Trex2 three prime repair exonuclease 2 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Trex2provided by MGI
Official Full Name: three prime repair exonuclease 2provided by MGI
Primary source: MGI:MGI:1346343
See related: Ensembl:ENSMUSG00000031372 AllianceGenome:MGI:1346343
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Summary: Predicted to enable several functions, including 3'-5'-DNA exonuclease activity; magnesium ion binding activity; and protein homodimerization activity. Predicted to be involved in DNA catabolic process. Predicted to be located in nucleus. Predicted to be active in cytoplasm. Orthologous to human TREX2 (three prime repair exonuclease 2). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Biased expression in stomach adult (RPKM 79.1) and lung adult (RPKM 22.1) See more
Orthologs: human all
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Location:: X A7.3; X 37.31 cM

Exon count:: 2

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	X	NC_000086.8 (72477311..72478949, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	X	NC_000086.7 (73433705..73435343, complement)

Chromosome X - NC_000086.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

This study reports that lack of Trex2 results in the accumulation of DNA fragments in the cytoplasm of cornifying lingual keratinocytes and co-deletion of DNase1L2 and Trex2 causes massive accumulation of DNA fragments throughout the cornified layers of the tongue epithelium.
Title: Double deficiency of Trex2 and DNase1L2 nucleases leads to accumulation of DNA in lingual cornifying keratinocytes without activating inflammatory responses.
Structural insights into the duplex DNA processing by TREX2 have been reported.
Title: Structural insights into the duplex DNA processing of TREX2.
TREX2 acts as a critical factor in the pathogenesis of psoriasis.
Title: The Exonuclease Trex2 Shapes Psoriatic Phenotype.
A tumor suppressor role for TREX2 in skin carcinogenesis through which it contributes to keratinocyte apoptosis under conditions of genotoxic stress.
Title: Increased Susceptibility to Skin Carcinogenesis in TREX2 Knockout Mice.
Trex2 deletion caused high levels of Robertsonian translocations (RbTs) showing Trex2 is important for chromosomal maintenance.
Title: TREX2 exonuclease defective cells exhibit double-strand breaks and chromosomal fragments but not Robertsonian translocations.

Submit: New GeneRIF Correction

Variation

Go to the top of the page Help

Alleles

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

Targeted (2) 1 citation

Interactions

Go to the top of the page Help

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

Go to the top of the page Help

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables 3'-5'-DNA exonuclease activity	IBA Inferred from Biological aspect of Ancestor more info
enables 3'-5'-DNA exonuclease activity	ISO Inferred from Sequence Orthology more info
enables 3'-5'-DNA exonuclease activity	ISS Inferred from Sequence or Structural Similarity more info
enables DNA binding	ISO Inferred from Sequence Orthology more info
enables double-stranded DNA 3'-5' DNA exonuclease activity	IEA Inferred from Electronic Annotation more info
enables magnesium ion binding	ISO Inferred from Sequence Orthology more info
enables magnesium ion binding	ISS Inferred from Sequence or Structural Similarity more info
enables molecular adaptor activity	ISO Inferred from Sequence Orthology more info
enables nucleic acid binding	IEA Inferred from Electronic Annotation more info
enables protein homodimerization activity	IEA Inferred from Electronic Annotation more info
enables protein homodimerization activity	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
involved_in DNA catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in DNA metabolic process	ISO Inferred from Sequence Orthology more info
involved_in DNA metabolic process	ISS Inferred from Sequence or Structural Similarity more info
involved_in DNA repair	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 nucleus	IEA Inferred from Electronic Annotation more info

General protein information

Go to the top of the page Help

Preferred Names: three prime repair exonuclease 2

Names: 3'-5' exonuclease TREX2

NP_036037.1

EC 3.1.11.2

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

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_011907.4 → NP_036037.1 three prime repair exonuclease 2

See identical proteins and their annotated locations for NP_036037.1

Status: VALIDATED

Source sequence(s)

AF151108, BY714289

Consensus CDS

CCDS30201.1

UniProtKB/Swiss-Prot

Q9R1A9

UniProtKB/TrEMBL

Q3SXB3

Related

ENSMUSP00000033738.8, ENSMUST00000033738.8

Conserved Domains (1) summary

cd06136
Location:10 → 204

TREX1_2; DEDDh 3'-5' exonuclease domain of three prime repair exonuclease (TREX)1, TREX2, and similar proteins