Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3 (EC 1.14.11.54) (Alkylated DNA repair protein alkB homolog 3) (hABH3) (DEPC-1) (Prostate cancer antigen 1)

 ALKB3_HUMAN             Reviewed;         286 AA.
Q96Q83; A6NDJ1; Q3SYI0; Q6NX57; Q96BU8;
30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
05-DEC-2018, entry version 151.
RecName: Full=Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3 {ECO:0000305};
EC=1.14.11.54 {ECO:0000269|PubMed:16858410, ECO:0000269|PubMed:22055184, ECO:0000305|PubMed:26863196};
AltName: Full=Alkylated DNA repair protein alkB homolog 3 {ECO:0000303|PubMed:12594517};
Short=hABH3 {ECO:0000303|PubMed:12594517};
AltName: Full=DEPC-1 {ECO:0000303|Ref.1};
AltName: Full=Prostate cancer antigen 1 {ECO:0000303|Ref.1};
Name=ALKBH3 {ECO:0000312|HGNC:HGNC:30141};
Synonyms=ABH3 {ECO:0000303|PubMed:12594517},
DEPC1 {ECO:0000303|Ref.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal thymus, and Prostatic carcinoma;
Tsujikawa K., Konishi N., Ono Y., Ichijou T., Sakamoto K.,
Yamamoto H.;
"Homo sapiens mRNA expressed in prostate cancer and thymus.";
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-164 AND GLU-228.
NIEHS SNPs program;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
GLU-228.
TISSUE=Lung, and PNS;
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).
[6]
FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=12486230; DOI=10.1073/pnas.262589799;
Duncan T., Trewick S.C., Koivisto P., Bates P.A., Lindahl T.,
Sedgwick B.;
"Reversal of DNA alkylation damage by two human dioxygenases.";
Proc. Natl. Acad. Sci. U.S.A. 99:16660-16665(2002).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12594517; DOI=10.1038/nature01363;
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.;
"Human and bacterial oxidative demethylases repair alkylation damage
in both RNA and DNA.";
Nature 421:859-863(2003).
[8]
FUNCTION, MUTAGENESIS OF ASP-193 AND HIS-257, 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).
[9]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17979886; DOI=10.1111/j.1582-4934.2007.00094.x;
Tsujikawa K., Koike K., Kitae K., Shinkawa A., Arima H., Suzuki T.,
Tsuchiya M., Makino Y., Furukawa T., Konishi N., Yamamoto H.;
"Expression and sub-cellular localization of human ABH family
molecules.";
J. Cell. Mol. Med. 11:1105-1116(2007).
[10]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH ASCC3, AND MUTAGENESIS
OF HIS-257.
PubMed=22055184; DOI=10.1016/j.molcel.2011.08.039;
Dango S., Mosammaparast N., Sowa M.E., Xiong L.J., Wu F., Park K.,
Rubin M., Gygi S., Harper J.W., Shi Y.;
"DNA unwinding by ASCC3 helicase is coupled to ALKBH3-dependent DNA
alkylation repair and cancer cell proliferation.";
Mol. Cell 44:373-384(2011).
[11]
FUNCTION, AND MUTAGENESIS OF ASP-193.
PubMed=26863196; DOI=10.1038/nature16998;
Dominissini D., Nachtergaele S., Moshitch-Moshkovitz S., Peer E.,
Kol N., Ben-Haim M.S., Dai Q., Di Segni A., Salmon-Divon M.,
Clark W.C., Zheng G., Pan T., Solomon O., Eyal E., Hershkovitz V.,
Han D., Dore L.C., Amariglio N., Rechavi G., He C.;
"The dynamic N(1)-methyladenosine methylome in eukaryotic messenger
RNA.";
Nature 530:441-446(2016).
[12]
FUNCTION, UBIQUITINATION, AND INTERACTION WITH OTUD4; USP7 AND USP9X.
PubMed=25944111; DOI=10.15252/embj.201490497;
Zhao Y., Majid M.C., Soll J.M., Brickner J.R., Dango S.,
Mosammaparast N.;
"Noncanonical regulation of alkylation damage resistance by the OTUD4
deubiquitinase.";
EMBO J. 34:1687-1703(2015).
[13]
FUNCTION.
PubMed=26863410; DOI=10.1038/nchembio.2040;
Li X., Xiong X., Wang K., Wang L., Shu X., Ma S., Yi C.;
"Transcriptome-wide mapping reveals reversible and dynamic N(1)-
methyladenosine methylome.";
Nat. Chem. Biol. 12:311-316(2016).
[14]
INTERACTION WITH ASCC3 AND THE ASCC COMPLEX, AND SUBCELLULAR LOCATION.
PubMed=29144457; DOI=10.1038/nature24484;
Brickner J.R., Soll J.M., Lombardi P.M., Vaagboe C.B., Mudge M.C.,
Oyeniran C., Rabe R., Jackson J., Sullender M.E., Blazosky E.,
Byrum A.K., Zhao Y., Corbett M.A., Gecz J., Field M., Vindigni A.,
Slupphaug G., Wolberger C., Mosammaparast N.;
"A ubiquitin-dependent signalling axis specific for ALKBH-mediated DNA
dealkylation repair.";
Nature 551:389-393(2017).
[15]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 70-286 IN COMPLEX WITH
ALPHA-KETOGLUTARATE AND IRON, COFACTOR, CATALYTIC ACTIVITY, FUNCTION,
IDENTIFICATION BY MASS SPECTROMETRY, HYDROXYLATION AT LEU-177, AND
OXIDATION AT LEU-177.
PubMed=16858410; DOI=10.1038/sj.emboj.7601219;
Sundheim O., Vaagboe C.B., Bjoeraas M., Sousa M.M.L., Talstad V.,
Aas P.A., Drabloes F., Krokan H.E., Tainer J.A., Slupphaug G.;
"Human ABH3 structure and key residues for oxidative demethylation to
reverse DNA/RNA damage.";
EMBO J. 25:3389-3397(2006).
-!- FUNCTION: Dioxygenase that mediates demethylation of DNA and RNA
containing 1-methyladenosine (m1A) (PubMed:12486230,
PubMed:12594517, PubMed:16174769, PubMed:26863196,
PubMed:26863410). Repairs alkylated DNA containing 1-
methyladenosine (m1A) and 3-methylcytosine (m3C) by oxidative
demethylation (PubMed:12486230, PubMed:12594517, PubMed:16174769,
PubMed:25944111). Has a strong preference for single-stranded DNA
(PubMed:12486230, PubMed:12594517, PubMed:16174769). Able to
process alkylated m3C within double-stranded regions via its
interaction with ASCC3, which promotes DNA unwinding to generate
single-stranded substrate needed for ALKBH3 (PubMed:22055184).
Also acts on RNA (PubMed:12594517, PubMed:16174769,
PubMed:26863196, PubMed:26863410, PubMed:16858410). Demethylates
N(1)-methyladenosine (m1A) RNA, an epigenetic internal
modification of messenger RNAs (mRNAs) highly enriched within 5'-
untranslated regions (UTRs) and in the vicinity of start codons
(PubMed:26863196, PubMed:26863410). Requires molecular oxygen,
alpha-ketoglutarate and iron (PubMed:22055184, PubMed:16858410).
{ECO:0000269|PubMed:12486230, ECO:0000269|PubMed:12594517,
ECO:0000269|PubMed:16174769, ECO:0000269|PubMed:16858410,
ECO:0000269|PubMed:22055184, ECO:0000269|PubMed:25944111,
ECO:0000269|PubMed:26863196, ECO:0000269|PubMed:26863410}.
-!- CATALYTIC ACTIVITY:
Reaction=2-oxoglutarate + N(1)-methyladenosine in mRNA + O2 =
adenosine in mRNA + CO2 + formaldehyde + succinate;
Xref=Rhea:RHEA:49516, Rhea:RHEA-COMP:12414, Rhea:RHEA-
COMP:12415, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031,
ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=1.14.11.54;
Evidence={ECO:0000305|PubMed:26863196};
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000269|PubMed:16858410};
Note=Binds 1 Fe(2+) ion per subunit.
{ECO:0000269|PubMed:16858410};
-!- ACTIVITY REGULATION: Activated by ascorbate.
{ECO:0000269|PubMed:12486230}.
-!- SUBUNIT: Interacts with the ASCC complex composed of ASCC1, ASCC2
and ASCC3 (PubMed:29144457, PubMed:22055184). Interacts directly
with ASCC3, and is thereby recruited to the ASCC complex
(PubMed:22055184, PubMed:29144457). Interacts with OTUD4; the
interaction is direct (PubMed:25944111). Interacts with USP7 and
USP9X (PubMed:25944111). {ECO:0000269|PubMed:22055184,
ECO:0000269|PubMed:25944111, ECO:0000269|PubMed:29144457}.
-!- INTERACTION:
Q96MA6:AK8; NbExp=3; IntAct=EBI-6658697, EBI-8466265;
O76003:GLRX3; NbExp=3; IntAct=EBI-6658697, EBI-374781;
Q08379:GOLGA2; NbExp=3; IntAct=EBI-6658697, EBI-618309;
Q13422:IKZF1; NbExp=3; IntAct=EBI-6658697, EBI-745305;
Q8TBB1:LNX1; NbExp=3; IntAct=EBI-6658697, EBI-739832;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12486230,
ECO:0000269|PubMed:12594517, ECO:0000269|PubMed:17979886,
ECO:0000269|PubMed:29144457}. Cytoplasm
{ECO:0000269|PubMed:12486230, ECO:0000269|PubMed:12594517,
ECO:0000269|PubMed:17979886}. Note=Colocalizes with ASCC2 and
ASCC3 in nuclear foci when cells have been exposed to alkylating
agents that cause DNA damage (PubMed:29144457). Predominantly
localizes to the nucleus. {ECO:0000269|PubMed:12486230,
ECO:0000269|PubMed:12594517, ECO:0000269|PubMed:17979886,
ECO:0000269|PubMed:29144457}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q96Q83-1; Sequence=Displayed;
Name=2;
IsoId=Q96Q83-2; Sequence=VSP_019125, VSP_019126, VSP_019127;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous. Detected in heart, pancreas,
skeletal muscle, thymus, testis, ovary, spleen, prostate, small
intestine, peripheral blood leukocytes, urinary bladder and colon.
{ECO:0000269|PubMed:12486230, ECO:0000269|PubMed:16174769,
ECO:0000269|PubMed:17979886}.
-!- PTM: Ubiquitinated; undergoes 'Lys-48'-linked polyubiquitination.
OTUD4 promotes USP7 and USP9X-dependent deubiquitination of 'Lys-
48'-polyubiquitinated ALKBH3 promoting the repair of alkylated DNA
lesions. {ECO:0000269|PubMed:25944111}.
-!- SIMILARITY: Belongs to the alkB family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH15155.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/depc1/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AB042029; BAB70508.1; -; mRNA.
EMBL; DQ196343; ABA27096.1; -; Genomic_DNA.
EMBL; AC087521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471064; EAW68078.1; -; Genomic_DNA.
EMBL; BC015155; AAH15155.1; ALT_INIT; mRNA.
EMBL; BC103812; AAI03813.1; -; mRNA.
EMBL; BC103813; AAI03814.1; -; mRNA.
EMBL; BC103814; AAI03815.1; -; mRNA.
EMBL; BC067257; AAH67257.1; -; mRNA.
CCDS; CCDS7906.1; -. [Q96Q83-1]
RefSeq; NP_631917.1; NM_139178.3. [Q96Q83-1]
UniGene; Hs.720708; -.
PDB; 2IUW; X-ray; 1.50 A; A=70-286.
PDBsum; 2IUW; -.
ProteinModelPortal; Q96Q83; -.
SMR; Q96Q83; -.
BioGrid; 128686; 50.
IntAct; Q96Q83; 8.
STRING; 9606.ENSP00000302232; -.
BindingDB; Q96Q83; -.
ChEMBL; CHEMBL3112376; -.
DrugBank; DB00126; Vitamin C.
iPTMnet; Q96Q83; -.
PhosphoSitePlus; Q96Q83; -.
BioMuta; ALKBH3; -.
DMDM; 74752087; -.
EPD; Q96Q83; -.
MaxQB; Q96Q83; -.
PaxDb; Q96Q83; -.
PeptideAtlas; Q96Q83; -.
PRIDE; Q96Q83; -.
ProteomicsDB; 77836; -.
ProteomicsDB; 77837; -. [Q96Q83-2]
Ensembl; ENST00000302708; ENSP00000302232; ENSG00000166199. [Q96Q83-1]
Ensembl; ENST00000530803; ENSP00000436788; ENSG00000166199. [Q96Q83-2]
GeneID; 221120; -.
KEGG; hsa:221120; -.
UCSC; uc001mxs.3; human. [Q96Q83-1]
CTD; 221120; -.
DisGeNET; 221120; -.
EuPathDB; HostDB:ENSG00000166199.12; -.
GeneCards; ALKBH3; -.
HGNC; HGNC:30141; ALKBH3.
HPA; HPA009674; -.
HPA; HPA046489; -.
MIM; 610603; gene.
neXtProt; NX_Q96Q83; -.
OpenTargets; ENSG00000166199; -.
PharmGKB; PA143485293; -.
eggNOG; ENOG410IETS; Eukaryota.
eggNOG; COG3145; LUCA.
GeneTree; ENSGT00940000157226; -.
HOGENOM; HOG000207105; -.
HOVERGEN; HBG056732; -.
InParanoid; Q96Q83; -.
KO; K10860; -.
OMA; FVFREPQ; -.
OrthoDB; EOG091G0S0P; -.
PhylomeDB; Q96Q83; -.
TreeFam; TF331732; -.
BRENDA; 1.14.11.33; 2681.
Reactome; R-HSA-112126; ALKBH3 mediated reversal of alkylation damage.
ChiTaRS; ALKBH3; human.
EvolutionaryTrace; Q96Q83; -.
GenomeRNAi; 221120; -.
PRO; PR:Q96Q83; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000166199; Expressed in 172 organ(s), highest expression level in skeletal muscle tissue.
CleanEx; HS_ALKBH3; -.
ExpressionAtlas; Q96Q83; baseline and differential.
Genevisible; Q96Q83; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0051747; F:cytosine C-5 DNA demethylase activity; IEA:Ensembl.
GO; GO:0043734; F:DNA-N1-methyladenine dioxygenase activity; IDA:UniProtKB.
GO; GO:0008198; F:ferrous iron binding; IDA:UniProtKB.
GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
GO; GO:1990930; F:RNA N1-methyladenosine dioxygenase activity; IDA:UniProtKB.
GO; GO:0008283; P:cell proliferation; IMP:UniProtKB.
GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IDA:UniProtKB.
GO; GO:0006281; P:DNA repair; IDA:UniProtKB.
GO; GO:0035552; P:oxidative single-stranded DNA demethylation; IDA:UniProtKB.
GO; GO:0035553; P:oxidative single-stranded RNA demethylation; IDA:UniProtKB.
Gene3D; 2.60.120.590; -; 1.
InterPro; IPR027450; AlkB-like.
InterPro; IPR037151; AlkB-like_sf.
InterPro; IPR032854; ALKBH3.
InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
PANTHER; PTHR31212; PTHR31212; 1.
Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
PROSITE; PS51471; FE2OG_OXY; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Dioxygenase; DNA damage; DNA repair; Hydroxylation; Iron;
Metal-binding; Nucleus; Oxidation; Oxidoreductase; Polymorphism;
Reference proteome; Ubl conjugation; Vitamin C.
CHAIN 1 286 Alpha-ketoglutarate-dependent dioxygenase
alkB homolog 3.
/FTId=PRO_0000239278.
DOMAIN 172 278 Fe2OG dioxygenase. {ECO:0000255|PROSITE-
ProRule:PRU00805}.
REGION 141 143 Substrate binding.
{ECO:0000250|UniProtKB:Q6NS38}.
REGION 179 181 Alpha-ketoglutarate binding.
{ECO:0000244|PDB:2IUW,
ECO:0000269|PubMed:16858410}.
REGION 269 275 Alpha-ketoglutarate binding.
{ECO:0000244|PDB:2IUW,
ECO:0000269|PubMed:16858410}.
METAL 191 191 Iron; catalytic. {ECO:0000244|PDB:2IUW,
ECO:0000255|PROSITE-ProRule:PRU00805,
ECO:0000269|PubMed:16858410}.
METAL 193 193 Iron; catalytic. {ECO:0000244|PDB:2IUW,
ECO:0000255|PROSITE-ProRule:PRU00805,
ECO:0000269|PubMed:16858410}.
METAL 257 257 Iron; catalytic. {ECO:0000244|PDB:2IUW,
ECO:0000255|PROSITE-ProRule:PRU00805,
ECO:0000269|PubMed:16858410}.
BINDING 115 115 Substrate.
{ECO:0000250|UniProtKB:Q6NS38}.
BINDING 194 194 Substrate.
{ECO:0000250|UniProtKB:Q6NS38}.
BINDING 275 275 Alpha-ketoglutarate.
{ECO:0000244|PDB:2IUW,
ECO:0000269|PubMed:16858410}.
MOD_RES 177 177 (4R)-5-hydroxyleucine; alternate.
{ECO:0000269|PubMed:16858410}.
MOD_RES 177 177 (4R)-5-oxoleucine; alternate.
{ECO:0000269|PubMed:16858410}.
VAR_SEQ 73 74 DR -> E (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_019125.
VAR_SEQ 125 172 ITYQQPRLTAWYGELPYTYSRITMEPNPHWHPVLRTLKNRI
EENTGHT -> SILQLTFKKSAPVSGTATAPQSCWYERPSP
PHIPGPAILTRTRLWAP (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_019126.
VAR_SEQ 173 286 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_019127.
VARIANT 164 164 R -> C (in dbSNP:rs2271815).
{ECO:0000269|Ref.2}.
/FTId=VAR_026632.
VARIANT 228 228 D -> E (in dbSNP:rs1130290).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.2}.
/FTId=VAR_026631.
MUTAGEN 122 122 R->A: Decreases activity towards ssDNA by
25%. Loss of activity towards dsDNA.
MUTAGEN 123 123 E->A: Strongly increases activity towards
dsDNA, possibly by facilitating access to
the active site.
MUTAGEN 131 131 R->A: Loss of activity.
MUTAGEN 177 177 L->A,N: Loss of activity against 1-
methyladenine.
MUTAGEN 177 177 L->E,Q: Loss of activity.
MUTAGEN 177 177 L->I: Decreases activity against 1-
methyladenine.
MUTAGEN 177 177 L->M: No effect.
MUTAGEN 179 179 N->A: Decreases activity by about 60%.
MUTAGEN 181 181 Y->A: Strong decrease of activity.
MUTAGEN 189 189 D->A: Strongly increases activity towards
dsDNA, possibly by facilitating access to
the active site.
MUTAGEN 191 191 H->A: Loss of activity.
MUTAGEN 193 193 D->A: Loss of activity.
{ECO:0000269|PubMed:16174769,
ECO:0000269|PubMed:26863196}.
MUTAGEN 257 257 H->A: Decreases activity by about 65%.
{ECO:0000269|PubMed:16174769,
ECO:0000269|PubMed:22055184}.
MUTAGEN 269 269 R->A: Strong decrease of activity.
MUTAGEN 271 271 N->A: No effect.
MUTAGEN 275 275 R->A: Loss of activity.
STRAND 69 71 {ECO:0000244|PDB:2IUW}.
STRAND 74 81 {ECO:0000244|PDB:2IUW}.
STRAND 84 86 {ECO:0000244|PDB:2IUW}.
STRAND 88 93 {ECO:0000244|PDB:2IUW}.
HELIX 99 112 {ECO:0000244|PDB:2IUW}.
STRAND 119 124 {ECO:0000244|PDB:2IUW}.
STRAND 126 128 {ECO:0000244|PDB:2IUW}.
STRAND 130 137 {ECO:0000244|PDB:2IUW}.
HELIX 145 148 {ECO:0000244|PDB:2IUW}.
STRAND 151 153 {ECO:0000244|PDB:2IUW}.
HELIX 156 169 {ECO:0000244|PDB:2IUW}.
STRAND 175 181 {ECO:0000244|PDB:2IUW}.
STRAND 188 191 {ECO:0000244|PDB:2IUW}.
HELIX 196 198 {ECO:0000244|PDB:2IUW}.
STRAND 204 211 {ECO:0000244|PDB:2IUW}.
STRAND 213 219 {ECO:0000244|PDB:2IUW}.
STRAND 234 239 {ECO:0000244|PDB:2IUW}.
STRAND 244 249 {ECO:0000244|PDB:2IUW}.
HELIX 251 254 {ECO:0000244|PDB:2IUW}.
STRAND 255 259 {ECO:0000244|PDB:2IUW}.
STRAND 269 275 {ECO:0000244|PDB:2IUW}.
SEQUENCE 286 AA; 33375 MW; F6563635B1F217D7 CRC64;
MEEKRRRARV QGAWAAPVKS QAIAQPATTA KSHLHQKPGQ TWKNKEHHLS DREFVFKEPQ
QVVRRAPEPR VIDREGVYEI SLSPTGVSRV CLYPGFVDVK EADWILEQLC QDVPWKQRTG
IREDITYQQP RLTAWYGELP YTYSRITMEP NPHWHPVLRT LKNRIEENTG HTFNSLLCNL
YRNEKDSVDW HSDDEPSLGR CPIIASLSFG ATRTFEMRKK PPPEENGDYT YVERVKIPLD
HGTLLIMEGA TQADWQHRVP KEYHSREPRV NLTFRTVYPD PRGAPW


Related products :

Catalog number Product name Quantity
ALKB3_RAT Rat ELISA Kit FOR Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3 96T
ALKBH3-970H Protein: Recombinant Human Alpha-Ketoglutarate-Dependent Dioxygenase AlkB Homolog 3, His-tagged 100ug
ALKBH3-970H Protein Recombinant Human Alpha-Ketoglutarate-Dependent Dioxygenase AlkB Homolog 3, His-tagged 100ug
ALKB2_MOUSE Mouse ELISA Kit FOR Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2 96T
ALKB3_MOUSE Mouse ELISA Kit FOR Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3 96T
CSB-EL001609RA Rat Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3(ALKBH3) ELISA kit 96T
CSB-EL001609BO Bovine Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3(ALKBH3) ELISA kit 96T
CSB-EL001609HU Human Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3(ALKBH3) ELISA kit 96T
CSB-EL001608BO Bovine Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2(ALKBH2) ELISA kit 96T
CSB-EL001608HU Human Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2(ALKBH2) ELISA kit 96T
CSB-EL001609RA Rat Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3(ALKBH3) ELISA kit SpeciesRat 96T
CSB-EL001609MO Mouse Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3(ALKBH3) ELISA kit 96T
CSB-EL001608MO Mouse Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2(ALKBH2) ELISA kit 96T
CSB-EL001608BO Bovine Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2(ALKBH2) ELISA kit SpeciesBovine 96T
CSB-EL001609HU Human Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3(ALKBH3) ELISA kit SpeciesHuman 96T
CSB-EL001608HU Human Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2(ALKBH2) ELISA kit SpeciesHuman 96T
CSB-EL001609MO Mouse Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3(ALKBH3) ELISA kit SpeciesMouse 96T
CSB-EL001608MO Mouse Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2(ALKBH2) ELISA kit SpeciesMouse 96T
CSB-EL001609BO Bovine Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3(ALKBH3) ELISA kit SpeciesBovine 96T
ALKB2_BOVIN ELISA Kit FOR Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2; organism: Bovine; gene name: ALKBH2 96T
ALKB3_BOVIN ELISA Kit FOR Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3; organism: Bovine; gene name: ALKBH3 96T
ALKB8_HUMAN Human ELISA Kit FOR Alkylated DNA repair protein alkB homolog 8 96T
ALKB1_HUMAN Human ELISA Kit FOR Alkylated DNA repair protein alkB homolog 1 96T
CSB-EL001614MO Mouse Alkylated DNA repair protein alkB homolog 8(ALKBH8) ELISA kit 96T
AE59412BO Bovine Alkylated DNA repair protein alkB homolog 8 (ALKBH8) ELISA Kit 48T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur