A7RRJ0 · FEN1_NEMVE

Function

function

Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.

Features

Showing features for binding site.

137750100150200250300350
TypeIDPosition(s)Description
Binding site34Mg2+ 1 (UniProtKB | ChEBI)
Binding site47DNA (UniProtKB | ChEBI)
Binding site70DNA (UniProtKB | ChEBI)
Binding site86Mg2+ 1 (UniProtKB | ChEBI)
Binding site158DNA (UniProtKB | ChEBI)
Binding site158Mg2+ 1 (UniProtKB | ChEBI)
Binding site160Mg2+ 1 (UniProtKB | ChEBI)
Binding site179Mg2+ 2 (UniProtKB | ChEBI)
Binding site181Mg2+ 2 (UniProtKB | ChEBI)
Binding site231DNA (UniProtKB | ChEBI)
Binding site233DNA (UniProtKB | ChEBI)
Binding site233Mg2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmitochondrion
Cellular Componentnucleolus
Cellular Componentnucleoplasm
Cellular Componentnucleus
Molecular Function5'-3' exonuclease activity
Molecular Function5'-flap endonuclease activity
Molecular FunctionDNA binding
Molecular Functionmagnesium ion binding
Molecular Functionmanganese ion binding
Molecular FunctionRNA-DNA hybrid ribonuclease activity
Biological Processbase-excision repair
Biological ProcessDNA replication, removal of RNA primer

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Flap endonuclease 1
  • EC number
  • Short names
    FEN-1
  • Alternative names
    • Flap structure-specific endonuclease 1

Gene names

    • Name
      FEN1
    • ORF names
      v1g201054

Organism names

Accessions

  • Primary accession
    A7RRJ0

Proteomes

Subcellular Location

Nucleus, nucleolus
Nucleus, nucleoplasm
Mitochondrion
Note: Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage.

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004035101-377Flap endonuclease 1

Post-translational modification

Phosphorylated. Phosphorylation upon DNA damage induces relocalization to the nuclear plasma.

Keywords

Interaction

Subunit

Interacts with PCNA. Three molecules of FEN1 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-104N-domain
Region122-253I-domain
Region336-344Interaction with PCNA
Region337-377Disordered

Sequence similarities

Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    377
  • Mass (Da)
    42,468
  • Last updated
    2007-10-02 v1
  • Checksum
    9122B8C8703BE613
MGIQGLAKLLGDIAPSGIKENEIKNYFGRKIAIDASMSIYQFLIAVRSDGSQLTNEAGETTSHLMGLFYRTIRMVENGIKPVYVFDGKPPQLKSGELAKRTERREEAQKALSKAEEAGDTENIDKFSRRLVRVTKEHNEECKQLLKLMGIPYVEAPCEAEAQCAALVKSGKVYATGTEDMDALTFGTTVMLRHLTFSEAKKMPIKEFHLQNVLSEAGLSQDEFIDLCILLGCDYCDSIKGIGPKRSVDLIRQHRSIDKILENIDTSKHPPPENWLYKEARELFKNPEVRNPEEIELKWEEPNEEALVTFMCQEKGFSEDRIRSGIKKLTKARHGSTQGRLDSFFKVLPSPANKRKLQDGKGSQNKKAKTGGKFKRPK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DS469531
EMBL· GenBank· DDBJ
EDO45961.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp