Exonuclease 1

EXO1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesEXO1, HEX1, hExoI, exonuclease 1
External IDsOMIM: 606063; MGI: 1349427; HomoloGene: 31352; GeneCards: EXO1; OMA:EXO1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_003686
NM_006027
NM_130398
NM_001319224

NM_012012

RefSeq (protein)

NP_001306153
NP_003677
NP_006018
NP_569082

NP_036142

Location (UCSC)Chr 1: 241.85 – 241.9 MbChr 1: 175.71 – 175.74 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Exonuclease 1 is an enzyme that in humans is encoded by the EXO1 gene.[5][6][7]

This gene encodes a protein with 5' to 3' exonuclease activity as well as RNase activity (endonuclease activity cleaving RNA on DNA/RNA hybrid).[8] It is similar to the Saccharomyces cerevisiae protein Exo1 which interacts with Msh2 and which is involved in DNA mismatch repair and homologous recombination. Alternative splicing of this gene results in three transcript variants encoding two different isoforms.[7]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000174371Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000039748Ensembl, 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. ^ Wilson DM III, Carney JP, Coleman MA, Adamson AW, Christensen M, Lamerdin JE (September 1998). "Hex1: a new human Rad2 nuclease family member with homology to yeast exonuclease 1". Nucleic Acids Res. 26 (16): 3762–8. doi:10.1093/nar/26.16.3762. PMC 147753. PMID 9685493.
  6. ^ Schmutte C, Marinescu RC, Sadoff MM, Guerrette S, Overhauser J, Fishel R (November 1998). "Human exonuclease I interacts with the mismatch repair protein hMSH2". Cancer Res. 58 (20): 4537–42. PMID 9788596.
  7. ^ a b "Entrez Gene: EXO1 exonuclease 1".
  8. ^ Qiu J, Qian Y, Chen V, Guan MX, Shen B (June 1999). "Human exonuclease 1 functionally complements its yeast homologues in DNA recombination, RNA primer removal, and mutation avoidance". J. Biol. Chem. 274 (25): 17893–900. doi:10.1074/jbc.274.25.17893. PMID 10364235.