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UniProtKB - P39748 (FEN1_HUMAN)

Entry version 193 (08 May 2019)
Sequence version 1 (01 Feb 1995)
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Protein

Flap endonuclease 1

Gene

FEN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.UniRule annotation6 Publications

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>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)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi34Magnesium 11
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei47DNA substrate1
Binding sitei70DNA substrate1
Metal bindingi86Magnesium 11
Metal bindingi158Magnesium 11
Binding sitei158DNA substrate1
Metal bindingi160Magnesium 11
Metal bindingi179Magnesium 21
Metal bindingi181Magnesium 21
Binding sitei231DNA substrate1
Metal bindingi233Magnesium 21
Binding sitei233DNA substrate1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionEndonuclease, Exonuclease, Hydrolase, Nuclease
Biological processDNA damage, DNA repair, DNA replication
LigandMagnesium, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-110362 POLB-Dependent Long Patch Base Excision Repair
R-HSA-162594 Early Phase of HIV Life Cycle
R-HSA-174437 Removal of the Flap Intermediate from the C-strand
R-HSA-5651801 PCNA-Dependent Long Patch Base Excision Repair
R-HSA-5685939 HDR through MMEJ (alt-NHEJ)
R-HSA-69166 Removal of the Flap Intermediate

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		P39748

SIGNOR Signaling Network Open Resource

More...SIGNORi		P39748

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:FEN1UniRule annotation
Synonyms:RAD2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:3650 FEN1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		600393 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P39748

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi29R → A: No significant effect on exonuclease activity or flap endonuclease activity. 1 Publication1
Mutagenesisi34D → A: Loss of flap endonuclease activity but substrate binding activity is retained. 1 Publication1
Mutagenesisi47R → A: Significantly reduced exonuclease activity and reduced substrate binding. The positions of the cleavage sites are also shifted. 1 Publication1
Mutagenesisi70R → A: Loss of exonuclease activity and reduced endonuclease activity. Reduced substrate binding. 1 Publication1
Mutagenesisi73R → A: No significant effect on exonuclease activity or flap endonuclease activity. 1 Publication1
Mutagenesisi80K → A: No significant effect on exonuclease activity or flap endonuclease activity. 1 Publication1
Mutagenesisi86D → A: Loss of flap endonuclease activity but substrate binding activity is retained. 1 Publication1
Mutagenesisi103R → A: No effect on flap endonuclease activity or substrate binding. 1 Publication1
Mutagenesisi158E → A: Loss of flap endonuclease activity and substrate binding. 1 Publication1
Mutagenesisi179D → A: No effect on flap endonuclease activity or substrate binding. 1 Publication1
Mutagenesisi181D → A: Loss of flap endonuclease activity but substrate binding activity is retained. 1 Publication1
Mutagenesisi187S → A: Fails to translocate from nucleoli to the nuclear plasma. 1 Publication1
Mutagenesisi187S → D: Diminishes nucleolar localization. 1 Publication1
Mutagenesisi192R → K: Impairs ability to localize to sites of DNA replication or repair. 1 Publication1
Mutagenesisi231G → A: Loss of flap endonuclease activity and substrate binding. 1 Publication1
Mutagenesisi233D → A: Loss of flap endonuclease activity and substrate binding. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		2237

Open Targets

More...OpenTargetsi		ENSG00000168496

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA28090

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL5027

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		FEN1

Domain mapping of disease mutations (DMDM)

More...DMDMi		729475

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001540691 – 380Flap endonuclease 1Add BLAST380

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei19Symmetric dimethylarginine; by PRMT5UniRule annotation1 Publication1
Modified residuei80N6-acetyllysineCombined sources1
Modified residuei100Symmetric dimethylarginine; by PRMT5UniRule annotation1 Publication1
Modified residuei104Symmetric dimethylarginine; by PRMT5UniRule annotation1 Publication1
Modified residuei187Phosphoserine; by CDK2UniRule annotation1 Publication1
Modified residuei192Symmetric dimethylarginine; by PRMT5UniRule annotation1 Publication1
Modified residuei197PhosphoserineCombined sources1
Modified residuei255PhosphoserineCombined sources1
Modified residuei293PhosphoserineCombined sources1
Modified residuei335PhosphoserineCombined sources1
Modified residuei336PhosphothreonineCombined sources1
Modified residuei354N6-acetyllysineUniRule annotation1 Publication1
Modified residuei364PhosphothreonineCombined sources1
Modified residuei375N6-acetyllysineUniRule annotationCombined sources1 Publication1
Modified residuei377N6-acetyllysineUniRule annotation1 Publication1
Modified residuei380N6-acetyllysineUniRule annotation1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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.UniRule annotation1 Publication
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.UniRule annotation1 Publication
Methylation at Arg-192 by PRMT5 impedes Ser-187 phosphorylation and increases interaction with PCNA.UniRule annotation1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P39748

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P39748

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P39748

PeptideAtlas

More...PeptideAtlasi		P39748

PRoteomics IDEntifications database

More...PRIDEi		P39748

ProteomicsDB human proteome resource

More...ProteomicsDBi		55319

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P39748-1 [P39748-1]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P39748

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P39748

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P39748

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000168496 Expressed in 219 organ(s), highest expression level in amniotic fluid

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P39748 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P39748 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB002262
HPA006748

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Three molecules of FEN1 bind to one PCNA trimer with each molecule binding to one PCNA monomer (PubMed:15616578). PCNA stimulates the nuclease activity without altering cleavage specificity (PubMed:15616578). The C-terminal domain binds EP300; can bind simultaneously to both PCNA and EP300 (PubMed:11430825). Interacts with PCNA; can bind simultaneously to both PCNA and EP300 (PubMed:9305916, PubMed:11430825). Interacts with DDX11; this interaction is direct and increases flap endonuclease activity of FEN1 (PubMed:18499658).UniRule annotation4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		108528, 82 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P39748

Database of interacting proteins

More...DIPi		DIP-24216N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P39748

Protein interaction database and analysis system

More...IntActi		P39748, 40 interactors

Molecular INTeraction database

More...MINTi		P39748

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000305480

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P39748

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1380
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB 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[»]
5E0VX-ray2.07C/D335-350[»]
5FV7X-ray2.84A/B1-336[»]
5K97X-ray2.10A2-336[»]
5KSEX-ray2.10A2-336[»]
5UM9X-ray2.81A2-336[»]
5ZODX-ray1.90A1-333[»]
5ZOEX-ray1.95A1-333[»]
5ZOFX-ray2.25A1-333[»]
5ZOGX-ray2.30A1-333[»]

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P39748

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P39748

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 104N-domainAdd BLAST104
Regioni122 – 253I-domainAdd BLAST132
Regioni336 – 344Interaction with PCNA1 Publication9

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2519 Eukaryota
COG0258 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155807

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000193853

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P39748

KEGG Orthology (KO)

More...KOi		K04799

Identification of Orthologs from Complete Genome Data

More...OMAi		CDYLDPI

Database of Orthologous Groups

More...OrthoDBi		1094524at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P39748

TreeFam database of animal gene trees

More...TreeFami		TF105701

Family and domain databases

Conserved Domains Database

More...CDDi		cd09867 PIN_FEN1, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00614 Fen, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR036279 5-3_exonuclease_C_sf
IPR023426 Flap_endonuc
IPR008918 HhH2
IPR029060 PIN-like_dom_sf
IPR006086 XPG-I_dom
IPR006084 XPG/Rad2
IPR019974 XPG_CS
IPR006085 XPG_DNA_repair_N

The PANTHER Classification System

More...PANTHERi		PTHR11081 PTHR11081, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00867 XPG_I, 1 hit
PF00752 XPG_N, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00853 XPGRADSUPER

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00279 HhH2, 1 hit
SM00484 XPGI, 1 hit
SM00485 XPGN, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47807 SSF47807, 1 hit
SSF88723 SSF88723, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00841 XPG_1, 1 hit
PS00842 XPG_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative initiation. AlignAdd to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F5H1Y3F5H1Y3_HUMAN
Flap endonuclease 1
FEN1
165Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
I3L3E9I3L3E9_HUMAN
Flap endonuclease 1
FEN1
154Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0475201 – 64Missing in isoform FENMIT. CuratedAdd BLAST64

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS8010.1 [P39748-1]

Protein sequence database of the Protein Information Resource

More...PIRi		A56531

NCBI Reference Sequences

More...RefSeqi		NP_004102.1, NM_004111.5 [P39748-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000305885; ENSP00000305480; ENSG00000168496 [P39748-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		2237

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:2237

Keywords - Coding sequence diversityi

Alternative initiation

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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
CCDSiCCDS8010.1 [P39748-1]
PIRiA56531
RefSeqiNP_004102.1, NM_004111.5 [P39748-1]

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5E0VX-ray2.07C/D335-350[»]
5FV7X-ray2.84A/B1-336[»]
5K97X-ray2.10A2-336[»]
5KSEX-ray2.10A2-336[»]
5UM9X-ray2.81A2-336[»]
5ZODX-ray1.90A1-333[»]
5ZOEX-ray1.95A1-333[»]
5ZOFX-ray2.25A1-333[»]
5ZOGX-ray2.30A1-333[»]
SMRiP39748
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108528, 82 interactors
CORUMiP39748
DIPiDIP-24216N
ELMiP39748
IntActiP39748, 40 interactors
MINTiP39748
STRINGi9606.ENSP00000305480

Chemistry databases

BindingDBiP39748
ChEMBLiCHEMBL5027

PTM databases

iPTMnetiP39748
PhosphoSitePlusiP39748
SwissPalmiP39748

Polymorphism and mutation databases

BioMutaiFEN1
DMDMi729475

Proteomic databases

EPDiP39748
jPOSTiP39748
PaxDbiP39748
PeptideAtlasiP39748
PRIDEiP39748
ProteomicsDBi55319
TopDownProteomicsiP39748-1 [P39748-1]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		2237
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000305885; ENSP00000305480; ENSG00000168496 [P39748-1]
GeneIDi2237
KEGGihsa:2237

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2237
DisGeNETi2237

GeneCards: human genes, protein and diseases

More...GeneCardsi		FEN1
HGNCiHGNC:3650 FEN1
HPAiCAB002262
HPA006748
MIMi600393 gene
neXtProtiNX_P39748
OpenTargetsiENSG00000168496
PharmGKBiPA28090

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG2519 Eukaryota
COG0258 LUCA
GeneTreeiENSGT00940000155807
HOGENOMiHOG000193853
InParanoidiP39748
KOiK04799
OMAiCDYLDPI
OrthoDBi1094524at2759
PhylomeDBiP39748
TreeFamiTF105701

Enzyme and pathway databases

ReactomeiR-HSA-110362 POLB-Dependent Long Patch Base Excision Repair
R-HSA-162594 Early Phase of HIV Life Cycle
R-HSA-174437 Removal of the Flap Intermediate from the C-strand
R-HSA-5651801 PCNA-Dependent Long Patch Base Excision Repair
R-HSA-5685939 HDR through MMEJ (alt-NHEJ)
R-HSA-69166 Removal of the Flap Intermediate
SignaLinkiP39748
SIGNORiP39748

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		FEN1 human
EvolutionaryTraceiP39748

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Flap_structure-specific_endonuclease_1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		2237

Protein Ontology

More...PROi		PR:P39748

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000168496 Expressed in 219 organ(s), highest expression level in amniotic fluid
ExpressionAtlasiP39748 baseline and differential
GenevisibleiP39748 HS

Family and domain databases

CDDicd09867 PIN_FEN1, 1 hit
HAMAPiMF_00614 Fen, 1 hit
InterProiView protein in InterPro
IPR036279 5-3_exonuclease_C_sf
IPR023426 Flap_endonuc
IPR008918 HhH2
IPR029060 PIN-like_dom_sf
IPR006086 XPG-I_dom
IPR006084 XPG/Rad2
IPR019974 XPG_CS
IPR006085 XPG_DNA_repair_N
PANTHERiPTHR11081 PTHR11081, 1 hit
PfamiView protein in Pfam
PF00867 XPG_I, 1 hit
PF00752 XPG_N, 1 hit
PRINTSiPR00853 XPGRADSUPER
SMARTiView protein in SMART
SM00279 HhH2, 1 hit
SM00484 XPGI, 1 hit
SM00485 XPGN, 1 hit
SUPFAMiSSF47807 SSF47807, 1 hit
SSF88723 SSF88723, 1 hit
PROSITEiView protein in PROSITE
PS00841 XPG_1, 1 hit
PS00842 XPG_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFEN1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P39748
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 8, 2019
This is version 193 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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