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DNA oxidative demethylase ALKBH2 (EC 1.14.11.33) (Alkylated DNA repair protein alkB homolog 2) (Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2)

 ALKB2_MOUSE             Reviewed;         239 AA.
Q6P6J4; Q8C591;
30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
25-OCT-2017, entry version 106.
RecName: Full=DNA oxidative demethylase ALKBH2;
EC=1.14.11.33;
AltName: Full=Alkylated DNA repair protein alkB homolog 2;
AltName: Full=Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2;
Name=Alkbh2; Synonyms=Abh2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Urinary bladder;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Jaw;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION, MUTAGENESIS OF ASP-151 AND HIS-214, AND TISSUE SPECIFICITY.
PubMed=16174769; DOI=10.1074/jbc.M509881200;
Lee D.-H., Jin S.-G., Cai S., Chen Y., Pfeifer G.P., O'Connor T.R.;
"Repair of methylation damage in DNA and RNA by mammalian AlkB
homologues.";
J. Biol. Chem. 280:39448-39459(2005).
[4]
DISRUPTION PHENOTYPE, FUNCTION, ENZYME REGULATION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=16642038; DOI=10.1038/sj.emboj.7601109;
Ringvoll J., Nordstrand L.M., Vaagboe C.B., Talstad V., Reite K.,
Aas P.A., Lauritzen K.H., Liabakk N.B., Bjoerk A., Doughty R.W.,
Falnes P.O., Krokan H.E., Klungland A.;
"Repair deficient mice reveal mABH2 as the primary oxidative
demethylase for repairing 1meA and 3meC lesions in DNA.";
EMBO J. 25:2189-2198(2006).
[5]
DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, FUNCTION, AND TISSUE
SPECIFICITY.
PubMed=18519673; DOI=10.1158/0008-5472.CAN-08-0796;
Ringvoll J., Moen M.N., Nordstrand L.M., Meira L.B., Pang B.,
Bekkelund A., Dedon P.C., Bjelland S., Samson L.D., Falnes P.O.,
Klungland A.;
"AlkB homologue 2-mediated repair of ethenoadenine lesions in
mammalian DNA.";
Cancer Res. 68:4142-4149(2008).
-!- FUNCTION: Dioxygenase that repairs alkylated DNA and RNA
containing 1-methyladenine and 3-methylcytosine by oxidative
demethylation. Can also repair alkylated DNA containing 1-
ethenoadenine. Has strong preference for double-stranded DNA. Has
low efficiency with single-stranded substrates. Requires molecular
oxygen, alpha-ketoglutarate and iron.
{ECO:0000269|PubMed:16174769, ECO:0000269|PubMed:16642038,
ECO:0000269|PubMed:18519673}.
-!- CATALYTIC ACTIVITY: DNA-base-CH(3) + 2-oxoglutarate + O(2) = DNA-
base + formaldehyde + succinate + CO(2).
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Note=Binds 1 Fe(2+) ion per subunit.;
-!- ENZYME REGULATION: Activated by magnesium ions.
{ECO:0000269|PubMed:16642038}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16642038,
ECO:0000269|PubMed:18519673}.
-!- TISSUE SPECIFICITY: Detected in liver, testis and kidney (at
protein level). Detected in heart and testis.
{ECO:0000269|PubMed:16174769, ECO:0000269|PubMed:16642038,
ECO:0000269|PubMed:18519673}.
-!- DISRUPTION PHENOTYPE: No visible phenotype, and no effect on the
level of 1-ethenoadenine in genomic DNA in aging mice. In
contrast, the levels of 1-methyladenine in genomic DNA increase
over time in aging adults. {ECO:0000269|PubMed:16642038,
ECO:0000269|PubMed:18519673}.
-!- SIMILARITY: Belongs to the alkB family. {ECO:0000305}.
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EMBL; AK079195; BAC37576.1; -; mRNA.
EMBL; BC062188; AAH62188.1; -; mRNA.
CCDS; CCDS19559.1; -.
RefSeq; NP_778181.2; NM_175016.2.
RefSeq; XP_006530352.1; XM_006530289.3.
RefSeq; XP_006530353.1; XM_006530290.3.
RefSeq; XP_006530354.1; XM_006530291.2.
RefSeq; XP_006530355.1; XM_006530292.3.
UniGene; Mm.332593; -.
ProteinModelPortal; Q6P6J4; -.
SMR; Q6P6J4; -.
STRING; 10090.ENSMUSP00000056043; -.
PhosphoSitePlus; Q6P6J4; -.
MaxQB; Q6P6J4; -.
PaxDb; Q6P6J4; -.
PeptideAtlas; Q6P6J4; -.
PRIDE; Q6P6J4; -.
DNASU; 231642; -.
Ensembl; ENSMUST00000053657; ENSMUSP00000056043; ENSMUSG00000044339.
Ensembl; ENSMUST00000112279; ENSMUSP00000107898; ENSMUSG00000044339.
GeneID; 231642; -.
KEGG; mmu:231642; -.
UCSC; uc008yzd.1; mouse.
CTD; 121642; -.
MGI; MGI:2141032; Alkbh2.
eggNOG; ENOG410IIVX; Eukaryota.
eggNOG; COG3145; LUCA.
GeneTree; ENSGT00530000063618; -.
HOGENOM; HOG000207105; -.
HOVERGEN; HBG080832; -.
InParanoid; Q6P6J4; -.
KO; K10859; -.
OMA; QATYGDT; -.
OrthoDB; EOG091G0S0P; -.
PhylomeDB; Q6P6J4; -.
TreeFam; TF331732; -.
PRO; PR:Q6P6J4; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000044339; -.
CleanEx; MM_ALKBH2; -.
ExpressionAtlas; Q6P6J4; baseline and differential.
Genevisible; Q6P6J4; MM.
GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0103053; F:1-ethyladenine demethylase activity; IEA:UniProtKB-EC.
GO; GO:0051747; F:cytosine C-5 DNA demethylase activity; IDA:MGI.
GO; GO:0043734; F:DNA-N1-methyladenine dioxygenase activity; ISS:UniProtKB.
GO; GO:0008198; F:ferrous iron binding; ISS:UniProtKB.
GO; GO:0016706; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; IDA:MGI.
GO; GO:0006307; P:DNA dealkylation involved in DNA repair; ISS:UniProtKB.
GO; GO:0035511; P:oxidative DNA demethylation; ISS:UniProtKB.
Gene3D; 2.60.120.590; -; 1.
InterPro; IPR027450; AlkB-like.
InterPro; IPR037151; AlkB-like_sf.
InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
PROSITE; PS51471; FE2OG_OXY; 1.
1: Evidence at protein level;
Complete proteome; Dioxygenase; DNA damage; DNA repair; Iron;
Magnesium; Metal-binding; Nucleus; Oxidoreductase; Reference proteome.
CHAIN 1 239 DNA oxidative demethylase ALKBH2.
/FTId=PRO_0000239276.
DOMAIN 130 235 Fe2OG dioxygenase. {ECO:0000255|PROSITE-
ProRule:PRU00805}.
REGION 80 82 Substrate binding. {ECO:0000250}.
REGION 100 102 Substrate binding. {ECO:0000250}.
REGION 137 139 Alpha-ketoglutarate binding.
{ECO:0000250}.
REGION 226 232 Alpha-ketoglutarate binding.
{ECO:0000250}.
METAL 149 149 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00805}.
METAL 151 151 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00805}.
METAL 214 214 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00805}.
BINDING 152 152 Substrate. {ECO:0000250}.
MUTAGEN 151 151 D->A: Loss of activity.
{ECO:0000269|PubMed:16174769}.
MUTAGEN 214 214 H->A: Reduces activity.
{ECO:0000269|PubMed:16174769}.
CONFLICT 149 149 H -> Q (in Ref. 1; BAC37576).
{ECO:0000305}.
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


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