Protein:CASP8 |
Protein Summary |
 Gene summary |
| Gene name: CASP8 | ASpdb.0 ID: 841 | Gene | Gene symbol | CASP8 | Gene ID | 841 |
| Gene name | caspase 8 |
| Synonyms | ALPS2B|CAP4|Casp-8|FLICE|MACH|MCH5 |
| Cytomap | 2q33.1 |
| Type of gene | protein-coding |
| Description | caspase-8FADD-homologous ICE/CED-3-like proteaseFADD-like ICEICE-like apoptotic protease 5MACH-alpha-1/2/3 proteinMACH-beta-1/2/3/4 proteinMORT1-associated ced-3 homologapoptotic cysteine proteaseapoptotic protease Mch-5caspase 8, apoptosis-relat |
| Modification date | 20240411 |
| UniProtAcc | Q14790 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | CASP8 | GO:0004197 | cysteine-type endopeptidase activity | 16920334|19240112|32929201|33852854|34012073|35594856 |
| Gene | CASP8 | GO:0005654 | nucleoplasm | - |
| Gene | CASP8 | GO:0005737 | cytoplasm | 17167422 |
| Gene | CASP8 | GO:0005829 | cytosol | 17167422 |
| Gene | CASP8 | GO:0006508 | proteolysis | 12888622 |
| Gene | CASP8 | GO:0008233 | peptidase activity | 19740745 |
| Gene | CASP8 | GO:0030027 | lamellipodium | 18216014 |
| Gene | CASP8 | GO:0030335 | positive regulation of cell migration | 18216014 |
| Gene | CASP8 | GO:0031264 | death-inducing signaling complex | 11101870|21803845 |
| Gene | CASP8 | GO:0031265 | CD95 death-inducing signaling complex | 11717445 |
| Gene | CASP8 | GO:0032991 | protein-containing complex | 22267217 |
| Gene | CASP8 | GO:0036462 | TRAIL-activated apoptotic signaling pathway | 21785459 |
| Gene | CASP8 | GO:0045862 | positive regulation of proteolysis | 18387192 |
| Gene | CASP8 | GO:0051604 | protein maturation | 16916640|33852854|35594856 |
| Gene | CASP8 | GO:0060546 | negative regulation of necroptotic process | 31827280 |
| Gene | CASP8 | GO:0097153 | cysteine-type endopeptidase activity involved in apoptotic process | 16916640|31827280 |
| Gene | CASP8 | GO:0097191 | extrinsic apoptotic signaling pathway | 21785459|35446120 |
| Gene | CASP8 | GO:0097199 | cysteine-type endopeptidase activity involved in apoptotic signaling pathway | 16916640|16920334 |
| Gene | CASP8 | GO:0097202 | activation of cysteine-type endopeptidase activity | 18387192 |
| Gene | CASP8 | GO:0097342 | ripoptosome | 21737330 |
AS Summary |
| Information of the canonical protein with experimentally identified structure from PDB (2023). |
| UniProt Acc | File name | PDB ID | Method | Resolution | Chain | Start | End |
| Q14790-1 | Q14790-1_6px9_D.pdb | 6PX9 | X-ray | 2.88 | D | 222 | 479 |
| ASpdb's canonical and alternatively spliced isoform information. |
| accession_id | gene_name | canonical_id | alternative_id | canonical_length | alternative_length | canonical_start | canonical_end | type | originalSEQ | variationSEQ | alternative_start | alternative_end |
| Q14790 | CASP8 | Q14790-1 | Q14790-2 | 479 | 464 | 184 | 198 | Deletion | none | none | 183 | 183 |
| Q14790 | CASP8 | Q14790-1 | Q14790-3 | 479 | 395 | 184 | 267 | Deletion | none | none | 183 | 183 |
| Q14790 | CASP8 | Q14790-1 | Q14790-4 | 479 | 496 | 102 | 102 | Substitution | R | RFHFCRMSWAEANSQCQTQSVPFWRRVDHLLIR | 102 | 134 |
| Q14790 | CASP8 | Q14790-1 | Q14790-4 | 479 | 496 | 184 | 198 | Deletion | none | none | 215 | 215 |
| Q14790 | CASP8 | Q14790-1 | Q14790-5 | 479 | 235 | 199 | 235 | Substitution | GEELCGVMTISDSPREQDSESQTLDKVYQMKSKPRGY | DFGQSLPNEKQTSGILSDHQQSQFCKSTGESAQTSQH | 199 | 235 |
| Q14790 | CASP8 | Q14790-1 | Q14790-5 | 479 | 235 | 236 | 479 | Deletion | none | none | 235 | 235 |
| Q14790 | CASP8 | Q14790-1 | Q14790-6 | 479 | 220 | 184 | 220 | Substitution | ERSSSLEGSPDEFSNGEELCGVMTISDSPREQDSESQ | DFGQSLPNEKQTSGILSDHQQSQFCKSTGESAQTSQH | 184 | 220 |
| Q14790 | CASP8 | Q14790-1 | Q14790-6 | 479 | 220 | 221 | 479 | Deletion | none | none | 220 | 220 |
| Q14790 | CASP8 | Q14790-1 | Q14790-7 | 479 | 276 | 269 | 276 | Substitution | ALTTTFEE | TVEPKREK | 269 | 276 |
| Q14790 | CASP8 | Q14790-1 | Q14790-7 | 479 | 276 | 277 | 479 | Deletion | none | none | 276 | 276 |
| Q14790 | CASP8 | Q14790-1 | Q14790-8 | 479 | 261 | 184 | 198 | Deletion | none | none | 183 | 183 |
| Q14790 | CASP8 | Q14790-1 | Q14790-8 | 479 | 261 | 269 | 276 | Substitution | ALTTTFEE | TVEPKREK | 254 | 261 |
| Q14790 | CASP8 | Q14790-1 | Q14790-8 | 479 | 261 | 277 | 479 | Deletion | none | none | 261 | 261 |
| Q14790 | CASP8 | Q14790-1 | Q14790-9 | 479 | 538 | 1 | 1 | Substitution | M | MEGGRRARVVIESKRNFFLGAFPTPFPAEHVELGRLGDSETAMVPGKGGADYILLPFKKM | 1 | 60 |
| Multiple sequence alignment of our canonical and alternatively spliced CASP8 |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of CASP8 |
| UniProt-id | ENSG | ENST | ENSP |
| Q14790-1 | ENSG00000064012.24 | ENST00000413726.6 | ENSP00000397528.2 |
| Q14790-1 | ENSG00000064012.24 | ENST00000432109.6 | ENSP00000412523.2 |
| Q14790-1 | ENSG00000064012.24 | ENST00000440732.6 | ENSP00000396869.2 |
| Q14790-1 | ENSG00000064012.24 | ENST00000673742.1 | ENSP00000501268.1 |
| Q14790-1 | ENSG00000064012.24 | ENST00000696067.1 | ENSP00000512369.1 |
| Q14790-2 | ENSG00000064012.24 | ENST00000323492.11 | ENSP00000325722.7 |
| Q14790-2 | ENSG00000064012.24 | ENST00000392263.6 | ENSP00000376091.2 |
| Q14790-2 | ENSG00000064012.24 | ENST00000696087.1 | ENSP00000512382.1 |
| Q14790-3 | ENSG00000064012.24 | ENST00000444430.3 | ENSP00000394434.3 |
| Q14790-4 | ENSG00000064012.24 | ENST00000264275.9 | ENSP00000264275.5 |
| Q14790-5 | ENSG00000064012.24 | ENST00000392258.7 | ENSP00000376087.3 |
| Q14790-6 | ENSG00000064012.24 | ENST00000447616.6 | ENSP00000388306.2 |
| Q14790-6 | ENSG00000064012.24 | ENST00000696068.1 | ENSP00000512370.1 |
| Q14790-9 | ENSG00000064012.24 | ENST00000358485.8 | ENSP00000351273.4 |
| UniProt-id | NM ID | NP ID |
| Q14790-1 | NM_033355.3 | NP_203519.1 |
| Q14790-2 | NM_001080124.1 | NP_001073593.1 |
| Q14790-2 | NM_033356.3 | NP_203520.1 |
| Q14790-4 | NM_001228.4 | NP_001219.2 |
| Q14790-9 | NM_001080125.1 | NP_001073594.1 |
| Amino acid sequences of our canonical and alternatively spliced CASP8 |
| accession_id | Protein sequence |
| Q14790-1 | MDFSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNTRKEEMEREL QTPGRAQISAYRVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKSLLKIINDYEE FSKERSSSLEGSPDEFSNGEELCGVMTISDSPREQDSESQTLDKVYQMKSKPRGYCLIINNHNFAKAREKVPKLHSIRDRNGTHLDAGAL TTTFEELHFEIKPHDDCTVEQIYEILKIYQLMDHSNMDCFICCILSHGDKGIIYGTDGQEAPIYELTSQFTGLKCPSLAGKPKVFFIQAC QGDNYQKGIPVETDSEEQPYLEMDLSSPQTRYIPDEADFLLGMATVNNCVSYRNPAEGTWYIQSLCQSLRERCPRGDDILTILTEVNYEV |
| Q14790-2 | MDFSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNTRKEEMEREL QTPGRAQISAYRVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKSLLKIINDYEE FSKGEELCGVMTISDSPREQDSESQTLDKVYQMKSKPRGYCLIINNHNFAKAREKVPKLHSIRDRNGTHLDAGALTTTFEELHFEIKPHD DCTVEQIYEILKIYQLMDHSNMDCFICCILSHGDKGIIYGTDGQEAPIYELTSQFTGLKCPSLAGKPKVFFIQACQGDNYQKGIPVETDS EEQPYLEMDLSSPQTRYIPDEADFLLGMATVNNCVSYRNPAEGTWYIQSLCQSLRERCPRGDDILTILTEVNYEVSNKDDKKNMGKQMPQ |
| Q14790-3 | MDFSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNTRKEEMEREL QTPGRAQISAYRVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKSLLKIINDYEE FSKGALTTTFEELHFEIKPHDDCTVEQIYEILKIYQLMDHSNMDCFICCILSHGDKGIIYGTDGQEAPIYELTSQFTGLKCPSLAGKPKV FFIQACQGDNYQKGIPVETDSEEQPYLEMDLSSPQTRYIPDEADFLLGMATVNNCVSYRNPAEGTWYIQSLCQSLRERCPRGDDILTILT |
| Q14790-4 | MDFSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNTRKEEMEREL QTPGRAQISAYRFHFCRMSWAEANSQCQTQSVPFWRRVDHLLIRVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEK RVILGEGKLDILKRVCAQINKSLLKIINDYEEFSKGEELCGVMTISDSPREQDSESQTLDKVYQMKSKPRGYCLIINNHNFAKAREKVPK LHSIRDRNGTHLDAGALTTTFEELHFEIKPHDDCTVEQIYEILKIYQLMDHSNMDCFICCILSHGDKGIIYGTDGQEAPIYELTSQFTGL KCPSLAGKPKVFFIQACQGDNYQKGIPVETDSEEQPYLEMDLSSPQTRYIPDEADFLLGMATVNNCVSYRNPAEGTWYIQSLCQSLRERC |
| Q14790-5 | MDFSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNTRKEEMEREL QTPGRAQISAYRVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKSLLKIINDYEE |
| Q14790-6 | MDFSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNTRKEEMEREL QTPGRAQISAYRVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKSLLKIINDYEE |
| Q14790-7 | MDFSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNTRKEEMEREL QTPGRAQISAYRVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKSLLKIINDYEE FSKERSSSLEGSPDEFSNGEELCGVMTISDSPREQDSESQTLDKVYQMKSKPRGYCLIINNHNFAKAREKVPKLHSIRDRNGTHLDAGTV |
| Q14790-8 | MDFSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNTRKEEMEREL QTPGRAQISAYRVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKSLLKIINDYEE |
| Q14790-9 | MEGGRRARVVIESKRNFFLGAFPTPFPAEHVELGRLGDSETAMVPGKGGADYILLPFKKMDFSRNLYDIGEQLDSEDLASLKFLSLDYIP QRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNTRKEEMERELQTPGRAQISAYRVMLYQISEEVSRSELRSFK FLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKSLLKIINDYEEFSKERSSSLEGSPDEFSNGEELCGVMTISDS PREQDSESQTLDKVYQMKSKPRGYCLIINNHNFAKAREKVPKLHSIRDRNGTHLDAGALTTTFEELHFEIKPHDDCTVEQIYEILKIYQL MDHSNMDCFICCILSHGDKGIIYGTDGQEAPIYELTSQFTGLKCPSLAGKPKVFFIQACQGDNYQKGIPVETDSEEQPYLEMDLSSPQTR |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| CASP8 (go to UniProt):Q14790 |
| Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at * Minus value of BPloci means that the break pointn is located before the CDS. |
| - Retained protein feature among the 13 regional features. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Q14790 | Domain | 100 | 177 | Note=DED 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00065 | Type=Substitution;Start=102;End=102 |
Gene Isoform Structures and Expression Levels for CASP8 |
| Gene structures of our canonical and alternative spliced genes of CASP8 * Click on the image to open the UCSC genome browser with custom track showing this image in a new window. |
| Expression levels of gene isoforms across GTEx. |
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| Expression levels of gene isoforms across TCGA. |
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Protein Structures |
| PDB and CIF files of the predicted protein structures * Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format. |
| 3D view using mol* of Q14790-1 |
| 3D view using mol* of Q14790-2 |
| 3D view using mol* of Q14790-3 |
| 3D view using mol* of Q14790-4 |
| 3D view using mol* of Q14790-5 |
| 3D view using mol* of Q14790-6 |
| 3D view using mol* of Q14790-7 |
| 3D view using mol* of Q14790-8 |
| 3D view using mol* of Q14790-9 |
pLDDT Score Distribution |
| pLDDT score distribution of the predicted protein structures from AlphaFold2 * AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. |
| pLDDT distribution across the protein length of Q14790-1 |
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| pLDDT distribution across the protein length of Q14790-2 |
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| pLDDT distribution across the protein length of Q14790-3 |
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| pLDDT distribution across the protein length of Q14790-4 |
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| pLDDT distribution across the protein length of Q14790-5 |
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| pLDDT distribution across the protein length of Q14790-6 |
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| pLDDT distribution across the protein length of Q14790-7 |
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| pLDDT distribution across the protein length of Q14790-8 |
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| pLDDT distribution across the protein length of Q14790-9 |
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Ramachandran Plot of Protein Structures |
| Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide. |
| Ramachandran plot of Q14790-1 |
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| Ramachandran plot of Q14790-2 |
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| Ramachandran plot of Q14790-5 |
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| Ramachandran plot of Q14790-7 |
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| Ramachandran plot of Q14790-8 |
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Potential Active Site Information |
| The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite. |
| UniProt-id | Site score | Size | D score | Volume | Exposure | Enclosure | Contact | Phobic | Philic | Balance | Don/Acc | Residues |
| Q14790-1 | 0.936 | 197 | 0.964 | 607.453 | 0.72 | 0.598 | 0.74 | 0.32 | 1.027 | 0.311 | 1.012 | 17,18,20,21,67,68,69,70,87,90,91,92,93,94,95,96,98 ,99,100,101,103,104,106,107,109,110,112,113,114,11 7,118,121,122,125,130,133,135,138,139,140,154,174, 177,178,181,182,184,185 |
| Q14790-2 | 1.009 | 205 | 1.062 | 557.718 | 0.639 | 0.647 | 0.826 | 0.757 | 0.816 | 0.927 | 1.003 | 67,68,90,91,92,93,94,95,96,99,100,103,104,107,174, 177,178,181,184,185,186,187,188,189,190,327,328,33 4,376,377,378,379,380,381,382,454,456 |
| Q14790-3 | 1.022 | 799 | 1.04 | 1851.171 | 0.507 | 0.728 | 0.927 | 0.684 | 1.033 | 0.662 | 0.652 | 67,68,70,81,82,84,85,87,88,90,91,92,93,94,95,96,98 ,99,100,103,104,106,107,173,174,176,177,178,180,18 1,184,185,186,187,190,193,194,195,196,197,198,199, 200,201,202,203,208,211,212,215,218,220,223,224,22 5,226,227,228,229,230,231,232,233,239,240,241,242, 266,267,268,274,275,276,281,314,326,327,328,329,33 0,331,332,333,334,335,336,338,339,340,343,344,346, 347,361,365,369,370,371,372,373,374,386,387,388,38 9,390,391,392,393 |
| Q14790-4 | 1.01 | 380 | 1.047 | 1159.683 | 0.603 | 0.679 | 0.895 | 0.724 | 0.922 | 0.786 | 0.888 | 17,18,21,67,68,69,70,72,83,101,103,104,105,106,107 ,108,109,110,112,113,114,116,117,120,121,122,123,1 24,125,126,127,128,129,130,131,132,135,186,213,214 ,216,217,238,239,240,241,351,359,360,366,367,370,3 98,399,400,401,402,403,408,409,410,411,412,413,414 ,415,486,487,488,489 |
| Q14790-5 | 0.948 | 103 | 0.96 | 387.933 | 0.715 | 0.621 | 0.748 | 0.353 | 1.082 | 0.326 | 0.623 | 67,68,70,72,83,90,91,92,93,94,95,96,98,99,100,101, 103,104,106,107,110,154,174,177,178,181,182,185 |
| Q14790-6 | 0.993 | 195 | 0.992 | 611.226 | 0.59 | 0.687 | 0.921 | 0.35 | 1.104 | 0.317 | 1.863 | 17,18,20,21,67,68,69,70,106,107,109,110,111,112,11 7,138,139,140,170,173,174,177,180,181,184,185,199, 200,201,203,204,206,207,210,211,214 |
| Q14790-7 | 0.97 | 155 | 1.004 | 527.191 | 0.696 | 0.633 | 0.75 | 0.421 | 0.968 | 0.435 | 0.57 | 67,68,70,72,90,91,92,93,94,95,96,98,99,100,101,103 ,104,106,107,110,153,154,155,156,157,158,174,177,1 78,179,181,182,184,185,220 |
| Q14790-8 | 0.958 | 194 | 0.995 | 708.981 | 0.725 | 0.61 | 0.74 | 0.293 | 0.954 | 0.307 | 1.219 | 17,18,20,21,67,68,70,90,92,93,94,95,96,98,99,100,1 01,103,104,106,107,109,110,112,113,114,117,118,121 ,122,125,133,135,138,139,140,141,154,155,156,157,1 58,161,174,177,178,179,181,182,183,185,186 |
| Q14790-9 | 0.959 | 92 | 0.978 | 303.212 | 0.684 | 0.666 | 0.817 | 0.512 | 0.991 | 0.517 | 0.611 | 126,127,129,131,142,146,149,150,152,153,155,157,15 8,159,160,162,163,165,166,169,213,233,236,237,240, 244 |
Protein Structure and Feature Comparision |
| Protein Structure Comparision Using Template Modeling Scores (TM-score). |
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| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green) |
| 3D view using mol* of Q14790-1_Q14790-1_6px9_D.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q14790-1_6px9_D_Q14790-2.pdb |
| 3D view using mol* of Q14790-1_6px9_D_Q14790-3.pdb |
| 3D view using mol* of Q14790-1_6px9_D_Q14790-4.pdb |
| 3D view using mol* of Q14790-1_6px9_D_Q14790-5.pdb |
| 3D view using mol* of Q14790-1_6px9_D_Q14790-6.pdb |
| 3D view using mol* of Q14790-1_6px9_D_Q14790-7.pdb |
| 3D view using mol* of Q14790-1_6px9_D_Q14790-8.pdb |
| 3D view using mol* of Q14790-1_6px9_D_Q14790-9.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q14790-1_Q14790-2.pdb |
| 3D view using mol* of Q14790-1_Q14790-3.pdb |
| 3D view using mol* of Q14790-1_Q14790-4.pdb |
| 3D view using mol* of Q14790-1_Q14790-5.pdb |
| 3D view using mol* of Q14790-1_Q14790-6.pdb |
| 3D view using mol* of Q14790-1_Q14790-7.pdb |
| 3D view using mol* of Q14790-1_Q14790-8.pdb |
| 3D view using mol* of Q14790-1_Q14790-9.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/Q14790-1_vs_Q14790-2.png |
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| ./stats/secondary_structure/figure/Q14790-1_vs_Q14790-3.png |
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| ./stats/secondary_structure/figure/Q14790-1_vs_Q14790-4.png |
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| ./stats/secondary_structure/figure/Q14790-1_vs_Q14790-5.png |
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| ./stats/secondary_structure/figure/Q14790-1_vs_Q14790-6.png |
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| ./stats/secondary_structure/figure/Q14790-1_vs_Q14790-7.png |
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| ./stats/secondary_structure/figure/Q14790-1_vs_Q14790-8.png |
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| ./stats/secondary_structure/figure/Q14790-1_vs_Q14790-9.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/Q14790-1_vs_Q14790-2.png |
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| ./stats/relative_asa/Q14790-1_vs_Q14790-3.png |
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| ./stats/relative_asa/Q14790-1_vs_Q14790-4.png |
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| ./stats/relative_asa/Q14790-1_vs_Q14790-5.png |
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| ./stats/relative_asa/Q14790-1_vs_Q14790-6.png |
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| ./stats/relative_asa/Q14790-1_vs_Q14790-7.png |
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| ./stats/relative_asa/Q14790-1_vs_Q14790-8.png |
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| ./stats/relative_asa/Q14790-1_vs_Q14790-9.png |
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Protein-Protein Interaction |
| Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to CASP8 |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
| Q14790 | CASP8 | DB04297 | Trichostatin A | experimental | activator |
| Q14790 | CASP8 | DB05103 | AN-9 | investigational | regulator |
