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Protein

Endonuclease 8-like 3

Gene

NEIL3

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

Functioni

DNA glycosylase which prefers single-stranded DNA (ssDNA), or partially ssDNA structures such as bubble and fork structures, to double-stranded DNA (dsDNA). In vitro, displays strong glycosylase activity towards the hydantoin lesions spiroiminodihydantoin (Sp) and guanidinohydantoin (Gh) in both ssDNA and dsDNA; also recognizes FapyA, FapyG, 5-OHU, 5-OHC, 5-OHMH, Tg and 8-oxoA lesions in ssDNA. No activity on 8-oxoG detected. Also shows weak DNA-(apurinic or apyrimidinic site) lyase activity. In vivo, appears to be the primary enzyme involved in removing Sp and Gh from ssDNA in neonatal tissues. Seems to be an important facilitator of cell proliferation in certain populations, for example neural stem/progenitor cells and tumor cells, suggesting a role in replication-associated DNA repair.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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21Schiff-base intermediate with DNA; via amino nitrogenPROSITE-ProRule annotation
Sitei2 – 21Important for monofunctional glycosylase activity
Sitei81 – 811Required for glycosylase and lyase activities
Binding sitei192 – 1921DNABy similarity
Binding sitei271 – 2711DNABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri247 – 28135FPG-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri317 – 34630RanBP2-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. bubble DNA binding Source: UniProtKB
  2. damaged DNA binding Source: InterPro
  3. DNA-(apurinic or apyrimidinic site) lyase activity Source: UniProtKB
  4. DNA N-glycosylase activity Source: UniProtKB
  5. double-stranded DNA binding Source: UniProtKB
  6. single-stranded DNA binding Source: UniProtKB
  7. zinc ion binding Source: InterPro

GO - Biological processi

  1. base-excision repair Source: UniProtKB
  2. DNA catabolic process, endonucleolytic Source: GOC
  3. 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 3 (EC:3.2.2.-, EC:4.2.99.18)
Alternative name(s):
DNA glycosylase FPG2
DNA glycosylase/AP lyase Neil3
Endonuclease VIII-like 3
Nei-like protein 3
Gene namesi
Name:NEIL3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:24573. NEIL3.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21V → P: No effect on AP lyase activity. Impairs monofunctional glycosylase activity. 2 Publications
Mutagenesisi3 – 31E → A: No effect on AP lyase activity. 1 Publication
Mutagenesisi81 – 811K → A: Loss of glycosylase and lyase activities. 1 Publication
Mutagenesisi276 – 2761C → S: Abolishes AP lyase activity. 1 Publication
Mutagenesisi279 – 2791C → S: Abolishes AP lyase activity. 1 Publication

Organism-specific databases

PharmGKBiPA134889634.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedCurated
Chaini2 – 605604Endonuclease 8-like 3PRO_0000170910Add
BLAST

Proteomic databases

MaxQBiQ8TAT5.
PaxDbiQ8TAT5.
PRIDEiQ8TAT5.

PTM databases

PhosphoSiteiQ8TAT5.

Expressioni

Tissue specificityi

Expressed in keratinocytes and embryonic fibroblasts (at protein level). Also detected in thymus, testis and fetal lung primary fibroblasts.4 Publications

Developmental stagei

Up-regulated during early S phase of the cell cycle, and sustained through G/M phase. Low expression levels in quiescent cells.1 Publication

Gene expression databases

BgeeiQ8TAT5.
CleanExiHS_NEIL3.
ExpressionAtlasiQ8TAT5. baseline and differential.
GenevestigatoriQ8TAT5.

Interactioni

Protein-protein interaction databases

BioGridi120538. 1 interaction.
STRINGi9606.ENSP00000264596.

Structurei

3D structure databases

ProteinModelPortaliQ8TAT5.
SMRiQ8TAT5. Positions 2-281.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The N-terminal region (2-281) contains the glycosylase and lyase activities.By similarity

Sequence similaritiesi

Belongs to the FPG family.PROSITE-ProRule annotation
Contains 1 FPG-type zinc finger.PROSITE-ProRule annotation
Contains 1 RanBP2-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri247 – 28135FPG-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri317 – 34630RanBP2-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0266.
GeneTreeiENSGT00730000110955.
HOGENOMiHOG000113754.
HOVERGENiHBG052594.
InParanoidiQ8TAT5.
KOiK10569.
OMAiCFFDSSV.
OrthoDBiEOG7W153D.
PhylomeDBiQ8TAT5.
TreeFamiTF331502.

Family and domain databases

InterProiIPR015886. DNA_glyclase/AP_lyase_DNA-bd.
IPR015887. DNA_glyclase_Znf_dom_DNA_BS.
IPR012319. DNA_glycosylase/AP_lyase_cat.
IPR010979. Ribosomal_S13-like_H2TH.
IPR000214. Znf_DNA_glyclase/AP_lyase.
IPR010666. Znf_GRF.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamiPF06831. H2TH. 1 hit.
PF06839. zf-GRF. 2 hits.
PF00641. zf-RanBP. 1 hit.
[Graphical view]
SMARTiSM00547. ZnF_RBZ. 1 hit.
[Graphical view]
SUPFAMiSSF46946. SSF46946. 1 hit.
SSF81624. SSF81624. 1 hit.
PROSITEiPS51068. FPG_CAT. 1 hit.
PS01242. ZF_FPG_1. 1 hit.
PS51066. ZF_FPG_2. 1 hit.
PS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8TAT5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVEGPGCTLN GEKIRARVLP GQAVTGVRGS ALRSLQGRAL RLAASTVVVS
60 70 80 90 100
PQAAALNNDS SQNVLSLFNG YVYSGVETLG KELFMYFGPK ALRIHFGMKG
110 120 130 140 150
FIMINPLEYK YKNGASPVLE VQLTKDLICF FDSSVELRNS MESQQRIRMM
160 170 180 190 200
KELDVCSPEF SFLRAESEVK KQKGRMLGDV LMDQNVLPGV GNIIKNEALF
210 220 230 240 250
DSGLHPAVKV CQLTDEQIHH LMKMIRDFSI LFYRCRKAGL ALSKHYKVYK
260 270 280 290 300
RPNCGQCHCR ITVCRFGDNN RMTYFCPHCQ KENPQHVDIC KLPTRNTIIS
310 320 330 340 350
WTSSRVDHVM DSVARKSEEH WTCVVCTLIN KPSSKACDAC LTSRPIDSVL
360 370 380 390 400
KSEENSTVFS HLMKYPCNTF GKPHTEVKIN RKTAFGTTTL VLTDFSNKSS
410 420 430 440 450
TLERKTKQNQ ILDEEFQNSP PASVCLNDIQ HPSKKTTNDI TQPSSKVNIS
460 470 480 490 500
PTISSESKLF SPAHKKPKTA QYSSPELKSC NPGYSNSELQ INMTDGPRTL
510 520 530 540 550
NPDSPRCSKH NRLCILRVVG KDGENKGRQF YACPLPREAQ CGFFEWADLS
560 570 580 590 600
FPFCNHGKRS TMKTVLKIGP NNGKNFFVCP LGKEKQCNFF QWAENGPGIK

IIPGC
Length:605
Mass (Da):67,769
Last modified:August 9, 2010 - v3
Checksum:i528B17873ABC9D89
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351L → P in BAA91860 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti38 – 381R → C.1 Publication
Corresponds to variant rs34007209 [ dbSNP | Ensembl ].
VAR_025806
Natural varianti58 – 581N → NN.1 Publication
VAR_025807
Natural varianti76 – 761V → M.1 Publication
Corresponds to variant rs34112288 [ dbSNP | Ensembl ].
VAR_025808
Natural varianti117 – 1171P → R.2 Publications
Corresponds to variant rs7689099 [ dbSNP | Ensembl ].
VAR_020590
Natural varianti172 – 1721Q → H.1 Publication
Corresponds to variant rs17064658 [ dbSNP | Ensembl ].
VAR_025809
Natural varianti286 – 2861H → R.1 Publication
Corresponds to variant rs34193982 [ dbSNP | Ensembl ].
VAR_025810
Natural varianti346 – 3461I → V.1 Publication
Corresponds to variant rs17064676 [ dbSNP | Ensembl ].
VAR_025811
Natural varianti443 – 4431P → L.4 Publications
Corresponds to variant rs13112358 [ dbSNP | Ensembl ].
VAR_020591
Natural varianti471 – 4711Q → H.4 Publications
Corresponds to variant rs13112390 [ dbSNP | Ensembl ].
VAR_025812
Natural varianti520 – 5201G → R.4 Publications
Corresponds to variant rs1876268 [ dbSNP | Ensembl ].
VAR_020592
Natural varianti547 – 5471A → S.1 Publication
Corresponds to variant rs36005630 [ dbSNP | Ensembl ].
VAR_025813
Natural varianti556 – 5561H → R.1 Publication
Corresponds to variant rs35418725 [ dbSNP | Ensembl ].
VAR_025814

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB079071 mRNA. Translation: BAC06479.1.
AK001720 mRNA. Translation: BAA91860.1.
DQ310721 Genomic DNA. Translation: ABC40719.1.
AC027627 Genomic DNA. No translation available.
BC025954 mRNA. Translation: AAH25954.1.
CCDSiCCDS3828.1.
RefSeqiNP_060718.2. NM_018248.2.
UniGeneiHs.405467.

Genome annotation databases

EnsembliENST00000264596; ENSP00000264596; ENSG00000109674.
GeneIDi55247.
KEGGihsa:55247.
UCSCiuc003iut.2. human.

Polymorphism databases

DMDMi302393810.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB079071 mRNA. Translation: BAC06479.1.
AK001720 mRNA. Translation: BAA91860.1.
DQ310721 Genomic DNA. Translation: ABC40719.1.
AC027627 Genomic DNA. No translation available.
BC025954 mRNA. Translation: AAH25954.1.
CCDSiCCDS3828.1.
RefSeqiNP_060718.2. NM_018248.2.
UniGeneiHs.405467.

3D structure databases

ProteinModelPortaliQ8TAT5.
SMRiQ8TAT5. Positions 2-281.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120538. 1 interaction.
STRINGi9606.ENSP00000264596.

PTM databases

PhosphoSiteiQ8TAT5.

Polymorphism databases

DMDMi302393810.

Proteomic databases

MaxQBiQ8TAT5.
PaxDbiQ8TAT5.
PRIDEiQ8TAT5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264596; ENSP00000264596; ENSG00000109674.
GeneIDi55247.
KEGGihsa:55247.
UCSCiuc003iut.2. human.

Organism-specific databases

CTDi55247.
GeneCardsiGC04P178230.
HGNCiHGNC:24573. NEIL3.
MIMi608934. gene.
neXtProtiNX_Q8TAT5.
PharmGKBiPA134889634.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0266.
GeneTreeiENSGT00730000110955.
HOGENOMiHOG000113754.
HOVERGENiHBG052594.
InParanoidiQ8TAT5.
KOiK10569.
OMAiCFFDSSV.
OrthoDBiEOG7W153D.
PhylomeDBiQ8TAT5.
TreeFamiTF331502.

Miscellaneous databases

GeneWikiiNEIL3_(gene).
GenomeRNAii55247.
NextBioi59296.
PROiQ8TAT5.
SOURCEiSearch...

Gene expression databases

BgeeiQ8TAT5.
CleanExiHS_NEIL3.
ExpressionAtlasiQ8TAT5. baseline and differential.
GenevestigatoriQ8TAT5.

Family and domain databases

InterProiIPR015886. DNA_glyclase/AP_lyase_DNA-bd.
IPR015887. DNA_glyclase_Znf_dom_DNA_BS.
IPR012319. DNA_glycosylase/AP_lyase_cat.
IPR010979. Ribosomal_S13-like_H2TH.
IPR000214. Znf_DNA_glyclase/AP_lyase.
IPR010666. Znf_GRF.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamiPF06831. H2TH. 1 hit.
PF06839. zf-GRF. 2 hits.
PF00641. zf-RanBP. 1 hit.
[Graphical view]
SMARTiSM00547. ZnF_RBZ. 1 hit.
[Graphical view]
SUPFAMiSSF46946. SSF46946. 1 hit.
SSF81624. SSF81624. 1 hit.
PROSITEiPS51068. FPG_CAT. 1 hit.
PS01242. ZF_FPG_1. 1 hit.
PS51066. ZF_FPG_2. 1 hit.
PS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LEU-443; HIS-471 AND ARG-520.
    Tissue: Skin.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS LEU-443; HIS-471 AND ARG-520.
  3. NIEHS SNPs program
    Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-38; ASN-58 INS; MET-76; ARG-117; HIS-172; ARG-286; VAL-346; LEU-443; HIS-471; ARG-520; SER-547 AND ARG-556.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ARG-117; LEU-443; HIS-471 AND ARG-520.
    Tissue: B-cell.
  6. "Human DNA glycosylases of the bacterial Fpg/MutM superfamily: an alternative pathway for the repair of 8-oxoguanine and other oxidation products in DNA."
    Morland I., Rolseth V., Luna L., Rognes T., Bjoeraas M., Seeberg E.
    Nucleic Acids Res. 30:4926-4936(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  7. "Hematopoietic tissue-specific expression of mouse Neil3 for endonuclease VIII-like protein."
    Torisu K., Tsuchimoto D., Ohnishi Y., Nakabeppu Y.
    J. Biochem. 138:763-772(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  8. "Expression patterns of Neil3 during embryonic brain development and neoplasia."
    Hildrestrand G.A., Neurauter C.G., Diep D.B., Castellanos C.G., Krauss S., Bjoras M., Luna L.
    BMC Neurosci. 10:45-45(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  9. "Human Nei-like protein NEIL3 has AP lyase activity specific for single-stranded DNA and confers oxidative stress resistance in Escherichia coli mutant."
    Takao M., Oohata Y., Kitadokoro K., Kobayashi K., Iwai S., Yasui A., Yonei S., Zhang Q.M.
    Genes Cells 14:261-270(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF VAL-2; GLU-3; CYS-276 AND CYS-279.
  10. "Expression and purification of NEIL3, a human DNA glycosylase homolog."
    Krokeide S.Z., Bolstad N., Laerdahl J.K., Bjoras M., Luna L.
    Protein Expr. Purif. 65:160-164(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
  11. "Release from quiescence stimulates the expression of human NEIL3 under the control of the Ras dependent ERK-MAP kinase pathway."
    Neurauter C.G., Luna L., Bjoras M.
    DNA Repair 11:401-409(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  12. "Expression and purification of active mouse and human NEIL3 proteins."
    Liu M., Bandaru V., Holmes A., Averill A.M., Cannan W., Wallace S.S.
    Protein Expr. Purif. 84:130-139(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A GLYCOSYLASE, PROBABLE CLEAVAGE OF INITIATOR METHIONINE.
  13. "Human NEIL3 is mainly a monofunctional DNA glycosylase removing spiroimindiohydantoin and guanidinohydantoin."
    Krokeide S.Z., Laerdahl J.K., Salah M., Luna L., Cederkvist F.H., Fleming A.M., Burrows C.J., Dalhus B., Bjoras M.
    DNA Repair 12:1159-1164(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PROBABLE CLEAVAGE OF INITIATOR METHIONINE, MUTAGENESIS OF VAL-2 AND LYS-81.

Entry informationi

Entry nameiNEIL3_HUMAN
AccessioniPrimary (citable) accession number: Q8TAT5
Secondary accession number(s): Q2PPJ3, Q8NG51, Q9NV95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2004
Last sequence update: August 9, 2010
Last modified: January 6, 2015
This is version 107 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

Caution

Was originally thought to be inactive as a glycosylase (PMID:12200441,PMID:19121397), but recent reports (PMID:22569481, PMID:20185759) demonstrate that cleavage of the initiator methionine is essential for catalytic activity.Curated

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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. 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.