+ |
PRKCB | up-regulates quantity by stabilization
phosphorylation
|
CFLAR |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276146 |
Ser193 |
LQAAIQKsLKDPSNN |
Homo sapiens |
K-562 Cell |
pmid |
sentence |
19343040 |
Here, we identify serine 193 as a novel in vivo phosphorylation site of all c-FLIP proteins. c-FLIP S193 phosphorylation is mediated by PKCa and PKCb.S193 phosphorylation increases the stability of the short c-FLIP proteins |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKCA | up-regulates quantity by stabilization
phosphorylation
|
CFLAR |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276147 |
Ser193 |
LQAAIQKsLKDPSNN |
Homo sapiens |
K-562 Cell |
pmid |
sentence |
19343040 |
Here, we identify serine 193 as a novel in vivo phosphorylation site of all c-FLIP proteins. c-FLIP S193 phosphorylation is mediated by PKCa and PKCb.S193 phosphorylation increases the stability of the short c-FLIP proteins |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AKT | down-regulates quantity
phosphorylation
|
CFLAR |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-245304 |
Ser273 |
LLRDTFTsLGYEVQK |
Homo sapiens |
|
pmid |
sentence |
19339247 |
TNFalpha enhanced FLIP(L) serine phosphorylation, which was increased by activated Akt-1. Serine 273, a putative Akt-1 phosphorylation site in FLIP(L), was critical for the activation-induced reduction of FLIP(L). Thus, these observations document a novel mechanism where by TNFalpha facilitates the reduction of FLIP(L) protein, which is dependent on the phosphatidylinositol 3-kinase/Akt signaling. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AKT1 | down-regulates quantity
phosphorylation
|
CFLAR |
0.48 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252548 |
Ser273 |
LLRDTFTsLGYEVQK |
Homo sapiens |
|
pmid |
sentence |
19339247 |
TNFalpha enhanced FLIP(L) serine phosphorylation, which was increased by activated Akt-1. Serine 273, a putative Akt-1 phosphorylation site in FLIP(L), was critical for the activation-induced reduction of FLIP(L). Thus, these observations document a novel mechanism where by TNFalpha facilitates the reduction of FLIP(L) protein, which is dependent on the phosphatidylinositol 3-kinase/Akt signaling. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CBL | down-regulates quantity by destabilization
ubiquitination
|
CFLAR |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-186998 |
|
|
Homo sapiens |
|
pmid |
sentence |
19597496 |
We therefore conclude that c-cbl is a e3 ubiquitin ligase for flips and that the interaction of flips with c-cbl requires phosphorylation of both ser4 and tyr211 of flips.This interaction triggered proteasomal degradation of FLIP(S), which promoted activation of caspase-8 and apoptosis. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RUNX3 | down-regulates quantity by repression
transcriptional regulation
|
CFLAR |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255087 |
|
|
Homo sapiens |
|
pmid |
sentence |
17956589 |
Comprehensive analysis using a cDNA microarray showed that RUNX3 upregulated 17 apoptosis-related genes (including FADD, TRAF6, caspase-2, ING1, ING4, Calpain 10, and DNase1) and downregulated 135 apoptosis-related genes (including FLIP, PEA15, TXN2, HSPD1, IKK, and TIAL1) in MKN-1 cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK14 | up-regulates
phosphorylation
|
CFLAR |
0.381 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-187001 |
|
|
Homo sapiens |
|
pmid |
sentence |
19597496 |
Here we demonstrate that m. tuberculosis?induced Tnf triggered reactive oxygen species?dependent Activation of ask1 and the tyrosine kinase c-abl (a000161) in mouse macrophages and that flips was phosphorylated on tyr211 and ser4 by c-abl and p38, respectively. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ITCH | down-regulates quantity
ubiquitination
|
CFLAR |
0.601 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-245307 |
|
|
Mus musculus |
|
pmid |
sentence |
16469705 |
Depends on JNK-mediated phosphorylation and activation of the E3 ubiquitin ligase Itch, which specifically ubiquitinates c-FLIP and induces its proteasomal degradation. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
CFLAR | down-regulates activity
binding
|
CASP8 |
0.76 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-61122 |
|
|
Homo sapiens |
|
pmid |
sentence |
9794838 |
Flip can be incorporated into the disc complex and blocks processing and activation of pro-caspase8 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-96402 |
|
|
Homo sapiens |
|
pmid |
sentence |
14585074 |
Flip can be incorporated into the disc complex and blocks processing and activation of pro-caspase8 |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | Death Receptor Signaling |