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Protein

Endonuclease III homolog 1

Gene

NTG1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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, but also purine-derived lesions, alkylation damage and cytosine photoproducts generated by UV irradiation as well as abasic sites. Has also 8-oxoguanine DNA glycosylase activity. The AP lyase can incise AP sites opposite all four bases. May also play a role in the regulation of mtDNA copy number by introducing a double-stranded break (DSB) at the mtDNA replication origin ori5, initiating the rolling-circle mtDNA replication.UniRule annotation13 Publications

Miscellaneous

Does not possess a consensus sequence for a C-terminal iron-sulfur center typical of all other endonuclease III homologs.1 Publication

Catalytic activityi

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.UniRule annotation3 Publications

Kineticsi

  1. KM=227 nM for dihydrouracil containing duplex oligonucleotides (N-glycosylase activity)3 Publications
  2. KM=250 nM for 5-hydroxy-6-hydrothymine containing duplex oligonucleotides (N-glycosylase activity)3 Publications
  3. KM=721 nM for 5-hydroxy-6-hydrouracil containing duplex oligonucleotides (N-glycosylase activity)3 Publications
  4. KM=755 nM for 5-hydroxy-5-methylhydantoin containing duplex oligonucleotides (N-glycosylase activity)3 Publications
  5. KM=997 nM for 5-hydroxyuracil containing duplex oligonucleotides (N-glycosylase activity)3 Publications
  6. KM=1380 nM for 5-hydroxycytosine containing duplex oligonucleotides (N-glycosylase activity)3 Publications
  7. KM=3250 nM for thymine glycol containing duplex oligonucleotides (N-glycosylase activity)3 Publications
  8. KM=1305 nM for 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyAde) containing duplex oligonucleotides (N-glycosylase activity)3 Publications
  9. KM=2460 nM for 4,6-diamino-5-formamidopyrimidine (FapyGua) containing duplex oligonucleotides (N-glycosylase activity)3 Publications
  10. KM=24.86 nM for AP/G abasic-site containing duplex oligonucleotides (AP lyase activity)3 Publications
  11. KM=11.37 nM for AP/A abasic-site containing duplex oligonucleotides (AP lyase activity)3 Publications
  12. KM=6.67 nM for AP/T abasic-site containing duplex oligonucleotides (AP lyase activity)3 Publications
  13. KM=36.58 nM for AP/C abasic-site containing duplex oligonucleotides (AP lyase activity)3 Publications
  1. Vmax=1.9 nmol/min/ng enzyme for dihydrouracil containing duplex oligonucleotides (N-glycosylase activity)3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei243Nucleophile; for N-glycosylase activityUniRule annotation1
Sitei262Important for catalytic activityUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase, Lyase
Biological processDNA damage, DNA repair

Enzyme and pathway databases

BioCyciYEAST:G3O-28827-MONOMER
ReactomeiR-SCE-110329 Cleavage of the damaged pyrimidine
R-SCE-110357 Displacement of DNA glycosylase by APEX1

Names & Taxonomyi

Protein namesi
Recommended name:
Endonuclease III homolog 1UniRule annotation (EC:3.2.2.-UniRule annotation, EC:4.2.99.18UniRule annotation)
Alternative name(s):
Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase 1UniRule annotation
Short name:
DNA glycosylase/AP lyase 1UniRule annotation
Endonuclease III-like glycosylase 1
Redoxyendonuclease 1
Gene namesi
Name:NTG1UniRule annotation
Synonyms:OGG2, SCR1
Ordered Locus Names:YAL015C
ORF Names:FUN33
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome I

Organism-specific databases

SGDiS000000013 NTG1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion, Nucleus

Pathology & Biotechi

Disruption phenotypei

Greatly increases spontaneous and hydrogen peroxide-induced mutation frequency. Causes mitochondrial genome instability. Suppresses mitochondrial point mutation rates, frameshifts and recombination rates, probably because NTG1 can generate mutagenic intermediates in yeast mitochondrial DNA.3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi3 – 6KISK → EISE in NTG1(mts); reduces mitochondrial localization by 40%. 1 Publication4
Mutagenesisi15 – 16KR → AA in NTG1(nls1); reduces nuclear localization by 60%. 1 Publication2
Mutagenesisi33 – 34KR → AA in NTG1(nls2); reduces nuclear localization by 60%. 1 Publication2
Mutagenesisi243K → Q: Abolishes cleavage of substrate oligonucleotides. 1 Publication1
Mutagenesisi364K → R: Cannot properly relocalize in response to oxidative stress. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 26MitochondrionUniRule annotationAdd BLAST26
ChainiPRO_000000174427 – 399Endonuclease III homolog 1Add BLAST373

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki194Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)Curated

Post-translational modificationi

Monosumoylated. Sumoylation is associated with targeting of NTG1 to nuclei containing oxidative DNA damage.1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP31378
PaxDbiP31378
PRIDEiP31378
TopDownProteomicsiP31378

Expressioni

Inductioni

By oxidizing agents.3 Publications

Interactioni

Protein-protein interaction databases

BioGridi31751, 105 interactors
DIPiDIP-6614N
IntActiP31378, 24 interactors
STRINGi4932.YAL015C

Structurei

3D structure databases

ProteinModelPortaliP31378
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini223 – 247HhHUniRule annotationAdd BLAST25

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi14 – 37Bipartite nuclear localization signalSequence analysisAdd BLAST24

Sequence similaritiesi

Belongs to the Nth/MutY family.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00510000047513
HOGENOMiHOG000252209
InParanoidiP31378
KOiK10773
OMAiFGQVICM
OrthoDBiEOG092C3TX5

Family and domain databases

CDDicd00056 ENDO3c, 1 hit
Gene3Di1.10.1670.10, 1 hit
HAMAPiMF_03183 Endonuclease_III_Nth, 1 hit
InterProiView protein in InterPro
IPR011257 DNA_glycosylase
IPR004036 Endonuclease-III-like_CS2
IPR003265 HhH-GPD_domain
IPR000445 HhH_motif
IPR023170 HTH_base_excis_C
IPR030841 NTH1
PfamiView protein in Pfam
PF00633 HHH, 1 hit
PF00730 HhH-GPD, 1 hit
SMARTiView protein in SMART
SM00478 ENDO3c, 1 hit
SUPFAMiSSF48150 SSF48150, 1 hit
PROSITEiView protein in PROSITE
PS01155 ENDONUCLEASE_III_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P31378-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQKISKYSSM AILRKRPLVK TETGPESELL PEKRTKIKQE EVVPQPVDID
60 70 80 90 100
WVKSLPNKQY FEWIVVRNGN VPNRWATPLD PSILVTPAST KVPYKFQETY
110 120 130 140 150
ARMRVLRSKI LAPVDIIGGS SIPVTVASKC GISKEQISPR DYRLQVLLGV
160 170 180 190 200
MLSSQTKDEV TAMAMLNIMR YCIDELHSEE GMTLEAVLQI NETKLDELIH
210 220 230 240 250
SVGFHTRKAK YILSTCKILQ DQFSSDVPAT INELLGLPGV GPKMAYLTLQ
260 270 280 290 300
KAWGKIEGIC VDVHVDRLTK LWKWVDAQKC KTPDQTRTQL QNWLPKGLWT
310 320 330 340 350
EINGLLVGFG QIITKSRNLG DMLQFLPPDD PRSSLDWDLQ SQLYKEIQQN
360 370 380 390
IMSYPKWVKY LEGKRELNVE AEINVKHEEK TVEETMVKLE NDISVKVED
Length:399
Mass (Da):45,577
Last modified:July 1, 1993 - v1
Checksum:iA3C878A3004908F3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05146 Genomic DNA Translation: AAC04942.1
BK006935 Genomic DNA Translation: DAA06973.1
PIRiS36719
RefSeqiNP_009387.1, NM_001178160.1

Genome annotation databases

EnsemblFungiiYAL015C; YAL015C; YAL015C
GeneIDi851218
KEGGisce:YAL015C

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05146 Genomic DNA Translation: AAC04942.1
BK006935 Genomic DNA Translation: DAA06973.1
PIRiS36719
RefSeqiNP_009387.1, NM_001178160.1

3D structure databases

ProteinModelPortaliP31378
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31751, 105 interactors
DIPiDIP-6614N
IntActiP31378, 24 interactors
STRINGi4932.YAL015C

Proteomic databases

MaxQBiP31378
PaxDbiP31378
PRIDEiP31378
TopDownProteomicsiP31378

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYAL015C; YAL015C; YAL015C
GeneIDi851218
KEGGisce:YAL015C

Organism-specific databases

SGDiS000000013 NTG1

Phylogenomic databases

GeneTreeiENSGT00510000047513
HOGENOMiHOG000252209
InParanoidiP31378
KOiK10773
OMAiFGQVICM
OrthoDBiEOG092C3TX5

Enzyme and pathway databases

BioCyciYEAST:G3O-28827-MONOMER
ReactomeiR-SCE-110329 Cleavage of the damaged pyrimidine
R-SCE-110357 Displacement of DNA glycosylase by APEX1

Miscellaneous databases

PROiPR:P31378

Family and domain databases

CDDicd00056 ENDO3c, 1 hit
Gene3Di1.10.1670.10, 1 hit
HAMAPiMF_03183 Endonuclease_III_Nth, 1 hit
InterProiView protein in InterPro
IPR011257 DNA_glycosylase
IPR004036 Endonuclease-III-like_CS2
IPR003265 HhH-GPD_domain
IPR000445 HhH_motif
IPR023170 HTH_base_excis_C
IPR030841 NTH1
PfamiView protein in Pfam
PF00633 HHH, 1 hit
PF00730 HhH-GPD, 1 hit
SMARTiView protein in SMART
SM00478 ENDO3c, 1 hit
SUPFAMiSSF48150 SSF48150, 1 hit
PROSITEiView protein in PROSITE
PS01155 ENDONUCLEASE_III_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiNTH1_YEAST
AccessioniPrimary (citable) accession number: P31378
Secondary accession number(s): D6VPK3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 7, 2018
This is version 161 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome I
    Yeast (Saccharomyces cerevisiae) chromosome I: entries and gene names
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