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Serine--tRNA ligase, mitochondrial (EC 6.1.1.11) (SerRSmt) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)

 SYSM_HUMAN              Reviewed;         518 AA.
Q9NP81; A6NHW7; B4DE10; Q9BVP3;
10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
13-FEB-2019, entry version 168.
RecName: Full=Serine--tRNA ligase, mitochondrial;
EC=6.1.1.11;
AltName: Full=SerRSmt;
AltName: Full=Seryl-tRNA synthetase;
Short=SerRS;
AltName: Full=Seryl-tRNA(Ser/Sec) synthetase;
Flags: Precursor;
Name=SARS2; Synonyms=SARSM;
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).
PubMed=10764807; DOI=10.1074/jbc.M908473199;
Yokogawa T., Shimada N., Takeuchi N., Benkowski L., Suzuki T.,
Omori A., Ueda T., Nishikawa K., Spremulli L.L., Watanabe K.;
"Characterization and tRNA recognition of mammalian mitochondrial
seryl-tRNA synthetase.";
J. Biol. Chem. 275:19913-19920(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Eye;
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).
[5]
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).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[7]
VARIANT HUPRAS GLY-390.
PubMed=21255763; DOI=10.1016/j.ajhg.2010.12.010;
Belostotsky R., Ben-Shalom E., Rinat C., Becker-Cohen R.,
Feinstein S., Zeligson S., Segel R., Elpeleg O., Nassar S.,
Frishberg Y.;
"Mutations in the mitochondrial seryl-tRNA synthetase cause
hyperuricemia, pulmonary hypertension, renal failure in infancy and
alkalosis, HUPRA syndrome.";
Am. J. Hum. Genet. 88:193-200(2011).
-!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also
probably able to aminoacylate tRNA(Sec) with serine, to form the
misacylated tRNA L-seryl-tRNA(Sec), which will be further
converted into selenocysteinyl-tRNA(Sec).
{ECO:0000250|UniProtKB:Q9N0F3}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) +
L-seryl-tRNA(Ser); Xref=Rhea:RHEA:12292, Rhea:RHEA-COMP:9669,
Rhea:RHEA-COMP:9703, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
Evidence={ECO:0000250|UniProtKB:Q9N0F3};
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) +
L-seryl-tRNA(Sec); Xref=Rhea:RHEA:42580, Rhea:RHEA-COMP:9742,
Rhea:RHEA-COMP:10128, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
Evidence={ECO:0000250|UniProtKB:Q9N0F3};
-!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step
1/1.
-!- SUBUNIT: Homodimer. The tRNA molecule probably binds across the
dimer. {ECO:0000250|UniProtKB:Q9N0F3}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000250|UniProtKB:Q9N0F3}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9NP81-1; Sequence=Displayed;
Name=2;
IsoId=Q9NP81-2; Sequence=VSP_043020;
Note=No experimental confirmation available.;
-!- DOMAIN: Consists of two distinct domains, a catalytic core and a
N-terminal extension that is involved in tRNA binding.
{ECO:0000250|UniProtKB:Q9N0F3}.
-!- DISEASE: Hyperuricemia, pulmonary hypertension, renal failure, and
alkalosis syndrome (HUPRAS) [MIM:613845]: A multisystem disorder
characterized by onset in infancy of progressive renal failure
leading to electrolyte imbalances, metabolic alkalosis, pulmonary
hypertension, hypotonia, and delayed development. Affected
individuals are born prematurely. {ECO:0000269|PubMed:21255763}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
family. Type-1 seryl-tRNA synthetase subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH01020.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB029948; BAA99557.1; -; mRNA.
EMBL; AK000457; BAA91176.1; -; mRNA.
EMBL; AK293414; BAG56921.1; -; mRNA.
EMBL; AC011455; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001020; AAH01020.2; ALT_INIT; mRNA.
EMBL; BC042912; AAH42912.1; -; mRNA.
CCDS; CCDS33017.1; -. [Q9NP81-1]
CCDS; CCDS54265.1; -. [Q9NP81-2]
RefSeq; NP_001139373.1; NM_001145901.1. [Q9NP81-2]
RefSeq; NP_060297.1; NM_017827.3. [Q9NP81-1]
UniGene; Hs.709416; -.
ProteinModelPortal; Q9NP81; -.
SMR; Q9NP81; -.
BioGrid; 120278; 35.
IntAct; Q9NP81; 24.
MINT; Q9NP81; -.
STRING; 9606.ENSP00000472847; -.
iPTMnet; Q9NP81; -.
PhosphoSitePlus; Q9NP81; -.
BioMuta; SARS2; -.
DMDM; 23822219; -.
EPD; Q9NP81; -.
jPOST; Q9NP81; -.
MaxQB; Q9NP81; -.
PaxDb; Q9NP81; -.
PeptideAtlas; Q9NP81; -.
PRIDE; Q9NP81; -.
ProteomicsDB; 81925; -.
ProteomicsDB; 81926; -. [Q9NP81-2]
Ensembl; ENST00000221431; ENSP00000221431; ENSG00000104835. [Q9NP81-1]
Ensembl; ENST00000600042; ENSP00000472847; ENSG00000104835. [Q9NP81-2]
Ensembl; ENST00000634687; ENSP00000489539; ENSG00000283104. [Q9NP81-1]
Ensembl; ENST00000635245; ENSP00000489453; ENSG00000283104. [Q9NP81-2]
GeneID; 54938; -.
KEGG; hsa:54938; -.
UCSC; uc002oka.3; human. [Q9NP81-1]
CTD; 54938; -.
DisGeNET; 54938; -.
EuPathDB; HostDB:ENSG00000104835.14; -.
GeneCards; SARS2; -.
HGNC; HGNC:17697; SARS2.
HPA; HPA052730; -.
HPA; HPA056957; -.
MalaCards; SARS2; -.
MIM; 612804; gene.
MIM; 613845; phenotype.
neXtProt; NX_Q9NP81; -.
OpenTargets; ENSG00000104835; -.
Orphanet; 363694; Hyperuricemia-pulmonary hypertension-renal failure-alkalosis syndrome.
PharmGKB; PA134899753; -.
eggNOG; KOG2509; Eukaryota.
eggNOG; COG0172; LUCA.
GeneTree; ENSGT00940000153792; -.
HOGENOM; HOG000035937; -.
HOVERGEN; HBG023869; -.
InParanoid; Q9NP81; -.
KO; K01875; -.
OMA; KHIRQNP; -.
OrthoDB; 726296at2759; -.
PhylomeDB; Q9NP81; -.
BRENDA; 6.1.1.11; 2681.
Reactome; R-HSA-379726; Mitochondrial tRNA aminoacylation.
UniPathway; UPA00906; UER00895.
ChiTaRS; SARS2; human.
GeneWiki; SARS2; -.
GenomeRNAi; 54938; -.
PRO; PR:Q9NP81; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000104835; Expressed in 88 organ(s), highest expression level in adult mammalian kidney.
ExpressionAtlas; Q9NP81; baseline and differential.
Genevisible; Q9NP81; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0004828; F:serine-tRNA ligase activity; ISS:UniProtKB.
GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006434; P:seryl-tRNA aminoacylation; ISS:UniProtKB.
GO; GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome.
CDD; cd00770; SerRS_core; 1.
InterPro; IPR002314; aa-tRNA-synt_IIb.
InterPro; IPR006195; aa-tRNA-synth_II.
InterPro; IPR002317; Ser-tRNA-ligase_type_1.
InterPro; IPR033729; SerRS_core.
InterPro; IPR010978; tRNA-bd_arm.
PANTHER; PTHR11778; PTHR11778; 1.
Pfam; PF00587; tRNA-synt_2b; 1.
PIRSF; PIRSF001529; Ser-tRNA-synth_IIa; 1.
PRINTS; PR00981; TRNASYNTHSER.
SUPFAM; SSF46589; SSF46589; 1.
TIGRFAMs; TIGR00414; serS; 1.
PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Aminoacyl-tRNA synthetase;
ATP-binding; Complete proteome; Ligase; Mitochondrion;
Nucleotide-binding; Polymorphism; Protein biosynthesis;
Reference proteome; Transit peptide.
TRANSIT 1 34 Mitochondrion.
{ECO:0000250|UniProtKB:Q9N0F3}.
CHAIN 35 518 Serine--tRNA ligase, mitochondrial.
/FTId=PRO_0000035822.
NP_BIND 330 332 ATP. {ECO:0000250|UniProtKB:Q9N0F3}.
NP_BIND 418 421 ATP. {ECO:0000250|UniProtKB:Q9N0F3}.
REGION 299 301 L-serine binding.
{ECO:0000250|UniProtKB:Q9N0F3}.
BINDING 345 345 ATP; via amide nitrogen and carbonyl
oxygen. {ECO:0000250|UniProtKB:Q9N0F3}.
BINDING 352 352 L-serine. {ECO:0000250|UniProtKB:Q9N0F3}.
BINDING 453 453 L-serine. {ECO:0000250|UniProtKB:Q9N0F3}.
MOD_RES 110 110 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9JJL8}.
MOD_RES 195 195 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9JJL8}.
VAR_SEQ 132 155 DPKYQGLRARGREIRKELVHLYPR -> VRLDPGAGSIFGP
TFLPFPGQLSLLV (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043020.
VARIANT 35 35 T -> A (in dbSNP:rs34264048).
/FTId=VAR_052645.
VARIANT 83 83 S -> L (in dbSNP:rs34050897).
/FTId=VAR_052646.
VARIANT 390 390 D -> G (in HUPRAS; dbSNP:rs727502784).
{ECO:0000269|PubMed:21255763}.
/FTId=VAR_065820.
SEQUENCE 518 AA; 58283 MW; C6516A9527B34EB7 CRC64;
MAASMARRLW PLLTRRGFRP RGGCISNDSP RRSFTTEKRN RNLLYEYARE GYSALPQLDI
ERFCACPEEA AHALELRKGE LRSADLPAII STWQELRQLQ EQIRSLEEEK AAVTEAVRAL
LANQDSGEVQ QDPKYQGLRA RGREIRKELV HLYPREAQLE EQFYLQALKL PNQTHPDVPV
GDESQARVLH MVGDKPVFSF QPRGHLEIGE KLDIIRQKRL SHVSGHRSYY LRGAGALLQH
GLVNFTFNKL LRRGFTPMTV PDLLRGAVFE GCGMTPNANP SQIYNIDPAR FKDLNLAGTA
EVGLAGYFMD HTVAFRDLPV RMVCSSTCYR AETNTGQEPR GLYRVHHFTK VEMFGVTGPG
LEQSSQLLEE FLSLQMEILT ELGLHFRVLD MPTQELGLPA YRKFDIEAWM PGRGRFGEVT
SASNCTDFQS RRLHIMFQTE AGELQFAHTV NATACAVPRL LIALLESNQQ KDGSVLVPPA
LQSYLGTDRI TAPTHVPLQY IGPNQPRKPG LPGQPAVS


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Pathways :
WP219: Cytoplasmic tRNA Synthetases
WP433: tRNA Synthetases
WP62: Mitochondrial tRNA Synthetases
WP106: Alanine and aspartate metabolism
WP1620: Aminoacyl-tRNA biosynthesis
WP1938: tRNA Aminoacylation
WP2199: Seed Development
WP1577: amino acid conjugation of benzoic acid
WP1708: Terpenoid backbone biosynthesis
WP2211: Geranylgeranyldiphosphate biosynthesis II (plastidic)
WP296: TCA Cycle - biocyc
WP521: amino acid conjugation of benzoic acid
WP1097: Non-homologous end joining
WP1107: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1201: Non-homologous end joining
WP1208: Non-homologous end joining
WP1222: Non-homologous end joining
WP1226: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1242: Non-homologous end joining
WP1263: Mitochondrial Gene Expression
WP1277: Non-homologous end joining
WP1301: Mitochondrial Gene Expression
WP1324: Non-homologous end joining
WP1368: Mitochondrial Gene Expression
WP1502: Mitochondrial biogenesis

Related Genes :
[SARS QccE-14020] Serine--tRNA ligase, cytoplasmic (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
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[serS OR16_34668] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS OR37_03554] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS OR214_02672] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS ATE51_03436 CC14983A_1504 NCTC11366_01668] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS HPHPH6_1663] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS HPHPA6_1621] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS HPHPP11_1453] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS HPHPH11_0081] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS OR221_0117] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS Loa_02333] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS MCAL106_1042 MCAL106E_1042 MCAL106L_1042] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS HPHPP1_0039] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[Eprs Qprs] 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)]
[serS MCAL160E_1042 MCAL160L_1042] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS MSMEG_6413 MSMEI_6245] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[EPRS GLNS PARS QARS QPRS PIG32] Bifunctional glutamate/proline--tRNA ligase (Bifunctional aminoacyl-tRNA synthetase) (Cell proliferation-inducing gene 32 protein) (Glutamatyl-prolyl-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)]
[serS OUG_0047] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS OUS_0164] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS OUM_1601] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS OUK_0115] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS OUO_1462] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS OUE_1624] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS HPHPP16_1399] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS HPHPA8_1507] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS HPHPA26_1457] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS HPHPP3_1606] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS HPNQ4099_1605] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)
[serS HPCPY1124_1577] Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)

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