P42574 (CASP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Caspase-3
Short name=CASP-3
EC=3.4.22.56

Alternative name(s):
Apopain
Cysteine protease CPP32
Short name=CPP-32
Protein Yama
SREBP cleavage activity 1
Short name=SCA-1

Cleaved into the following 2 chains:

1. Caspase-3 subunit p17
2. Caspase-3 subunit p12

Gene names

Name:	CASP3
Synonyms:	CPP32

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	277 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	Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage. Ref.8 Ref.14
Catalytic activity	Strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position.
Enzyme regulation	Inhibited by isatin sulfonamides.
Subunit structure	Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 17 kDa (p17) and a 12 kDa (p12) subunit. Interacts with BIRC6/bruce. Ref.12
Subcellular location	Cytoplasm.
Tissue specificity	Highly expressed in lung, spleen, heart, liver and kidney. Moderate levels in brain and skeletal muscle, and low in testis. Also found in many cell lines, highest expression in cells of the immune system.
Post-translational modification	Cleavage by granzyme B, caspase-6, caspase-8 and caspase-10 generates the two active subunits. Additional processing of the propeptides is likely due to the autocatalytic activity of the activated protease. Active heterodimers between the small subunit of caspase-7 protease and the large subunit of caspase-3 also occur and vice versa. S-nitrosylated on its catalytic site cysteine in unstimulated human cell lines and denitrosylated upon activation of the Fas apoptotic pathway, associated with an increase in intracellular caspase activity. Fas therefore activates caspase-3 not only by inducing the cleavage of the caspase zymogen to its active subunits, but also by stimulating the denitrosylation of its active site thiol.
Sequence similarities	Belongs to the peptidase C14A family.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein S-nitrosylation Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	B cell homeostasis Inferred from electronic annotation. Source: Compara T cell homeostasis Inferred from electronic annotation. Source: Compara activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c Traceable author statement. Source: Reactome apoptotic DNA fragmentation Traceable author statement. Source: Reactome apoptotic signaling pathway Traceable author statement PubMed 10521396. Source: BHF-UCL cell fate commitment Inferred from electronic annotation. Source: Compara cellular response to organic substance Inferred from electronic annotation. Source: Compara extrinsic apoptotic signaling pathway via death domain receptors Inferred from electronic annotation. Source: Compara heart development Inferred from electronic annotation. Source: Compara hippo signaling cascade Traceable author statement. Source: Reactome induction of apoptosis Traceable author statement Ref.1. Source: ProtInc intrinsic apoptotic signaling pathway in response to oxidative stress Inferred from electronic annotation. Source: Compara keratinocyte differentiation Inferred from electronic annotation. Source: Compara negative regulation of B cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of activated T cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from genetic interaction PubMed 9353287. Source: MGI negative regulation of cyclin-dependent protein serine/threonine kinase activity Inferred from electronic annotation. Source: Compara nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome neuron apoptotic process Inferred from electronic annotation. Source: Compara nuclear fragmentation involved in apoptotic nuclear change Inferred from mutant phenotype PubMed 11350920. Source: HGNC positive regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara protein processing Inferred from electronic annotation. Source: Compara proteolysis Inferred from direct assay PubMed 12888622. Source: UniProtKB release of cytochrome c from mitochondria Inferred from electronic annotation. Source: Compara response to DNA damage stimulus Inferred from electronic annotation. Source: Compara response to UV Inferred from electronic annotation. Source: Compara response to tumor necrosis factor Traceable author statement PubMed 10521396. Source: BHF-UCL response to wounding Inferred from electronic annotation. Source: Compara sensory perception of sound Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Inferred from direct assay PubMed 17167422. Source: UniProtKB mitochondrion Inferred from direct assay. Source: HPA nucleoplasm Traceable author statement. Source: Reactome plasma membrane Traceable author statement. Source: Reactome
Molecular_function	aspartic-type endopeptidase activity Inferred from electronic annotation. Source: Compara cyclin-dependent protein serine/threonine kinase inhibitor activity Inferred from electronic annotation. Source: Compara cysteine-type endopeptidase activity Inferred from direct assay PubMed 19240112PubMed 21726810. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
WNK3	Q9BYP7	2	EBI-524064,EBI-1182602

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 9

9

PRO_0000004569

Propeptide

10 – 28

19

PRO_0000004570

Chain

29 – 175

147

Caspase-3 subunit p17

PRO_0000004571

Chain

176 – 277

102

Caspase-3 subunit p12

PRO_0000004572

Sites

Active site

121

1

By similarity

Active site

163

1

By similarity

Amino acid modifications

Modified residue

26

1

Phosphoserine By similarity

Modified residue

163

1

S-nitrosocysteine; in inhibited form

Natural variations

Natural variant

22

1

H → R.
Corresponds to variant rs35578277 [ dbSNP | Ensembl ].

VAR_048616

Natural variant

190

1

E → D. Ref.1 Ref.3 Ref.8
Corresponds to variant rs1049210 [ dbSNP | Ensembl ].

VAR_001401

Experimental info

Sequence conflict

31 – 36

6

ISLDNS → MSWDTG in CAC88866. Ref.3

Secondary structure

1

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277

Helix Strand Turn

Details...

Beta strand

41 – 51

11

Helix

57 – 59

3

Helix

67 – 80

14

Beta strand

84 – 90

7

Helix

93 – 104

12

Beta strand

111 – 120

10

Beta strand

126 – 129

4

Beta strand

132 – 135

4

Helix

136 – 141

6

Turn

145 – 147

3

Helix

149 – 151

3

Beta strand

156 – 162

7

Beta strand

164 – 167

4

Turn

183 – 185

3

Turn

189 – 192

4

Beta strand

193 – 199

7

Beta strand

206 – 208

3

Turn

209 – 211

3

Helix

214 – 226

13

Turn

227 – 229

3

Helix

232 – 246

15

Turn

254 – 258

5

Beta strand

264 – 267

4

Beta strand

270 – 272

3

Sequences

	Sequence		Length	Mass (Da)
	P42574 [UniParc]. Last modified October 11, 2005. Version 2. Checksum: 2F35CD3BCF7FF64A	FASTA	277	31,608
	10 20 30 40 50 60 MENTENSVDS KSIKNLEPKI IHGSESMDSG ISLDNSYKMD YPEMGLCIII NNKNFHKSTG 70 80 90 100 110 120 MTSRSGTDVD AANLRETFRN LKYEVRNKND LTREEIVELM RDVSKEDHSK RSSFVCVLLS 130 140 150 160 170 180 HGEEGIIFGT NGPVDLKKIT NFFRGDRCRS LTGKPKLFII QACRGTELDC GIETDSGVDD 190 200 210 220 230 240 DMACHKIPVE ADFLYAYSTA PGYYSWRNSK DGSWFIQSLC AMLKQYADKL EFMHILTRVN 250 260 270 RKVATEFESF SFDATFHAKK QIPCIVSMLT KELYFYH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 beta-converting enzyme." Fernandes-Alnemri T., Litwack G., Alnemri E.S. J. Biol. Chem. 269:30761-30764(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASP-190. Tissue: T-cell.
[2]	"Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase." Tewari M., Quan L.T., O'Rourke K., Desnoyers S., Zeng Z., Beidler D.R., Poirier G.G., Salvesen G.S., Dixit V.M. Cell 81:801-809(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Caspase 3 activation is controlled by a sequence located in the N-terminus of its large subunit." Pelletier M., Cartron P.F., Delaval F., Meflah K., Vallette F.M., Oliver L. Biochem. Biophys. Res. Commun. 316:93-99(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASP-190.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Tongue.
[5]	NIEHS SNPs program Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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]. Tissue: Lymph.
[8]	"Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis." Nicholson D.W., Ali A., Thornberry N.A., Vaillancourt J.P., Ding C.K., Gallant M., Gareau Y., Griffin P.R., Labelle M., Lazebnik Y.A., Munday N.A., Raju S.M., Smulson M.E., Yamin T.-T., Li V.L., Miller D.K. Nature 376:37-43(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 29-46 AND 175-193, FUNCTION, VARIANT ASP-190.
[9]	"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: PROTEOLYTIC PROCESSING.
[10]	"Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract." Goldberg Y.P., Nicholson D.W., Rasper D.M., Kalchman M.A., Koide H.B., Graham R.K., Bromm M., Kazemi-Esfarjani P., Thornberry N.A., Vaillancourt J.P., Hayden M.R. Nat. Genet. 13:442-449(1996) [PubMed] [Europe PMC] [Abstract] Cited for: CLEAVAGE OF HUNTINGTIN.
[11]	"Fas-induced caspase denitrosylation." Mannick J.B., Hausladen A., Liu L., Hess D.T., Zeng M., Miao Q.X., Kane L.S., Gow A.J., Stamler J.S. Science 284:651-654(1999) [PubMed] [Europe PMC] [Abstract] Cited for: S-NITROSYLATION.
[12]	"Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3 ubiquitin ligase." Bartke T., Pohl C., Pyrowolakis G., Jentsch S. Mol. Cell 14:801-811(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BIRC6/BRUCE.
[13]	"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].
[14]	"RET modulates cell adhesion via its cleavage by caspase in sympathetic neurons." Cabrera J.R., Bouzas-Rodriguez J., Tauszig-Delamasure S., Mehlen P. J. Biol. Chem. 286:14628-14638(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CELL ADHESION.
[15]	"The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis." Rotonda J., Nicholson D.W., Fazil K.M., Gallant M., Gareau Y., Labelle M., Peterson E.P., Rasper D.M., Ruel R., Vaillancourt J.P., Thornberry N.A., Becker J.W. Nat. Struct. Biol. 3:619-625(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 28-277.
[16]	"Structure of recombinant human CPP32 in complex with the tetrapeptide acetyl-Asp-Val-Ala-Asp fluoromethyl ketone." Mittl P.R.E., di Marco S., Krebs J.F., Bai X., Karanewsky D.S., Priestle J.P., Tomaselli K.J., Gruetter M.G. J. Biol. Chem. 272:6539-6547(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 35-173 AND 185-277.
[17]	"Potent and selective nonpeptide inhibitors of caspases 3 and 7 inhibit apoptosis and maintain cell functionality." Lee D., Long S.A., Adams J.L., Chan G., Vaidya K.S., Francis T.A., Kikly K., Winkler J.D., Sung C.-M., Debouck C., Richardson S., Levy M.A., DeWolf W.E. Jr., Keller P.M., Tomaszek T., Head M.S., Ryan M.D., Haltiwanger R.C. , Liang P.-H., Janson C.A., McDevitt P.J., Johanson K., Concha N.O., Chan W., Abdel-Meguid S.S., Badger A.M., Lark M.W., Nadeau D.P., Suva L.J., Gowen M., Nuttall M.E. J. Biol. Chem. 275:16007-16014(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U13737 mRNA. Translation: AAA65015.1.
U13738 mRNA. Translation: AAB60355.1.
U26943 mRNA. Translation: AAA74929.1.
AJ413269 mRNA. Translation: CAC88866.1.
AK291337 mRNA. Translation: BAF84026.1.
AY219866 Genomic DNA. Translation: AAO25654.1.
CH471056 Genomic DNA. Translation: EAX04673.1.
CH471056 Genomic DNA. Translation: EAX04674.1.
CH471056 Genomic DNA. Translation: EAX04675.1.
BC016926 mRNA. Translation: AAH16926.1.

IPI

IPI00292140.

PIR

A55315.

RefSeq

NP_004337.2. NM_004346.3.
NP_116786.1. NM_032991.2.

UniGene

Hs.141125.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CP3	X-ray	2.30	A/B	1-277	[»]
1GFW	X-ray	2.80	A	29-175	[»]
			B	181-277	[»]
1I3O	X-ray	2.70	A/C	1-175	[»]
			B/D	176-277	[»]
1NME	X-ray	1.60	A	29-174	[»]
			B	186-277	[»]
1NMQ	X-ray	2.40	A/B	29-277	[»]
1NMS	X-ray	1.70	A/B	29-277	[»]
1PAU	X-ray	2.50	A	29-175	[»]
			B	176-277	[»]
1QX3	X-ray	1.90	A	29-277	[»]
1RE1	X-ray	2.50	A	29-175	[»]
			B	176-277	[»]
1RHJ	X-ray	2.20	A/C	29-175	[»]
			B/D	176-277	[»]
1RHK	X-ray	2.50	A	29-175	[»]
			B	176-277	[»]
1RHM	X-ray	2.50	A/C	29-175	[»]
			B/D	176-277	[»]
1RHQ	X-ray	3.00	A/D	29-175	[»]
			B/E	176-277	[»]
1RHR	X-ray	3.00	A	29-175	[»]
			B	176-277	[»]
1RHU	X-ray	2.51	A	29-175	[»]
			B	176-277	[»]
2C1E	X-ray	1.77	A	29-175	[»]
			B	176-277	[»]
2C2K	X-ray	1.87	A	29-175	[»]
			B	176-277	[»]
2C2M	X-ray	1.94	A	29-175	[»]
			B	176-277	[»]
2C2O	X-ray	2.45	A	29-175	[»]
			B	176-277	[»]
2CDR	X-ray	1.70	A	29-175	[»]
			B	176-277	[»]
2CJX	X-ray	1.70	A	29-175	[»]
			B	176-277	[»]
2CJY	X-ray	1.67	A	29-175	[»]
			B	176-277	[»]
2CNK	X-ray	1.75	A	29-175	[»]
			B	176-277	[»]
2CNL	X-ray	1.67	A	29-175	[»]
			B	176-277	[»]
2CNN	X-ray	1.70	A	29-175	[»]
			B	176-277	[»]
2CNO	X-ray	1.95	A	29-175	[»]
			B	176-277	[»]
2DKO	X-ray	1.06	A	29-174	[»]
			B	176-277	[»]
2H5I	X-ray	1.69	A	29-174	[»]
			B	184-277	[»]
2H5J	X-ray	2.00	A/C	29-174	[»]
			B/D	184-277	[»]
2H65	X-ray	2.30	A/C	29-174	[»]
			B/D	184-277	[»]
2J30	X-ray	1.40	A	29-277	[»]
2J31	X-ray	1.50	A	29-277	[»]
2J32	X-ray	1.30	A	29-277	[»]
2J33	X-ray	2.00	A	29-277	[»]
2XYG	X-ray	1.54	A	29-174	[»]
			B	185-277	[»]
2XYH	X-ray	1.89	A	29-174	[»]
			B	185-277	[»]
2XYP	X-ray	1.86	A	29-174	[»]
			B	185-277	[»]
2XZD	X-ray	2.10	A/C	29-175	[»]
			B/D	176-277	[»]
2XZT	X-ray	2.70	A/C	29-175	[»]
			B/D	176-277	[»]
2Y0B	X-ray	2.10	A/C	29-175	[»]
			B/D	176-277	[»]
3DEH	X-ray	2.50	A/B/C/D	29-277	[»]
3DEI	X-ray	2.80	A/B/C/D	29-277	[»]
3DEJ	X-ray	2.60	A/B/C/D	29-277	[»]
3DEK	X-ray	2.40	A/B/C/D	29-277	[»]
3EDQ	X-ray	1.61	A/C	29-175	[»]
			B/D	176-277	[»]
3GJQ	X-ray	2.60	A/C	29-175	[»]
			B/D	176-277	[»]
3GJR	X-ray	2.20	A/C	29-175	[»]
			B/D	176-277	[»]
3GJS	X-ray	1.90	A/C	29-175	[»]
			B/D	176-277	[»]
3GJT	X-ray	2.20	A/C	29-175	[»]
			B/D	176-277	[»]
3H0E	X-ray	2.00	A/B	29-277	[»]
3ITN	X-ray	1.63	A	29-277	[»]
3KJF	X-ray	2.00	A	29-175	[»]
			B	176-277	[»]
3PCX	X-ray	1.50	A	29-277	[»]
3PD0	X-ray	2.00	A	29-277	[»]
3PD1	X-ray	1.62	A	29-277	[»]
4DCJ	X-ray	1.70	A/D	29-175	[»]
			B/E	176-277	[»]
4DCO	X-ray	1.70	A/D	29-175	[»]
			B/E	176-277	[»]
4DCP	X-ray	1.70	A/D	29-175	[»]
			B/E	176-277	[»]
4EHA	X-ray	1.70	A/C	1-277	[»]
4EHD	X-ray	1.58	A	1-277	[»]
4EHF	X-ray	1.66	A	1-277	[»]
4EHH	X-ray	1.78	A	1-277	[»]
4EHK	X-ray	1.67	A/C	1-277	[»]
4EHL	X-ray	1.80	A/C	1-277	[»]
4EHN	X-ray	1.69	A	1-277	[»]

ProteinModelPortal

P42574.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-268N.

IntAct

P42574. 12 interactions.

MINT

MINT-147180.

STRING

9606.ENSP00000311032.

Protein family/group databases

MEROPS

C14.003.

PTM databases

PhosphoSite

P42574.

Polymorphism databases

DMDM

77416852.

2D gel databases

OGP

P42574.

Proteomic databases

PaxDb

P42574.

PeptideAtlas

P42574.

PRIDE

P42574.

Protocols and materials databases

DNASU

836.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000308394; ENSP00000311032; ENSG00000164305.
ENST00000523916; ENSP00000428929; ENSG00000164305.

GeneID

836.

KEGG

hsa:836.

UCSC

uc003iwh.3. human.

Organism-specific databases

CTD

836.

GeneCards

GC04M185548.

HGNC

HGNC:1504. CASP3.

HPA

CAB000091.
CAB008381.
HPA002643.

MIM

600636. gene.

neXtProt

NX_P42574.

PharmGKB

PA26087.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG279444.

HOGENOM

HOG000231878.

HOVERGEN

HBG050802.

InParanoid

P42574.

KO

K02187.

OMA

SSFVCVL.

OrthoDB

EOG4CZBGR.

PhylomeDB

P42574.

Enzyme and pathway databases

BRENDA

3.4.22.56. 2681.

Pathway_Interaction_DB

a6b1_a6b4_integrin_pathway. a6b1 and a6b4 Integrin signaling.
nfat_tfpathway. Calcineurin-regulated NFAT-dependent transcription in lymphocytes.
caspase_pathway. Caspase cascade in apoptosis.
faspathway. FAS signaling pathway (CD95).
hivnefpathway. HIV-1 Nef: Negative effector of Fas and TNF-alpha.
lysophospholipid_pathway. LPA receptor mediated events.
p75ntrpathway. p75(NTR)-mediated signaling.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.
syndecan_2_pathway. Syndecan-2-mediated signaling events.

Reactome

REACT_111102. Signal Transduction.
REACT_578. Apoptosis.

Gene expression databases

ArrayExpress

P42574.

Bgee

P42574.

CleanEx

HS_CASP3.

Genevestigator

P42574.

GermOnline

ENSG00000164305. Homo sapiens.

Family and domain databases

InterPro

IPR015470. Caspase_3.
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.
PTHR10454:SF30. PTHR10454:SF30. 1 hit.

Pfam

PF00656. Peptidase_C14. 1 hit.
[Graphical view]

PRINTS

PR00376. IL1BCENZYME.

SMART

SM00115. CASc. 1 hit.
[Graphical view]

PROSITE

PS01122. CASPASE_CYS. 1 hit.
PS01121. CASPASE_HIS. 1 hit.
PS50207. CASPASE_P10. 1 hit.
PS50208. CASPASE_P20. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P42574.

ChEMBL

CHEMBL2334.

DrugBank

DB01065. Melatonin.
DB01017. Minocycline.
DB00641. Simvastatin.

EvolutionaryTrace

P42574.

GenomeRNAi

836.

NextBio

3478.

PMAP-CutDB

P42574.

SOURCE

Search...

Entry information

Entry name

CASP3_HUMAN

Accession

Primary (citable) accession number: P42574
Secondary accession number(s): A8K5M2 , D3DP53, Q96AN1, Q96KP2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	October 11, 2005
Last modified:	May 1, 2013
This is version 159 of the entry and version 2 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.