NEIL2_HUMAN
ID NEIL2_HUMAN Reviewed; 332 AA.
AC Q969S2; B4DFR7; Q7Z3Q7; Q8N842; Q8NG52;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Endonuclease 8-like 2;
DE EC=3.2.2.-;
DE EC=4.2.99.18;
DE AltName: Full=DNA glycosylase/AP lyase Neil2;
DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase Neil2;
DE AltName: Full=Endonuclease VIII-like 2;
DE AltName: Full=Nei homolog 2;
DE Short=NEH2;
DE AltName: Full=Nei-like protein 2;
GN Name=NEIL2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLN-103.
RX PubMed=12200441; DOI=10.1074/jbc.m206884200;
RA Takao M., Kanno S., Kobayashi K., Zhang Q.-M., Yonei S.,
RA van der Horst G.T.J., Yasui A.;
RT "A back-up glycosylase in Nth1 knock-out mice is a functional Nei
RT (endonuclease VIII) homologue.";
RL J. Biol. Chem. 277:42205-42213(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Amygdala, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-70; GLN-103; TRP-103;
RP LEU-257 AND THR-304.
RG NIEHS SNPs program;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 2-10, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=12097317; DOI=10.1074/jbc.c200355200;
RA Hazra T.K., Kow Y.W., Hatahet Z., Imhoff B., Boldogh I., Mokkapati S.K.,
RA Mitra S., Izumi T.;
RT "Identification and characterization of a novel human DNA glycosylase for
RT repair of cytosine-derived lesions.";
RL J. Biol. Chem. 277:30417-30420(2002).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF LYS-50.
RX PubMed=14522990; DOI=10.1074/jbc.m308658200;
RA Dou H., Mitra S., Hazra T.K.;
RT "Repair of oxidized bases in DNA bubble structures by human DNA
RT glycosylases NEIL1 and NEIL2.";
RL J. Biol. Chem. 278:49679-49684(2003).
RN [9]
RP PROTEIN SEQUENCE OF 40-57 AND 142-161, FUNCTION, MUTAGENESIS OF LYS-50 AND
RP LYS-154, INTERACTION WITH EP300, AND ACETYLATION AT LYS-50 AND LYS-154.
RX PubMed=15175427; DOI=10.1093/nar/gkh632;
RA Bhakat K.K., Hazra T.K., Mitra S.;
RT "Acetylation of the human DNA glycosylase NEIL2 and inhibition of its
RT activity.";
RL Nucleic Acids Res. 32:3033-3039(2004).
RN [10]
RP MUTAGENESIS OF CYS-291; HIS-295; ARG-310; CYS-315 AND CYS-318, FUNCTION,
RP IDENTIFICATION OF ZINC-FINGER, ZINC-BINDING, 3D-STRUCTURE MODELING OF
RP 192-319, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15339932; DOI=10.1074/jbc.m406224200;
RA Das A., Rajagopalan L., Mathura V.S., Rigby S.J., Mitra S., Hazra T.K.;
RT "Identification of a zinc finger domain in the human NEIL2 (Nei-like-2)
RT protein.";
RL J. Biol. Chem. 279:47132-47138(2004).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Involved in base excision repair of DNA damaged by oxidation
CC or by mutagenic agents. Has DNA glycosylase activity towards 5-
CC hydroxyuracil and other oxidized derivatives of cytosine with a
CC preference for mismatched double-stranded DNA (DNA bubbles). Has low or
CC no DNA glycosylase activity towards thymine glycol, 2-hydroxyadenine,
CC hypoxanthine and 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase
CC activity and introduces nicks in the DNA strand. Cleaves the DNA
CC backbone by beta-delta elimination to generate a single-strand break at
CC the site of the removed base with both 3'- and 5'-phosphates.
CC {ECO:0000269|PubMed:12097317, ECO:0000269|PubMed:14522990,
CC ECO:0000269|PubMed:15175427, ECO:0000269|PubMed:15339932}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-
CC deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-
CC dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-
CC 2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-
CC COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695,
CC ChEBI:CHEBI:167181; EC=4.2.99.18; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00392};
CC -!- ACTIVITY REGULATION: Acetylation of Lys-50 leads to loss of DNA nicking
CC activity. Acetylation of Lys-154 has no effect.
CC -!- SUBUNIT: Binds EP300.
CC -!- INTERACTION:
CC Q969S2; Q6ZTQ4: CDHR3; NbExp=3; IntAct=EBI-10281234, EBI-12143631;
CC Q969S2; O43186: CRX; NbExp=3; IntAct=EBI-10281234, EBI-748171;
CC Q969S2; Q0VD86: INCA1; NbExp=3; IntAct=EBI-10281234, EBI-6509505;
CC Q969S2; P80188: LCN2; NbExp=3; IntAct=EBI-10281234, EBI-11911016;
CC Q969S2; P50221: MEOX1; NbExp=6; IntAct=EBI-10281234, EBI-2864512;
CC Q969S2; Q02548: PAX5; NbExp=3; IntAct=EBI-10281234, EBI-296331;
CC Q969S2; Q04864: REL; NbExp=3; IntAct=EBI-10281234, EBI-307352;
CC Q969S2; Q04864-2: REL; NbExp=3; IntAct=EBI-10281234, EBI-10829018;
CC Q969S2; P14373: TRIM27; NbExp=6; IntAct=EBI-10281234, EBI-719493;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12097317}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q969S2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q969S2-2; Sequence=VSP_012209;
CC Name=3;
CC IsoId=Q969S2-3; Sequence=VSP_012208;
CC Name=4;
CC IsoId=Q969S2-4; Sequence=VSP_043343;
CC -!- TISSUE SPECIFICITY: Detected in testis, skeletal muscle, heart, brain,
CC placenta, lung, pancreas, kidney and liver.
CC {ECO:0000269|PubMed:12097317}.
CC -!- DOMAIN: The zinc-finger domain is important for DNA binding.
CC -!- SIMILARITY: Belongs to the FPG family. {ECO:0000255|PROSITE-
CC ProRule:PRU00392}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/neil2/";
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DR EMBL; AB079070; BAC06478.1; -; mRNA.
DR EMBL; AK056206; BAB71120.1; -; mRNA.
DR EMBL; AK097389; BAC05030.1; -; mRNA.
DR EMBL; AK294224; BAG57528.1; -; mRNA.
DR EMBL; BX537529; CAD97774.1; -; mRNA.
DR EMBL; AY306127; AAP45052.1; -; Genomic_DNA.
DR EMBL; AC069185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013952; AAH13952.1; -; mRNA.
DR EMBL; BC013964; AAH13964.1; -; mRNA.
DR CCDS; CCDS47802.1; -. [Q969S2-4]
DR CCDS; CCDS47803.1; -. [Q969S2-3]
DR CCDS; CCDS5984.1; -. [Q969S2-1]
DR RefSeq; NP_001129218.1; NM_001135746.1. [Q969S2-1]
DR RefSeq; NP_001129219.1; NM_001135747.1. [Q969S2-3]
DR RefSeq; NP_001129220.1; NM_001135748.1. [Q969S2-4]
DR RefSeq; NP_659480.1; NM_145043.2. [Q969S2-1]
DR RefSeq; XP_005272439.1; XM_005272382.2.
DR RefSeq; XP_005272440.1; XM_005272383.2.
DR RefSeq; XP_016868790.1; XM_017013301.1.
DR AlphaFoldDB; Q969S2; -.
DR SMR; Q969S2; -.
DR BioGRID; 128946; 22.
DR CORUM; Q969S2; -.
DR IntAct; Q969S2; 9.
DR STRING; 9606.ENSP00000284503; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB14490; Ferrous ascorbate.
DR DrugBank; DB14491; Ferrous fumarate.
DR DrugBank; DB14488; Ferrous gluconate.
DR DrugBank; DB14501; Ferrous glycine sulfate.
DR DrugBank; DB14489; Ferrous succinate.
