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Q8TAT5

- NEIL3_HUMAN

UniProt

Q8TAT5 - NEIL3_HUMAN

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Protein
Endonuclease 8-like 3
Gene
NEIL3
Organism
Homo sapiens (Human)
Status
Reviewed - 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.2 Publications
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.2 Publications

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri247 – 28135FPG-type
Add
BLAST
Zinc fingeri317 – 34630RanBP2-type
Add
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. DNA catabolic process, endonucleolytic Source: GOC
  2. base-excision repair Source: UniProtKB
  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: 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 – 11Removed Inferred
Chaini2 – 605604Endonuclease 8-like 3
PRO_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

ArrayExpressiQ8TAT5.
BgeeiQ8TAT5.
CleanExiHS_NEIL3.
GenevestigatoriQ8TAT5.

Interactioni

Protein-protein interaction databases

BioGridi120538. 2 interactions.
STRINGi9606.ENSP00000264596.

Structurei

3D structure databases

ProteinModelPortaliQ8TAT5.
SMRiQ8TAT5. Positions 2-281.

Family & Domainsi

Domaini

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

Sequence similaritiesi

Belongs to the FPG family.

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0266.
HOGENOMiHOG000113754.
HOVERGENiHBG052594.
InParanoidiQ8TAT5.
KOiK10569.
OMAiICFFDSS.
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

MVEGPGCTLN GEKIRARVLP GQAVTGVRGS ALRSLQGRAL RLAASTVVVS    50
PQAAALNNDS SQNVLSLFNG YVYSGVETLG KELFMYFGPK ALRIHFGMKG 100
FIMINPLEYK YKNGASPVLE VQLTKDLICF FDSSVELRNS MESQQRIRMM 150
KELDVCSPEF SFLRAESEVK KQKGRMLGDV LMDQNVLPGV GNIIKNEALF 200
DSGLHPAVKV CQLTDEQIHH LMKMIRDFSI LFYRCRKAGL ALSKHYKVYK 250
RPNCGQCHCR ITVCRFGDNN RMTYFCPHCQ KENPQHVDIC KLPTRNTIIS 300
WTSSRVDHVM DSVARKSEEH WTCVVCTLIN KPSSKACDAC LTSRPIDSVL 350
KSEENSTVFS HLMKYPCNTF GKPHTEVKIN RKTAFGTTTL VLTDFSNKSS 400
TLERKTKQNQ ILDEEFQNSP PASVCLNDIQ HPSKKTTNDI TQPSSKVNIS 450
PTISSESKLF SPAHKKPKTA QYSSPELKSC NPGYSNSELQ INMTDGPRTL 500
NPDSPRCSKH NRLCILRVVG KDGENKGRQF YACPLPREAQ CGFFEWADLS 550
FPFCNHGKRS TMKTVLKIGP NNGKNFFVCP LGKEKQCNFF QWAENGPGIK 600
IIPGC 605
Length:605
Mass (Da):67,769
Last modified:August 10, 2010 - v3
Checksum:i528B17873ABC9D89
GO

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351L → P in BAA91860. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS3828.1.
RefSeqi NP_060718.2. NM_018248.2.
UniGenei Hs.405467.

3D structure databases

ProteinModelPortali Q8TAT5.
SMRi Q8TAT5. Positions 2-281.
ModBasei Search...

Protein-protein interaction databases

BioGridi 120538. 2 interactions.
STRINGi 9606.ENSP00000264596.

PTM databases

PhosphoSitei Q8TAT5.

Polymorphism databases

DMDMi 302393810.

Proteomic databases

MaxQBi Q8TAT5.
PaxDbi Q8TAT5.
PRIDEi Q8TAT5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264596 ; ENSP00000264596 ; ENSG00000109674 .
GeneIDi 55247.
KEGGi hsa:55247.
UCSCi uc003iut.2. human.

Organism-specific databases

CTDi 55247.
GeneCardsi GC04P178230.
HGNCi HGNC:24573. NEIL3.
MIMi 608934. gene.
neXtProti NX_Q8TAT5.
PharmGKBi PA134889634.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0266.
HOGENOMi HOG000113754.
HOVERGENi HBG052594.
InParanoidi Q8TAT5.
KOi K10569.
OMAi ICFFDSS.
OrthoDBi EOG7W153D.
PhylomeDBi Q8TAT5.
TreeFami TF331502.

Miscellaneous databases

GeneWikii NEIL3_(gene).
GenomeRNAii 55247.
NextBioi 59296.
PROi Q8TAT5.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8TAT5.
Bgeei Q8TAT5.
CleanExi HS_NEIL3.
Genevestigatori Q8TAT5.

Family and domain databases

InterProi IPR015886. 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 ]
Pfami PF06831. H2TH. 1 hit.
PF06839. zf-GRF. 2 hits.
PF00641. zf-RanBP. 1 hit.
[Graphical view ]
SMARTi SM00547. ZnF_RBZ. 1 hit.
[Graphical view ]
SUPFAMi SSF46946. SSF46946. 1 hit.
SSF81624. SSF81624. 1 hit.
PROSITEi PS51068. 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 ]
ProtoNeti Search...

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], 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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS LEU-443; HIS-471 AND ARG-520.
  3. NIEHS SNPs program
    Submitted (NOV-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(2005) [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(2004) [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(2002) [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(2005) [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(2009) [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(2009) [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(2009) [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(2012) [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(2012) [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(2013) [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 7, 2004
Last sequence update: August 10, 2010
Last modified: July 9, 2014
This is version 104 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.

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

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