| + |
TRAF2 | up-regulates activity 
ubiquitination
|
MAP3K7 |
0.582 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-162638 |
Lys158 |
ALIHRDLkPPNLLLV |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 20038579 |
Tumor necrosis factor receptor-associated factors 2 and 6 (traf2 and -6) act as the ubiquitin e3 ligases to mediate lys63-linked tak1 polyubiquitination at the lys158 residue in vivo and in vitro. Lys(63)-linked TAK1 polyubiquitination at the Lys(158) residue is required for TAK1-mediated IKK complex recruitment. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | IL1 Signaling , Inhibition of Apoptosis, NF-KB Canonical, P38 Signaling, SAPK/JNK Signaling |
| + |
TRAF2 | up-regulates activity
ubiquitination, binding
|
RIPK1 |
0.892 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-42984 |
Lys377 |
NEPSLQSkLQDEANY |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 8702708 |
Following binding to tradd, traf2 was thought to mediate non-degradative lys-63-linked polyubiquitination of rip1 via its ring e3 ligase domain. Rip1 is known to directly interact with traf2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235407 |
Lys377 |
NEPSLQSkLQDEANY |
Mus musculus |
MEF Cell, Macrophage |
| pmid |
sentence |
| 21232017 |
Following binding to tradd, traf2 was thought to mediate non-degradative lys-63-linked polyubiquitination of rip1 via its ring e3 ligase domain. Rip1 is known to directly interact with traf2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179456 |
Lys377 |
NEPSLQSkLQDEANY |
Homo sapiens |
|
| pmid |
sentence |
| 18621737 |
Following binding to tradd, traf2 was thought to mediate non-degradative lys-63-linked polyubiquitination of rip1 via its ring e3 ligase domain. Rip1 is known to directly interact with traf2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-59689 |
Lys377 |
NEPSLQSkLQDEANY |
Homo sapiens |
|
| pmid |
sentence |
| 9712898 |
Following binding to tradd, traf2 was thought to mediate non-degradative lys-63-linked polyubiquitination of rip1 via its ring e3 ligase domain. Rip1 is known to directly interact with traf2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271423 |
|
|
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 15175328 |
Taken together, these data suggest that Traf2 may be the E3 ubiquitin ligase that initiates TNF-α signaling, potentially by ubiquitinating Rip1. In the absence of Traf2, TNF-alpha-induced ubiquitination of Rip1 is impaired, suggesting that Traf2 may be the E3 ubiquitin ligase responsible for the TNF-alpha-dependent, ubiquitination of Rip1. Finally, recruitment of the ubiquitinated Tak1 complex is dependent on the presence of Rip1, suggesting that Rip1 ubiquitination rather than its phosphorylation is critical in signaling. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245032 |
|
|
Mus musculus |
MEF Cell, Macrophage |
| pmid |
sentence |
| 21232017 |
Rip1 is known to directly interact with traf2 |
|
| Publications: |
6 |
Organism: |
Homo Sapiens, Mus Musculus |
| Pathways: | Multiple sclerosis, NF-KB Canonical, SAPK/JNK Signaling, TNF-alpha Signaling |
| + |
PRKCZ |
phosphorylation
|
TRAF2 |
0.415 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-184941 |
Ser55 |
QCGHRYCsFCLASIL |
Homo sapiens |
Lymphoma Cell |
| pmid |
sentence |
| 19336568 |
Here, we report that protein kinase czeta phosphorylates traf2 at ser(55), within the ring domain of the protein, after tnfalpha stimulation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP2CA | down-regulates activity 
dephosphorylation
|
TRAF2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248640 |
Thr117 |
DGCTWKGtLKEYESC |
Mus musculus |
|
| pmid |
sentence |
| 17188031 |
We show that the Thr117 residue in TRAF2 is phosphorylated following TNFalpha stimulation. This phosphorylation process is modulated by PP2A and is required for TRAF2 functional activity. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PPP2CB | down-regulates activity
dephosphorylation
|
TRAF2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248597 |
Thr117 |
DGCTWKGtLKEYESC |
Mus musculus |
|
| pmid |
sentence |
| 17188031 |
We show that the Thr117 residue in TRAF2 is phosphorylated following TNFalpha stimulation. This phosphorylation process is modulated by PP2A and is required for TRAF2 functional activity. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
TRAF2 | up-regulates
binding
|
BIRC3 |
0.889 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164785 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20385093 |
A traf2 trimer interacts with one ciap2 both in the crystal and in solution through its death domain and amino-terminal region, tradd recruits rip1 (receptor-interacting protein), traf2, and through its interaction with traf2, c-iap1 and c-iap2 (13). Traf2 recruit ciap1 and ciap2. A traf2 trimer interacts with one ciap2 both in the crystal and in solution. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-39596 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8548810 |
The c-iaps associate with traf1 and traf2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179452 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18621737 |
A traf2 trimer interacts with one ciap2 both in the crystal and in solution through its death domain and amino-terminal region, tradd recruits rip1 (receptor-interacting protein), traf2, and through its interaction with traf2, c-iap1 and c-iap2 (13). Traf2 recruit ciap1 and ciap2. A traf2 trimer interacts with one ciap2 both in the crystal and in solution. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182124 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18997792 |
A traf2 trimer interacts with one ciap2 both in the crystal and in solution through its death domain and amino-terminal region, tradd recruits rip1 (receptor-interacting protein), traf2, and through its interaction with traf2, c-iap1 and c-iap2 (13). Traf2 recruit ciap1 and ciap2. A traf2 trimer interacts with one ciap2 both in the crystal and in solution. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182137 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18997794 |
A traf2 trimer interacts with one ciap2 both in the crystal and in solution through its death domain and amino-terminal region, tradd recruits rip1 (receptor-interacting protein), traf2, and through its interaction with traf2, c-iap1 and c-iap2 (13). Traf2 recruit ciap1 and ciap2. A traf2 trimer interacts with one ciap2 both in the crystal and in solution. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| Pathways: | IL1 Signaling |
| + |
TRADD | up-regulates activity
binding
|
TRAF2 |
0.867 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-42980 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27383048 |
Upon stimulation with TNFα, TNFR1 recruits TRADD, which provides a scaffold for the assembly of complex I at the plasma membrane by binding with RIP1, TRAF2 and cIAP. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179446 |
|
|
Mus musculus |
Fibrosarcoma Cell |
| pmid |
sentence |
| 18621737 |
The high affinity of the tradd-traf2 interaction is required for efficient suppression of apoptosis upon stimulation of the tumor necrosis factor receptor1 (tnfr1), tnf-receptor-associated death domain (tradd) provides a scaffold for the assembly of complex i at the plasma membrane by binding receptor interacting protein 1 (rip1), tnfreceptor- associated factor 2 ,traf2 these results provide evidence that tradd can serve as an adaptor protein and recruit traf1, traf2, or both to tnfrsf1a. The demonstration that tradd interacts with traf2 and fadd, and can recruit both to tnfrsf1a, suggested that traf2 and fadd may be involved in tnfrsf1a tradd-mediated signaling. That these interactions define two distinct signaling pathways emanating from tradd (figure 9) is supported by the ability of traf2 and fadd to activate nf-kb and induce apoptosis, respectively. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-118770 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 14585074 |
Tradd mediates recruitment of the traf2 adaptor protein |
|
| Publications: |
3 |
Organism: |
Homo Sapiens, Mus Musculus |
| Pathways: | Inhibition of Apoptosis, NF-KB Canonical, P38 Signaling, TNF-alpha Signaling |
| + |
ERN1 | up-regulates activity
binding
|
TRAF2 |
0.669 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262790 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 18519638 |
Activated IRE1 has been demonstrated to recruit TRAF2 and ASK1 on the ER membrane and thus to activate ASK1|ASK1 was found to associate with IRE1 only in the presence of TRAF2 and SOD1mut (Fig. 4B), suggesting that SOD1mut induces formation of an IRE1–TRAF2–ASK1 complex on the ER membrane and thus activates ASK1 by triggering ER stress-induced IRE1 activation. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
BIRC2 | down-regulates quantity by destabilization
ubiquitination
|
TRAF2 |
0.869 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182128 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18997794 |
Traf3-binding receptors stabilize nik by activating ciap-dependent degradation of traf2 and traf3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167057 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20651737 |
Engagement of cd40 with its ligand cd40l results in the recruitment of the TRAF3/TRAF2/cIAP Complex to the receptor. At the receptor, traf3 undergoes ciap-dependent k48-linked polyubiquitylation (ub) that targets it for proteasomal degradation. In the absence of traf3, nik protein levels accumulate as it can no longer be recruited to the TRAF2/cIAP Complex. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | NF-KB Non Canonical |
| + |
CYLD | down-regulates activity
deubiquitination
|
TRAF2 |
0.666 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-117860 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12917691 |
Cyld also interacts directly with tumour-necrosis factor receptor (tnfr)-associated factor 2 (traf2), an adaptor molecule involved in by members of the family of tnf/nerve growth factor receptors. (articolo-abstract) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | NF-KB Canonical |
| + |
TANK | down-regulates activity
binding
|
TRAF2 |
0.723 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262714 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 10759890 |
IKK-i phosphorylates I-TRAF. In vitro kinase assays demonstrate that IKK‐i phosphorylates I‐TRAF in the middle portion that associates with TRAF2. Interestingly, TRAF2 is freed from the I‐TRAF/TRAF2 complex after I‐TRAF phosphorylation. TRAF2 isdistributed throughout the cytoplasm, in the formof inactive an I-TRAF/TRAF2 complex |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
UBE2N | up-regulates activity
ubiquitination
|
TRAF2 |
0.437 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121274 |
|
|
Homo sapiens |
Lymphoma Cell |
| pmid |
sentence |
| 14713952 |
Intact ring and zinc finger domains are required for tnfalfa-induced traf2 ubiquitination, which is also dependent on ubc13. Traf2 ubiquitination coincides with its translocation to the insoluble cellular fraction, resulting in selective activation of jnk. Ubc13 expression by rnai resulted in tnfalfa-induced traf2 translocation and impaired activation of jnk but not of ikk or p38. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | IL1 Signaling , NF-KB Canonical |
| + |
TRAF2 | up-regulates activity
binding
|
MAP3K5 |
0.729 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-75334 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10688666 |
Tnf receptor (tnfr) associated factor 2 (traf2), an adapter protein that couples tnfrs to the sapks and p38s, can activate ask1 in vivo and can interact in vivo with the amino- and carboxyl-terminal noncatalytic domains of the ask1 polypeptide |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-60747 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9774977 |
Traf2 is a strong activator of ask1 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | P38 Signaling, TNF-alpha Signaling |
| + |
LTBR | up-regulates activity
binding
|
TRAF2 |
0.571 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-97950 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12571250 |
Endogenous association of traf2, traf3, ciap1, and smac with lymphotoxin beta receptor reveals a novel mechanism of apoptosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | NF-KB Non Canonical |
| + |
TRAF2 | down-regulates quantity by destabilization
binding, ubiquitination
|
MAP3K14 |
0.572 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124233 |
|
|
Mus musculus |
Lymphoma Cell |
| pmid |
sentence |
| 15084608 |
We report here that one important mechanism of nik regulation is through its dynamic interaction with the tumor necrosis factor receptor-associated factor 3 (traf3). Traf3 physically associates with nik via a specific sequence motif located in the n-terminal region of nik; this molecular interaction appears to target nik for degradation by the proteasome. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167066 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20651737 |
Under resting conditions cellular inhibitor of apoptosis (ciap) proteins target nuclear factor-kb (nf-kb)-inducing kinase (nik) for ubiquitylation and proteasomal degradation. |
|
| Publications: |
2 |
Organism: |
Mus Musculus, Homo Sapiens |
| Pathways: | NF-KB Non Canonical |
| + |
TRAF2 | up-regulates
polyubiquitination
|
TICAM1 |
0.44 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271427 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20047764 |
Here, we show that the TRAF family proteins directly bind TICAM-1 and demonstrate that TRAF2 and TRAF6 bind different sites of the N-terminal TICAM-1 and accelerate its polyubiquitination. we speculate that polyubiquitination of TICAM-1 by TRAF2 and TRAF6 is required for TICAM-1 to induce IRF-3 and NF-κB activation. This is supported by the observation that polyubiquitination of TICAM-1 was required for TRAF3-binding to TICAM-1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TRAF2 | up-regulates activity
binding
|
BIRC2 |
0.869 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-39527 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8548810 |
The c-iaps associate with traf1 and traf3 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179449 |
|
|
Homo sapiens |
Fibrosarcoma Cell |
| pmid |
sentence |
| 18621737 |
Through its death domain and amino-terminal region, tradd recruits rip1 (receptor-interacting protein), traf2, and through its interaction with traf2, c-iap1 and c-iap2. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | NF-KB Non Canonical |
| + |
TRAF1 | up-regulates
binding
|
TRAF2 |
0.621 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-34768 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8069916 |
Traf1 and traf2 can form homo- and heterotypic dimers. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | SAPK/JNK Signaling |
| + |
