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P39748 (FEN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Flap endonuclease 1

Short name=FEN-1
EC=3.1.-.-
Alternative name(s):
DNase IV
Flap structure-specific endonuclease 1
Maturation factor 1
Short name=MF1
Short name=hFEN-1
Gene names
Name:FEN1
Synonyms:RAD2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length380 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.6 Ref.7 Ref.9 Ref.11 Ref.13 Ref.15

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 structure

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. Ref.8 Ref.10 Ref.12

Subcellular location

Isoform 1: Nucleusnucleolus. Nucleusnucleoplasm. Note: Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage. Ref.6 Ref.13 Ref.19

Isoform FENMIT: Mitochondrion Ref.6 Ref.13 Ref.19.

Post-translational modification

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. Ref.10

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. HAMAP-Rule MF_03140

Methylation at Arg-192 by PRMT5 impedes Ser-187 phosphorylation and increases interaction with PCNA. Ref.15

Sequence similarities

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

Ontologies

Keywords
   Biological processDNA damage
DNA repair
DNA replication
   Cellular componentMitochondrion
Nucleus
   Coding sequence diversityAlternative initiation
   LigandMagnesium
Metal-binding
   Molecular functionEndonuclease
Exonuclease
Hydrolase
Nuclease
   PTMAcetylation
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA catabolic process, endonucleolytic

Inferred from direct assay PubMed 18995831. Source: GOC

DNA catabolic process, exonucleolytic

Traceable author statement PubMed 8131753. Source: GOC

DNA repair

Non-traceable author statement PubMed 15504738. Source: UniProtKB

DNA replication

Non-traceable author statement PubMed 15504738. Source: UniProtKB

DNA replication, removal of RNA primer

Inferred from direct assay PubMed 18995831. Source: UniProtKB

DNA strand elongation involved in DNA replication

Traceable author statement. Source: Reactome

RNA phosphodiester bond hydrolysis, endonucleolytic

Inferred from direct assay Ref.6. Source: GOC

UV protection

Traceable author statement Ref.1. Source: ProtInc

base-excision repair

Traceable author statement. Source: Reactome

double-strand break repair

Traceable author statement PubMed 8131753. Source: ProtInc

memory

Inferred from electronic annotation. Source: Ensembl

mitotic cell cycle

Traceable author statement. Source: Reactome

nucleic acid phosphodiester bond hydrolysis

Inferred from direct assay Ref.6. Source: GOC

phosphatidylinositol-mediated signaling

Non-traceable author statement PubMed 15504738. Source: UniProtKB

telomere maintenance

Traceable author statement. Source: Reactome

telomere maintenance via recombination

Traceable author statement. Source: Reactome

telomere maintenance via semi-conservative replication

Traceable author statement. Source: Reactome

   Cellular_componentmitochondrion

Inferred from direct assay PubMed 18995831. Source: UniProtKB

nucleolus

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 18995831Ref.6. Source: UniProtKB

   Molecular_function5'-3' exonuclease activity

Inferred from direct assay Ref.6. Source: UniProtKB

5'-flap endonuclease activity

Inferred from direct assay PubMed 18995831. Source: UniProtKB

DNA binding

Inferred from mutant phenotype Ref.11. Source: UniProtKB

RNA-DNA hybrid ribonuclease activity

Inferred from direct assay Ref.6. Source: UniProtKB

damaged DNA binding

Traceable author statement Ref.1. Source: ProtInc

double-stranded DNA binding

Traceable author statement PubMed 8131753. Source: ProtInc

double-stranded DNA exodeoxyribonuclease activity

Traceable author statement PubMed 8131753. Source: ProtInc

endonuclease activity

Traceable author statement PubMed 8131753. Source: ProtInc

exonuclease activity

Traceable author statement PubMed 9778254. Source: ProtInc

magnesium ion binding

Inferred from electronic annotation. Source: Ensembl

manganese ion binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform 1 (identifier: P39748-1)

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.
Isoform FENMIT (identifier: P39748-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 380380Flap endonuclease 1 HAMAP-Rule MF_03140
PRO_0000154069

Regions

Region1 – 104104N-domain HAMAP-Rule MF_03140
Region122 – 253132I-domain HAMAP-Rule MF_03140
Region336 – 3449Interaction with PCNA HAMAP-Rule MF_03140

Sites

Metal binding341Magnesium 1
Metal binding861Magnesium 1
Metal binding1581Magnesium 1
Metal binding1601Magnesium 1
Metal binding1791Magnesium 2
Metal binding1811Magnesium 2
Metal binding2331Magnesium 2
Binding site471DNA substrate
Binding site701DNA substrate
Binding site1581DNA substrate
Binding site2311DNA substrate
Binding site2331DNA substrate

Amino acid modifications

Modified residue191Symmetric dimethylarginine; by PRMT5 Ref.15
Modified residue801N6-acetyllysine Ref.14
Modified residue1001Symmetric dimethylarginine; by PRMT5 Ref.15
Modified residue1041Symmetric dimethylarginine; by PRMT5 Ref.15
Modified residue1871Phosphoserine; by CDK2 Ref.15
Modified residue1921Symmetric dimethylarginine; by PRMT5 Ref.15
Modified residue1971Phosphoserine Ref.16
Modified residue3541N6-acetyllysine Ref.10
Modified residue3641Phosphothreonine Ref.16
Modified residue3751N6-acetyllysine Ref.10 Ref.14
Modified residue3771N6-acetyllysine Ref.10
Modified residue3801N6-acetyllysine Ref.10

Natural variations

Alternative sequence1 – 6464Missing in isoform FENMIT.
VSP_047520

Experimental info

Mutagenesis291R → A: No significant effect on exonuclease activity or flap endonuclease activity. Ref.11
Mutagenesis341D → A: Loss of flap endonuclease activity but substrate binding activity is retained. Ref.7
Mutagenesis471R → A: Significantly reduced exonuclease activity and reduced substrate binding. The positions of the cleavage sites are also shifted. Ref.11
Mutagenesis701R → A: Loss of exonuclease activity and reduced endonuclease activity. Reduced substrate binding. Ref.11
Mutagenesis731R → A: No significant effect on exonuclease activity or flap endonuclease activity. Ref.11
Mutagenesis801K → A: No significant effect on exonuclease activity or flap endonuclease activity. Ref.11
Mutagenesis861D → A: Loss of flap endonuclease activity but substrate binding activity is retained. Ref.7
Mutagenesis1031R → A: No effect on flap endonuclease activity or substrate binding. Ref.7
Mutagenesis1581E → A: Loss of flap endonuclease activity and substrate binding. Ref.7
Mutagenesis1791D → A: No effect on flap endonuclease activity or substrate binding. Ref.7
Mutagenesis1811D → A: Loss of flap endonuclease activity but substrate binding activity is retained. Ref.7
Mutagenesis1871S → A: Fails to translocate from nucleoli to the nuclear plasma. Ref.13
Mutagenesis1871S → D: Diminishes nucleolar localization. Ref.13
Mutagenesis1921R → K: Impairs ability to localize to sites of DNA replication or repair. Ref.15
Mutagenesis2311G → A: Loss of flap endonuclease activity and substrate binding. Ref.7
Mutagenesis2331D → A: Loss of flap endonuclease activity and substrate binding. Ref.7

Secondary structure

............................................................ 380
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 5154F2F6E57592C5

FASTA38042,593
        10         20         30         40         50         60 
MGIQGLAKLI ADVAPSAIRE NDIKSYFGRK VAIDASMSIY QFLIAVRQGG DVLQNEEGET 

        70         80         90        100        110        120 
TSHLMGMFYR TIRMMENGIK PVYVFDGKPP QLKSGELAKR SERRAEAEKQ LQQAQAAGAE 

       130        140        150        160        170        180 
QEVEKFTKRL VKVTKQHNDE CKHLLSLMGI PYLDAPSEAE ASCAALVKAG KVYAAATEDM 

       190        200        210        220        230        240 
DCLTFGSPVL MRHLTASEAK KLPIQEFHLS RILQELGLNQ EQFVDLCILL GSDYCESIRG 

       250        260        270        280        290        300 
IGPKRAVDLI QKHKSIEEIV RRLDPNKYPV PENWLHKEAH QLFLEPEVLD PESVELKWSE 

       310        320        330        340        350        360 
PNEEELIKFM CGEKQFSEER IRSGVKRLSK SRQGSTQGRL DDFFKVTGSL SSAKRKEPEP 

       370        380 
KGSTKKKAKT GAAGKFKRGK 

« Hide

Isoform FENMIT [UniParc].

Checksum: 7D5CA94548F0ED99
Show »

FASTA31635,673

References

« Hide 'large scale' references
[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]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA56531.
RefSeqNP_004102.1. NM_004111.5.
UniGeneHs.409065.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP39748.
SMRP39748. Positions 2-336.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108528. 35 interactions.
DIPDIP-24216N.
IntActP39748. 12 interactions.
MINTMINT-5004212.
STRING9606.ENSP00000305480.

Chemistry

BindingDBP39748.
ChEMBLCHEMBL5027.

PTM databases

PhosphoSiteP39748.

Polymorphism databases

DMDM729475.

Proteomic databases

PaxDbP39748.
PeptideAtlasP39748.
PRIDEP39748.

Protocols and materials databases

DNASU2237.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000305885; ENSP00000305480; ENSG00000168496. [P39748-1]
GeneID2237.
KEGGhsa:2237.
UCSCuc001nsg.3. human. [P39748-1]

Organism-specific databases

CTD2237.
GeneCardsGC11P061560.
HGNCHGNC:3650. FEN1.
HPACAB002262.
HPA006748.
MIM600393. gene.
neXtProtNX_P39748.
PharmGKBPA28090.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0258.
HOGENOMHOG000193853.
HOVERGENHBG000844.
InParanoidP39748.
KOK04799.
OMAGSQDYDS.
OrthoDBEOG72JWHG.
PhylomeDBP39748.
TreeFamTF105701.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_216. DNA Repair.
REACT_383. DNA Replication.
SignaLinkP39748.

Gene expression databases

ArrayExpressP39748.
BgeeP39748.
CleanExHS_FEN1.
GenevestigatorP39748.

Family and domain databases

HAMAPMF_00614. Fen.
InterProIPR020045. 5-3_exonuclease_C.
IPR023426. Flap_endonuc.
IPR008918. HhH2.
IPR006086. XPG-I_dom.
IPR006084. XPG/Rad2.
IPR019974. XPG_CS.
IPR006085. XPG_DNA_repair_N.
[Graphical view]
PANTHERPTHR11081. PTHR11081. 1 hit.
PfamPF00867. XPG_I. 1 hit.
PF00752. XPG_N. 1 hit.
[Graphical view]
PRINTSPR00853. XPGRADSUPER.
SMARTSM00279. HhH2. 1 hit.
SM00484. XPGI. 1 hit.
SM00485. XPGN. 1 hit.
[Graphical view]
SUPFAMSSF47807. SSF47807. 1 hit.
PROSITEPS00841. XPG_1. 1 hit.
PS00842. XPG_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFEN1. human.
EvolutionaryTraceP39748.
GeneWikiFlap_structure-specific_endonuclease_1.
GenomeRNAi2237.
NextBio9055.
PROP39748.
SOURCESearch...

Entry information

Entry nameFEN1_HUMAN
AccessionPrimary (citable) accession number: P39748
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM