HAMAP rule MF_03140
General rule information
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Accession | MF_03140 |
Dates | 18-NOV-2010 (Created) 19-NOV-2022 (Last updated, Version 12) |
Name | Fen_euk |
Scope | Eukaryota |
Templates | P39748 (FEN1_HUMAN); P26793 (FEN1_YEAST); P39749 (FEN1_MOUSE): [Recover all] |
case <OC:Eukaryota>
Triggered by |
end case
Propagated annotation
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Identifier, protein and gene names
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Identifier |
|
Protein name |
|
case <OC:Saccharomyces> or <OC:Candida>
Gene name |
|
else case <OC:Schizosaccharomyces>
Gene name |
|
else case <OC:Caenorhabditis>
Gene name |
|
else case <OC:Dictyostelia>
Gene name |
|
else case <OC:Arthropoda>
Gene name |
|
else
Gene name |
|
end case
Comments
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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 | Mg(2+) 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. |
case <OC:Mammalia>
Subunit | Interacts with PCNA. Three molecules of |
else
Subunit | Interacts with PCNA. Three molecules of |
end case
Subcellular location | Nucleus, nucleolus. Nucleus, nucleoplasm. Mitochondrion. Note=Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage. |
case <OC:Mammalia>
Ptm | 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. |
end case
case <OC:Mammalia> and <FTTag:phospho187> and <FTTag:meth192>
Ptm | Methylation at #{Arg-192} by PRMT5 impedes #{Ser-187} phosphorylation and increases interaction with PCNA. |
end case
case <OC:Mammalia> and <FTTag:phospho187>
Ptm | Phosphorylation upon DNA damage induces relocalization to the nuclear plasma. Phosphorylation at #{Ser-187} by CDK2 occurs during late S-phase and results in dissociation from PCNA. |
else
Ptm | Phosphorylated. Phosphorylation upon DNA damage induces relocalization to the nuclear plasma. |
end case
Similarity | Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily. |
Keywords
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case <FTTag:acet>
end case
case <FTTag:meth>
end case
Endonuclease
Exonuclease
DNA damage
DNA repair
DNA replication
Hydrolase
Magnesium
Metal-binding
Mitochondrion
Nuclease
Nucleus
Phosphoprotein
Exonuclease
DNA damage
DNA repair
DNA replication
Hydrolase
Magnesium
Metal-binding
Mitochondrion
Nuclease
Nucleus
Phosphoprotein
Gene Ontology
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GO:0005634; Cellular component: nucleus.
GO:0005739; Cellular component: mitochondrion.
GO:0003677; Molecular function: DNA binding.
GO:0008409; Molecular function: 5'-3' exonuclease activity.
GO:0017108; Molecular function: 5'-flap endonuclease activity.
GO:0000287; Molecular function: magnesium ion binding.
GO:0006284; Biological process: base-excision repair.
GO:0043137; Biological process: DNA replication, removal of RNA primer.
GO:0005739; Cellular component: mitochondrion.
GO:0003677; Molecular function: DNA binding.
GO:0008409; Molecular function: 5'-3' exonuclease activity.
GO:0017108; Molecular function: 5'-flap endonuclease activity.
GO:0000287; Molecular function: magnesium ion binding.
GO:0006284; Biological process: base-excision repair.
GO:0043137; Biological process: DNA replication, removal of RNA primer.
Cross-references
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Pfam | PF00867; XPG_I; 1; |
PF00752; XPG_N; 1; | |
PRINTS | PR00853; XPGRADSUPER; 1; |
PROSITE | PS00841; XPG_1; 1; |
PS00842; XPG_2; 1; |
Features
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From: FEN1_HUMAN (P39748) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
REGION | 1 | 104 | N-domain | |||||||||
REGION | 122 | 253 | I-domain | |||||||||
REGION (Optional) | 336 | 344 | Interaction with PCNA | x-Q-x(2)-[ILM]-x(2)-F-[FYLI] | ||||||||
BINDING | 34 | 34 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="1 | D | ||||||||
BINDING | 86 | 86 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="1 | D | ||||||||
BINDING | 158 | 158 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="1 | E | ||||||||
BINDING | 160 | 160 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="1 | E | ||||||||
BINDING | 179 | 179 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="2 | D | ||||||||
BINDING | 181 | 181 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="2 | D | ||||||||
BINDING | 233 | 233 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="2 | D | ||||||||
BINDING | 47 | 47 | /ligand="DNA" /ligand_id="ChEBI:CHEBI:16991 | R | ||||||||
BINDING | 70 | 70 | /ligand="DNA" /ligand_id="ChEBI:CHEBI:16991 | R | ||||||||
BINDING | 158 | 158 | /ligand="DNA" /ligand_id="ChEBI:CHEBI:16991 | E | ||||||||
BINDING | 231 | 231 | /ligand="DNA" /ligand_id="ChEBI:CHEBI:16991 | G | ||||||||
BINDING | 233 | 233 | /ligand="DNA" /ligand_id="ChEBI:CHEBI:16991 | D |
case <OC:Mammalia>
end case
Additional information
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Size range | 345-672 amino acids |
Related rules | None |
Fusion | None |