C7GVJ8 · FEN1_YEAS2

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.

138250100150200250300350
TypeIDPosition(s)Description
Binding site34Mg2+ 1 (UniProtKB | ChEBI)
Binding site47DNA (UniProtKB | ChEBI)
Binding site71DNA (UniProtKB | ChEBI)
Binding site87Mg2+ 1 (UniProtKB | ChEBI)
Binding site156DNA (UniProtKB | ChEBI)
Binding site156Mg2+ 1 (UniProtKB | ChEBI)
Binding site158Mg2+ 1 (UniProtKB | ChEBI)
Binding site177Mg2+ 2 (UniProtKB | ChEBI)
Binding site179Mg2+ 2 (UniProtKB | ChEBI)
Binding site229DNA (UniProtKB | ChEBI)
Binding site231DNA (UniProtKB | ChEBI)
Binding site231Mg2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmitochondrion
Cellular Componentnucleolus
Cellular Componentnucleoplasm
Molecular Function5'-3' exonuclease activity
Molecular Function5'-flap endonuclease activity
Molecular FunctionDNA binding
Molecular Functionmagnesium ion binding
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
      RAD27
    • Synonyms
      FEN1
    • ORF names
      C1Q_04506

Organism names

Accessions

  • Primary accession
    C7GVJ8

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_00004035961-382Flap 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 RAD27 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.

Structure

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region1-105N-domain
Region120-251I-domain
Region339-347Interaction with PCNA
Region358-382Disordered
Compositional bias359-373Basic and acidic residues

Sequence similarities

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    382
  • Mass (Da)
    43,279
  • Last updated
    2009-10-13 v1
  • Checksum
    1F54B08720121C8C
MGIKGLNAIISEHVPSAIRKSDIKSFFGRKVAIDASMSLYQFLIAVRQQDGGQLTNEAGETTSHLMGMFYRTLRMIDNGIKPCYVFDGKPPDLKSHELTKRSSRRVETEKKLAEATTELEKMKQERRLVKVSKEHNEEAQKLLGLMGIPYIIAPTEAEAQCAELAKKGKVYAAASEDMDTLCYRTPFLLRHLTFSEAKKEPIHEIDTELVLRGLDLTIEQFVDLCIMLGCDYCESIRGVGPVTALKLIKTHGSIEKIVEFIESGESNNTKWKIPEDWPYKQARMLFLDPEVIDGNEINLKWSPPKEKELIEYLCDDKKFSEERVKSGISRLKKGLKSGIQGRLDGFFQVVPKTKEQLAAAAKRAQENKKLNKNKNKVTKGRR

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias359-373Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ACFL01000357
EMBL· GenBank· DDBJ
EEU05165.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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