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 24-JAN-2024, entry version 181. 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/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 10. 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; 9606-ENSP00000284503; -. DR PeptideAtlas; Q969S2; -. DR ProteomicsDB; 75827; -. [Q969S2-1] DR ProteomicsDB; 75828; -. [Q969S2-2] DR ProteomicsDB; 75829; -. [Q969S2-3] DR ProteomicsDB; 75830; -. [Q969S2-4] DR Pumba; Q969S2; -. DR Antibodypedia; 22115; 157 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 Ensembl; ENST00000710791.1; ENSP00000518488.1; ENSG00000292286.1. [Q969S2-1] DR Ensembl; ENST00000710792.1; ENSP00000518489.1; ENSG00000292286.1. [Q969S2-3] DR Ensembl; ENST00000710793.1; ENSP00000518490.1; ENSG00000292286.1. [Q969S2-1] DR Ensembl; ENST00000710794.1; ENSP00000518491.1; ENSG00000292286.1. [Q969S2-1] DR Ensembl; ENST00000710795.1; ENSP00000518492.1; ENSG00000292286.1. [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 AGR; HGNC:18956; -. 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; LTWWCPH; -. DR OrthoDB; 38342at2759; -. 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; 9 hits in 1155 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 165 other cell types or tissues. DR ExpressionAtlas; Q969S2; baseline and differential. 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:0005634; C:nucleus; IBA:GO_Central. 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 CDD; cd08968; MeNeil2_N; 1. DR Gene3D; 1.10.8.50; -; 1. DR InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd. DR InterPro; IPR012319; FPG_cat. DR InterPro; IPR010979; Ribosomal_uS13-like_H2TH. DR InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase. DR PANTHER; PTHR22993:SF29; ENDONUCLEASE 8-LIKE 2; 1. DR PANTHER; PTHR22993; FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE; 1. DR Pfam; PF06831; H2TH; 1. DR SMART; SM01232; H2TH; 1. DR SUPFAM; SSF46946; S13-like H2TH domain; 1. DR PROSITE; PS51068; FPG_CAT; 1. DR PROSITE; PS51066; ZF_FPG_2; 1. DR Genevisible; Q969S2; HS. 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 //