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

Endonuclease III-like protein 1 (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase) (DNA glycosylase/AP lyase)

 NTH_MOUSE               Reviewed;         300 AA.
O35980; E9QMW1;
28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 2.
28-MAR-2018, entry version 138.
RecName: Full=Endonuclease III-like protein 1 {ECO:0000255|HAMAP-Rule:MF_03183};
EC=3.2.2.- {ECO:0000255|HAMAP-Rule:MF_03183};
EC=4.2.99.18 {ECO:0000255|HAMAP-Rule:MF_03183};
AltName: Full=Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase {ECO:0000255|HAMAP-Rule:MF_03183};
Short=DNA glycosylase/AP lyase {ECO:0000255|HAMAP-Rule:MF_03183};
Flags: Precursor;
Name=Nthl1; Synonyms=Nth1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND TISSUE
SPECIFICITY.
STRAIN=BALB/cJ; TISSUE=Leukocyte, and T-cell;
PubMed=9743625; DOI=10.1006/jmbi.1998.2042;
Sarker A.H., Ikeda S., Nakano H., Terato H., Ide H., Imai K.,
Akiyama K., Tsutsui K., Bo Z., Kubo K., Yamamoto K., Yasui A.,
Yoshida M.C., Seki S.;
"Cloning and characterization of a mouse homologue (mNthl1) of
Escherichia coli endonuclease III.";
J. Mol. Biol. 282:761-774(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Embryonic stem cell, and Lung;
Luna L., Bjoras M., Rognes T., Hoff E., Seeberg E.;
"Complete genomic DNA sequence of the Mus musculus endonuclease III
homologue 1 gene (NTH1).";
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Cecum;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5] {ECO:0000305}
SUBCELLULAR LOCATION.
PubMed=12531031; DOI=10.1016/S1568-7864(02)00145-3;
Ikeda S., Kohmoto T., Tabata R., Seki Y.;
"Differential intracellular localization of the human and mouse
endonuclease III homologs and analysis of the sorting signals.";
DNA Repair 1:847-854(2002).
-!- FUNCTION: Bifunctional DNA N-glycosylase with associated
apurinic/apyrimidinic (AP) lyase function that catalyzes the first
step in base excision repair (BER), the primary repair pathway for
the repair of oxidative DNA damage. The DNA N-glycosylase activity
releases the damaged DNA base from DNA by cleaving the N-
glycosidic bond, leaving an AP site. The AP lyase activity cleaves
the phosphodiester bond 3' to the AP site by a beta-elimination.
Primarily recognizes and repairs oxidative base damage of
pyrimidines. {ECO:0000255|HAMAP-Rule:MF_03183,
ECO:0000269|PubMed:9743625}.
-!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
apyrimidinic site in DNA is broken by a beta-elimination reaction,
leaving a 3'-terminal unsaturated sugar and a product with a
terminal 5'-phosphate. {ECO:0000250|UniProtKB:P20625,
ECO:0000255|HAMAP-Rule:MF_03183}.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000255|HAMAP-Rule:MF_03183};
Note=Binds 1 [4Fe-4S] cluster. The cluster does not appear to play
a role in catalysis, but is probably involved in the proper
positioning of the enzyme along the DNA strand.
{ECO:0000255|HAMAP-Rule:MF_03183};
-!- SUBUNIT: Interacts with YBX1. {ECO:0000255|HAMAP-Rule:MF_03183}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03183}.
Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03183,
ECO:0000269|PubMed:12531031}.
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:9743625}.
-!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000255|HAMAP-
Rule:MF_03183}.
-!- SEQUENCE CAUTION:
Sequence=AK033701; Type=Frameshift; Positions=33; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB006812; BAA22080.1; -; mRNA.
EMBL; AB009371; BAA28846.1; -; Genomic_DNA.
EMBL; AJ001617; CAB65239.1; -; Genomic_DNA.
EMBL; Y09688; CAA70866.1; -; mRNA.
EMBL; AK033701; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC132367; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS28487.1; -.
RefSeq; NP_032769.2; NM_008743.2.
UniGene; Mm.148315; -.
ProteinModelPortal; O35980; -.
SMR; O35980; -.
STRING; 10090.ENSMUSP00000047413; -.
iPTMnet; O35980; -.
PhosphoSitePlus; O35980; -.
MaxQB; O35980; -.
PaxDb; O35980; -.
PRIDE; O35980; -.
Ensembl; ENSMUST00000047611; ENSMUSP00000047413; ENSMUSG00000041429.
GeneID; 18207; -.
KEGG; mmu:18207; -.
UCSC; uc008axi.2; mouse.
CTD; 4913; -.
MGI; MGI:1313275; Nthl1.
eggNOG; KOG1921; Eukaryota.
eggNOG; COG0177; LUCA.
GeneTree; ENSGT00510000047513; -.
HOGENOM; HOG000252209; -.
HOVERGEN; HBG052675; -.
InParanoid; O35980; -.
KO; K10773; -.
OMA; WQQFTHL; -.
OrthoDB; EOG091G0IVB; -.
TreeFam; TF314967; -.
BRENDA; 4.2.99.18; 3474.
Reactome; R-MMU-110329; Cleavage of the damaged pyrimidine.
Reactome; R-MMU-110357; Displacement of DNA glycosylase by APEX1.
ChiTaRS; Nthl1; mouse.
PRO; PR:O35980; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000041429; -.
CleanEx; MM_NTHL1; -.
Genevisible; O35980; MM.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) lyase activity; IEA:UniProtKB-EC.
GO; GO:0140080; F:class III/IV DNA-(apurinic or apyrimidinic site) lyase activity; IEA:UniProtKB-EC.
GO; GO:0019104; F:DNA N-glycosylase activity; IDA:UniProtKB.
GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IDA:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000703; F:oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity; IBA:GO_Central.
GO; GO:0006285; P:base-excision repair, AP site formation; ISO:MGI.
GO; GO:0006281; P:DNA repair; TAS:MGI.
GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; IDA:UniProtKB.
CDD; cd00056; ENDO3c; 1.
Gene3D; 1.10.1670.10; -; 1.
HAMAP; MF_03183; Endonuclease_III_Nth; 1.
InterPro; IPR011257; DNA_glycosylase.
InterPro; IPR004036; Endonuclease-III-like_CS2.
InterPro; IPR003651; Endonuclease3_FeS-loop_motif.
InterPro; IPR003265; HhH-GPD_domain.
InterPro; IPR000445; HhH_motif.
InterPro; IPR023170; HTH_base_excis_C.
InterPro; IPR030841; NTH1.
Pfam; PF00633; HHH; 1.
Pfam; PF00730; HhH-GPD; 1.
SMART; SM00478; ENDO3c; 1.
SMART; SM00525; FES; 1.
SUPFAM; SSF48150; SSF48150; 1.
PROSITE; PS01155; ENDONUCLEASE_III_2; 1.
2: Evidence at transcript level;
4Fe-4S; Complete proteome; DNA damage; DNA repair; Glycosidase;
Hydrolase; Iron; Iron-sulfur; Lyase; Metal-binding; Mitochondrion;
Nucleus; Reference proteome; Transit peptide.
TRANSIT 1 19 Mitochondrion. {ECO:0000255|HAMAP-
Rule:MF_03183}.
CHAIN 20 300 Endonuclease III-like protein 1.
/FTId=PRO_0000102228.
DOMAIN 187 211 HhH. {ECO:0000255|HAMAP-Rule:MF_03183}.
ACT_SITE 208 208 Nucleophile; for N-glycosylase activity.
{ECO:0000255|HAMAP-Rule:MF_03183}.
METAL 278 278 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
Rule:MF_03183}.
METAL 285 285 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
Rule:MF_03183}.
METAL 288 288 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
Rule:MF_03183}.
METAL 294 294 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
Rule:MF_03183}.
SITE 227 227 Important for catalytic activity.
{ECO:0000255|HAMAP-Rule:MF_03183}.
SEQUENCE 300 AA; 33637 MW; 09CAA1FD066F18EB CRC64;
MNSGVRMVTR SRSRATRIAS EGCREELAPR EAAAEGRKSH RPVRHPRRTQ KTHVAYEAAN
GEEGEDAEPL KVPVWEPQNW QQQLANIRIM RSKKDAPVDQ LGAEHCYDAS ASPKVRRYQV
LLSLMLSSQT KDQVTAGAMQ RLRARGLTVE SILQTDDDTL GRLIYPVGFW RNKVKYIKQT
TAILQQRYEG DIPASVAELV ALPGVGPKMA HLAMAVAWGT ISGIAVDTHV HRIANRLRWT
KKMTKTPEET RKNLEEWLPR VLWSEVNGLL VGFGQQICLP VHPRCQACLN KALCPAAQDL


Related products :

Catalog number Product name Quantity
EIAAB26879 DNA glycosylase_AP lyase Neil2,DNA-(apurinic or apyrimidinic site) lyase Neil2,Endonuclease 8-like 2,Endonuclease VIII-like 2,Homo sapiens,Human,NEH2,Nei homolog 2,NEIL2,Nei-like protein 2
EIAAB26876 DNA glycosylase_AP lyase Neil1,DNA-(apurinic or apyrimidinic site) lyase Neil1,Endonuclease 8-like 1,Endonuclease VIII-like 1,Mouse,Mus musculus,NEH1,Nei homolog 1,Nei1,Neil1,Nei-like protein 1
EIAAB26878 DNA glycosylase_AP lyase Neil2,DNA-(apurinic or apyrimidinic site) lyase Neil2,Endonuclease 8-like 2,Endonuclease VIII-like 2,Gm1212,Mouse,Mus musculus,NEH2,Nei homolog 2,Neil2,Nei-like protein 2
EIAAB26880 Bos taurus,Bovine,DNA glycosylase_AP lyase Neil2,DNA-(apurinic or apyrimidinic site) lyase Neil2,Endonuclease 8-like 2,Endonuclease VIII-like 2,NEH2,Nei homolog 2,NEIL2,Nei-like protein 2
EIAAB26877 DNA glycosylase_AP lyase Neil1,DNA-(apurinic or apyrimidinic site) lyase Neil1,Endonuclease 8-like 1,Endonuclease VIII-like 1,FPG1,Homo sapiens,Human,NEH1,Nei homolog 1,NEIL1,Nei-like protein 1
18-003-43422 DNA-(apurinic or apyrimidinic site) lyase - EC 4.2.99.18; AP endonuclease 1; APEX nuclease; APEN; Protein REF-1 Polyclonal 0.1 mg Protein A
18-003-43958 DNA-(apurinic or apyrimidinic site) lyase - EC 4.2.99.18; AP endonuclease 1; APEX nuclease; APEN Polyclonal 0.1 mg Protein A
18-003-43959 DNA-(apurinic or apyrimidinic site) lyase - EC 4.2.99.18; AP endonuclease 1; APEX nuclease; APEN Polyclonal 0.1 mg Protein A
EH2009 DNA-(apurinic or apyrimidinic site) lyase Elisa Kit 96T
CSB-EP001900HU Recombinant human DNA-(apurinic or apyrimidinic site) lyase 500ug
CSB-EL001900RA Rat DNA-(apurinic or apyrimidinic site) lyase (APEX1) ELISA kit 96T
E14887d Mouse ELISA Kit FOR DNA-(apurinic or apyrimidinic site) lyase 2 96T
AE56100RA Rat DNA- (apurinic or apyrimidinic site) lyase (APEX1) ELISA Kit 48T
CSB-EL001901BO Bovine DNA-(apurinic or apyrimidinic site) lyase (APEX2) ELISA kit 96T
CSB-EL001900BO Bovine DNA-(apurinic or apyrimidinic site) lyase (APEX1) ELISA kit 96T
CSB-EL001900MO Mouse DNA-(apurinic or apyrimidinic site) lyase (APEX1) ELISA kit 96T
CSB-EL001901HU Human DNA-(apurinic or apyrimidinic site) lyase (APEX2) ELISA kit 96T
CSB-EL001900HU Human DNA-(apurinic or apyrimidinic site) lyase (APEX1) ELISA kit 96T
abx108186 Polyclonal Rabbit DNA-(apurinic or apyrimidinic site) lyase Antibody (HRP) 100 μg
CSB-EL001901MO Mouse DNA-(apurinic or apyrimidinic site) lyase (APEX2) ELISA kit 96T
abx109730 Polyclonal Rabbit DNA-(apurinic or apyrimidinic site) lyase Antibody 100 μg
abx105348 Polyclonal Rabbit DNA-(apurinic or apyrimidinic site) lyase Antibody (Biotin) 100 μg
abx106767 Polyclonal Rabbit DNA-(apurinic or apyrimidinic site) lyase Antibody (FITC) 100 μg
CSB-EP001900HU Recombinant human DNA-(apurinic or apyrimidinic site) lyase Source: E.coli 1mg
CSB-EP001900HU Recombinant human DNA-(apurinic or apyrimidinic site) lyase Source: E.coli 200ug


 

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