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Reviewed, UniProtKB/Swiss-Prot Q6NS38 (ALKB2_HUMAN)

Last modified November 24, 2009. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2
    EC=1.14.11.-
Alternative name(s):
    Alkylated DNA repair protein alkB homolog 2
    Oxy DC1
Gene names
Name: ALKBH2
Synonyms: ABH2
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length261 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Dioxygenase that repairs alkylated DNA and RNA containing 1-methyladenine and 3-methylcytosine by oxidative demethylation. Has strong preference for double-stranded DNA. Has low efficiency with single-stranded substrates. Requires molecular oxygen, alpha-ketoglutarate and iron. Ref.3 Ref.4 Ref.5

Cofactor

Binds 1 Fe2+ ion per subunit.

Enzyme regulation

Activated by ascorbate. Ref.3

Subcellular location

Nucleus. Note: Detected in replication foci during S-phase. Ref.3 Ref.4

Tissue specificity

Detected in colon, small intestine, ovary, testis, prostate, skeletal muscle, heart, liver and urinary bladder. Ref.3 Ref.5

Sequence similarities

Belongs to the alkB family.

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Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   LigandIron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processDNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnucleoplasm Ref.3

Inferred from Experiment. Source: Reactome

   Molecular functiondamaged DNA binding Ref.3

Inferred from Experiment. Source: Reactome

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 261261Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2
PRO_0000239275

Regions

Region122 – 1243Substrate binding By similarity
Region248 – 2547Alpha-ketoglutarate binding By similarity

Sites

Metal binding1711Iron; catalytic By similarity
Metal binding1731Iron; catalytic By similarity
Metal binding2361Iron; catalytic By similarity
Binding site911Substrate By similarity
Binding site1101Substrate Potential
Binding site1591Alpha-ketoglutarate By similarity
Binding site1611Alpha-ketoglutarate By similarity
Binding site1741Substrate By similarity

Natural variations

Natural variant2031R → H: dbSNP rs33962311.
VAR_048223

Experimental info

Mutagenesis1731D → A: Loss of activity. Ref.5
Mutagenesis2361H → A: Reduced activity. Ref.5
Sequence conflict431R → G in AAV28301. Ref.1

Secondary structure

1 .......................................... 261
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q6NS38-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: A376E13F92621A01

FASTA26129,322
        10         20         30         40         50         60 
MDRFLVKGAQ GGLLRKQEEQ EPTGEEPAVL GGDKESTRKR PRREAPGNGG HSAGPSWRHI 

        70         80         90        100        110        120 
RAEGLDCSYT VLFGKAEADE IFQELEKEVE YFTGALARVQ VFGKWHSVPR KQATYGDAGL 

       130        140        150        160        170        180 
TYTFSGLTLS PKPWIPVLER IRDHVSGVTG QTFNFVLINR YKDGCDHIGE HRDDERELAP 

       190        200        210        220        230        240 
GSPIASVSFG ACRDFVFRHK DSRGKSPSRR VAVVRLPLAH GSLLMMNHPT NTHWYHSLPV 

       250        260 
RKKVLAPRVN LTFRKILLTK K

« Hide

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References

« Hide 'large scale' references
[1]"Cloning and expression of human 2OG-Fe(II) oxy DC1."
Lin Y., Xie Y., Mao Y.
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skin.
[3]"Reversal of DNA alkylation damage by two human dioxygenases."
Duncan T., Trewick S.C., Koivisto P., Bates P.A., Lindahl T., Sedgwick B.
Proc. Natl. Acad. Sci. U.S.A. 99:16660-16665(2002) [PubMed: 12486230] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[4]"Human and bacterial oxidative demethylases repair alkylation damage in both RNA and DNA."
Aas P.A., Otterlei M., Falnes P.O., Vaagboe C.B., Skorpen F., Akbari M., Sundheim O., Bjoeraas M., Slupphaug G., Seeberg E., Krokan H.E.
Nature 421:859-863(2003) [PubMed: 12594517] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[5]"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: 16174769] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASP-173 AND HIS-236, TISSUE SPECIFICITY.
[6]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AY754389 mRNA. Translation: AAV28301.1.
BC070489 mRNA. Translation: AAH70489.1.
IPIIPI00055405.
RefSeqNP_001001655.1.
NP_001138846.1.
NP_001138847.1.
UniGeneHs.191334
Hs.374458

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
3BTXX-ray2.00A56-258[»]
3BTYX-ray2.35A56-258[»]
3BTZX-ray3.00A57-258[»]
3BU0X-ray2.50A56-258[»]
3BUCX-ray2.59A56-258[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6NS38.

Proteomic databases

PRIDEQ6NS38.

Genome annotation databases

EnsemblENST00000343075; ENSP00000343021; ENSG00000189046; Homo sapiens. [Genome view]
ENST00000429722; ENSP00000398181; ENSG00000189046; Homo sapiens. [Genome view]
ENST00000435370; ENSP00000398509; ENSG00000189046; Homo sapiens. [Genome view]
GeneID121642.
KEGGhsa:121642.
UCSCuc001tnx.1. human.

Organism-specific databases

CTD121642.
GeneCardsGC12M108010.
HGNCHGNC:32487. ALKBH2.
HPACAB011198.
MIM610602. gene.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ6NS38.
HOVERGENQ6NS38.
OMAHRDDEKE
OrthoDBEOG97DD18

Enzyme and pathway databases

ReactomeREACT_216. DNA Repair.

Gene expression databases

ArrayExpressQ6NS38.
BgeeQ6NS38.
CleanExHS_ALKBH2.
GenevestigatorQ6NS38.
GermOnlineENSG00000189046. Homo sapiens.

Family and domain databases

InterProIPR005123. Oxoglutarate/Fe-dep_oxygenase.
[Graphical view]
PfamPF03171. 2OG-FeII_Oxy. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00126. Vitamin C.
NextBio80790.
SOURCESearch...

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Entry information

Entry nameALKB2_HUMAN
AccessionPrimary (citable) accession number: Q6NS38
Secondary accession number(s): Q5XLE3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: July 5, 2004
Last modified: November 24, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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Relevant documents

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents