Gene
KWMTBOMO12176  
Validated by peptides from experiments
Pre Gene Modal
BGIBMGA004227
Annotation
flap_endonuclease-1_[Bombyx_mori]
Full name
Flap endonuclease 1
Alternative Name
Flap structure-specific endonuclease 1
Location in the cell
Cytoplasmic   Reliability : 3.031
Sequence
CDS
ATGGGTATTCTAGGTTTATCTAAGTTAATTGCTGACATAGCACCTCATGCTGTCAAAGAAATGGAAATCAAAAATTACTTTGGAAGAAAAATAGCTATTGATGCTTCTATGAGCTTATATCAGTTCCTTATCGCCGTAAGAAGTGAAGGAGCCCAACTAGTCTCTGTAGACGGAGAGACTACATCACATCTGATGGGTACATTTTACCGTACTATAAGACTGGTAGAAAATGGGATTAAACCAGTGTATGTCTTTGACGGGAAACCTCCAGACATGAAGGCTCATCAGTTGAATAAGAGAGCAGAAAGGAGAGAGGAAGCAGAGAAAGAATTGCAAAAAGCTACTGAAGCCGGTGACACAGCTTCAGTGGACAAGTTCAACAGACGTTTGGTTAAAGTAACAAAACAACACAGTGAAGAGGCTAAACAACTCCTCAAATTGATGGGTGTCCCGGTTGTTGATGCACCCTGTGAGGCTGAAGCCCAGTGTGCAGCTCTTGTAAAATCCGGTAAAGTTTTTGCAGCAGCCACAGAAGATATGGATGCCCTAACCTTTGGTGCACCAGTGCTATTGAGACACTTAACGTTTTCTGAAGCAAGGAAAATGCCCGTGCAAGAATTCCATTTAAATAATGTACTACAGGGATTGGAATTGAAACAGAATGAGTTTATTGACCTCTGCATACTCCTTGGCTGTGATTACTGTGGTTCCATTAGAGGGGTTGGCCCAAAACGAGCCATCGACCTCATAAGACAACATCGGACACTGGATGAAGTACTCAAGAATATAGACACTGAGAAGTACCAACCTCCCACTGACTGGGATTACGAGCGAGCTAGGAGTCTGTTCATGGAACCTGAAGTCGCTGACCCTAAAGACATTGAGCTGAAATGGACTGATCCCGATGAAGAGGGCCTCGTGAAGTTTCTGTGTGGGGACAGACAGTTCAATGAAGAACGAGTGAGGAATGGAGCTAAGAAGTTAATTAAAGCCAGGACGGGCACCACACAGGCCAGATTAGATGGGTTCTTCACGTTAACGACAACGCCTAATTCGAAACGTAAAGCTGAAGAGGACAAGAAGAATTCAGCAAAGAAGAAAACTAAGACCGGAGGTGGAGGACGCGGTCGGAAACCGAAATGA
Protein
MGILGLSKLIADIAPHAVKEMEIKNYFGRKIAIDASMSLYQFLIAVRSEGAQLVSVDGETTSHLMGTFYRTIRLVENGIKPVYVFDGKPPDMKAHQLNKRAERREEAEKELQKATEAGDTASVDKFNRRLVKVTKQHSEEAKQLLKLMGVPVVDAPCEAEAQCAALVKSGKVFAAATEDMDALTFGAPVLLRHLTFSEARKMPVQEFHLNNVLQGLELKQNEFIDLCILLGCDYCGSIRGVGPKRAIDLIRQHRTLDEVLKNIDTEKYQPPTDWDYERARSLFMEPEVADPKDIELKWTDPDEEGLVKFLCGDRQFNEERVRNGAKKLIKARTGTTQARLDGFFTLTTTPNSKRKAEEDKKNSAKKKTKTGGGGRGRKPK
Summary
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.
Subunit
Interacts with PCNA. Three molecules of 101741812 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
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.
Interacts with PCNA. Three molecules of Fen1_1 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
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.
Interacts with PCNA. Three molecules of 100160968 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of 109401579 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of LOC108744458 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of CSON014361 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of CSON009372 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of 109542723 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of HaOG214678 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of LOC412308 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of 100114897 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of putative Flap endonuclease 1 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of 101891979 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of 8232021 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of Fen1_0 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of DsimGD25512 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Interacts with PCNA. Three molecules of LOC108090516 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Similarity
Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily.
Keywords
Complete proteome
DNA damage
DNA repair
DNA replication
Endonuclease
Exonuclease
Hydrolase
Magnesium
Metal-binding
Mitochondrion
Nuclease
Nucleus
Phosphoprotein
Reference proteome
Feature
chain Flap endonuclease 1
PDB
1UL1
E-value=8.13901e-128,
Score=1170
Ontologies
Topology
Subcellular location
Mitochondrion
Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage. With evidence from 1 publications.
Nucleus
Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage. With evidence from 1 publications.
Nucleolus
Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage. With evidence from 1 publications.
Nucleoplasm
Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage. With evidence from 1 publications.
Number of predicted TMHs:
0
Exp number of AAs in TMHs:
0.00591
Exp number, first 60 AAs:
0.00383
Total prob of N-in:
0.00183
Population Genetic Test Statistics