Endonuclease 8-like 2 - Mus musculus (Mouse)

Contribute

Send feedback

Read comments (?) or add your own

Q6R2P8 (NEIL2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 64. History...

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

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

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
Synonyms:	Gm1212

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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	Removes damaged bases from DNA, leaving an abasic site. 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 direct assay PubMed 15725623. Source: MGI nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell spindle microtubule Inferred from direct assay PubMed 15725623. Source: MGI
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 microtubule binding Inferred from direct assay PubMed 15725623. Source: MGI 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_0000170909

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

150

N6-acetyllysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q6R2P8 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 6A9464C18FB5DD11
Show »

FASTA

329

36,865

        10         20         30         40         50         60 
MPEGPSVRKF HHLVSPFVGQ KVVKTGGSSK KLHPAAFQSL WLQDAQVHGK KLFLRFDPDE 

        70         80         90        100        110        120 
EMEPLNSSPQ PIQGMWQKEA VDRELALGPS AQEPSAGPSG SGEPVXSRSA ETYNLGKIPS 

       130        140        150        160        170        180 
ADAQRWLEVR FGLFGSXWVN DFSRAKKANK KGDWRDPVPR LVLHFSGGGF LVFYNCQMSW 

       190        200        210        220        230        240 
SXXPVIEPTC DILSEKFHRG QALEALSQAQ PVCYTLLDQK YFSGLGNIIK NEALYRARIH 

       250        260        270        280        290        300 
PLSLGSCLSS SSREAFVDHV VEFSKDWLRD KFQGKERHTQ IYQKEQCPSG HQVMKETFGP 

       310        320 
PDGLQRLTWW CPQCQPQPSS KGPQNLPSS

« Hide

References

[1]	"Gene identification signature analysis: a novel method for genome annotation." Ang C.C., Ng P.W.P., Wei C.L., Ruan Y. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: 129/Ola.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY518221 mRNA. Translation: AAR98807.1.
IPI	IPI00400063.
UniGene	Mm.239490.
3D structure databases
ProteinModelPortal	Q6R2P8.
SMR	Q6R2P8. Positions 181-275.
ModBase	Search...
PTM databases
PhosphoSite	Q6R2P8.
Proteomic databases
PRIDE	Q6R2P8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
MGI	MGI:2686058. Neil2.
Phylogenomic databases
eggNOG	NOG73546.
HOGENOM	HOG000069913.
HOVERGEN	HBG082014.
InParanoid	Q6R2P8.
OrthoDB	EOG4GTKDB.
Gene expression databases
CleanEx	MM_NEIL2.
Genevestigator	Q6R2P8.
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
SOURCE	Search...

Entry information

Entry name

NEIL2_MOUSE

Accession

Primary (citable) accession number: Q6R2P8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 7, 2004
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 64 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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

PTM databases

Proteomic databases

Protocols and materials databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents