Endonuclease 8-like 2 - Bos taurus (Bovine)

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Q6IE77 (NEIL2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 66. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Endonuclease 8-like 2
EC=3.2.2.-
EC=4.2.99.18

Alternative name(s):
DNA glycosylase/AP lyase Neil2
DNA-(apurinic or apyrimidinic site) lyase Neil2
Endonuclease VIII-like 2
Nei homolog 2
Short name=NEH2
Nei-like protein 2

Gene names

Name:

NEIL2

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	329 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Has DNA glycosylase activity towards 5-hydroxyuracil and other oxidized derivatives of cytosine with a preference for mismatched double stranded DNA (DNA bubbles). Has low or no DNA glycosylase activity towards thymine glycol, 2-hydroxyadenine, hypoxanthine and 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates By similarity.
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.
Enzyme regulation	Acetylation of Lys-50 leads to loss of DNA nicking activity By similarity.
Subunit structure	Binds EP300 By similarity.
Subcellular location	Nucleus By similarity.
Domain	The zinc-finger domain is important for DNA binding.
Sequence similarities	Belongs to the FPG family. Contains 1 FPG-type zinc finger.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Glycosidase Hydrolase Lyase
PTM	Acetylation
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	base-excision repair Inferred from electronic annotation. Source: InterPro nucleotide-excision repair Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: Compara nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell spindle microtubule Inferred from electronic annotation. Source: Compara
Molecular_function	DNA-(apurinic or apyrimidinic site) lyase activity Inferred from electronic annotation. Source: EC damaged DNA binding Inferred from electronic annotation. Source: InterPro hydrolase activity, hydrolyzing N-glycosyl compounds Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 329

328

Endonuclease 8-like 2

PRO_0000170907

Regions

Zinc finger

280 – 316

FPG-type

Sites

Active site

Schiff-base intermediate with DNA By similarity

Active site

Proton donor By similarity

Active site

Proton donor; for beta-elimination activity By similarity

Active site

306

Proton donor; for delta-elimination activity By similarity

Binding site

227

DNA By similarity

Amino acid modifications

Modified residue

N6-acetyllysine By similarity

Modified residue

149

N6-acetyllysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q6IE77 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 0D48CC7BEDA526EA
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FASTA

329

36,392

        10         20         30         40         50         60 
MPEGPSVRKF HHLVSPFVGQ QVVKTGGSSK KLNPTSFQSL WLQDSQVHGK KLFLRFDPDE 

        70         80         90        100        110        120 
EAVSLGNSLL SEPLREGEQK DKARHHQEAS DPSSWSPGGD SAVPSGDDGL QCLGGDTPAG 

       130        140        150        160        170        180 
GAERWLQVSF GLFGSIRVNE FSRAKKANKR GDWRDPVPRL VLHFSGSGFL AFYNCQMTWR 

       190        200        210        220        230        240 
FSSPVVSPAS DILSEKFHRG QALEALGREQ PICYTLLDQR YFSGLGNIIK NEALFRAGIH 

       250        260        270        280        290        300 
PLSPGSLLGL PRLEALVDHV VAFSADWLQG KFQGTRQHTQ IYQKEQCPAG HQVVRESLGP 

       310        320 
PGGFQRLTWW CPQCQPRLSA DEPKQLQPS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of taurine cattle: a window to ruminant biology and evolution." The bovine genome sequencing and analysis consortium Science 324:522-528(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Hereford.
[2]	"Mapping of the GATA4, NEIL2, FDFT1 genes and CTSB-associated microsatellites to the centromeric region of BTA8." Plis-Finarov A., Hudson H., Roe B., Ron M., Seroussi E. Anim. Genet. 35:154-155(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC107065 Genomic DNA. No translation available. BN000316 mRNA. Translation: CAE48362.1.
IPI	IPI00687805.
RefSeq	NP_001013021.1. NM_001013003.1.
UniGene	Bt.26303.
3D structure databases
ProteinModelPortal	Q6IE77.
ModBase	Search...
Protein-protein interaction databases
STRING	9913.ENSBTAP00000006262.
Proteomic databases
PRIDE	Q6IE77.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000006262; ENSBTAP00000006262; ENSBTAG00000004769.
GeneID	444987.
KEGG	bta:444987.
Organism-specific databases
CTD	252969.
Phylogenomic databases
eggNOG	NOG73546.
GeneTree	ENSGT00510000048740.
HOGENOM	HOG000069913.
HOVERGEN	HBG082014.
InParanoid	Q6IE77.
KO	K10568.
OMA	GHQVMKE.
OrthoDB	EOG4GTKDB.
Family and domain databases
InterPro	IPR015886. DNA_glyclase/AP_lyase_DNA-bd. IPR012319. DNA_glycosylase/AP_lyase_cat. IPR010979. Ribosomal_S13-like_H2TH. IPR000214. Znf_DNA_glyclase/AP_lyase. [Graphical view]
Pfam	PF01149. Fapy_DNA_glyco. 1 hit. PF06831. H2TH. 1 hit. [Graphical view]
SUPFAM	SSF46946. Ribosomal_H2TH. 1 hit.
PROSITE	PS51068. FPG_CAT. 1 hit. PS01242. ZF_FPG_1. False negative. PS51066. ZF_FPG_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20831770.

Entry information

Entry name

NEIL2_BOVIN

Accession

Primary (citable) accession number: Q6IE77

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 7, 2004
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 66 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents