Human Gene FEN1 (ENST00000305885.3_4) from GENCODE V47lift37
  Description: flap structure-specific endonuclease 1 (from RefSeq NM_004111.6)
Gencode Transcript: ENST00000305885.3_4
Gencode Gene: ENSG00000168496.4_9
Transcript (Including UTRs)
   Position: hg19 chr11:61,560,383-61,564,710 Size: 4,328 Total Exon Count: 2 Strand: +
Coding Region
   Position: hg19 chr11:61,562,834-61,563,976 Size: 1,143 Coding Exon Count: 1 

Page IndexSequence and LinksUniProtKB CommentsPrimersMalaCardsCTD
Gene AllelesRNA-Seq ExpressionMicroarray ExpressionRNA StructureProtein StructureOther Species
GO AnnotationsmRNA DescriptionsOther NamesModel InformationMethods
Data last updated at UCSC: 2024-08-22 23:36:26

-  Sequence and Links to Tools and Databases
 
Genomic Sequence (chr11:61,560,383-61,564,710)mRNA (may differ from genome)Protein (380 aa)
Gene SorterGenome BrowserOther Species FASTAGene interactionsTable SchemaAlphaFold
BioGPSEnsemblEntrez GeneExonPrimerGeneCardsHGNC
MalacardsMGIOMIMPubMedUniProtKBWikipedia
BioGrid CRISPR DB

-  Comments and Description Text from UniProtKB
  ID: Q6FHX6_HUMAN
DESCRIPTION: RecName: Full=Flap endonuclease 1; Short=FEN-1; EC=3.1.-.-; AltName: Full=Flap structure-specific endonuclease 1;
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 (By similarity).
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 (By similarity).
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 (By similarity).
SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm. Mitochondrion. Note=Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage (By similarity).
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 (By similarity).
PTM: Methylation at Arg-192 by PRMT5 impedes Ser-187 phosphorylation and increases interaction with PCNA (By similarity).
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 (By similarity).
SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily.

-  Primer design for this transcript
 

Primer3Plus can design qPCR Primers that straddle exon-exon-junctions, which amplify only cDNA, not genomic DNA.
Click here to load the transcript sequence and exon structure into Primer3Plus

Exonprimer can design one pair of Sanger sequencing primers around every exon, located in non-genic sequence.
Click here to open Exonprimer with this transcript

To design primers for a non-coding sequence, zoom to a region of interest and select from the drop-down menu: View > In External Tools > Primer3


-  MalaCards Disease Associations
  MalaCards Gene Search: FEN1
Diseases sorted by gene-association score: xeroderma pigmentosum, group g (16), werner syndrome (14), vitelliform macular dystrophy (13), bloom syndrome (12), best vitelliform macular dystrophy (7), adenoid squamous cell carcinoma (6), uv-sensitive syndrome (5), fanconi anemia, complementation group a (2)

-  Comparative Toxicogenomics Database (CTD)
  The following chemicals interact with this gene

+  Common Gene Haplotype Alleles
  Press "+" in the title bar above to open this section.

-  RNA-Seq Expression Data from GTEx (53 Tissues, 570 Donors)
  Highest median expression: 58.44 RPKM in Cells - EBV-transformed lymphocytes
Total median expression: 353.73 RPKM



View in GTEx track of Genome Browser    View at GTEx portal     View GTEx Body Map

+  Microarray Expression Data
  Press "+" in the title bar above to open this section.

-  mRNA Secondary Structure of 3' and 5' UTRs
 
RegionFold EnergyBasesEnergy/Base
Display As
5' UTR -53.00139-0.381 Picture PostScript Text
3' UTR -218.00734-0.297 Picture PostScript Text

The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.

-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR020045 - 5-3_exonuclease_C
IPR023426 - Flap_endonuc
IPR008918 - HhH2
IPR006086 - XPG/RAD2_endonuclease
IPR019974 - XPG_CS
IPR006085 - XPG_DNA_repair_N
IPR006084 - XPGC_Rad_DNA_repair

Pfam Domains:
PF00752 - XPG N-terminal domain
PF00867 - XPG I-region

SCOP Domains:
47781 - RuvA domain 2-like
47807 - 5' to 3' exonuclease, C-terminal subdomain
88723 - PIN domain-like

ModBase Predicted Comparative 3D Structure on Q6FHX6
FrontTopSide
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.

-  Orthologous Genes in Other Species
  Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
MouseRatZebrafishD. melanogasterC. elegansS. cerevisiae
No orthologNo orthologNo orthologNo orthologGenome BrowserGenome Browser
Gene DetailsGene Details Gene DetailsGene DetailsGene Details
Gene SorterGene Sorter Gene SorterGene SorterGene Sorter
 RGDEnsembl WormBaseSGD
    Protein SequenceProtein Sequence
    AlignmentAlignment

-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0000287 magnesium ion binding
GO:0003677 DNA binding
GO:0003824 catalytic activity
GO:0004518 nuclease activity
GO:0004519 endonuclease activity
GO:0004527 exonuclease activity
GO:0008409 5'-3' exonuclease activity
GO:0016787 hydrolase activity
GO:0016788 hydrolase activity, acting on ester bonds
GO:0017108 5'-flap endonuclease activity
GO:0046872 metal ion binding

Biological Process:
GO:0006260 DNA replication
GO:0006281 DNA repair
GO:0006284 base-excision repair
GO:0006974 cellular response to DNA damage stimulus
GO:0007613 memory
GO:0043137 DNA replication, removal of RNA primer
GO:0090305 nucleic acid phosphodiester bond hydrolysis

Cellular Component:
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005730 nucleolus
GO:0005739 mitochondrion


-  Descriptions from all associated GenBank mRNAs
  X76771 - Homo sapiens mRNA for flap endonuclease-1.
AK301743 - Homo sapiens cDNA FLJ51365 complete cds, highly similar to Flap endonuclease 1 (EC 3.1.-.-).
BC000323 - Homo sapiens flap structure-specific endonuclease 1, mRNA (cDNA clone MGC:8478 IMAGE:2821792), complete cds.
AK312761 - Homo sapiens cDNA, FLJ93171, Homo sapiens flap structure-specific endonuclease 1 (FEN1), mRNA.
JD410704 - Sequence 391728 from Patent EP1572962.
KJ891158 - Synthetic construct Homo sapiens clone ccsbBroadEn_00552 FEN1 gene, encodes complete protein.
AB464524 - Synthetic construct DNA, clone: pF1KB9851, Homo sapiens FEN1 gene for flap structure-specific endonuclease 1, without stop codon, in Flexi system.
BT019524 - Homo sapiens flap structure-specific endonuclease 1 mRNA, complete cds.
CR536562 - Homo sapiens full open reading frame cDNA clone RZPDo834H1220D for gene FEN1, flap structure-specific endonuclease 1; complete cds, incl. stopcodon.
L37374 - Homo sapiens endonuclease (FEN-1) mRNA, complete cds.
BC019599 - Homo sapiens mRNA similar to flap structure-specific endonuclease 1 (cDNA clone IMAGE:3862385).
JD022380 - Sequence 3404 from Patent EP1572962.
JD031192 - Sequence 12216 from Patent EP1572962.
JD019107 - Sequence 131 from Patent EP1572962.
JD108313 - Sequence 89337 from Patent EP1572962.
JD034598 - Sequence 15622 from Patent EP1572962.
JD083784 - Sequence 64808 from Patent EP1572962.
JD546739 - Sequence 527763 from Patent EP1572962.
JD120191 - Sequence 101215 from Patent EP1572962.
JD039429 - Sequence 20453 from Patent EP1572962.
JD312917 - Sequence 293941 from Patent EP1572962.
JD440430 - Sequence 421454 from Patent EP1572962.
JD088895 - Sequence 69919 from Patent EP1572962.
JD268567 - Sequence 249591 from Patent EP1572962.
JD060863 - Sequence 41887 from Patent EP1572962.
JD474236 - Sequence 455260 from Patent EP1572962.
JD400695 - Sequence 381719 from Patent EP1572962.
JD524040 - Sequence 505064 from Patent EP1572962.
JD368116 - Sequence 349140 from Patent EP1572962.

-  Other Names for This Gene
  Alternate Gene Symbols: ENST00000305885.1, ENST00000305885.2, FEN1 , hCG_40848 , NM_004111, Q6FHX6, Q6FHX6_HUMAN, uc317nsg.1, uc317nsg.2
UCSC ID: ENST00000305885.3_4
RefSeq Accession: NM_004111.6
Protein: Q6FHX6

-  Gene Model Information
  Click here for a detailed description of the fields of the table above.

-  Methods, Credits, and Use Restrictions
  Click here for details on how this gene model was made and data restrictions if any.