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Protein

Endonuclease 8-like 1

Gene

Neil1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, formamidopyrimidine (Fapy) and 5-hydroxyuracil. Has marginal activity towards 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. Has DNA glycosylase/lyase activity towards mismatched uracil and thymine, in particular in U:C and T:C mismatches. Specifically binds 5-hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of 5hmC.2 Publications

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.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21Schiff-base intermediate with DNACurated
Active sitei3 – 31Proton donorCurated
Active sitei54 – 541Proton donor; for beta-elimination activityCurated
Binding sitei176 – 1761DNABy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase, Lyase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_342323. Cleavage of the damaged pyrimidine.
REACT_359415. APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Endonuclease 8-like 1 (EC:3.2.2.-, EC:4.2.99.18)
Alternative name(s):
DNA glycosylase/AP lyase Neil1
DNA-(apurinic or apyrimidinic site) lyase Neil1
Endonuclease VIII-like 1
Nei homolog 1
Short name:
NEH1
Nei-like protein 1
Gene namesi
Name:Neil1
Synonyms:Nei1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1920024. Neil1.

Subcellular locationi

GO - Cellular componenti

  • chromosome Source: UniProtKB-SubCell
  • cytoplasm Source: MGI
  • microtubule organizing center Source: UniProtKB-SubCell
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 389388Endonuclease 8-like 1PRO_0000170906Add
BLAST

Proteomic databases

PRIDEiQ8K4Q6.

PTM databases

PhosphoSiteiQ8K4Q6.

Expressioni

Tissue specificityi

Detected in heart, spleen and lung.1 Publication

Inductioni

Up-regulated during S-phase.By similarity

Gene expression databases

BgeeiQ8K4Q6.
CleanExiMM_NEIL1.
GenevisibleiQ8K4Q6. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034842.

Structurei

3D structure databases

ProteinModelPortaliQ8K4Q6.
SMRiQ8K4Q6. Positions 2-290.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FPG family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG75119.
GeneTreeiENSGT00390000016671.
HOGENOMiHOG000067872.
HOVERGENiHBG052592.
InParanoidiQ8K4Q6.
KOiK10567.
OMAiCVLLEYE.
OrthoDBiEOG7H1JM2.
PhylomeDBiQ8K4Q6.
TreeFamiTF333272.

Family and domain databases

InterProiIPR015886. DNA_glyclase/AP_lyase_DNA-bd.
IPR012319. DNA_glycosylase/AP_lyase_cat.
IPR015371. Endonuclease-VIII_DNA-bd.
IPR010979. Ribosomal_S13-like_H2TH.
[Graphical view]
PfamiPF01149. Fapy_DNA_glyco. 1 hit.
PF06831. H2TH. 1 hit.
PF09292. Neil1-DNA_bind. 1 hit.
[Graphical view]
SMARTiSM00898. Fapy_DNA_glyco. 1 hit.
[Graphical view]
SUPFAMiSSF46946. SSF46946. 1 hit.
SSF81624. SSF81624. 1 hit.
PROSITEiPS51068. FPG_CAT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8K4Q6-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPEGPELHLA SHFVNETCKG LVFGGCVEKS SVSRNPEVPF ESSAYHISAL
60 70 80 90 100
ARGKELRLTL SPLPGSQPPQ KPLSLVFRFG MSGSFQLVPA EALPRHAHLR
110 120 130 140 150
FYTAPPAPRL ALCFVDIRRF GHWDPGGEWQ PGRGPCVLLE YERFRENVLR
160 170 180 190 200
NLSDKAFDRP ICEALLDQRF FNGIGNYLRA EILYRLKIPP FEKARTVLEA
210 220 230 240 250
LQQCRPSPEL TLSQKIKAKL QNPDLLELCH LVPKEVVQLG GKGYGPERGE
260 270 280 290 300
EDFAAFRAWL RCYGVPGMSS LRDRHGRTIW FQGDPGPLAP KGGRSQKKKS
310 320 330 340 350
QETQLGAEDR KEDLPLSSKS VSRMRRARKH PPKRIAQQSE GAGLQQNQET
360 370 380
PTAPEKGKRR GQRASTGHRR RPKTIPDTRP REAGESSAS
Length:389
Mass (Da):43,586
Last modified:January 23, 2007 - v3
Checksum:iE3F1A21DDE2CB5AD
GO
Isoform 2 (identifier: Q8K4Q6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     241-389: GKGYGPERGE...PREAGESSAS → EAWGGQDGRRPLP

Note: No experimental confirmation available.
Show »
Length:253
Mass (Da):28,453
Checksum:i8BE7DE61651A166A
GO

Sequence cautioni

The sequence BAB28790.1 differs from that shown. Reason: Frameshift at position 344. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei241 – 389149GKGYG…ESSAS → EAWGGQDGRRPLP in isoform 2. 1 PublicationVSP_012207Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB079069 mRNA. Translation: BAC06477.1.
AK013322 mRNA. Translation: BAB28790.1. Frameshift.
BC043297 mRNA. Translation: AAH43297.1.
CCDSiCCDS23217.1. [Q8K4Q6-1]
RefSeqiNP_082623.1. NM_028347.2. [Q8K4Q6-1]
XP_006511548.1. XM_006511485.2. [Q8K4Q6-1]
XP_006511549.1. XM_006511486.2. [Q8K4Q6-1]
XP_011241120.1. XM_011242818.1. [Q8K4Q6-1]
UniGeneiMm.35749.
Mm.488747.

Genome annotation databases

EnsembliENSMUST00000034842; ENSMUSP00000034842; ENSMUSG00000032298. [Q8K4Q6-1]
ENSMUST00000186410; ENSMUSP00000141048; ENSMUSG00000032298. [Q8K4Q6-1]
ENSMUST00000190245; ENSMUSP00000139917; ENSMUSG00000032298. [Q8K4Q6-1]
GeneIDi72774.
KEGGimmu:72774.
UCSCiuc009puh.1. mouse. [Q8K4Q6-1]
uc009puk.1. mouse. [Q8K4Q6-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB079069 mRNA. Translation: BAC06477.1.
AK013322 mRNA. Translation: BAB28790.1. Frameshift.
BC043297 mRNA. Translation: AAH43297.1.
CCDSiCCDS23217.1. [Q8K4Q6-1]
RefSeqiNP_082623.1. NM_028347.2. [Q8K4Q6-1]
XP_006511548.1. XM_006511485.2. [Q8K4Q6-1]
XP_006511549.1. XM_006511486.2. [Q8K4Q6-1]
XP_011241120.1. XM_011242818.1. [Q8K4Q6-1]
UniGeneiMm.35749.
Mm.488747.

3D structure databases

ProteinModelPortaliQ8K4Q6.
SMRiQ8K4Q6. Positions 2-290.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034842.

PTM databases

PhosphoSiteiQ8K4Q6.

Proteomic databases

PRIDEiQ8K4Q6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034842; ENSMUSP00000034842; ENSMUSG00000032298. [Q8K4Q6-1]
ENSMUST00000186410; ENSMUSP00000141048; ENSMUSG00000032298. [Q8K4Q6-1]
ENSMUST00000190245; ENSMUSP00000139917; ENSMUSG00000032298. [Q8K4Q6-1]
GeneIDi72774.
KEGGimmu:72774.
UCSCiuc009puh.1. mouse. [Q8K4Q6-1]
uc009puk.1. mouse. [Q8K4Q6-2]

Organism-specific databases

CTDi79661.
MGIiMGI:1920024. Neil1.

Phylogenomic databases

eggNOGiNOG75119.
GeneTreeiENSGT00390000016671.
HOGENOMiHOG000067872.
HOVERGENiHBG052592.
InParanoidiQ8K4Q6.
KOiK10567.
OMAiCVLLEYE.
OrthoDBiEOG7H1JM2.
PhylomeDBiQ8K4Q6.
TreeFamiTF333272.

Enzyme and pathway databases

ReactomeiREACT_342323. Cleavage of the damaged pyrimidine.
REACT_359415. APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.

Miscellaneous databases

NextBioi336897.
PROiQ8K4Q6.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K4Q6.
CleanExiMM_NEIL1.
GenevisibleiQ8K4Q6. MM.

Family and domain databases

InterProiIPR015886. DNA_glyclase/AP_lyase_DNA-bd.
IPR012319. DNA_glycosylase/AP_lyase_cat.
IPR015371. Endonuclease-VIII_DNA-bd.
IPR010979. Ribosomal_S13-like_H2TH.
[Graphical view]
PfamiPF01149. Fapy_DNA_glyco. 1 hit.
PF06831. H2TH. 1 hit.
PF09292. Neil1-DNA_bind. 1 hit.
[Graphical view]
SMARTiSM00898. Fapy_DNA_glyco. 1 hit.
[Graphical view]
SUPFAMiSSF46946. SSF46946. 1 hit.
SSF81624. SSF81624. 1 hit.
PROSITEiPS51068. FPG_CAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A back-up glycosylase in Nth1 knock-out mice is a functional Nei (endonuclease VIII) homologue."
    Takao M., Kanno S., Kobayashi K., Zhang Q.-M., Yonei S., van der Horst G.T.J., Yasui A.
    J. Biol. Chem. 277:42205-42213(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    Tissue: Liver.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Embryo.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: FVB/N.
    Tissue: Mammary gland.
  4. Cited for: FUNCTION.

Entry informationi

Entry nameiNEIL1_MOUSE
AccessioniPrimary (citable) accession number: Q8K4Q6
Secondary accession number(s): Q80V58, Q9CYT9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 109 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.