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Alkylated DNA repair protein alkB homolog 8 (EC 1.14.11.-) (Probable alpha-ketoglutarate-dependent dioxygenase ABH8) (S-adenosyl-L-methionine-dependent tRNA methyltransferase ABH8) (tRNA (carboxymethyluridine(34)-5-O)-methyltransferase ABH8) (EC 2.1.1.229)

 ALKB8_HUMAN             Reviewed;         664 AA.
Q96BT7; B1Q2M0; B4DEF6; Q8N989;
20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
20-MAY-2008, sequence version 2.
18-JUL-2018, entry version 148.
RecName: Full=Alkylated DNA repair protein alkB homolog 8;
EC=1.14.11.-;
AltName: Full=Probable alpha-ketoglutarate-dependent dioxygenase ABH8;
AltName: Full=S-adenosyl-L-methionine-dependent tRNA methyltransferase ABH8;
AltName: Full=tRNA (carboxymethyluridine(34)-5-O)-methyltransferase ABH8;
EC=2.1.1.229;
Name=ALKBH8; Synonyms=ABH8;
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), 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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
TISSUE=Brain, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Uterus;
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.
PubMed=19293182; DOI=10.1158/0008-5472.CAN-08-3530;
Shimada K., Nakamura M., Anai S., De Velasco M., Tanaka M.,
Tsujikawa K., Ouji Y., Konishi N.;
"A novel human AlkB homologue, ALKBH8, contributes to human bladder
cancer progression.";
Cancer Res. 69:3157-3164(2009).
[7]
FUNCTION, AND INTERACTION WITH TRMT112.
PubMed=20123966; DOI=10.1128/MCB.01602-09;
Songe-Moller L., van den Born E., Leihne V., Vagbo C.B.,
Kristoffersen T., Krokan H.E., Kirpekar F., Falnes P.O., Klungland A.;
"Mammalian ALKBH8 possesses tRNA methyltransferase activity required
for the biogenesis of multiple wobble uridine modifications implicated
in translational decoding.";
Mol. Cell. Biol. 30:1814-1827(2010).
[8]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH
TRMT112, INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=20308323; DOI=10.1128/MCB.01604-09;
Fu D., Brophy J.A., Chan C.T., Atmore K.A., Begley U., Paules R.S.,
Dedon P.C., Begley T.J., Samson L.D.;
"Human AlkB homolog ABH8 is a tRNA methyltransferase required for
wobble uridine modification and DNA damage survival.";
Mol. Cell. Biol. 30:2449-2459(2010).
[9]
FUNCTION, COFACTOR, AND INTERACTION WITH TRMT112.
PubMed=21285950; DOI=10.1038/ncomms1173;
van den Born E., Vagbo C.B., Songe-Moller L., Leihne V., Lien G.F.,
Leszczynska G., Malkiewicz A., Krokan H.E., Kirpekar F., Klungland A.,
Falnes P.O.;
"ALKBH8-mediated formation of a novel diastereomeric pair of wobble
nucleosides in mammalian tRNA.";
Nat. Commun. 2:172-172(2011).
[10]
STRUCTURE BY NMR OF 25-125.
RIKEN structural genomics initiative (RSGI);
"Solution structure of RNA binding domain in hypothetical protein
LOC91801.";
Submitted (NOV-2005) to the PDB data bank.
[11]
X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 25-355 IN COMPLEX WITH
ALPHA-KETOGLUTARATE; MANGANESE AND ZINC, COFACTOR, INTERACTION WITH
TRMT112, AND RNA-BINDING.
PubMed=22065580; DOI=10.1074/jbc.M111.286187;
Pastore C., Topalidou I., Forouhar F., Yan A.C., Levy M., Hunt J.F.;
"Crystal structure and RNA binding properties of the RNA recognition
motif (RRM) and AlkB domains in human AlkB homolog 8 (ABH8), an enzyme
catalyzing tRNA hypermodification.";
J. Biol. Chem. 287:2130-2143(2012).
-!- FUNCTION: Catalyzes the methylation of 5-carboxymethyl uridine to
5-methylcarboxymethyl uridine at the wobble position of the
anticodon loop in tRNA via its methyltransferase domain
(PubMed:20123966, PubMed:20308323). Catalyzes the last step in the
formation of 5-methylcarboxymethyl uridine at the wobble position
of the anticodon loop in target tRNA (PubMed:20123966,
PubMed:20308323). Has a preference for tRNA(Arg) and tRNA(Glu),
and does not bind tRNA(Lys)(PubMed:20308323). Binds tRNA and
catalyzes the iron and alpha-ketoglutarate dependent hydroxylation
of 5-methylcarboxymethyl uridine at the wobble position of the
anticodon loop in tRNA via its dioxygenase domain, giving rise to
5-(S)-methoxycarbonylhydroxymethyluridine; has a preference for
tRNA(Gly) (PubMed:21285950). Required for normal survival after
DNA damage (PubMed:20308323). May inhibit apoptosis and promote
cell survival and angiogenesis (PubMed:19293182).
{ECO:0000269|PubMed:19293182, ECO:0000269|PubMed:20123966,
ECO:0000269|PubMed:20308323, ECO:0000269|PubMed:21285950}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine +
carboxymethyluridine(34) in tRNA = S-adenosyl-L-homocysteine + 5-
(2-methoxy-2-oxoethyl)uridine(34) in tRNA.
{ECO:0000269|PubMed:20308323}.
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000269|PubMed:21285950,
ECO:0000305|PubMed:22065580};
Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000305};
-!- SUBUNIT: Interacts with TRMT112. {ECO:0000269|PubMed:20123966,
ECO:0000269|PubMed:20308323, ECO:0000269|PubMed:21285950,
ECO:0000269|PubMed:22065580}.
-!- INTERACTION:
Q9UI30:TRMT112; NbExp=5; IntAct=EBI-10825637, EBI-373326;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17979886,
ECO:0000269|PubMed:20308323}. Nucleus
{ECO:0000269|PubMed:20308323}. Note=Predominantly cytoplasmic.
{ECO:0000269|PubMed:20308323}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q96BT7-1; Sequence=Displayed;
Name=2;
IsoId=Q96BT7-2; Sequence=VSP_033927, VSP_033928;
Note=No experimental confirmation available. May be produced at
very low levels due to a premature stop codon in the mRNA,
leading to nonsense-mediated mRNA decay.;
Name=3;
IsoId=Q96BT7-3; Sequence=VSP_033925, VSP_033926;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q96BT7-4; Sequence=VSP_039159;
Note=May be due to competing donor splice site. No experimental
confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed, with highest expression in
spleen, followed by pancreas and lung.
{ECO:0000269|PubMed:17979886}.
-!- INDUCTION: Up-regulated after DNA damage. Induction is mediated
via ATM. {ECO:0000269|PubMed:20308323}.
-!- SIMILARITY: Belongs to the alkB family. {ECO:0000305}.
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EMBL; AB218768; BAG16270.1; -; mRNA.
EMBL; AK095523; BAC04566.1; -; mRNA.
EMBL; AK293603; BAG57067.1; -; mRNA.
EMBL; AK304413; BAG65244.1; -; mRNA.
EMBL; AP001823; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471065; EAW67089.1; -; Genomic_DNA.
EMBL; CH471065; EAW67090.1; -; Genomic_DNA.
EMBL; BC015183; AAH15183.1; -; mRNA.
CCDS; CCDS73376.1; -. [Q96BT7-4]
CCDS; CCDS8337.2; -. [Q96BT7-1]
RefSeq; NP_001287939.1; NM_001301010.1. [Q96BT7-4]
RefSeq; NP_620130.2; NM_138775.2. [Q96BT7-1]
UniGene; Hs.503763; -.
PDB; 2CQ2; NMR; -; A=25-125.
PDB; 3THP; X-ray; 3.20 A; A=25-355.
PDB; 3THT; X-ray; 3.01 A; A/B/C/D=25-355.
PDBsum; 2CQ2; -.
PDBsum; 3THP; -.
PDBsum; 3THT; -.
ProteinModelPortal; Q96BT7; -.
SMR; Q96BT7; -.
BioGrid; 124880; 3.
IntAct; Q96BT7; 13.
STRING; 9606.ENSP00000374219; -.
iPTMnet; Q96BT7; -.
PhosphoSitePlus; Q96BT7; -.
BioMuta; ALKBH8; -.
DMDM; 189027650; -.
EPD; Q96BT7; -.
MaxQB; Q96BT7; -.
PaxDb; Q96BT7; -.
PeptideAtlas; Q96BT7; -.
PRIDE; Q96BT7; -.
ProteomicsDB; 76112; -.
ProteomicsDB; 76113; -. [Q96BT7-2]
ProteomicsDB; 76114; -. [Q96BT7-3]
ProteomicsDB; 76115; -. [Q96BT7-4]
DNASU; 91801; -.
Ensembl; ENST00000260318; ENSP00000260318; ENSG00000137760. [Q96BT7-2]
Ensembl; ENST00000389568; ENSP00000374219; ENSG00000137760. [Q96BT7-1]
Ensembl; ENST00000417449; ENSP00000397673; ENSG00000137760. [Q96BT7-4]
Ensembl; ENST00000428149; ENSP00000415885; ENSG00000137760. [Q96BT7-1]
Ensembl; ENST00000429370; ENSP00000391225; ENSG00000137760. [Q96BT7-3]
GeneID; 91801; -.
KEGG; hsa:91801; -.
UCSC; uc009yxp.4; human. [Q96BT7-1]
CTD; 91801; -.
EuPathDB; HostDB:ENSG00000137760.14; -.
GeneCards; ALKBH8; -.
HGNC; HGNC:25189; ALKBH8.
HPA; HPA038724; -.
HPA; HPA038725; -.
HPA; HPA061514; -.
MIM; 613306; gene.
neXtProt; NX_Q96BT7; -.
OpenTargets; ENSG00000137760; -.
PharmGKB; PA143485296; -.
eggNOG; KOG1331; Eukaryota.
eggNOG; KOG4176; Eukaryota.
eggNOG; COG0500; LUCA.
eggNOG; COG3145; LUCA.
GeneTree; ENSGT00530000063536; -.
HOGENOM; HOG000007984; -.
HOVERGEN; HBG067234; -.
InParanoid; Q96BT7; -.
KO; K10770; -.
OMA; PCNCSYP; -.
OrthoDB; EOG091G03UR; -.
PhylomeDB; Q96BT7; -.
TreeFam; TF316056; -.
BioCyc; MetaCyc:ENSG00000137760-MONOMER; -.
BRENDA; 2.1.1.229; 2681.
Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol.
ChiTaRS; ALKBH8; human.
EvolutionaryTrace; Q96BT7; -.
GenomeRNAi; 91801; -.
PRO; PR:Q96BT7; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000137760; -.
CleanEx; HS_ALKBH8; -.
ExpressionAtlas; Q96BT7; baseline and differential.
Genevisible; Q96BT7; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
GO; GO:0005506; F:iron ion 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:UniProtKB.
GO; GO:0016300; F:tRNA (uracil) methyltransferase activity; IDA:UniProtKB.
GO; GO:0000049; F:tRNA binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
GO; GO:0030488; P:tRNA methylation; IDA:UniProtKB.
GO; GO:0002098; P:tRNA wobble uridine modification; IDA:UniProtKB.
CDD; cd12431; RRM_ALKBH8; 1.
Gene3D; 3.30.70.330; -; 1.
InterPro; IPR027450; AlkB-like.
InterPro; IPR015095; AlkB_hom8_N.
InterPro; IPR032863; ALKBH8.
InterPro; IPR034256; ALKBH8_RRM.
InterPro; IPR013216; Methyltransf_11.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR029063; SAM-dependent_MTases.
PANTHER; PTHR13069:SF28; PTHR13069:SF28; 1.
Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
Pfam; PF09004; DUF1891; 1.
Pfam; PF08241; Methyltransf_11; 1.
SUPFAM; SSF53335; SSF53335; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS51471; FE2OG_OXY; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Iron; Metal-binding; Methyltransferase; Multifunctional enzyme;
Nucleus; Oxidoreductase; Reference proteome; RNA-binding;
S-adenosyl-L-methionine; Transferase; Zinc.
CHAIN 1 664 Alkylated DNA repair protein alkB homolog
8.
/FTId=PRO_0000337125.
DOMAIN 43 120 RRM.
DOMAIN 220 337 Fe2OG dioxygenase. {ECO:0000255|PROSITE-
ProRule:PRU00805}.
REGION 227 229 Alpha-ketoglutarate binding.
{ECO:0000269|PubMed:22065580}.
REGION 411 664 Methyltransferase domain.
METAL 238 238 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00805, ECO:0000305}.
METAL 240 240 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00805, ECO:0000305}.
METAL 242 242 Zinc; via pros nitrogen.
{ECO:0000269|PubMed:22065580}.
METAL 292 292 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00805, ECO:0000305}.
METAL 341 341 Zinc. {ECO:0000269|PubMed:22065580}.
METAL 343 343 Zinc. {ECO:0000269|PubMed:22065580}.
METAL 349 349 Zinc. {ECO:0000269|PubMed:22065580}.
BINDING 328 328 Alpha-ketoglutarate.
{ECO:0000269|PubMed:22065580}.
BINDING 334 334 Alpha-ketoglutarate.
{ECO:0000269|PubMed:22065580}.
VAR_SEQ 1 1 M -> MFAM (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_039159.
VAR_SEQ 215 224 GYIKHKPDQM -> AEKNLEVGIH (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_033925.
VAR_SEQ 225 664 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_033926.
VAR_SEQ 234 238 GIPAH -> DCHGF (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_033927.
VAR_SEQ 239 664 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_033928.
CONFLICT 210 210 K -> R (in Ref. 2; BAC04566).
{ECO:0000305}.
STRAND 26 28 {ECO:0000244|PDB:2CQ2}.
TURN 30 34 {ECO:0000244|PDB:3THT}.
STRAND 38 40 {ECO:0000244|PDB:3THP}.
STRAND 43 48 {ECO:0000244|PDB:3THT}.
HELIX 52 54 {ECO:0000244|PDB:3THT}.
HELIX 58 66 {ECO:0000244|PDB:3THT}.
STRAND 71 75 {ECO:0000244|PDB:3THT}.
STRAND 81 89 {ECO:0000244|PDB:3THT}.
HELIX 90 99 {ECO:0000244|PDB:3THT}.
TURN 100 102 {ECO:0000244|PDB:3THT}.
STRAND 104 106 {ECO:0000244|PDB:3THT}.
STRAND 112 114 {ECO:0000244|PDB:3THT}.
STRAND 116 119 {ECO:0000244|PDB:3THT}.
STRAND 121 129 {ECO:0000244|PDB:3THT}.
STRAND 137 140 {ECO:0000244|PDB:3THT}.
HELIX 146 153 {ECO:0000244|PDB:3THT}.
STRAND 175 177 {ECO:0000244|PDB:3THT}.
HELIX 202 214 {ECO:0000244|PDB:3THT}.
STRAND 222 229 {ECO:0000244|PDB:3THT}.
STRAND 235 238 {ECO:0000244|PDB:3THT}.
TURN 242 244 {ECO:0000244|PDB:3THT}.
STRAND 249 256 {ECO:0000244|PDB:3THT}.
STRAND 258 263 {ECO:0000244|PDB:3THT}.
STRAND 269 274 {ECO:0000244|PDB:3THT}.
STRAND 278 282 {ECO:0000244|PDB:3THT}.
HELIX 285 288 {ECO:0000244|PDB:3THT}.
STRAND 290 294 {ECO:0000244|PDB:3THT}.
STRAND 298 304 {ECO:0000244|PDB:3THT}.
STRAND 307 309 {ECO:0000244|PDB:3THT}.
STRAND 315 318 {ECO:0000244|PDB:3THT}.
STRAND 320 324 {ECO:0000244|PDB:3THT}.
STRAND 328 334 {ECO:0000244|PDB:3THT}.
TURN 346 348 {ECO:0000244|PDB:3THT}.
TURN 350 355 {ECO:0000244|PDB:3THT}.
SEQUENCE 664 AA; 75208 MW; 4BE595D6757C2A43 CRC64;
MDSNHQSNYK LSKTEKKFLR KQIKAKHTLL RHEGIETVSY ATQSLVVANG GLGNGVSRNQ
LLPVLEKCGL VDALLMPPNK PYSFARYRTT EESKRAYVTL NGKEVVDDLG QKITLYLNFV
EKVQWKELRP QALPPGLMVV EEIISSEEEK MLLESVDWTE DTDNQNSQKS LKHRRVKHFG
YEFHYENNNV DKDKPLSGGL PDICESFLEK WLRKGYIKHK PDQMTINQYE PGQGIPAHID
THSAFEDEIV SLSLGSEIVM DFKHPDGIAV PVMLPRRSLL VMTGESRYLW THGITCRKFD
TVQASESLKS GIITSDVGDL TLSKRGLRTS FTFRKVRQTP CNCSYPLVCD SQRKETPPSF
PESDKEASRL EQEYVHQVYE EIAGHFSSTR HTPWPHIVEF LKALPSGSIV ADIGCGNGKY
LGINKELYMI GCDRSQNLVD ICRERQFQAF VCDALAVPVR SGSCDACISI AVIHHFATAE
RRVAALQEIV RLLRPGGKAL IYVWAMEQEY NKQKSKYLRG NRNSQGKKEE MNSDTSVQRS
LVEQMRDMGS RDSASSVPRI NDSQEGGCNS RQVSNSKLPV HVNRTSFYSQ DVLVPWHLKG
NPDKGKPVEP FGPIGSQDPS PVFHRYYHVF REGELEGACR TVSDVRILQS YYDQGNWCVI
LQKA


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26-321 TRMT11 belongs to the methyltransferase superfamily. It is a catalytic subunit of an S-adenosyl-L-methionine-dependent tRNA methyltransferase complex that mediates the methylation of the guanosine nuc 0.05 mg
26-374 METT5D1 belongs to the methyltransferase superfamily, mraW family. METT5D1 is a probable S-adenosyl-L-methionine-dependent methyltransferase. 0.05 mg
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
EIAAB44050 Homo sapiens,Human,KIAA1393,M1G-methyltransferase,TRM5,TRMT5,tRNA (guanine-N(1)-)-methyltransferase,tRNA [GM37] methyltransferase,tRNA methyltransferase 5
ALKB3_RAT Rat 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
ALKB3_MOUSE Mouse ELISA Kit FOR Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3 96T
ALKB2_MOUSE Mouse ELISA Kit FOR Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2 96T
EIAAB44052 Kiaa1393,M1G-methyltransferase,Mouse,Mus musculus,Trmt5,tRNA (guanine-N(1)-)-methyltransferase,tRNA [GM37] methyltransferase,tRNA methyltransferase 5
CSB-EL001609RA Rat Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3(ALKBH3) ELISA kit SpeciesRat 96T
CSB-EL001608HU Human Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2(ALKBH2) ELISA kit 96T
CSB-EL001608MO Mouse Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2(ALKBH2) ELISA kit 96T
CSB-EL001609MO Mouse 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-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
26-362 TRMT2B (CXorf34) is probable S-adenosyl-L-methionine-dependent methlytransferase that catalyzes the formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNA. And it may also have a role in t 0.05 mg
EIAAB44051 Bos taurus,Bovine,M1G-methyltransferase,TRMT5,tRNA (guanine-N(1)-)-methyltransferase,tRNA [GM37] methyltransferase,tRNA methyltransferase 5
CSB-EL001609MO Mouse Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3(ALKBH3) ELISA kit SpeciesMouse 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-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


 

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