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Q5RAJ7

- NEIL2_PONAB

UniProt

Q5RAJ7 - NEIL2_PONAB

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Protein

Endonuclease 8-like 2

Gene
NEIL2
Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

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 activityi

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 regulationi

Acetylation of Lys-50 leads to loss of DNA nicking activity By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21Schiff-base intermediate with DNA By similarity
Active sitei3 – 31Proton donor By similarity
Active sitei50 – 501Proton donor; for beta-elimination activity By similarity
Binding sitei231 – 2311DNA By similarity
Active sitei310 – 3101Proton donor; for delta-elimination activity By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri284 – 32037FPG-typeAdd
BLAST

GO - Molecular functioni

  1. damaged DNA binding Source: InterPro
  2. DNA-(apurinic or apyrimidinic site) lyase activity Source: UniProtKB-EC
  3. hydrolase activity, hydrolyzing N-glycosyl compounds Source: InterPro
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. base-excision repair Source: InterPro
  2. nucleotide-excision repair Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase, Lyase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
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-like protein 2
Gene namesi
Name:NEIL2
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 332331Endonuclease 8-like 2PRO_0000248635Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei50 – 501N6-acetyllysine By similarity
Modified residuei154 – 1541N6-acetyllysine By similarity

Keywords - PTMi

Acetylation

Interactioni

Subunit structurei

Binds EP300 By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ5RAJ7.

Family & Domainsi

Domaini

The zinc-finger domain is important for DNA binding.

Sequence similaritiesi

Belongs to the FPG family.

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri284 – 32037FPG-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

HOVERGENiHBG082014.
InParanoidiQ5RAJ7.
KOiK10568.

Family and domain databases

InterProiIPR015886. 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]
PfamiPF01149. Fapy_DNA_glyco. 1 hit.
PF06831. H2TH. 1 hit.
[Graphical view]
SUPFAMiSSF46946. SSF46946. 1 hit.
PROSITEiPS51068. FPG_CAT. 1 hit.
PS51066. ZF_FPG_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q5RAJ7-1 [UniParc]FASTAAdd to Basket

« Hide

MPEGPLVRKF HHLVSPFVGQ QVVKTGGSSK KLQPASLQCL WLQDTQVNGK    50
KLFLRFDPDE EMGPPGSSPP PEPPQKEAQK EGAADPKQVG EPSGQKTPDG 100
SSQSAELVPQ GEDDSEYLER DAPAGDAGRW LRVSFGLFGS VWVNEFSRAK 150
QANKRGDWRD PSPRLVLHCG GGGFLAFYNC QMSWSSSPVV TPTCDILSEK 200
FHRGQALEAL GQAQPVCYTL LDQRYFSGLG NIIKNEALYR AGIHPLSLGS 250
VLSASRREVL VDHVVEFSTA WLQGKFQGRP QRTQVYQREQ CPAGHQVMKE 300
AFGPQDGLQR LTWWCPQCQP QLSEEPEQRQ FS 332
Length:332
Mass (Da):36,814
Last modified:January 23, 2007 - v3
Checksum:i607670A7EFE6E6C5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR859018 mRNA. Translation: CAH91213.1.
RefSeqiNP_001125714.1. NM_001132242.1.

Genome annotation databases

GeneIDi100172638.
KEGGipon:100172638.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR859018 mRNA. Translation: CAH91213.1 .
RefSeqi NP_001125714.1. NM_001132242.1.

3D structure databases

ProteinModelPortali Q5RAJ7.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100172638.
KEGGi pon:100172638.

Organism-specific databases

CTDi 252969.

Phylogenomic databases

HOVERGENi HBG082014.
InParanoidi Q5RAJ7.
KOi K10568.

Family and domain databases

InterProi 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 ]
Pfami PF01149. Fapy_DNA_glyco. 1 hit.
PF06831. H2TH. 1 hit.
[Graphical view ]
SUPFAMi SSF46946. SSF46946. 1 hit.
PROSITEi PS51068. FPG_CAT. 1 hit.
PS51066. ZF_FPG_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

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

Entry informationi

Entry nameiNEIL2_PONAB
AccessioniPrimary (citable) accession number: Q5RAJ7
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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