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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P42574: Variant p.Glu190Asp

Caspase-3
Gene: CASP3
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Variant information Variant position: help 190 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LB/B The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance

Residue change: help From Glutamate (E) to Aspartate (D) at position 190 (E190D, p.Glu190Asp). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Similar physico-chemical property. Both residues are medium size and acidic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 2 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page

Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 190 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 277 The length of the canonical sequence.
Location on the sequence: help CGIETDSGVDDDMACHKIPV E ADFLYAYSTAPGYYSWRNSK The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: help The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human                         CGIETDSGVDDDMACHKIPVEADFLYAYSTAPGYYSWRNSK

                              CGIETDSGIEDDMACQKIPVEADFLYAYSTAPGYYSWRNSK

Chimpanzee                    CGIETDSGVDDDMACHKIPVEADFLYAYSTAPGYYSWRNSK

Mouse                         CGIETDSGTDEEMACQKIPVEADFLYAYSTAPGYYSWRNSK

Rat                           CGIETDSGTDDDMACQKIPVEADFLYAYSTAPGYYSWRNSR

Pig                           CGIETDSGTEDDMACQKIPVEADFLYAYSTAPGYYSWRNSK

Bovine                        CGIETDSGAEDDMACQKIPVEADFLYAYSTAPGYFSWRNAK

Rabbit                        SGIETDSGVDYDMACQKIPVEADFLYAYSTAPGYYSWRNSE

Cat                           CGIETDSGTEDDIACQKIPVEADFLYAYSTAPGYYSWRNSK

Xenopus laevis                SGIETDSCSEPREEIQRIPVEADFLYAYSTVPGYCSWRDKM

Sequence annotation in neighborhood: help The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
  • Type: the type of sequence feature.
  • Positions: endpoints of the sequence feature.
  • Description: contains additional information about the feature.
TypePositionsDescription
Chain 176 – 277 Caspase-3 subunit p12
Modified residue 207 – 207 (Microbial infection) ADP-riboxanated arginine
Mutagenesis 175 – 175 D -> A. In P3-D3A mutant; abolished cleavage and activation, leading to prevent thiol protease activity; when associated with A-9 and A-28.
Mutagenesis 207 – 207 R -> A. Abolished ADP-riboxanation by C.violaceum CopC.
Turn 189 – 192



Literature citations
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)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; VARIANT ASP-190; TISSUE SPECIFICITY; 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)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; SUBCELLULAR LOCATION; VARIANT ASP-190; 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)
Cited for: PROTEIN SEQUENCE OF 29-46 AND 176-193; FUNCTION; CATALYTIC ACTIVITY; VARIANT ASP-190;
Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.