CAEEL:D3YT61

Species (Taxon ID)	Caenorhabditis elegans. (6239)
Gene Name(s)	No Information Provided.
Protein Name(s)	Protein CED-3, isoform b (ECO:0000313 with EMBL:CBK19388.1)
External Links
UniProt	D3YT61
EMBL	Z81049
RefSeq	NP_001255709.1
UniGene	Cel.19438
ProteinModelPortal	D3YT61
SMR	D3YT61
EnsemblMetazoa	C48D1.2b
GeneID	178272
KEGG	cel:CELE_C48D1.2
CTD	178272
WormBase	C48D1.2b
GeneTree	ENSGT00760000118912
KO	K04489
OrthoDB	EOG7TTQ7K
Proteomes	UP000001940
ExpressionAtlas	D3YT61
GO	GO:0005737 GO:0016020 GO:0048471 GO:0004197 GO:0004175 GO:0006915 GO:0009792 GO:0097194 GO:0012501 GO:0016540 GO:0030163
Gene3D	3.40.50.1460
InterPro	IPR029030 IPR011600 IPR001309 IPR016129 IPR002138 IPR015917
Pfam	PF00656
PRINTS	PR00376
SMART	SM00115
PROSITE	PS01122 PS01121 PS50207 PS50208

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
involved_in	GO:0097194	execution phase of apoptosis	PMID:20223951^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	PMID:20970339^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
	GO:0006508	proteolysis	PMID:8654923^[3]	ECO:0000314			P	Figure 1B shows that CED-3 is a cysteine protease because when the mutant CED or an inhibitor was used, cleavage products were not present.	complete CACAO 9327
involved_in	GO:0030163	protein catabolic process	PMID:10764728^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0030163	protein catabolic process	PMID:9285582^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0030163	protein catabolic process	PMID:8654923^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0030163	protein catabolic process	PMID:8631956^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0016540	protein autoprocessing	PMID:16208361^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:9651369^[8]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0012501	programmed cell death	PMID:17237514^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion	WB:WBVar00090471 WB:WBVar00090693 WB:WBVar00090694 WB:WBVar00090697 WB:WBVar00090699 WB:WBVar00090700 WB:WBVar00090701	P	Seeded From UniProt	complete
involved_in	GO:0009792	embryo development ending in birth or egg hatching	PMID:21502138^[10]	ECO:0000316	genetic interaction evidence used in manual assertion	WB:WBGene00018294	P	Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	PMID:9604928^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	PMID:3955651^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:9651369^[8]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0004197	cysteine-type endopeptidase activity	PMID:9384385^[13]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004197	cysteine-type endopeptidase activity	PMID:20223951^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004197	cysteine-type endopeptidase activity	PMID:10764728^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004197	cysteine-type endopeptidase activity	PMID:9285582^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004197	cysteine-type endopeptidase activity	PMID:8654923^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004197	cysteine-type endopeptidase activity	PMID:8631956^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004175	endopeptidase activity	PMID:16208361^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004197	cysteine-type endopeptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001309 InterPro:IPR002138 InterPro:IPR002398	F	Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001309 InterPro:IPR002138 InterPro:IPR002398	P	Seeded From UniProt	complete
enables	GO:0008234	cysteine-type peptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR015917	F	Seeded From UniProt	complete
enables	GO:0008234	cysteine-type peptidase activity	GO_REF:0000038	ECO:0000323	imported automatically asserted information used in automatic assertion	UniProtKB-KW:KW-0788	F	Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000038	ECO:0000323	imported automatically asserted information used in automatic assertion	UniProtKB-KW:KW-0645	P	Seeded From UniProt	complete
enables	GO:0008233	peptidase activity	GO_REF:0000038	ECO:0000323	imported automatically asserted information used in automatic assertion	UniProtKB-KW:KW-0645	F	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000038	ECO:0000323	imported automatically asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F	Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Nakagawa, A et al. (2010) Caspase-dependent conversion of Dicer ribonuclease into a death-promoting deoxyribonuclease. Science 328 327-34 PubMed GONUTS page
↑ Jaramillo-Lambert, A et al. (2010) Meiotic errors activate checkpoints that improve gamete quality without triggering apoptosis in male germ cells. Curr. Biol. 20 2078-89 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Xue, D et al. (1996) The Caenorhabditis elegans cell-death protein CED-3 is a cysteine protease with substrate specificities similar to those of the human CPP32 protease. Genes Dev. 10 1073-83 PubMed GONUTS page
↑ ^4.0 ^4.1 Chan, SL et al. (2000) The Caenorhabditis elegans sex determination protein FEM-1 is a CED-3 substrate that associates with CED-4 and mediates apoptosis in mammalian cells. J. Biol. Chem. 275 17925-8 PubMed GONUTS page
↑ ^5.0 ^5.1 Chinnaiyan, AM et al. (1997) Role of CED-4 in the activation of CED-3. Nature 388 728-9 PubMed GONUTS page
↑ ^6.0 ^6.1 Hugunin, M et al. (1996) Protease activity of in vitro transcribed and translated Caenorhabditis elegans cell death gene (ced-3) product. J. Biol. Chem. 271 3517-22 PubMed GONUTS page
↑ ^7.0 ^7.1 Yan, N et al. (2005) Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans. Nature 437 831-7 PubMed GONUTS page
↑ ^8.0 ^8.1 Chaudhary, D et al. (1998) The death inhibitory molecules CED-9 and CED-4L use a common mechanism to inhibit the CED-3 death protease. J. Biol. Chem. 273 17708-12 PubMed GONUTS page
↑ Reddien, PW et al. (2007) DPL-1 DP, LIN-35 Rb and EFL-1 E2F act with the MCD-1 zinc-finger protein to promote programmed cell death in Caenorhabditis elegans. Genetics 175 1719-33 PubMed GONUTS page
↑ Erdélyi, P et al. (2011) Shared developmental roles and transcriptional control of autophagy and apoptosis in Caenorhabditis elegans. J. Cell. Sci. 124 1510-8 PubMed GONUTS page
↑ Conradt, B & Horvitz, HR (1998) The C. elegans protein EGL-1 is required for programmed cell death and interacts with the Bcl-2-like protein CED-9. Cell 93 519-29 PubMed GONUTS page
↑ Ellis, HM & Horvitz, HR (1986) Genetic control of programmed cell death in the nematode C. elegans. Cell 44 817-29 PubMed GONUTS page
↑ Xue, D & Horvitz, HR (1997) Caenorhabditis elegans CED-9 protein is a bifunctional cell-death inhibitor. Nature 390 305-8 PubMed GONUTS page

[PMID:20223951-1] 1.0 ^1.1 Nakagawa, A et al. (2010) Caspase-dependent conversion of Dicer ribonuclease into a death-promoting deoxyribonuclease. Science 328 327-34 PubMed GONUTS page

[PMID:20970339-2] Jaramillo-Lambert, A et al. (2010) Meiotic errors activate checkpoints that improve gamete quality without triggering apoptosis in male germ cells. Curr. Biol. 20 2078-89 PubMed GONUTS page

[PMID:8654923-3] 3.0 ^3.1 ^3.2 Xue, D et al. (1996) The Caenorhabditis elegans cell-death protein CED-3 is a cysteine protease with substrate specificities similar to those of the human CPP32 protease. Genes Dev. 10 1073-83 PubMed GONUTS page

[PMID:10764728-4] 4.0 ^4.1 Chan, SL et al. (2000) The Caenorhabditis elegans sex determination protein FEM-1 is a CED-3 substrate that associates with CED-4 and mediates apoptosis in mammalian cells. J. Biol. Chem. 275 17925-8 PubMed GONUTS page

[PMID:9285582-5] 5.0 ^5.1 Chinnaiyan, AM et al. (1997) Role of CED-4 in the activation of CED-3. Nature 388 728-9 PubMed GONUTS page

[PMID:8631956-6] 6.0 ^6.1 Hugunin, M et al. (1996) Protease activity of in vitro transcribed and translated Caenorhabditis elegans cell death gene (ced-3) product. J. Biol. Chem. 271 3517-22 PubMed GONUTS page

[PMID:16208361-7] 7.0 ^7.1 Yan, N et al. (2005) Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans. Nature 437 831-7 PubMed GONUTS page

[PMID:9651369-8] 8.0 ^8.1 Chaudhary, D et al. (1998) The death inhibitory molecules CED-9 and CED-4L use a common mechanism to inhibit the CED-3 death protease. J. Biol. Chem. 273 17708-12 PubMed GONUTS page

[PMID:17237514-9] Reddien, PW et al. (2007) DPL-1 DP, LIN-35 Rb and EFL-1 E2F act with the MCD-1 zinc-finger protein to promote programmed cell death in Caenorhabditis elegans. Genetics 175 1719-33 PubMed GONUTS page

[PMID:21502138-10] Erdélyi, P et al. (2011) Shared developmental roles and transcriptional control of autophagy and apoptosis in Caenorhabditis elegans. J. Cell. Sci. 124 1510-8 PubMed GONUTS page

[PMID:9604928-11] Conradt, B & Horvitz, HR (1998) The C. elegans protein EGL-1 is required for programmed cell death and interacts with the Bcl-2-like protein CED-9. Cell 93 519-29 PubMed GONUTS page

[PMID:3955651-12] Ellis, HM & Horvitz, HR (1986) Genetic control of programmed cell death in the nematode C. elegans. Cell 44 817-29 PubMed GONUTS page

[PMID:9384385-13] Xue, D & Horvitz, HR (1997) Caenorhabditis elegans CED-9 protein is a bifunctional cell-death inhibitor. Nature 390 305-8 PubMed GONUTS page

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

[13]

CAEEL:D3YT61

Contents

Annotations

Notes

References

a

c

e

h

m

n

p

r

Navigation menu

Personal tools

Namespaces

Variants

Views

More

Search

Navigation

Cacao

Links

Tools