Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Flap endonuclease 1 (FEN-1) (EC 3.1.-.-) (Flap structure-specific endonuclease 1)

 FEN1_VANPO              Reviewed;         377 AA.
A7TJ59;
11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
02-OCT-2007, sequence version 1.
10-OCT-2018, entry version 63.
RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140};
Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140};
EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140};
AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140};
Name=FEN1 {ECO:0000255|HAMAP-Rule:MF_03140}; ORFNames=Kpol_1033p65;
Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294)
(Kluyveromyces polysporus).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae;
Vanderwaltozyma.
NCBI_TaxID=436907;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 22028 / DSM 70294;
PubMed=17494770; DOI=10.1073/pnas.0608218104;
Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M.,
Wolfe K.H.;
"Independent sorting-out of thousands of duplicated gene pairs in two
yeast species descended from a whole-genome duplication.";
Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
-!- 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.
{ECO:0000255|HAMAP-Rule:MF_03140}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_03140};
Note=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. {ECO:0000255|HAMAP-
Rule:MF_03140};
-!- SUBUNIT: 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. {ECO:0000255|HAMAP-Rule:MF_03140}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
Rule:MF_03140}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-
Rule:MF_03140}. Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03140}.
Note=Resides mostly in the nucleoli and relocalizes to the
nucleoplasm upon DNA damage. {ECO:0000255|HAMAP-Rule:MF_03140}.
-!- PTM: Phosphorylated. Phosphorylation upon DNA damage induces
relocalization to the nuclear plasma. {ECO:0000255|HAMAP-
Rule:MF_03140}.
-!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. FEN1
subfamily. {ECO:0000255|HAMAP-Rule:MF_03140}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; DS480399; EDO17758.1; -; Genomic_DNA.
RefSeq; XP_001645616.1; XM_001645566.1.
ProteinModelPortal; A7TJ59; -.
STRING; 436907.XP_001645616.1; -.
EnsemblFungi; EDO17758; EDO17758; Kpol_1033p65.
GeneID; 5546005; -.
KEGG; vpo:Kpol_1033p65; -.
eggNOG; KOG2519; Eukaryota.
eggNOG; COG0258; LUCA.
InParanoid; A7TJ59; -.
KO; K04799; -.
OrthoDB; EOG092C2ISI; -.
PhylomeDB; A7TJ59; -.
Proteomes; UP000000267; Unassembled WGS sequence.
GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
GO; GO:0035861; C:site of double-strand break; IEA:EnsemblFungi.
GO; GO:1904162; F:5'-3' exodeoxyribonuclease activity involved in UV-damage excision repair; IEA:EnsemblFungi.
GO; GO:0017108; F:5'-flap endonuclease activity; IEA:UniProtKB-UniRule.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
GO; GO:0051908; F:double-stranded DNA 5'-3' exodeoxyribonuclease activity; IEA:EnsemblFungi.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0045145; F:single-stranded DNA 5'-3' exodeoxyribonuclease activity; IEA:EnsemblFungi.
GO; GO:0006286; P:base-excision repair, base-free sugar-phosphate removal; IEA:EnsemblFungi.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:EnsemblFungi.
GO; GO:0000734; P:gene conversion at mating-type locus, DNA repair synthesis; IEA:EnsemblFungi.
GO; GO:0035753; P:maintenance of DNA trinucleotide repeats; IEA:EnsemblFungi.
GO; GO:1903469; P:removal of RNA primer involved in mitotic DNA replication; IEA:EnsemblFungi.
GO; GO:0001302; P:replicative cell aging; IEA:EnsemblFungi.
CDD; cd09867; PIN_FEN1; 1.
HAMAP; MF_00614; Fen; 1.
InterPro; IPR036279; 5-3_exonuclease_C_sf.
InterPro; IPR023426; Flap_endonuc.
InterPro; IPR008918; HhH2.
InterPro; IPR029060; PIN-like_dom_sf.
InterPro; IPR006086; XPG-I_dom.
InterPro; IPR006084; XPG/Rad2.
InterPro; IPR019974; XPG_CS.
InterPro; IPR006085; XPG_DNA_repair_N.
PANTHER; PTHR11081; PTHR11081; 1.
Pfam; PF00867; XPG_I; 1.
Pfam; PF00752; XPG_N; 1.
PRINTS; PR00853; XPGRADSUPER.
SMART; SM00279; HhH2; 1.
SMART; SM00484; XPGI; 1.
SMART; SM00485; XPGN; 1.
SUPFAM; SSF47807; SSF47807; 1.
SUPFAM; SSF88723; SSF88723; 1.
PROSITE; PS00841; XPG_1; 1.
PROSITE; PS00842; XPG_2; 1.
3: Inferred from homology;
Complete proteome; DNA damage; DNA repair; DNA replication;
Endonuclease; Exonuclease; Hydrolase; Magnesium; Metal-binding;
Mitochondrion; Nuclease; Nucleus; Phosphoprotein; Reference proteome.
CHAIN 1 377 Flap endonuclease 1.
/FTId=PRO_0000403605.
REGION 1 105 N-domain.
REGION 120 251 I-domain.
REGION 338 346 Interaction with PCNA.
{ECO:0000255|HAMAP-Rule:MF_03140}.
METAL 34 34 Magnesium 1. {ECO:0000255|HAMAP-
Rule:MF_03140}.
METAL 87 87 Magnesium 1. {ECO:0000255|HAMAP-
Rule:MF_03140}.
METAL 156 156 Magnesium 1. {ECO:0000255|HAMAP-
Rule:MF_03140}.
METAL 158 158 Magnesium 1. {ECO:0000255|HAMAP-
Rule:MF_03140}.
METAL 177 177 Magnesium 2. {ECO:0000255|HAMAP-
Rule:MF_03140}.
METAL 179 179 Magnesium 2. {ECO:0000255|HAMAP-
Rule:MF_03140}.
METAL 231 231 Magnesium 2. {ECO:0000255|HAMAP-
Rule:MF_03140}.
BINDING 47 47 DNA substrate. {ECO:0000255|HAMAP-
Rule:MF_03140}.
BINDING 71 71 DNA substrate. {ECO:0000255|HAMAP-
Rule:MF_03140}.
BINDING 156 156 DNA substrate. {ECO:0000255|HAMAP-
Rule:MF_03140}.
BINDING 229 229 DNA substrate. {ECO:0000255|HAMAP-
Rule:MF_03140}.
BINDING 231 231 DNA substrate. {ECO:0000255|HAMAP-
Rule:MF_03140}.
SEQUENCE 377 AA; 42468 MW; 4DCBD6F588FC3DF5 CRC64;
MGIKGLNAII SEHVPSAVRK SDIKTFFGRK VAIDASMSLY QFLIAVRQQD GGQLTNEAGE
TTSHLMGMFY RTLRMIDNGI KPCYVFDGKP PVLKSHELSK RTARREETEK KLQEATDQAE
KMKQERRLVK VSKEHNDEAK QLLELMGIPY ITAPCEAESQ CAELAKCGKV YAAASEDMDT
LCYRTPYLLR HLTFSEAKKE PIHEIDTELV LKGLDLTLEQ FVDLGIMLGC DYCDSIKGVG
PVTALKLIKE YGSLEKIIEY IESDSSNSKW KIPNDWPYKD ARELFLKPDV INGNEVELKW
QPPNEKGLID FLCGEKKFSE ERVKSGIERL KKGLKSGVQG RLDGFFQVVP KTKEQLAKAA
AKAKAAKKSG KVTKKRR


Related products :

Catalog number Product name Quantity
EIAAB14713 DNase IV,FEN1,FEN-1,Flap endonuclease 1,Flap structure-specific endonuclease 1,hFEN-1,Homo sapiens,Human,Maturation factor 1,MF1,RAD2
EIAAB14710 Fen1,FEN-1,Flap endonuclease 1,Flap structure-specific endonuclease 1,Rat,Rattus norvegicus
EIAAB14712 Bos taurus,Bovine,FEN1,FEN-1,Flap endonuclease 1,Flap structure-specific endonuclease 1,RTH-1
EIAAB14711 Fen1,FEN-1,Fen-1,Flap endonuclease 1,Flap structure-specific endonuclease 1,Mouse,Mus musculus
EIAAB14709 Chicken,FEN1,FEN-1,Flap endonuclease 1,Flap structure-specific endonuclease 1,Gallus gallus,RCJMB04_5g12
FER FEN1 Gene flap structure-specific endonuclease 1
enz-468 Recombinant Human Flap Structure-Specific Endonuclease 1 20
REN-468 Recombinant Human Flap Structure-Specific Endonuclease 1 5
enz-468 Recombinant Human Flap Structure-Specific Endonuclease 1 5
enz-468 Recombinant Human Flap Structure-Specific Endonuclease 1 1mg
enz-468 Recombinant Human Flap Structure-Specific Endonuclease 1 ENZYMES 5
enz-468 Recombinant Human Flap Structure-Specific Endonuclease 1 FEN1 5
OETENZ-468 Flap Structure-Specific Endonuclease 1 Human Recombinant 5
201-20-2028 FEN1{flap structure-specific endonuclease 1}rabbit.pAb 0.2ml
OETENZ-468 Flap Structure-Specific Endonuclease 1 Human Recombinant 20
enz-468 Recombinant Human Flap Structure-Specific Endonuclease 1 FEN1 20
7-02755 Recombinant Human Flap Structure-Specific Endonuclease 1 5
enz-468 Recombinant Human Flap Structure-Specific Endonuclease 1 FEN1 1mg
enz-468 Recombinant Human Flap Structure-Specific Endonuclease 1 ENZYMES 20
enz-468 Recombinant Human Flap Structure-Specific Endonuclease 1 ENZYMES 1mg
7-02757 Recombinant Human Flap Structure-Specific Endonuclease 1 1mg
7-02756 Recombinant Human Flap Structure-Specific Endonuclease 1 20
orb90092 Human Flap Structure-Specific Endonuclease 1 protein Enzymes 5
GS-0761a flap structure-specific endonuclease 1 primary antibody, Host: Rabbit 200ul
FEN1-488H Protein Recombinant Human Flap Structure-Specific Endonuclease 1 0.5mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur