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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Caspase-3

UniprotKB/SwissProt ID: CASP3_HUMAN (P42574)

Gene Name: CASP3

Synonyms: CPP32

Organism: Homo sapiens (Human).

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.

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm.

PDB :
( If your security settings prevent Jmol from running, please register http://140.138.144.145/ as a safe location in your Java settings. )

Protein disease:
Disease database Database Entry Disease information
KEGGH00020 Colorectal cancer
Network with metabolic pathway:
Kegg map ID Pathway Link
map05014Amyotrophic lateral sclerosis (ALS)
map05120Epithelial cell signaling in Helicobacter pylori infection
map05134Legionellosis
map04115p53 signaling pathway
map04210Apoptosis
map04650Natural killer cell mediated cytotoxicity
map04726Serotonergic synapse
map05133Pertussis
map05145Toxoplasmosis
map05146Amoebiasis
map05210Colorectal cancer
map05416Viral myocarditis
map04010MAPK signaling pathway
map05010Alzheimer's disease
map05012Parkinson's disease
map05016Huntington's disease
map05152Tuberculosis
map05161Hepatitis B
map05168Herpes simplex infection
map05200Pathways in cancer
map05203Viral carcinogenesis
Graphical Visualization of S-nitrosylation Sites:
Overview of Protein S-nitrosylation Sites with Functional and Structural Information
InterPro ID Domain
IPR001309
IPR002138
IPR002398
IPR011600
IPR015470
IPR015917
3D Structure Databases:
3D structure databases
EntryMethodResolution (A)ChainPositionsView
1CP3 X-ray 2.30 A A/B1-277Link
1GFW X-ray 2.80 A A29-175Link
B181-277
1I3O X-ray 2.70 A A/C1-175Link
1NME X-ray 1.60 A A29-174Link
B186-277
1NMQ X-ray 2.40 A A/B29-277Link
1NMS X-ray 1.70 A A/B29-277Link
1PAU X-ray 2.50 A A29-175Link
1QX3 X-ray 1.90 A A29-277Link
1RE1 X-ray 2.50 A A29-175Link
1RHJ X-ray 2.20 A A/C29-175Link
B/D176-277
1RHK X-ray 2.50 A A29-175Link
1RHM X-ray 2.50 A A/C29-175Link
B/D176-277
1RHQ X-ray 3.00 A A/D29-175Link
1RHR X-ray 3.00 A A29-175Link
B176-277
1RHU X-ray 2.51 A A29-175Link
2C1E X-ray 1.77 A A29-175Link
B176-277
2C2K X-ray 1.87 A A29-175Link
2C2M X-ray 1.94 A A29-175Link
B176-277
2C2O X-ray 2.45 A A29-175Link
2CDR X-ray 1.70 A A29-175Link
B176-277
2CJX X-ray 1.70 A A29-175Link
2CJY X-ray 1.67 A A29-175Link
B176-277
2CNK X-ray 1.75 A A29-175Link
2CNL X-ray 1.67 A A29-175Link
B176-277
2CNN X-ray 1.70 A A29-175Link
2CNO X-ray 1.95 A A29-175Link
B176-277
2DKO X-ray 1.06 A A29-174Link
2H5I X-ray 1.69 A A29-174Link
B184-277
2H5J X-ray 2.00 A A/C29-174Link
2H65 X-ray 2.30 A A/C29-174Link
B/D184-277
2J30 X-ray 1.40 A A29-277Link
2J31 X-ray 1.50 A A29-277Link
2J32 X-ray 1.30 A A29-277Link
2J33 X-ray 2.00 A A29-277Link
2XYG X-ray 1.54 A A29-174Link
2XYH X-ray 1.89 A A29-174Link
B185-277
2XYP X-ray 1.86 A A29-174Link
2XZD X-ray 2.10 A A/C29-175Link
B/D176-277
2XZT X-ray 2.70 A A/C29-175Link
2Y0B X-ray 2.10 A A/C29-175Link
B/D176-277
3DEH X-ray 2.50 A A/B/C/D29-277Link
3DEI X-ray 2.80 A A/B/C/D29-277Link
3DEJ X-ray 2.60 A A/B/C/D29-277Link
3DEK X-ray 2.40 A A/B/C/D29-277Link
3EDQ X-ray 1.61 A A/C29-175Link
3GJQ X-ray 2.60 A A/C29-175Link
B/D176-277
3GJR X-ray 2.20 A A/C29-175Link
3GJS X-ray 1.90 A A/C29-175Link
B/D176-277
3GJT X-ray 2.20 A A/C29-175Link
3H0E X-ray 2.00 A A/B29-277Link
3ITN X-ray 1.63 A A29-277Link
3KJF X-ray 2.00 A A29-175Link
B176-277
3PCX X-ray 1.50 A A29-277Link
3PD0 X-ray 2.00 A A29-277Link
3PD1 X-ray 1.62 A A29-277Link
4DCJ X-ray 1.70 A A/D29-175Link
B/E176-277
4DCO X-ray 1.70 A A/D29-175Link
4DCP X-ray 1.70 A A/D29-175Link
B/E176-277
4EHA X-ray 1.70 A A/C1-277Link
4EHD X-ray 1.58 A A1-277Link
4EHF X-ray 1.66 A A1-277Link
4EHH X-ray 1.78 A A1-277Link
4EHK X-ray 1.67 A A/C1-277Link
4EHL X-ray 1.80 A A/C1-277Link
4EHN X-ray 1.69 A A1-277Link
4JJE X-ray 1.48 A A29-277Link
4JQY X-ray 2.50 A A/B34-277Link
4JQZ X-ray 2.89 A A/B34-277Link
4JR0 X-ray 1.80 A A/B34-277Link
The S-nitrosylation sites of CASP3_HUMAN

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site Substrate Motifs PubMed ID Experiment
1163GKPKLFIIQA C RGTELDCGIE CCCEEEEEEC C CCCCCCCCCC 2.06%HC1122178444-
2163GKPKLFIIQA C RGTELDCGIE CCCEEEEEEC C CCCCCCCCCC 2.06%HC119034139in vivo