| Tag | Content |
|---|
| CPLM ID | CPLM-014196 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Flap endonuclease 1 |
Protein Synonyms/Alias | FEN-1; Flap structure-specific endonuclease 1 |
Gene Name | Fen1 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 200 | HLTASEAKKLPIQEF | acetylation | [1] |
|
Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
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 1 104 N-domain.
REGION 122 253 I-domain.
REGION 336 344 Interaction with PCNA (By similarity).
METAL 34 34 Magnesium 1 (By similarity).
METAL 86 86 Magnesium 1 (By similarity).
METAL 158 158 Magnesium 1 (By similarity).
METAL 160 160 Magnesium 1 (By similarity).
METAL 179 179 Magnesium 2 (By similarity).
METAL 181 181 Magnesium 2 (By similarity).
METAL 233 233 Magnesium 2 (By similarity).
BINDING 47 47 DNA substrate (By similarity).
BINDING 70 70 DNA substrate (By similarity).
BINDING 158 158 DNA substrate (By similarity).
BINDING 231 231 DNA substrate (By similarity).
BINDING 233 233 DNA substrate (By similarity).
MOD_RES 19 19 Symmetric dimethylarginine; by PRMT5 (By
MOD_RES 80 80 N6-acetyllysine (By similarity).
MOD_RES 100 100 Symmetric dimethylarginine; by PRMT5 (By
MOD_RES 104 104 Symmetric dimethylarginine; by PRMT5 (By
MOD_RES 187 187 Phosphoserine; by CDK2 (By similarity).
MOD_RES 192 192 Symmetric dimethylarginine; by PRMT5 (By
MOD_RES 267 267 N6-acetyllysine (By similarity).
MOD_RES 354 354 N6-acetyllysine (By similarity).
MOD_RES 375 375 N6-acetyllysine (By similarity).
MOD_RES 380 380 N6-acetyllysine (By similarity). |
Keyword | Acetylation; Complete proteome; 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 | 380 AA |
Protein Sequence | MGIQGLAKLI ADVAPSAIRE NDIKSYFGRK VAIDASMSIY QFLIAVRQGG DVLQNEEGET 60
TSHLMGMFYR TIRMMENGIK PVYIFDGKPP QLKSGELAKR SERRAEAEKQ LQQAQEAGAE 120
EEVEKFTKRL VKVTKQHNDE CKHLLSLMGI PYLDAPSEAE ASCAALAKAG KVYAAATEDM 180
DCLTFGSPVL MRHLTASEAK KLPIQEFHLS RVLQELGLNQ EQFVDLCILL GSDYCESVRG 240
IGPKRAVDLI QKHKSIEEIV RRLDPSKYPV PENWLHKEAR QLFLEPEVLD PESVELKWSE 300
PNEEELVKFM CGEKQFSEER IRSGVKRLNK SRQGSTQGRL DDFFKVTGSL SSAKRKEPEP 360
KGPAKKKAKT GGAGKFRRGK 380 |
Gene Ontology | |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |