Casp2 caspase 2 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Casp2provided by MGI
Official Full Name: caspase 2provided by MGI
Primary source: MGI:MGI:97295
See related: Ensembl:ENSMUSG00000029863 AllianceGenome:MGI:97295
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: ICH-1; Nedd2; CASP-2; NEDD-2
Summary: This gene encodes the evolutionarily ancient and most conserved member of the cysteine proteases that plays important role in stress-induced apoptosis, DNA repair and tumor suppression. Mice lacking the encoded protein develop normally but display cell type-specific apoptotic defects. Germ cells and oocytes from such mice were found to be resistant to cell death after treatment with chemotherapeutic drugs. [provided by RefSeq, Apr 2015]
Expression: Ubiquitous expression in thymus adult (RPKM 27.3), limb E14.5 (RPKM 22.2) and 27 other tissues See more
Orthologs: human all
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Genomic context

Location:: 6 B2.1; 6 20.54 cM

Exon count:: 12

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	6	NC_000072.7 (42241942..42259442)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	6	NC_000072.6 (42264902..42282508)

Chromosome 6 - NC_000072.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Knockdown of Golgi Stress-Responsive Caspase-2 Ameliorates HLD17-Associated AIMP2 Mutant-Mediated Inhibition of Oligodendroglial Cell Morphological Differentiation.
Title: Knockdown of Golgi Stress-Responsive Caspase-2 Ameliorates HLD17-Associated AIMP2 Mutant-Mediated Inhibition of Oligodendroglial Cell Morphological Differentiation.
MiR-17-5p protects neonatal mice from hypoxic-ischemic brain damage by targeting Casp2.
Title: MiR-17-5p protects neonatal mice from hypoxic-ischemic brain damage by targeting Casp2.
A rough Brucella mutant induced macrophage death depends on secretion activity of T4SS, but not on cellular Txnip- and Caspase-2-mediated signaling pathway.
Title: A rough Brucella mutant induced macrophage death depends on secretion activity of T4SS, but not on cellular Txnip- and Caspase-2-mediated signaling pathway.
miR-1247-3p mediates apoptosis of cerebral neurons by targeting caspase-2 in stroke.
Title: miR-1247-3p mediates apoptosis of cerebral neurons by targeting caspase-2 in stroke.
Findings suggest that Casp2 deficiency augments immune signaling pathways that may be in turn, enhance lymphomagenesis.
Title: Transcriptome profiling of caspase-2 deficient EμMyc and Th-MYCN mouse tumors identifies distinct putative roles for caspase-2 in neuronal differentiation and immune signaling.
A novel function for caspase-2 in myocyte differentiation and myogenesis.
Title: Caspase-2 is required for skeletal muscle differentiation and myogenesis.
Casp2(-/-) mice, which are more susceptible to genomic instability, are limited in their ability to respond to DNA damage and thus carry more damaged cells resulting in accelerated tumourigenesis.
Title: Caspase-2 deficiency accelerates chemically induced liver cancer in mice.
BECN1/Beclin 1 binding to viral phosphoprotein (P) induced an incomplete autophagy via activating the pathways CASP2-AMPK-AKT-MTOR and CASP2-AMPK-MAPK by decreasing CASP2.
Title: BECN1-dependent CASP2 incomplete autophagy induction by binding to rabies virus phosphoprotein.
We further generated Casp2(C320S) mutant mice to demonstrate that caspase-2 catalytic activity is essential for its function in limiting aneuploidy. Our results provide direct evidence that the apoptotic activity of caspase-2 is necessary for deleting cells with mitotic aberrations to limit aneuploidy
Title: Caspase-2-mediated cell death is required for deleting aneuploid cells.
These results provide the first evidence of caspase-2 in regulating haematopoietic stem cell and progenitor differentiation, as well as aneuploidy, in vivo.
Title: Impaired haematopoietic stem cell differentiation and enhanced skewing towards myeloid progenitors in aged caspase-2-deficient mice.

