HUMAN:FEN1

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	FEN1 (ECO:0000255 with HAMAP-Rule:MF_03140) (synonyms: RAD2)
Protein Name(s)	Flap endonuclease 1 (ECO:0000255 with HAMAP-Rule:MF_03140) FEN-1 (ECO:0000255 with HAMAP-Rule:MF_03140) DNase IV Flap structure-specific endonuclease 1 (ECO:0000255 with HAMAP-Rule:MF_03140) Maturation factor 1 MF1 hFEN-1
External Links
UniProt	P39748
EMBL	X76771 L37374 AF523117 AC004770 BC000323
CCDS	CCDS8010.1
PIR	A56531
RefSeq	NP_004102.1
UniGene	Hs.409065
PDB	1U7B 1UL1 3Q8K 3Q8L 3Q8M 3UVU
PDBsum	1U7B 1UL1 3Q8K 3Q8L 3Q8M 3UVU
ProteinModelPortal	P39748
SMR	P39748
BioGrid	108528
DIP	DIP-24216N
IntAct	P39748
MINT	MINT-5004212
STRING	9606.ENSP00000305480
BindingDB	P39748
ChEMBL	CHEMBL5027
PhosphoSite	P39748
DMDM	729475
MaxQB	P39748
PaxDb	P39748
PeptideAtlas	P39748
PRIDE	P39748
DNASU	2237
Ensembl	ENST00000305885
GeneID	2237
KEGG	hsa:2237
UCSC	uc001nsg.3
CTD	2237
GeneCards	GC11P061560
HGNC	HGNC:3650
HPA	CAB002262 HPA006748
MIM	600393
neXtProt	NX_P39748
PharmGKB	PA28090
eggNOG	COG0258
HOGENOM	HOG000193853
HOVERGEN	HBG000844
InParanoid	P39748
KO	K04799
OMA	GSQDYDS
OrthoDB	EOG72JWHG
PhylomeDB	P39748
TreeFam	TF105701
Reactome	REACT_2192 REACT_70 REACT_7999
SignaLink	P39748
ChiTaRS	FEN1
EvolutionaryTrace	P39748
GeneWiki	Flap_structure-specific_endonuclease_1
GenomeRNAi	2237
NextBio	9055
PRO	PR:P39748
Proteomes	UP000005640
Bgee	P39748
CleanEx	HS_FEN1
ExpressionAtlas	P39748
Genevestigator	P39748
GO	GO:0016020 GO:0005739 GO:0005730 GO:0005654 GO:0005634 GO:0008409 GO:0017108 GO:0003684 GO:0003677 GO:0003690 GO:0008309 GO:0004519 GO:0004527 GO:0000287 GO:0030145 GO:0004523 GO:0006284 GO:0000737 GO:0000738 GO:0006281 GO:0006260 GO:0043137 GO:0006271 GO:0006302 GO:0007613 GO:0000278 GO:0090502 GO:0000723 GO:0000722 GO:0032201 GO:0009650
Gene3D	3.40.50.1010
HAMAP	MF_00614
InterPro	IPR020045 IPR023426 IPR008918 IPR029060 IPR006086 IPR019974 IPR006085
Pfam	PF00867 PF00752
SMART	SM00279 SM00484 SM00485
SUPFAM	SSF47807 SSF88723
PROSITE	PS00841 PS00842

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
enables	GO:0048256	flap endonuclease activity	PMID:18499658^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	PMID:18499658^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045876	positive regulation of sister chromatid cohesion	PMID:18499658^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
colocalizes_with	GO:0000784	nuclear chromosome, telomeric region	PMID:24270157^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0000784	nuclear chromosome, telomeric region	PMID:19135898^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:19946888^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0043137	DNA replication, removal of RNA primer	PMID:18995831^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0017108	5'-flap endonuclease activity	PMID:8621570^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0017108	5'-flap endonuclease activity	PMID:11986308^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0017108	5'-flap endonuclease activity	PMID:18995831^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008409	5'-3' exonuclease activity	PMID:7961795^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:18995831^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:18995831^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:7961795^[8]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0004523	RNA-DNA hybrid ribonuclease activity	PMID:7961795^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
Contributes to	GO:0004519	endonuclease activity	PMID:25650046^[9]	ECO:0000314			F	Cold adapted enzyme based on salt dependence	complete CACAO 10572
enables	GO:0003677	DNA binding	PMID:11986308^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0048256	flap endonuclease activity	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0263831 MGI:MGI:102779 PANTHER:PTN000118612 PomBase:SPAC3G6.06c SGD:S000001596 SGD:S000005559 UniProtKB:P39748 UniProtKB:Q17RS7 UniProtKB:Q64MA3 UniProtKB:Q7K734 UniProtKB:Q9UQ84 WB:WBGene00000794	F	Seeded From UniProt	complete
enables	GO:0030145	manganese ion binding	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:102779 PANTHER:PTN000871763	F	Seeded From UniProt	complete
enables	GO:0017108	5'-flap endonuclease activity	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0263831 PANTHER:PTN000118612 PomBase:SPAC3G6.06c SGD:S000001596 SGD:S000005559 UniProtKB:P39748 UniProtKB:Q17RS7	F	Seeded From UniProt	complete
enables	GO:0008409	5'-3' exonuclease activity	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000118791 PomBase:SPAC3G6.06c SGD:S000001596 UniProtKB:P39748	F	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000118792 RGD:621821 SGD:S000000843 SGD:S000001596 UniProtKB:P39748 WB:WBGene00000794	C	Seeded From UniProt	complete
enables	GO:0004523	RNA-DNA hybrid ribonuclease activity	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000871763 UniProtKB:P39748	F	Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:102779 PANTHER:PTN000871763	F	Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:25378300^[11]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005730	nucleolus	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0090502	RNA phosphodiester bond hydrolysis, endonucleolytic	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004523	P	Seeded From UniProt	complete
involved_in	GO:0090502	RNA phosphodiester bond hydrolysis, endonucleolytic	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004523	P	Seeded From UniProt	complete
involved_in	GO:0007613	memory	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5XIP6 ensembl:ENSRNOP00000027842	P	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5XIP6 ensembl:ENSRNOP00000027842	C	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR008918	F	Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR008918	F	Seeded From UniProt	complete
enables	GO:0004518	nuclease activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006084 InterPro:IPR006085 InterPro:IPR006086	F	Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006084 InterPro:IPR006085	P	Seeded From UniProt	complete
enables	GO:0016788	hydrolase activity, acting on ester bonds	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR019974 InterPro:IPR023426	F	Seeded From UniProt	complete
involved_in	GO:0006284	base-excision repair	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000337265	P	Seeded From UniProt	complete
enables	GO:0017108	5'-flap endonuclease activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000337265	F	Seeded From UniProt	complete
enables	GO:0008409	5'-3' exonuclease activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000337265	F	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000337265	C	Seeded From UniProt	complete
involved_in	GO:0043137	DNA replication, removal of RNA primer	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000337265	P	Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000337265	F	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000337265	F	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000337265	C	Seeded From UniProt	complete
involved_in	GO:0009650	UV protection	PMID:8007985^[12]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0008309	double-stranded DNA exodeoxyribonuclease activity	PMID:8131753^[13]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006302	double-strand break repair	PMID:8131753^[13]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	PMID:8007985^[12]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006260	DNA replication	PMID:9778254^[14]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0004527	exonuclease activity	PMID:9778254^[14]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004519	endonuclease activity	PMID:8131753^[13]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003690	double-stranded DNA binding	PMID:8131753^[13]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003684	damaged DNA binding	PMID:8007985^[12]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0032201	telomere maintenance via semi-conservative replication	Reactome:R-HSA-174446	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0017108	5'-flap endonuclease activity	Reactome:R-HSA-69152 Reactome:R-HSA-5687664 Reactome:R-HSA-5651782 Reactome:R-HSA-174446 Reactome:R-HSA-110363	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-HSA-69152 Reactome:R-HSA-5687664 Reactome:R-HSA-5687653 Reactome:R-HSA-5687640 Reactome:R-HSA-5687484 Reactome:R-HSA-5651782 Reactome:R-HSA-5651739 Reactome:R-HSA-5651723 Reactome:R-HSA-5649883 Reactome:R-HSA-5649873 Reactome:R-HSA-174446 Reactome:R-HSA-110368 Reactome:R-HSA-110364 Reactome:R-HSA-110363	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0000724	double-strand break repair via homologous recombination	Reactome:R-HSA-5693538	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0004527	exonuclease activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0269	F	Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0234	P	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0496 UniProtKB-SubCell:SL-0173	C	Seeded From UniProt	complete
involved_in	GO:0006260	DNA replication	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0235	P	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
enables	GO:0004519	endonuclease activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0255	F	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539	C	Seeded From UniProt	complete
enables	GO:0004518	nuclease activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0540	F	Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0227	P	Seeded From UniProt	complete
part_of	GO:0005730	nucleolus	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0188	C	Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0190	C	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 Farina, A et al. (2008) Studies with the human cohesin establishment factor, ChlR1. Association of ChlR1 with Ctf18-RFC and Fen1. J. Biol. Chem. 283 20925-36 PubMed GONUTS page
↑ Grolimund, L et al. (2013) A quantitative telomeric chromatin isolation protocol identifies different telomeric states. Nat Commun 4 2848 PubMed GONUTS page
↑ Déjardin, J & Kingston, RE (2009) Purification of proteins associated with specific genomic Loci. Cell 136 175-86 PubMed GONUTS page
↑ Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 Zheng, L et al. (2008) Human DNA2 is a mitochondrial nuclease/helicase for efficient processing of DNA replication and repair intermediates. Mol. Cell 32 325-36 PubMed GONUTS page
↑ Shen, B et al. (1996) Essential amino acids for substrate binding and catalysis of human flap endonuclease 1. J. Biol. Chem. 271 9173-6 PubMed GONUTS page
↑ ^7.0 ^7.1 Qiu, J et al. (2002) Arginine residues 47 and 70 of human flap endonuclease-1 are involved in DNA substrate interactions and cleavage site determination. J. Biol. Chem. 277 24659-66 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 Robins, P et al. (1994) Structural and functional homology between mammalian DNase IV and the 5'-nuclease domain of Escherichia coli DNA polymerase I. J. Biol. Chem. 269 28535-8 PubMed GONUTS page
↑ Benrezkallah, D et al. (2015) Molecular dynamics of the salt dependence of a cold-adapted enzyme: endonuclease I. J. Biomol. Struct. Dyn. 33 2511-21 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 ^10.4 ^10.5 ^10.6 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Szczesny, B et al. (2014) Opposing roles of mitochondrial and nuclear PARP1 in the regulation of mitochondrial and nuclear DNA integrity: implications for the regulation of mitochondrial function. Nucleic Acids Res. 42 13161-73 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 Murray, JM et al. (1994) 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. Mol. Cell. Biol. 14 4878-88 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 ^13.3 Harrington, JJ & Lieber, MR (1994) The characterization of a mammalian DNA structure-specific endonuclease. EMBO J. 13 1235-46 PubMed GONUTS page
↑ ^14.0 ^14.1 Hosfield, DJ et al. (1998) Structure of the DNA repair and replication endonuclease and exonuclease FEN-1: coupling DNA and PCNA binding to FEN-1 activity. Cell 95 135-46 PubMed GONUTS page

[PMID:18499658-1] 1.0 ^1.1 ^1.2 Farina, A et al. (2008) Studies with the human cohesin establishment factor, ChlR1. Association of ChlR1 with Ctf18-RFC and Fen1. J. Biol. Chem. 283 20925-36 PubMed GONUTS page

[PMID:24270157-2] Grolimund, L et al. (2013) A quantitative telomeric chromatin isolation protocol identifies different telomeric states. Nat Commun 4 2848 PubMed GONUTS page

[PMID:19135898-3] Déjardin, J & Kingston, RE (2009) Purification of proteins associated with specific genomic Loci. Cell 136 175-86 PubMed GONUTS page

[PMID:19946888-4] Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page

[PMID:18995831-5] 5.0 ^5.1 ^5.2 ^5.3 Zheng, L et al. (2008) Human DNA2 is a mitochondrial nuclease/helicase for efficient processing of DNA replication and repair intermediates. Mol. Cell 32 325-36 PubMed GONUTS page

[PMID:8621570-6] Shen, B et al. (1996) Essential amino acids for substrate binding and catalysis of human flap endonuclease 1. J. Biol. Chem. 271 9173-6 PubMed GONUTS page

[PMID:11986308-7] 7.0 ^7.1 Qiu, J et al. (2002) Arginine residues 47 and 70 of human flap endonuclease-1 are involved in DNA substrate interactions and cleavage site determination. J. Biol. Chem. 277 24659-66 PubMed GONUTS page

[PMID:7961795-8] 8.0 ^8.1 ^8.2 Robins, P et al. (1994) Structural and functional homology between mammalian DNase IV and the 5'-nuclease domain of Escherichia coli DNA polymerase I. J. Biol. Chem. 269 28535-8 PubMed GONUTS page

[PMID:25650046-9] Benrezkallah, D et al. (2015) Molecular dynamics of the salt dependence of a cold-adapted enzyme: endonuclease I. J. Biomol. Struct. Dyn. 33 2511-21 PubMed GONUTS page

[PMID:21873635-10] 10.0 ^10.1 ^10.2 ^10.3 ^10.4 ^10.5 ^10.6 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:25378300-11] Szczesny, B et al. (2014) Opposing roles of mitochondrial and nuclear PARP1 in the regulation of mitochondrial and nuclear DNA integrity: implications for the regulation of mitochondrial function. Nucleic Acids Res. 42 13161-73 PubMed GONUTS page

[PMID:8007985-12] 12.0 ^12.1 ^12.2 Murray, JM et al. (1994) 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. Mol. Cell. Biol. 14 4878-88 PubMed GONUTS page

[PMID:8131753-13] 13.0 ^13.1 ^13.2 ^13.3 Harrington, JJ & Lieber, MR (1994) The characterization of a mammalian DNA structure-specific endonuclease. EMBO J. 13 1235-46 PubMed GONUTS page

[PMID:9778254-14] 14.0 ^14.1 Hosfield, DJ et al. (1998) Structure of the DNA repair and replication endonuclease and exonuclease FEN-1: coupling DNA and PCNA binding to FEN-1 activity. Cell 95 135-46 PubMed GONUTS page

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HUMAN:FEN1

Contents

Annotations

Notes

References

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