UniProtKB - Q14790 (CASP8_HUMAN)
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Protein
Caspase-8
Gene
CASP8
Organism
Homo sapiens (Human)
Status
Functioni
Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein. Isoform 5, isoform 6, isoform 7 and isoform 8 lack the catalytic site and may interfere with the pro-apoptotic activity of the complex.2 Publications
Catalytic activityi
Strict requirement for Asp at position P1 and has a preferred cleavage sequence of (Leu/Asp/Val)-Glu-Thr-Asp-|-(Gly/Ser/Ala).1 Publication
Enzyme regulationi
Inhibited by the effector protein NleF that is produced by pathogenic E.coli; this inhibits apoptosis.1 Publication
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Active sitei | 317 | 1 | ||
| Active sitei | 360 | 1 |
GO - Molecular functioni
- cysteine-type endopeptidase activity Source: UniProtKB
- cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
- cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: UniProtKB
- cysteine-type endopeptidase activity involved in execution phase of apoptosis Source: GO_Central
- cysteine-type peptidase activity Source: ProtInc
- death effector domain binding Source: UniProtKB
- death receptor binding Source: Ensembl
- identical protein binding Source: IntAct
- peptidase activity Source: BHF-UCL
- protein complex binding Source: Ensembl
- scaffold protein binding Source: ParkinsonsUK-UCL
- tumor necrosis factor receptor binding Source: Ensembl
- ubiquitin protein ligase binding Source: UniProtKB
GO - Biological processi
- activation of cysteine-type endopeptidase activity Source: BHF-UCL
- activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Reactome
- activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: Reactome
- apoptotic process Source: UniProtKB
- apoptotic signaling pathway Source: BHF-UCL
- B cell activation Source: UniProtKB
- cell surface receptor signaling pathway Source: Reactome
- cellular response to mechanical stimulus Source: UniProtKB
- cellular response to organic cyclic compound Source: Ensembl
- death-inducing signaling complex assembly Source: Reactome
- execution phase of apoptosis Source: UniProtKB
- extrinsic apoptotic signaling pathway Source: UniProtKB
- macrophage differentiation Source: UniProtKB
- natural killer cell activation Source: UniProtKB
- negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Reactome
- negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
- nucleotide-binding oligomerization domain containing signaling pathway Source: Reactome
- positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
- positive regulation of macrophage differentiation Source: UniProtKB
- positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
- positive regulation of proteolysis Source: BHF-UCL
- proteolysis Source: UniProtKB
- proteolysis involved in cellular protein catabolic process Source: BHF-UCL
- regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Reactome
- regulation of necroptotic process Source: Reactome
- regulation of tumor necrosis factor-mediated signaling pathway Source: Reactome
- response to antibiotic Source: Ensembl
- response to cobalt ion Source: Ensembl
- response to cold Source: Ensembl
- response to estradiol Source: Ensembl
- response to ethanol Source: Ensembl
- response to lipopolysaccharide Source: Ensembl
- response to tumor necrosis factor Source: BHF-UCL
- suppression by virus of host cysteine-type endopeptidase activity involved in apoptotic process Source: Reactome
- syncytiotrophoblast cell differentiation involved in labyrinthine layer development Source: UniProtKB
- T cell activation Source: UniProtKB
- TRAIL-activated apoptotic signaling pathway Source: ParkinsonsUK-UCL
- TRIF-dependent toll-like receptor signaling pathway Source: Reactome
Keywordsi
| Molecular function | Hydrolase, Protease, Thiol protease |
| Biological process | Apoptosis, Host-virus interaction |
Enzyme and pathway databases
| BRENDAi | 3.4.22.61. 2681. |
| Reactomei | R-HSA-111465. Apoptotic cleavage of cellular proteins. R-HSA-140534. Ligand-dependent caspase activation. R-HSA-168638. NOD1/2 Signaling Pathway. R-HSA-2562578. TRIF-mediated programmed cell death. R-HSA-264870. Caspase-mediated cleavage of cytoskeletal proteins. R-HSA-3371378. Regulation by c-FLIP. R-HSA-5213460. RIPK1-mediated regulated necrosis. R-HSA-5218900. CASP8 activity is inhibited. R-HSA-5357786. TNFR1-induced proapoptotic signaling. R-HSA-5357905. Regulation of TNFR1 signaling. R-HSA-5660668. CLEC7A/inflammasome pathway. R-HSA-5675482. Regulation of necroptotic cell death. R-HSA-69416. Dimerization of procaspase-8. R-HSA-75108. Activation, myristolyation of BID and translocation to mitochondria. R-HSA-75153. Apoptotic execution phase. R-HSA-75157. FasL/ CD95L signaling. R-HSA-75158. TRAIL signaling. R-HSA-933543. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10. |
| SignaLinki | Q14790. |
| SIGNORi | Q14790. |
Protein family/group databases
| MEROPSi | C14.009. |
Names & Taxonomyi
| Protein namesi | Recommended name: Caspase-8 (EC:3.4.22.61)Short name: CASP-8 Alternative name(s): Apoptotic cysteine protease Apoptotic protease Mch-5 CAP4 FADD-homologous ICE/ced-3-like protease FADD-like ICE Short name: FLICE ICE-like apoptotic protease 5 MORT1-associated ced-3 homolog Short name: MACH Cleaved into the following 2 chains: |
| Gene namesi | Name:CASP8 Synonyms:MCH5 |
| Organismi | Homo sapiens (Human) |
| Taxonomic identifieri | 9606 [NCBI] |
| Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
| Proteomesi |
|
Organism-specific databases
| HGNCi | HGNC:1509. CASP8. |
Subcellular locationi
GO - Cellular componenti
- CD95 death-inducing signaling complex Source: UniProtKB
- cell body Source: Ensembl
- cytoskeleton Source: ProtInc
- cytosol Source: UniProtKB
- death-inducing signaling complex Source: UniProtKB
- membrane raft Source: Ensembl
- mitochondrial outer membrane Source: Reactome
- mitochondrion Source: ProtInc
- neuron projection Source: Ensembl
- nucleoplasm Source: HPA
- ripoptosome Source: UniProtKB
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Involvement in diseasei
Caspase-8 deficiency (CASP8D)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionDisorder resembling autoimmune lymphoproliferative syndrome (ALPS). It is characterized by lymphadenopathy, splenomegaly, and defective CD95-induced apoptosis of peripheral blood lymphocytes (PBLs). It leads to defects in activation of T-lymphocytes, B-lymphocytes, and natural killer cells leading to immunodeficiency characterized by recurrent sinopulmonary and herpes simplex virus infections and poor responses to immunization.
See also OMIM:607271| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Natural variantiVAR_014204 | 248 | R → W in CASP8D. 1 PublicationCorresponds to variant dbSNP:rs17860424Ensembl. | 1 |
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Mutagenesisi | 73 | D → A: Abolishes binding to FLASH. Induces NF-kappa-B activation. 1 Publication | 1 | |
| Mutagenesisi | 387 | S → A: Impaired CDK1-mediated phosphorylation and enhanced apoptosis. | 1 |
Keywords - Diseasei
Disease mutationOrganism-specific databases
| DisGeNETi | 841. |
| MalaCardsi | CASP8. |
| MIMi | 211980. phenotype. 607271. phenotype. |
| OpenTargetsi | ENSG00000064012. |
| Orphaneti | 275517. Autoimmune lymphoproliferative syndrome with recurrent viral infections. |
| PharmGKBi | PA26092. |
Chemistry databases
| ChEMBLi | CHEMBL3776. |
| GuidetoPHARMACOLOGYi | 1624. |
Polymorphism and mutation databases
| BioMutai | CASP8. |
| DMDMi | 2493531. |
PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| PropeptideiPRO_0000004628 | 1 – 216 | Add BLAST | 216 | |
| ChainiPRO_0000004629 | 217 – 374 | Caspase-8 subunit p18Add BLAST | 158 | |
| PropeptideiPRO_0000004630 | 375 – 384 | 10 | ||
| ChainiPRO_0000004631 | 385 – 479 | Caspase-8 subunit p10Add BLAST | 95 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Modified residuei | 188 | PhosphoserineBy similarity | 1 | |
| Modified residuei | 211 | PhosphoserineBy similarity | 1 | |
| Modified residuei | 224 | N6-acetyllysineBy similarity | 1 | |
| Modified residuei | 334 | PhosphotyrosineCombined sources | 1 | |
| Modified residuei | 387 | Phosphoserine; by CDK11 Publication | 1 |
Post-translational modificationi
Generation of the subunits requires association with the death-inducing signaling complex (DISC), whereas additional processing is likely due to the autocatalytic activity of the activated protease. GZMB and CASP10 can be involved in these processing events.2 Publications
Phosphorylation on Ser-387 during mitosis by CDK1 inhibits activation by proteolysis and prevents apoptosis. This phosphorylation occurs in cancer cell lines, as well as in primary breast tissues and lymphocytes.1 Publication
Keywords - PTMi
Acetylation, Phosphoprotein, ZymogenProteomic databases
| EPDi | Q14790. |
| MaxQBi | Q14790. |
| PaxDbi | Q14790. |
| PeptideAtlasi | Q14790. |
| PRIDEi | Q14790. |
PTM databases
| iPTMneti | Q14790. |
| PhosphoSitePlusi | Q14790. |
| SwissPalmi | Q14790. |
Miscellaneous databases
| PMAP-CutDBi | Q14790. |
Expressioni
Tissue specificityi
Isoform 1, isoform 5 and isoform 7 are expressed in a wide variety of tissues. Highest expression in peripheral blood leukocytes, spleen, thymus and liver. Barely detectable in brain, testis and skeletal muscle.
Gene expression databases
| Bgeei | ENSG00000064012. |
| ExpressionAtlasi | Q14790. baseline and differential. |
| Genevisiblei | Q14790. HS. |
Organism-specific databases
| HPAi | CAB002047. HPA001302. HPA005688. HPA006191. |
Interactioni
Subunit structurei
Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 18 kDa (p18) and a 10 kDa (p10) subunit. Interacts with FADD, CFLAR and PEA15. Isoform 9 interacts at the endoplasmic reticulum with a complex containing BCAP31, BAP29, BCL2 and/or BCL2L1. Interacts with TNFAIP8L2 (By similarity). Interacts with CASP8AP2. Interacts with RFFL and RNF34; negatively regulate CASP8 through proteasomal degradation. Interacts with human cytomegalovirus/HHV-5 protein vICA/UL36; this interaction inhibits CASP8 activation. Interacts with NleF from pathogenic E.coli. Interacts with NOL3; decreases CASP8 activity in a mitochondria localization- and phosphorylation-dependent manner and this interaction is dissociated by calcium.By similarity9 Publications
Binary interactionsi
GO - Molecular functioni
- death effector domain binding Source: UniProtKB
- death receptor binding Source: Ensembl
- identical protein binding Source: IntAct
- protein complex binding Source: Ensembl
- scaffold protein binding Source: ParkinsonsUK-UCL
- tumor necrosis factor receptor binding Source: Ensembl
- ubiquitin protein ligase binding Source: UniProtKB
Protein-protein interaction databases
| BioGridi | 107291. 148 interactors. |
| DIPi | DIP-30915N. |
| IntActi | Q14790. 106 interactors. |
| MINTi | MINT-91645. |
| STRINGi | 9606.ENSP00000351273. |
Chemistry databases
| BindingDBi | Q14790. |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Helixi | 3 – 13 | Combined sources | 11 | |
| Helixi | 16 – 25 | Combined sources | 10 | |
| Turni | 26 – 29 | Combined sources | 4 | |
| Helixi | 32 – 34 | Combined sources | 3 | |
| Helixi | 41 – 50 | Combined sources | 10 | |
| Beta strandi | 53 – 55 | Combined sources | 3 | |
| Helixi | 60 – 68 | Combined sources | 9 | |
| Helixi | 72 – 79 | Combined sources | 8 | |
| Helixi | 83 – 91 | Combined sources | 9 | |
| Turni | 93 – 95 | Combined sources | 3 | |
| Helixi | 100 – 111 | Combined sources | 12 | |
| Helixi | 114 – 127 | Combined sources | 14 | |
| Helixi | 139 – 148 | Combined sources | 10 | |
| Beta strandi | 151 – 153 | Combined sources | 3 | |
| Helixi | 158 – 165 | Combined sources | 8 | |
| Helixi | 169 – 180 | Combined sources | 12 | |
| Beta strandi | 230 – 232 | Combined sources | 3 | |
| Beta strandi | 235 – 240 | Combined sources | 6 | |
| Helixi | 245 – 250 | Combined sources | 6 | |
| Helixi | 252 – 254 | Combined sources | 3 | |
| Beta strandi | 255 – 257 | Combined sources | 3 | |
| Helixi | 263 – 276 | Combined sources | 14 | |
| Beta strandi | 280 – 286 | Combined sources | 7 | |
| Helixi | 289 – 301 | Combined sources | 13 | |
| Helixi | 304 – 306 | Combined sources | 3 | |
| Beta strandi | 310 – 316 | Combined sources | 7 | |
| Beta strandi | 322 – 324 | Combined sources | 3 | |
| Beta strandi | 326 – 328 | Combined sources | 3 | |
| Beta strandi | 330 – 332 | Combined sources | 3 | |
| Helixi | 333 – 337 | Combined sources | 5 | |
| Helixi | 338 – 340 | Combined sources | 3 | |
| Turni | 342 – 344 | Combined sources | 3 | |
| Helixi | 346 – 348 | Combined sources | 3 | |
| Beta strandi | 353 – 359 | Combined sources | 7 | |
| Beta strandi | 361 – 364 | Combined sources | 4 | |
| Beta strandi | 369 – 371 | Combined sources | 3 | |
| Beta strandi | 377 – 379 | Combined sources | 3 | |
| Beta strandi | 392 – 394 | Combined sources | 3 | |
| Turni | 395 – 398 | Combined sources | 4 | |
| Beta strandi | 399 – 405 | Combined sources | 7 | |
| Beta strandi | 412 – 414 | Combined sources | 3 | |
| Turni | 415 – 417 | Combined sources | 3 | |
| Helixi | 420 – 432 | Combined sources | 13 | |
| Helixi | 433 – 435 | Combined sources | 3 | |
| Helixi | 439 – 450 | Combined sources | 12 | |
| Turni | 456 – 459 | Combined sources | 4 | |
| Beta strandi | 465 – 468 | Combined sources | 4 | |
| Beta strandi | 471 – 473 | Combined sources | 3 |
3D structure databases
| Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1F9E | X-ray | 2.90 | A/C/E/G/I/K | 222-374 | [»] | |
| B/D/F/H/J/L | 390-478 | [»] | ||||
| 1I4E | X-ray | 3.00 | B | 222-479 | [»] | |
| 1QDU | X-ray | 2.80 | A/C/E/G/I/K | 222-374 | [»] | |
| B/D/F/H/J/L | 390-477 | [»] | ||||
| 1QTN | X-ray | 1.20 | A | 211-374 | [»] | |
| B | 385-479 | [»] | ||||
| 2C2Z | X-ray | 1.95 | A | 218-374 | [»] | |
| B | 376-479 | [»] | ||||
| 2FUN | X-ray | 3.00 | B/D | 222-479 | [»] | |
| 2K7Z | NMR | - | A | 217-479 | [»] | |
| 2Y1L | X-ray | 1.80 | A/C | 218-374 | [»] | |
| B/D | 376-479 | [»] | ||||
| 3H11 | X-ray | 1.90 | B | 217-479 | [»] | |
| 3KJN | X-ray | 1.80 | A | 211-374 | [»] | |
| B | 385-479 | [»] | ||||
| 3KJQ | X-ray | 1.80 | A | 211-374 | [»] | |
| B | 385-479 | [»] | ||||
| 4JJ7 | X-ray | 1.18 | A | 217-479 | [»] | |
| 4PRZ | X-ray | 2.12 | A | 217-479 | [»] | |
| 4PS1 | X-ray | 1.73 | A/B/C/D | 217-479 | [»] | |
| 4ZBW | X-ray | 2.20 | A/B | 2-188 | [»] | |
| 5JQE | X-ray | 3.16 | A | 1-186 | [»] | |
| 5L08 | electron microscopy | 4.60 | A/B/C/D/E/F/G/H/I | 1-184 | [»] | |
| ProteinModelPortali | Q14790. | |||||
| SMRi | Q14790. | |||||
| ModBasei | Search... | |||||
| MobiDBi | Search... | |||||
Miscellaneous databases
| EvolutionaryTracei | Q14790. |
Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Domaini | 2 – 80 | DED 1PROSITE-ProRule annotationAdd BLAST | 79 | |
| Domaini | 100 – 177 | DED 2PROSITE-ProRule annotationAdd BLAST | 78 |
Domaini
Isoform 9 contains a N-terminal extension that is required for interaction with the BCAP31 complex.
Sequence similaritiesi
Belongs to the peptidase C14A family.Curated
Keywords - Domaini
RepeatPhylogenomic databases
| eggNOGi | KOG3573. Eukaryota. ENOG410ZQIE. LUCA. |
| GeneTreei | ENSGT00760000118912. |
| HOVERGENi | HBG050803. |
| InParanoidi | Q14790. |
| KOi | K04398. |
| OMAi | IFIEMEK. |
| OrthoDBi | EOG091G05YD. |
| PhylomeDBi | Q14790. |
| TreeFami | TF102023. |
Family and domain databases
| CDDi | cd00032. CASc. 1 hit. |
| InterProi | View protein in InterPro IPR029030. Caspase-like_dom. IPR033139. Caspase_cys_AS. IPR016129. Caspase_his_AS. IPR011029. DEATH-like_dom. IPR001875. DED_dom. IPR002138. Pept_C14_p10. IPR001309. Pept_C14_p20. IPR015917. Pept_C14A. |
| Pfami | View protein in Pfam PF01335. DED. 2 hits. |
| PRINTSi | PR00376. IL1BCENZYME. |
| SMARTi | View protein in SMART SM00115. CASc. 1 hit. SM00031. DED. 2 hits. |
| SUPFAMi | SSF47986. SSF47986. 2 hits. SSF52129. SSF52129. 1 hit. |
| PROSITEi | View protein in PROSITE PS01122. CASPASE_CYS. 1 hit. PS01121. CASPASE_HIS. 1 hit. PS50207. CASPASE_P10. 1 hit. PS50208. CASPASE_P20. 1 hit. PS50168. DED. 2 hits. |
Sequences (9)i
Sequence statusi: Complete.
Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 9 isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: Q14790-1) [UniParc]FASTAAdd to basket
Also known as: Alpha-1
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
10 20 30 40 50
MDFSRNLYDI GEQLDSEDLA SLKFLSLDYI PQRKQEPIKD ALMLFQRLQE
60 70 80 90 100
KRMLEESNLS FLKELLFRIN RLDLLITYLN TRKEEMEREL QTPGRAQISA
110 120 130 140 150
YRVMLYQISE EVSRSELRSF KFLLQEEISK CKLDDDMNLL DIFIEMEKRV
160 170 180 190 200
ILGEGKLDIL KRVCAQINKS LLKIINDYEE FSKERSSSLE GSPDEFSNGE
210 220 230 240 250
ELCGVMTISD SPREQDSESQ TLDKVYQMKS KPRGYCLIIN NHNFAKAREK
260 270 280 290 300
VPKLHSIRDR NGTHLDAGAL TTTFEELHFE IKPHDDCTVE QIYEILKIYQ
310 320 330 340 350
LMDHSNMDCF ICCILSHGDK GIIYGTDGQE APIYELTSQF TGLKCPSLAG
360 370 380 390 400
KPKVFFIQAC QGDNYQKGIP VETDSEEQPY LEMDLSSPQT RYIPDEADFL
410 420 430 440 450
LGMATVNNCV SYRNPAEGTW YIQSLCQSLR ERCPRGDDIL TILTEVNYEV
460 470
SNKDDKKNMG KQMPQPTFTL RKKLVFPSD
Isoform 7 (identifier: Q14790-7) [UniParc]FASTAAdd to basket
Also known as: Beta-3, 8L
The sequence of this isoform differs from the canonical sequence as follows:
269-276: ALTTTFEE → TVEPKREK
277-479: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »Sequence cautioni
The sequence CAA66858 differs from that shown.Curated
The sequence CAA66859 differs from that shown.Curated
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length | |
|---|---|---|---|---|---|
| Sequence conflicti | 294 | E → D in AAD24962 (PubMed:9931493).Curated | 1 | ||
| Sequence conflicti | 331 | A → P in AAC50602 (PubMed:8681377).Curated | 1 | ||
| Sequence conflicti | 331 | A → P in AAD24962 (PubMed:9931493).Curated | 1 | ||
| Sequence conflicti | 343 – 344 | LK → FG in AAL87631 (PubMed:11917123).Curated | 2 | ||
| Isoform 9 (identifier: Q14790-9) | |||||
| Sequence conflicti | 14 | K → R in AAL87628 (PubMed:11917123).Curated | 1 | ||
Polymorphismi
Genetic variations in CASP8 are associated with reduced risk of lung cancer [MIMi:211980] in a population of Han Chinese subjects. Genetic variations are also associated with decreased risk of cancer of various other forms including esophageal, gastric, colorectal, cervical, and breast, acting in an allele dose-dependent manner.1 Publication
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Natural variantiVAR_025816 | 219 | S → T1 PublicationCorresponds to variant dbSNP:rs35976359Ensembl. | 1 | |
| Natural variantiVAR_014204 | 248 | R → W in CASP8D. 1 PublicationCorresponds to variant dbSNP:rs17860424Ensembl. | 1 | |
| Natural variantiVAR_020127 | 285 | D → H Associated with protection against breast cancer; also associated with a lower risk of cutaneous melanoma. 7 PublicationsCorresponds to variant dbSNP:rs1045485Ensembl. | 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Alternative sequenceiVSP_000808 | 1 | M → MEGGRRARVVIESKRNFFLG AFPTPFPAEHVELGRLGDSE TAMVPGKGGADYILLPFKKM in isoform 9. 1 Publication | 1 | |
| Alternative sequenceiVSP_000809 | 102 | R → RFHFCRMSWAEANSQCQTQS VPFWRRVDHLLIR in isoform 4. 1 Publication | 1 | |
| Alternative sequenceiVSP_000813 | 184 – 267 | Missing in isoform 3. 1 PublicationAdd BLAST | 84 | |
| Alternative sequenceiVSP_000811 | 184 – 220 | ERSSS…DSESQ → DFGQSLPNEKQTSGILSDHQ QSQFCKSTGESAQTSQH in isoform 6. 1 PublicationAdd BLAST | 37 | |
| Alternative sequenceiVSP_000810 | 184 – 198 | Missing in isoform 2, isoform 4 and isoform 8. 4 PublicationsAdd BLAST | 15 | |
| Alternative sequenceiVSP_000814 | 199 – 235 | GEELC…KPRGY → DFGQSLPNEKQTSGILSDHQ QSQFCKSTGESAQTSQH in isoform 5. 1 PublicationAdd BLAST | 37 | |
| Alternative sequenceiVSP_000812 | 221 – 479 | Missing in isoform 6. 1 PublicationAdd BLAST | 259 | |
| Alternative sequenceiVSP_000815 | 236 – 479 | Missing in isoform 5. 1 PublicationAdd BLAST | 244 | |
| Alternative sequenceiVSP_000816 | 269 – 276 | ALTTTFEE → TVEPKREK in isoform 7 and isoform 8. 3 Publications | 8 | |
| Alternative sequenceiVSP_000817 | 277 – 479 | Missing in isoform 7 and isoform 8. 3 PublicationsAdd BLAST | 203 |
Sequence databases
Genome annotation databases
Keywords - Coding sequence diversityi
Alternative splicing, PolymorphismSimilar proteinsi
Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:| 100% | UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry. |
| 90% | UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence). |
| 50% | UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster. |
Entry informationi
| Entry namei | CASP8_HUMAN | |
| Accessioni | Q14790Primary (citable) accession number: Q14790 Secondary accession number(s): O14676 Q9UQ81 | |
| Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1997 |
| Last sequence update: | November 1, 1996 | |
| Last modified: | June 7, 2017 | |
| This is version 212 of the entry and version 1 of the sequence. See complete history. | ||
| Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
Miscellaneousi
Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 2
Human chromosome 2: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - Peptidase families
Classification of peptidase families and list of entries - SIMILARITY comments
Index of protein domains and families