| Q14790 | CASP8 | DB12843 | Oleandrin | experimental, investigational | regulator |
| Q14790 | CASP8 | DB12651 | Bardoxolone | investigational | |
| Q14790 | CASP8 | DB11752 | Bryostatin 1 | investigational | inhibitor |
Related Diseases to CASP8 |
| Previous studies relating to the alternative splicing of CASP8 and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| CASP8 | 10860845 | Dominant expression of a novel splice variant of caspase-8 in human peripheral blood lymphocytes. | Caspase-8 is an apical and critical proteolytic enzyme in the cascade of apoptosis. As a result of alternative splicing, the generation of at least 7 isoforms of caspase-8 has been reported. The existence of multiple isoforms that lack the essential domains for apoptosis suggests the possible role of these isoforms on the regulation of apoptosis. Here we report a novel longer isoform of caspase-8 (caspase-8L) that was generated by alternative splicing of intron 8, thereby carrying a 136-bp insertion and frame shift of the transcript. The transcript encoded N-terminal two repeats of death effector domain (DED) of caspase-8, but lacking the C-terminal half of the proteolytic domain. Reverse transcriptase (RT)-polymerase chain reaction (PCR) analysis revealed the dominant expression of caspase-8L transcript compared to the intact form of caspase-8 in human peripheral blood lymphocyte (PBL) and T cells. In patients with systemic lupus erythematosus (SLE), imbalanced expression of caspase-8L transcript was identified. These results suggest the important role of caspase-8L in the modulation of apoptosis. | D008180 | Lupus Erythematosus, Systemic |
| CASP8 | 12010809 | Characterization of caspase-8L: a novel isoform of caspase-8 that behaves as an inhibitor of the caspase cascade. | Caspase-8 (Fas-associating protein with death domain-like interleukin-1beta- converting enzyme [FLICE]/MACH/Mch5) belongs to a family of cysteine proteases presumed to be the apex of the apoptotic signaling pathways. We recently reported the presence of a novel isoform of caspase-8, named caspase-8L, generated by the alternative splicing of human caspase-8 gene, from human peripheral blood lymphocytes by reverse transcriptase-polymerase chain reaction. We herein report a functional analysis of caspase-8L in the Fas-mediated apoptotic pathway. Caspase-8L is missing the catalytic site of caspase-8 but retains 2 N-terminal repeats of the death-effector domain. The caspase-8L messenger RNA was detected in various tissues but not in any cell lines examined. In human peripheral blood lymphocytes, caspase-8L was strongly suggested to be expressed at the protein level. In MCF-7 cells, caspase-8L transfection itself did not affect cell viability but instead inhibited the apoptosis induced by the cotransfection of caspase-8 in a dominant negative manner. Moreover, Fas-mediated apoptosis was inhibited in caspase-8L-transfected Jurkat cells, which were associated with a reduction in the caspase-8 catalytic activity. In vitro binding assays demonstrated that caspase-8L bound to FADD (Fas-associating protein with death domain) and caspase-8a and blocked the binding of caspase-8 to FADD. In in vivo binding assays, transfected caspase-8L bound to endogenous FADD. Thus, caspase-8L acts as an inhibitor of caspase-8 by interfering with the binding of caspase-8 to FADD and is involved in the regulation of Fas-mediated apoptosis. | D001943 | Breast Neoplasms |
Clinically important variants in CASP8 |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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