DR DrugBank; DB01592; Iron.
DR iPTMnet; Q969S2; -.
DR PhosphoSitePlus; Q969S2; -.
DR BioMuta; NEIL2; -.
DR DMDM; 56404653; -.
DR EPD; Q969S2; -.
DR jPOST; Q969S2; -.
DR MassIVE; Q969S2; -.
DR MaxQB; Q969S2; -.
DR PaxDb; Q969S2; -.
DR PeptideAtlas; Q969S2; -.
DR PRIDE; Q969S2; -.
DR ProteomicsDB; 75827; -. [Q969S2-1]
DR ProteomicsDB; 75828; -. [Q969S2-2]
DR ProteomicsDB; 75829; -. [Q969S2-3]
DR ProteomicsDB; 75830; -. [Q969S2-4]
DR Antibodypedia; 22115; 144 antibodies from 24 providers.
DR DNASU; 252969; -.
DR Ensembl; ENST00000284503.7; ENSP00000284503.6; ENSG00000154328.16. [Q969S2-1]
DR Ensembl; ENST00000403422.7; ENSP00000384070.3; ENSG00000154328.16. [Q969S2-3]
DR Ensembl; ENST00000436750.7; ENSP00000394023.2; ENSG00000154328.16. [Q969S2-1]
DR Ensembl; ENST00000455213.6; ENSP00000397538.2; ENSG00000154328.16. [Q969S2-1]
DR Ensembl; ENST00000528323.5; ENSP00000435657.1; ENSG00000154328.16. [Q969S2-4]
DR GeneID; 252969; -.
DR KEGG; hsa:252969; -.
DR MANE-Select; ENST00000284503.7; ENSP00000284503.6; NM_145043.4; NP_659480.1.
DR UCSC; uc003wue.3; human. [Q969S2-1]
DR CTD; 252969; -.
DR DisGeNET; 252969; -.
DR GeneCards; NEIL2; -.
DR HGNC; HGNC:18956; NEIL2.
DR HPA; ENSG00000154328; Low tissue specificity.
DR MIM; 608933; gene.
DR neXtProt; NX_Q969S2; -.
DR OpenTargets; ENSG00000154328; -.
DR PharmGKB; PA38769; -.
DR VEuPathDB; HostDB:ENSG00000154328; -.
DR eggNOG; ENOG502RIIB; Eukaryota.
DR GeneTree; ENSGT00940000153230; -.
DR HOGENOM; CLU_072818_0_0_1; -.
DR InParanoid; Q969S2; -.
DR OMA; YNCQMAW; -.
DR OrthoDB; 1467835at2759; -.
DR PhylomeDB; Q969S2; -.
DR TreeFam; TF331502; -.
DR BRENDA; 3.2.2.23; 2681.
DR PathwayCommons; Q969S2; -.
DR Reactome; R-HSA-110328; Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
DR Reactome; R-HSA-110329; Cleavage of the damaged pyrimidine.
DR Reactome; R-HSA-5649702; APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.
DR SignaLink; Q969S2; -.
DR BioGRID-ORCS; 252969; 8 hits in 1079 CRISPR screens.
DR ChiTaRS; NEIL2; human.
DR GeneWiki; NEIL2; -.
DR GenomeRNAi; 252969; -.
DR Pharos; Q969S2; Tbio.
DR PRO; PR:Q969S2; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q969S2; protein.
DR Bgee; ENSG00000154328; Expressed in oviduct epithelium and 164 other tissues.
DR ExpressionAtlas; Q969S2; baseline and differential.
DR Genevisible; Q969S2; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0019104; F:DNA N-glycosylase activity; IBA:GO_Central.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
DR GO; GO:0045008; P:depyrimidination; TAS:Reactome.
DR InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR InterPro; IPR012319; FPG_cat.
DR InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
DR Pfam; PF06831; H2TH; 1.
DR SMART; SM01232; H2TH; 1.
DR SUPFAM; SSF46946; SSF46946; 1.
DR PROSITE; PS51068; FPG_CAT; 1.
DR PROSITE; PS51066; ZF_FPG_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Direct protein sequencing; DNA damage;
KW DNA repair; DNA-binding; Glycosidase; Hydrolase; Lyase; Metal-binding;
KW Multifunctional enzyme; Nucleus; Phosphoprotein; Reference proteome; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12097317"
FT CHAIN 2..332
FT /note="Endonuclease 8-like 2"
FT /id="PRO_0000170908"
FT ZN_FING 284..320
FT /note="FPG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00391"
FT REGION 59..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2
FT /note="Schiff-base intermediate with DNA"
FT /evidence="ECO:0000305"
FT ACT_SITE 3
FT /note="Proton donor"
FT /evidence="ECO:0000305"
FT ACT_SITE 50
FT /note="Proton donor; for beta-elimination activity"
FT /evidence="ECO:0000305"
FT ACT_SITE 310
FT /note="Proton donor; for delta-elimination activity"
FT /evidence="ECO:0000305"
FT BINDING 231
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT MOD_RES 50
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:15175427"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 154
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:15175427"
FT VAR_SEQ 1..61
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012208"
FT VAR_SEQ 48..163
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043343"
FT VAR_SEQ 79..94
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_012209"
FT VARIANT 70
FT /note="T -> S (in dbSNP:rs8191611)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_020585"
FT VARIANT 103
FT /note="R -> Q (in dbSNP:rs8191613)"
FT /evidence="ECO:0000269|PubMed:12200441, ECO:0000269|Ref.4"
FT /id="VAR_020586"
FT VARIANT 103
FT /note="R -> W (in dbSNP:rs8191612)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_020587"
FT VARIANT 257
FT /note="R -> L (in dbSNP:rs8191664)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_020588"
FT VARIANT 304
FT /note="P -> T (in dbSNP:rs8191666)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_020589"
FT MUTAGEN 50
FT /note="K->R: Loss of glycosylase and AP lyase activity."
FT /evidence="ECO:0000269|PubMed:14522990,
FT ECO:0000269|PubMed:15175427"
FT MUTAGEN 154
FT /note="K->R: No effect on glycosylase and AP lyase
FT activity."
FT /evidence="ECO:0000269|PubMed:15175427"
FT MUTAGEN 291
FT /note="C->S: Loss of glycosylase and AP lyase activity."
FT /evidence="ECO:0000269|PubMed:15339932"
FT MUTAGEN 295
FT /note="H->A: Loss of glycosylase and AP lyase activity."
FT /evidence="ECO:0000269|PubMed:15339932"
FT MUTAGEN 310
FT /note="R->Q: Strongly reduces strand AP lyase activity."
FT /evidence="ECO:0000269|PubMed:15339932"
FT MUTAGEN 315
FT /note="C->S: Loss of glycosylase and AP lyase activity."
FT /evidence="ECO:0000269|PubMed:15339932"
FT MUTAGEN 318
FT /note="C->S: Loss of glycosylase and AP lyase activity."
FT /evidence="ECO:0000269|PubMed:15339932"
SQ SEQUENCE 332 AA; 36826 MW; 8A8E76B75ABADE6D CRC64;
MPEGPLVRKF HHLVSPFVGQ QVVKTGGSSK KLQPASLQSL WLQDTQVHGK KLFLRFDLDE
EMGPPGSSPT PEPPQKEVQK EGAADPKQVG EPSGQKTLDG SSRSAELVPQ GEDDSEYLER
DAPAGDAGRW LRVSFGLFGS VWVNDFSRAK KANKRGDWRD PSPRLVLHFG GGGFLAFYNC
QLSWSSSPVV TPTCDILSEK FHRGQALEAL GQAQPVCYTL LDQRYFSGLG NIIKNEALYR
AGIHPLSLGS VLSASRREVL VDHVVEFSTA WLQGKFQGRP QHTQVYQKEQ CPAGHQVMKE
AFGPEDGLQR LTWWCPQCQP QLSEEPEQCQ FS