TRAF2 | up-regulates activity
binding
|
UBE2N |
0.437 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179479 |
|
|
Homo sapiens |
Fibrosarcoma Cell |
| pmid |
sentence |
| 18635759 |
Traf2, ubc13, and ikkgamma were required for complex assembly and activation of mekk1 and mapk cascades. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | IL1 Signaling , NF-KB Canonical |
| + |
TRAF2 | up-regulates
binding
|
MAP3K1 |
0.707 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179476 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18635759 |
Traf2, ubc13, and ikkgamma were required for complex assembly and activation of mekk1 and mapk cascades. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-67552 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10346818 |
Oligomerization of the traf2 effector domain results in specific binding to mekk1, a protein kinase capable of jnk, p38, and ikk activation |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | SAPK/JNK Signaling, TNF-alpha Signaling |
| + |
TRAF2 | up-regulates
binding
|
TRAF1 |
0.621 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-35881 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8069916 |
Our analysis indicates that traf1 and traf2 are associated with the cytoplasmic domain of tnf-r2 in a heterodimeric complex in which traf2 contacts the receptor directly. Traf1 interacts with tnf-r2 indirectly through heterodimer formation with traf2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | SAPK/JNK Signaling |
| + |
TRAF2 | up-regulates
binding
|
MAP4K2 |
0.518 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-59685 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9712898 |
Both full-lenght gck and the gck-ctd can form complexes in vivo with traf2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | SAPK/JNK Signaling |
| + |
BIRC3 | down-regulates quantity by destabilization
ubiquitination
|
TRAF2 |
0.889 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182131 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18997794 |
Traf3-binding receptors stabilize nik by activating ciap-dependent degradation of traf2 and traf3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | IL1 Signaling |
| + |
Ub:E2 | up-regulates activity
ubiquitination
|
TRAF2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270988 |
|
|
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 |
| + |
TNFRSF1A | up-regulates
|
TRAF2 |
0.828 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256251 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10795740 |
We found that TNF-R1-mediated IKK activation requires both RIP and TRAF2 proteins. Although TRAF2 or RIP can be independently recruited to the TNF-R1 complex, neither one of them alone is capable of transducing the TNF signal that leads to IKK activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Inhibition of Apoptosis, Multiple sclerosis, NF-KB Canonical, P38 Signaling, TNF-alpha Signaling |
| + |
TRAF2 | up-regulates
|
RIPK1 |
0.892 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256252 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10795740 |
We found that TNF-R1-mediated IKK activation requires both RIP and TRAF2 proteins. Although TRAF2 or RIP can be independently recruited to the TNF-R1 complex, neither one of them alone is capable of transducing the TNF signal that leads to IKK activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Multiple sclerosis, NF-KB Canonical, SAPK/JNK Signaling, TNF-alpha Signaling |
| + |
TRAF2 | up-regulates activity
binding
|
MAP3K14 |
0.572 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-46215 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9020361 |
NIK binds to Traf2 and stimulates NF-kappaB activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | NF-KB Non Canonical |
| + |
RELA | up-regulates quantity by expression 
transcriptional regulation
|
TRAF2 |
0.52 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-59960 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9733516 |
Thus, our data indicate that nf-kb controls the expression of traf1 and traf2 and c-iap1 and c-iap2 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CD40 | up-regulates activity
binding
|
TRAF2 |
0.839 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179473 |
|
|
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 18635759 |
Cd40, a tumor necrosis factor receptor (tnfr) family member, forms a complex containing adaptor molecules traf2 and traf3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Multiple sclerosis, NF-KB Non Canonical |
| + |
TNFRSF1B | up-regulates activity
binding
|
TRAF2 |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-34645 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8069916 |
Our analysis indicates that traf1 and traf2 are associated with the cytoplasmic domain of tnf-r2 in a heterodimeric complex in which traf2 contacts the receptor directly. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | SAPK/JNK Signaling |
3.0
TRAF2
- 
- 