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Bifunctional glutamate/proline--tRNA ligase (Bifunctional aminoacyl-tRNA synthetase) [Includes: Glutamate--tRNA ligase (EC 6.1.1.17) (Glutamyl-tRNA synthetase) (GluRS); Proline--tRNA ligase (EC 6.1.1.15) (Prolyl-tRNA synthetase) (ProRS)]

 SYEP_MOUSE              Reviewed;        1512 AA.
Q8CGC7; E9QKC4; Q3UFJ2; Q4VC16;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 4.
31-JAN-2018, entry version 134.
RecName: Full=Bifunctional glutamate/proline--tRNA ligase;
AltName: Full=Bifunctional aminoacyl-tRNA synthetase;
Includes:
RecName: Full=Glutamate--tRNA ligase;
EC=6.1.1.17;
AltName: Full=Glutamyl-tRNA synthetase;
Short=GluRS;
Includes:
RecName: Full=Proline--tRNA ligase;
EC=6.1.1.15 {ECO:0000250|UniProtKB:P07814};
AltName: Full=Prolyl-tRNA synthetase;
Short=ProRS;
Name=Eprs; Synonyms=Qprs;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and FVB/N; TISSUE=Eye, and Mammary tumor;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-962.
STRAIN=C57BL/6J; TISSUE=Pancreas;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 406-1512.
Knippers R.;
"M.musculus mRNA for glutamyl-tRNA synthetase.";
Submitted (JUL-1990) to the EMBL/GenBank/DDBJ databases.
[5]
SUBUNIT.
PubMed=12060739; DOI=10.1073/pnas.122110199;
Kim J.Y., Kang Y.-S., Lee J.-W., Kim H.J., Ahn Y.H., Park H.,
Ko Y.-G., Kim S.;
"p38 is essential for the assembly and stability of macromolecular
tRNA synthetase complex: implications for its physiological
significance.";
Proc. Natl. Acad. Sci. U.S.A. 99:7912-7916(2002).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
FUNCTION, PHOSPHORYLATION AT SER-999, SUBUNIT, RECONSTITUTION OF THE
GAIT COMPLEX, AND MUTAGENESIS OF SER-999.
PubMed=23071094; DOI=10.1128/MCB.01168-12;
Arif A., Chatterjee P., Moodt R.A., Fox P.L.;
"Heterotrimeric GAIT complex drives transcript-selective translation
inhibition in murine macrophages.";
Mol. Cell. Biol. 32:5046-5055(2012).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-300; LYS-788 AND LYS-861,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: Catalyzes the attachment of the cognate amino acid to
the corresponding tRNA in a two-step reaction: the amino acid is
first activated by ATP to form a covalent intermediate with AMP
and is then transferred to the acceptor end of the cognate tRNA
(By similarity). Component of the GAIT (gamma interferon-activated
inhibitor of translation) complex which mediates interferon-gamma-
induced transcript-selective translation inhibition in
inflammation processes. Upon interferon-gamma activation and
subsequent phosphorylation dissociates from the multisynthetase
complex and assembles into the GAIT complex which binds to stem
loop-containing GAIT elements in the 3'-UTR of diverse
inflammatory mRNAs (such as ceruplasmin) and suppresses their
translation (PubMed:23071094). {ECO:0000250|UniProtKB:P07814,
ECO:0000269|PubMed:23071094}.
-!- CATALYTIC ACTIVITY: ATP + L-glutamate + tRNA(Glu) = AMP +
diphosphate + L-glutamyl-tRNA(Glu).
-!- CATALYTIC ACTIVITY: ATP + L-proline + tRNA(Pro) = AMP +
diphosphate + L-prolyl-tRNA(Pro). {ECO:0000250|UniProtKB:P07814}.
-!- SUBUNIT: Homodimer (By similarity). Part of a multisubunit complex
that groups tRNA ligases for Arg (RARS), Asp (DARS), Gln (QARS),
Ile (IARS), Leu (LARS), Lys (KARS), Met (MARS) the bifunctional
ligase for Glu and Pro (EPRS) and the auxiliary subunits
AIMP1/p43, AIMP2/p38 and EEF1E1/p18 (PubMed:12060739). Forms a
linear complex that contains MARS, EEF1E1, EPRS and AIMP2 that is
at the core of the multisubunit complex. Interacts with DUS2L (By
similarity). Component of the GAIT complex; in humans the complex
assembly seems to be a two-step process in which EPRS first
associates with SYNCRIP to form a pre-GAIT complex which is
deficient in GAIT element binding (PubMed:23071094).
