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CASP8 and FADD-like apoptosis regulator (Caspase homolog) (CASH) (Caspase-eight-related protein) (Casper) (Caspase-like apoptosis regulatory protein) (CLARP) (Cellular FLICE-like inhibitory protein) (c-FLIP) (FADD-like antiapoptotic molecule 1) (FLAME-1) (Inhibitor of FLICE) (I-FLICE) (MACH-related inducer of toxicity) (MRIT) (Usurpin) [Cleaved into: CASP8 and FADD-like apoptosis regulator subunit p43; CASP8 and FADD-like apoptosis regulator subunit p12]

 CFLAR_HUMAN             Reviewed;         480 AA.
O15519; B4DJE0; B7Z9F9; O14673; O14674; O14675; O15137; O15138;
O15356; O15510; O43618; O43619; O43620; O60458; O60459; Q53TS6;
Q54AF1; Q96TE4; Q9UEW1;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
22-NOV-2017, entry version 183.
RecName: Full=CASP8 and FADD-like apoptosis regulator;
AltName: Full=Caspase homolog;
Short=CASH;
AltName: Full=Caspase-eight-related protein;
Short=Casper;
AltName: Full=Caspase-like apoptosis regulatory protein;
Short=CLARP;
AltName: Full=Cellular FLICE-like inhibitory protein;
Short=c-FLIP;
AltName: Full=FADD-like antiapoptotic molecule 1;
Short=FLAME-1;
AltName: Full=Inhibitor of FLICE;
Short=I-FLICE;
AltName: Full=MACH-related inducer of toxicity;
Short=MRIT;
AltName: Full=Usurpin;
Contains:
RecName: Full=CASP8 and FADD-like apoptosis regulator subunit p43;
Contains:
RecName: Full=CASP8 and FADD-like apoptosis regulator subunit p12;
Flags: Precursor;
Name=CFLAR; Synonyms=CASH, CASP8AP1, CLARP, MRIT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 13 AND 14), AND MUTAGENESIS OF
TYR-360.
TISSUE=Embryonic kidney, and Umbilical vein endothelial cell;
PubMed=9208847; DOI=10.1016/S1074-7613(00)80450-1;
Shu H.-B., Halpin D.R., Goeddel D.V.;
"Casper is a FADD- and caspase-related inducer of apoptosis.";
Immunity 6:751-763(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
PubMed=9326610; DOI=10.1073/pnas.94.21.11333;
Han D.K.M., Chaudhary P.M., Wright M.E., Friedman C., Trask B.J.,
Riedel R.T., Baskin D.G., Schwartz S.M., Hood L.;
"MRIT, a novel death-effector domain-containing protein, interacts
with caspases and BclXL and initiates cell death.";
Proc. Natl. Acad. Sci. U.S.A. 94:11333-11338(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Peripheral blood lymphocyte;
PubMed=9217161; DOI=10.1038/40657;
Irmler M., Thome M., Hahne M., Schneider P., Hofmann K., Steiner V.,
Bodmer J.-L., Schroeter M., Burns K., Mattmann C., Rimoldi D.,
French L.E., Tschopp J.;
"Inhibition of death receptor signals by cellular FLIP.";
Nature 388:190-195(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 8; 9 AND 10), AND MUTAGENESIS
OF ASP-376.
TISSUE=T-cell;
PubMed=9228018; DOI=10.1074/jbc.272.30.18542;
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.;
"FLAME-1, a novel FADD-like anti-apoptotic molecule that regulates
Fas/TNFR1-induced apoptosis.";
J. Biol. Chem. 272:18542-18545(1997).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Umbilical vein endothelial cell;
PubMed=9211860; DOI=10.1074/jbc.272.28.17255;
Hu S., Vincenz C., Ni J., Gentz R., Dixit V.M.;
"I-FLICE, a novel inhibitor of tumor necrosis factor receptor-1- and
CD-95-induced apoptosis.";
J. Biol. Chem. 272:17255-17257(1997).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5; 6 AND 7).
Hu S., Dixit V.M.;
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Skin fibroblast;
PubMed=9289491; DOI=10.1074/jbc.272.32.19641;
Goltsev Y.V., Kovalenko A.V., Arnold E., Varfolomeev E.E.,
Brodianskii V.M., Wallach D.;
"CASH, a novel caspase homologue with death effector domains.";
J. Biol. Chem. 272:19641-19644(1997).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Colon carcinoma;
PubMed=9380701; DOI=10.1073/pnas.94.20.10717;
Inohara N., Koseki T., Hu Y., Chen S., Nunez G.;
"CLARP, a death effector domain-containing protein interacts with
caspase-8 and regulates apoptosis.";
Proc. Natl. Acad. Sci. U.S.A. 94:10717-10722(1997).
[9]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 11 AND 12).
TISSUE=Kidney;
PubMed=10200473; DOI=10.1038/sj.cdd.4400370;
Rasper D.M., Vaillancourt J.P., Hadano S., Houtzager V.M., Seiden I.,
Keen S.L.C., Tawa P., Xanthoudakis S., Nasir J., Martindale D.,
Koop B.F., Peterson E.P., Thornberry N.A., Huang J., MacPherson D.P.,
Black S.C., Hornung F., Lenardo M.J., Hayden M.R., Roy S.,
Nicholson D.W.;
"Cell death attenuation by 'Usurpin', a mammalian DED-caspase
homologue that precludes caspase-8 recruitment and activation by the
CD-95 (Fas, APO-1) receptor complex.";
Cell Death Differ. 5:271-288(1998).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11161814; DOI=10.1006/geno.2000.6392;
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.;
"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.";
Genomics 71:200-213(2001).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 15).
TISSUE=Cerebellum, Corpus callosum, and Subthalamic nucleus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
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.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[15]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[16]
FUNCTION.
PubMed=9880531; DOI=10.1074/jbc.274.3.1541;
Scaffidi C., Schmitz I., Krammer P.H., Peter M.E.;
"The role of c-FLIP in modulation of CD95-induced apoptosis.";
J. Biol. Chem. 274:1541-1548(1999).
[17]
INDUCTION.
PubMed=10227994;
Algeciras-Schimnich A., Griffith T.S., Lynch D.H., Paya C.V.;
"Cell cycle-dependent regulation of FLIP levels and susceptibility to
Fas-mediated apoptosis.";
J. Immunol. 162:5205-5211(1999).
[18]
INTERACTION WITH HBV PROTEIN X.
PubMed=12727877; DOI=10.1093/emboj/cdg210;
Kim K.H., Seong B.L.;
"Pro-apoptotic function of HBV X protein is mediated by interaction
with c-FLIP and enhancement of death-inducing signal.";
EMBO J. 22:2104-2116(2003).
[19]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
-!- FUNCTION: Apoptosis regulator protein which may function as a
crucial link between cell survival and cell death pathways in
mammalian cells. Acts as an inhibitor of TNFRSF6 mediated
apoptosis. A proteolytic fragment (p43) is likely retained in the
death-inducing signaling complex (DISC) thereby blocking further
recruitment and processing of caspase-8 at the complex. Full
length and shorter isoforms have been shown either to induce
apoptosis or to reduce TNFRSF-triggered apoptosis. Lacks enzymatic
(caspase) activity. {ECO:0000269|PubMed:9880531}.
-!- SUBUNIT: TNFRSF6 stimulation triggers recruitment to the death-
inducing signaling complex (DISC) formed by TNFRSF6, FADD and
caspase-8. A proteolytic fragment (p43) stays associated with the
DISC. Also interacts with caspase-10, caspase-3, TRAF1, TRAF2 and
Bcl-X(L) (in vitro). Interacts with HBV protein X.
{ECO:0000269|PubMed:12727877}.
-!- INTERACTION:
Q92851:CASP10; NbExp=3; IntAct=EBI-514941, EBI-495095;
Q92851-4:CASP10; NbExp=3; IntAct=EBI-4478097, EBI-6621134;
Q14790:CASP8; NbExp=9; IntAct=EBI-514941, EBI-78060;
Q14790-2:CASP8; NbExp=3; IntAct=EBI-4567563, EBI-15777741;
Q02750:MAP2K1; NbExp=3; IntAct=EBI-4567563, EBI-492564;
O14733:MAP2K7; NbExp=2; IntAct=EBI-4567563, EBI-492605;
Q13077:TRAF1; NbExp=5; IntAct=EBI-514941, EBI-359224;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=15;
Name=1; Synonyms=FLIP-L, CLARP1, MRIT alpha-1, CASH alpha, I-FLICE
1, FLAME-1 gamma, Usurpin alpha;
IsoId=O15519-1; Sequence=Displayed;
Name=2; Synonyms=FLIP-S, CLARP2, MRIT beta-1, CASH beta;
IsoId=O15519-2; Sequence=VSP_000828, VSP_000829;
Name=3; Synonyms=MRIT alpha-2;
IsoId=O15519-3; Sequence=VSP_000824, VSP_000838;
Name=4; Synonyms=I-FLICE 2;
IsoId=O15519-4; Sequence=VSP_000825;
Name=5; Synonyms=I-FLICE 3;
IsoId=O15519-5; Sequence=VSP_000840;
Name=6; Synonyms=I-FLICE 4;
IsoId=O15519-6; Sequence=VSP_000826, VSP_000841;
Name=7; Synonyms=I-FLICE 5;
IsoId=O15519-7; Sequence=VSP_000824, VSP_000827, VSP_000838;
Name=8; Synonyms=FLAME-1 alpha;
IsoId=O15519-8; Sequence=VSP_000830;
Name=9; Synonyms=FLAME-1 beta;
IsoId=O15519-9; Sequence=VSP_000830, VSP_000836, VSP_000837;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=10; Synonyms=FLAME-1 delta;
IsoId=O15519-10; Sequence=VSP_000834, VSP_000835;
Name=11; Synonyms=Usurpin beta;
IsoId=O15519-11; Sequence=VSP_000838;
Name=12; Synonyms=Usurpin gamma;
IsoId=O15519-12; Sequence=VSP_000832, VSP_000833;
Name=13;
IsoId=O15519-13; Sequence=VSP_000831;
Name=14;
IsoId=O15519-14; Sequence=VSP_000839;
Name=15;
IsoId=O15519-15; Sequence=VSP_000824;
-!- TISSUE SPECIFICITY: Widely expressed. Higher expression in
skeletal muscle, pancreas, heart, kidney, placenta, and peripheral
blood leukocytes. Also detected in diverse cell lines. Isoform 8
is predominantly expressed in testis and skeletal muscle.
-!- INDUCTION: Repressed by IL2/interleukin-2 after TCR stimulation,
during progression to the S phase of the cell cycle.
{ECO:0000269|PubMed:10227994}.
-!- DOMAIN: The caspase domain lacks the active site residues involved
in catalysis.
-!- PTM: Proteolytically processed; probably by caspase-8. Processing
likely occurs at the DISC and generates subunit p43 and p12.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CFLARID40065ch2q33.html";
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EMBL; AF010127; AAB64110.1; -; mRNA.
EMBL; U85059; AAB82648.1; -; mRNA.
EMBL; U97074; AAC51622.1; -; mRNA.
EMBL; U97075; AAC51623.1; -; mRNA.
EMBL; AF009616; AAB70909.1; -; mRNA.
EMBL; AF009617; AAB70910.1; -; mRNA.
EMBL; AF009618; AAB70911.1; -; mRNA.
EMBL; AF009619; AAB70912.1; -; mRNA.
EMBL; AF041458; AAB99790.1; -; mRNA.
EMBL; AF041459; AAB99791.1; -; mRNA.
EMBL; AF041462; AAB99794.1; -; mRNA.
EMBL; AF041461; AAB99793.1; -; mRNA.
EMBL; AF041460; AAB99792.1; -; mRNA.
EMBL; Y14039; CAA74366.1; -; mRNA.
EMBL; Y14040; CAA74367.1; -; mRNA.
EMBL; AF005774; AAC15825.1; -; mRNA.
EMBL; AF005775; AAC15826.1; -; mRNA.
EMBL; AF015450; AAC16439.1; -; mRNA.
EMBL; AF015451; AAC16440.1; -; mRNA.
EMBL; AF015452; AAC16441.1; -; mRNA.
EMBL; AB038972; BAB32551.1; -; Genomic_DNA.
EMBL; AB038972; BAB32552.1; -; Genomic_DNA.
EMBL; BT006751; AAP35397.1; -; mRNA.
EMBL; AK289913; BAF82602.1; -; mRNA.
EMBL; AK296036; BAG58802.1; -; mRNA.
EMBL; AK315208; BAG37645.1; -; mRNA.
EMBL; AK315924; BAH14295.1; -; mRNA.
EMBL; AC007283; AAY24290.1; -; Genomic_DNA.
EMBL; CH471063; EAW70237.1; -; Genomic_DNA.
EMBL; CH471063; EAW70244.1; -; Genomic_DNA.
EMBL; BC001602; AAH01602.1; -; mRNA.
CCDS; CCDS2337.1; -. [O15519-1]
CCDS; CCDS46487.1; -. [O15519-2]
CCDS; CCDS56157.1; -. [O15519-8]
CCDS; CCDS56158.1; -. [O15519-15]
CCDS; CCDS59436.1; -. [O15519-3]
CCDS; CCDS77505.1; -. [O15519-11]
RefSeq; NP_001120655.1; NM_001127183.2. [O15519-1]
RefSeq; NP_001120656.1; NM_001127184.2. [O15519-2]
RefSeq; NP_001189444.1; NM_001202515.1. [O15519-4]
RefSeq; NP_001189445.1; NM_001202516.1. [O15519-8]
RefSeq; NP_001189446.1; NM_001202517.1. [O15519-15]
RefSeq; NP_001189447.1; NM_001202518.1. [O15519-3]
RefSeq; NP_001189448.1; NM_001202519.1. [O15519-3]
RefSeq; NP_001294971.1; NM_001308042.1. [O15519-11]
RefSeq; NP_003870.4; NM_003879.5. [O15519-1]
RefSeq; XP_016860679.1; XM_017005190.1. [O15519-1]
RefSeq; XP_016860680.1; XM_017005191.1. [O15519-1]
RefSeq; XP_016860681.1; XM_017005192.1.
RefSeq; XP_016860682.1; XM_017005193.1. [O15519-11]
RefSeq; XP_016860683.1; XM_017005194.1.
RefSeq; XP_016860684.1; XM_017005195.1. [O15519-15]
RefSeq; XP_016860685.1; XM_017005196.1. [O15519-4]
RefSeq; XP_016860686.1; XM_017005197.1.
RefSeq; XP_016860687.1; XM_017005198.1.
UniGene; Hs.390736; -.
UniGene; Hs.731912; -.
PDB; 2N5R; NMR; -; A=62-73.
PDB; 3H11; X-ray; 1.90 A; A=209-480.
PDB; 3H13; X-ray; 2.20 A; A=209-480.
PDBsum; 2N5R; -.
PDBsum; 3H11; -.
PDBsum; 3H13; -.
ProteinModelPortal; O15519; -.
SMR; O15519; -.
BioGrid; 114364; 40.
CORUM; O15519; -.
DIP; DIP-27629N; -.
IntAct; O15519; 30.
MINT; MINT-1529273; -.
STRING; 9606.ENSP00000312455; -.
ChEMBL; CHEMBL1955713; -.
MEROPS; C14.971; -.
iPTMnet; O15519; -.
PhosphoSitePlus; O15519; -.
BioMuta; CFLAR; -.
EPD; O15519; -.
MaxQB; O15519; -.
PaxDb; O15519; -.
PeptideAtlas; O15519; -.
PRIDE; O15519; -.
DNASU; 8837; -.
Ensembl; ENST00000309955; ENSP00000312455; ENSG00000003402. [O15519-1]
Ensembl; ENST00000341222; ENSP00000339335; ENSG00000003402. [O15519-2]
Ensembl; ENST00000341582; ENSP00000345807; ENSG00000003402. [O15519-8]
Ensembl; ENST00000342795; ENSP00000342809; ENSG00000003402. [O15519-12]
Ensembl; ENST00000423241; ENSP00000399420; ENSG00000003402. [O15519-1]
Ensembl; ENST00000440180; ENSP00000406775; ENSG00000003402. [O15519-2]
Ensembl; ENST00000443227; ENSP00000413270; ENSG00000003402. [O15519-15]
Ensembl; ENST00000457277; ENSP00000411535; ENSG00000003402. [O15519-11]
Ensembl; ENST00000479953; ENSP00000471805; ENSG00000003402. [O15519-3]
GeneID; 8837; -.
KEGG; hsa:8837; -.
UCSC; uc002uwz.4; human. [O15519-1]
CTD; 8837; -.
DisGeNET; 8837; -.
