Q14790 (CASP8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Caspase-8
Short name=CASP-8
EC=3.4.22.61

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:

1. Caspase-8 subunit p18
2. Caspase-8 subunit p10

Gene names

Name:	CASP8
Synonyms:	MCH5

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	479 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.7 Ref.13 Ref.25
Catalytic activity	Strict requirement for Asp at position P1 and has a preferred cleavage sequence of (Leu/Asp/Val)-Glu-Thr-Asp-|-(Gly/Ser/Ala). Ref.25
Enzyme regulation	Inhibited by the effector protein NleF that is produced by pathogenic E.coli; this inhibits apoptosis. Ref.25
Subunit structure	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 human cytomegalovirus/HHV-5 protein vICA/UL36; this interaction inhibits CASP8 activation. Interacts with NleF from pathogenic E.coli. Ref.8 Ref.16 Ref.17 Ref.18 Ref.22 Ref.25 Ref.27
Subcellular location	Cytoplasm.
Tissue specificity	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.
Domain	Isoform 9 contains a N-terminal extension that is required for interaction with the BCAP31 complex.
Post-translational modification	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.
Polymorphism	Genetic variations in CASP8 are associated with reduced risk of lung cancer [MIM: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.
Involvement in disease	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. Ref.28
Sequence similarities	Belongs to the peptidase C14A family. Contains 2 DED (death effector) domains.
Sequence caution	The sequence CAA66858.1 differs from that shown. Reason: The sequence CAA66859.1 differs from that shown. Reason:

Ontologies

Keywords
Biological process	Apoptosis Host-virus interaction
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Repeat
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	TRIF-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome activation of cysteine-type endopeptidase activity involved in apoptotic process Traceable author statement. Source: Reactome angiogenesis Inferred from electronic annotation. Source: Compara cellular component disassembly involved in execution phase of apoptosis Traceable author statement. Source: Reactome cellular response to mechanical stimulus Inferred from expression pattern PubMed 19593445. Source: UniProtKB extrinsic apoptotic signaling pathway Inferred from direct assay PubMed 21785459. Source: UniProtKB heart development Inferred from electronic annotation. Source: Compara innate immune response Traceable author statement. Source: Reactome intrinsic apoptotic signaling pathway Traceable author statement. Source: Reactome macrophage differentiation Inferred from electronic annotation. Source: Compara negative regulation of I-kappaB kinase/NF-kappaB cascade Inferred from mutant phenotype PubMed 17047155. Source: UniProtKB neural tube formation Inferred from electronic annotation. Source: Compara nucleotide-binding oligomerization domain containing signaling pathway Traceable author statement. Source: Reactome positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from mutant phenotype PubMed 12884866. Source: UniProtKB positive regulation of macrophage differentiation Inferred from mutant phenotype PubMed 17047155. Source: UniProtKB positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Traceable author statement. Source: Reactome positive regulation of proteolysis Inferred from direct assay PubMed 18387192. Source: BHF-UCL protein heterooligomerization Inferred from electronic annotation. Source: Compara proteolysis involved in cellular protein catabolic process Inferred from mutant phenotype PubMed 10521396. Source: BHF-UCL response to antibiotic Inferred from electronic annotation. Source: Compara response to cobalt ion Inferred from electronic annotation. Source: Compara response to cold Inferred from electronic annotation. Source: Compara response to estradiol stimulus Inferred from electronic annotation. Source: Compara response to ethanol Inferred from electronic annotation. Source: Compara response to lipopolysaccharide Inferred from electronic annotation. Source: Compara response to tumor necrosis factor Inferred from mutant phenotype PubMed 10521396. Source: BHF-UCL toll-like receptor 3 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 4 signaling pathway Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	CD95 death-inducing signaling complex Inferred from electronic annotation. Source: Compara Noc1p-Noc2p complex Inferred from electronic annotation. Source: Compara cell body Inferred from electronic annotation. Source: Compara centrosome Inferred from direct assay. Source: HPA cytosol Traceable author statement. Source: Reactome death-inducing signaling complex Inferred from direct assay PubMed 21803845. Source: UniProtKB membrane raft Inferred from electronic annotation. Source: Compara mitochondrial outer membrane Traceable author statement. Source: Reactome neuron projection Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay. Source: HPA
Molecular_function	cysteine-type endopeptidase activity Inferred from direct assay PubMed 19240112. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-78060,EBI-78060
BCAP31	P51572	3	EBI-78060,EBI-77683
CASP10	Q92851	5	EBI-78060,EBI-495095
CUL3	Q13618	6	EBI-78060,EBI-456129
FADD	Q13158	30	EBI-78060,EBI-494804
FAS	P25445	12	EBI-78060,EBI-494743
ILK	Q13418	2	EBI-78060,EBI-747644
MALT1	Q9UDY8	8	EBI-78060,EBI-1047372
NOL3	O60936	3	EBI-78060,EBI-740992
RIPK1	Q13546	23	EBI-78060,EBI-358507
TNFRSF10A	O00220	9	EBI-78060,EBI-518861

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q14790-1)

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.

Isoform 2 (identifier: Q14790-2)

Also known as: Alpha-2; MCH5-beta;

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

Isoform 3 (identifier: Q14790-3)

Also known as: Alpha-3;

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

Isoform 4 (identifier: Q14790-4)

Also known as: Alpha-4;

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

Isoform 5 (identifier: Q14790-5)

Also known as: Beta-1;

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

Isoform 6 (identifier: Q14790-6)

Also known as: Beta-2;

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

Isoform 7 (identifier: Q14790-7)

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.

Isoform 8 (identifier: Q14790-8)

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.

Isoform 9 (identifier: Q14790-9)

Also known as: 8L;

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 216

216

PRO_0000004628

Chain

217 – 374

158

Caspase-8 subunit p18

PRO_0000004629

Propeptide

375 – 384

10

PRO_0000004630

Chain

385 – 479

95

Caspase-8 subunit p10

PRO_0000004631

Regions

Domain

2 – 80

79

DED 1

Domain

100 – 177

78

DED 2

Sites

Active site

317

1

Active site

360

1

Amino acid modifications

Modified residue

188

1

Phosphoserine By similarity

Modified residue

334

1

Phosphotyrosine Ref.20

Modified residue

387

1

Phosphoserine; by CDK1 Ref.23

Natural variations

Alternative sequence

1

1

M → MEGGRRARVVIESKRNFFLG AFPTPFPAEHVELGRLGDSE TAMVPGKGGADYILLPFKKM in isoform 9.

VSP_000808

Alternative sequence

102

1

R → RFHFCRMSWAEANSQCQTQS VPFWRRVDHLLIR in isoform 4.

VSP_000809

Alternative sequence

184 – 267

84

Missing in isoform 3.

VSP_000813

Alternative sequence

184 – 220

37

ERSSS…DSESQ → DFGQSLPNEKQTSGILSDHQ QSQFCKSTGESAQTSQH in isoform 6.

VSP_000811

Alternative sequence

184 – 198

15

Missing in isoform 2, isoform 4 and isoform 8.

VSP_000810

Alternative sequence

199 – 235

37

GEELC…KPRGY → DFGQSLPNEKQTSGILSDHQ QSQFCKSTGESAQTSQH in isoform 5.

VSP_000814

Alternative sequence

221 – 479

259

Missing in isoform 6.

VSP_000812

Alternative sequence

236 – 479

244

Missing in isoform 5.

VSP_000815

Alternative sequence

269 – 276

8

ALTTTFEE → TVEPKREK in isoform 7 and isoform 8.

VSP_000816

Alternative sequence

277 – 479

203

Missing in isoform 7 and isoform 8.

VSP_000817

Natural variant

219

1

S → T. Ref.9
Corresponds to variant rs35976359 [ dbSNP | Ensembl ].

VAR_025816

Natural variant

248

1

R → W in CASP8D. Ref.28
Corresponds to variant rs17860424 [ dbSNP | Ensembl ].

VAR_014204

Natural variant

285

1

D → H Associated with protection against breast cancer; also associated with a lower risk of cutaneous melanoma. Ref.3 Ref.4 Ref.6 Ref.9 Ref.29 Ref.30 Ref.33
Corresponds to variant rs1045485 [ dbSNP | Ensembl ].

VAR_020127

Experimental info

Mutagenesis

73

1

D → A: Abolishes binding to FLASH. Induces NF-kappa-B activation. Ref.21

Mutagenesis

387

1

S → A: Impaired CDK1-mediated phosphorylation and enhanced apoptosis.

Sequence conflict

294

1

E → D in AAD24962. Ref.5

Sequence conflict

331

1

A → P in AAC50602. Ref.2

Sequence conflict

331

1

A → P in AAD24962. Ref.5

Sequence conflict

343 – 344

2

LK → FG in AAL87631. Ref.8

Isoform 9:

Sequence conflict

14

1

K → R in AAL87628. Ref.8

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

479

Helix Strand Turn

Details...

Beta strand

230 – 232

3

Beta strand

235 – 240

6

Helix

246 – 249

4

Helix

252 – 254

3

Beta strand

255 – 257

3

Helix

263 – 276

14

Beta strand

280 – 286

7

Helix

289 – 301

13

Beta strand

310 – 316

7

Beta strand

322 – 324

3

Beta strand

326 – 328

3

Beta strand

330 – 332

3

Helix

333 – 337

5

Helix

338 – 340

3

Turn

342 – 344

3

Helix

346 – 348

3

Beta strand

353 – 359

7

Beta strand

362 – 364

3

Beta strand

377 – 379

3

Beta strand

395 – 405

11

Beta strand

412 – 414

3

Turn

415 – 417

3

Helix

420 – 432

13

Helix

433 – 435

3

Helix

439 – 451

13

Turn

456 – 459

4

Beta strand

465 – 468

4

Beta strand

471 – 473

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Alpha-1) [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 7A5FEAA6B39B582F	FASTA	479	55,391
	10 20 30 40 50 60 MDFSRNLYDI GEQLDSEDLA SLKFLSLDYI PQRKQEPIKD ALMLFQRLQE KRMLEESNLS 70 80 90 100 110 120 FLKELLFRIN RLDLLITYLN TRKEEMEREL QTPGRAQISA YRVMLYQISE EVSRSELRSF 130 140 150 160 170 180 KFLLQEEISK CKLDDDMNLL DIFIEMEKRV ILGEGKLDIL KRVCAQINKS LLKIINDYEE 190 200 210 220 230 240 FSKERSSSLE GSPDEFSNGE ELCGVMTISD SPREQDSESQ TLDKVYQMKS KPRGYCLIIN 250 260 270 280 290 300 NHNFAKAREK VPKLHSIRDR NGTHLDAGAL TTTFEELHFE IKPHDDCTVE QIYEILKIYQ 310 320 330 340 350 360 LMDHSNMDCF ICCILSHGDK GIIYGTDGQE APIYELTSQF TGLKCPSLAG KPKVFFIQAC 370 380 390 400 410 420 QGDNYQKGIP VETDSEEQPY LEMDLSSPQT RYIPDEADFL LGMATVNNCV SYRNPAEGTW 430 440 450 460 470 YIQSLCQSLR ERCPRGDDIL TILTEVNYEV SNKDDKKNMG KQMPQPTFTL RKKLVFPSD
	Isoform 2 (Alpha-2) (MCH5-beta) [UniParc]. Checksum: 7F52F14ADE6A02B6	FASTA	464	53,768
	10 20 30 40 50 60 MDFSRNLYDI GEQLDSEDLA SLKFLSLDYI PQRKQEPIKD ALMLFQRLQE KRMLEESNLS 70 80 90 100 110 120 FLKELLFRIN RLDLLITYLN TRKEEMEREL QTPGRAQISA YRVMLYQISE EVSRSELRSF 130 140 150 160 170 180 KFLLQEEISK CKLDDDMNLL DIFIEMEKRV ILGEGKLDIL KRVCAQINKS LLKIINDYEE 190 200 210 220 230 240 FSKGEELCGV MTISDSPREQ DSESQTLDKV YQMKSKPRGY CLIINNHNFA KAREKVPKLH 250 260 270 280 290 300 SIRDRNGTHL DAGALTTTFE ELHFEIKPHD DCTVEQIYEI LKIYQLMDHS NMDCFICCIL 310 320 330 340 350 360 SHGDKGIIYG TDGQEAPIYE LTSQFTGLKC PSLAGKPKVF FIQACQGDNY QKGIPVETDS 370 380 390 400 410 420 EEQPYLEMDL SSPQTRYIPD EADFLLGMAT VNNCVSYRNP AEGTWYIQSL CQSLRERCPR 430 440 450 460 GDDILTILTE VNYEVSNKDD KKNMGKQMPQ PTFTLRKKLV FPSD
	Isoform 3 (Alpha-3) [UniParc]. Checksum: 2787AE831A2B36EF	FASTA	395	45,929
	10 20 30 40 50 60 MDFSRNLYDI GEQLDSEDLA SLKFLSLDYI PQRKQEPIKD ALMLFQRLQE KRMLEESNLS 70 80 90 100 110 120 FLKELLFRIN RLDLLITYLN TRKEEMEREL QTPGRAQISA YRVMLYQISE EVSRSELRSF 130 140 150 160 170 180 KFLLQEEISK CKLDDDMNLL DIFIEMEKRV ILGEGKLDIL KRVCAQINKS LLKIINDYEE 190 200 210 220 230 240 FSKGALTTTF EELHFEIKPH DDCTVEQIYE ILKIYQLMDH SNMDCFICCI LSHGDKGIIY 250 260 270 280 290 300 GTDGQEAPIY ELTSQFTGLK CPSLAGKPKV FFIQACQGDN YQKGIPVETD SEEQPYLEMD 310 320 330 340 350 360 LSSPQTRYIP DEADFLLGMA TVNNCVSYRN PAEGTWYIQS LCQSLRERCP RGDDILTILT 370 380 390 EVNYEVSNKD DKKNMGKQMP QPTFTLRKKL VFPSD
	Isoform 4 (Alpha-4) [UniParc]. Checksum: 68136650A49159D9	FASTA	496	57,701
	10 20 30 40 50 60 MDFSRNLYDI GEQLDSEDLA SLKFLSLDYI PQRKQEPIKD ALMLFQRLQE KRMLEESNLS 70 80 90 100 110 120 FLKELLFRIN RLDLLITYLN TRKEEMEREL QTPGRAQISA YRFHFCRMSW AEANSQCQTQ 130 140 150 160 170 180 SVPFWRRVDH LLIRVMLYQI SEEVSRSELR SFKFLLQEEI SKCKLDDDMN LLDIFIEMEK 190 200 210 220 230 240 RVILGEGKLD ILKRVCAQIN KSLLKIINDY EEFSKGEELC GVMTISDSPR EQDSESQTLD 250 260 270 280 290 300 KVYQMKSKPR GYCLIINNHN FAKAREKVPK LHSIRDRNGT HLDAGALTTT FEELHFEIKP 310 320 330 340 350 360 HDDCTVEQIY EILKIYQLMD HSNMDCFICC ILSHGDKGII YGTDGQEAPI YELTSQFTGL 370 380 390 400 410 420 KCPSLAGKPK VFFIQACQGD NYQKGIPVET DSEEQPYLEM DLSSPQTRYI PDEADFLLGM 430 440 450 460 470 480 ATVNNCVSYR NPAEGTWYIQ SLCQSLRERC PRGDDILTIL TEVNYEVSNK DDKKNMGKQM 490 PQPTFTLRKK LVFPSD
	Isoform 5 (Beta-1) [UniParc]. Checksum: 7C9013CEA85A77DE	FASTA	235	27,484
	10 20 30 40 50 60 MDFSRNLYDI GEQLDSEDLA SLKFLSLDYI PQRKQEPIKD ALMLFQRLQE KRMLEESNLS 70 80 90 100 110 120 FLKELLFRIN RLDLLITYLN TRKEEMEREL QTPGRAQISA YRVMLYQISE EVSRSELRSF 130 140 150 160 170 180 KFLLQEEISK CKLDDDMNLL DIFIEMEKRV ILGEGKLDIL KRVCAQINKS LLKIINDYEE 190 200 210 220 230 FSKERSSSLE GSPDEFSNDF GQSLPNEKQT SGILSDHQQS QFCKSTGESA QTSQH
	Isoform 6 (Beta-2) [UniParc]. Checksum: F3DA0380D12006C7	FASTA	220	25,862
	10 20 30 40 50 60 MDFSRNLYDI GEQLDSEDLA SLKFLSLDYI PQRKQEPIKD ALMLFQRLQE KRMLEESNLS 70 80 90 100 110 120 FLKELLFRIN RLDLLITYLN TRKEEMEREL QTPGRAQISA YRVMLYQISE EVSRSELRSF 130 140 150 160 170 180 KFLLQEEISK CKLDDDMNLL DIFIEMEKRV ILGEGKLDIL KRVCAQINKS LLKIINDYEE 190 200 210 220 FSKDFGQSLP NEKQTSGILS DHQQSQFCKS TGESAQTSQH
	Isoform 7 (Beta-3) (8L) [UniParc]. Checksum: 227ED77718788F92	FASTA	276	32,330
	10 20 30 40 50 60 MDFSRNLYDI GEQLDSEDLA SLKFLSLDYI PQRKQEPIKD ALMLFQRLQE KRMLEESNLS 70 80 90 100 110 120 FLKELLFRIN RLDLLITYLN TRKEEMEREL QTPGRAQISA YRVMLYQISE EVSRSELRSF 130 140 150 160 170 180 KFLLQEEISK CKLDDDMNLL DIFIEMEKRV ILGEGKLDIL KRVCAQINKS LLKIINDYEE 190 200 210 220 230 240 FSKERSSSLE GSPDEFSNGE ELCGVMTISD SPREQDSESQ TLDKVYQMKS KPRGYCLIIN 250 260 270 NHNFAKAREK VPKLHSIRDR NGTHLDAGTV EPKREK
	Isoform 8 (Beta-4) [UniParc]. Checksum: 19ACAE80171E0572	FASTA	261	30,707
	10 20 30 40 50 60 MDFSRNLYDI GEQLDSEDLA SLKFLSLDYI PQRKQEPIKD ALMLFQRLQE KRMLEESNLS 70 80 90 100 110 120 FLKELLFRIN RLDLLITYLN TRKEEMEREL QTPGRAQISA YRVMLYQISE EVSRSELRSF 130 140 150 160 170 180 KFLLQEEISK CKLDDDMNLL DIFIEMEKRV ILGEGKLDIL KRVCAQINKS LLKIINDYEE 190 200 210 220 230 240 FSKGEELCGV MTISDSPREQ DSESQTLDKV YQMKSKPRGY CLIINNHNFA KAREKVPKLH 250 260 SIRDRNGTHL DAGTVEPKRE K
	Isoform 9 (8L) [UniParc]. Checksum: 54402ECFA9FE5E14	FASTA	538	61,836
	10 20 30 40 50 60 MEGGRRARVV IESKRNFFLG AFPTPFPAEH VELGRLGDSE TAMVPGKGGA DYILLPFKKM 70 80 90 100 110 120 DFSRNLYDIG EQLDSEDLAS LKFLSLDYIP QRKQEPIKDA LMLFQRLQEK RMLEESNLSF 130 140 150 160 170 180 LKELLFRINR LDLLITYLNT RKEEMERELQ TPGRAQISAY RVMLYQISEE VSRSELRSFK 190 200 210 220 230 240 FLLQEEISKC KLDDDMNLLD IFIEMEKRVI LGEGKLDILK RVCAQINKSL LKIINDYEEF 250 260 270 280 290 300 SKERSSSLEG SPDEFSNGEE LCGVMTISDS PREQDSESQT LDKVYQMKSK PRGYCLIINN 310 320 330 340 350 360 HNFAKAREKV PKLHSIRDRN GTHLDAGALT TTFEELHFEI KPHDDCTVEQ IYEILKIYQL 370 380 390 400 410 420 MDHSNMDCFI CCILSHGDKG IIYGTDGQEA PIYELTSQFT GLKCPSLAGK PKVFFIQACQ 430 440 450 460 470 480 GDNYQKGIPV ETDSEEQPYL EMDLSSPQTR YIPDEADFLL GMATVNNCVS YRNPAEGTWY 490 500 510 520 530 IQSLCQSLRE RCPRGDDILT ILTEVNYEVS NKDDKKNMGK QMPQPTFTLR KKLVFPSD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"FLAME-1, a novel FADD-like anti-apoptotic molecule that regulates Fas/TNFR1-induced apoptosis." Srinivasula S.M., Ahmad M., Ottilie S., Bullrich F., Banks S., Wang Y., Fernandes-Alnemri T., Croce C.M., Litwack G., Tomaselli K.J., Armstrong R.C., Alnemri E.S. J. Biol. Chem. 272:18542-18545(1997) [PubMed] [Europe PMC] [Abstract] 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]	"An unappreciated role for RNA surveillance." Hillman R.T., Green R.E., Brenner S.E. Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[20]	"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, MASS SPECTROMETRY.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]	"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.
[26]	"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).
[27]	"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.
[28]	"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.
[29]	"Association of a common variant of the CASP8 gene with reduced risk of breast cancer." MacPherson G., Healey C.S., Teare M.D., Balasubramanian S.P., Reed M.W.R., Pharoah P.D., Ponder B.A.J., Meuth M., Bhattacharyya N.P., Cox A. J. Natl. Cancer Inst. 96:1866-1869(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HIS-285, PROTECTION AGAINST BREAST CANCER.
[30]	"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.
[31]	Erratum 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. 39:688-688(2007)
[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.
+	Additional computationally mapped references.

Web resources

CASP8base

CASP8 mutation db

GeneReviews

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00000149.
IPI00073318.
IPI00220721.
IPI00220722.
IPI00220723.
IPI00220724.
IPI00220725.
IPI00220726.
IPI00305242.

RefSeq

NP_001073593.1. NM_001080124.1.
NP_001073594.1. NM_001080125.1.
NP_001219.2. NM_001228.4.
NP_203519.1. NM_033355.3.
NP_203520.1. NM_033356.3.
NP_203522.1. NM_033358.3.

UniGene

Hs.599762.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q14790.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-30915N.

IntAct

Q14790. 49 interactions.

MINT

MINT-91645.

Protein family/group databases

MEROPS

C14.009.

PTM databases

PhosphoSite

Q14790.

Polymorphism databases

DMDM

2493531.

Proteomic databases

PaxDb

Q14790.

PRIDE

Q14790.

Protocols and materials databases

DNASU

841.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000264274; ENSP00000264274; ENSG00000064012.
ENST00000264275; ENSP00000264275; ENSG00000064012.
ENST00000323492; ENSP00000325722; ENSG00000064012.
ENST00000358485; ENSP00000351273; ENSG00000064012.
ENST00000392258; ENSP00000376087; ENSG00000064012.
ENST00000392259; ENSP00000376088; ENSG00000064012.
ENST00000392263; ENSP00000376091; ENSG00000064012.
ENST00000392266; ENSP00000376094; ENSG00000064012.
ENST00000432109; ENSP00000412523; ENSG00000064012.

GeneID

841.

KEGG

hsa:841.

UCSC

uc002uxo.1. human.
uc002uxp.1. human.
uc002uxq.1. human.
uc002uxr.1. human.
uc002uxt.1. human.
uc002uxv.1. human.
uc010fte.1. human.
uc010ftf.2. human.

Organism-specific databases

CTD

841.

GeneCards

GC02P202062.

HGNC

HGNC:1509. CASP8.

HPA

CAB002047.
HPA001302.
HPA005688.

MIM

211980. phenotype.
601763. gene.
607271. phenotype.

neXtProt

NX_Q14790.

Orphanet

275517. Autoimmune lymphoproliferative syndrome with recurrent infections.

PharmGKB

PA26092.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG303276.

HOVERGEN

HBG050803.

InParanoid

Q14790.

KO

K04398.

OMA

RVMLFQI.

Enzyme and pathway databases

BRENDA

3.4.22.61. 2681.

Pathway_Interaction_DB

caspase_pathway. Caspase cascade in apoptosis.
ceramidepathway. Ceramide signaling pathway.
ar_pathway. Coregulation of Androgen receptor activity.
faspathway. FAS signaling pathway (CD95).
hivnefpathway. HIV-1 Nef: Negative effector of Fas and TNF-alpha.
avb3_integrin_pathway. Integrins in angiogenesis.
tnfpathway. TNF receptor signaling pathway.
trail_pathway. TRAIL signaling pathway.

Reactome

REACT_578. Apoptosis.
REACT_6900. Immune System.

SignaLink

Q14790.

Gene expression databases

ArrayExpress

Q14790.

Bgee

Q14790.

Genevestigator

Q14790.

GermOnline

ENSG00000064012. Homo sapiens.

Family and domain databases

Gene3D

1.10.533.10. 2 hits.

InterPro

IPR011029. DEATH-like_dom.
IPR001875. DED.
IPR011600. Pept_C14_cat.
IPR001309. Pept_C14_ICE_p20.
IPR016129. Pept_C14_ICE_p20_AS.
IPR002138. Pept_C14_p10.
IPR002398. Pept_C14_p45.
IPR015917. Pept_C14_p45_core.
[Graphical view]

PANTHER

PTHR10454. PTHR10454. 1 hit.

Pfam

PF01335. DED. 2 hits.
PF00656. Peptidase_C14. 1 hit.
[Graphical view]

PRINTS

PR00376. IL1BCENZYME.

SMART

SM00115. CASc. 1 hit.
SM00031. DED. 2 hits.
[Graphical view]

SUPFAM

SSF47986. DEATH_like. 2 hits.

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.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q14790.

ChEMBL

CHEMBL3776.

ChiTaRS

CASP8. human.

EvolutionaryTrace

Q14790.

GenomeRNAi

841.

NextBio

3510.

PMAP-CutDB

Q14790.

SOURCE

Search...

Entry information

Entry name

CASP8_HUMAN

Accession

Primary (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 history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	May 29, 2013
This is version 167 of the entry and version 1 of the sequence. [Complete history]

Entry status

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.