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Protein Page:
FEN1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
FEN1 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. 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. Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily. Note: This description may include information from UniProtKB.
Protein type: Ribonuclease; EC 3.1.-.-; Deoxyribonuclease; DNA binding protein; DNA repair, damage
Cellular Component: nucleoplasm; mitochondrion; nucleolus; nucleus
Molecular Function: 5'-3' exonuclease activity; protein binding; DNA binding; 5'-flap endonuclease activity; endonuclease activity; manganese ion binding; double-stranded DNA binding; exonuclease activity; magnesium ion binding; damaged DNA binding; ribonuclease H activity; double-stranded DNA specific exodeoxyribonuclease activity
Biological Process: DNA replication, removal of RNA primer; phosphoinositide-mediated signaling; DNA strand elongation during DNA replication; DNA repair; DNA catabolic process, endonucleolytic; memory; telomere maintenance via semi-conservative replication; UV protection; base-excision repair; double-strand break repair; telomere maintenance via recombination; mitotic cell cycle; DNA catabolic process, exonucleolytic; DNA replication; telomere maintenance
Reference #:  P39748 (UniProtKB)
Alt. Names/Synonyms: DNase IV; FEN-1; FEN1; Flap endonuclease 1; Flap structure-specific endonuclease 1; hFEN-1; Maturation factor 1; maturation factor-1; MF1; RAD2
Gene Symbols: FEN1
Molecular weight: 42,593 Da
Basal Isoelectric point: 8.8  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

FEN1

Protein Structure Not Found.


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Sites Implicated In
cell cycle regulation: S187‑p, R192‑m
enzymatic activity, inhibited: S187‑p
intracellular localization: S187‑p, R192‑m
molecular association, regulation: S187‑p, R192‑m
phosphorylation: R192‑m
protein degradation: K168‑s, S187‑p, K354‑u
sumoylation: S187‑p
ubiquitination: K168‑s, K354‑u

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 4 K8-u MGIQGLAkLIADVAP
0 1 S16-p LIADVAPsAIrENDI
1 0 R19-m DVAPsAIrENDIkSY
0 3 K24-u AIrENDIkSYFGRKV
0 1 S25 IrENDIkSYFGRKVA
0 2 K80-a RMMENGIkPVYVFDG
1 0 R100-m KSGELAKrsERrAEA
0 3 S101-p SGELAKrsERrAEAE
1 0 R104-m LAKrsERrAEAEkQL
0 20 K109-a ERrAEAEkQLQQAQA
0 3 K109-u ERrAEAEkQLQQAQA
0 2 K125-u GAEQEVEkFTKRLVK
1 1 K168-s ASCAALVkAGkVYAA
0 2 K171-u AALVkAGkVYAAATE
4 1 S187-p MDCLTFGsPVLMrHL
1 0 R192-m FGsPVLMrHLtAsEA
1 3 T195-p PVLMrHLtAsEAkKL
0 1 S197-p LMrHLtAsEAkKLPI
0 32 K200-a HLtAsEAkKLPIQEF
0 2 Y234-p CILLGSDyCESIRGI
0 4 K252-u RAVDLIQkHKsIEEI
0 1 S255-p DLIQkHKsIEEIVRR
0 1 K267-a VRRLDPNkYPVPENW
0 1 K277-u VPENWLHkEAHQLFL
0 1 S293-p PEVLDPEsVELkWSE
0 1 K297-u DPEsVELkWSEPNEE
0 3 K314-u IKFMCGEkQFSEERI
0 1 S331-p GVKRLSKsRQGstQG
0 4 S335-p LSKsRQGstQGRLDD
0 1 T336-p SKsRQGstQGRLDDF
1 1 K354-a TGSLSSAkRKEPEPK
1 2 K354-u TGSLSSAkRKEPEPK
0 2 T364-p EPEPKGStKKKAKTG
1 20 K375-a AKTGAAGkFkRGk__
1 0 K377-a TGAAGkFkRGk____
1 0 K380-a AGkFkRGk_______
0 1 - gap
  mouse

 
K8 MGIHGLAKLIADVAP
S16 LIADVAPSAIRENDI
R19 DVAPSAIRENDIKsY
K24 AIRENDIKsYFGRKV
S25-p IRENDIKsYFGRKVA
K80-a RMMENGIkPVYVFDG
R100 KSGELAKRSERRAEA
S101 SGELAKRSERRAEAE
R104 LAKRSERRAEAEKQL
K109 ERRAEAEKQLQQAQE
K109 ERRAEAEKQLQQAQE
K125 GMEEEVEKFTKRLVK
K168 ASCAALAKAGKVYAA
K171 AALAKAGKVYAAATE
S187 MDCLTFGSPVLMRHL
R192 FGSPVLMRHLTASEA
T195 PVLMRHLTASEAkKL
S197 LMRHLTASEAkKLPI
K200-a HLTASEAkKLPIQEF
Y234 CILLGSDYCESIRGI
K252 RAVDLIQKHKSIEEI
S255 DLIQKHKSIEEIVRR
K267 VRRLDPSKYPVPENW
K277 VPENWLHKEAQQLFL
S293 PEVLDPESVELKWSE
K297 DPESVELKWSEPNEE
K314 VKFMCGEKQFSEERI
S331 GVKRLSKSRQGSTQG
S335 LSKSRQGSTQGRLDD
T336 SKSRQGSTQGRLDDF
K354 TGSLSSAKRKEPEPK
K354 TGSLSSAKRKEPEPK
A364 EPEPKGPAKKKAKTG
K375 AKTGGAGKFRRGKIN
R377 TGGAGKFRRGKINLs
K380 AGKFRRGKINLsFPS
S384-p RRGKINLsFPSTVLD
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