TREX2

Protein-coding gene in the species Homo sapiens
TREX2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1Y97

Identifiers
AliasesTREX2, three prime repair exonuclease 2
External IDsOMIM: 300370; MGI: 1346343; HomoloGene: 8046; GeneCards: TREX2; OMA:TREX2 - orthologs
Gene location (Human)
X chromosome (human)
Chr.X chromosome (human)[1]
X chromosome (human)
Genomic location for TREX2
Genomic location for TREX2
BandXq28Start153,444,473 bp[1]
End153,470,587 bp[1]
Gene location (Mouse)
X chromosome (mouse)
Chr.X chromosome (mouse)[2]
X chromosome (mouse)
Genomic location for TREX2
Genomic location for TREX2
BandX|X A7.3Start72,477,311 bp[2]
End72,478,950 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • skin of abdomen

  • skin of leg

  • ascending aorta

  • Descending thoracic aorta

  • right coronary artery

  • tibial arteries

  • granulocyte

  • left coronary artery

  • ectocervix

  • spleen
Top expressed in
  • esophagus

  • lip

  • embryo

  • embryo

  • skin of external ear

  • skin of abdomen

  • submandibular gland

  • skin of back

  • stomach

  • belly cord
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • nuclease activity
  • exodeoxyribonuclease III activity
  • exonuclease activity
  • hydrolase activity
  • protein homodimerization activity
  • magnesium ion binding
  • 3'-5'-exodeoxyribonuclease activity
  • metal ion binding
  • nucleic acid binding
  • 3'-5' exonuclease activity
Cellular component
  • nucleus
Biological process
  • DNA repair
  • cellular response to DNA damage stimulus
  • nucleic acid phosphodiester bond hydrolysis
  • DNA metabolic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

11219

24102

Ensembl

ENSG00000183479

ENSMUSG00000031372

UniProt

Q9BQ50

Q9R1A9

RefSeq (mRNA)

NM_080701
NM_080699
NM_080700

NM_011907

RefSeq (protein)

NP_542432

NP_036037

Location (UCSC)Chr X: 153.44 – 153.47 MbChr X: 72.48 – 72.48 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Three prime repair exonuclease 2 is an enzyme that in humans is encoded by the TREX2 gene.[5][6]

This gene encodes a protein with 3' exonuclease activity. Enzymes with this activity are involved in DNA replication, repair, and recombination. Similarity to an E. coli protein suggests that this enzyme may be a subunit of DNA polymerase III, which does not have intrinsic exonuclease activity.[6]

Mutations in this gene may lead to Aicardi-Goutieres syndrome

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000183479 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031372 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Mazur DJ, Perrino FW (Aug 1999). "Identification and expression of the TREX1 and TREX2 cDNA sequences encoding mammalian 3'-->5' exonucleases". J Biol Chem. 274 (28): 19655–60. doi:10.1074/jbc.274.28.19655. PMID 10391904.
  6. ^ a b "Entrez Gene: TREX2 three prime repair exonuclease 2".

Further reading

  • Shevelev IV, Hübscher U (2002). "The 3' 5' exonucleases". Nat. Rev. Mol. Cell Biol. 3 (5): 364–76. doi:10.1038/nrm804. PMID 11988770. S2CID 31605786.
  • Esposito T, Ciccodicola A, Flagiello L, et al. (1997). "Expressed STSs and transcription of human Xq28". Gene. 187 (2): 185–91. doi:10.1016/S0378-1119(96)00772-X. PMID 9099879.
  • Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
  • Li T, Duan W, Yang H, et al. (2001). "Identification of two proteins, S14 and UIP1, that interact with UCH37". FEBS Lett. 488 (3): 201–5. Bibcode:2001FEBSL.488..201L. doi:10.1016/S0014-5793(00)02436-4. hdl:10536/DRO/DU:30009147. PMID 11163772. S2CID 40717095.
  • Simpson JC, Wellenreuther R, Poustka A, et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMC 1083732. PMID 11256614.
  • Mazur DJ, Perrino FW (2001). "Structure and expression of the TREX1 and TREX2 3' --> 5' exonuclease genes". J. Biol. Chem. 276 (18): 14718–27. doi:10.1074/jbc.M010051200. PMID 11278605.
  • Mazur DJ, Perrino FW (2001). "Excision of 3' termini by the Trex1 and TREX2 3'-->5' exonucleases. Characterization of the recombinant proteins". J. Biol. Chem. 276 (20): 17022–9. doi:10.1074/jbc.M100623200. PMID 11279105.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Shevelev IV, Beliakova NV, Kravetskaia TP, Krutiakov VM (2003). "[The correcting role of autonomous 3'-->5' exonucleases in mammalian multienzyme DNA polymerase complexes]". Mol. Biol. (Mosk.). 36 (6): 1055–61. PMID 12500544.
  • Shevelev IV, Ramadan K, Hübscher U (2004). "The TREX2 3'-->5' exonuclease physically interacts with DNA polymerase delta and increases its accuracy". ScientificWorldJournal. 2: 275–81. doi:10.1100/tsw.2002.99. PMC 6009725. PMID 12806015.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Wiemann S, Arlt D, Huber W, et al. (2004). "From ORFeome to biology: a functional genomics pipeline". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
  • Perrino FW, Krol A, Harvey S, et al. (2005). "Sequence variants in the 3'-->5' deoxyribonuclease TREX2: identification in a genetic screen and effects on catalysis by the recombinant proteins". Adv. Enzyme Regul. 44: 37–49. doi:10.1016/j.advenzreg.2003.11.010. PMID 15581481.
  • Perrino FW, Harvey S, McMillin S, Hollis T (2005). "The human TREX2 3' -> 5'-exonuclease structure suggests a mechanism for efficient nonprocessive DNA catalysis". J. Biol. Chem. 280 (15): 15212–8. doi:10.1074/jbc.M500108200. PMID 15661738.
  • Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  • Mehrle A, Rosenfelder H, Schupp I, et al. (2006). "The LIFEdb database in 2006". Nucleic Acids Res. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.
  • Hahn Y, Lee B (2007). "Human-specific nonsense mutations identified by genome sequence comparisons". Hum. Genet. 119 (1–2): 169–78. doi:10.1007/s00439-005-0125-6. PMID 16395595. S2CID 21059468.
  • Chen MJ, Ma SM, Dumitrache LC, Hasty P (2007). "Biochemical and cellular characteristics of the 3' -> 5' exonuclease TREX2". Nucleic Acids Res. 35 (8): 2682–94. doi:10.1093/nar/gkm151. PMC 1885668. PMID 17426129.
  • Parra D, Manils J, Castellana B, Viña-Vilaseca A, Morán-Salvador E, Vázquez-Villoldo N, Tarancón G, Borràs M, Sancho S, Benito C, Ortega S, and Soler C (2009). "Increased Susceptibility to Skin Carcinogenesis in TREX2 Knockout Mice". Cancer Research. 69 (16): 6676–84. doi:10.1158/0008-5472.CAN-09-1208. PMID 19654293.
  • Overview of all the structural information available in the PDB for UniProt: Q9BQ50 (Human Three prime repair exonuclease 2) at the PDBe-KB.
  • Overview of all the structural information available in the PDB for UniProt: Q9R1A9 (Mouse Three prime repair exonuclease 2) at the PDBe-KB.
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  • 1y97: The human TREX2 3' exonuclease structure suggests a mechanism for efficient non-processive DNA catalysis
    1y97: The human TREX2 3' exonuclease structure suggests a mechanism for efficient non-processive DNA catalysis
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