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Q5RAJ7 (NEIL2_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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-like protein 2
Gene names
Name:NEIL2
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length332 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 – 332331Endonuclease 8-like 2
PRO_0000248635

Regions

Zinc finger284 – 32037FPG-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 site3101Proton donor; for delta-elimination activity By similarity
Binding site2311DNA By similarity

Amino acid modifications

Modified residue501N6-acetyllysine By similarity
Modified residue1541N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5RAJ7 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 607670A7EFE6E6C5

FASTA33236,814
        10         20         30         40         50         60 
MPEGPLVRKF HHLVSPFVGQ QVVKTGGSSK KLQPASLQCL WLQDTQVNGK KLFLRFDPDE 

        70         80         90        100        110        120 
EMGPPGSSPP PEPPQKEAQK EGAADPKQVG EPSGQKTPDG SSQSAELVPQ GEDDSEYLER 

       130        140        150        160        170        180 
DAPAGDAGRW LRVSFGLFGS VWVNEFSRAK QANKRGDWRD PSPRLVLHCG GGGFLAFYNC 

       190        200        210        220        230        240 
QMSWSSSPVV TPTCDILSEK FHRGQALEAL GQAQPVCYTL LDQRYFSGLG NIIKNEALYR 

       250        260        270        280        290        300 
AGIHPLSLGS VLSASRREVL VDHVVEFSTA WLQGKFQGRP QRTQVYQREQ CPAGHQVMKE 

       310        320        330 
AFGPQDGLQR LTWWCPQCQP QLSEEPEQRQ FS 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR859018 mRNA. Translation: CAH91213.1.
RefSeqNP_001125714.1. NM_001132242.1.

3D structure databases

ProteinModelPortalQ5RAJ7.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100172638.
KEGGpon:100172638.

Organism-specific databases

CTD252969.

Phylogenomic databases

HOVERGENHBG082014.
InParanoidQ5RAJ7.
KOK10568.

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...

Entry information

Entry nameNEIL2_PONAB
AccessionPrimary (citable) accession number: Q5RAJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 48 of the entry and version 3 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