UniProtKB - Q6FHX6 (Q6FHX6_HUMAN)
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Protein
Flap endonuclease 1
Gene
FEN1
Organism
Homo sapiens (Human)
Status
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 annotationSAAS annotation
Cofactori
Mg2+UniRule annotationNote: 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.UniRule annotation
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 34 | Magnesium 1UniRule annotation | 1 | |
Binding sitei | 47 | DNA substrateUniRule annotation | 1 | |
Binding sitei | 70 | DNA substrateUniRule annotation | 1 | |
Metal bindingi | 86 | Magnesium 1UniRule annotation | 1 | |
Metal bindingi | 158 | Magnesium 1UniRule annotation | 1 | |
Binding sitei | 158 | DNA substrateUniRule annotation | 1 | |
Metal bindingi | 160 | Magnesium 1UniRule annotation | 1 | |
Metal bindingi | 179 | Magnesium 2UniRule annotation | 1 | |
Metal bindingi | 181 | Magnesium 2UniRule annotation | 1 | |
Binding sitei | 231 | DNA substrateUniRule annotation | 1 | |
Metal bindingi | 233 | Magnesium 2UniRule annotation | 1 | |
Binding sitei | 233 | DNA substrateUniRule annotation | 1 |
GO - Molecular functioni
- 5'-3' exonuclease activity Source: UniProtKB-UniRule
- 5'-flap endonuclease activity Source: UniProtKB-UniRule
- DNA binding Source: UniProtKB-UniRule
- magnesium ion binding Source: UniProtKB-UniRule
GO - Biological processi
- base-excision repair Source: UniProtKB-UniRule
- DNA replication, removal of RNA primer Source: UniProtKB-UniRule
- memory Source: Ensembl
Keywordsi
Molecular function | EndonucleaseUniRule annotationImported, ExonucleaseUniRule annotation, Hydrolase, Nuclease |
Biological process | DNA damage, DNA repairUniRule annotation, DNA replicationUniRule annotation |
Ligand | MagnesiumUniRule annotation, Metal-bindingUniRule annotation |
Names & Taxonomyi
Protein namesi | Recommended name: Flap endonuclease 1UniRule annotation (EC:3.1.-.-UniRule annotation)Short name: FEN-1UniRule annotation Alternative name(s): Flap structure-specific endonuclease 1UniRule annotation |
Gene namesi | Name:FEN1UniRule annotationImported ORF Names:hCG_40848Imported |
Organismi | Homo sapiens (Human)Imported |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Organism-specific databases
EuPathDBi | HostDB:ENSG00000168496.3. |
Subcellular locationi
Keywords - Cellular componenti
MitochondrionUniRule annotationSAAS annotation, NucleusUniRule annotationSAAS annotationPTM / Processingi
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 19 | Symmetric dimethylarginine; by PRMT5UniRule annotation | 1 | |
Modified residuei | 100 | Symmetric dimethylarginine; by PRMT5UniRule annotation | 1 | |
Modified residuei | 104 | Symmetric dimethylarginine; by PRMT5UniRule annotation | 1 | |
Modified residuei | 187 | Phosphoserine; by CDK2UniRule annotation | 1 | |
Modified residuei | 192 | Symmetric dimethylarginine; by PRMT5UniRule annotation | 1 |
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 annotation
Methylation at Arg-192 by PRMT5 impedes Ser-187 phosphorylation and increases interaction with PCNA.UniRule 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.UniRule annotation
Keywords - PTMi
MethylationUniRule annotation, PhosphoproteinUniRule annotationInteractioni
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.UniRule annotation
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 1 – 107 | XPGNInterPro annotationAdd BLAST | 107 | |
Domaini | 146 – 218 | XPGIInterPro annotationAdd BLAST | 73 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 104 | N-domainUniRule annotationAdd BLAST | 104 | |
Regioni | 122 – 253 | I-domainUniRule annotationAdd BLAST | 132 | |
Regioni | 336 – 344 | Interaction with PCNAUniRule annotation | 9 |
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Coiled coili | 97 – 136 | Sequence analysisAdd BLAST | 40 |
Sequence similaritiesi
Keywords - Domaini
Coiled coilSequence analysisPhylogenomic databases
eggNOGi | KOG2519. Eukaryota. COG0258. LUCA. |
HOVERGENi | HBG000844. |
KOi | K04799. |
OMAi | GSQDYDS. |
OrthoDBi | EOG091G0C0E. |
Family and domain databases
CDDi | cd09867. PIN_FEN1. 1 hit. |
HAMAPi | MF_00614. Fen. 1 hit. |
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. |
PANTHERi | PTHR11081. PTHR11081. 1 hit. |
Pfami | View protein in Pfam PF00867. XPG_I. 1 hit. PF00752. XPG_N. 1 hit. |
PRINTSi | PR00853. XPGRADSUPER. |
SMARTi | View protein in SMART SM00279. HhH2. 1 hit. SM00484. XPGI. 1 hit. SM00485. XPGN. 1 hit. |
SUPFAMi | SSF47807. SSF47807. 1 hit. SSF88723. SSF88723. 1 hit. |
PROSITEi | View protein in PROSITE PS00841. XPG_1. 1 hit. PS00842. XPG_2. 1 hit. |
i Sequence
Sequence statusi: Complete.
Q6FHX6-1 [UniParc]FASTAAdd to basket
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BT019524 mRNA. Translation: AAV38331.1. AK312761 mRNA. Translation: BAG35627.1. CR536562 mRNA. Translation: CAG38799.1. CH471076 Genomic DNA. Translation: EAW73972.1. |
RefSeqi | NP_004102.1. NM_004111.5. |
UniGenei | Hs.409065. |
Genome annotation databases
GeneIDi | 2237. |
KEGGi | hsa:2237. |
UCSCi | uc001nsg.4. human. |
Similar proteinsi
Entry informationi
Entry namei | Q6FHX6_HUMAN | |
Accessioni | Q6FHX6Primary (citable) accession number: Q6FHX6 | |
Entry historyi | Integrated into UniProtKB/TrEMBL: | May 10, 2005 |
Last sequence update: | May 10, 2005 | |
Last modified: | March 28, 2018 | |
This is version 122 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Unreviewed (UniProtKB/TrEMBL) | |
Disclaimer | Any 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. |