Accession_id | Subsection | Start | End | Funcitonal feature | Spricing information |
P25445 | Topological domain | 26 | 173 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=66;End=103 |
P25445 | Topological domain | 26 | 173 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=104;End=335 |
P25445 | Topological domain | 26 | 173 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=66;End=86 |
P25445 | Topological domain | 26 | 173 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=87;End=335 |
P25445 | Topological domain | 26 | 173 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=112;End=149 |
P25445 | Topological domain | 26 | 173 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=150;End=335 |
P25445 | Topological domain | 26 | 173 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=112;End=132 |
P25445 | Topological domain | 26 | 173 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=133;End=335 |
P25445 | Topological domain | 26 | 173 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=169;End=189 |
P25445 | Transmembrane | 174 | 190 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=104;End=335 |
P25445 | Transmembrane | 174 | 190 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=87;End=335 |
P25445 | Transmembrane | 174 | 190 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=150;End=335 |
P25445 | Transmembrane | 174 | 190 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=133;End=335 |
P25445 | Transmembrane | 174 | 190 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=169;End=189 |
P25445 | Topological domain | 191 | 335 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=104;End=335 |
P25445 | Topological domain | 191 | 335 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=87;End=335 |
P25445 | Topological domain | 191 | 335 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=150;End=335 |
P25445 | Topological domain | 191 | 335 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=133;End=335 |
P25445 | Topological domain | 191 | 335 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=218;End=220 |
P25445 | Topological domain | 191 | 335 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=221;End=335 |
P25445 | Repeat | 47 | 83 | Note=TNFR-Cys 1 | Type=Substitution;Start=66;End=103 |
P25445 | Repeat | 47 | 83 | Note=TNFR-Cys 1 | Type=Substitution;Start=66;End=86 |
P25445 | Repeat | 84 | 127 | Note=TNFR-Cys 2 | Type=Substitution;Start=66;End=103 |
P25445 | Repeat | 84 | 127 | Note=TNFR-Cys 2 | Type=Deletion;Start=104;End=335 |
P25445 | Repeat | 84 | 127 | Note=TNFR-Cys 2 | Type=Substitution;Start=66;End=86 |
P25445 | Repeat | 84 | 127 | Note=TNFR-Cys 2 | Type=Deletion;Start=87;End=335 |
P25445 | Repeat | 84 | 127 | Note=TNFR-Cys 2 | Type=Substitution;Start=112;End=149 |
P25445 | Repeat | 84 | 127 | Note=TNFR-Cys 2 | Type=Substitution;Start=112;End=132 |
P25445 | Repeat | 128 | 166 | Note=TNFR-Cys 3 | Type=Deletion;Start=104;End=335 |
P25445 | Repeat | 128 | 166 | Note=TNFR-Cys 3 | Type=Deletion;Start=87;End=335 |
P25445 | Repeat | 128 | 166 | Note=TNFR-Cys 3 | Type=Substitution;Start=112;End=149 |
P25445 | Repeat | 128 | 166 | Note=TNFR-Cys 3 | Type=Deletion;Start=150;End=335 |
P25445 | Repeat | 128 | 166 | Note=TNFR-Cys 3 | Type=Substitution;Start=112;End=132 |
P25445 | Repeat | 128 | 166 | Note=TNFR-Cys 3 | Type=Deletion;Start=133;End=335 |
P25445 | Domain | 230 | 314 | Note=Death;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00064 | Type=Deletion;Start=104;End=335 |
P25445 | Domain | 230 | 314 | Note=Death;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00064 | Type=Deletion;Start=87;End=335 |
P25445 | Domain | 230 | 314 | Note=Death;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00064 | Type=Deletion;Start=150;End=335 |
P25445 | Domain | 230 | 314 | Note=Death;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00064 | Type=Deletion;Start=133;End=335 |
P25445 | Domain | 230 | 314 | Note=Death;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00064 | Type=Deletion;Start=221;End=335 |
P25445 | Region | 212 | 317 | Note=Interaction with HIPK3;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=104;End=335 |
P25445 | Region | 212 | 317 | Note=Interaction with HIPK3;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=87;End=335 |
P25445 | Region | 212 | 317 | Note=Interaction with HIPK3;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=150;End=335 |
P25445 | Region | 212 | 317 | Note=Interaction with HIPK3;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=133;End=335 |
P25445 | Region | 212 | 317 | Note=Interaction with HIPK3;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Substitution;Start=218;End=220 |
P25445 | Region | 212 | 317 | Note=Interaction with HIPK3;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=221;End=335 |
P25445 | Region | 230 | 254 | Note=Interaction with CALM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24914971;Dbxref=PMID:24914971 | Type=Deletion;Start=104;End=335 |
P25445 | Region | 230 | 254 | Note=Interaction with CALM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24914971;Dbxref=PMID:24914971 | Type=Deletion;Start=87;End=335 |
P25445 | Region | 230 | 254 | Note=Interaction with CALM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24914971;Dbxref=PMID:24914971 | Type=Deletion;Start=150;End=335 |
P25445 | Region | 230 | 254 | Note=Interaction with CALM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24914971;Dbxref=PMID:24914971 | Type=Deletion;Start=133;End=335 |
P25445 | Region | 230 | 254 | Note=Interaction with CALM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24914971;Dbxref=PMID:24914971 | Type=Deletion;Start=221;End=335 |
UniProt-id | Site score | Size | D score | Volume | Exposure | Enclosure | Contact | Phobic | Philic | Balance | Don/Acc | Residues |
P25445-1 | 0.673 | 33 | 0.477 | 120.736 | 0.68 | 0.675 | 0.955 | 0.203 | 1.435 | 0.142 | 0.854 | 105,125,126,127,128,129,135,136,137,138,139,140,15 9,160
|
P25445-2 | 0.684 | 14 | 0.71 | 22.981 | 0.588 | 0.631 | 1.034 | 2.397 | 0.064 | 37.342 | | 8,9,12,13,16,98,102
|
P25445-3 | 0.513 | 14 | 0.457 | 38.416 | 0.77 | 0.56 | 0.782 | 0.713 | 0.707 | 1.008 | 0.862 | 59,60,61,62,63,76
|
P25445-4 | 0.972 | 224 | 1.019 | 568.694 | 0.66 | 0.611 | 0.841 | 0.495 | 0.884 | 0.56 | 0.914 | 65,66,88,89,91,92,93,94,96,98,100,101,102,103,104, 105,106,107,108,109,111,113,115,117,120,121,122,12 3,124,126,136,137,138,139,140,141,142,143,144,145, 146,147,148,149
|
P25445-5 | 1.026 | 105 | 1.089 | 188.307 | 0.516 | 0.65 | 0.9 | 0.864 | 0.737 | 1.172 | 1.81 | 65,66,67,84,85,86,87,88,90,91,92,93,104,121,122,12 3,124,125
|
P25445-6 | 0.987 | 93 | 1.043 | 282.632 | 0.711 | 0.632 | 0.668 | 0.401 | 0.744 | 0.54 | 1.069 | 170,171,172,173,174,175,178,179,181,182,183,185,18 6,271,274,275,278,281,282,283,284,287
|
P25445-7 | 0.734 | 54 | 0.668 | 133.084 | 0.686 | 0.592 | 0.777 | 0.12 | 1.158 | 0.103 | 1.157 | 105,124,125,126,127,128,129,135,137,138,139,140,15 9,160
|
Accession_id | Subsection | Start | End | Funcitonal feature | Spricing information |
P25445 | Region | 212 | 317 | Note=Interaction with HIPK3;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=104;End=335 |
P25445 | Region | 212 | 317 | Note=Interaction with HIPK3;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=87;End=335 |
P25445 | Region | 212 | 317 | Note=Interaction with HIPK3;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=150;End=335 |
P25445 | Region | 212 | 317 | Note=Interaction with HIPK3;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=133;End=335 |
P25445 | Region | 212 | 317 | Note=Interaction with HIPK3;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Substitution;Start=218;End=220 |
P25445 | Region | 212 | 317 | Note=Interaction with HIPK3;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=221;End=335 |
P25445 | Region | 230 | 254 | Note=Interaction with CALM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24914971;Dbxref=PMID:24914971 | Type=Deletion;Start=104;End=335 |
P25445 | Region | 230 | 254 | Note=Interaction with CALM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24914971;Dbxref=PMID:24914971 | Type=Deletion;Start=87;End=335 |
P25445 | Region | 230 | 254 | Note=Interaction with CALM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24914971;Dbxref=PMID:24914971 | Type=Deletion;Start=150;End=335 |
P25445 | Region | 230 | 254 | Note=Interaction with CALM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24914971;Dbxref=PMID:24914971 | Type=Deletion;Start=133;End=335 |
P25445 | Region | 230 | 254 | Note=Interaction with CALM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24914971;Dbxref=PMID:24914971 | Type=Deletion;Start=221;End=335 |
Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
FAS | 12855687 | Oligomerization of soluble Fas antigen induces its cytotoxicity. | "Soluble Fas antigen can protect cells against Fas-mediated apoptosis. High level soluble Fas antigen characteristic for blood of patients with autoimmune disease or cancer is believed to prevent the elimination of autoimmune lymphocytes or tumor cells. Here we first report that human recombinant FasDeltaTM, i.e. soluble Fas generated by alternative splicing of the intact exon 6, is capable of inducing death of transformed cells by ""reverse"" apoptotic signaling via transmembrane Fas ligand. FasDeltaTM, as well as transmembrane Fas antigen, can be either monomeric or oligomeric, and both its forms are efficient in blocking Fas-mediated apoptosis, although the cytotoxic activity is exhibited solely by the latter. An in vivo analysis of soluble Fas antigen showed that unlike in healthy controls, nearly the total FasDeltaTM present in sera of rheumatoid arthritis patients was oligomeric. This resulted in suppression of cell proliferation in the experimental sera and in its promotion in controls. Thus, oligomerization/depolymerization of soluble Fas antigen can regulate its activity and contribute to the pathogenesis of autoimmune diseases and cancer." | D001172 | Arthritis, Rheumatoid |
FAS | 12855687 | Oligomerization of soluble Fas antigen induces its cytotoxicity. | "Soluble Fas antigen can protect cells against Fas-mediated apoptosis. High level soluble Fas antigen characteristic for blood of patients with autoimmune disease or cancer is believed to prevent the elimination of autoimmune lymphocytes or tumor cells. Here we first report that human recombinant FasDeltaTM, i.e. soluble Fas generated by alternative splicing of the intact exon 6, is capable of inducing death of transformed cells by ""reverse"" apoptotic signaling via transmembrane Fas ligand. FasDeltaTM, as well as transmembrane Fas antigen, can be either monomeric or oligomeric, and both its forms are efficient in blocking Fas-mediated apoptosis, although the cytotoxic activity is exhibited solely by the latter. An in vivo analysis of soluble Fas antigen showed that unlike in healthy controls, nearly the total FasDeltaTM present in sera of rheumatoid arthritis patients was oligomeric. This resulted in suppression of cell proliferation in the experimental sera and in its promotion in controls. Thus, oligomerization/depolymerization of soluble Fas antigen can regulate its activity and contribute to the pathogenesis of autoimmune diseases and cancer." | D009369 | Neoplasms |
FAS | 19751723 | Identification, characterisation and regulation by CD40 activation of novel CD95 splice variants in CD95-apoptosis-resistant, human, B-cell non-Hodgkin's lymphoma. | CD95 gene and splicing aberrations have been detected in B-cell non-Hodgkin lymphoma (B-NHL) where they are thought to contribute to CD95 apoptosis resistance. To further investigate this, we have performed extensive CD95 transcript sequencing and functional analysis in B-NHL with demonstrated resistance to CD95-induced apoptosis (B-NHLr). Strikingly, instead of showing CD95 mutations per se, B cells from B-NHLr co-expressed wild-type and multiple, normal (CD95nv) and novel alternatively spliced variant CD95 transcripts (CD95av). CD95av were predicted, by sequencing, to encode soluble, potentially apoptosis inhibitory proteins. However, their overexpression, by transfection, in Jurkat cells did not interfere with endogenous CD95 death signalling. Furthermore, CD95av-expressing B-NHLr did not show mutations in CD95 splice-regulatory elements and CD95av expression was 'reversible' by CD40 activation. This, in conjunction with treatment by the protein synthesis inhibitor, cycloheximide, could sensitise a subset of B-NHLr to CD95 apoptosis. In normal and lymphoma B cells, this correlated to increased CD95 membrane expression, enhanced DISC activity and engagement of the mitochondrial death pathway via Bid cleavage, although the latter occurred less efficiently in B-NHLr. Thus, immune modulation of CD95 transcription and alternative splicing combined with enhanced engagement of mitochondrial death signalling offer potential for restoration of CD95 apoptosis sensitivity in B-NHLr. | D016393 | Lymphoma, B-Cell |
FAS | 25411246 | Interleukin 7 up-regulates CD95 protein on CD4+ T cells by affecting mRNA alternative splicing: priming for a synergistic effect on HIV-1 reservoir maintenance. | Interleukin-7 (IL-7) has been used as an immunoregulatory and latency-reversing agent in human immunodeficiency virus type 1 (HIV-1) infection. Although IL-7 can restore circulating CD4(+) T cell counts in HIV-1-infected patients, the anti-apoptotic and proliferative effects of IL-7 appear to benefit survival and expansion of HIV-1-latently infected memory CD4(+) T lymphocytes. IL-7 has been shown to elevate CD95 on CD4(+) T cells in HIV-1-infected individuals and prime CD4(+) T lymphocytes to CD95-mediated proliferative or apoptotic signals. Here we observed that through increasing microRNA-124, IL-7 down-regulates the splicing regulator polypyrimidine tract binding protein (PTB), leading to inclusion of the transmembrane domain-encoding exon 6 of CD95 mRNA and, subsequently, elevation of CD95 on memory CD4(+) T cells. Moreover, IL-7 up-regulates cellular FLICE-like inhibitory protein (c-FLIP) and stimulates c-Jun N-terminal kinase (JNK) phosphorylation, which switches CD95 signaling to survival mode in memory CD4(+) T lymphocytes. As a result, co-stimulation through IL-7/IL-7R and FasL/CD95 signal pathways augments IL-7-mediated survival and expansion of HIV-1-latently infected memory CD4(+) T lymphocytes. Collectively, we have demonstrated a novel mechanism for IL-7-mediated maintenance of HIV-1 reservoir. | D015658 | HIV Infections |