ALKB2_MOUSE
ID ALKB2_MOUSE Reviewed; 239 AA.
AC Q6P6J4; Q8C591;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=DNA oxidative demethylase ALKBH2;
DE EC=1.14.11.33 {ECO:0000269|PubMed:16174769, ECO:0000269|PubMed:16642038, ECO:0000269|PubMed:18519673};
DE AltName: Full=Alkylated DNA repair protein alkB homolog 2;
DE AltName: Full=Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2;
GN Name=Alkbh2; Synonyms=Abh2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Jaw;
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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-151 AND HIS-214, AND
RP TISSUE SPECIFICITY.
RX PubMed=16174769; DOI=10.1074/jbc.m509881200;
RA Lee D.-H., Jin S.-G., Cai S., Chen Y., Pfeifer G.P., O'Connor T.R.;
RT "Repair of methylation damage in DNA and RNA by mammalian AlkB
RT homologues.";
RL J. Biol. Chem. 280:39448-39459(2005).
RN [4]
RP DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16642038; DOI=10.1038/sj.emboj.7601109;
RA Ringvoll J., Nordstrand L.M., Vaagboe C.B., Talstad V., Reite K., Aas P.A.,
RA Lauritzen K.H., Liabakk N.B., Bjoerk A., Doughty R.W., Falnes P.O.,
RA Krokan H.E., Klungland A.;
RT "Repair deficient mice reveal mABH2 as the primary oxidative demethylase
RT for repairing 1meA and 3meC lesions in DNA.";
RL EMBO J. 25:2189-2198(2006).
RN [5]
RP DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=18519673; DOI=10.1158/0008-5472.can-08-0796;
RA Ringvoll J., Moen M.N., Nordstrand L.M., Meira L.B., Pang B., Bekkelund A.,
RA Dedon P.C., Bjelland S., Samson L.D., Falnes P.O., Klungland A.;
RT "AlkB homologue 2-mediated repair of ethenoadenine lesions in mammalian
RT DNA.";
RL Cancer Res. 68:4142-4149(2008).
CC -!- FUNCTION: Dioxygenase that repairs alkylated nucleic acid bases by
CC direct reversal oxidative dealkylation. Can process both double-
CC stranded (ds) and single-stranded (ss) DNA substrates, with a strong
CC preference for dsDNA (PubMed:16174769, PubMed:16642038,
CC PubMed:18519673). Uses molecular oxygen, 2-oxoglutarate and iron as
CC cofactors to oxidize the alkyl groups that are subsequently released as
CC aldehydes, regenerating the undamaged bases. Probes the base pair
CC stability, locates a weakened base pair and flips the damaged base to
CC accommodate the lesion in its active site for efficient catalysis
CC (PubMed:16174769, PubMed:16642038, PubMed:18519673) (By similarity).
CC Repairs monoalkylated bases, specifically N1-methyladenine and N3-
CC methylcytosine, as well as higher order alkyl adducts such as bases
CC modified with exocyclic bridged adducts known as etheno adducts
CC including 1,N6-ethenoadenine, 3,N4-ethenocytosine and 1,N2-
CC ethenoguanine (By similarity). Acts as a gatekeeper of genomic
CC integrity under alkylation stress. Efficiently repairs alkylated
CC lesions in ribosomal DNA (rDNA). These lesions can cause ss- and dsDNA
CC strand breaks that severely impair rDNA transcription (By similarity).
CC In a response mechanism to DNA damage, associates with PCNA at
CC replication forks to repair alkylated adducts prior to replication (By
CC similarity). {ECO:0000250|UniProtKB:Q6NS38,
CC ECO:0000269|PubMed:16174769, ECO:0000269|PubMed:16642038,
CC ECO:0000269|PubMed:18519673}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + a methylated nucleobase within DNA + O2 = a
CC nucleobase within DNA + CO2 + formaldehyde + succinate;
CC Xref=Rhea:RHEA:30299, Rhea:RHEA-COMP:12192, Rhea:RHEA-COMP:12193,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:32875,
CC ChEBI:CHEBI:64428; EC=1.14.11.33;
CC Evidence={ECO:0000269|PubMed:16174769, ECO:0000269|PubMed:16642038,
CC ECO:0000269|PubMed:18519673};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30300;
CC Evidence={ECO:0000305|PubMed:16174769, ECO:0000305|PubMed:16642038,
CC ECO:0000305|PubMed:18519673};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + an N(1)-methyl-2'-deoxyadenosine in double-
CC stranded DNA + O2 = a 2'-deoxyadenosine in double-stranded DNA + CO2
CC + formaldehyde + H(+) + succinate; Xref=Rhea:RHEA:70443, Rhea:RHEA-
CC COMP:14236, Rhea:RHEA-COMP:17897, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:90615,
CC ChEBI:CHEBI:139096; Evidence={ECO:0000269|PubMed:16642038};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70444;
CC Evidence={ECO:0000305|PubMed:16642038};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + an N(1)-methyl-2'-deoxyadenosine in single-
CC stranded DNA + O2 = a 2'-deoxyadenosine in single-stranded DNA + CO2
CC + formaldehyde + H(+) + succinate; Xref=Rhea:RHEA:70447, Rhea:RHEA-
CC COMP:17895, Rhea:RHEA-COMP:17896, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:90615,
CC ChEBI:CHEBI:139096; Evidence={ECO:0000269|PubMed:16174769};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70448;
CC Evidence={ECO:0000305|PubMed:16174769};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + an N(3)-methyl-2'-deoxycytidine in double-
CC stranded DNA + O2 = a 2'-deoxycytidine in double-stranded DNA + CO2 +
CC formaldehyde + H(+) + succinate; Xref=Rhea:RHEA:70439, Rhea:RHEA-
CC COMP:14237, Rhea:RHEA-COMP:17070, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:85452,
CC ChEBI:CHEBI:139075; Evidence={ECO:0000269|PubMed:16642038,
CC ECO:0000269|PubMed:18519673};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70440;
CC Evidence={ECO:0000305|PubMed:16642038, ECO:0000305|PubMed:18519673};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + an N(3)-methyl-2'-deoxycytidine in single-
CC stranded DNA + O2 = a 2'-deoxycytidine in single-stranded DNA + CO2 +
CC formaldehyde + H(+) + succinate; Xref=Rhea:RHEA:70435, Rhea:RHEA-
CC COMP:12846, Rhea:RHEA-COMP:17894, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:85452,
CC ChEBI:CHEBI:139075; Evidence={ECO:0000269|PubMed:16174769};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70436;
CC Evidence={ECO:0000305|PubMed:16174769};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + a 1,N(6)-etheno-2'-deoxyadenosine in double-
CC stranded DNA + H2O + O2 = a 2'-deoxyadenosine in double-stranded DNA
CC + CO2 + glyoxal + succinate; Xref=Rhea:RHEA:70463, Rhea:RHEA-
CC COMP:17897, Rhea:RHEA-COMP:17903, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:34779, ChEBI:CHEBI:90615,
CC ChEBI:CHEBI:189583; Evidence={ECO:0000269|PubMed:18519673};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70464;
CC Evidence={ECO:0000305|PubMed:18519673};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + a 1,N(6)-etheno-2'-deoxyadenosine in single-
CC stranded DNA + H2O + O2 = a 2'-deoxyadenosine in single-stranded DNA
CC + CO2 + glyoxal + succinate; Xref=Rhea:RHEA:70459, Rhea:RHEA-
CC COMP:17896, Rhea:RHEA-COMP:17904, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:34779, ChEBI:CHEBI:90615,
CC ChEBI:CHEBI:189583; Evidence={ECO:0000250|UniProtKB:Q6NS38};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70460;
CC Evidence={ECO:0000250|UniProtKB:Q6NS38};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + a 3,N(4)-etheno-2'-deoxycytidine in double-
CC stranded DNA + H2O + O2 = a 2'-deoxycytidine in double-stranded DNA +
CC CO2 + glyoxal + succinate; Xref=Rhea:RHEA:70467, Rhea:RHEA-
CC COMP:17070, Rhea:RHEA-COMP:17905, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:34779, ChEBI:CHEBI:85452,
CC ChEBI:CHEBI:189585; Evidence={ECO:0000250|UniProtKB:Q6NS38};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70468;
CC Evidence={ECO:0000250|UniProtKB:Q6NS38};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + a 3,N(4)-etheno-2'-deoxycytidine in single-
CC stranded DNA + H2O + O2 = a 2'-deoxycytidine in single-stranded DNA +
CC CO2 + glyoxal + succinate; Xref=Rhea:RHEA:70471, Rhea:RHEA-
CC COMP:12846, Rhea:RHEA-COMP:17906, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:34779, ChEBI:CHEBI:85452,
CC ChEBI:CHEBI:189585; Evidence={ECO:0000250|UniProtKB:Q6NS38};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70472;
CC Evidence={ECO:0000250|UniProtKB:Q6NS38};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + a 1,N(2)-etheno-2'-deoxyguanosine in double-
CC stranded DNA + H2O + O2 = a 2'-deoxyguanosine in double-stranded DNA
CC + CO2 + glyoxal + succinate; Xref=Rhea:RHEA:70487, Rhea:RHEA-
CC COMP:17910, Rhea:RHEA-COMP:17912, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:34779, ChEBI:CHEBI:85445,
CC ChEBI:CHEBI:189586; Evidence={ECO:0000250|UniProtKB:Q6NS38};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70488;
CC Evidence={ECO:0000250|UniProtKB:Q6NS38};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:Q6NS38,
CC ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q6NS38};
CC -!- ACTIVITY REGULATION: Activated by magnesium ions.
CC {ECO:0000269|PubMed:16642038}.
CC -!- SUBUNIT: Interacts with PCNA homotrimer; this interaction is enhanced
CC during the S-phase of the cell cycle. Interacts with nucleolar proteins
CC NCL, UBTF and NPM1. Interacts with XRCC5-XRCC6 heterodimer.
CC {ECO:0000250|UniProtKB:Q6NS38}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16642038,
CC ECO:0000269|PubMed:18519673}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q6NS38}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q6NS38}. Note=Relocates to the replication foci
CC during S-phase. {ECO:0000250|UniProtKB:Q6NS38}.
CC -!- TISSUE SPECIFICITY: Detected in liver, testis and kidney (at protein
CC level). Detected in heart and testis. {ECO:0000269|PubMed:16174769,
CC ECO:0000269|PubMed:16642038, ECO:0000269|PubMed:18519673}.
CC -!- DOMAIN: The PCNA-binding motif (AlkB homolog 2 PCNA-interacting motif,
CC APIM), mediates the colocalization of ALKBH2 with PCNA at the
CC replication foci, coordinating the repair of alkylated DNA damage with
CC DNA replication. {ECO:0000250|UniProtKB:Q6NS38}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, and no effect on the level
CC of 1-ethenoadenine in genomic DNA in aging mice. In contrast, the
CC levels of 1-methyladenine in genomic DNA increase over time in aging
CC adults. {ECO:0000269|PubMed:16642038, ECO:0000269|PubMed:18519673}.
CC -!- SIMILARITY: Belongs to the alkB family. {ECO:0000305}.
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DR EMBL; AK079195; BAC37576.1; -; mRNA.
DR EMBL; BC062188; AAH62188.1; -; mRNA.
DR CCDS; CCDS19559.1; -.
DR RefSeq; NP_778181.2; NM_175016.2.
DR RefSeq; XP_006530352.1; XM_006530289.3.
DR RefSeq; XP_006530353.1; XM_006530290.3.
DR RefSeq; XP_006530354.1; XM_006530291.2.
DR RefSeq; XP_006530355.1; XM_006530292.3.
DR AlphaFoldDB; Q6P6J4; -.
DR SMR; Q6P6J4; -.
DR STRING; 10090.ENSMUSP00000056043; -.
DR PhosphoSitePlus; Q6P6J4; -.
DR EPD; Q6P6J4; -.
DR MaxQB; Q6P6J4; -.
DR PaxDb; Q6P6J4; -.
DR PeptideAtlas; Q6P6J4; -.
DR PRIDE; Q6P6J4; -.
DR ProteomicsDB; 296096; -.
DR Antibodypedia; 4403; 145 antibodies from 30 providers.
DR DNASU; 231642; -.
DR Ensembl; ENSMUST00000053657; ENSMUSP00000056043; ENSMUSG00000044339.
DR Ensembl; ENSMUST00000112279; ENSMUSP00000107898; ENSMUSG00000044339.
DR GeneID; 231642; -.
DR KEGG; mmu:231642; -.
DR UCSC; uc008yzd.1; mouse.
DR CTD; 121642; -.
DR MGI; MGI:2141032; Alkbh2.
DR VEuPathDB; HostDB:ENSMUSG00000044339; -.
DR eggNOG; ENOG502QTDK; Eukaryota.
DR GeneTree; ENSGT00940000159009; -.
DR HOGENOM; CLU_048788_5_0_1; -.
DR InParanoid; Q6P6J4; -.
DR OMA; TQHHWQH; -.
DR OrthoDB; 1379174at2759; -.
DR PhylomeDB; Q6P6J4; -.
DR TreeFam; TF331732; -.
DR BioGRID-ORCS; 231642; 2 hits in 110 CRISPR screens.
DR PRO; PR:Q6P6J4; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q6P6J4; protein.
DR Bgee; ENSMUSG00000044339; Expressed in cleaving embryo and 120 other tissues.
DR ExpressionAtlas; Q6P6J4; baseline and differential.
DR Genevisible; Q6P6J4; MM.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IDA:MGI.
DR GO; GO:0051747; F:cytosine C-5 DNA demethylase activity; IDA:MGI.
DR GO; GO:0043734; F:DNA-N1-methyladenine dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0008198; F:ferrous iron binding; ISS:UniProtKB.
DR GO; GO:0035516; F:oxidative DNA demethylase activity; IDA:UniProtKB.
DR GO; GO:0000182; F:rDNA binding; ISO:MGI.
DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IMP:UniProtKB.
DR GO; GO:0035511; P:oxidative DNA demethylation; ISS:UniProtKB.
DR Gene3D; 2.60.120.590; -; 1.
DR InterPro; IPR027450; AlkB-like.
DR InterPro; IPR037151; AlkB-like_sf.
DR InterPro; IPR032852; ALKBH2.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR PANTHER; PTHR31573; PTHR31573; 1.
DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; DNA damage; DNA repair; Iron; Magnesium; Metal-binding;
KW Nucleus; Oxidoreductase; Reference proteome.
FT CHAIN 1..239
FT /note="DNA oxidative demethylase ALKBH2"
FT /id="PRO_0000239276"
FT DOMAIN 130..235
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 11..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 3..7
FT /note="PCNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q6NS38"
FT BINDING 80..82
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6NS38"
FT BINDING 100..102
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6NS38"
FT BINDING 137
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q6NS38"
FT BINDING 139
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q6NS38"
FT BINDING 149
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q6NS38"
FT BINDING 149
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 151
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6NS38"
FT BINDING 214
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q6NS38"
FT BINDING 214
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 226
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q6NS38"
FT BINDING 230
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q6NS38"
FT BINDING 232
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q6NS38"
FT MUTAGEN 151
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16174769"
FT MUTAGEN 214
FT /note="H->A: Reduces activity."
FT /evidence="ECO:0000269|PubMed:16174769"
FT CONFLICT 149
FT /note="H -> Q (in Ref. 1; BAC37576)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 239 AA; 27129 MW; A38259C6B1472095 CRC64;
MDKFLVRPDL RDLQGGGEEP APTGGASGDL KSPDWRHLRA EGLSCDYTVL FGKAEADKIF
RELEQEVEYF TGALAKVQVF GKWHSVPRKQ ATYGDAGLTY TFSGLTLTPK PWVPVLERVR
DRVCEVTGQT FNFVLVNRYK DGCDHIGEHR DDERELAPGS PIASVSFGAC RDFIFRHKDS
RGKRPRRTVE VVRLQLAHGS LLMMNPPTNT HWYHSLPIRK RVLAPRVNLT FRKILPTKK
