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The annotation and conditions in this rule are derived from the following entries: P39748 (FEN1_HUMAN), P26793 (FEN1_YEAST), P39749 (FEN1_MOUSE)

If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_00614
    • taxon = Eukaryota
    • fragment ≠ the sequence is fragmented

Special conditions

    • taxon = Mammalia Subsequence at position 377 - 377 aligns to "K" in entry P39748 Subsequence at position 354 - 354 aligns to "K" in entry P39748 Subsequence at position 380 - 380 aligns to "K" in entry P39748 Subsequence at position 375 - 375 aligns to "K" in entry P39748
    • taxon = Mammalia Subsequence at position 100 - 100 aligns to "R" in entry P39748 Subsequence at position 19 - 19 aligns to "R" in entry P39748 Subsequence at position 104 - 104 aligns to "R" in entry P39748
    • taxon ≠ Mammalia Subsequence at position 187 - 187 does not align to "S" in entry P39748
    • Subsequence at position 86 - 86 aligns to "D" in entry P39748 (individually applies "Magnesium 1")
    • Subsequence at position 158 - 158 aligns to "E" in entry P39748 (individually applies "DNA substrate")
    • Subsequence at position 233 - 233 aligns to "D" in entry P39748 (individually applies "Magnesium 2")
    • Subsequence at position 158 - 158 aligns to "E" in entry P39748 (individually applies "Magnesium 1")
    • Subsequence at position 122 - 253 aligns to entry P39748 (individually applies "I-domain")
    • Subsequence at position 231 - 231 aligns to "G" in entry P39748 (individually applies "DNA substrate")
    • Subsequence at position 233 - 233 aligns to "D" in entry P39748 (individually applies "DNA substrate")
    • Subsequence at position 160 - 160 aligns to "E" in entry P39748 (individually applies "Magnesium 1")
    • Subsequence at position 34 - 34 aligns to "D" in entry P39748 (individually applies "Magnesium 1")
    • Subsequence at position 70 - 70 aligns to "R" in entry P39748 (individually applies "DNA substrate")
    • Subsequence at position 336 - 344 aligns to "x-Q-x(2)-[ILM]-x(2)-F-[FYLI]" in entry P39748 (individually applies "Interaction with PCNA")
    • Subsequence at position 179 - 179 aligns to "D" in entry P39748 (individually applies "Magnesium 2")
    • Subsequence at position 1 - 104 aligns to entry P39748 (individually applies "N-domain")
    • Subsequence at position 47 - 47 aligns to "R" in entry P39748 (individually applies "DNA substrate")
    • Subsequence at position 181 - 181 aligns to "D" in entry P39748 (individually applies "Magnesium 2")
    • taxon = Mammalia
    • Subsequence at position 192 - 192 aligns to "R" in entry P39748
    • taxon = Mammalia
    • Subsequence at position 377 - 377 aligns to "K" in entry P39748 (individually applies "N6-acetyllysine")
    • Subsequence at position 354 - 354 aligns to "K" in entry P39748 (individually applies "N6-acetyllysine")
    • Subsequence at position 380 - 380 aligns to "K" in entry P39748 (individually applies "N6-acetyllysine")
    • Subsequence at position 375 - 375 aligns to "K" in entry P39748 (individually applies "N6-acetyllysine")
    • taxon = Mammalia
    • Subsequence at position 100 - 100 aligns to "R" in entry P39748 (individually applies "Symmetric dimethylarginine; by PRMT5")
    • Subsequence at position 19 - 19 aligns to "R" in entry P39748 (individually applies "Symmetric dimethylarginine; by PRMT5")
    • Subsequence at position 104 - 104 aligns to "R" in entry P39748 (individually applies "Symmetric dimethylarginine; by PRMT5")
    • taxon = Mammalia
    • Subsequence at position 187 - 187 aligns to "S" in entry P39748

... then these annotations are applied i

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namei

  • Recommended name:
    Flap endonuclease 1 (EC:3.1.-.-)
    Short name:
    FEN-1
    Alternative name(s):
    Flap structure-specific endonuclease 1

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi

  • Name:Fen1
  • Name:repG
  • Name:crn-1
  • Name:rad2, Synonym:fen1
  • Name:RAD27, Synonym:FEN1
  • Name:FEN1

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> describes the function(s) of a protein.<p><a href='/help/function' target='_top'>More...</a></p>Functioni

  • 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 structurs 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.

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

  • Acetylated by EP300. Acetylation inhibits both endonuclease and exonuclease activity. Acetylation also reduces DNA-binding activity but does not affect interaction with PCNA or EP300.
  • Phosphorylation upon DNA damage induces relocalization to the nuclear plasma. Phosphorylation at @RESIDUE_NAME_AT_POS|Ser|187|@i by CDK2 occurs during late S-phase and results in dissociation from PCNA.
  • Phosphorylated. Phosphorylation upon DNA damage induces relocalization to the nuclear plasma.
  • Methylation at @RESIDUE_NAME_AT_POS|Arg|192|@i by PRMT5 impedes @RESIDUE_NAME_AT_POS|Ser|187|@i phosphorylation and increases interaction with PCNA.

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

  • Interacts with PCNA. Three molecules of @GENE_NAME@i bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity. The C-terminal domain binds EP300. Can bind simultaneously to both PCNA and EP300. Interacts with DDX11.
  • Interacts with PCNA. Three molecules of @GENE_NAME@i bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

  • Mg2+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.

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi

  • Magnesium 1 (to residues corresponding to position 86)
  • Magnesium 2 (to residues corresponding to position 233)
  • Magnesium 1 (to residues corresponding to position 158)
  • Magnesium 1 (to residues corresponding to position 160)
  • Magnesium 1 (to residues corresponding to position 34)
  • Magnesium 2 (to residues corresponding to position 179)
  • Magnesium 2 (to residues corresponding to position 181)

<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni

  • I-domain (to residues corresponding to positions 122 - 253)
  • Interaction with PCNA (to residues corresponding to positions 336 - 344)
  • N-domain (to residues corresponding to positions 1 - 104)

<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei

  • Symmetric dimethylarginine; by PRMT5 (to residues corresponding to position 192)
  • N6-acetyllysine (to residues corresponding to position 377)
  • N6-acetyllysine (to residues corresponding to position 354)
  • N6-acetyllysine (to residues corresponding to position 380)
  • N6-acetyllysine (to residues corresponding to position 375)
  • Symmetric dimethylarginine; by PRMT5 (to residues corresponding to position 100)
  • Symmetric dimethylarginine; by PRMT5 (to residues corresponding to position 19)
  • Symmetric dimethylarginine; by PRMT5 (to residues corresponding to position 104)
  • Phosphoserine; by CDK2 (to residues corresponding to position 187)

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei

  • DNA substrate (to residues corresponding to position 158)
  • DNA substrate (to residues corresponding to position 231)
  • DNA substrate (to residues corresponding to position 233)
  • DNA substrate (to residues corresponding to position 70)
  • DNA substrate (to residues corresponding to position 47)

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO (Gene Ontology) termsi

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