EuPathDB; HostDB:ENSG00000003402.19; -.
GeneCards; CFLAR; -.
HGNC; HGNC:1876; CFLAR.
HPA; CAB022157; -.
HPA; CAB025216; -.
HPA; HPA019044; -.
MIM; 603599; gene.
neXtProt; NX_O15519; -.
OpenTargets; ENSG00000003402; -.
PharmGKB; PA26425; -.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00530000064199; -.
HOGENOM; HOG000069972; -.
HOVERGEN; HBG050918; -.
InParanoid; O15519; -.
KO; K04724; -.
OMA; YDWNSRV; -.
OrthoDB; EOG091G05YD; -.
PhylomeDB; O15519; -.
TreeFam; TF352765; -.
Reactome; R-HSA-3371378; Regulation by c-FLIP.
Reactome; R-HSA-5213460; RIPK1-mediated regulated necrosis.
Reactome; R-HSA-5218900; CASP8 activity is inhibited.
Reactome; R-HSA-69416; Dimerization of procaspase-8.
Reactome; R-HSA-75158; TRAIL signaling.
SignaLink; O15519; -.
SIGNOR; O15519; -.
ChiTaRS; CFLAR; human.
EvolutionaryTrace; O15519; -.
GeneWiki; CFLAR; -.
GenomeRNAi; 8837; -.
PRO; PR:O15519; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000003402; -.
ExpressionAtlas; O15519; baseline and differential.
Genevisible; O15519; HS.
GO; GO:0031265; C:CD95 death-inducing signaling complex; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0031264; C:death-inducing signaling complex; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0097342; C:ripoptosome; IDA:UniProtKB.
GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IBA:GO_Central.
GO; GO:0005123; F:death receptor binding; IEA:Ensembl.
GO; GO:0008047; F:enzyme activator activity; IDA:UniProtKB.
GO; GO:0002020; F:protease binding; IPI:UniProtKB.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl.
GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
GO; GO:0071732; P:cellular response to nitric oxide; IEA:Ensembl.
GO; GO:0097194; P:execution phase of apoptosis; IBA:GO_Central.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:ProtInc.
GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IEA:Ensembl.
GO; GO:1903845; P:negative regulation of cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IDA:MGI.
GO; GO:1903944; P:negative regulation of hepatocyte apoptotic process; IEA:Ensembl.
GO; GO:1901740; P:negative regulation of myoblast fusion; ISS:BHF-UCL.
GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; IEA:Ensembl.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:1903055; P:positive regulation of extracellular matrix organization; IEA:Ensembl.
GO; GO:0072126; P:positive regulation of glomerular mesangial cell proliferation; IEA:Ensembl.
GO; GO:2000347; P:positive regulation of hepatocyte proliferation; IEA:Ensembl.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEP:UniProtKB.
GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:BHF-UCL.
GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; TAS:Reactome.
GO; GO:0060544; P:regulation of necroptotic process; IDA:UniProtKB.
GO; GO:0014842; P:regulation of skeletal muscle satellite cell proliferation; ISS:BHF-UCL.
GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
GO; GO:0014732; P:skeletal muscle atrophy; ISS:BHF-UCL.
GO; GO:0007519; P:skeletal muscle tissue development; ISS:BHF-UCL.
GO; GO:0043403; P:skeletal muscle tissue regeneration; ISS:BHF-UCL.
GO; GO:0014866; P:skeletal myofibril assembly; ISS:BHF-UCL.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd00032; CASc; 1.
InterPro; IPR029030; Caspase-like_dom_sf.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR001875; DED_dom.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
Pfam; PF01335; DED; 2.
SMART; SM00115; CASc; 1.
SMART; SM00031; DED; 2.
SUPFAM; SSF47986; SSF47986; 2.
SUPFAM; SSF52129; SSF52129; 1.
PROSITE; PS50208; CASPASE_P20; 1.
PROSITE; PS50168; DED; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Complete proteome;
Host-virus interaction; Polymorphism; Reference proteome; Repeat.
CHAIN 1 376 CASP8 and FADD-like apoptosis regulator
subunit p43.
/FTId=PRO_0000004678.
CHAIN 377 480 CASP8 and FADD-like apoptosis regulator
subunit p12. {ECO:0000255}.
/FTId=PRO_0000004679.
DOMAIN 1 73 DED 1. {ECO:0000255|PROSITE-
ProRule:PRU00065}.
DOMAIN 92 170 DED 2. {ECO:0000255|PROSITE-
ProRule:PRU00065}.
REGION 1 435 Not proteolytically processed and
involved in apoptosis inhibition.
REGION 1 305 Interaction with caspase-8 propeptide.
REGION 1 227 Interaction with FADD.
REGION 1 195 Interaction with caspase-8.
REGION 192 480 Interaction with TRAF1 and TRAF2.
REGION 192 435 Interaction with caspase-3.
REGION 217 480 Interaction with caspase-8 subunits p18
and p10.
REGION 263 358 Caspase.
REGION 370 480 Interaction with caspase-8.
VAR_SEQ 1 245 Missing (in isoform 4).
{ECO:0000303|Ref.6}.
/FTId=VSP_000825.
VAR_SEQ 1 96 Missing (in isoform 3, isoform 7 and
isoform 15).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:9326610,
ECO:0000303|Ref.6}.
/FTId=VSP_000824.
VAR_SEQ 2 30 SAEVIHQVEEALDTDEKEMLLFLCRDVAI -> LERPPVCS
KV (in isoform 6). {ECO:0000303|Ref.6}.
/FTId=VSP_000826.
VAR_SEQ 203 480 Missing (in isoform 13).
{ECO:0000303|PubMed:9208847}.
/FTId=VSP_000831.
VAR_SEQ 203 237 Missing (in isoform 8 and isoform 9).
{ECO:0000303|PubMed:9228018}.
/FTId=VSP_000830.
VAR_SEQ 203 221 LHNGRSKEQRLKEQLGAQQ -> MITPYAHCPDLKILGNCS
M (in isoform 2).
{ECO:0000303|PubMed:9217161,
ECO:0000303|PubMed:9289491,
ECO:0000303|PubMed:9326610,
ECO:0000303|PubMed:9380701}.
/FTId=VSP_000828.
VAR_SEQ 203 221 LHNGRSKEQRLKEQLGAQQ -> E (in isoform 7).
{ECO:0000303|Ref.6}.
/FTId=VSP_000827.
VAR_SEQ 222 480 Missing (in isoform 2).
{ECO:0000303|PubMed:9217161,
ECO:0000303|PubMed:9289491,
ECO:0000303|PubMed:9326610,
ECO:0000303|PubMed:9380701}.
/FTId=VSP_000829.
VAR_SEQ 265 292 ELLRDTFTSLGYEVQKFLHLSMHGISQI -> GWSAMAQSQ
LTAISTSQVQAILLPQPPE (in isoform 12).
{ECO:0000303|PubMed:10200473}.
/FTId=VSP_000832.
VAR_SEQ 266 300 LLRDTFTSLGYEVQKFLHLSMHGISQILGQFACMP -> NA
HSWIFTLNSMATCMIGTAEFLPRRNIMFGCSTL (in
isoform 10).
{ECO:0000303|PubMed:9228018}.
/FTId=VSP_000834.
VAR_SEQ 267 305 LRDTFTSLGYEVQKFLHLSMHGISQILGQFACMPEHRDY
-> CGVRGPAGGQQPLGGGWASDEECGIQGSEARAVHSSPR
S (in isoform 9).
{ECO:0000303|PubMed:9228018}.
/FTId=VSP_000836.
VAR_SEQ 293 480 Missing (in isoform 12).
{ECO:0000303|PubMed:10200473}.
/FTId=VSP_000833.
VAR_SEQ 301 480 Missing (in isoform 10).
{ECO:0000303|PubMed:9228018}.
/FTId=VSP_000835.
VAR_SEQ 306 480 Missing (in isoform 9).
{ECO:0000303|PubMed:9228018}.
/FTId=VSP_000837.
VAR_SEQ 436 480 KRPLLDLHIELNGYMYDWNSRVSAKEKYYVWLQHTLRKKLI
LSYT -> GTIPGSGITESKDMHFSSLGCILLDVL (in
isoform 11, isoform 7 and isoform 3).
{ECO:0000303|PubMed:10200473,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:9326610,
ECO:0000303|Ref.6}.
/FTId=VSP_000838.
VAR_SEQ 436 480 Missing (in isoform 14).
{ECO:0000303|PubMed:9208847}.
/FTId=VSP_000839.
VAR_SEQ 449 480 YMYDWNSRVSAKEKYYVWLQHTLRKKLILSYT -> L (in
isoform 5). {ECO:0000303|Ref.6}.
/FTId=VSP_000840.
VAR_SEQ 453 480 WNSRVSAKEKYYVWLQHTLRKKLILSYT -> SLEHTGGRY
(in isoform 6). {ECO:0000303|Ref.6}.
/FTId=VSP_000841.
VARIANT 203 203 L -> I (in dbSNP:rs13424615).
/FTId=VAR_048619.
MUTAGEN 360 360 Y->F: Decreases apoptosis-inducing
activity. Reduces interaction with
caspase-3 and proteolytic processing.
{ECO:0000269|PubMed:9208847}.
MUTAGEN 376 376 D->N,A: Abolishes proteolytic processing.
{ECO:0000269|PubMed:9228018}.
CONFLICT 130 132 SFL -> ISW (in Ref. 8; AAC15825/
AAC15826). {ECO:0000305}.
CONFLICT 343 343 D -> E (in Ref. 8; AAC15825).
{ECO:0000305}.
CONFLICT 364 364 E -> D (in Ref. 6; AAB99794).
{ECO:0000305}.
CONFLICT 366 368 QLE -> PAG (in Ref. 8; AAC15825).
{ECO:0000305}.
CONFLICT 369 369 D -> N (in Ref. 7; CAA74366).
{ECO:0000305}.
CONFLICT 372 372 L -> F (in Ref. 6; AAB99793).
{ECO:0000305}.
CONFLICT 373 374 LE -> WR (in Ref. 8; AAC15825).
{ECO:0000305}.
HELIX 67 71 {ECO:0000244|PDB:2N5R}.
STRAND 239 241 {ECO:0000244|PDB:3H11}.
STRAND 249 260 {ECO:0000244|PDB:3H11}.
HELIX 266 274 {ECO:0000244|PDB:3H11}.
STRAND 276 283 {ECO:0000244|PDB:3H11}.
HELIX 286 297 {ECO:0000244|PDB:3H11}.
HELIX 300 304 {ECO:0000244|PDB:3H11}.
STRAND 306 317 {ECO:0000244|PDB:3H11}.
HELIX 333 340 {ECO:0000244|PDB:3H11}.
TURN 342 344 {ECO:0000244|PDB:3H11}.
HELIX 346 348 {ECO:0000244|PDB:3H11}.
STRAND 353 361 {ECO:0000244|PDB:3H11}.
STRAND 400 409 {ECO:0000244|PDB:3H11}.
HELIX 410 412 {ECO:0000244|PDB:3H11}.
HELIX 422 433 {ECO:0000244|PDB:3H11}.
HELIX 439 454 {ECO:0000244|PDB:3H11}.
HELIX 459 461 {ECO:0000244|PDB:3H11}.
STRAND 463 469 {ECO:0000244|PDB:3H11}.
SEQUENCE 480 AA; 55344 MW; 8C6D7E92AE1EB672 CRC64;
MSAEVIHQVE EALDTDEKEM LLFLCRDVAI DVVPPNVRDL LDILRERGKL SVGDLAELLY
RVRRFDLLKR ILKMDRKAVE THLLRNPHLV SDYRVLMAEI GEDLDKSDVS SLIFLMKDYM
GRGKISKEKS FLDLVVELEK LNLVAPDQLD LLEKCLKNIH RIDLKTKIQK YKQSVQGAGT
SYRNVLQAAI QKSLKDPSNN FRLHNGRSKE QRLKEQLGAQ QEPVKKSIQE SEAFLPQSIP
EERYKMKSKP LGICLIIDCI GNETELLRDT FTSLGYEVQK FLHLSMHGIS QILGQFACMP
EHRDYDSFVC VLVSRGGSQS VYGVDQTHSG LPLHHIRRMF MGDSCPYLAG KPKMFFIQNY
VVSEGQLEDS SLLEVDGPAM KNVEFKAQKR GLCTVHREAD FFWSLCTADM SLLEQSHSSP
SLYLQCLSQK LRQERKRPLL DLHIELNGYM YDWNSRVSAK EKYYVWLQHT LRKKLILSYT


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