Publications: |
2 |
Organism: |
Chlorocebus Aethiops, Homo Sapiens |
| Tissue: |
Bone |
| + |
AIMP1 | up-regulates
binding
|
SMURF2 |
0.399 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178498 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18448069 |
Here, we report that aimp1 negatively regulates tgf-? Signaling via stabilization of smurf2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMURF2 | down-regulates activity
ubiquitination
|
TGFBR2 |
0.577 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-195681 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22298955 |
Smurf1 and smurf2 are e3 ubiquitin ligases known to suppress tgf-beta signaling through degradation of smads and receptors for tgf-beta and bmps. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMURF2 | down-regulates activity
ubiquitination
|
TGFBR1 |
0.698 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-104999 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11163210 |
Smurf2 is nuclear, but binding to Smad7 induces export and recruitment to the activated TGF beta receptor, where it causes degradation of receptors and Smad7 via proteasomal and lysosomal pathways. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-153423 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17317136 |
Recruitment of ww and hect domain e3-ubiquitin ligases smurf1 and 2 to induce type i receptor ubiquitination and subsequent receptor degradation; |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
SMURF2 | down-regulates activity
ubiquitination
|
SKIL |
0.728 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236090 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11389444 |
Tgf-beta also induces the association of smurf2 with the transcriptional co-repressor snon and we show that smad2 can function to mediate this interaction. This allows smurf2 hect domain to target snon for ubiquitin-mediated degradation by the proteasome. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
HEK-293T Cell, Mv1Lu Cell |
| + |
SMURF2 | down-regulates
ubiquitination
|
BMPR1A |
0.533 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-192898 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22298955 |
Smurf1 and smurf2 are e3 ubiquitin ligases known to suppress tgf-beta signaling through degra-dation of smads and receptors for tgf-beta and bmps |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMURF2 | form complex 
binding
|
SMAD2/SMURF2 |
0.77 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-108496 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11389444 |
We show that in the presence of tgf-beta, smad2 interacts through its proline-rich ppxy motif with the tryptophan-rich ww domains of smurf2, a recently identified e3 ubiquitin ligases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMURF2 | down-regulates quantity by destabilization
polyubiquitination
|
SMAD2 |
0.77 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272935 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11016919 |
The ability of Smurf2 to promote Smad2 destruction required the HECT catalytic activity of Smurf2 and depended on the proteasome-dependent pathway. Consistent with these results, Smurf2 potently reduced the transcriptional activity of Smad2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMURF2 | down-regulates quantity by destabilization
polyubiquitination
|
TGFBR2 |
0.577 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272939 |
|
|
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 11163210 |
Smad7 Recruits Smurf2 to the TGFβ Receptor Complex. Here, we identify Smurf2, a C2-WW-HECT domain ubiquitin ligase and show that Smurf2 associates constitutively with Smad7. Smurf2 is nuclear, but binding to Smad7 induces export and recruitment to the activated TGF beta receptor, where it causes degradation of receptors and Smad7 via proteasomal and lysosomal pathways. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
ZNF165 | down-regulates quantity by repression
transcriptional regulation
|
SMURF2 |
0.271 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266095 |
|
|
Homo sapiens |
Breast Cancer Cell Line |
| pmid |
sentence |
| 26567849 |
ZNF165 drives the unrestrained activation of transforming growth factor β (TGFβ) signalling by directly inactivating the expression of negative feedback pathway regulators, SMURF2, SMAD7 and PMEPA1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMURF2 | down-regulates activity
ubiquitination
|
SMAD7 |
0.865 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178501 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18448069 |
The association of Smurf2 with Smad7 and its ubiquitination were inhibited by AIMP1, thereby protecting its autocatalytic degradation stimulated by Smad7. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Ub:E2 | up-regulates activity
ubiquitination
|
SMURF2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271298 |
|
|
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 |
| + |
AIMP1 | up-regulates activity
binding
|
SMURF2 |
0.399 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-227470 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18448069 |
Here, we report that AIMP1 negatively regulates TGF-_ signaling via stabilization of Smurf2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMURF2 | down-regulates activity
ubiquitination
|
SMAD2 |
0.77 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236133 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11016919 |
The ability of smurf2 to promote smad2 destruction required the hect catalytic activity of smurf2 and depended on the proteasome-dependent pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
HEK-293 Cell |
| + |
SMAD2 | up-regulates activity
binding
|
SMURF2 |
0.77 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-108490 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11389444 |
We show that in the presence of TGF-beta signalling, Smad2 interacts through its proline-rich PPXY motif with the tryptophan-rich WW domains of Smurf2, a recently identified E3 ubiquitin ligases.Thus, stimulation by TGF-beta can induce the assembly of a Smad2-Smurf2 ubiquitin ligase complex that functions to target substrates for degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMURF2 | down-regulates quantity by destabilization
polyubiquitination
|
STAMBP |
0.546 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272951 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 14755250 |
RNF11 recruits AMSH to Smurf2 E3 ligase. Smurf2 promotes ubiquitination of AMSH in the presence of wt RNF11. Previously, we have shown that RNF11 interacts with the HECT-type E3 ligases AIP4 and Smurf2. Here, we show that RNF11 binds to AMSH in mammalian cells and that this interaction is independent of the RNF11 RING-finger domain and the PY motif. Our results also demonstrate that AMSH is ubiquitinated by Smurf2 E3 ligase in the presence of RNF11 and that a consequent reduction in its steady-state level requires both RNF11 and Smurf2. RNF11 therefore recruits AMSH to Smurf2 for ubiquitination, leading to its degradation by the 26S proteasome. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMURF2 | down-regulates
ubiquitination
|
SMAD5 |
0.725 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-193378 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22298955 |
Smurf1 and smurf2 are e3 ubiquitin ligases known to suppress tgf-beta signaling through degra-dation of smads and receptors for tgf-beta and bmps |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMURF2 | down-regulates quantity by destabilization
ubiquitination
|
SMAD5 |
0.725 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-153420 |
|
|
Homo sapiens |
Osteoblast |
| pmid |
sentence |
| 22298955 |
Smurf1 and smurf2 are e3 ubiquitin ligases known to suppress tgf-beta signaling through degra-dation of smads and receptors for tgf-beta and bmps |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Bone |
3.0
SMURF2
- 
- 