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Protein Page:
FEN1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

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: Nuclear receptor co-regulator; DNA repair, damage; Deoxyribonuclease; Nucleolus; EC 3.1.-.-; Ribonuclease; DNA binding protein
Chromosomal Location of Human Ortholog: 11q12
Cellular Component: nucleoplasm; membrane; 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‑me
enzymatic activity, inhibited: S187‑p
intracellular localization: S187‑p, R192‑me
molecular association, regulation: S187‑p, R192‑me
phosphorylation: R192‑me
protein degradation: K168‑sm, S187‑p, K354‑ub
sumoylation: S187‑p
ubiquitination: K168‑sm, K354‑ub

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-ub MGIQGLAkLIADVAP
0 1 S16-p LIADVAPsAIrENDI
1 0 R19-me DVAPsAIrENDIkSY
0 3 K24-ub AIrENDIkSYFGRKV
0 1 S25 IrENDIkSYFGRKVA
0 2 K80-ac RMMENGIkPVYVFDG
0 1 K88 PVYVFDGKPPQLKSG
0 1 K99-ub LKSGELAkrsERrAE
1 0 R100-me KSGELAkrsERrAEA
0 3 S101-p SGELAkrsERrAEAE
1 0 R104-me LAkrsERrAEAEkQL
0 21 K109-ac ERrAEAEkQLQQAQA
0 3 K109-ub ERrAEAEkQLQQAQA
0 1 K125-ac GAEQEVEkFTKRLVk
0 2 K125-ub GAEQEVEkFTKRLVk
0 1 K132-ub kFTKRLVkVTKQHND
1 1 K168-sm ASCAALVkAGkVYAA
0 2 K171-ub AALVkAGkVYAAATE
4 1 S187-p MDCLTFGsPVLMrHL
1 0 R192-me FGsPVLMrHLtAsEA
1 3 T195-p PVLMrHLtAsEAkkL
0 2 S197-p LMrHLtAsEAkkLPI
0 33 K200-ac HLtAsEAkkLPIQEF
0 1 K200-sc HLtAsEAkkLPIQEF
0 1 K201-ac LtAsEAkkLPIQEFH
0 2 Y234-p CILLGSDyCESIRGI
0 4 K252-ub RAVDLIQkHKsIEEI
0 1 S255-p DLIQkHKsIEEIVRR
0 1 K267-ac VRRLDPNkyPVPENW
0 1 Y268-p RRLDPNkyPVPENWL
0 1 K277-ub VPENWLHkEAHQLFL
0 1 S293-p PEVLDPEsVELkWSE
0 1 K297-ub DPEsVELkWSEPNEE
0 3 K314-ub IKFMCGEkQFsEERI
0 1 S317-p MCGEkQFsEERIRSG
0 1 S329-p RSGVKRLsKsRQGst
0 2 S331-p GVKRLsKsRQGstQG
0 6 S335-p LsKsRQGstQGRLDD
0 1 T336-p sKsRQGstQGRLDDF
0 1 K345-ub GRLDDFFkVTGSLss
0 1 S351-p FkVTGSLssAkRKEP
0 1 S352-p kVTGSLssAkRKEPE
1 1 K354-ac TGSLssAkRKEPEPK
1 2 K354-ub TGSLssAkRKEPEPK
0 1 K354-sc TGSLssAkRKEPEPK
0 2 T364-p EPEPKGStKKKAKTG
1 20 K375-ac AKTGAAGkFkRGk__
1 0 K377-ac TGAAGkFkRGk____
1 0 K380-ac AGkFkRGk_______
0 1 - gap
  mouse

► Hide Isoforms
 
K8 MGIHGLAKLIADVAP
S16 LIADVAPSAIRENDI
R19 DVAPSAIRENDIKsY
K24 AIRENDIKsYFGRKV
S25-p IRENDIKsYFGRKVA
K78-ac IRMENGIkPVYVFDG
K86-ac PVYVFDGkPPQLKSG
K97 LKSGELAKRSERRAE
R98 KSGELAKRSERRAEA
S99 SGELAKRSERRAEAE
R102 LAKRSERRAEAEKQL
K107 ERRAEAEKQLQQAQE
K107 ERRAEAEKQLQQAQE
K123 GMEEEVEKFTKRLVK
K123 GMEEEVEKFTKRLVK
K130 KFTKRLVKVTKQHND
K166 ASCAALAKAGKVYAA
K169 AALAKAGKVYAAATE
S185 MDCLTFGSPVLMRHL
R190 FGSPVLMRHLTASEA
T193 PVLMRHLTASEAkKL
S195 LMRHLTASEAkKLPI
K198-ac HLTASEAkKLPIQEF
K198 HLTASEAKKLPIQEF
K199 LTASEAkKLPIQEFH
Y232 CILLGSDYCESIRGI
K250 RAVDLIQKHKSIEEI
S253 DLIQKHKSIEEIVRR
K265 VRRLDPSKYPVPENW
Y266 RRLDPSKYPVPENWL
K275 VPENWLHKEAQQLFL
S291 PEVVDPESVELKWSE
K295 DPESVELKWSEPNEE
K312 VKFMCGEKQFSEERI
S315 MCGEKQFSEERIRSG
S327 RSGVKRLSKSRQGST
S329 GVKRLSKSRQGSTQG
S333 LSKSRQGSTQGRLDD
T334 SKSRQGSTQGRLDDF
K343 GRLDDFFKVTGSLSS
S349 FKVTGSLSSAKRKEP
S350 KVTGSLSSAKRKEPE
K352 TGSLSSAKRKEPEPK
K352 TGSLSSAKRKEPEPK
K352 TGSLSSAKRKEPEPK
A362 EPEPKGPAKKKAKTG
K373 AKTGGAGKFRRGK__
R375 TGGAGKFRRGK____
K378 AGKFRRGK_______
- gap
  FEN1 iso2  
K8 MGIHGLAKLIADVAP
S16 LIADVAPSAIRENDI
R19 DVAPSAIRENDIKSY
K24 AIRENDIKSYFGRKV
S25 IRENDIKSYFGRKVA
K80 RMMENGIKPVYVFDG
K88 PVYVFDGKPPQLKSG
K99 LKSGELAKRSERRAE
R100 KSGELAKRSERRAEA
S101 SGELAKRSERRAEAE
R104 LAKRSERRAEAEKQL
K109 ERRAEAEKQLQQAQE
K109 ERRAEAEKQLQQAQE
K125 GMEEEVEKFTKRLVK
K125 GMEEEVEKFTKRLVK
K132 KFTKRLVKVTKQHND
K168 ASCAALAKAGKVYAA
K171 AALAKAGKVYAAATE
S187 MDCLTFGSPVLMRHL
R192 FGSPVLMRHLTASEA
T195 PVLMRHLTASEAKKL
S197 LMRHLTASEAKKLPI
K200 HLTASEAKKLPIQEF
K200 HLTASEAKKLPIQEF
K201 LTASEAKKLPIQEFH
Y234 CILLGSDYCESIRGI
K252 RAVDLIQKHKSIEEI
S255 DLIQKHKSIEEIVRR
K267 VRRLDPSKYPVPENW
Y268 RRLDPSKYPVPENWL
K277 VPENWLHKEAQQLFL
S293 PEVLDPESVELKWSE
K297 DPESVELKWSEPNEE
K314 VKFMCGEKQFSEERI
S317 MCGEKQFSEERIRSG
S329 RSGVKRLSKSRQGST
S331 GVKRLSKSRQGSTQG
S335 LSKSRQGSTQGRLDD
T336 SKSRQGSTQGRLDDF
K345 GRLDDFFKVTGSLSS
S351 FKVTGSLSSAKRKEP
S352 KVTGSLSSAKRKEPE
K354 TGSLSSAKRKEPEPK
K354 TGSLSSAKRKEPEPK
K354 TGSLSSAKRKEPEPK
A364 EPEPKGPAKKKAKTG
K375 AKTGGAGKFRRGKIN
R377 TGGAGKFRRGKINLs
K380 AGKFRRGKINLsFPS
S384-p RRGKINLsFPSTVLD
  rat

 
K8 MGIQGLAKLIADVAP
S16 LIADVAPSAIRENDI
R19 DVAPSAIRENDIKSY
K24 AIRENDIKSYFGRKV
S25 IRENDIKSYFGRKVA
K80 RMMENGIKPVYIFDG
K88 PVYIFDGKPPQLKSG
K99 LKSGELAKRSERRAE
R100 KSGELAKRSERRAEA
S101 SGELAKRSERRAEAE
R104 LAKRSERRAEAEKQL
K109 ERRAEAEKQLQQAQE
K109 ERRAEAEKQLQQAQE
K125 GAEEEVEKFTKRLVK
K125 GAEEEVEKFTKRLVK
K132 KFTKRLVKVTKQHND
K168 ASCAALAKAGKVYAA
K171 AALAKAGKVYAAATE
S187 MDCLTFGSPVLMRHL
R192 FGSPVLMRHLTASEA
T195 PVLMRHLTASEAKKL
S197 LMRHLTASEAKKLPI
K200 HLTASEAKKLPIQEF
K200 HLTASEAKKLPIQEF
K201 LTASEAKKLPIQEFH
Y234 CILLGSDYCESVRGI
K252 RAVDLIQKHKSIEEI
S255 DLIQKHKSIEEIVRR
K267 VRRLDPSKYPVPENW
Y268 RRLDPSKYPVPENWL
K277 VPENWLHKEARQLFL
S293 PEVLDPESVELKWSE
K297 DPESVELKWSEPNEE
K314 VKFMCGEKQFSEERI
S317 MCGEKQFSEERIRSG
N329 RSGVKRLNKSRQGST
S331 GVKRLNKSRQGSTQG
S335 LNKSRQGSTQGRLDD
T336 NKSRQGSTQGRLDDF
K345 GRLDDFFKVTGSLSS
S351 FKVTGSLSSAKRKEP
S352 KVTGSLSSAKRKEPE
K354 TGSLSSAKRKEPEPK
K354 TGSLSSAKRKEPEPK
K354 TGSLSSAKRKEPEPK
A364 EPEPKGPAKKKAKTG
K375 AKTGGAGKFRRGK__
R377 TGGAGKFRRGK____
K380 AGKFRRGK_______
- under review  
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