Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DNA oxidative demethylase ALKBH2

Gene

Alkbh2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

DNA-base-CH3 + 2-oxoglutarate + O2 = DNA-base + formaldehyde + succinate + CO2.

Cofactori

Fe2+Note: Binds 1 Fe2+ ion per subunit.

Enzyme regulationi

Activated by magnesium ions.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi149 – 1491Iron; catalyticPROSITE-ProRule annotation
Metal bindingi151 – 1511Iron; catalyticPROSITE-ProRule annotation
Binding sitei152 – 1521SubstrateBy similarity
Metal bindingi214 – 2141Iron; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

Iron, Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DNA oxidative demethylase ALKBH2 (EC:1.14.11.33)
Alternative name(s):
Alkylated DNA repair protein alkB homolog 2
Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2
Gene namesi
Name:Alkbh2
Synonyms:Abh2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:2141032. Alkbh2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

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.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi151 – 1511D → A: Loss of activity. 1 Publication
Mutagenesisi214 – 2141H → A: Reduces activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 239239DNA oxidative demethylase ALKBH2PRO_0000239276Add
BLAST

Proteomic databases

EPDiQ6P6J4.
MaxQBiQ6P6J4.
PaxDbiQ6P6J4.
PRIDEiQ6P6J4.

PTM databases

PhosphoSiteiQ6P6J4.

Expressioni

Tissue specificityi

Detected in liver, testis and kidney (at protein level). Detected in heart and testis.3 Publications

Gene expression databases

BgeeiQ6P6J4.
CleanExiMM_ALKBH2.
ExpressionAtlasiQ6P6J4. baseline and differential.
GenevisibleiQ6P6J4. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000056043.

Structurei

3D structure databases

ProteinModelPortaliQ6P6J4.
SMRiQ6P6J4. Positions 35-235.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini130 – 235106Fe2OG dioxygenasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni80 – 823Substrate bindingBy similarity
Regioni100 – 1023Substrate bindingBy similarity
Regioni137 – 1393Alpha-ketoglutarate bindingBy similarity
Regioni226 – 2327Alpha-ketoglutarate bindingBy similarity

Sequence similaritiesi

Belongs to the alkB family.Curated
Contains 1 Fe2OG dioxygenase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IIVX. Eukaryota.
COG3145. LUCA.
GeneTreeiENSGT00530000063618.
HOGENOMiHOG000207105.
HOVERGENiHBG080832.
InParanoidiQ6P6J4.
KOiK10859.
OMAiQATYGDT.
OrthoDBiEOG77T159.
PhylomeDBiQ6P6J4.
TreeFamiTF331732.

Family and domain databases

Gene3Di2.60.120.590. 1 hit.
InterProiIPR027450. AlkB-like.
IPR032852. ALKBH2.
IPR005123. Oxoglu/Fe-dep_dioxygenase.
[Graphical view]
PANTHERiPTHR31573. PTHR31573. 1 hit.
PfamiPF13532. 2OG-FeII_Oxy_2. 1 hit.
[Graphical view]
PROSITEiPS51471. FE2OG_OXY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6P6J4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDKFLVRPDL RDLQGGGEEP APTGGASGDL KSPDWRHLRA EGLSCDYTVL
60 70 80 90 100
FGKAEADKIF RELEQEVEYF TGALAKVQVF GKWHSVPRKQ ATYGDAGLTY
110 120 130 140 150
TFSGLTLTPK PWVPVLERVR DRVCEVTGQT FNFVLVNRYK DGCDHIGEHR
160 170 180 190 200
DDERELAPGS PIASVSFGAC RDFIFRHKDS RGKRPRRTVE VVRLQLAHGS
210 220 230
LLMMNPPTNT HWYHSLPIRK RVLAPRVNLT FRKILPTKK
Length:239
Mass (Da):27,129
Last modified:July 5, 2004 - v1
Checksum:iA38259C6B1472095
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti149 – 1491H → Q in BAC37576 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK079195 mRNA. Translation: BAC37576.1.
BC062188 mRNA. Translation: AAH62188.1.
CCDSiCCDS19559.1.
RefSeqiNP_778181.2. NM_175016.2.
XP_006530352.1. XM_006530289.2.
XP_006530353.1. XM_006530290.2.
XP_006530354.1. XM_006530291.2.
XP_006530355.1. XM_006530292.2.
UniGeneiMm.332593.