Submit: New GeneRIF Correction See all GeneRIFs (63)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (4) 1 citation
Gene trapped (1)
Targeted (3) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

Y13085 (e-PCR)
- UniSTS:159495

NoName (e-PCR)
- UniSTS:493102

RH127476 (e-PCR)
- UniSTS:210786

Casp2 (e-PCR), detects polymorphism
- UniSTS:265593

Casp2 (e-PCR), detects polymorphism
- UniSTS:259199

Casp2 (e-PCR), detects polymorphism
- UniSTS:141230

Casp2 (e-PCR), detects polymorphism
- UniSTS:141231

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables cysteine-type endopeptidase activity	ISO Inferred from Sequence Orthology more info
enables cysteine-type endopeptidase activity involved in apoptotic process	IDA Inferred from Direct Assay more info	PubMed
enables cysteine-type endopeptidase activity involved in apoptotic signaling pathway	IBA Inferred from Biological aspect of Ancestor more info
enables cysteine-type endopeptidase activity involved in execution phase of apoptosis	IEA Inferred from Electronic Annotation more info
enables cysteine-type peptidase activity	IEA Inferred from Electronic Annotation more info
enables hydrolase activity	IEA Inferred from Electronic Annotation more info
enables identical protein binding	ISO Inferred from Sequence Orthology more info
enables peptidase activity	RCA inferred from Reviewed Computational Analysis more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein domain specific binding	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
involved_in DNA damage response	NAS Non-traceable Author Statement more info	PubMed
involved_in DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest	ISO Inferred from Sequence Orthology more info
involved_in activation of cysteine-type endopeptidase activity involved in apoptotic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in apoptotic process	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within apoptotic signaling pathway	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within ectopic germ cell programmed cell death	IGI Inferred from Genetic Interaction more info	PubMed
involved_in extrinsic apoptotic signaling pathway in absence of ligand	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within extrinsic apoptotic signaling pathway in absence of ligand	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in intrinsic apoptotic signaling pathway in response to DNA damage	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within negative regulation of apoptotic process	ISO Inferred from Sequence Orthology more info	PubMed
acts_upstream_of_or_within positive regulation of apoptotic process	ISO Inferred from Sequence Orthology more info	PubMed
involved_in positive regulation of apoptotic process	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of apoptotic process	NAS Non-traceable Author Statement more info	PubMed
acts_upstream_of_or_within positive regulation of apoptotic signaling pathway	IGI Inferred from Genetic Interaction more info	PubMed
involved_in positive regulation of neuron apoptotic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in positive regulation of neuron apoptotic process	ISO Inferred from Sequence Orthology more info
involved_in protein processing	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within proteolysis	RCA inferred from Reviewed Computational Analysis more info	PubMed
involved_in regulation of apoptotic process	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
part_of endopeptidase complex	ISO Inferred from Sequence Orthology more info
located_in nucleolus	NAS Non-traceable Author Statement more info	PubMed
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: caspase-2

Names: neural precursor cell expressed developmentally down-regulated protein 2; protease ICH-1

NP_001396468.1

EC 3.4.22.55

NP_031636.1

EC 3.4.22.55

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001409539.1 → NP_001396468.1 caspase-2 isoform 2

Status: REVIEWED

Source sequence(s)

AC153915
NM_007610.3 → NP_031636.1 caspase-2 isoform 1 precursor

See identical proteins and their annotated locations for NP_031636.1

Status: REVIEWED

Source sequence(s)

AC153915

Consensus CDS

CCDS20064.1

UniProtKB/Swiss-Prot

O08737, P29594, Q3TCM0, Q8C9H7, Q8K241

Related

ENSMUSP00000031895.7, ENSMUST00000031895.13

Conserved Domains (2) summary

smart00115
Location:192 → 447

CASc; Caspase, interleukin-1 beta converting enzyme (ICE) homologues

cd08332
Location:32 → 118

CARD_CASP2; Caspase activation and recruitment domain of Caspase-2