{ECO:0000250|UniProtKB:P07814, ECO:0000269|PubMed:12060739,
ECO:0000269|PubMed:23071094}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:P07814}.
-!- DOMAIN: The WHEP-TRS domain is involved in RNA binding.
{ECO:0000250}.
-!- PTM: Phosphorylated at Ser-999 in macrophages in a IFN-gamma-
dependent manner; the phosphorylation is involving CDK5 and is
causing release from the multisynthetase complex, association with
the GAIT complex and subsequent involvement in transcript-
selective translation inhibition. Phosphorylation at Ser-999 is
specifically required for the interaction of GAIT complex-
associated RPL13A with eIF4G (By similarity). {ECO:0000250}.
-!- SIMILARITY: In the N-terminal section; belongs to the class-I
aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 2
subfamily. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the class-II
aminoacyl-tRNA synthetase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH40802.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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EMBL; AC129195; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC131980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC040802; AAH40802.1; ALT_SEQ; mRNA.
EMBL; BC094679; AAH94679.1; -; mRNA.
EMBL; AK148463; BAE28568.1; -; mRNA.
EMBL; X54327; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS35818.1; -.
RefSeq; NP_084011.1; NM_029735.1.
UniGene; Mm.154511; -.
UniGene; Mm.490980; -.
ProteinModelPortal; Q8CGC7; -.
SMR; Q8CGC7; -.
BioGrid; 223350; 5.
IntAct; Q8CGC7; 7.
MINT; MINT-1869828; -.
STRING; 10090.ENSMUSP00000045841; -.
iPTMnet; Q8CGC7; -.
PhosphoSitePlus; Q8CGC7; -.
SwissPalm; Q8CGC7; -.
EPD; Q8CGC7; -.
MaxQB; Q8CGC7; -.
PaxDb; Q8CGC7; -.
PeptideAtlas; Q8CGC7; -.
PRIDE; Q8CGC7; -.
Ensembl; ENSMUST00000046514; ENSMUSP00000045841; ENSMUSG00000026615.
GeneID; 107508; -.
KEGG; mmu:107508; -.
UCSC; uc007dze.1; mouse.
CTD; 2058; -.
MGI; MGI:97838; Eprs.
eggNOG; KOG1147; Eukaryota.
eggNOG; KOG4163; Eukaryota.
eggNOG; COG0008; LUCA.
eggNOG; COG0442; LUCA.
GeneTree; ENSGT00550000074815; -.
HOGENOM; HOG000022047; -.
HOVERGEN; HBG017875; -.
InParanoid; Q8CGC7; -.
KO; K14163; -.
OMA; VAMLHIK; -.
OrthoDB; EOG091G04TK; -.
TreeFam; TF300380; -.
ChiTaRS; Eprs; mouse.
PRO; PR:Q8CGC7; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000026615; -.
CleanEx; MM_EPRS; -.
ExpressionAtlas; Q8CGC7; baseline and differential.
Genevisible; Q8CGC7; MM.
GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IDA:CAFA.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0097452; C:GAIT complex; IDA:UniProtKB.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; ISO:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004818; F:glutamate-tRNA ligase activity; IBA:GO_Central.
GO; GO:0051020; F:GTPase binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0004827; F:proline-tRNA ligase activity; IMP:CAFA.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0035613; F:RNA stem-loop binding; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0071346; P:cellular response to interferon-gamma; IDA:UniProtKB.
GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IBA:GO_Central.
GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
GO; GO:0006433; P:prolyl-tRNA aminoacylation; IDA:CAFA.
CDD; cd00778; ProRS_core_arch_euk; 1.
Gene3D; 1.10.1160.10; -; 1.
Gene3D; 1.10.287.10; -; 3.
Gene3D; 2.40.240.10; -; 2.
Gene3D; 3.30.110.30; -; 1.
Gene3D; 3.40.50.620; -; 2.
Gene3D; 3.40.50.800; -; 1.
HAMAP; MF_02076; Glu_tRNA_synth_type2; 1.
HAMAP; MF_01571; Pro_tRNA_synth_type3; 1.
InterPro; IPR002314; aa-tRNA-synt_IIb.
InterPro; IPR001412; aa-tRNA-synth_I_CS.
InterPro; IPR006195; aa-tRNA-synth_II.
InterPro; IPR004154; Anticodon-bd.
InterPro; IPR036621; Anticodon-bd_dom_sf.
InterPro; IPR004526; Glu-tRNA-synth_arc/euk.
InterPro; IPR000924; Glu/Gln-tRNA-synth.
InterPro; IPR020061; Glu/Gln-tRNA-synth_Ib_a-bdl.
InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
InterPro; IPR004046; GST_C.
InterPro; IPR004499; Pro-tRNA-ligase_IIa_arc-type.
InterPro; IPR016061; Pro-tRNA_ligase_II_C.
InterPro; IPR017449; Pro-tRNA_synth_II.
InterPro; IPR033721; ProRS_core_arch_euk.
InterPro; IPR020056; Rbsml_L25/Gln-tRNA_synth_N.
InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
InterPro; IPR014729; Rossmann-like_a/b/a_fold.
InterPro; IPR009068; S15_NS1_RNA-bd.
InterPro; IPR000738; WHEP-TRS_dom.
Pfam; PF00043; GST_C; 1.
Pfam; PF03129; HGTP_anticodon; 1.
Pfam; PF09180; ProRS-C_1; 1.
Pfam; PF00749; tRNA-synt_1c; 1.
Pfam; PF03950; tRNA-synt_1c_C; 1.
Pfam; PF00587; tRNA-synt_2b; 1.
Pfam; PF00458; WHEP-TRS; 3.
PRINTS; PR00987; TRNASYNTHGLU.
SMART; SM00946; ProRS-C_1; 1.
SMART; SM00991; WHEP-TRS; 3.
SUPFAM; SSF47060; SSF47060; 3.
SUPFAM; SSF47616; SSF47616; 1.
SUPFAM; SSF50715; SSF50715; 1.
SUPFAM; SSF52954; SSF52954; 1.
SUPFAM; SSF64586; SSF64586; 1.
TIGRFAMs; TIGR00463; gltX_arch; 1.
TIGRFAMs; TIGR00408; proS_fam_I; 1.
PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PROSITE; PS00762; WHEP_TRS_1; 2.
PROSITE; PS51185; WHEP_TRS_2; 3.
1: Evidence at protein level;
Acetylation; Aminoacyl-tRNA synthetase; ATP-binding;
Complete proteome; Cytoplasm; Ligase; Metal-binding; Methylation;
Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
Polymorphism; Protein biosynthesis; Reference proteome; Repeat;
RNA-binding; Translation regulation; Zinc.
CHAIN 1 1512 Bifunctional glutamate/proline--tRNA
ligase.
/FTId=PRO_0000119744.
DOMAIN 749 805 WHEP-TRS 1.
DOMAIN 822 878 WHEP-TRS 2.
DOMAIN 900 956 WHEP-TRS 3.
NP_BIND 432 436 ATP. {ECO:0000250}.
NP_BIND 1152 1154 ATP. {ECO:0000250|UniProtKB:P07814}.
NP_BIND 1163 1164 ATP. {ECO:0000250|UniProtKB:P07814}.
NP_BIND 1237 1240 ATP. {ECO:0000250|UniProtKB:P07814}.
REGION 164 759 Glutamate--tRNA ligase.
REGION 760 956 3 X 57 AA approximate repeats.
REGION 1007 1512 Proline--tRNA ligase.
REGION 1121 1123 L-proline binding.
{ECO:0000250|UniProtKB:P07814}.
MOTIF 204 214 "HIGH" region.
MOTIF 432 436 "KMSKS" region.
COMPBIAS 959 991 Asp/Glu/Lys-rich.
METAL 1448 1448 Zinc. {ECO:0000250|UniProtKB:P07814}.
METAL 1453 1453 Zinc. {ECO:0000250|UniProtKB:P07814}.
METAL 1495 1495 Zinc. {ECO:0000250|UniProtKB:P07814}.
METAL 1497 1497 Zinc. {ECO:0000250|UniProtKB:P07814}.
BINDING 211 211 ATP. {ECO:0000250}.
BINDING 398 398 ATP. {ECO:0000250}.
BINDING 1152 1152 L-proline.
{ECO:0000250|UniProtKB:P07814}.
BINDING 1242 1242 L-proline.
{ECO:0000250|UniProtKB:P07814}.
BINDING 1276 1276 ATP. {ECO:0000250|UniProtKB:P07814}.
MOD_RES 300 300 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 300 300 N6-malonyllysine; alternate.
{ECO:0000250}.
MOD_RES 355 355 Phosphothreonine.
{ECO:0000250|UniProtKB:P07814}.
MOD_RES 417 417 N6-acetyllysine.
{ECO:0000250|UniProtKB:P07814}.
MOD_RES 434 434 Phosphoserine.
{ECO:0000250|UniProtKB:P07814}.
MOD_RES 498 498 N6-acetyllysine.
{ECO:0000250|UniProtKB:P07814}.
MOD_RES 535 535 N6-acetyllysine.
{ECO:0000250|UniProtKB:P07814}.
MOD_RES 542 542 N6-acetyllysine.
{ECO:0000250|UniProtKB:P07814}.
MOD_RES 637 637 N6-acetyllysine.
{ECO:0000250|UniProtKB:P07814}.
MOD_RES 788 788 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 861 861 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 872 872 Phosphotyrosine.
{ECO:0000250|UniProtKB:P07814}.
MOD_RES 885 885 Phosphoserine.
{ECO:0000250|UniProtKB:P07814}.
MOD_RES 998 998 Phosphoserine.
{ECO:0000250|UniProtKB:P07814}.
MOD_RES 999 999 Phosphoserine.
{ECO:0000269|PubMed:23071094}.
MOD_RES 1152 1152 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P07814}.
MOD_RES 1350 1350 Phosphoserine.
{ECO:0000250|UniProtKB:P07814}.
MOD_RES 1503 1503 N6-acetyllysine.
{ECO:0000250|UniProtKB:P07814}.
VARIANT 871 871 D -> E.
MUTAGEN 999 999 S->A: Not active in translation
inhibition.
{ECO:0000269|PubMed:23071094}.
MUTAGEN 999 999 S->D: Active in translation inhibition
(phosphomimetic).
{ECO:0000269|PubMed:23071094}.
CONFLICT 94 94 R -> G (in Ref. 2; AAH40802).
{ECO:0000305}.
CONFLICT 172 172 N -> S (in Ref. 2; AAH40802).
{ECO:0000305}.
CONFLICT 618 618 S -> P (in Ref. 2; AAH40802).
{ECO:0000305}.
CONFLICT 986 986 G -> R (in Ref. 4; X54327).
{ECO:0000305}.
CONFLICT 1290 1290 N -> S (in Ref. 2; AAH94679).
{ECO:0000305}.
SEQUENCE 1512 AA; 170079 MW; D14F6EA015B1BB6A CRC64;
MAALCLTVNA GNPPLEALLA VEHVKGDVSI SVEEGKENLL RVSETVAFTD VNSILRYLAR
IATTSGLYGT NLMEHTEIDH WLEFSATKLS SCDRLTSAIN ELNHCLSLRT YLVGNSLTLA
DLCVWATLKG SAAWQEHLKQ NKTLVHVKRW FGFLEAQQAF RSVGTKWDVS GNRATVAPDK
KQDVGKFVEL PGAEMGKVTV RFPPEASGYL HIGHAKAALL NQHYQVNFKG KLIMRFDDTN
PEKEKEDFEK VILEDVAMLH IKPDQFTYTS DHFETIMKYA EKLIQEGKAY VDDTPAEQMK
AEREQRTESK HRKNSVEKNL QMWEEMKKGS QFGQSCCLRA KIDMSSNNGC MRDPTLYRCK
IQPHPRTGNK YNVYPTYDFA CPIVDSIEGV THALRTTEYH DRDEQFYWII EALGIRKPYI
WEYSRLNLNN TVLSKRKLTW FVNEGLVDGW DDPRFPTVRG VLRRGMTVEG LKQFIAAQGS
SRSVVNMEWD KIWAFNKKVI DPVAPRYVAL LKKEVVPVNV LDAQEEMKEV ARHPKNPDVG
LKPVWYSPKV FIEGADAETF SEGEMVTFIN WGNINITKIH KNADGKITSL DAKLNLENKD
YKKTTKITWL AESTHALSIP AVCVTYEHLI TKPVLGKDED FKQYINKDSK HEELMLGDPC
LKDLKKGDII QLQRRGFFIC DQPYEPVSPY SCREAPCILI YIPDGHTKEM PTSGSKEKTK
VEISKKETSS APKERPAPAV SSTCATAEDS SVLYSRVAVQ GDVVRELKAK KAPKEDIDAA
VKQLLTLKAE YKEKTGQEYK PGNPSAAAVQ TVSTKSSSNT VESTSLYNKV AAQGEVVRKL
KAEKAPKAKV TEAVECLLSL KAEYKEKTGK DYVPGQPPAS QNSHSNPVSN AQPAGAEKPE
AKVLFDRVAC QGEVVRKLKA EKASKDQVDS AVQELLQLKA QYKSLTGIEY KPVSATGAED
KDKKKKEKEN KSEKQNKPQK QNDGQGKDSS KSQGSGLSSG GAGEGQGPKK QTRLGLEAKK
EENLAEWYSQ VITKSEMIEY YDVSGCYILR PWSYSIWESI KDFFDAEIKK LGVENCYFPI
FVSQAALEKE KNHIEDFAPE VAWVTRSGKT ELAEPIAIRP TSETVMYPAY AKWVQSHRDL
PVRLNQWCNV VRWEFKHPQP FLRTREFLWQ EGHSAFATFE EAADEVLQIL ELYARVYEEL
LAIPVVRGRK TEKEKFAGGD YTTTIEAFIS ASGRAIQGAT SHHLGQNFSK MCEIVFEDPK
TPGEKQFAYQ CSWGLTTRTI GVMVMVHGDN MGLVLPPRVA SVQVVVIPCG ITNALSEEDR
EALMAKCNEY RRRLLGANIR VRVDLRDNYS PGWKFNHWEL KGVPVRLEVG PRDMKSCQFV
AVRRDTGEKL TIAEKEAEAK LEKVLEDIQL NLFTRASEDL KTHMVVSNTL EDFQKVLDAG
KVAQIPFCGE IDCEDWIKKM TARDQDVEPG APSMGAKSLC IPFNPLCELQ PGAMCVCGKN
PAKFYTLFGR SY


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EIAAB40834 Homo sapiens,Human,PARS2,Probable prolyl-tRNA synthetase, mitochondrial,Proline--tRNA ligase,ProRS
EIAAB40724 Chicken,EARS2,Gallus gallus,GluRS,Glutamate--tRNA ligase,Probable glutamyl-tRNA synthetase, mitochondrial,RCJMB04_20f12
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
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EIAAB40853 Homo sapiens,Human,SARS2,SARSM,Serine--tRNA ligase,SerRS,SerRSmt,Seryl-tRNA synthetase, mitochondrial,Seryl-tRNA(Ser_Sec) synthetase
EIAAB40938 Homo sapiens,Human,KIAA1885,Valine--tRNA ligase,ValRS,Valyl-tRNA synthetase, mitochondrial,Valyl-tRNA synthetase-like,VARS2,VARS2L,VARSL
EIAAB40848 Homo sapiens,Human,SARS,Serine--tRNA ligase,SerRS,SERS,Seryl-tRNA synthetase, cytoplasmic,Seryl-tRNA(Ser_Sec) synthetase
EIAAB40855 Bos taurus,Bovine,SARS2,SARSM,Serine--tRNA ligase,SerRS,SerRSmt,Seryl-tRNA synthetase, mitochondrial,Seryl-tRNA(Ser_Sec) synthetase
EIAAB40851 Mouse,Mus musculus,Sars,Sars1,Serine--tRNA ligase,SerRS,Sers,Seryl-tRNA synthetase, cytoplasmic,Seryl-tRNA(Ser_Sec) synthetase
EIAAB40844 Arginine--tRNA ligase,Arginyl-tRNA synthetase-like,ArgRS,Homo sapiens,Human,Probable arginyl-tRNA synthetase, mitochondrial,RARS2,RARSL
EIAAB40854 Mouse,Mus musculus,Sars2,Sarsm,Serine--tRNA ligase,SerRS,SerRSmt,Seryl-tRNA synthetase, mitochondrial,Seryl-tRNA(Ser_Sec) synthetase
EIAAB40912 Homo sapiens,Human,Probable threonyl-tRNA synthetase 2, cytoplasmic,TARSL2,Threonine--tRNA ligase,Threonyl-tRNA synthetase-like protein 2,ThrRS
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EIAAB40843 Arginine--tRNA ligase,Arginyl-tRNA synthetase-like,ArgRS,Bos taurus,Bovine,Probable arginyl-tRNA synthetase, mitochondrial,RARS2,RARSL
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