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P39748

- FEN1_HUMAN

UniProt

P39748 - FEN1_HUMAN

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Protein

Flap endonuclease 1

Gene

FEN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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.6 PublicationsUniRule annotation

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi34 – 341Magnesium 1
Binding sitei47 – 471DNA substrate
Binding sitei70 – 701DNA substrate
Metal bindingi86 – 861Magnesium 1
Metal bindingi158 – 1581Magnesium 1
Binding sitei158 – 1581DNA substrate
Metal bindingi160 – 1601Magnesium 1
Metal bindingi179 – 1791Magnesium 2
Metal bindingi181 – 1811Magnesium 2
Binding sitei231 – 2311DNA substrate
Metal bindingi233 – 2331Magnesium 2
Binding sitei233 – 2331DNA substrate

GO - Molecular functioni

  1. 5'-3' exonuclease activity Source: UniProtKB
  2. 5'-flap endonuclease activity Source: UniProtKB
  3. damaged DNA binding Source: ProtInc
  4. DNA binding Source: UniProtKB
  5. double-stranded DNA binding Source: ProtInc
  6. double-stranded DNA exodeoxyribonuclease activity Source: ProtInc
  7. endonuclease activity Source: ProtInc
  8. exonuclease activity Source: ProtInc
  9. magnesium ion binding Source: UniProtKB-HAMAP
  10. manganese ion binding Source: Ensembl
  11. RNA-DNA hybrid ribonuclease activity Source: UniProtKB

GO - Biological processi

  1. base-excision repair Source: Reactome
  2. DNA catabolic process, endonucleolytic Source: GOC
  3. DNA catabolic process, exonucleolytic Source: GOC
  4. DNA repair Source: Reactome
  5. DNA replication Source: ProtInc
  6. DNA replication, removal of RNA primer Source: UniProtKB
  7. DNA strand elongation involved in DNA replication Source: Reactome
  8. double-strand break repair Source: ProtInc
  9. memory Source: Ensembl
  10. mitotic cell cycle Source: Reactome
  11. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
  12. telomere maintenance Source: Reactome
  13. telomere maintenance via recombination Source: Reactome
  14. telomere maintenance via semi-conservative replication Source: Reactome
  15. UV protection Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

DNA damage, DNA repair, DNA replication

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_2192. Removal of DNA patch containing abasic residue.
REACT_70. Removal of the Flap Intermediate.
REACT_7999. Removal of the Flap Intermediate from the C-strand.
SignaLinkiP39748.

Names & Taxonomyi

Protein namesi
Recommended name:
Flap endonuclease 1UniRule annotation (EC:3.1.-.-UniRule annotation)
Short name:
FEN-1UniRule annotation
Alternative name(s):
DNase IV
Flap structure-specific endonuclease 1UniRule annotation
Maturation factor 1
Short name:
MF1
Short name:
hFEN-1
Gene namesi
Name:FEN1UniRule annotation
Synonyms:RAD2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:3650. FEN1.

Subcellular locationi

Isoform 1 : Nucleusnucleolus. Nucleusnucleoplasm
Note: Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage.
Isoform FENMIT : Mitochondrion 1 PublicationUniRule annotation

GO - Cellular componenti

  1. membrane Source: UniProtKB
  2. mitochondrion Source: UniProtKB
  3. nucleolus Source: HPA
  4. nucleoplasm Source: Reactome
  5. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi29 – 291R → A: No significant effect on exonuclease activity or flap endonuclease activity. 1 Publication
Mutagenesisi34 – 341D → A: Loss of flap endonuclease activity but substrate binding activity is retained. 1 Publication
Mutagenesisi47 – 471R → A: Significantly reduced exonuclease activity and reduced substrate binding. The positions of the cleavage sites are also shifted. 1 Publication
Mutagenesisi70 – 701R → A: Loss of exonuclease activity and reduced endonuclease activity. Reduced substrate binding. 1 Publication
Mutagenesisi73 – 731R → A: No significant effect on exonuclease activity or flap endonuclease activity. 1 Publication
Mutagenesisi80 – 801K → A: No significant effect on exonuclease activity or flap endonuclease activity. 1 Publication
Mutagenesisi86 – 861D → A: Loss of flap endonuclease activity but substrate binding activity is retained. 1 Publication
Mutagenesisi103 – 1031R → A: No effect on flap endonuclease activity or substrate binding. 1 Publication
Mutagenesisi158 – 1581E → A: Loss of flap endonuclease activity and substrate binding. 1 Publication
Mutagenesisi179 – 1791D → A: No effect on flap endonuclease activity or substrate binding. 1 Publication
Mutagenesisi181 – 1811D → A: Loss of flap endonuclease activity but substrate binding activity is retained. 1 Publication
Mutagenesisi187 – 1871S → A: Fails to translocate from nucleoli to the nuclear plasma. 1 Publication
Mutagenesisi187 – 1871S → D: Diminishes nucleolar localization. 1 Publication
Mutagenesisi192 – 1921R → K: Impairs ability to localize to sites of DNA replication or repair. 1 Publication
Mutagenesisi231 – 2311G → A: Loss of flap endonuclease activity and substrate binding. 1 Publication
Mutagenesisi233 – 2331D → A: Loss of flap endonuclease activity and substrate binding. 1 Publication

Organism-specific databases

PharmGKBiPA28090.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 380380Flap endonuclease 1PRO_0000154069Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Symmetric dimethylarginine; by PRMT51 PublicationUniRule annotation
Modified residuei80 – 801N6-acetyllysine1 PublicationUniRule annotation
Modified residuei100 – 1001Symmetric dimethylarginine; by PRMT51 PublicationUniRule annotation
Modified residuei104 – 1041Symmetric dimethylarginine; by PRMT51 PublicationUniRule annotation
Modified residuei187 – 1871Phosphoserine; by CDK21 PublicationUniRule annotation
Modified residuei192 – 1921Symmetric dimethylarginine; by PRMT51 PublicationUniRule annotation
Modified residuei197 – 1971Phosphoserine1 Publication
Modified residuei354 – 3541N6-acetyllysine1 PublicationUniRule annotation
Modified residuei364 – 3641Phosphothreonine1 Publication
Modified residuei375 – 3751N6-acetyllysine2 PublicationsUniRule annotation
Modified residuei377 – 3771N6-acetyllysine1 PublicationUniRule annotation
Modified residuei380 – 3801N6-acetyllysine1 PublicationUniRule annotation

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 EP300.2 PublicationsUniRule annotation
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.1 PublicationUniRule annotation
Methylation at Arg-192 by PRMT5 impedes Ser-187 phosphorylation and increases interaction with PCNA.1 PublicationUniRule annotation

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiP39748.
PaxDbiP39748.
PeptideAtlasiP39748.
PRIDEiP39748.

PTM databases

PhosphoSiteiP39748.

Expressioni

Gene expression databases

BgeeiP39748.
CleanExiHS_FEN1.
ExpressionAtlasiP39748. baseline and differential.
GenevestigatoriP39748.

Organism-specific databases

HPAiCAB002262.
HPA006748.

Interactioni

Subunit structurei

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 DDX11.4 PublicationsUniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
BLMP541324EBI-707816,EBI-621372
MUS81Q96NY95EBI-707816,EBI-2370806
PCNAP120044EBI-707816,EBI-358311
WRNQ141919EBI-707816,EBI-368417

Protein-protein interaction databases

BioGridi108528. 38 interactions.
DIPiDIP-24216N.
IntActiP39748. 12 interactions.
MINTiMINT-5004212.
STRINGi9606.ENSP00000305480.

Structurei

Secondary structure

1
380
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 138Combined sources
Helixi15 – 173Combined sources
Beta strandi18 – 225Combined sources
Helixi23 – 264Combined sources
Beta strandi30 – 345Combined sources
Helixi35 – 4511Combined sources
Beta strandi47 – 526Combined sources
Helixi62 – 7514Combined sources
Turni76 – 783Combined sources
Beta strandi80 – 856Combined sources
Helixi91 – 933Combined sources
Helixi94 – 11522Combined sources
Helixi120 – 12910Combined sources
Helixi135 – 14814Combined sources
Beta strandi152 – 1543Combined sources
Helixi159 – 16810Combined sources
Beta strandi171 – 1766Combined sources
Helixi181 – 1844Combined sources
Beta strandi188 – 1936Combined sources
Beta strandi203 – 2086Combined sources
Helixi209 – 2168Combined sources
Helixi220 – 23011Combined sources
Beta strandi233 – 2353Combined sources
Helixi243 – 25311Combined sources
Helixi256 – 2627Combined sources
Turni265 – 2673Combined sources
Helixi276 – 2849Combined sources
Turni291 – 2933Combined sources
Helixi303 – 3108Combined sources
Turni311 – 3144Combined sources
Helixi318 – 33518Combined sources
Helixi340 – 3423Combined sources
Beta strandi344 – 3518Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U7BX-ray1.88B331-350[»]
1UL1X-ray2.90X/Y/Z2-380[»]
3Q8KX-ray2.20A2-336[»]
3Q8LX-ray2.32A2-336[»]
3Q8MX-ray2.60A/B2-336[»]
3UVUX-ray2.38B352-370[»]
ProteinModelPortaliP39748.
SMRiP39748. Positions 2-336.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39748.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 104104N-domainAdd
BLAST
Regioni122 – 253132I-domainAdd
BLAST
Regioni336 – 3449Interaction with PCNA

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0258.
HOGENOMiHOG000193853.
HOVERGENiHBG000844.
InParanoidiP39748.
KOiK04799.
OMAiVKFMCGE.
OrthoDBiEOG72JWHG.
PhylomeDBiP39748.
TreeFamiTF105701.

Family and domain databases

Gene3Di3.40.50.1010. 1 hit.
HAMAPiMF_00614. Fen.
InterProiIPR020045. 5-3_exonuclease_C.
IPR023426. Flap_endonuc.
IPR008918. HhH2.
IPR029060. PIN_domain-like.
IPR006086. XPG-I_dom.
IPR019974. XPG_CS.
IPR006085. XPG_DNA_repair_N.
[Graphical view]
PfamiPF00867. XPG_I. 1 hit.
PF00752. XPG_N. 1 hit.
[Graphical view]
SMARTiSM00279. HhH2. 1 hit.
SM00484. XPGI. 1 hit.
SM00485. XPGN. 1 hit.
[Graphical view]
SUPFAMiSSF47807. SSF47807. 1 hit.
SSF88723. SSF88723. 1 hit.
PROSITEiPS00841. XPG_1. 1 hit.
PS00842. XPG_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative initiation. Align

Isoform 1 (identifier: P39748-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGIQGLAKLI ADVAPSAIRE NDIKSYFGRK VAIDASMSIY QFLIAVRQGG
60 70 80 90 100
DVLQNEEGET TSHLMGMFYR TIRMMENGIK PVYVFDGKPP QLKSGELAKR
110 120 130 140 150
SERRAEAEKQ LQQAQAAGAE QEVEKFTKRL VKVTKQHNDE CKHLLSLMGI
160 170 180 190 200
PYLDAPSEAE ASCAALVKAG KVYAAATEDM DCLTFGSPVL MRHLTASEAK
210 220 230 240 250
KLPIQEFHLS RILQELGLNQ EQFVDLCILL GSDYCESIRG IGPKRAVDLI
260 270 280 290 300
QKHKSIEEIV RRLDPNKYPV PENWLHKEAH QLFLEPEVLD PESVELKWSE
310 320 330 340 350
PNEEELIKFM CGEKQFSEER IRSGVKRLSK SRQGSTQGRL DDFFKVTGSL
360 370 380
SSAKRKEPEP KGSTKKKAKT GAAGKFKRGK
Length:380
Mass (Da):42,593
Last modified:February 1, 1995 - v1
Checksum:i5154F2F6E57592C5
GO
Isoform FENMIT (identifier: P39748-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-64: Missing.

Note: No nuclease activity. Binds preferentially to RNA flap structures and R-loops.

Show »
Length:316
Mass (Da):35,673
Checksum:i7D5CA94548F0ED99
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6464Missing in isoform FENMIT. CuratedVSP_047520Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76771 mRNA. Translation: CAA54166.1.
L37374 mRNA. Translation: AAA91331.1.
AF523117 Genomic DNA. Translation: AAM74238.1.
AC004770 Genomic DNA. Translation: AAC23394.1.
BC000323 mRNA. Translation: AAH00323.1.
CCDSiCCDS8010.1. [P39748-1]
PIRiA56531.
RefSeqiNP_004102.1. NM_004111.5. [P39748-1]
UniGeneiHs.409065.

Genome annotation databases

EnsembliENST00000305885; ENSP00000305480; ENSG00000168496. [P39748-1]
GeneIDi2237.
KEGGihsa:2237.
UCSCiuc001nsg.3. human. [P39748-1]

Polymorphism databases

DMDMi729475.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76771 mRNA. Translation: CAA54166.1 .
L37374 mRNA. Translation: AAA91331.1 .
AF523117 Genomic DNA. Translation: AAM74238.1 .
AC004770 Genomic DNA. Translation: AAC23394.1 .
BC000323 mRNA. Translation: AAH00323.1 .
CCDSi CCDS8010.1. [P39748-1 ]
PIRi A56531.
RefSeqi NP_004102.1. NM_004111.5. [P39748-1 ]
UniGenei Hs.409065.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1U7B X-ray 1.88 B 331-350 [» ]
1UL1 X-ray 2.90 X/Y/Z 2-380 [» ]
3Q8K X-ray 2.20 A 2-336 [» ]
3Q8L X-ray 2.32 A 2-336 [» ]
3Q8M X-ray 2.60 A/B 2-336 [» ]
3UVU X-ray 2.38 B 352-370 [» ]
ProteinModelPortali P39748.
SMRi P39748. Positions 2-336.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108528. 38 interactions.
DIPi DIP-24216N.
IntActi P39748. 12 interactions.
MINTi MINT-5004212.
STRINGi 9606.ENSP00000305480.

Chemistry

BindingDBi P39748.
ChEMBLi CHEMBL5027.

PTM databases

PhosphoSitei P39748.

Polymorphism databases

DMDMi 729475.

Proteomic databases

MaxQBi P39748.
PaxDbi P39748.
PeptideAtlasi P39748.
PRIDEi P39748.

Protocols and materials databases

DNASUi 2237.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000305885 ; ENSP00000305480 ; ENSG00000168496 . [P39748-1 ]
GeneIDi 2237.
KEGGi hsa:2237.
UCSCi uc001nsg.3. human. [P39748-1 ]

Organism-specific databases

CTDi 2237.
GeneCardsi GC11P061560.
HGNCi HGNC:3650. FEN1.
HPAi CAB002262.
HPA006748.
MIMi 600393. gene.
neXtProti NX_P39748.
PharmGKBi PA28090.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0258.
HOGENOMi HOG000193853.
HOVERGENi HBG000844.
InParanoidi P39748.
KOi K04799.
OMAi VKFMCGE.
OrthoDBi EOG72JWHG.
PhylomeDBi P39748.
TreeFami TF105701.

Enzyme and pathway databases

Reactomei REACT_2192. Removal of DNA patch containing abasic residue.
REACT_70. Removal of the Flap Intermediate.
REACT_7999. Removal of the Flap Intermediate from the C-strand.
SignaLinki P39748.

Miscellaneous databases

ChiTaRSi FEN1. human.
EvolutionaryTracei P39748.
GeneWikii Flap_structure-specific_endonuclease_1.
GenomeRNAii 2237.
NextBioi 9055.
PROi P39748.
SOURCEi Search...

Gene expression databases

Bgeei P39748.
CleanExi HS_FEN1.
ExpressionAtlasi P39748. baseline and differential.
Genevestigatori P39748.

Family and domain databases

Gene3Di 3.40.50.1010. 1 hit.
HAMAPi MF_00614. Fen.
InterProi IPR020045. 5-3_exonuclease_C.
IPR023426. Flap_endonuc.
IPR008918. HhH2.
IPR029060. PIN_domain-like.
IPR006086. XPG-I_dom.
IPR019974. XPG_CS.
IPR006085. XPG_DNA_repair_N.
[Graphical view ]
Pfami PF00867. XPG_I. 1 hit.
PF00752. XPG_N. 1 hit.
[Graphical view ]
SMARTi SM00279. HhH2. 1 hit.
SM00484. XPGI. 1 hit.
SM00485. XPGN. 1 hit.
[Graphical view ]
SUPFAMi SSF47807. SSF47807. 1 hit.
SSF88723. SSF88723. 1 hit.
PROSITEi PS00841. XPG_1. 1 hit.
PS00842. XPG_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structural and functional conservation of the human homolog of the Schizosaccharomyces pombe rad2 gene, which is required for chromosome segregation and recovery from DNA damage."
    Murray J.M., Tavassoli M., Al-Harithy R., Sheldrick K.S., Lehmann A.R., Carr A.M., Watts F.Z.
    Mol. Cell. Biol. 14:4878-4888(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Sequence of human FEN-1, a structure-specific endonuclease, and chromosomal localization of the gene (FEN1) in mouse and human."
    Hiraoka L.R., Harrington J.J., Gerhard D.S., Lieber M.R., Hsieh C.-L.
    Genomics 25:220-225(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Leukemic T-cell.
  3. NIEHS SNPs program
    Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  6. "Structural and functional homology between mammalian DNase IV and the 5'-nuclease domain of Escherichia coli DNA polymerase I."
    Robins P., Pappin D.J.C., Wood R.D., Lindahl T.
    J. Biol. Chem. 269:28535-28538(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION.
  7. "Essential amino acids for substrate binding and catalysis of human flap endonuclease 1."
    Shen B., Nolan J.P., Sklar L.A., Park M.S.
    J. Biol. Chem. 271:9173-9176(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE-BINDING SITES, MUTAGENESIS OF ASP-34; ASP-86; ARG-103; GLU-158; ASP-179; ASP-181; GLY-231 AND ASP-233.
  8. "The DNA repair endonuclease XPG binds to proliferating cell nuclear antigen (PCNA) and shares sequence elements with the PCNA-binding regions of FEN-1 and cyclin-dependent kinase inhibitor p21."
    Gary R., Ludwig D.L., Cornelius H.L., MacInnes M.A., Park M.S.
    J. Biol. Chem. 272:24522-24529(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PCNA.
  9. "Mechanism whereby proliferating cell nuclear antigen stimulates flap endonuclease 1."
    Tom S., Henricksen L.A., Bambara R.A.
    J. Biol. Chem. 275:10498-10505(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Regulation of human flap endonuclease-1 activity by acetylation through the transcriptional coactivator p300."
    Hasan S., Stucki M., Hassa P.O., Imhof R., Gehrig P., Hunziker P., Hubscher U., Hottiger M.O.
    Mol. Cell 7:1221-1231(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH P300, ACETYLATION AT LYS-354; LYS-375; LYS-377 AND LYS-380.
  11. "Arginine residues 47 and 70 of human flap endonuclease-1 are involved in DNA substrate interactions and cleavage site determination."
    Qiu J., Bimston D.N., Partikian A., Shen B.
    J. Biol. Chem. 277:24659-24666(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBSTRATE-BINDING SITES ARG-47 AND ARG-70, MUTAGENESIS OF ARG-29; ARG-47; ARG-70; ARG-73 AND LYS-80.
  12. "Studies with the human cohesin establishment factor, ChlR1. Association of ChlR1 with Ctf18-RFC and Fen1."
    Farina A., Shin J.H., Kim D.H., Bermudez V.P., Kelman Z., Seo Y.S., Hurwitz J.
    J. Biol. Chem. 283:20925-20936(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDX11.
  13. "Nucleolar localization and dynamic roles of flap endonuclease 1 in ribosomal DNA replication and damage repair."
    Guo Z., Qian L., Liu R., Dai H., Zhou M., Zheng L., Shen B.
    Mol. Cell. Biol. 28:4310-4319(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF SER-187.
  14. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-80 AND LYS-375, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Methylation of FEN1 suppresses nearby phosphorylation and facilitates PCNA binding."
    Guo Z., Zheng L., Xu H., Dai H., Zhou M., Pascua M.R., Chen Q.M., Shen B.
    Nat. Chem. Biol. 6:766-773(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ARG-192, METHYLATION AT ARG-19; ARG-100; ARG-104 AND ARG-192, PHOSPHORYLATION AT SER-187.
  16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND THR-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "A cryptic targeting signal creates a mitochondrial FEN1 isoform with tailed R-loop binding properties."
    Kazak L., Reyes A., He J., Wood S.R., Brea-Calvo G., Holen T.T., Holt I.J.
    PLoS ONE 8:E62340-E62340(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE INITIATION (ISOFORM FENMIT), SUBCELLULAR LOCATION (ISOFORM FENMIT).
  20. "Structural and thermodynamic analysis of human PCNA with peptides derived from DNA polymerase-delta p66 subunit and flap endonuclease-1."
    Bruning J.B., Shamoo Y.
    Structure 12:2209-2219(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 331-350.
  21. "Structural basis for recruitment of human flap endonuclease 1 to PCNA."
    Sakurai S., Kitano K., Yamaguchi H., Hamada K., Okada K., Fukuda K., Uchida M., Ohtsuka E., Morioka H., Hakoshima T.
    EMBO J. 24:683-693(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 2-380 IN COMPLEX WITH PCNA.

Entry informationi

Entry nameiFEN1_HUMAN
AccessioniPrimary (citable) accession number: P39748
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 26, 2014
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3