[1]
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NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF CYS-258, AND 3D-STRUCTURE MODELING.
TISSUE=Placenta;
PubMed=7743998 [NCBI, ExPASy, EBI, Israel, Japan]
Faucheu C.,
Diu A.,
Chan A.W.E.,
Blanchet A.-M.,
Miossec C.,
Herve F.,
Collard-Dutilleul V.,
Gu Y.,
Aldape R.A.,
Lippke J.A.,
Rocher C.,
Su M.S.-S.,
Livingston D.J.,
Hercend T.,
Lalanne J.-L.;
"A novel human protease similar to the interleukin-1 beta converting enzyme induces apoptosis in transfected cells.";
EMBO J. 14:1914-1922(1995).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1074/jbc.270.26.15870; PubMed=7797592 [NCBI, ExPASy, EBI, Israel, Japan]
Munday N.A.,
Vaillancourt J.P.,
Ali A.,
Casano F.J.,
Miller D.K.,
Molineaux S.M.,
Yamin T.-T.,
Yu V.L.,
Nicholson D.W.;
"Molecular cloning and pro-apoptotic activity of ICErelII and ICErelIII, members of the ICE/CED-3 family of cysteine proteases.";
J. Biol. Chem. 270:15870-15876(1995).
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[3]
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NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
TISSUE=Thymus;
DOI=10.1074/jbc.270.25.15250; PubMed=7797510 [NCBI, ExPASy, EBI, Israel, Japan]
Kamens J.,
Paskind M.,
Hugunin M.,
Talanian R.V.,
Allen H.,
Banach D.,
Bump N.J.,
Hackett M.C.,
Johnston C.G.,
Li P.,
Mankovich J.A.,
Terranova M.,
Ghayur T.;
"Identification and characterization of ICH-2, a novel member of the interleukin-1 beta-converting enzyme family of cysteine proteases.";
J. Biol. Chem. 270:15250-15256(1995).
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[4]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[5]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N.,
Zhou C.,
Villen J.,
Beausoleil S.A.,
Bakalarski C.E.,
Elledge S.J.,
Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
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- FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves caspase-1.
- CATALYTIC ACTIVITY: Strict requirement for Asp at the P1 position. It has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|- but also cleaves at Asp-Glu-Val-Asp-|-.
- SUBUNIT: Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a small and a large subunit (By similarity).
- INTERACTION:
P24941:CDK2; NbExp=1; IntAct=EBI-1057327, EBI-375096;
Q9NSA3:CTNNBIP1; NbExp=1; IntAct=EBI-1057327, EBI-747082;
P41091:EIF2S3; NbExp=1; IntAct=EBI-1057327, EBI-1054228;
P06396:GSN; NbExp=1; IntAct=EBI-1057327, EBI-351506;
Q86Y56:HEATR2; NbExp=1; IntAct=EBI-1057327, EBI-719966;
Q9Y241:HIGD1A; NbExp=1; IntAct=EBI-1057327, EBI-1051940;
O94874:KIAA0776; NbExp=1; IntAct=EBI-1057327, EBI-1048088;
P52701:MSH6; NbExp=1; IntAct=EBI-1057327, EBI-395529;
Q6UB35:MTHFD1L; NbExp=1; IntAct=EBI-1057327, EBI-1046835;
Q8N1F7:NUP93; NbExp=1; IntAct=EBI-1057327, EBI-1042703;
P20618:PSMB1; NbExp=1; IntAct=EBI-1057327, EBI-372273;
Q9H936:SLC25A22; NbExp=1; IntAct=EBI-1057327, EBI-1050588;
Q14683:SMC1A; NbExp=1; IntAct=EBI-1057327, EBI-80690;
Q9UQE7:SMC3; NbExp=1; IntAct=EBI-1057327, EBI-80718;
Q9Y5M8:SRPRB; NbExp=1; IntAct=EBI-1057327, EBI-355393;
Q9Y277:VDAC3; NbExp=1; IntAct=EBI-1057327, EBI-354196;
- TISSUE SPECIFICITY: Widely expressed, with highest levels in spleen and lung. Moderate expression in heart and liver, low expression in skeletal muscle, kidney and testis. Not found in the brain.
- PTM: The two subunits are derived from the precursor sequence by an autocatalytic mechanism or by cleavage by Caspase-8.
- SIMILARITY: Belongs to the peptidase C14A family [view classification].
- SIMILARITY: Contains 1 CARD domain.
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