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P39750 (FEN1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Flap endonuclease 1
Short name=FEN-1
EC=3.1.-.-
Alternative name(s):
DNA repair protein rad2
Flap structure-specific endonuclease 1
Gene names
Name:rad2
Synonyms:fen1
ORF Names:SPAC3G6.06c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces ›

Protein attributes

Sequence length380 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_03140

Cofactor

Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding By similarity.

Subunit structure

Interacts with PCNA. Three molecules of rad2 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity By similarity.

Subcellular location

Nucleus › nucleolus By similarity. Nucleus › nucleoplasm By similarity. Mitochondrion By similarity. Note: Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage By similarity.

Post-translational modification

Phosphorylated. Phosphorylation upon DNA damage induces relocalization to the nuclear plasma By similarity. HAMAP-Rule MF_03140

Sequence similarities

Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 380380Flap endonuclease 1 HAMAP-Rule MF_03140
PRO_0000154037

Regions

Region1 – 105105N-domain HAMAP-Rule MF_03140
Region123 – 254132I-domain HAMAP-Rule MF_03140
Region337 – 3459Interaction with PCNA By similarity

Sites

Metal binding341Magnesium 1 By similarity
Metal binding871Magnesium 1 By similarity
Metal binding1591Magnesium 1 By similarity
Metal binding1611Magnesium 1 By similarity
Metal binding1801Magnesium 2 By similarity
Metal binding1821Magnesium 2 By similarity
Metal binding2341Magnesium 2 By similarity
Binding site471DNA substrate By similarity
Binding site711DNA substrate By similarity
Binding site1591DNA substrate By similarity
Binding site2321DNA substrate By similarity
Binding site2341DNA substrate By similarity

Amino acid modifications

Modified residue3501Phosphoserine Ref.3
Modified residue3511Phosphoserine Ref.3

Sequences

Sequence LengthMass (Da)Tools
P39750 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 3604065D9B934CBF

FASTA38042,866
        10         20         30         40         50         60 
MGIKGLAQVL SEHAPASVKH NDIKNYFGRK VAIDASMSLY QFLIQVRSQD GQQLMNEQGE 

        70         80         90        100        110        120 
TTSHLMGMFY RTLRIVDNGI KPCFVFDGKP PTLKSGELAK RVARHQKARE DQEETKEVGT 

       130        140        150        160        170        180 
AEMVDRFAKR TVKVTRQHND EAKRLLELMG IPFVNAPCEA EAQCAALARS GKVYAAASED 

       190        200        210        220        230        240 
MDTLCFQAPV LLRHLTFSEQ RKEPISEYNI EKALNGLDMS VEQFVDLCIL LGCDYCEPIR 

       250        260        270        280        290        300 
GVGPARAVEL IRQYGTLDRF VKEADRSKYP IPEDWPYEDA RRLFLDAEVL PGEEIELKWK 

       310        320        330        340        350        360 
SPDADGIIQF LVKEKGFNED RVKLGINRLE KASKTIPQGR LDSFFKPVPS SPKKPVDTKS 

       370        380 
KGSAKRKRDS NKGGESKKKR

« Hide

References

« Hide 'large scale' references
[1]"Structural and functional conservation of the human homolog of the Schizosaccharomyces pombe rad2 gene, which is required for chromosome segregation and recovery from DNA damage."
Murray J.M., Tavassoli M., Al-Harithy R., Sheldrick K.S., Lehmann A.R., Carr A.M., Watts F.Z.
Mol. Cell. Biol. 14:4878-4888(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[3]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350 AND SER-351, MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X77041 Genomic DNA. Translation: CAB36991.1.
CU329670 Genomic DNA. Translation: CAB16282.1.
PIRA56054.
RefSeqNP_594972.1. NM_001020403.2.

3D structure databases

ProteinModelPortalP39750.
ModBaseSearch...

Protein-protein interaction databases

STRING4896.SPAC3G6.06c-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC3G6.06c.1; SPAC3G6.06c.1:pep; SPAC3G6.06c.
GeneID2543164.
KEGGspo:SPAC3G6.06c.

Organism-specific databases

PomBaseSPAC3G6.06c.

Phylogenomic databases

eggNOGCOG0258.
HOGENOMHOG000193853.
KOK04799.
OMADYDSLLF.
OrthoDBEOG41VPBP.

Family and domain databases

HAMAPMF_00614. Fen.
InterProIPR020045. 5-3_exonuclease_C.
IPR023426. Flap_endonuc.
IPR008918. HhH2.
IPR006086. XPG-I_dom.
IPR006084. XPG/Rad2.
IPR019974. XPG_CS.
IPR006085. XPG_DNA_repair_N.
[Graphical view]
PANTHERPTHR11081. PTHR11081. 1 hit.
PfamPF00867. XPG_I. 1 hit.
PF00752. XPG_N. 1 hit.
[Graphical view]
PRINTSPR00853. XPGRADSUPER.
SMARTSM00279. HhH2. 1 hit.
SM00484. XPGI. 1 hit.
SM00485. XPGN. 1 hit.
[Graphical view]
SUPFAMSSF47807. 5_3_exo_C. 1 hit.
PROSITEPS00841. XPG_1. 1 hit.
PS00842. XPG_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20804190.

Entry information

Entry nameFEN1_SCHPO
AccessionPrimary (citable) accession number: P39750
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 1, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents