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Q6R2P8 (NEIL2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 329328Endonuclease 8-like 2
PRO_0000170909

Regions

Zinc finger280 – 31637FPG-type

Sites

Active site21Schiff-base intermediate with DNA By similarity
Active site31Proton donor By similarity
Active site501Proton donor; for beta-elimination activity By similarity
Active site3061Proton donor; for delta-elimination activity By similarity
Binding site2271DNA By similarity

Amino acid modifications

Modified residue501N6-acetyllysine By similarity
Modified residue1501N6-acetyllysine By similarity

Experimental info

Sequence conflict2201R → K in AAR98807. Ref.1
Sequence conflict2561L → F in AAR98807. Ref.1
Sequence conflict3181L → P in AAR98807. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q6R2P8 [UniParc].

Last modified September 18, 2013. Version 4.
Checksum: 221781934B9EB5A5

FASTA32936,834
        10         20         30         40         50         60 
MPEGPSVRKF HHLVSPFVGQ KVVKTGGSSK KLHPAAFQSL WLQDAQVHGK KLFLRFDPDE 

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

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

       190        200        210        220        230        240 
SPPPVIEPTC DILSEKFHRG QALEALSQAQ PVCYTLLDQR YFSGLGNIIK NEALYRARIH 

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

       310        320 
PDGLQRLTWW CPQCQPQLSS KGPQNLPSS 

« Hide

References

« Hide 'large scale' 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.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
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. expand/collapse author list , 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.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY518221 mRNA. Translation: AAR98807.1.
AC090654 Genomic DNA. No translation available.
CH466535 Genomic DNA. Translation: EDL36068.1.
CCDSCCDS36949.1.
RefSeqNP_963904.2. NM_201610.2.
XP_006519262.1. XM_006519199.1.
UniGeneMm.239490.

3D structure databases

ProteinModelPortalQ6R2P8.
SMRQ6R2P8. Positions 115-315.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ6R2P8.

Proteomic databases

PRIDEQ6R2P8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000038229; ENSMUSP00000045200; ENSMUSG00000035121.
GeneID382913.
KEGGmmu:382913.
UCSCuc007uhk.1. mouse.

Organism-specific databases

CTD252969.
MGIMGI:2686058. Neil2.

Phylogenomic databases

eggNOGNOG73546.
GeneTreeENSGT00730000110955.
HOGENOMHOG000069913.
HOVERGENHBG082014.
InParanoidQ6R2P8.
KOK10568.
OMASVRKFHH.
OrthoDBEOG7Z69CR.
TreeFamTF331502.

Gene expression databases

CleanExMM_NEIL2.
GenevestigatorQ6R2P8.

Family and domain databases

InterProIPR015886. 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]
PfamPF01149. Fapy_DNA_glyco. 1 hit.
PF06831. H2TH. 1 hit.
[Graphical view]
SUPFAMSSF46946. SSF46946. 1 hit.
PROSITEPS51068. FPG_CAT. 1 hit.
PS51066. ZF_FPG_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio403564.
PROQ6R2P8.
SOURCESearch...

Entry information

Entry nameNEIL2_MOUSE
AccessionPrimary (citable) accession number: Q6R2P8
Secondary accession number(s): G3X969
Entry history
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: September 18, 2013
Last modified: July 9, 2014
This is version 76 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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