CASP3
entrez
836
canonical
uniprot
P42574
canonical
ensembl
ENSG00000164305
resolver
ensp
ENSP00000311032
resolver
ensp
ENSP00000377210
resolver
ensp
ENSP00000377213
resolver
ensp
ENSP00000428372
resolver
ensp
ENSP00000428929
resolver
ensp
ENSP00000514797
resolver
ensp
ENSP00000514798
resolver
ensp
ENSP00000542398
resolver
ensp
ENSP00000542399
resolver
ensp
ENSP00000542400
resolver
ensp
ENSP00000542401
resolver
ensp
ENSP00000542402
resolver
ensp
ENSP00000542403
resolver
ensp
ENSP00000542404
resolver
ensp
ENSP00000542405
resolver
ensp
ENSP00000542406
resolver
ensp
ENSP00000609998
resolver
ensp
ENSP00000609999
resolver
ensp
ENSP00000610000
resolver
ensp
ENSP00000610002
resolver
ensp
ENSP00000610003
resolver
ensp
ENSP00000610004
resolver
ensp
ENSP00000610005
resolver
ensp
ENSP00000642099
resolver
ensp
ENSP00000642100
resolver
ensp
ENSP00000642101
resolver
ensp
ENSP00000642102
resolver
enst
ENST00000308394
resolver
enst
ENST00000393585
resolver
enst
ENST00000393588
resolver
enst
ENST00000517513
resolver
enst
ENST00000523916
resolver
enst
ENST00000700100
resolver
enst
ENST00000700101
resolver
enst
ENST00000872339
resolver
enst
ENST00000872340
resolver
enst
ENST00000872341
resolver
enst
ENST00000872342
resolver
enst
ENST00000872343
resolver
enst
ENST00000872344
resolver
enst
ENST00000872345
resolver
enst
ENST00000872346
resolver
enst
ENST00000872347
resolver
enst
ENST00000939939
resolver
enst
ENST00000939940
resolver
enst
ENST00000939941
resolver
enst
ENST00000939943
resolver
enst
ENST00000939944
resolver
enst
ENST00000939945
resolver
enst
ENST00000939946
resolver
enst
ENST00000972040
resolver
enst
ENST00000972041
resolver
enst
ENST00000972042
resolver
enst
ENST00000972043
resolver
genesymbol
CASP3
resolver
genesymbol_syn
CPP32
resolver
hgnc
HGNC:1504
resolver
uniprot
A8K5M2
resolver
uniprot
A8MVM1
resolver
uniprot
D3DP53
resolver
uniprot
Q96AN1
resolver
uniprot
Q96KP2
resolver
uniprot_entry
A8MVM1_HUMAN
resolver
uniprot_entry
CASP3_HUMAN
resolver
uniprot_sec
A8K5M2
resolver
uniprot_sec
D3DP53
resolver
uniprot_sec
Q96AN1
resolver
uniprot_sec
Q96KP2
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by isatin sulfonamides (PubMed:10821855). Inhibited by BIRC6; following inhibition of BIRC6-caspase binding by DIABLO/SMAC, BIRC6 is subjected to caspase cleavage, leading to an increase in active caspases (PubMed:36758104, PubMed:36758106). {ECO:0000269|PubMed:10821855, ECO:0000269|PubMed:36758104, ECO:0000269|PubMed:36758106}.
uniprot
proteins
amino_acid_sequence
MENTENSVDSKSIKNLEPKIIHGSESMDSGISLDNSYKMDYPEMGLCIIINNKNFHKSTGMTSRSGTDVDAANLRETFRNLKYEVRNKNDLTREEIVELMRDVSKEDHSKRSSFVCVLLSHGEEGIIFGTNGPVDLKKITNFFRGDRCRSLTGKPKLFIIQACRGTELDCGIETDSGVDDDMACHKIPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCAMLKQYADKLEFMHILTRVNRKVATEFESFSFDATFHAKKQIPCIVSMLTKELYFYH
uniprot
proteins
ec_number
3.4.22.56
uniprot
proteins
function
FUNCTION: Thiol protease that acts as a major effector caspase involved in the execution phase of apoptosis (PubMed:18723680, PubMed:20566630, PubMed:23650375, PubMed:35338844, PubMed:35446120, PubMed:7596430). Following cleavage and activation by initiator caspases (CASP8, CASP9 and/or CASP10), mediates execution of apoptosis by catalyzing cleavage of many proteins (PubMed:18723680, PubMed:20566630, PubMed:23650375, PubMed:7596430). At the onset of apoptosis, it proteolytically cleaves poly(ADP-ribose) polymerase PARP1 at a '216-Asp-|-Gly-217' bond (PubMed:10497198, PubMed:16374543, PubMed:7596430, PubMed:7774019). Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain (By similarity). Cleaves and activates caspase-6, -7 and -9 (CASP6, CASP7 and CASP9, respectively) (PubMed:7596430). Cleaves and inactivates interleukin-18 (IL18) (PubMed:37993714, PubMed:9334240). Involved in the cleavage of huntingtin (PubMed:8696339). Triggers cell adhesion in sympathetic neurons through RET cleavage (PubMed:21357690). Also involved in axon pruning during brain development (By similarity). Cleaves DSG2 in response to apoptosis resulting in a loss of full length DSG2 at desmosome cell junctions and subsequent loss of cell-cell adhesion (PubMed:17559062). Also cleaves JUP in response to apoptosis (PubMed:17559062). Cleaves and inhibits serine/threonine-protein kinase AKT1 in response to oxidative stress (PubMed:23152800). Acts as an inhibitor of type I interferon production during virus-induced apoptosis by mediating cleavage of antiviral proteins CGAS, IRF3 and MAVS, thereby preventing cytokine overproduction (PubMed:30878284). Also involved in pyroptosis by mediating cleavage and activation of gasdermin-E (GSDME) (PubMed:35338844, PubMed:35446120). Cleaves XRCC4 and phospholipid scramblase proteins XKR4, XKR8 and XKR9, leading to promote phosphatidylserine exposure on apoptotic cell surface (PubMed:23845944, PubMed:33725486). Cleaves BIRC6 following inhibition of BIRC6-caspase binding by DIABLO/SMAC (PubMed:36758104, PubMed:36758106). {ECO:0000250|UniProtKB:Q60431, ECO:0000269|PubMed:10497198, ECO:0000269|PubMed:16374543, ECO:0000269|PubMed:17559062, ECO:0000269|PubMed:18723680, ECO:0000269|PubMed:20566630, ECO:0000269|PubMed:21357690, ECO:0000269|PubMed:23152800, ECO:0000269|PubMed:23650375, ECO:0000269|PubMed:23845944, ECO:0000269|PubMed:30878284, ECO:0000269|PubMed:33725486, ECO:0000269|PubMed:35338844, ECO:0000269|PubMed:35446120, ECO:0000269|PubMed:36758104, ECO:0000269|PubMed:36758106, ECO:0000269|PubMed:37993714, ECO:0000269|PubMed:7596430, ECO:0000269|PubMed:7774019, ECO:0000269|PubMed:8696339, ECO:0000269|PubMed:9334240}.
uniprot
proteins
mass_dalton
31608
uniprot
proteins
mutagenesis
MUTAGEN 9; /note="D->A: In P3-D3A mutant; abolished cleavage and activation, leading to prevent thiol protease activity; when associated with A-28 and A-175."; /evidence="ECO:0000269|PubMed:23650375"; MUTAGEN 28; /note="D->A: In P3-D3A mutant; abolished cleavage and activation, leading to prevent thiol protease activity; when associated with A-9 and A-175."; /evidence="ECO:0000269|PubMed:23650375"; MUTAGEN 175; /note="D->A: In P3-D3A mutant; abolished cleavage and activation, leading to prevent thiol protease activity; when associated with A-9 and A-28."; /evidence="ECO:0000269|PubMed:23650375"; MUTAGEN 207; /note="R->A: Abolished ADP-riboxanation by C.violaceum CopC."; /evidence="ECO:0000269|PubMed:35446120, ECO:0000269|PubMed:36423631
uniprot
proteins
post_translational_modification
PTM: Cleavage by granzyme B, caspase-6, caspase-8 and caspase-10 generates the two active subunits (PubMed:35338844, PubMed:35446120, PubMed:7596430, PubMed:8755496). Additional processing of the propeptides is likely due to the autocatalytic activity of the activated protease (PubMed:7596430, PubMed:8755496). Active heterodimers between the small subunit of caspase-7 protease and the large subunit of caspase-3 also occur and vice versa (PubMed:7596430, PubMed:8755496). {ECO:0000269|PubMed:35338844, ECO:0000269|PubMed:35446120, ECO:0000269|PubMed:7596430, ECO:0000269|PubMed:8755496}.; PTM: 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. {ECO:0000269|PubMed:10213689}.; PTM: Ubiquitinated by BIRC6; this activity is inhibited by DIABLO/SMAC. {ECO:0000269|PubMed:36758104, ECO:0000269|PubMed:36758106}.; PTM: (Microbial infection) ADP-riboxanation by C.violaceum CopC blocks CASP3 processing, preventing CASP3 activation and ability to recognize and cleave substrates. {ECO:0000269|PubMed:35338844, ECO:0000269|PubMed:35446120, ECO:0000269|PubMed:36423631}.
uniprot
proteins
protein_family
Peptidase C14A family
uniprot
proteins
pubmed
10213689
uniprot
proteins
pubmed
10497198
uniprot
proteins
pubmed
10821855
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15003516
uniprot
proteins
pubmed
15200957
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16374543
uniprot
proteins
pubmed
17559062
uniprot
proteins
pubmed
18723680
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
20566630
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21357690
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
23152800
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23650375
uniprot
proteins
pubmed
23845944
uniprot
proteins
pubmed
28045099
uniprot
proteins
pubmed
28459430
uniprot
proteins
pubmed
30878284
uniprot
proteins
pubmed
33725486
uniprot
proteins
pubmed
35338844
uniprot
proteins
pubmed
35446120
uniprot
proteins
pubmed
36423631
uniprot
proteins
pubmed
36758104
uniprot
proteins
pubmed
36758106
uniprot
proteins
pubmed
37993714
uniprot
proteins
pubmed
7596430
uniprot
proteins
pubmed
7774019
uniprot
proteins
pubmed
7983002
uniprot
proteins
pubmed
8673606
uniprot
proteins
pubmed
8696339
uniprot
proteins
pubmed
8755496
uniprot
proteins
pubmed
9045680
uniprot
proteins
pubmed
9334240
uniprot
proteins
sequence_length
277
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15003516}.
uniprot
proteins