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P39748

- FEN1_HUMAN

UniProt

P39748 - FEN1_HUMAN

Protein

Flap endonuclease 1

Gene

FEN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    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

    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. protein binding Source: UniProtKB
    12. 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: UniProtKB
    5. DNA replication Source: UniProtKB
    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. nucleic acid phosphodiester bond hydrolysis Source: GOC
    12. phosphatidylinositol-mediated signaling Source: UniProtKB
    13. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
    14. telomere maintenance Source: Reactome
    15. telomere maintenance via recombination Source: Reactome
    16. telomere maintenance via semi-conservative replication Source: Reactome
    17. UV protection Source: ProtInc

    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

    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 CDK22 PublicationsUniRule annotation
    Modified residuei192 – 1921Symmetric dimethylarginine; by PRMT51 PublicationUniRule annotation
    Modified residuei197 – 1971Phosphoserine2 Publications
    Modified residuei354 – 3541N6-acetyllysine1 PublicationUniRule annotation
    Modified residuei364 – 3641Phosphothreonine2 Publications
    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

    ArrayExpressiP39748.
    BgeeiP39748.
    CleanExiHS_FEN1.
    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
    WRNQ1419110EBI-707816,EBI-368417

    Protein-protein interaction databases

    BioGridi108528. 36 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 – 138
    Helixi15 – 173
    Beta strandi18 – 225
    Helixi23 – 264
    Beta strandi30 – 345
    Helixi35 – 4511
    Beta strandi47 – 526
    Helixi62 – 7514
    Turni76 – 783
    Beta strandi80 – 856
    Helixi91 – 933
    Helixi94 – 11522
    Helixi120 – 12910
    Helixi135 – 14814
    Beta strandi152 – 1543
    Helixi159 – 16810
    Beta strandi171 – 1766
    Helixi181 – 1844
    Beta strandi188 – 1936
    Beta strandi203 – 2086
    Helixi209 – 2168
    Helixi220 – 23011
    Beta strandi233 – 2353
    Helixi243 – 25311
    Helixi256 – 2627
    Turni265 – 2673
    Helixi276 – 2849
    Turni291 – 2933
    Helixi303 – 3108
    Turni311 – 3144
    Helixi318 – 33518
    Helixi340 – 3423
    Beta strandi344 – 3518

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MGIQGLAKLI ADVAPSAIRE NDIKSYFGRK VAIDASMSIY QFLIAVRQGG    50
    DVLQNEEGET TSHLMGMFYR TIRMMENGIK PVYVFDGKPP QLKSGELAKR 100
    SERRAEAEKQ LQQAQAAGAE QEVEKFTKRL VKVTKQHNDE CKHLLSLMGI 150
    PYLDAPSEAE ASCAALVKAG KVYAAATEDM DCLTFGSPVL MRHLTASEAK 200
    KLPIQEFHLS RILQELGLNQ EQFVDLCILL GSDYCESIRG IGPKRAVDLI 250
    QKHKSIEEIV RRLDPNKYPV PENWLHKEAH QLFLEPEVLD PESVELKWSE 300
    PNEEELIKFM CGEKQFSEER IRSGVKRLSK SRQGSTQGRL DDFFKVTGSL 350
    SSAKRKEPEP KGSTKKKAKT GAAGKFKRGK 380
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 36 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

    ArrayExpressi P39748.
    Bgeei P39748.
    CleanExi HS_FEN1.
    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

    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: October 1, 2014
    This is version 147 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