Go Annotations as Summary Text (Tabular View) (GO Graph)

GO curators for mouse genes have assigned the following annotations to the gene product of Casp12. (This text reflects annotations as of Tuesday, May 21, 2013.)

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Summary from NCBI RefSeq

[Summary is not available for the mouse gene. This summary is for the human ortholog.] Caspases are cysteine proteases that cleave C-terminal aspartic acid residues on their substrate molecules. This gene is most highly related to members of the ICE subfamily of caspases that process inflammatory cytokines. In rodents, the homolog of this gene mediates apoptosis in response to endoplasmic reticulum stress. However, in humans this gene contains a polymorphism for the presence or absence of a premature stop codon. The majority of human individuals have the premature stop codon and produce a truncated non-functional protein. The read-through codon occurs primarily in individuals of African descent and carriers have endotoxin hypo-responsiveness and an increased susceptibility to severe sepsis. Several alternatively spliced transcript variants have been noted for this gene. [provided by RefSeq, Feb 2011]

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Summary text based on GO annotations supported by experimental evidence in mouse

• Researchers have inferred from direct assay, that the gene product of Casp12
  • participates in the following biological processes:
    • apoptotic process ^[5]
    • endoplasmic reticulum unfolded protein response ^[2]
    • virus-infected cell apoptotic process ^[1]
• The gene product of Casp12 has been shown to bind to the gene products of Pdcd6, Vcp. ^{[3, 4]}
• Researchers have inferred, based on genetic interactions, that the gene product of Casp12
  • participates in the following biological processes:
    • intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress based on interactions with Bak1, Bax ^[5]
  • is located in the following cellular components:
    • intracellular based on interactions with Bak1, Bax ^[5]

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Summary text based on GO annotations supported by experimental evidence in other organisms

• From comparative sequence analysis (see table for details), MGI curators have determined that the gene product of Casp12:
  • participates in the following biological processes:
    • positive regulation of apoptotic process
    • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process
    • protein autoprocessing
    • proteolysis
  • performs the following molecular functions:
    • cysteine-type peptidase activity
    • endopeptidase activity
    • protease binding
  • is located in the following cellular components:
    • cytosol
    • intracellular membrane-bounded organelle
    • nucleus

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Summary text based on GO annotations supported by structural data

• Casp12 encodes a protein or proteins that contain the following InterPro domains: Caspase Recruitment, Caspase, interleukin-1 beta convertase, Death-like domain, Peptidase C14, caspase catalytic, Peptidase C14, caspase non-catalytic subunit p10, Peptidase C14, caspase precursor p45, Peptidase C14, caspase precursor p45, core, Peptidase C14, ICE, catalytic subunit p20, Peptidase C14, ICE, catalytic subunit p20, active site, indicating that the gene product:
  • participates in the following biological processes:
    • regulation of apoptotic process
  • performs the following molecular functions:
    • cysteine-type endopeptidase activity

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Summary text for additional MGI annotations

• Automated translation to GO terms of SwissProt keywords that describe Casp12 indicates that it:
  • performs the following molecular functions:
    • hydrolase activity
• Predictions based on reviewed computational analyses of large-scale experimental data sets indicates that Casp12:
  • participates in the following biological processes:
    • induction of apoptosis
    • proteolysis
  • performs the following molecular functions:
    • peptidase activity

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References

1. Baltzis D et al. (2004) Resistance to vesicular stomatitis virus infection requires a functional cross talk between the eukaryotic translation initiation factor 2alpha kinases PERK and PKR. J Virol, 78:12747-61. (PubMed:15542627)
2. Harding HP et al. (2000) Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol Cell, 5:897-904. (PubMed:10882126)
3. Rao RV et al. (2004) Molecular components of a cell death pathway activated by endoplasmic reticulum stress. J Biol Chem, 279:177-87. (PubMed:14561754)
4. Yoneda T et al. (2001) Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress. J Biol Chem, 276:13935-40. (PubMed:11278723)
5. Zong WX et al. (2003) Bax and Bak can localize to the endoplasmic reticulum to initiate apoptosis. J Cell Biol, 162:59-69. (PubMed:12847083)

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Gene Ontology Evidence Code Abbreviations:

EXP Inferred from experiment

IC Inferred by curator

IDA Inferred from direct assay

IEA Inferred from electronic annotation

IGI Inferred from genetic interaction

IMP Inferred from mutant phenotype

IPI Inferred from physical interaction

ISS Inferred from sequence or structural similarity

ISO Inferred from sequence orthology

ISA Inferred from sequence alignment

ISM Inferred from sequence model

NAS Non-traceable author statement

ND No biological data available

RCA Reviewed computational analysis

TAS Traceable author statement

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