SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q14790

- CASP8_HUMAN

UniProt

Q14790 - CASP8_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Caspase-8
Gene
CASP8, MCH5
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.3 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

Probably negatively regulated by RFFL through proteasomal degradation. Inhibited by the effector protein NleF that is produced by pathogenic E.coli; this inhibits apoptosis.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei317 – 3171
Active sitei360 – 3601

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: UniProtKB
  2. cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  3. cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: UniProtKB
  4. cysteine-type peptidase activity Source: ProtInc
  5. death effector domain binding Source: UniProtKB
  6. peptidase activity Source: UniProtKB
  7. protein binding Source: IntAct
  8. receptor binding Source: UniProtKB
  9. scaffold protein binding Source: ParkinsonsUK-UCL
  10. ubiquitin protein ligase binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. B cell activation Source: UniProtKB
  2. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  3. T cell activation Source: UniProtKB
  4. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
  5. activation of cysteine-type endopeptidase activity Source: BHF-UCL
  6. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Reactome
  7. angiogenesis Source: Ensembl
  8. apoptotic process Source: UniProtKB
  9. apoptotic signaling pathway Source: BHF-UCL
  10. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  11. cellular response to mechanical stimulus Source: UniProtKB
  12. cellular response to organic cyclic compound Source: Ensembl
  13. execution phase of apoptosis Source: UniProtKB
  14. extrinsic apoptotic signaling pathway Source: UniProtKB
  15. extrinsic apoptotic signaling pathway via death domain receptors Source: RefGenome
  16. heart development Source: Ensembl
  17. hepatocyte apoptotic process Source: Ensembl
  18. innate immune response Source: Reactome
  19. intrinsic apoptotic signaling pathway Source: Reactome
  20. macrophage differentiation Source: UniProtKB
  21. natural killer cell activation Source: UniProtKB
  22. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  23. neural tube formation Source: Ensembl
  24. nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome
  25. nucleotide-binding oligomerization domain containing signaling pathway Source: Reactome
  26. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  27. positive regulation of extrinsic apoptotic signaling pathway Source: Ensembl
  28. positive regulation of macrophage differentiation Source: UniProtKB
  29. positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
  30. positive regulation of proteolysis Source: BHF-UCL
  31. protein heterooligomerization Source: Ensembl
  32. proteolysis Source: UniProtKB
  33. proteolysis involved in cellular protein catabolic process Source: BHF-UCL
  34. regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Reactome
  35. regulation of thymocyte apoptotic process Source: Ensembl
  36. response to antibiotic Source: Ensembl
  37. response to cobalt ion Source: Ensembl
  38. response to cold Source: Ensembl
  39. response to estradiol Source: Ensembl
  40. response to ethanol Source: Ensembl
  41. response to lipopolysaccharide Source: Ensembl
  42. response to tumor necrosis factor Source: BHF-UCL
  43. syncytiotrophoblast cell differentiation involved in labyrinthine layer development Source: UniProtKB
  44. toll-like receptor 3 signaling pathway Source: Reactome
  45. toll-like receptor 4 signaling pathway Source: Reactome
  46. toll-like receptor signaling pathway Source: Reactome
  47. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Apoptosis, Host-virus interaction

Enzyme and pathway databases

BRENDAi3.4.22.61. 2681.
ReactomeiREACT_107. Apoptotic cleavage of cellular proteins.
REACT_13541. Caspase-mediated cleavage of cytoskeletal proteins.
REACT_1432. TNF signaling.
REACT_1503. Caspase-8 activation.
REACT_150361. TRIF-mediated programmed cell death.
REACT_164011. Regulation by c-FLIP.
REACT_25039. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
REACT_402. TRAIL signaling.
REACT_701. Activation, myristolyation of BID and translocation to mitochondria.
REACT_75776. NOD1/2 Signaling Pathway.
REACT_832. Dimerization of procaspase-8.
REACT_900. FasL/ CD95L signaling.
REACT_995. Apoptotic execution phase.
SignaLinkiQ14790.

Protein family/group databases

MEROPSiC14.009.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:1509. CASP8.

Subcellular locationi

GO - Cellular componenti

  1. CD95 death-inducing signaling complex Source: UniProtKB
  2. Noc1p-Noc2p complex Source: Ensembl
  3. cell body Source: Ensembl
  4. cytoplasm Source: HPA
  5. cytoskeleton Source: ProtInc
  6. cytosol Source: UniProtKB
  7. death-inducing signaling complex Source: UniProtKB
  8. membrane raft Source: Ensembl
  9. microtubule organizing center Source: HPA
  10. mitochondrial outer membrane Source: Reactome
  11. mitochondrion Source: HPA
  12. neuron projection Source: Ensembl
  13. nucleus Source: HPA
  14. ripoptosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Caspase-8 deficiency (CASP8D) [MIM:607271]: Disorder 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti248 – 2481R → W in CASP8D. 1 Publication
Corresponds to variant rs17860424 [ dbSNP | Ensembl ].
VAR_014204

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi73 – 731D → A: Abolishes binding to FLASH. Induces NF-kappa-B activation. 1 Publication
Mutagenesisi387 – 3871S → A: Impaired CDK1-mediated phosphorylation and enhanced apoptosis.

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi211980. phenotype.
607271. phenotype.
Orphaneti275517. Autoimmune lymphoproliferative syndrome with recurrent infections.
PharmGKBiPA26092.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 216216
PRO_0000004628Add
BLAST
Chaini217 – 374158Caspase-8 subunit p18
PRO_0000004629Add
BLAST
Propeptidei375 – 38410
PRO_0000004630
Chaini385 – 47995Caspase-8 subunit p10
PRO_0000004631Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei188 – 1881Phosphoserine By similarity
Modified residuei211 – 2111Phosphoserine By similarity
Modified residuei224 – 2241N6-acetyllysine By similarity
Modified residuei334 – 3341Phosphotyrosine1 Publication
Modified residuei387 – 3871Phosphoserine; by CDK11 Publication

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.
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.

Keywords - PTMi

Acetylation, Phosphoprotein, Zymogen

Proteomic databases

MaxQBiQ14790.
PaxDbiQ14790.
PRIDEiQ14790.

PTM databases

PhosphoSiteiQ14790.

Miscellaneous databases

PMAP-CutDBQ14790.

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

ArrayExpressiQ14790.
BgeeiQ14790.
GenevestigatoriQ14790.

Organism-specific databases

HPAiCAB002047.
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. Interacts with human cytomegalovirus/HHV-5 protein vICA/UL36; this interaction inhibits CASP8 activation. Interacts with NleF from pathogenic E.coli.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BCAP31P515723EBI-78060,EBI-77683
CASP10Q928513EBI-78060,EBI-495095
CASP8AP2Q9UKL33EBI-78060,EBI-2339650
CFLARO155199EBI-78060,EBI-514941
CFLARO15519-12EBI-78060,EBI-4567563
CUL3Q136186EBI-78060,EBI-456129
FADDQ1315832EBI-78060,EBI-494804
FASP2544514EBI-78060,EBI-494743
FASLGP480234EBI-78060,EBI-495538
ILKQ134182EBI-78060,EBI-747644
MALT1Q9UDY810EBI-78060,EBI-1047372
NOL3O609363EBI-78060,EBI-740992
PTPN6P293503EBI-78060,EBI-78260
RIPK1Q1354623EBI-78060,EBI-358507
RNF34Q969K33EBI-78060,EBI-2340642
TNFRSF10AO002209EBI-78060,EBI-518861

Protein-protein interaction databases

BioGridi107291. 91 interactions.
DIPiDIP-30915N.
IntActiQ14790. 67 interactions.
MINTiMINT-91645.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi230 – 2323
Beta strandi235 – 2406
Helixi245 – 2506
Helixi252 – 2543
Beta strandi255 – 2573
Helixi263 – 27614
Beta strandi280 – 2867
Helixi289 – 30113
Helixi304 – 3063
Beta strandi310 – 3167
Beta strandi322 – 3243
Beta strandi326 – 3283
Beta strandi330 – 3323
Helixi333 – 3375
Helixi338 – 3403
Turni342 – 3443
Helixi346 – 3483
Beta strandi353 – 3597
Beta strandi361 – 3644
Beta strandi369 – 3713
Beta strandi377 – 3793
Beta strandi392 – 3943
Turni395 – 3984
Beta strandi399 – 4057
Beta strandi412 – 4143
Turni415 – 4173
Helixi420 – 43213
Helixi433 – 4353
Helixi439 – 45012
Turni456 – 4594
Beta strandi465 – 4684
Beta strandi471 – 4733

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F9EX-ray2.90A/C/E/G/I/K222-374[»]
B/D/F/H/J/L390-478[»]
1I4EX-ray3.00B222-479[»]
1QDUX-ray2.80A/C/E/G/I/K222-374[»]
B/D/F/H/J/L390-477[»]
1QTNX-ray1.20A211-374[»]
B385-479[»]
2C2ZX-ray1.95A218-374[»]
B376-479[»]
2FUNX-ray3.00B/D222-479[»]
2K7ZNMR-A217-479[»]
2Y1LX-ray1.80A/C218-374[»]
B/D376-479[»]
3H11X-ray1.90B217-479[»]
3KJNX-ray1.80A211-374[»]
B385-479[»]
3KJQX-ray1.80A211-374[»]
B385-479[»]
4JJ7X-ray1.18A217-479[»]
ProteinModelPortaliQ14790.
SMRiQ14790. Positions 223-479.

Miscellaneous databases

EvolutionaryTraceiQ14790.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8079DED 1
Add
BLAST
Domaini100 – 17778DED 2
Add
BLAST

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.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG303276.
HOVERGENiHBG050803.
InParanoidiQ14790.
KOiK04398.
OMAiIFIEMEK.
OrthoDBiEOG7CRTQM.
PhylomeDBiQ14790.
TreeFamiTF102023.

Family and domain databases

Gene3Di1.10.533.10. 2 hits.
3.40.50.1460. 1 hit.
InterProiIPR029030. Caspase-like_dom.
IPR011029. DEATH-like_dom.
IPR001875. DED.
IPR011600. Pept_C14_caspase.
IPR001309. Pept_C14_ICE_p20.
IPR016129. Pept_C14_ICE_p20_AS.
IPR002138. Pept_C14_p10.
IPR015917. Pept_C14A_p45_core.
[Graphical view]
PfamiPF01335. DED. 2 hits.
PF00656. Peptidase_C14. 1 hit.
[Graphical view]
PRINTSiPR00376. IL1BCENZYME.
SMARTiSM00115. CASc. 1 hit.
SM00031. DED. 2 hits.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 2 hits.
PROSITEiPS01122. CASPASE_CYS. 1 hit.
PS01121. CASPASE_HIS. 1 hit.
PS50207. CASPASE_P10. 1 hit.
PS50208. CASPASE_P20. 1 hit.
PS50168. DED. 2 hits.
[Graphical view]

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. Align

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.

« Hide

MDFSRNLYDI GEQLDSEDLA SLKFLSLDYI PQRKQEPIKD ALMLFQRLQE    50
KRMLEESNLS FLKELLFRIN RLDLLITYLN TRKEEMEREL QTPGRAQISA 100
YRVMLYQISE EVSRSELRSF KFLLQEEISK CKLDDDMNLL DIFIEMEKRV 150
ILGEGKLDIL KRVCAQINKS LLKIINDYEE FSKERSSSLE GSPDEFSNGE 200
ELCGVMTISD SPREQDSESQ TLDKVYQMKS KPRGYCLIIN NHNFAKAREK 250
VPKLHSIRDR NGTHLDAGAL TTTFEELHFE IKPHDDCTVE QIYEILKIYQ 300
LMDHSNMDCF ICCILSHGDK GIIYGTDGQE APIYELTSQF TGLKCPSLAG 350
KPKVFFIQAC QGDNYQKGIP VETDSEEQPY LEMDLSSPQT RYIPDEADFL 400
LGMATVNNCV SYRNPAEGTW YIQSLCQSLR ERCPRGDDIL TILTEVNYEV 450
SNKDDKKNMG KQMPQPTFTL RKKLVFPSD 479
Length:479
Mass (Da):55,391
Last modified:November 1, 1996 - v1
Checksum:i7A5FEAA6B39B582F
GO
Isoform 2 (identifier: Q14790-2) [UniParc]FASTAAdd to Basket

Also known as: Alpha-2, MCH5-beta

The sequence of this isoform differs from the canonical sequence as follows:
     184-198: Missing.

Show »
Length:464
Mass (Da):53,768
Checksum:i7F52F14ADE6A02B6
GO
Isoform 3 (identifier: Q14790-3) [UniParc]FASTAAdd to Basket

Also known as: Alpha-3

The sequence of this isoform differs from the canonical sequence as follows:
     184-267: Missing.

Show »
Length:395
Mass (Da):45,929
Checksum:i2787AE831A2B36EF
GO
Isoform 4 (identifier: Q14790-4) [UniParc]FASTAAdd to Basket

Also known as: Alpha-4

The sequence of this isoform differs from the canonical sequence as follows:
     102-102: R → RFHFCRMSWAEANSQCQTQSVPFWRRVDHLLIR
     184-198: Missing.

Show »
Length:496
Mass (Da):57,701
Checksum:i68136650A49159D9
GO
Isoform 5 (identifier: Q14790-5) [UniParc]FASTAAdd to Basket

Also known as: Beta-1

The sequence of this isoform differs from the canonical sequence as follows:
     199-235: GEELCGVMTISDSPREQDSESQTLDKVYQMKSKPRGY → DFGQSLPNEKQTSGILSDHQQSQFCKSTGESAQTSQH
     236-479: Missing.

Show »
Length:235
Mass (Da):27,484
Checksum:i7C9013CEA85A77DE
GO
Isoform 6 (identifier: Q14790-6) [UniParc]FASTAAdd to Basket

Also known as: Beta-2

The sequence of this isoform differs from the canonical sequence as follows:
     184-220: ERSSSLEGSPDEFSNGEELCGVMTISDSPREQDSESQ → DFGQSLPNEKQTSGILSDHQQSQFCKSTGESAQTSQH
     221-479: Missing.

Show »
Length:220
Mass (Da):25,862
Checksum:iF3DA0380D12006C7
GO
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 »
Length:276
Mass (Da):32,330
Checksum:i227ED77718788F92
GO
Isoform 8 (identifier: Q14790-8) [UniParc]FASTAAdd to Basket

Also known as: Beta-4

The sequence of this isoform differs from the canonical sequence as follows:
     184-198: Missing.
     269-276: ALTTTFEE → TVEPKREK
     277-479: Missing.

Show »
Length:261
Mass (Da):30,707
Checksum:i19ACAE80171E0572
GO
Isoform 9 (identifier: Q14790-9) [UniParc]FASTAAdd to Basket

Also known as: 8L

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEGGRRARVVIESKRNFFLGAFPTPFPAEHVELGRLGDSETAMVPGKGGADYILLPFKKM

Show »
Length:538
Mass (Da):61,836
Checksum:i54402ECFA9FE5E14
GO

Sequence cautioni

The sequence CAA66858.1 differs from that shown. Reason:
The sequence CAA66859.1 differs from that shown. Reason:

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti219 – 2191S → T.1 Publication
Corresponds to variant rs35976359 [ dbSNP | Ensembl ].
VAR_025816
Natural varianti248 – 2481R → W in CASP8D. 1 Publication
Corresponds to variant rs17860424 [ dbSNP | Ensembl ].
VAR_014204
Natural varianti285 – 2851D → H Associated with protection against breast cancer; also associated with a lower risk of cutaneous melanoma. 7 Publications
Corresponds to variant rs1045485 [ dbSNP | Ensembl ].
VAR_020127

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MEGGRRARVVIESKRNFFLG AFPTPFPAEHVELGRLGDSE TAMVPGKGGADYILLPFKKM in isoform 9.
VSP_000808
Alternative sequencei102 – 1021R → RFHFCRMSWAEANSQCQTQS VPFWRRVDHLLIR in isoform 4.
VSP_000809
Alternative sequencei184 – 26784Missing in isoform 3.
VSP_000813Add
BLAST
Alternative sequencei184 – 22037ERSSS…DSESQ → DFGQSLPNEKQTSGILSDHQ QSQFCKSTGESAQTSQH in isoform 6.
VSP_000811Add
BLAST
Alternative sequencei184 – 19815Missing in isoform 2, isoform 4 and isoform 8.
VSP_000810Add
BLAST
Alternative sequencei199 – 23537GEELC…KPRGY → DFGQSLPNEKQTSGILSDHQ QSQFCKSTGESAQTSQH in isoform 5.
VSP_000814Add
BLAST
Alternative sequencei221 – 479259Missing in isoform 6.
VSP_000812Add
BLAST
Alternative sequencei236 – 479244Missing in isoform 5.
VSP_000815Add
BLAST
Alternative sequencei269 – 2768ALTTTFEE → TVEPKREK in isoform 7 and isoform 8.
VSP_000816
Alternative sequencei277 – 479203Missing in isoform 7 and isoform 8.
VSP_000817Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti294 – 2941E → D in AAD24962. 1 Publication
Sequence conflicti331 – 3311A → P in AAC50602. 1 Publication
Sequence conflicti331 – 3311A → P in AAD24962. 1 Publication
Sequence conflicti343 – 3442LK → FG in AAL87631. 1 Publication
Isoform 9 (identifier: Q14790-9)
Sequence conflicti14 – 141K → R in AAL87628. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X98172 mRNA. Translation: CAA66853.1.
X98173 mRNA. Translation: CAA66854.1.
X98174 mRNA. Translation: CAA66855.1.
X98175 mRNA. Translation: CAA66856.1.
X98176 mRNA. Translation: CAA66857.1.
X98177 mRNA. Translation: CAA66858.1. Sequence problems.
X98178 mRNA. Translation: CAA66859.1. Sequence problems.
U58143 mRNA. Translation: AAC50602.1.
U60520 mRNA. Translation: AAC50645.1.
AF009620 mRNA. Translation: AAB70913.1.
AF102146
, AF102139, AF102140, AF102141, AF102142, AF102143, AF102144, AF102145 Genomic DNA. Translation: AAD24962.1.
AB038985 Genomic DNA. Translation: BAB32555.1.
AF380342 mRNA. Translation: AAK57437.1.
AF422925 mRNA. Translation: AAL87628.1.
AF422926 mRNA. Translation: AAL87629.1.
AF422927 mRNA. Translation: AAL87630.1.
AF422928 mRNA. Translation: AAL87631.1.
AF422929 mRNA. Translation: AAL87632.1.
DQ355026 Genomic DNA. Translation: ABC67468.1.
AC007256 Genomic DNA. Translation: AAY24225.1.
BC028223 mRNA. No translation available.
CCDSiCCDS2342.1. [Q14790-1]
CCDS2343.1. [Q14790-2]
CCDS2345.1. [Q14790-5]
CCDS42798.1. [Q14790-9]
CCDS42799.1. [Q14790-4]
RefSeqiNP_001073593.1. NM_001080124.1. [Q14790-2]
NP_001073594.1. NM_001080125.1. [Q14790-9]
NP_001219.2. NM_001228.4. [Q14790-4]
NP_203519.1. NM_033355.3. [Q14790-1]
NP_203520.1. NM_033356.3. [Q14790-2]
NP_203522.1. NM_033358.3. [Q14790-5]
XP_005246943.1. XM_005246886.1. [Q14790-1]
XP_005246944.1. XM_005246887.1. [Q14790-1]
XP_005246945.1. XM_005246888.1. [Q14790-1]
XP_005246946.1. XM_005246889.1. [Q14790-1]
XP_005246947.1. XM_005246890.1. [Q14790-1]
XP_005246948.1. XM_005246891.2. [Q14790-1]
XP_005246949.1. XM_005246892.1. [Q14790-2]
XP_006712852.1. XM_006712789.1. [Q14790-1]
XP_006712853.1. XM_006712790.1. [Q14790-1]
XP_006712856.1. XM_006712793.1. [Q14790-5]
UniGeneiHs.599762.

Genome annotation databases

EnsembliENST00000264274; ENSP00000264274; ENSG00000064012. [Q14790-3]
ENST00000264275; ENSP00000264275; ENSG00000064012. [Q14790-4]
ENST00000323492; ENSP00000325722; ENSG00000064012. [Q14790-2]
ENST00000358485; ENSP00000351273; ENSG00000064012. [Q14790-9]
ENST00000392258; ENSP00000376087; ENSG00000064012. [Q14790-5]
ENST00000392259; ENSP00000376088; ENSG00000064012. [Q14790-5]
ENST00000392263; ENSP00000376091; ENSG00000064012. [Q14790-2]
ENST00000392266; ENSP00000376094; ENSG00000064012. [Q14790-6]
ENST00000432109; ENSP00000412523; ENSG00000064012. [Q14790-1]
GeneIDi841.
KEGGihsa:841.
UCSCiuc002uxo.1. human. [Q14790-5]
uc002uxp.1. human. [Q14790-4]
uc002uxq.1. human. [Q14790-2]
uc002uxr.1. human. [Q14790-1]
uc002uxt.1. human. [Q14790-9]
uc002uxv.1. human. [Q14790-8]
uc010fte.1. human. [Q14790-6]
uc010ftf.2. human. [Q14790-3]

Polymorphism databases

DMDMi2493531.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

CASP8base

CASP8 mutation db

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X98172 mRNA. Translation: CAA66853.1 .
X98173 mRNA. Translation: CAA66854.1 .
X98174 mRNA. Translation: CAA66855.1 .
X98175 mRNA. Translation: CAA66856.1 .
X98176 mRNA. Translation: CAA66857.1 .
X98177 mRNA. Translation: CAA66858.1 . Sequence problems.
X98178 mRNA. Translation: CAA66859.1 . Sequence problems.
U58143 mRNA. Translation: AAC50602.1 .
U60520 mRNA. Translation: AAC50645.1 .
AF009620 mRNA. Translation: AAB70913.1 .
AF102146
, AF102139 , AF102140 , AF102141 , AF102142 , AF102143 , AF102144 , AF102145 Genomic DNA. Translation: AAD24962.1 .
AB038985 Genomic DNA. Translation: BAB32555.1 .
AF380342 mRNA. Translation: AAK57437.1 .
AF422925 mRNA. Translation: AAL87628.1 .
AF422926 mRNA. Translation: AAL87629.1 .
AF422927 mRNA. Translation: AAL87630.1 .
AF422928 mRNA. Translation: AAL87631.1 .
AF422929 mRNA. Translation: AAL87632.1 .
DQ355026 Genomic DNA. Translation: ABC67468.1 .
AC007256 Genomic DNA. Translation: AAY24225.1 .
BC028223 mRNA. No translation available.
CCDSi CCDS2342.1. [Q14790-1 ]
CCDS2343.1. [Q14790-2 ]
CCDS2345.1. [Q14790-5 ]
CCDS42798.1. [Q14790-9 ]
CCDS42799.1. [Q14790-4 ]
RefSeqi NP_001073593.1. NM_001080124.1. [Q14790-2 ]
NP_001073594.1. NM_001080125.1. [Q14790-9 ]
NP_001219.2. NM_001228.4. [Q14790-4 ]
NP_203519.1. NM_033355.3. [Q14790-1 ]
NP_203520.1. NM_033356.3. [Q14790-2 ]
NP_203522.1. NM_033358.3. [Q14790-5 ]
XP_005246943.1. XM_005246886.1. [Q14790-1 ]
XP_005246944.1. XM_005246887.1. [Q14790-1 ]
XP_005246945.1. XM_005246888.1. [Q14790-1 ]
XP_005246946.1. XM_005246889.1. [Q14790-1 ]
XP_005246947.1. XM_005246890.1. [Q14790-1 ]
XP_005246948.1. XM_005246891.2. [Q14790-1 ]
XP_005246949.1. XM_005246892.1. [Q14790-2 ]
XP_006712852.1. XM_006712789.1. [Q14790-1 ]
XP_006712853.1. XM_006712790.1. [Q14790-1 ]
XP_006712856.1. XM_006712793.1. [Q14790-5 ]
UniGenei Hs.599762.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q14790.
SMRi Q14790. Positions 223-479.
ModBasei Search...

Protein-protein interaction databases

BioGridi 107291. 91 interactions.
DIPi DIP-30915N.
IntActi Q14790. 67 interactions.
MINTi MINT-91645.

Chemistry

BindingDBi Q14790.
ChEMBLi CHEMBL3776.
GuidetoPHARMACOLOGYi 1624.

Protein family/group databases

MEROPSi C14.009.

PTM databases

PhosphoSitei Q14790.

Polymorphism databases

DMDMi 2493531.

Proteomic databases

MaxQBi Q14790.
PaxDbi Q14790.
PRIDEi Q14790.

Protocols and materials databases

DNASUi 841.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264274 ; ENSP00000264274 ; ENSG00000064012 . [Q14790-3 ]
ENST00000264275 ; ENSP00000264275 ; ENSG00000064012 . [Q14790-4 ]
ENST00000323492 ; ENSP00000325722 ; ENSG00000064012 . [Q14790-2 ]
ENST00000358485 ; ENSP00000351273 ; ENSG00000064012 . [Q14790-9 ]
ENST00000392258 ; ENSP00000376087 ; ENSG00000064012 . [Q14790-5 ]
ENST00000392259 ; ENSP00000376088 ; ENSG00000064012 . [Q14790-5 ]
ENST00000392263 ; ENSP00000376091 ; ENSG00000064012 . [Q14790-2 ]
ENST00000392266 ; ENSP00000376094 ; ENSG00000064012 . [Q14790-6 ]
ENST00000432109 ; ENSP00000412523 ; ENSG00000064012 . [Q14790-1 ]
GeneIDi 841.
KEGGi hsa:841.
UCSCi uc002uxo.1. human. [Q14790-5 ]
uc002uxp.1. human. [Q14790-4 ]
uc002uxq.1. human. [Q14790-2 ]
uc002uxr.1. human. [Q14790-1 ]
uc002uxt.1. human. [Q14790-9 ]
uc002uxv.1. human. [Q14790-8 ]
uc010fte.1. human. [Q14790-6 ]
uc010ftf.2. human. [Q14790-3 ]

Organism-specific databases

CTDi 841.
GeneCardsi GC02P202062.
HGNCi HGNC:1509. CASP8.
HPAi CAB002047.
HPA001302.
HPA005688.
HPA006191.
MIMi 211980. phenotype.
601763. gene.
607271. phenotype.
neXtProti NX_Q14790.
Orphaneti 275517. Autoimmune lymphoproliferative syndrome with recurrent infections.
PharmGKBi PA26092.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG303276.
HOVERGENi HBG050803.
InParanoidi Q14790.
KOi K04398.
OMAi IFIEMEK.
OrthoDBi EOG7CRTQM.
PhylomeDBi Q14790.
TreeFami TF102023.

Enzyme and pathway databases

BRENDAi 3.4.22.61. 2681.
Reactomei REACT_107. Apoptotic cleavage of cellular proteins.
REACT_13541. Caspase-mediated cleavage of cytoskeletal proteins.
REACT_1432. TNF signaling.
REACT_1503. Caspase-8 activation.
REACT_150361. TRIF-mediated programmed cell death.
REACT_164011. Regulation by c-FLIP.
REACT_25039. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
REACT_402. TRAIL signaling.
REACT_701. Activation, myristolyation of BID and translocation to mitochondria.
REACT_75776. NOD1/2 Signaling Pathway.
REACT_832. Dimerization of procaspase-8.
REACT_900. FasL/ CD95L signaling.
REACT_995. Apoptotic execution phase.
SignaLinki Q14790.

Miscellaneous databases

ChiTaRSi CASP8. human.
EvolutionaryTracei Q14790.
GeneWikii Caspase_8.
GenomeRNAii 841.
NextBioi 3510.
PMAP-CutDB Q14790.
PROi Q14790.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q14790.
Bgeei Q14790.
Genevestigatori Q14790.

Family and domain databases

Gene3Di 1.10.533.10. 2 hits.
3.40.50.1460. 1 hit.
InterProi IPR029030. Caspase-like_dom.
IPR011029. DEATH-like_dom.
IPR001875. DED.
IPR011600. Pept_C14_caspase.
IPR001309. Pept_C14_ICE_p20.
IPR016129. Pept_C14_ICE_p20_AS.
IPR002138. Pept_C14_p10.
IPR015917. Pept_C14A_p45_core.
[Graphical view ]
Pfami PF01335. DED. 2 hits.
PF00656. Peptidase_C14. 1 hit.
[Graphical view ]
PRINTSi PR00376. IL1BCENZYME.
SMARTi SM00115. CASc. 1 hit.
SM00031. DED. 2 hits.
[Graphical view ]
SUPFAMi SSF47986. SSF47986. 2 hits.
PROSITEi PS01122. CASPASE_CYS. 1 hit.
PS01121. CASPASE_HIS. 1 hit.
PS50207. CASPASE_P10. 1 hit.
PS50208. CASPASE_P20. 1 hit.
PS50168. DED. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death."
    Boldin M.P., Goncharov T.M., Goltsev Y.V., Wallach D.
    Cell 85:803-815(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 5; 6; 7 AND 8).
    Tissue: B-cell and Thymus.
  2. "FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex."
    Muzio M., Chinnaiyan A.M., Kischkel F.C., O'Rourke K., Shevchenko A., Ni J., Scaffidi C., Bretz J.D., Zhang M., Gentz R., Mann M., Krammer P.H., Peter M.E., Dixit V.M.
    Cell 85:817-827(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
  3. "In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains."
    Fernandes-Alnemri T., Armstrong R.C., Krebs J.F., Srinivasula S.M., Wang L., Bullrich F., Fritz L.C., Trapani J.A., Tomaselli K.J., Litwack G., Alnemri E.S.
    Proc. Natl. Acad. Sci. U.S.A. 93:7464-7469(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), VARIANT HIS-285.
    Tissue: T-cell.
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT HIS-285.
  5. "Structure and chromosome localization of the human CASP8 gene."
    Grenet J., Teitz T., Wei T., Valentine V., Kidd V.J.
    Gene 226:225-232(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "Cloning and characterization of three novel genes, ALS2CR1, ALS2CR2, and ALS2CR3, in the juvenile amyotrophic lateral sclerosis (ALS2) critical region at chromosome 2q33-q34: candidate genes for ALS2."
    Hadano S., Yanagisawa Y., Skaug J., Fichter K., Nasir J., Martindale D., Koop B.F., Scherer S.W., Nicholson D.W., Rouleau G.A., Ikeda J.-E., Hayden M.R.
    Genomics 71:200-213(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-285.
  7. "Characterization of caspase-8L: a novel isoform of caspase-8 that behaves as an inhibitor of the caspase cascade."
    Himeji D., Horiuchi T., Tsukamoto H., Hayashi K., Watanabe T., Harada M.
    Blood 99:4070-4078(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), FUNCTION (ISOFORM 7).
    Tissue: Leukocyte.
  8. "The procaspase-8 isoform, procaspase-8L, recruited to the BAP31 complex at the endoplasmic reticulum."
    Breckenridge D.G., Nguyen M., Kuppig S., Reth M., Shore G.C.
    Proc. Natl. Acad. Sci. U.S.A. 99:4331-4336(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 9), INTERACTION OF ISOFORM 9 WITH BCAP31 AT THE ENDOPLASMIC RETICULUM.
  9. NIEHS SNPs program
    Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-219 AND HIS-285.
  10. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
    Tissue: Leukocyte.
  12. "Molecular ordering of the Fas-apoptotic pathway: the Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases."
    Srinivasula S.M., Ahmad M., Fernandes-Alnemri T., Litwack G., Alnemri E.S.
    Proc. Natl. Acad. Sci. U.S.A. 93:14486-14491(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, PROTEOLYTIC PROCESSING.
  13. "FLICE induced apoptosis in a cell-free system. Cleavage of caspase zymogens."
    Muzio M., Salvesen G.S., Dixit V.M.
    J. Biol. Chem. 272:2952-2956(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "FLICE is activated by association with the CD95 death-inducing signaling complex (DISC)."
    Medema J.P., Scaffidi C., Kischkel F.C., Shevchenko A., Mann M., Krammer P.H., Peter M.E.
    EMBO J. 16:2794-2804(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING.
  15. "Dominant expression of a novel splice variant of caspase-8 in human peripheral blood lymphocytes."
    Horiuchi T., Himeji D., Tsukamoto H., Harashima S., Hashimura C., Hayashi K.
    Biochem. Biophys. Res. Commun. 272:877-881(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION (ISOFORM 7).
  16. "p28 Bap31, a Bcl-2/Bcl-XL- and procaspase-8-associated protein in the endoplasmic reticulum."
    Ng F.W.H., Nguyen M., Kwan T., Branton P.E., Nicholson D.W., Cromlish J.A., Shore G.C.
    J. Cell Biol. 139:327-338(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BCL2; BCL2L1 AND BCAP31.
  17. "PED/PEA-15: an anti-apoptotic molecule that regulates FAS/TNFR1-induced apoptosis."
    Condorelli G., Vigliotta G., Cafieri A., Trencia A., Andalo P., Oriente F., Miele C., Caruso M., Formisano P., Beguinot F.
    Oncogene 18:4409-4415(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PEA15.
  18. "A cytomegalovirus-encoded inhibitor of apoptosis that suppresses caspase-8 activation."
    Skaletskaya A., Bartle L.M., Chittenden T., McCormick A.L., Mocarski E.S., Goldmacher V.S.
    Proc. Natl. Acad. Sci. U.S.A. 98:7829-7834(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HHV-5 PROTEIN UL36.
  19. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
  20. "Suppression of caspase-8- and -10-associated RING proteins results in sensitization to death ligands and inhibition of tumor cell growth."
    McDonald E.R. III, El-Deiry W.S.
    Proc. Natl. Acad. Sci. U.S.A. 101:6170-6175(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RFFL.
  21. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-334, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Role of FLASH in caspase-8-mediated activation of NF-kappaB: dominant-negative function of FLASH mutant in NF-kappaB signaling pathway."
    Jun J.-I., Chung C.-W., Lee H.-J., Pyo J.-O., Lee K.N., Kim N.-S., Kim Y.S., Yoo H.-S., Lee T.-H., Kim E., Jung Y.-K.
    Oncogene 24:688-696(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-73.
  23. "FLASH links the CD95 signaling pathway to the cell nucleus and nuclear bodies."
    Milovic-Holm K., Krieghoff E., Jensen K., Will H., Hofmann T.G.
    EMBO J. 26:391-401(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CASP8P2.
  24. "Cdk1/cyclin B1 controls Fas-mediated apoptosis by regulating caspase-8 activity."
    Matthess Y., Raab M., Sanhaji M., Lavrik I.N., Strebhardt K.
    Mol. Cell. Biol. 30:5726-5740(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-387 BY CDK1.
  25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "The E.coli effector protein NleF is a caspase inhibitor."
    Blasche S., Moertl M., Steuber H., Siszler G., Nisa S., Schwarz F., Lavrik I., Gronewold T.M.A., Maskos K., Donnenberg M.S., Ullmann D., Uetz P., Koegl M.
    PLoS ONE 0:0-0(2013)
    Cited for: INTERACTION WITH E.COLI NLEF, CATALYTIC ACTIVITY, FUNCTION, ENZYME REGULATION.
  27. "The three-dimensional structure of caspase-8: an initiator enzyme in apoptosis."
    Blanchard H., Kodandapani L., Mittl P.R.E., Di Marco S., Krebs J.F., Wu J.C., Tomaselli K.J., Gruetter M.G.
    Structure 7:1125-1133(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
  28. "The atomic-resolution structure of human caspase-8, a key activator of apoptosis."
    Watt W., Koeplinger K.A., Mildner A.M., Heinrikson R.L., Tomasselli A.G., Watenpaugh K.D.
    Structure 7:1135-1143(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 211-479, SUBUNIT.
  29. "Pleiotropic defects in lymphocyte activation caused by caspase-8 mutations lead to human immunodeficiency."
    Chun H.J., Zheng L., Ahmad M., Wang J., Speirs C.K., Siegel R.M., Dale J.K., Puck J., Davis J., Hall C.G., Skoda-Smith S., Atkinson T.P., Straus S.E., Lenardo M.J.
    Nature 419:395-399(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CASP8D TRP-248.
  30. Cited for: VARIANT HIS-285, PROTECTION AGAINST BREAST CANCER.
  31. "A common coding variant in CASP8 is associated with breast cancer risk."
    The Kathleen Cunningham foundation consortium for research into familial breast cancer, Breast cancer association consortium
    Cox A., Dunning A.M., Garcia-Closas M., Balasubramanian S., Reed M.W.R., Pooley K.A., Scollen S., Baynes C., Ponder B.A.J., Chanock S., Lissowska J., Brinton L., Peplonska B., Southey M.C., Hopper J.L., McCredie M.R.E., Giles G.G., Fletcher O.
    , Johnson N., dos Santos Silva I., Gibson L., Bojesen S.E., Nordestgaard B.G., Axelsson C.K., Torres D., Hamann U., Justenhoven C., Brauch H., Chang-Claude J., Kropp S., Risch A., Wang-Gohrke S., Schuermann P., Bogdanova N., Doerk T., Fagerholm R., Aaltonen K., Blomqvist C., Nevanlinna H., Seal S., Renwick A., Stratton M.R., Rahman N., Sangrajrang S., Hughes D., Odefrey F., Brennan P., Spurdle A.B., Chenevix-Trench G., Beesley J., Mannermaa A., Hartikainen J., Kataja V., Kosma V.M., Couch F.J., Olson J.E., Goode E.L., Broeks A., Schmidt M.K., Hogervorst F.B.L., Van't Veer L.J., Kang D., Yoo K.-Y., Noh D.-Y., Ahn S.-H., Wedren S., Hall P., Low Y.-L., Liu J., Milne R.L., Ribas G., Gonzalez-Neira A., Benitez J., Sigurdson A.J., Stredrick D.L., Alexander B.H., Struewing J.P., Pharoah P.D.P., Easton D.F.
    Nat. Genet. 39:352-358(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HIS-285, PROTECTION AGAINST BREAST CANCER.
  32. "A six-nucleotide insertion-deletion polymorphism in the CASP8 promoter is associated with susceptibility to multiple cancers."
    Sun T., Gao Y., Tan W., Ma S., Shi Y., Yao J., Guo Y., Yang M., Zhang X., Zhang Q., Zeng C., Lin D.
    Nat. Genet. 39:605-613(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN PROTECTION AGAINST LUNG CANCER.
  33. "Genetic variants and haplotypes of the caspase-8 and caspase-10 genes contribute to susceptibility to cutaneous melanoma."
    Li C., Zhao H., Hu Z., Liu Z., Wang L.-E., Gershenwald J.E., Prieto V.G., Lee J.E., Duvic M., Grimm E.A., Wei Q.
    Hum. Mutat. 29:1443-1451(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HIS-285, RISK FACTOR FOR CUTANEOUS MELANOMA.

Entry informationi

Entry nameiCASP8_HUMAN
AccessioniPrimary (citable) accession number: Q14790
Secondary accession number(s): O14676
, Q14791, Q14792, Q14793, Q14794, Q14795, Q14796, Q15780, Q15806, Q53TT5, Q8TDI1, Q8TDI2, Q8TDI3, Q8TDI4, Q8TDI5, Q96T22, Q9C0K4, Q9UQ81
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: September 3, 2014
This is version 181 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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 proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi