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D-aminoacyl-tRNA deacylase 1 (DTD) (EC 3.1.1.96) (DNA-unwinding element-binding protein B) (DUE-B) (Gly-tRNA(Ala) deacylase) (EC 3.1.1.-) (Histidyl-tRNA synthase-related)

 DTD1_HUMAN              Reviewed;         209 AA.
Q8TEA8; A8K5X5; D3DW37; Q496D1; Q5W184; Q8WXU8; Q9BW67; Q9H464;
Q9H474;
28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
28-MAR-2003, sequence version 2.
20-JUN-2018, entry version 139.
RecName: Full=D-aminoacyl-tRNA deacylase 1 {ECO:0000250|UniProtKB:Q8IIS0};
Short=DTD;
EC=3.1.1.96 {ECO:0000250|UniProtKB:Q8IIS0};
AltName: Full=DNA-unwinding element-binding protein B {ECO:0000303|PubMed:15653697};
Short=DUE-B {ECO:0000303|PubMed:15653697};
AltName: Full=Gly-tRNA(Ala) deacylase {ECO:0000250|UniProtKB:Q8IIS0};
EC=3.1.1.- {ECO:0000250|UniProtKB:Q8IIS0};
AltName: Full=Histidyl-tRNA synthase-related;
Name=DTD1; Synonyms=C20orf88, DUEB, HARS2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Fetal brain;
PubMed=12392168; DOI=10.1023/A:1020256718720;
Meng X.X., Chen J.J., Yang Q.Q., Wang S., Chao Y., Ying K., Xie Y.,
Mao Y.;
"Cloning and identification of a novel cDNA which may be associated
with FKBP25.";
Biochem. Genet. 40:303-310(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Hepatoma;
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=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[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].
TISSUE=Brain, and Skin;
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, PHOSPHORYLATION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=15653697; DOI=10.1074/jbc.M404754200;
Casper J.M., Kemp M.G., Ghosh M., Randall G.M., Vaillant A.,
Leffak M.;
"The c-myc DNA-unwinding element-binding protein modulates the
assembly of DNA replication complexes in vitro.";
J. Biol. Chem. 280:13071-13083(2005).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND SER-205, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND SER-205, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[11]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH
CDC45 AND TOPBP1.
PubMed=20065034; DOI=10.1128/MCB.00710-09;
Chowdhury A., Liu G., Kemp M., Chen X., Katrangi N., Myers S.,
Ghosh M., Yao J., Gao Y., Bubulya P., Leffak M.;
"The DNA unwinding element binding protein DUE-B interacts with Cdc45
in preinitiation complex formation.";
Mol. Cell. Biol. 30:1495-1507(2010).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SUBUNIT, AND MAGNESIUM-BINDING
SITES.
PubMed=17264083; DOI=10.1074/jbc.M609632200;
Kemp M., Bae B., Yu J.P., Ghosh M., Leffak M., Nair S.K.;
"Structure and function of the c-myc DNA-unwinding element-binding
protein DUE-B.";
J. Biol. Chem. 282:10441-10448(2007).
-!- FUNCTION: Possible ATPase (PubMed:15653697) involved in DNA
replication, may facilitate loading of CDC45 onto pre-replication
complexes (PubMed:20065034). {ECO:0000269|PubMed:15653697,
ECO:0000269|PubMed:20065034}.
-!- FUNCTION: An aminoacyl-tRNA editing enzyme that deacylates
mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-
tRNA(Ala), protecting cells against glycine mischarging by AlaRS.
Acts via tRNA-based rather than protein-based catalysis; rejects
L-amino acids rather than detecting D-amino acids in the active
site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA
molecules, this enzyme counteracts the toxicity associated with
the formation of D-aminoacyl-tRNA entities in vivo and helps
enforce protein L-homochirality. {ECO:0000250|UniProtKB:Q8IIS0}.
-!- CATALYTIC ACTIVITY: Glycyl-tRNA(Ala) + H(2)O = glycine +
tRNA(Ala). {ECO:0000250|UniProtKB:Q8IIS0}.
-!- CATALYTIC ACTIVITY: A D-aminoacyl-tRNA + H(2)O = a D-amino acid +
tRNA. {ECO:0000250|UniProtKB:Q8IIS0}.
-!- SUBUNIT: Homodimer (PubMed15653697). Interacts with CDC45 and
TOPBP1 (PubMed:20065034). {ECO:0000269|PubMed:15653697,
ECO:0000269|PubMed:17264083, ECO:0000269|PubMed:20065034}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15653697,
ECO:0000269|PubMed:20065034}. Cytoplasm
{ECO:0000250|UniProtKB:Q8IIS0}. Note=Associated with chromatin at
some replication origins containing functional DNA-unwinding
elements (PubMed:20065034).
-!- TISSUE SPECIFICITY: Expressed in many adult and fetal tissues.
Highest levels in testis, ovary, spleen and in adult and fetal
brain. {ECO:0000269|PubMed:12392168}.
-!- DOMAIN: A Gly-cisPro motif from one monomer fits into the active
site of the other monomer to allow specific chiral rejection of L-
amino acids. {ECO:0000250|UniProtKB:Q8IIS0}.
-!- PTM: Preferentially phosphorylated in cells arrested early in S
phase (PubMed:15653697). Phosphorylation in the C-terminus weakens
the interaction with CDC45 (PubMed:20065034).
{ECO:0000269|PubMed:15653697, ECO:0000269|PubMed:20065034}.
-!- SIMILARITY: Belongs to the DTD family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB85044.1; Type=Miscellaneous discrepancy; Note=Presence of Alu-repeat DNA.; Evidence={ECO:0000305};
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EMBL; AF332356; AAL57046.1; -; mRNA.
EMBL; AK074304; BAB85044.1; ALT_SEQ; mRNA.
EMBL; AK291440; BAF84129.1; -; mRNA.
EMBL; AL121900; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL121780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471133; EAX10227.1; -; Genomic_DNA.
EMBL; BC000599; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; CH471133; EAX10228.1; -; Genomic_DNA.
EMBL; BC045167; AAH45167.1; -; mRNA.
EMBL; BC100923; AAI00924.1; -; mRNA.
EMBL; BC100924; AAI00925.1; -; mRNA.
EMBL; BC100925; AAI00926.1; -; mRNA.
CCDS; CCDS13138.1; -.
RefSeq; NP_001304972.1; NM_001318043.1.
RefSeq; NP_543010.3; NM_080820.5.
UniGene; Hs.659442; -.
PDB; 2OKV; X-ray; 2.00 A; A/B/C/D=1-209.
PDBsum; 2OKV; -.
ProteinModelPortal; Q8TEA8; -.
SMR; Q8TEA8; -.
BioGrid; 124965; 15.
IntAct; Q8TEA8; 1.
STRING; 9606.ENSP00000366672; -.
iPTMnet; Q8TEA8; -.
PhosphoSitePlus; Q8TEA8; -.
BioMuta; DTD1; -.
DMDM; 29427856; -.
EPD; Q8TEA8; -.
MaxQB; Q8TEA8; -.
PaxDb; Q8TEA8; -.
PeptideAtlas; Q8TEA8; -.
PRIDE; Q8TEA8; -.
ProteomicsDB; 74433; -.
DNASU; 92675; -.
Ensembl; ENST00000377452; ENSP00000366672; ENSG00000125821.
GeneID; 92675; -.
KEGG; hsa:92675; -.
UCSC; uc002wrf.5; human.
CTD; 92675; -.
DisGeNET; 92675; -.
EuPathDB; HostDB:ENSG00000125821.11; -.
GeneCards; DTD1; -.
HGNC; HGNC:16219; DTD1.
HPA; HPA040981; -.
HPA; HPA042653; -.
MIM; 610996; gene.
neXtProt; NX_Q8TEA8; -.
OpenTargets; ENSG00000125821; -.
PharmGKB; PA162384107; -.
eggNOG; KOG3323; Eukaryota.
eggNOG; COG1490; LUCA.
GeneTree; ENSGT00390000008298; -.
HOVERGEN; HBG039436; -.
InParanoid; Q8TEA8; -.
KO; K07560; -.
OMA; ELAQPFY; -.
PhylomeDB; Q8TEA8; -.
TreeFam; TF314886; -.
ChiTaRS; DTD1; human.
EvolutionaryTrace; Q8TEA8; -.
GenomeRNAi; 92675; -.
PRO; PR:Q8TEA8; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000125821; -.
CleanEx; HS_DTD1; -.
CleanEx; HS_HARS2; -.
ExpressionAtlas; Q8TEA8; baseline and differential.
Genevisible; Q8TEA8; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0002161; F:aminoacyl-tRNA editing activity; IBA:GO_Central.
GO; GO:0051500; F:D-tyrosyl-tRNA(Tyr) deacylase activity; IBA:GO_Central.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0006399; P:tRNA metabolic process; IBA:GO_Central.
CDD; cd00563; Dtyr_deacylase; 1.
Gene3D; 3.50.80.10; -; 1.
HAMAP; MF_00518; Deacylase_Dtd; 1.
InterPro; IPR003732; Daa-tRNA_deacyls_DTD.
InterPro; IPR023509; DTD-like_sf.
PANTHER; PTHR10472; PTHR10472; 1.
Pfam; PF02580; Tyr_Deacylase; 1.
SUPFAM; SSF69500; SSF69500; 1.
TIGRFAMs; TIGR00256; TIGR00256; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; DNA replication;
DNA-binding; Hydrolase; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; RNA-binding; tRNA-binding.
CHAIN 1 209 D-aminoacyl-tRNA deacylase 1.
/FTId=PRO_0000164626.
MOTIF 139 140 Gly-cisPro motif, important for rejection
of L-amino acids.
{ECO:0000250|UniProtKB:Q8IIS0}.
METAL 4 4 Magnesium; via carbonyl oxygen.
{ECO:0000269|PubMed:17264083}.
METAL 6 6 Magnesium. {ECO:0000269|PubMed:17264083}.
METAL 28 28 Magnesium; via carbonyl oxygen.
{ECO:0000269|PubMed:17264083}.
MOD_RES 197 197 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 204 204 Phosphoserine.
{ECO:0000250|UniProtKB:Q9DD18}.
MOD_RES 205 205 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
CONFLICT 94 94 H -> N (in Ref. 5; AAH45167).
{ECO:0000305}.
CONFLICT 134 134 H -> R (in Ref. 1; AAL57046).
{ECO:0000305}.
STRAND 2 15 {ECO:0000244|PDB:2OKV}.
STRAND 18 32 {ECO:0000244|PDB:2OKV}.
HELIX 39 51 {ECO:0000244|PDB:2OKV}.
HELIX 67 70 {ECO:0000244|PDB:2OKV}.
STRAND 73 78 {ECO:0000244|PDB:2OKV}.
HELIX 80 82 {ECO:0000244|PDB:2OKV}.
STRAND 87 90 {ECO:0000244|PDB:2OKV}.
HELIX 99 116 {ECO:0000244|PDB:2OKV}.
HELIX 119 121 {ECO:0000244|PDB:2OKV}.
STRAND 122 124 {ECO:0000244|PDB:2OKV}.
STRAND 131 146 {ECO:0000244|PDB:2OKV}.
SEQUENCE 209 AA; 23424 MW; F006ED14974ACC92 CRC64;
MKAVVQRVTR ASVTVGGEQI SAIGRGICVL LGISLEDTQK ELEHMVRKIL NLRVFEDESG
KHWSKSVMDK QYEILCVSQF TLQCVLKGNK PDFHLAMPTE QAEGFYNSFL EQLRKTYRPE
LIKDGKFGAY MQVHIQNDGP VTIELESPAP GTATSDPKQL SKLEKQQQRK EKTRAKGPSE
SSKERNTPRK EDRSASSGAE GDVSSEREP


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25-598 CARS is a class 1 aminoacyl-tRNA synthetase, cysteinyl-tRNA synthetase. Each of the twenty aminoacyl-tRNA synthetases catalyzes the aminoacylation of a specific tRNA or tRNA isoaccepting family with t 0.05 mg
29-250 CARS is a class 1 aminoacyl-tRNA synthetase, cysteinyl-tRNA synthetase. Each of the twenty aminoacyl-tRNA synthetases catalyzes the aminoacylation of a specific tRNA or tRNA isoaccepting family with t 0.05 mg
EIAAB33196 Ccdc139,Coiled-coil domain-containing protein 139,Mouse,Mus musculus,Psi55 synthase,Pus10,Putative tRNA pseudouridine synthase Pus10,tRNA pseudouridine 55 synthase,tRNA pseudouridylate synthase,tRNA-u
E1045m ELISA D5Ertd135e,Mouse,Mus musculus,O-phosphoseryl-tRNA(Sec) selenium transferase,Sec synthase,Selenocysteine synthase,Selenocysteinyl-tRNA(Sec) synthase,SepSecS,Sepsecs,Sep-tRNA Sec-tRNA synthase,UGA 96T
U1045m CLIA D5Ertd135e,Mouse,Mus musculus,O-phosphoseryl-tRNA(Sec) selenium transferase,Sec synthase,Selenocysteine synthase,Selenocysteinyl-tRNA(Sec) synthase,SepSecS,Sepsecs,Sep-tRNA Sec-tRNA synthase,UGA 96T
E1045m ELISA kit D5Ertd135e,Mouse,Mus musculus,O-phosphoseryl-tRNA(Sec) selenium transferase,Sec synthase,Selenocysteine synthase,Selenocysteinyl-tRNA(Sec) synthase,SepSecS,Sepsecs,Sep-tRNA Sec-tRNA synthas 96T
EIAAB44136 Homo sapiens,Human,PP8985,PUS1,tRNA pseudouridine synthase A, mitochondrial,tRNA pseudouridine(38-40) synthase,tRNA pseudouridylate synthase I,tRNA-uridine isomerase I
EIAAB44137 MNCb-0873,Mouse,Mus musculus,Pus1,tRNA pseudouridine synthase A, mitochondrial,tRNA pseudouridine(38-40) synthase,tRNA pseudouridylate synthase I,tRNA-uridine isomerase I
EIAAB44135 Pus1,Rat,Rattus norvegicus,tRNA pseudouridine synthase A, mitochondrial,tRNA pseudouridine(38-40) synthase,tRNA pseudouridylate synthase I,tRNA-uridine isomerase I
EIAAB32694 Homo sapiens,Human,NCRNA00117,PrdX deacylase domain-containing protein 1,PRDXDD1P,Prolyl-tRNA synthetase associated domain-containing protein 1 pseudogene,PRORSD1P,Putative prolyl-tRNA synthetase asso
26-103 Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. EPRS is a multifunctional aminoacyl-tRNA synthetase that catalyzes the aminoacylation of glutamic ac 0.05 mg
EIAAB33200 FKSG32,Homo sapiens,Human,PUS3,tRNA pseudouridine synthase 3,tRNA pseudouridylate synthase 3,tRNA-uridine isomerase 3
EIAAB33206 Homo sapiens,Human,PUSL1,tRNA pseudouridine synthase-like 1,tRNA pseudouridylate synthase-like 1,tRNA-uridine isomerase-like 1
EIAAB33197 CCDC139,Coiled-coil domain-containing protein 139,DOBI,Homo sapiens,Human,Psi55 synthase,PUS10,Putative tRNA pseudouridine synthase Pus10,tRNA pseudouridine 55 synthase,tRNA pseudouridylate synthase,t
EIAAB33205 Mouse,Mus musculus,Pusl1,tRNA pseudouridine synthase-like 1,tRNA pseudouridylate synthase-like 1,tRNA-uridine isomerase-like 1
EIAAB33198 Mouse,Mus musculus,Pus3,tRNA pseudouridine synthase 3,tRNA pseudouridylate synthase 3,tRNA-uridine isomerase 3
EIAAB33199 Bos taurus,Bovine,PUS3,tRNA pseudouridine synthase 3,tRNA pseudouridylate synthase 3,tRNA-uridine isomerase 3
25-086 Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. MARS belongs to the class I family of tRNA synthetases.Aminoacyl-tRNA synthetases are a class of enz 0.05 mg
orb90155 Human Histidyl-tRNA Synthetase protein Histidyl-tRNA Synthetase Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 55 kDa.The Histidyl-tRN 10
enz-671 Recombinant Human D-Tyrosyl-tRNA Deacylase 1 2
enz-671 Recombinant Human D-Tyrosyl-tRNA Deacylase 1 10
REN-671 Recombinant Human D-Tyrosyl-tRNA Deacylase 1 2
enz-671 Recombinant Human D-Tyrosyl-tRNA Deacylase 1 100


 

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