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Protein

Endonuclease III-like protein 1

Gene

NTHL1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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.UniRule annotation

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 annotation

Cofactori

[4Fe-4S] clusterUniRule annotationNote: 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.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei213 – 2131Nucleophile; for N-glycosylase activityUniRule annotation
Sitei232 – 2321Important for catalytic activityUniRule annotation
Metal bindingi283 – 2831Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi290 – 2901Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi293 – 2931Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi299 – 2991Iron-sulfur (4Fe-4S)UniRule annotation

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. DNA-(apurinic or apyrimidinic site) lyase activity Source: UniProtKB-EC
  3. DNA N-glycosylase activity Source: Ensembl
  4. double-stranded DNA binding Source: Ensembl
  5. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. base-excision repair, AP site formation Source: Ensembl
  2. nucleotide-excision repair, DNA incision, 5'-to lesion Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase, Lyase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_203635. Displacement of DNA glycosylase by APE1.
REACT_227493. Recognition and association of DNA glycosylase with site containing an affected pyrimidine.

Names & Taxonomyi

Protein namesi
Recommended name:
Endonuclease III-like protein 1UniRule annotation (EC:3.2.2.-UniRule annotation, EC:4.2.99.18UniRule annotation)
Alternative name(s):
Bifunctional DNA N-glycoslyase/DNA-(apurinic or apyrimidinic site) lyaseUniRule annotation
Short name:
DNA glycoslyase/AP lyaseUniRule annotation
Gene namesi
Name:NTHL1UniRule annotation
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 25

Subcellular locationi

Nucleus UniRule annotation. Mitochondrion UniRule annotation

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2828MitochondrionUniRule annotationAdd
BLAST
Chaini29 – 305277Endonuclease III-like protein 1PRO_0000244406Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei64 – 641PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ2KID2.

Interactioni

Subunit structurei

Interacts with YBX1.UniRule annotation

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000046623.

Structurei

3D structure databases

ProteinModelPortaliQ2KID2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini192 – 21625HhHUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the Nth/MutY family.UniRule annotation
Contains 1 HhH domain.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0177.
GeneTreeiENSGT00510000047513.
HOGENOMiHOG000252209.
HOVERGENiHBG052675.
InParanoidiQ2KID2.
KOiK10773.
OMAiWRNKVKY.
OrthoDBiEOG76MK8Z.
TreeFamiTF314967.

Family and domain databases

Gene3Di1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
HAMAPiMF_03183. Endonuclease_III_Nth.
InterProiIPR011257. DNA_glycosylase.
IPR004036. Endonuclease-III-like_CS2.
IPR004035. Endouclease-III_FeS-bd_BS.
IPR003651. Endouclease3_FeS-loop_motif.
IPR003265. HhH-GPD_domain.
IPR000445. HhH_motif.
IPR023170. HTH_base_excis_C.
[Graphical view]
PfamiPF00633. HHH. 1 hit.
PF00730. HhH-GPD. 1 hit.
[Graphical view]
SMARTiSM00478. ENDO3c. 1 hit.
SM00525. FES. 1 hit.
[Graphical view]
SUPFAMiSSF48150. SSF48150. 1 hit.
PROSITEiPS00764. ENDONUCLEASE_III_1. 1 hit.
PS01155. ENDONUCLEASE_III_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q2KID2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNAAGVRMVV TRARSRGTGA SLRRRGEKAA PLRSGEAAAE ERKSYSPVKR
60 70 80 90 100
RRKAQRLSVA YEASEGEGGE GAEHLQAPSW QPQDWRQQLD NIRTMRSGKD
110 120 130 140 150
APVDQLGAEH CFDPSASPKV RRYQVLLSLM LSSQTKDQVT AGAMQRLRAR
160 170 180 190 200
GLTVDSILQT DDSTLGALIY PVGFWRSKVK YIKQTSAILQ QRYDGDIPAS
210 220 230 240 250
VAELVALPGV GPKMAHLAMA VAWGTVSGIA VDTHVHRIAN RLRWTKKATK
260 270 280 290 300
SPEETRRALE EWLPRELWSE INGLLVGFGQ QTCLPIRPRC QACLNRALCP

AARGL
Length:305
Mass (Da):33,645
Last modified:March 7, 2006 - v1
Checksum:i9318553C857F500C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GJ062847 Genomic DNA. Translation: DAA15605.1.
BC112681 mRNA. Translation: AAI12682.1.
RefSeqiNP_001039862.1. NM_001046397.2.
UniGeneiBt.6550.

Genome annotation databases

EnsembliENSBTAT00000049780; ENSBTAP00000046623; ENSBTAG00000006272.
GeneIDi535203.
KEGGibta:535203.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GJ062847 Genomic DNA. Translation: DAA15605.1.
BC112681 mRNA. Translation: AAI12682.1.
RefSeqiNP_001039862.1. NM_001046397.2.
UniGeneiBt.6550.

3D structure databases

ProteinModelPortaliQ2KID2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000046623.

Proteomic databases

PRIDEiQ2KID2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000049780; ENSBTAP00000046623; ENSBTAG00000006272.
GeneIDi535203.
KEGGibta:535203.

Organism-specific databases

CTDi4913.

Phylogenomic databases

eggNOGiCOG0177.
GeneTreeiENSGT00510000047513.
HOGENOMiHOG000252209.
HOVERGENiHBG052675.
InParanoidiQ2KID2.
KOiK10773.
OMAiWRNKVKY.
OrthoDBiEOG76MK8Z.
TreeFamiTF314967.

Enzyme and pathway databases

ReactomeiREACT_203635. Displacement of DNA glycosylase by APE1.
REACT_227493. Recognition and association of DNA glycosylase with site containing an affected pyrimidine.

Miscellaneous databases

NextBioi20876660.

Family and domain databases

Gene3Di1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
HAMAPiMF_03183. Endonuclease_III_Nth.
InterProiIPR011257. DNA_glycosylase.
IPR004036. Endonuclease-III-like_CS2.
IPR004035. Endouclease-III_FeS-bd_BS.
IPR003651. Endouclease3_FeS-loop_motif.
IPR003265. HhH-GPD_domain.
IPR000445. HhH_motif.
IPR023170. HTH_base_excis_C.
[Graphical view]
PfamiPF00633. HHH. 1 hit.
PF00730. HhH-GPD. 1 hit.
[Graphical view]
SMARTiSM00478. ENDO3c. 1 hit.
SM00525. FES. 1 hit.
[Graphical view]
SUPFAMiSSF48150. SSF48150. 1 hit.
PROSITEiPS00764. ENDONUCLEASE_III_1. 1 hit.
PS01155. ENDONUCLEASE_III_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], GENOME REANNOTATION.
    Strain: HerefordImported.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Hypothalamus.

Entry informationi

Entry nameiNTH_BOVIN
AccessioniPrimary (citable) accession number: Q2KID2
Secondary accession number(s): M5FK15
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: March 7, 2006
Last modified: February 4, 2015
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.