CASP3 | ENSG00000164305 | NCBI 836

Details for: CASP3

Gene ID: 836

Symbol: CASP3

Ensembl ID: ENSG00000164305

Description: caspase 3

Associated with

Activation of caspases through apoptosome-mediated cleavage
(R-HSA-111459)
Apoptosis
(R-HSA-109581)
Apoptosis induced dna fragmentation
(R-HSA-140342)
Apoptotic cleavage of cell adhesion proteins
(R-HSA-351906)
Apoptotic cleavage of cellular proteins
(R-HSA-111465)
Apoptotic execution phase
(R-HSA-75153)
Apoptotic factor-mediated response
(R-HSA-111471)
Caspase-mediated cleavage of cytoskeletal proteins
(R-HSA-264870)
Caspase activation via dependence receptors in the absence of ligand
(R-HSA-418889)
Caspase activation via extrinsic apoptotic signalling pathway
(R-HSA-5357769)
Cell death signalling via nrage, nrif and nade
(R-HSA-204998)
Cytochrome c-mediated apoptotic response
(R-HSA-111461)
Cytokine signaling in immune system
(R-HSA-1280215)
Death receptor signaling
(R-HSA-73887)
Degradation of the extracellular matrix
(R-HSA-1474228)
Extracellular matrix organization
(R-HSA-1474244)
Immune system
(R-HSA-168256)
Intrinsic pathway for apoptosis
(R-HSA-109606)
Nade modulates death signalling
(R-HSA-205025)
Other interleukin signaling
(R-HSA-449836)
P75 ntr receptor-mediated signalling
(R-HSA-193704)
Programmed cell death
(R-HSA-5357801)
Pyroptosis
(R-HSA-5620971)
Regulated necrosis
(R-HSA-5218859)
Signaling by hippo
(R-HSA-2028269)
Signaling by interleukins
(R-HSA-449147)
Signal transduction
(R-HSA-162582)
Smac(diablo)-mediated dissociation of iap:caspase complexes
(R-HSA-111464)
Smac (diablo) binds to iaps
(R-HSA-111463)
Smac, xiap-regulated apoptotic response
(R-HSA-111469)
Stimulation of the cell death response by pak-2p34
(R-HSA-211736)
Apoptotic process
(GO:0006915)
Aspartic-type endopeptidase activity
(GO:0004190)
Axonal fasciculation
(GO:0007413)
B cell homeostasis
(GO:0001782)
Cell fate commitment
(GO:0045165)
Cyclin-dependent protein serine/threonine kinase inhibitor activity
(GO:0004861)
Cysteine-type endopeptidase activity
(GO:0004197)
Cysteine-type endopeptidase activity involved in apoptotic process
(GO:0097153)
Cysteine-type endopeptidase activity involved in apoptotic signaling pathway
(GO:0097199)
Cysteine-type endopeptidase activity involved in execution phase of apoptosis
(GO:0097200)
Death receptor binding
(GO:0005123)
Dna damage response
(GO:0006974)
Enzyme activator activity
(GO:0008047)
Erythrocyte differentiation
(GO:0030218)
Fibroblast apoptotic process
(GO:0044346)
Glial cell apoptotic process
(GO:0034349)
Heart development
(GO:0007507)
Hippocampus development
(GO:0021766)
Intrinsic apoptotic signaling pathway in response to osmotic stress
(GO:0008627)
Keratinocyte differentiation
(GO:0030216)
Learning or memory
(GO:0007611)
Luteolysis
(GO:0001554)
Negative regulation of activated t cell proliferation
(GO:0046007)
Negative regulation of b cell proliferation
(GO:0030889)
Negative regulation of cell cycle
(GO:0045786)
Negative regulation of cytokine production
(GO:0001818)
Neuron apoptotic process
(GO:0051402)
Neuron differentiation
(GO:0030182)
Neurotrophin trk receptor signaling pathway
(GO:0048011)
Peptidase activity
(GO:0008233)
Phospholipase a2 activator activity
(GO:0016005)
Platelet formation
(GO:0030220)
Positive regulation of neuron apoptotic process
(GO:0043525)
Protease binding
(GO:0002020)
Protein-containing complex binding
(GO:0044877)
Protein binding
(GO:0005515)
Protein catabolic process
(GO:0030163)
Protein maturation
(GO:0051604)
Protein processing
(GO:0016485)
Proteolysis
(GO:0006508)
Regulation of macroautophagy
(GO:0016241)
Regulation of protein stability
(GO:0031647)
Response to amino acid
(GO:0043200)
Response to cobalt ion
(GO:0032025)
Response to estradiol
(GO:0032355)
Response to glucocorticoid
(GO:0051384)
Response to glucose
(GO:0009749)
Response to hydrogen peroxide
(GO:0042542)
Response to hypoxia
(GO:0001666)
Response to lipopolysaccharide
(GO:0032496)
Response to nicotine
(GO:0035094)
Response to tumor necrosis factor
(GO:0034612)
Response to uv
(GO:0009411)
Response to wounding
(GO:0009611)
Response to x-ray
(GO:0010165)
Response to xenobiotic stimulus
(GO:0009410)
Sensory perception of sound
(GO:0007605)
Striated muscle cell differentiation
(GO:0051146)
T cell homeostasis
(GO:0043029)

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: polychromatophilic erythroblast (CL0000550)
Fold Change: 163.2323
Cell Significance Index: -25.3900
Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
Fold Change: 106.6458
Cell Significance Index: -27.0500
Cell Name: embryonic stem cell (CL0002322)
Fold Change: 74.1721
Cell Significance Index: -30.5600
Cell Name: smooth muscle fiber of ileum (CL1000278)
Fold Change: 63.5216
Cell Significance Index: -29.9900
Cell Name: mucosal type mast cell (CL0000485)
Fold Change: 61.2666
Cell Significance Index: -24.8900
Cell Name: peripheral blood mononuclear cell (CL2000001)
Fold Change: 55.1921
Cell Significance Index: -28.3900
Cell Name: ileal goblet cell (CL1000326)
Fold Change: 44.5738
Cell Significance Index: -29.9100
Cell Name: ciliated cell of the bronchus (CL0002332)
Fold Change: 26.1379
Cell Significance Index: -24.9600
Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 22.8638
Cell Significance Index: -28.1900
Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
Fold Change: 9.4219
Cell Significance Index: -25.2400
Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 7.3694
Cell Significance Index: -29.0800
Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
Fold Change: 6.4953
Cell Significance Index: -19.9500
Cell Name: epidermal Langerhans cell (CL0002457)
Fold Change: 4.9781
Cell Significance Index: -10.9000
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: 2.5550
Cell Significance Index: 34.8600
Cell Name: intestinal crypt stem cell of colon (CL0009043)
Fold Change: 1.5588
Cell Significance Index: 169.5600
Cell Name: tuft cell of colon (CL0009041)
Fold Change: 0.8520
Cell Significance Index: 769.2800
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: 0.7242
Cell Significance Index: 15.6900
Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
Fold Change: 0.6696
Cell Significance Index: 19.6700
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 0.5833
Cell Significance Index: 105.1500
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 0.5504
Cell Significance Index: 67.6800
Cell Name: colon goblet cell (CL0009039)
Fold Change: 0.4940
Cell Significance Index: 48.8700
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: 0.4550
Cell Significance Index: 23.6400
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: 0.4132
Cell Significance Index: 11.9100
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: 0.4002
Cell Significance Index: 47.2000
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 0.3946
Cell Significance Index: 79.1500
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: 0.3856
Cell Significance Index: 18.1300
Cell Name: cell in vitro (CL0001034)
Fold Change: 0.3853
Cell Significance Index: 210.4100
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: 0.3520
Cell Significance Index: 9.4000
Cell Name: neoplastic cell (CL0001063)
Fold Change: 0.3430
Cell Significance Index: 68.0800
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: 0.3345
Cell Significance Index: 15.1600
Cell Name: umbrella cell of urothelium (CL4030056)
Fold Change: 0.3214
Cell Significance Index: 2.9600
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: 0.2788
Cell Significance Index: 7.5900
Cell Name: lactocyte (CL0002325)
Fold Change: 0.2734
Cell Significance Index: 35.3200
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: 0.2703
Cell Significance Index: 43.9700
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 0.2148
Cell Significance Index: 94.9800
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: 0.2130
Cell Significance Index: 16.3500
Cell Name: GABAergic interneuron (CL0011005)
Fold Change: 0.1865
Cell Significance Index: 128.9700
Cell Name: early pro-B cell (CL0002046)
Fold Change: 0.1765
Cell Significance Index: 11.3900
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 0.1748
Cell Significance Index: 62.7200
Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
Fold Change: 0.1727
Cell Significance Index: 6.0000
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 0.1349
Cell Significance Index: 18.5200
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.1210
Cell Significance Index: 23.0200
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: 0.1057
Cell Significance Index: 5.9300
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: 0.0918
Cell Significance Index: 4.2800
Cell Name: odontoblast (CL0000060)
Fold Change: 0.0751
Cell Significance Index: 9.6300
Cell Name: cortical cell of adrenal gland (CL0002097)
Fold Change: 0.0606
Cell Significance Index: 1.6200
Cell Name: sebum secreting cell (CL0000317)
Fold Change: 0.0580
Cell Significance Index: 4.1000
Cell Name: Purkinje cell (CL0000121)
Fold Change: 0.0543
Cell Significance Index: 1.1900
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: 0.0336
Cell Significance Index: 0.9400
Cell Name: mesenchymal cell (CL0008019)
Fold Change: 0.0161
Cell Significance Index: 0.2700
Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
Fold Change: 0.0141
Cell Significance Index: 0.3000
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: 0.0056
Cell Significance Index: 10.4800
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: 0.0016
Cell Significance Index: 1.0400
Cell Name: lens epithelial cell (CL0002224)
Fold Change: -0.0095
Cell Significance Index: -14.6600
Cell Name: anterior lens cell (CL0002223)
Fold Change: -0.0116
Cell Significance Index: -21.3500
Cell Name: secondary lens fiber (CL0002225)
Fold Change: -0.0169
Cell Significance Index: -22.9300
Cell Name: endothelial cell of placenta (CL0009092)
Fold Change: -0.0248
Cell Significance Index: -0.1500
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: -0.0294
Cell Significance Index: -21.5400
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.0303
Cell Significance Index: -22.4400
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: -0.0314
Cell Significance Index: -14.2300
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: -0.0314
Cell Significance Index: -23.7400
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.0466
Cell Significance Index: -26.3000
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.0574
Cell Significance Index: -35.8600
Cell Name: forebrain neuroblast (CL1000042)
Fold Change: -0.0687
Cell Significance Index: -4.2200
Cell Name: abnormal cell (CL0001061)
Fold Change: -0.0694
Cell Significance Index: -7.0900
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: -0.0766
Cell Significance Index: -8.9300
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: -0.0781
Cell Significance Index: -22.4800
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: -0.0843
Cell Significance Index: -14.4000
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -0.0896
Cell Significance Index: -13.0300
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: -0.0925
Cell Significance Index: -5.8300
Cell Name: pro-T cell (CL0000827)
Fold Change: -0.1288
Cell Significance Index: -3.2900
Cell Name: cerebellar granule cell (CL0001031)
Fold Change: -0.1354
Cell Significance Index: -2.3200
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.1539
Cell Significance Index: -32.4100
Cell Name: hippocampal granule cell (CL0001033)
Fold Change: -0.1602
Cell Significance Index: -10.7800
Cell Name: foveolar cell of stomach (CL0002179)
Fold Change: -0.1726
Cell Significance Index: -1.1300
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.1864
Cell Significance Index: -21.3600
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: -0.1883
Cell Significance Index: -6.0300
Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: -0.1895
Cell Significance Index: -8.3800
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: -0.2328
Cell Significance Index: -17.3500
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -0.2585
Cell Significance Index: -26.9200
Cell Name: glycinergic neuron (CL1001509)
Fold Change: -0.2644
Cell Significance Index: -13.8800
Cell Name: corneal epithelial cell (CL0000575)
Fold Change: -0.2645
Cell Significance Index: -3.7700
Cell Name: direct pathway medium spiny neuron (CL4023026)
Fold Change: -0.2746
Cell Significance Index: -10.4000
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: -0.3161
Cell Significance Index: -9.0600
Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: -0.3290
Cell Significance Index: -26.0600
Cell Name: granulosa cell (CL0000501)
Fold Change: -0.3458
Cell Significance Index: -9.0900
Cell Name: neutrophil progenitor cell (CL0000834)
Fold Change: -0.3593
Cell Significance Index: -9.6100
Cell Name: fibroblast of dermis (CL0002551)
Fold Change: -0.3860
Cell Significance Index: -8.0800
Cell Name: lung endothelial cell (CL1001567)
Fold Change: -0.4486
Cell Significance Index: -23.3700
Cell Name: paneth cell of colon (CL0009009)
Fold Change: -0.4545
Cell Significance Index: -6.8100
Cell Name: skeletal muscle fiber (CL0008002)
Fold Change: -0.4692
Cell Significance Index: -12.0600
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -0.4729
Cell Significance Index: -29.0000
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: -0.5141
Cell Significance Index: -12.8500
Cell Name: intestinal epithelial cell (CL0002563)
Fold Change: -0.5154
Cell Significance Index: -5.3400
Cell Name: pvalb GABAergic cortical interneuron (CL4023018)
Fold Change: -0.6116
Cell Significance Index: -12.9800
Cell Name: type I muscle cell (CL0002211)
Fold Change: -0.6209
Cell Significance Index: -15.1500
Cell Name: endothelial cell of venule (CL1000414)
Fold Change: -0.6215
Cell Significance Index: -7.0600
Cell Name: fibro/adipogenic progenitor cell (CL0009099)
Fold Change: -0.6256
Cell Significance Index: -31.6200
Cell Name: L6b glutamatergic cortical neuron (CL4023038)
Fold Change: -0.6475
Cell Significance Index: -21.2000
Cell Name: L5 extratelencephalic projecting glutamatergic cortical neuron (CL4023041)
Fold Change: -0.6486
Cell Significance Index: -22.7200

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

**Key Characteristics:** Caspase 3 is a cysteine-aspartic protease, specifically a caspase, which is a family of proteases that play a central role in the regulation of programmed cell death. It is a member of the initiator caspase family and is activated by the apoptosome, a complex formed by the binding of cytochrome c to Apaf-1. Once activated, Casp3 cleaves a wide range of cellular substrates, including those involved in cell survival, adhesion, and cytoskeletal organization. Its activity is tightly regulated by various inhibitors and activators, ensuring that apoptosis is executed in a controlled manner. **Pathways and Functions:** Caspase 3 is involved in multiple signaling pathways, including: 1. **Apoptosis**: Casp3 is a key effector caspase in the intrinsic and extrinsic apoptotic pathways, mediating the cleavage of cellular substrates and promoting cell death. 2. **Cell death**: Casp3 is also involved in other forms of cell death, including pyroptosis and necrosis. 3. **Immune responses**: Casp3 is activated by death receptors and modulates the immune response by regulating cytokine production and T cell proliferation. 4. **Inflammation**: Casp3 is involved in the regulation of inflammation by modulating the production of pro-inflammatory cytokines. 5. **Cell differentiation**: Casp3 is required for the differentiation of certain cell types, including keratinocytes and neurons. **Clinical Significance:** Dysregulation of Casp3 has been implicated in various diseases, including: 1. **Cancer**: Casp3 is often overexpressed in cancer cells, contributing to resistance to chemotherapy and radiotherapy. 2. **Neurodegenerative disorders**: Casp3 is involved in the pathogenesis of neurodegenerative diseases, including Alzheimer's disease, Parkinson's disease, and Huntington's disease. 3. **Autoimmune conditions**: Casp3 is implicated in the regulation of immune responses and the pathogenesis of autoimmune diseases, including rheumatoid arthritis and multiple sclerosis. 4. **Inflammatory disorders**: Casp3 is involved in the regulation of inflammation and the pathogenesis of inflammatory disorders, including asthma and chronic obstructive pulmonary disease (COPD). In conclusion, Caspase 3 is a critical component of the apoptotic machinery, playing a pivotal role in programmed cell death and other cellular processes. Its dysregulation has been linked to various diseases, highlighting the importance of understanding its function and regulation in the context of human health and disease.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

SREBP cleavage activity 1

Genular Protein ID: 2558045105

Symbol: CASP3_HUMAN

Name: SREBP cleavage activity 1

UniProtKB Accession Codes:

P42574 A8K5M2 D3DP53 Q96AN1 Q96KP2

Database IDs:

Citations:

PubMed ID: 7983002

Title: CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 beta-converting enzyme.

PubMed ID: 7983002

DOI: 10.1016/s0021-9258(18)47344-9

PubMed ID: 7774019

Title: Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase.

PubMed ID: 7774019

DOI: 10.1016/0092-8674(95)90541-3

PubMed ID: 15003516

Title: Caspase 3 activation is controlled by a sequence located in the N-terminus of its large subunit.

PubMed ID: 15003516

DOI: 10.1016/j.bbrc.2004.02.021

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 7596430

Title: Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis.

PubMed ID: 7596430

DOI: 10.1038/376037a0

PubMed ID: 8755496

Title: In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains.

PubMed ID: 8755496

DOI: 10.1073/pnas.93.15.7464

PubMed ID: 8696339

Title: Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract.

PubMed ID: 8696339

DOI: 10.1038/ng0896-442

PubMed ID: 9334240

Title: Involvement of caspase-1 and caspase-3 in the production and processing of mature human interleukin 18 in monocytic THP.1 cells.

PubMed ID: 9334240

DOI: 10.1074/jbc.272.42.26595

PubMed ID: 10497198

Title: Cleavage of automodified poly(ADP-ribose) polymerase during apoptosis. Evidence for involvement of caspase-7.

PubMed ID: 10497198

DOI: 10.1074/jbc.274.40.28379

PubMed ID: 10213689

Title: Fas-induced caspase denitrosylation.

PubMed ID: 10213689

DOI: 10.1126/science.284.5414.651

PubMed ID: 15200957

Title: Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3 ubiquitin ligase.

PubMed ID: 15200957

DOI: 10.1016/j.molcel.2004.05.018

PubMed ID: 16374543

Title: Nuclear caspase-3 and caspase-7 activation, and poly(ADP-ribose) polymerase cleavage are early events in camptothecin-induced apoptosis.

PubMed ID: 16374543

DOI: 10.1007/s10495-005-3276-y

PubMed ID: 18723680

Title: Executioner caspase-3 and caspase-7 are functionally distinct proteases.

PubMed ID: 18723680

DOI: 10.1073/pnas.0707715105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 20566630

Title: Identification of functional regions defining different activity in caspase-3 and caspase-7 within cells.

PubMed ID: 20566630

DOI: 10.1074/jbc.m110.126573

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21357690

Title: RET modulates cell adhesion via its cleavage by caspase in sympathetic neurons.

PubMed ID: 21357690

DOI: 10.1074/jbc.m110.195461

PubMed ID: 22223895

Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.

PubMed ID: 22223895

DOI: 10.1074/mcp.m111.015131

PubMed ID: 23152800

Title: OGDHL is a modifier of AKT-dependent signaling and NF-kappaB function.

PubMed ID: 23152800

DOI: 10.1371/journal.pone.0048770

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 23845944

Title: Xk-Related protein 8 and CED-8 promote phosphatidylserine exposure in apoptotic cells.

PubMed ID: 23845944

DOI: 10.1126/science.1236758

PubMed ID: 28459430

Title: Chemotherapy drugs induce pyroptosis through caspase-3 cleavage of a gasdermin.

PubMed ID: 28459430

DOI: 10.1038/nature22393

PubMed ID: 28045099

Title: Cleavage of DFNA5 by caspase-3 during apoptosis mediates progression to secondary necrotic/pyroptotic cell death.

PubMed ID: 28045099

DOI: 10.1038/ncomms14128

PubMed ID: 30878284

Title: Apoptotic caspases suppress type i interferon production via the cleavage of cGAS, MAVS, and IRF3.

PubMed ID: 30878284

DOI: 10.1016/j.molcel.2019.02.013

PubMed ID: 33725486

Title: Caspase cleavage releases a nuclear protein fragment that stimulates phospholipid scrambling at the plasma membrane.

PubMed ID: 33725486

DOI: 10.1016/j.molcel.2021.02.025

PubMed ID: 35446120

Title: Calmodulin binding activates chromobacterium CopC effector to ADP-riboxanate host apoptotic caspases.

PubMed ID: 35446120

DOI: 10.1128/mbio.00690-22

PubMed ID: 35338844

Title: Pathogen hijacks programmed cell death signaling by arginine ADPR-deacylization of caspases.

PubMed ID: 35338844

DOI: 10.1016/j.molcel.2022.03.010

PubMed ID: 37993714

Title: Recognition and maturation of IL-18 by caspase-4 noncanonical inflammasome.

PubMed ID: 37993714

DOI: 10.1038/s41586-023-06742-w

PubMed ID: 36758104

Title: Structures of BIRC6-client complexes provide a mechanism of SMAC-mediated release of caspases.

PubMed ID: 36758104

DOI: 10.1126/science.ade5750

PubMed ID: 36758106

Title: Structural basis for SMAC-mediated antagonism of caspase inhibition by the giant ubiquitin ligase BIRC6.

PubMed ID: 36758106

DOI: 10.1126/science.ade8840

PubMed ID: 8673606

Title: The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis.

PubMed ID: 8673606

DOI: 10.1038/nsb0796-619

PubMed ID: 9045680

Title: Structure of recombinant human CPP32 in complex with the tetrapeptide acetyl-Asp-Val-Ala-Asp fluoromethyl ketone.

PubMed ID: 9045680

DOI: 10.1074/jbc.272.10.6539

PubMed ID: 10821855

Title: Potent and selective nonpeptide inhibitors of caspases 3 and 7 inhibit apoptosis and maintain cell functionality.

PubMed ID: 10821855

DOI: 10.1074/jbc.275.21.16007

PubMed ID: 23650375

Title: Structural snapshots reveal distinct mechanisms of procaspase-3 and -7 activation.

PubMed ID: 23650375

DOI: 10.1073/pnas.1306759110

PubMed ID: 36423631

Title: Structural insights into caspase ADPR deacylization catalyzed by a bacterial effector and host calmodulin.

PubMed ID: 36423631

DOI: 10.1016/j.molcel.2022.10.032

Sequence Information:

Length: 277
Mass: 31608
Checksum: 2F35CD3BCF7FF64A
Sequence:

MENTENSVDS KSIKNLEPKI IHGSESMDSG ISLDNSYKMD YPEMGLCIII NNKNFHKSTG 
MTSRSGTDVD AANLRETFRN LKYEVRNKND LTREEIVELM RDVSKEDHSK RSSFVCVLLS 
HGEEGIIFGT NGPVDLKKIT NFFRGDRCRS LTGKPKLFII QACRGTELDC GIETDSGVDD 
DMACHKIPVE ADFLYAYSTA PGYYSWRNSK DGSWFIQSLC AMLKQYADKL EFMHILTRVN 
RKVATEFESF SFDATFHAKK QIPCIVSMLT KELYFYH

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: CASP3

Associated with

Cells (max top 100)

Other Information

CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 beta-converting enzyme. PubMed ID: 7983002

Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. PubMed ID: 7774019

Caspase 3 activation is controlled by a sequence located in the N-terminus of its large subunit. PubMed ID: 15003516

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis. PubMed ID: 7596430

In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains. PubMed ID: 8755496

Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract. PubMed ID: 8696339

Involvement of caspase-1 and caspase-3 in the production and processing of mature human interleukin 18 in monocytic THP.1 cells. PubMed ID: 9334240

Cleavage of automodified poly(ADP-ribose) polymerase during apoptosis. Evidence for involvement of caspase-7. PubMed ID: 10497198

Fas-induced caspase denitrosylation. PubMed ID: 10213689

Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3 ubiquitin ligase. PubMed ID: 15200957

Nuclear caspase-3 and caspase-7 activation, and poly(ADP-ribose) polymerase cleavage are early events in camptothecin-induced apoptosis. PubMed ID: 16374543

Executioner caspase-3 and caspase-7 are functionally distinct proteases. PubMed ID: 18723680

Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. PubMed ID: 19413330

Identification of functional regions defining different activity in caspase-3 and caspase-7 within cells. PubMed ID: 20566630

Initial characterization of the human central proteome. PubMed ID: 21269460

RET modulates cell adhesion via its cleavage by caspase in sympathetic neurons. PubMed ID: 21357690

Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features. PubMed ID: 22223895

OGDHL is a modifier of AKT-dependent signaling and NF-kappaB function. PubMed ID: 23152800

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

Xk-Related protein 8 and CED-8 promote phosphatidylserine exposure in apoptotic cells. PubMed ID: 23845944

Chemotherapy drugs induce pyroptosis through caspase-3 cleavage of a gasdermin. PubMed ID: 28459430

Cleavage of DFNA5 by caspase-3 during apoptosis mediates progression to secondary necrotic/pyroptotic cell death. PubMed ID: 28045099

Apoptotic caspases suppress type i interferon production via the cleavage of cGAS, MAVS, and IRF3. PubMed ID: 30878284

Caspase cleavage releases a nuclear protein fragment that stimulates phospholipid scrambling at the plasma membrane. PubMed ID: 33725486

Calmodulin binding activates chromobacterium CopC effector to ADP-riboxanate host apoptotic caspases. PubMed ID: 35446120

Pathogen hijacks programmed cell death signaling by arginine ADPR-deacylization of caspases. PubMed ID: 35338844

Recognition and maturation of IL-18 by caspase-4 noncanonical inflammasome. PubMed ID: 37993714

Structures of BIRC6-client complexes provide a mechanism of SMAC-mediated release of caspases. PubMed ID: 36758104

Structural basis for SMAC-mediated antagonism of caspase inhibition by the giant ubiquitin ligase BIRC6. PubMed ID: 36758106

The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis. PubMed ID: 8673606

Structure of recombinant human CPP32 in complex with the tetrapeptide acetyl-Asp-Val-Ala-Asp fluoromethyl ketone. PubMed ID: 9045680

Potent and selective nonpeptide inhibitors of caspases 3 and 7 inhibit apoptosis and maintain cell functionality. PubMed ID: 10821855

Structural snapshots reveal distinct mechanisms of procaspase-3 and -7 activation. PubMed ID: 23650375

Structural insights into caspase ADPR deacylization catalyzed by a bacterial effector and host calmodulin. PubMed ID: 36423631