Genome annotation databases

EnsembliENSMUST00000053657; ENSMUSP00000056043; ENSMUSG00000044339.
ENSMUST00000112279; ENSMUSP00000107898; ENSMUSG00000044339.
GeneIDi231642.
KEGGimmu:231642.
UCSCiuc008yzd.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK079195 mRNA. Translation: BAC37576.1.
BC062188 mRNA. Translation: AAH62188.1.
CCDSiCCDS19559.1.
RefSeqiNP_778181.2. NM_175016.2.
XP_006530352.1. XM_006530289.2.
XP_006530353.1. XM_006530290.2.
XP_006530354.1. XM_006530291.2.
XP_006530355.1. XM_006530292.2.
UniGeneiMm.332593.

3D structure databases

ProteinModelPortaliQ6P6J4.
SMRiQ6P6J4. Positions 35-235.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000056043.

PTM databases

PhosphoSiteiQ6P6J4.

Proteomic databases

EPDiQ6P6J4.
MaxQBiQ6P6J4.
PaxDbiQ6P6J4.
PRIDEiQ6P6J4.

Protocols and materials databases

DNASUi231642.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000053657; ENSMUSP00000056043; ENSMUSG00000044339.
ENSMUST00000112279; ENSMUSP00000107898; ENSMUSG00000044339.
GeneIDi231642.
KEGGimmu:231642.
UCSCiuc008yzd.1. mouse.

Organism-specific databases

CTDi121642.
MGIiMGI:2141032. Alkbh2.

Phylogenomic databases

eggNOGiENOG410IIVX. Eukaryota.
COG3145. LUCA.
GeneTreeiENSGT00530000063618.
HOGENOMiHOG000207105.
HOVERGENiHBG080832.
InParanoidiQ6P6J4.
KOiK10859.
OMAiQATYGDT.
OrthoDBiEOG77T159.
PhylomeDBiQ6P6J4.
TreeFamiTF331732.

Miscellaneous databases

NextBioi380677.
PROiQ6P6J4.
SOURCEiSearch...

Gene expression databases

BgeeiQ6P6J4.
CleanExiMM_ALKBH2.
ExpressionAtlasiQ6P6J4. baseline and differential.
GenevisibleiQ6P6J4. MM.

Family and domain databases

Gene3Di2.60.120.590. 1 hit.
InterProiIPR027450. AlkB-like.
IPR032852. ALKBH2.
IPR005123. Oxoglu/Fe-dep_dioxygenase.
[Graphical view]
PANTHERiPTHR31573. PTHR31573. 1 hit.
PfamiPF13532. 2OG-FeII_Oxy_2. 1 hit.
[Graphical view]
PROSITEiPS51471. FE2OG_OXY. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Urinary bladder.
  2. "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].
    Tissue: Jaw.
  3. "Repair of methylation damage in DNA and RNA by mammalian AlkB homologues."
    Lee D.-H., Jin S.-G., Cai S., Chen Y., Pfeifer G.P., O'Connor T.R.
    J. Biol. Chem. 280:39448-39459(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-151 AND HIS-214, TISSUE SPECIFICITY.
  4. "Repair deficient mice reveal mABH2 as the primary oxidative demethylase for repairing 1meA and 3meC lesions in DNA."
    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.
    EMBO J. 25:2189-2198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  5. Cited for: DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiALKB2_MOUSE
AccessioniPrimary (citable) accession number: Q6P6J4
Secondary accession number(s): Q8C591
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: July 5, 2004
Last modified: March 16, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.