CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007184
UniProt Accession
Genbank Protein ID
 L26320 
Genbank Nucleotide ID
Protein Name
 Flap endonuclease 1 
Protein Synonyms/Alias
 FEN-1; Flap structure-specific endonuclease 1 
Gene Name
 Fen1 
Gene Synonyms/Alias
 Fen-1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
107ERRAEAEKQLQQAQEacetylation[1]
312VKFMCGEKQFSEERIacetylation[1]
373AKTGGAGKFRRGK**acetylation[2]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 
Functional Description
 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 (By similarity). 
Sequence Annotation
 REGION 1 102 N-domain.
 REGION 120 251 I-domain.
 REGION 334 342 Interaction with PCNA (By similarity).
 METAL 34 34 Magnesium 1 (By similarity).
 METAL 84 84 Magnesium 1 (By similarity).
 METAL 156 156 Magnesium 1 (By similarity).
 METAL 158 158 Magnesium 1 (By similarity).
 METAL 177 177 Magnesium 2 (By similarity).
 METAL 179 179 Magnesium 2 (By similarity).
 METAL 231 231 Magnesium 2 (By similarity).
 BINDING 47 47 DNA substrate (By similarity).
 BINDING 69 69 DNA substrate (By similarity).
 BINDING 156 156 DNA substrate (By similarity).
 BINDING 229 229 DNA substrate (By similarity).
 BINDING 231 231 DNA substrate (By similarity).
 MOD_RES 19 19 Symmetric dimethylarginine; by PRMT5 (By
 MOD_RES 78 78 N6-acetyllysine (By similarity).
 MOD_RES 98 98 Symmetric dimethylarginine; by PRMT5 (By
 MOD_RES 102 102 Symmetric dimethylarginine; by PRMT5 (By
 MOD_RES 185 185 Phosphoserine; by CDK2 (By similarity).
 MOD_RES 190 190 Symmetric dimethylarginine; by PRMT5 (By
 MOD_RES 265 265 N6-acetyllysine (By similarity).
 MOD_RES 352 352 N6-acetyllysine (By similarity).
 MOD_RES 373 373 N6-acetyllysine (By similarity).
 MOD_RES 378 378 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Complete proteome; Direct protein sequencing; DNA damage; DNA repair; DNA replication; Endonuclease; Exonuclease; Hydrolase; Magnesium; Metal-binding; Methylation; Mitochondrion; Nuclease; Nucleus; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 378 AA 
Protein Sequence
MGIHGLAKLI ADVAPSAIRE NDIKSYFGRK VAIDASMSIY QFLIAVRQGG DVLQNEEGET 60
TSLMGMFYRT IRMENGIKPV YVFDGKPPQL KSGELAKRSE RRAEAEKQLQ QAQEAGMEEE 120
VEKFTKRLVK VTKQHNDECK HLLSLMGIPY LDAPSEAEAS CAALAKAGKV YAAATEDMDC 180
LTFGSPVLMR HLTASEAKKL PIQEFHLSRV LQELGLNQEQ FVDLCILLGS DYCESIRGIG 240
AKRAVDLIQK HKSIEEIVRR LDPSKYPVPE NWLHKEAQQL FLEPEVVDPE SVELKWSEPN 300
EEELVKFMCG EKQFSEERIR SGVKRLSKSR QGSTQGRLDD FFKVTGSLSS AKRKEPEPKG 360
PAKKKAKTGG AGKFRRGK 378 
Gene Ontology
 GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; TAS:MGI.
 GO:0008409; F:5'-3' exonuclease activity; IEA:HAMAP.
 GO:0017108; F:5'-flap endonuclease activity; IEA:HAMAP.
 GO:0003677; F:DNA binding; IDA:MGI.
 GO:0004527; F:exonuclease activity; IDA:MGI.
 GO:0048256; F:flap endonuclease activity; IDA:MGI.
 GO:0000287; F:magnesium ion binding; IDA:MGI.
 GO:0030145; F:manganese ion binding; IDA:MGI.
 GO:0006284; P:base-excision repair; IEA:HAMAP.
 GO:0006281; P:DNA repair; IMP:MGI.
 GO:0006260; P:DNA replication; IMP:MGI.
 GO:0043137; P:DNA replication, removal of RNA primer; IEA:HAMAP. 
Interpro
 IPR020045; 5-3_exonuclease_C.
 IPR023426; Flap_endonuc.
 IPR008918; HhH2.
 IPR006086; XPG-I_dom.
 IPR006084; XPG/Rad2.
 IPR019974; XPG_CS.
 IPR006085; XPG_DNA_repair_N. 
Pfam
 PF00867; XPG_I
 PF00752; XPG_N 
SMART
 SM00279; HhH2
 SM00484; XPGI
 SM00485; XPGN 
PROSITE
 PS00841; XPG_1
 PS00842; XPG_2 
PRINTS
 PR00853; XPGRADSUPER.