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Protein

Endonuclease 8-like 2

Gene

NEIL2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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.4 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

Enzyme regulationi

Acetylation of Lys-50 leads to loss of DNA nicking activity. Acetylation of Lys-154 has no effect.

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri284 – 32037FPG-typePROSITE-ProRule annotationAdd
BLAST

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, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.2.2.23. 2681.
ReactomeiREACT_2156. Cleavage of the damaged pyrimidine.
REACT_355367. APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.
REACT_702. Recognition and association of DNA glycosylase with site containing an affected pyrimidine.

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 homolog 2
Short name:
NEH2
Nei-like protein 2
Gene namesi
Name:NEIL2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:18956. NEIL2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi50 – 501K → R: Loss of glycosylase and AP lyase activity. 2 Publications
Mutagenesisi154 – 1541K → R: No effect on glycosylase and AP lyase activity. 1 Publication
Mutagenesisi291 – 2911C → S: Loss of glycosylase and AP lyase activity. 1 Publication
Mutagenesisi295 – 2951H → A: Loss of glycosylase and AP lyase activity. 1 Publication
Mutagenesisi310 – 3101R → Q: Strongly reduces strand AP lyase activity. 1 Publication
Mutagenesisi315 – 3151C → S: Loss of glycosylase and AP lyase activity. 1 Publication
Mutagenesisi318 – 3181C → S: Loss of glycosylase and AP lyase activity. 1 Publication

Organism-specific databases

PharmGKBiPA38769.

Polymorphism and mutation databases

BioMutaiNEIL2.
DMDMi56404653.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 332331Endonuclease 8-like 2PRO_0000170908Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei50 – 501N6-acetyllysine1 Publication
Modified residuei154 – 1541N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ969S2.
PaxDbiQ969S2.
PRIDEiQ969S2.

PTM databases

PhosphoSiteiQ969S2.

Expressioni

Tissue specificityi

Detected in testis, skeletal muscle, heart, brain, placenta, lung, pancreas, kidney and liver.1 Publication

Gene expression databases

BgeeiQ969S2.
CleanExiHS_NEIL2.
ExpressionAtlasiQ969S2. baseline and differential.
GenevisibleiQ969S2. HS.

Interactioni

Subunit structurei

Binds EP300.

Binary interactionsi

WithEntry#Exp.IntActNotes
MEOX1P502213EBI-10281234,EBI-2864512
RELQ048643EBI-10281234,EBI-307352
TRIM27P143733EBI-10281234,EBI-719493

Protein-protein interaction databases

BioGridi128946. 6 interactions.
IntActiQ969S2. 3 interactions.
MINTiMINT-4720021.
STRINGi9606.ENSP00000284503.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VZPmodel-A192-319[»]
ProteinModelPortaliQ969S2.
SMRiQ969S2. Positions 129-319.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The zinc-finger domain is important for DNA binding.

Sequence similaritiesi

Belongs to the FPG family.PROSITE-ProRule annotation
Contains 1 FPG-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri284 – 32037FPG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG73546.
GeneTreeiENSGT00730000110955.
HOGENOMiHOG000069913.
HOVERGENiHBG082014.
InParanoidiQ969S2.
KOiK10568.
OMAiSVRKFHH.
OrthoDBiEOG7Z69CR.
PhylomeDBiQ969S2.
TreeFamiTF331502.

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]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q969S2-1) [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
MPEGPLVRKF HHLVSPFVGQ QVVKTGGSSK KLQPASLQSL WLQDTQVHGK
60 70 80 90 100
KLFLRFDLDE EMGPPGSSPT PEPPQKEVQK EGAADPKQVG EPSGQKTLDG
110 120 130 140 150
SSRSAELVPQ GEDDSEYLER DAPAGDAGRW LRVSFGLFGS VWVNDFSRAK
160 170 180 190 200
KANKRGDWRD PSPRLVLHFG GGGFLAFYNC QLSWSSSPVV TPTCDILSEK
210 220 230 240 250
FHRGQALEAL GQAQPVCYTL LDQRYFSGLG NIIKNEALYR AGIHPLSLGS
260 270 280 290 300
VLSASRREVL VDHVVEFSTA WLQGKFQGRP QHTQVYQKEQ CPAGHQVMKE
310 320 330
AFGPEDGLQR LTWWCPQCQP QLSEEPEQCQ FS
Length:332
Mass (Da):36,826
Last modified:January 23, 2007 - v3
Checksum:i8A8E76B75ABADE6D
GO
Isoform 2 (identifier: Q969S2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     79-94: Missing.

Note: No experimental confirmation available.
Show »
Length:316
Mass (Da):35,247
Checksum:i3183DDC0C41936DC
GO
Isoform 3 (identifier: Q969S2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: Missing.

Note: No experimental confirmation available.
Show »
Length:271
Mass (Da):29,930
Checksum:iA23E2B89F5256AE6
GO
Isoform 4 (identifier: Q969S2-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     48-163: Missing.

Note: No experimental confirmation available.
Show »
Length:216
Mass (Da):24,136
Checksum:i250E84C5B5DAF3CB
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti70 – 701T → S.1 Publication
Corresponds to variant rs8191611 [ dbSNP | Ensembl ].
VAR_020585
Natural varianti103 – 1031R → Q.2 Publications
Corresponds to variant rs8191613 [ dbSNP | Ensembl ].
VAR_020586
Natural varianti103 – 1031R → W.1 Publication
Corresponds to variant rs8191612 [ dbSNP | Ensembl ].
VAR_020587
Natural varianti257 – 2571R → L.1 Publication
Corresponds to variant rs8191664 [ dbSNP | Ensembl ].
VAR_020588
Natural varianti304 – 3041P → T.1 Publication
Corresponds to variant rs8191666 [ dbSNP | Ensembl ].
VAR_020589

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6161Missing in isoform 3. 1 PublicationVSP_012208Add
BLAST
Alternative sequencei48 – 163116Missing in isoform 4. 1 PublicationVSP_043343Add
BLAST
Alternative sequencei79 – 9416Missing in isoform 2. 1 PublicationVSP_012209Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB079070 mRNA. Translation: BAC06478.1.
AK056206 mRNA. Translation: BAB71120.1.
AK097389 mRNA. Translation: BAC05030.1.
AK294224 mRNA. Translation: BAG57528.1.
BX537529 mRNA. Translation: CAD97774.1.
AY306127 Genomic DNA. Translation: AAP45052.1.
AC069185 Genomic DNA. No translation available.
BC013952 mRNA. Translation: AAH13952.1.
BC013964 mRNA. Translation: AAH13964.1.
CCDSiCCDS47802.1. [Q969S2-4]
CCDS47803.1. [Q969S2-3]
CCDS5984.1. [Q969S2-1]
RefSeqiNP_001129218.1. NM_001135746.1. [Q969S2-1]
NP_001129219.1. NM_001135747.1. [Q969S2-3]
NP_001129220.1. NM_001135748.1. [Q969S2-4]
NP_659480.1. NM_145043.2. [Q969S2-1]
XP_005272438.1. XM_005272381.1. [Q969S2-1]
XP_005272439.1. XM_005272382.1. [Q969S2-3]
XP_005272440.1. XM_005272383.1. [Q969S2-3]
UniGeneiHs.293818.

Genome annotation databases

EnsembliENST00000284503; ENSP00000284503; ENSG00000154328.
ENST00000403422; ENSP00000384070; ENSG00000154328. [Q969S2-3]
ENST00000436750; ENSP00000394023; ENSG00000154328.
ENST00000455213; ENSP00000397538; ENSG00000154328.
ENST00000528323; ENSP00000435657; ENSG00000154328. [Q969S2-4]
GeneIDi252969.
KEGGihsa:252969.
UCSCiuc003wue.2. human. [Q969S2-1]
uc011kxd.1. human. [Q969S2-4]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB079070 mRNA. Translation: BAC06478.1.
AK056206 mRNA. Translation: BAB71120.1.
AK097389 mRNA. Translation: BAC05030.1.
AK294224 mRNA. Translation: BAG57528.1.
BX537529 mRNA. Translation: CAD97774.1.
AY306127 Genomic DNA. Translation: AAP45052.1.
AC069185 Genomic DNA. No translation available.
BC013952 mRNA. Translation: AAH13952.1.
BC013964 mRNA. Translation: AAH13964.1.
CCDSiCCDS47802.1. [Q969S2-4]
CCDS47803.1. [Q969S2-3]
CCDS5984.1. [Q969S2-1]
RefSeqiNP_001129218.1. NM_001135746.1. [Q969S2-1]
NP_001129219.1. NM_001135747.1. [Q969S2-3]
NP_001129220.1. NM_001135748.1. [Q969S2-4]
NP_659480.1. NM_145043.2. [Q969S2-1]
XP_005272438.1. XM_005272381.1. [Q969S2-1]
XP_005272439.1. XM_005272382.1. [Q969S2-3]
XP_005272440.1. XM_005272383.1. [Q969S2-3]
UniGeneiHs.293818.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VZPmodel-A192-319[»]
ProteinModelPortaliQ969S2.
SMRiQ969S2. Positions 129-319.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128946. 6 interactions.
IntActiQ969S2. 3 interactions.
MINTiMINT-4720021.
STRINGi9606.ENSP00000284503.

PTM databases

PhosphoSiteiQ969S2.

Polymorphism and mutation databases

BioMutaiNEIL2.
DMDMi56404653.

Proteomic databases

MaxQBiQ969S2.
PaxDbiQ969S2.
PRIDEiQ969S2.

Protocols and materials databases

DNASUi252969.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000284503; ENSP00000284503; ENSG00000154328.
ENST00000403422; ENSP00000384070; ENSG00000154328. [Q969S2-3]
ENST00000436750; ENSP00000394023; ENSG00000154328.
ENST00000455213; ENSP00000397538; ENSG00000154328.
ENST00000528323; ENSP00000435657; ENSG00000154328. [Q969S2-4]
GeneIDi252969.
KEGGihsa:252969.
UCSCiuc003wue.2. human. [Q969S2-1]
uc011kxd.1. human. [Q969S2-4]

Organism-specific databases

CTDi252969.
GeneCardsiGC08P011627.
HGNCiHGNC:18956. NEIL2.
MIMi608933. gene.
neXtProtiNX_Q969S2.
PharmGKBiPA38769.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG73546.
GeneTreeiENSGT00730000110955.
HOGENOMiHOG000069913.
HOVERGENiHBG082014.
InParanoidiQ969S2.
KOiK10568.
OMAiSVRKFHH.
OrthoDBiEOG7Z69CR.
PhylomeDBiQ969S2.
TreeFamiTF331502.

Enzyme and pathway databases

BRENDAi3.2.2.23. 2681.
ReactomeiREACT_2156. Cleavage of the damaged pyrimidine.
REACT_355367. APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.
REACT_702. Recognition and association of DNA glycosylase with site containing an affected pyrimidine.

Miscellaneous databases

ChiTaRSiNEIL2. human.
GeneWikiiNEIL2.
GenomeRNAii252969.
NextBioi92030.
PROiQ969S2.
SOURCEiSearch...

Gene expression databases

BgeeiQ969S2.
CleanExiHS_NEIL2.
ExpressionAtlasiQ969S2. baseline and differential.
GenevisibleiQ969S2. HS.

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]
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), VARIANT GLN-103.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
    Tissue: Amygdala and Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Fetal kidney.
  4. NIEHS SNPs program
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-70; GLN-103; TRP-103; LEU-257 AND THR-304.
  5. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 1).
    Tissue: Muscle.
  7. "Identification and characterization of a novel human DNA glycosylase for repair of cytosine-derived lesions."
    Hazra T.K., Kow Y.W., Hatahet Z., Imhoff B., Boldogh I., Mokkapati S.K., Mitra S., Izumi T.
    J. Biol. Chem. 277:30417-30420(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-10, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. "Repair of oxidized bases in DNA bubble structures by human DNA glycosylases NEIL1 and NEIL2."
    Dou H., Mitra S., Hazra T.K.
    J. Biol. Chem. 278:49679-49684(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF LYS-50.
  9. "Acetylation of the human DNA glycosylase NEIL2 and inhibition of its activity."
    Bhakat K.K., Hazra T.K., Mitra S.
    Nucleic Acids Res. 32:3033-3039(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 40-57 AND 142-161, FUNCTION, MUTAGENESIS OF LYS-50 AND LYS-154, INTERACTION WITH EP300, ACETYLATION AT LYS-50 AND LYS-154.
  10. "Identification of a zinc finger domain in the human NEIL2 (Nei-like-2) protein."
    Das A., Rajagopalan L., Mathura V.S., Rigby S.J., Mitra S., Hazra T.K.
    J. Biol. Chem. 279:47132-47138(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-291; HIS-295; ARG-310; CYS-315 AND CYS-318, FUNCTION, IDENTIFICATION OF ZINC-FINGER, ZINC-BINDING, 3D-STRUCTURE MODELING OF 192-319, IDENTIFICATION BY MASS SPECTROMETRY.
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiNEIL2_HUMAN
AccessioniPrimary (citable) accession number: Q969S2
Secondary accession number(s): B4DFR7
, Q7Z3Q7, Q8N842, Q8NG52
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 121 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.