| Predicate | Object |
|---|---|
| rdf:type | |
| biopax3:comment |
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 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. COFACTOR: 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. 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. The C-terminal domain binds EP300. Can bind simultaneously to both PCNA and EP300. Interacts with DDX11. SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm. Mitochondrion (By similarity). Note=Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage. 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. 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. PTM: Methylation at Arg-192 by PRMT5 impedes Ser-187 phosphorylation and increases interaction with PCNA. SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily. WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/fen1/"; GENE SYNONYMS:FEN1 RAD2. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
SEQUENCE 380 AA; 42593 MW; 5154F2F6E57592C5 CRC64;
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| biopax3:xref | |
| biopax3:displayName |
FEN1_HUMAN
|
| biopax3:name |
3.1.-.-,
DNase IV,
FEN-1,
FEN1,
Flap structure-specific endonuclease 1,
MF1,
Maturation factor 1,
hFEN-1
|
| biopax3:entityFeature |
urn:biopax:ModificationFeature:FEN1_HUMAN_1,
urn:biopax:ModificationFeature:FEN1_HUMAN_10,
urn:biopax:ModificationFeature:FEN1_HUMAN_11,
urn:biopax:ModificationFeature:FEN1_HUMAN_2,
urn:biopax:ModificationFeature:FEN1_HUMAN_3,
urn:biopax:ModificationFeature:FEN1_HUMAN_4,
urn:biopax:ModificationFeature:FEN1_HUMAN_5,
urn:biopax:ModificationFeature:FEN1_HUMAN_6,
urn:biopax:ModificationFeature:FEN1_HUMAN_7,
urn:biopax:ModificationFeature:FEN1_HUMAN_8,
urn:biopax:ModificationFeature:FEN1_HUMAN_9
|
| biopax3:organism | |
| biopax3:sequence |
MGIQGLAKLIADVAPSAIRENDIKSYFGRKVAIDASMSIYQFLIAVRQGGDVLQNEEGETTSHLMGMFYRTIRMMENGIKPVYVFDGKPPQLKSGELAKRSERRAEAEKQLQQAQAAGAEQEVEKFTKRLVKVTKQHNDECKHLLSLMGIPYLDAPSEAEASCAALVKAGKVYAAATEDMDCLTFGSPVLMRHLTASEAKKLPIQEFHLSRILQELGLNQEQFVDLCILLGSDYCESIRGIGPKRAVDLIQKHKSIEEIVRRLDPNKYPVPENWLHKEAHQLFLEPEVLDPESVELKWSEPNEEELIKFMCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGSTKKKAKTGAAGKFKRGK
|
| biopax3:standardName |
Flap endonuclease 1
|