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Alanine--tRNA ligase, cytoplasmic (EC 6.1.1.7) (Alanyl-tRNA synthetase) (AlaRS) (Renal carcinoma antigen NY-REN-42)

 SYAC_HUMAN              Reviewed;         968 AA.
P49588; A6NF14; B4DR45; Q53GV7; Q96FA0;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
03-OCT-2006, sequence version 2.
22-NOV-2017, entry version 168.
RecName: Full=Alanine--tRNA ligase, cytoplasmic {ECO:0000255|HAMAP-Rule:MF_03133};
EC=6.1.1.7 {ECO:0000255|HAMAP-Rule:MF_03133, ECO:0000269|PubMed:25817015, ECO:0000269|PubMed:27622773, ECO:0000269|PubMed:27911835};
AltName: Full=Alanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_03133};
Short=AlaRS {ECO:0000255|HAMAP-Rule:MF_03133};
AltName: Full=Renal carcinoma antigen NY-REN-42;
Name=AARS {ECO:0000255|HAMAP-Rule:MF_03133};
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=7654687; DOI=10.1021/bi00033a004;
Shiba K., Ripmaster T.L., Suzuki N., Nichols R., Plotz P., Noda T.,
Schimmel P.;
"Human alanyl-tRNA synthetase: conservation in evolution of catalytic
core and microhelix recognition.";
Biochemistry 34:10340-10349(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 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 MRNA] (ISOFORM 1).
TISSUE=Liver;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[5]
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
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).
[7]
PROTEIN SEQUENCE OF 1-11; 304-320 AND 684-695, ACETYLATION AT MET-1,
AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Osteosarcoma;
Bienvenut W.V., Glen H., Brunton V.G., Frame M.C.;
Submitted (JUL-2007) to UniProtKB.
[8]
IDENTIFICATION AS A RENAL CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
PubMed=10508479;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
Old L.J.;
"Antigens recognized by autologous antibody in patients with renal-
cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[9]
ISGYLATION.
PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
"Proteomic identification of proteins conjugated to ISG15 in mouse and
human cells.";
Biochem. Biophys. Res. Commun. 336:496-506(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-555, 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).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND 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).
[12]
DOMAIN EXCHANGE EXPERIMENTS.
PubMed=19661429; DOI=10.1126/science.1174343;
Guo M., Chong Y.E., Beebe K., Shapiro R., Yang X.-L., Schimmel P.;
"The C-Ala domain brings together editing and aminoacylation functions
on one tRNA.";
Science 325:744-747(2009).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-19 AND LYS-876, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399, AND 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).
[15]
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).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND 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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-8 AND SER-555,
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).
[19]
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).
[20]
BIOPHYSICOCHEMICAL PROPERTIES, INVOLVEMENT IN EIEE29, VARIANTS EIEE29
THR-81 AND GLY-751, CHARACTERIZATION OF VARIANTS EIEE29 THR-81 AND
GLY-751, AND CATALYTIC ACTIVITY.
PubMed=25817015; DOI=10.1016/j.ajhg.2015.02.012;
Simons C., Griffin L.B., Helman G., Golas G., Pizzino A., Bloom M.,
Murphy J.L., Crawford J., Evans S.H., Topper S., Whitehead M.T.,
Schreiber J.M., Chapman K.A., Tifft C., Lu K.B., Gamper H.,
Shigematsu M., Taft R.J., Antonellis A., Hou Y.M., Vanderver A.;
"Loss-of-function alanyl-tRNA synthetase mutations cause an autosomal-
recessive early-onset epileptic encephalopathy with persistent
myelination defect.";
Am. J. Hum. Genet. 96:675-681(2015).
[21]
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).
[22] {ECO:0000244|PDB:4XEM}
X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS) OF 1-455 IN COMPLEX WITH
L-ALANINYL-ADENYLATE ANALOG.
Zhou H., Yang X.L.;
"Crystal structure of wild type human AlaRS catalytic domain.";
Submitted (DEC-2014) to the PDB data bank.
[23] {ECO:0000244|PDB:5KNN}
X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) OF 4-453 IN COMPLEX WITH
L-ALANINYL-ADENYLATE ANALOG, CATALYTIC ACTIVITY, FUNCTION, AND
MUTAGENESIS OF ALA-448.
PubMed=27622773; DOI=10.1021/jacs.6b07121;
Sun L., Gomes A.C., He W., Zhou H., Wang X., Pan D.W., Schimmel P.,
Pan T., Yang X.L.;
"Evolutionary Gain of Alanine Mischarging to Noncognate tRNAs with a
G4:U69 Base Pair.";
J. Am. Chem. Soc. 138:12948-12955(2016).
[24] {ECO:0000244|PDB:5T5S, ECO:0000244|PDB:5T76}
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 757-965, CATALYTIC ACTIVITY,
FUNCTION, DOMAIN, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=27911835; DOI=10.1073/pnas.1617316113;
Sun L., Song Y., Blocquel D., Yang X.L., Schimmel P.;
"Two crystal structures reveal design for repurposing the C-Ala domain
of human AlaRS.";
Proc. Natl. Acad. Sci. U.S.A. 113:14300-14305(2016).
[25]
VARIANT CMT2N HIS-329.
PubMed=20045102; DOI=10.1016/j.ajhg.2009.12.005;
Latour P., Thauvin-Robinet C., Baudelet-Mery C., Soichot P., Cusin V.,
Faivre L., Locatelli M.C., Mayencon M., Sarcey A., Broussolle E.,
Camu W., David A., Rousson R.;
"A major determinant for binding and aminoacylation of tRNA(Ala) in
cytoplasmic Alanyl-tRNA synthetase is mutated in dominant axonal
Charcot-Marie-Tooth disease.";
Am. J. Hum. Genet. 86:77-82(2010).
[26]
VARIANT CMT2N TYR-71.
PubMed=22206013; DOI=10.1371/journal.pone.0029393;
Lin K.P., Soong B.W., Yang C.C., Huang L.W., Chang M.H., Lee I.H.,
Antonellis A., Lee Y.C.;
"The mutational spectrum in a cohort of Charcot-Marie-Tooth disease
type 2 among the Han Chinese in Taiwan.";
PLoS ONE 6:E29393-E29393(2011).
[27]
VARIANT CMT2N HIS-329, AND CHARACTERIZATION OF VARIANT CMT2N HIS-329.
PubMed=22009580; DOI=10.1002/humu.21635;
McLaughlin H.M., Sakaguchi R., Giblin W., Wilson T.E., Biesecker L.,
Lupski J.R., Talbot K., Vance J.M., Zuchner S., Lee Y.C.,
Kennerson M., Hou Y.M., Nicholson G., Antonellis A.;
"A recurrent loss-of-function alanyl-tRNA synthetase (AARS) mutation
in patients with Charcot-Marie-Tooth disease type 2N (CMT2N).";
Hum. Mutat. 33:244-253(2012).
[28]
VARIANT MET-608.
PubMed=24627108; DOI=10.1007/s00415-014-7289-8;
Schabhuettl M., Wieland T., Senderek J., Baets J., Timmerman V.,
De Jonghe P., Reilly M.M., Stieglbauer K., Laich E., Windhager R.,
Erwa W., Trajanoski S., Strom T.M., Auer-Grumbach M.;
"Whole-exome sequencing in patients with inherited neuropathies:
outcome and challenges.";
J. Neurol. 261:970-982(2014).
-!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a
two-step reaction: alanine is first activated by ATP to form Ala-
AMP and then transferred to the acceptor end of tRNA(Ala). Also
edits incorrectly charged tRNA(Ala) via its editing domain.
{ECO:0000255|HAMAP-Rule:MF_03133, ECO:0000269|PubMed:27622773,
ECO:0000269|PubMed:27911835}.
-!- CATALYTIC ACTIVITY: ATP + L-alanine + tRNA(Ala) = AMP +
diphosphate + L-alanyl-tRNA(Ala). {ECO:0000255|HAMAP-
Rule:MF_03133, ECO:0000269|PubMed:25817015,
ECO:0000269|PubMed:27622773, ECO:0000269|PubMed:27911835}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000255|HAMAP-Rule:MF_03133};
Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-
Rule:MF_03133};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3.1 uM for tRNA(Ala) (at 37 Celsius)
{ECO:0000269|PubMed:25817015};
Note=kcat is 0.4 sec(-1). {ECO:0000269|PubMed:25817015};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:27911835}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03133,
ECO:0000269|PubMed:27911835}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P49588-1; Sequence=Displayed;
Name=2;
IsoId=P49588-2; Sequence=VSP_057201, VSP_057202;
Note=No experimental confirmation available.;
-!- DOMAIN: Consists of three domains; the N-terminal catalytic
domain, the editing domain and the C-terminal C-Ala domain. The
editing domain removes incorrectly charged amino acids, while the
C-Ala domain, along with tRNA(Ala), serves as a bridge to
cooperatively bring together the editing and aminoacylation
centers thus stimulating deacylation of misacylated tRNAs.
{ECO:0000255|HAMAP-Rule:MF_03133}.
-!- DOMAIN: The C-terminal C-Ala domain (residues 756 to 968) is not
required for catalytic activity and can bind DNA (in vitro)
(PubMed:27911835). The C-terminal C-Ala domain (residues 756 to
968), along with tRNA(Ala), serves as a bridge to cooperatively
bring together the editing and aminoacylation centers thus
stimulating deacylation of misacylated tRNAs. The human domain can
be used in vitro to replace the corresponding domain in E.coli
(PubMed:19661429). {ECO:0000269|PubMed:19661429}.
-!- PTM: ISGylated. {ECO:0000255|HAMAP-Rule:MF_03133,
ECO:0000269|PubMed:16139798}.
-!- DISEASE: Charcot-Marie-Tooth disease 2N (CMT2N) [MIM:613287]: An
axonal form of Charcot-Marie-Tooth disease, a disorder of the
peripheral nervous system, characterized by progressive weakness
and atrophy, initially of the peroneal muscles and later of the
distal muscles of the arms. Charcot-Marie-Tooth disease is
classified in two main groups on the basis of electrophysiologic
properties and histopathology: primary peripheral demyelinating
neuropathies (designated CMT1 when they are dominantly inherited)
and primary peripheral axonal neuropathies (CMT2). Neuropathies of
the CMT2 group are characterized by signs of axonal degeneration
in the absence of obvious myelin alterations, normal or slightly
reduced nerve conduction velocities, and progressive distal muscle
weakness and atrophy. Nerve conduction velocities are normal or
slightly reduced. {ECO:0000269|PubMed:20045102,
ECO:0000269|PubMed:22009580, ECO:0000269|PubMed:22206013}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Epileptic encephalopathy, early infantile, 29 (EIEE29)
[MIM:616339]: A form of epileptic encephalopathy, a heterogeneous
group of severe childhood onset epilepsies characterized by
refractory seizures, neurodevelopmental impairment, and poor
prognosis. Development is normal prior to seizure onset, after
which cognitive and motor delays become apparent. EIEE29 patients
manifest severe infantile epileptic encephalopathy, clubfoot,
absent deep tendon reflexes, extrapyramidal symptoms, and
persistently deficient myelination. {ECO:0000269|PubMed:25817015}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
family. {ECO:0000255|HAMAP-Rule:MF_03133}.
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EMBL; D32050; BAA06808.1; -; mRNA.
EMBL; AK299098; BAG61157.1; -; mRNA.
EMBL; AK222824; BAD96544.1; -; mRNA.
EMBL; AC012184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471241; EAW51839.1; -; Genomic_DNA.
EMBL; BC011451; AAH11451.1; -; mRNA.
CCDS; CCDS32474.1; -. [P49588-1]
PIR; I60107; I60107.
RefSeq; NP_001596.2; NM_001605.2. [P49588-1]
UniGene; Hs.315137; -.
PDB; 4XEM; X-ray; 1.28 A; A=1-455.
PDB; 4XEO; X-ray; 1.38 A; A/B=1-455.
PDB; 5KNN; X-ray; 2.68 A; A/B/C/D/E/F/G/H=4-453.
PDB; 5T5S; X-ray; 2.20 A; A=757-965.
PDB; 5T76; X-ray; 2.00 A; A=757-965.
PDBsum; 4XEM; -.
PDBsum; 4XEO; -.
PDBsum; 5KNN; -.
PDBsum; 5T5S; -.
PDBsum; 5T76; -.
ProteinModelPortal; P49588; -.
SMR; P49588; -.
BioGrid; 106534; 54.
IntAct; P49588; 6.
MINT; MINT-1490092; -.
STRING; 9606.ENSP00000261772; -.
BindingDB; P49588; -.
ChEMBL; CHEMBL3574; -.
DrugBank; DB00160; L-Alanine.
iPTMnet; P49588; -.
PhosphoSitePlus; P49588; -.
SwissPalm; P49588; -.
BioMuta; AARS; -.
DMDM; 115502460; -.
EPD; P49588; -.
MaxQB; P49588; -.
PaxDb; P49588; -.
PeptideAtlas; P49588; -.
PRIDE; P49588; -.
DNASU; 16; -.
Ensembl; ENST00000261772; ENSP00000261772; ENSG00000090861. [P49588-1]
GeneID; 16; -.
KEGG; hsa:16; -.
UCSC; uc002eyn.2; human. [P49588-1]
CTD; 16; -.
DisGeNET; 16; -.
EuPathDB; HostDB:ENSG00000090861.15; -.
GeneCards; AARS; -.
GeneReviews; AARS; -.
HGNC; HGNC:20; AARS.
HPA; CAB034261; -.
HPA; HPA040870; -.
HPA; HPA044223; -.
MalaCards; AARS; -.
MIM; 601065; gene.
MIM; 613287; phenotype.
MIM; 616339; phenotype.
neXtProt; NX_P49588; -.
OpenTargets; ENSG00000090861; -.
Orphanet; 228174; Autosomal dominant Charcot-Marie-Tooth disease type 2N.
PharmGKB; PA24367; -.
eggNOG; KOG0188; Eukaryota.
eggNOG; COG0013; LUCA.
GeneTree; ENSGT00390000016019; -.
HOGENOM; HOG000156964; -.
HOVERGEN; HBG017874; -.
InParanoid; P49588; -.
KO; K01872; -.
OMA; FEMMAHH; -.
OrthoDB; EOG091G00Z9; -.
PhylomeDB; P49588; -.
TreeFam; TF300737; -.
Reactome; R-HSA-379716; Cytosolic tRNA aminoacylation.
ChiTaRS; AARS; human.
GenomeRNAi; 16; -.
PRO; PR:P49588; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000090861; -.
CleanEx; HS_AARS; -.
ExpressionAtlas; P49588; baseline and differential.
Genevisible; P49588; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0004813; F:alanine-tRNA ligase activity; IDA:UniProtKB.
GO; GO:0016597; F:amino acid binding; IBA:GO_Central.
GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
GO; GO:0006419; P:alanyl-tRNA aminoacylation; IDA:UniProtKB.
GO; GO:0021680; P:cerebellar Purkinje cell layer development; IEA:Ensembl.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
GO; GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome.
GO; GO:0006400; P:tRNA modification; IBA:GO_Central.
GO; GO:0008033; P:tRNA processing; TAS:ProtInc.
HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1.
InterPro; IPR002318; Ala-tRNA-lgiase_IIc.
InterPro; IPR018162; Ala-tRNA-ligase_IIc_anticod-bd.
InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
InterPro; IPR023033; Ala_tRNA_ligase_euk/bac.
InterPro; IPR003156; DHHA1_dom.
InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
InterPro; IPR009000; Transl_B-barrel_sf.
InterPro; IPR012947; tRNA_SAD.
Pfam; PF02272; DHHA1; 1.
Pfam; PF01411; tRNA-synt_2c; 1.
Pfam; PF07973; tRNA_SAD; 1.
PRINTS; PR00980; TRNASYNTHALA.
SMART; SM00863; tRNA_SAD; 1.
SUPFAM; SSF101353; SSF101353; 1.
SUPFAM; SSF50447; SSF50447; 1.
SUPFAM; SSF55186; SSF55186; 1.
TIGRFAMs; TIGR00344; alaS; 1.
PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing;
Aminoacyl-tRNA synthetase; ATP-binding; Charcot-Marie-Tooth disease;
Complete proteome; Cytoplasm; Direct protein sequencing;
Disease mutation; Epilepsy; Ligase; Metal-binding; Neurodegeneration;
Neuropathy; Nucleotide-binding; Phosphoprotein; Polymorphism;
Protein biosynthesis; Reference proteome; RNA-binding; tRNA-binding;
Ubl conjugation; Zinc.
CHAIN 1 968 Alanine--tRNA ligase, cytoplasmic.
/FTId=PRO_0000075281.
NP_BIND 214 216 ATP. {ECO:0000244|PDB:4XEM,
ECO:0000244|PDB:4XEO,
ECO:0000244|PDB:5KNN,
ECO:0000269|PubMed:27622773,
ECO:0000269|Ref.22}.
METAL 605 605 Zinc. {ECO:0000255|HAMAP-Rule:MF_03133}.
METAL 609 609 Zinc. {ECO:0000255|HAMAP-Rule:MF_03133}.
METAL 723 723 Zinc. {ECO:0000255|HAMAP-Rule:MF_03133}.
METAL 727 727 Zinc. {ECO:0000255|HAMAP-Rule:MF_03133}.
BINDING 77 77 ATP. {ECO:0000244|PDB:4XEM,
ECO:0000244|PDB:4XEO,
ECO:0000244|PDB:5KNN,
ECO:0000269|PubMed:27622773,
ECO:0000269|Ref.22}.
BINDING 95 95 ATP; via amide nitrogen and carbonyl
oxygen. {ECO:0000244|PDB:4XEM,
ECO:0000244|PDB:4XEO,
ECO:0000244|PDB:5KNN,
ECO:0000269|PubMed:27622773,
ECO:0000269|Ref.22}.
BINDING 176 176 ATP. {ECO:0000244|PDB:4XEM,
ECO:0000244|PDB:4XEO,
ECO:0000244|PDB:5KNN,
ECO:0000269|PubMed:27622773,
ECO:0000269|Ref.22}.
BINDING 216 216 L-alanine. {ECO:0000244|PDB:4XEM,
ECO:0000244|PDB:4XEO,
ECO:0000244|PDB:5KNN,
ECO:0000269|PubMed:27622773,
ECO:0000269|Ref.22}.
BINDING 239 239 L-alanine. {ECO:0000244|PDB:4XEM,
ECO:0000244|PDB:4XEO,
ECO:0000244|PDB:5KNN,
ECO:0000269|PubMed:27622773,
ECO:0000269|Ref.22}.
BINDING 243 243 ATP; via amide nitrogen.
{ECO:0000244|PDB:4XEM,
ECO:0000244|PDB:4XEO,
ECO:0000244|PDB:5KNN,
ECO:0000269|PubMed:27622773,
ECO:0000269|Ref.22}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000255|HAMAP-Rule:MF_03133,
ECO:0000269|Ref.7}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 8 8 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 19 19 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 399 399 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 555 555 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 876 876 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 160 160 G -> GTYLYSFVR (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_057201.
VAR_SEQ 869 869 K -> KATQGPGSPPLGLISSL (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_057202.
VARIANT 71 71 N -> Y (in CMT2N; dbSNP:rs387906792).
{ECO:0000269|PubMed:22206013}.
/FTId=VAR_067084.
VARIANT 81 81 K -> T (in EIEE29; hypomorphic allele;
results in only 2-fold reduction in
aminoacylation efficiency;
dbSNP:rs786205157).
{ECO:0000269|PubMed:25817015}.
/FTId=VAR_073719.
VARIANT 275 275 G -> D (in dbSNP:rs11537667).
/FTId=VAR_028204.
VARIANT 329 329 R -> H (in CMT2N; severely reduces enzyme
activity; dbSNP:rs267606621).
{ECO:0000269|PubMed:20045102,
ECO:0000269|PubMed:22009580}.
/FTId=VAR_063527.
VARIANT 608 608 T -> M (found in a patient with distal
hereditary motor neuropathy; unknown
pathological significance).
{ECO:0000269|PubMed:24627108}.
/FTId=VAR_073293.
VARIANT 751 751 R -> G (in EIEE29; results in 10-fold
reduction in aminoacylation efficiency;
dbSNP:rs143370729).
{ECO:0000269|PubMed:25817015}.
/FTId=VAR_073720.
MUTAGEN 448 448 A->Q: Decreases misincorporation of Cys
instead of Ala.
{ECO:0000269|PubMed:27622773}.
CONFLICT 82 82 H -> Q (in Ref. 1; BAA06808).
{ECO:0000305}.
CONFLICT 334 334 Y -> C (in Ref. 2; BAG61157).
{ECO:0000305}.
CONFLICT 763 763 A -> T (in Ref. 2; BAG61157).
{ECO:0000305}.
CONFLICT 867 867 S -> T (in Ref. 3; BAD96544).
{ECO:0000305}.
HELIX 7 20 {ECO:0000244|PDB:4XEM}.
STRAND 34 36 {ECO:0000244|PDB:5KNN}.
HELIX 45 49 {ECO:0000244|PDB:4XEM}.
HELIX 50 53 {ECO:0000244|PDB:4XEM}.
HELIX 62 65 {ECO:0000244|PDB:4XEM}.
STRAND 68 76 {ECO:0000244|PDB:4XEM}.
STRAND 78 81 {ECO:0000244|PDB:4XEO}.
HELIX 85 87 {ECO:0000244|PDB:4XEM}.
STRAND 90 93 {ECO:0000244|PDB:4XEM}.
STRAND 96 109 {ECO:0000244|PDB:4XEM}.
HELIX 111 123 {ECO:0000244|PDB:4XEM}.
HELIX 130 132 {ECO:0000244|PDB:4XEM}.
STRAND 133 138 {ECO:0000244|PDB:4XEM}.
HELIX 142 144 {ECO:0000244|PDB:4XEM}.
HELIX 150 158 {ECO:0000244|PDB:4XEM}.
HELIX 163 165 {ECO:0000244|PDB:4XEM}.
STRAND 166 169 {ECO:0000244|PDB:4XEM}.
HELIX 171 174 {ECO:0000244|PDB:4XEM}.
STRAND 178 195 {ECO:0000244|PDB:4XEM}.
HELIX 201 203 {ECO:0000244|PDB:4XEM}.
TURN 204 207 {ECO:0000244|PDB:4XEM}.
STRAND 211 224 {ECO:0000244|PDB:4XEM}.
STRAND 230 243 {ECO:0000244|PDB:4XEM}.
HELIX 244 251 {ECO:0000244|PDB:4XEM}.
HELIX 257 259 {ECO:0000244|PDB:4XEM}.
TURN 261 263 {ECO:0000244|PDB:4XEM}.
HELIX 264 274 {ECO:0000244|PDB:4XEM}.
HELIX 284 286 {ECO:0000244|PDB:4XEM}.
HELIX 291 310 {ECO:0000244|PDB:4XEM}.
HELIX 319 339 {ECO:0000244|PDB:4XEM}.
TURN 343 345 {ECO:0000244|PDB:4XEM}.
HELIX 346 349 {ECO:0000244|PDB:4XEM}.
HELIX 350 357 {ECO:0000244|PDB:4XEM}.
TURN 358 360 {ECO:0000244|PDB:4XEM}.
HELIX 362 365 {ECO:0000244|PDB:4XEM}.
HELIX 368 383 {ECO:0000244|PDB:4XEM}.
HELIX 386 399 {ECO:0000244|PDB:5KNN}.
TURN 400 402 {ECO:0000244|PDB:5KNN}.
HELIX 408 416 {ECO:0000244|PDB:5KNN}.
HELIX 422 431 {ECO:0000244|PDB:5KNN}.
HELIX 438 450 {ECO:0000244|PDB:5KNN}.
HELIX 759 782 {ECO:0000244|PDB:5T76}.
HELIX 789 804 {ECO:0000244|PDB:5T76}.
HELIX 809 851 {ECO:0000244|PDB:5T76}.
STRAND 856 861 {ECO:0000244|PDB:5T76}.
HELIX 868 881 {ECO:0000244|PDB:5T76}.
STRAND 886 893 {ECO:0000244|PDB:5T76}.
TURN 894 897 {ECO:0000244|PDB:5T76}.
STRAND 898 904 {ECO:0000244|PDB:5T76}.
HELIX 907 912 {ECO:0000244|PDB:5T76}.
HELIX 916 924 {ECO:0000244|PDB:5T76}.
TURN 925 928 {ECO:0000244|PDB:5T76}.
STRAND 929 933 {ECO:0000244|PDB:5T76}.
STRAND 935 943 {ECO:0000244|PDB:5T76}.
HELIX 945 947 {ECO:0000244|PDB:5T76}.
HELIX 948 960 {ECO:0000244|PDB:5T76}.
SEQUENCE 968 AA; 106810 MW; 8683F111CEE42506 CRC64;
MDSTLTASEI RQRFIDFFKR NEHTYVHSSA TIPLDDPTLL FANAGMNQFK PIFLNTIDPS
HPMAKLSRAA NTQKCIRAGG KHNDLDDVGK DVYHHTFFEM LGSWSFGDYF KELACKMALE
LLTQEFGIPI ERLYVTYFGG DEAAGLEADL ECKQIWQNLG LDDTKILPGN MKDNFWEMGD
TGPCGPCSEI HYDRIGGRDA AHLVNQDDPN VLEIWNLVFI QYNREADGIL KPLPKKSIDT
GMGLERLVSV LQNKMSNYDT DLFVPYFEAI QKGTGARPYT GKVGAEDADG IDMAYRVLAD
HARTITVALA DGGRPDNTGR GYVLRRILRR AVRYAHEKLN ASRGFFATLV DVVVQSLGDA
FPELKKDPDM VKDIINEEEV QFLKTLSRGR RILDRKIQSL GDSKTIPGDT AWLLYDTYGF
PVDLTGLIAE EKGLVVDMDG FEEERKLAQL KSQGKGAGGE DLIMLDIYAI EELRARGLEV
TDDSPKYNYH LDSSGSYVFE NTVATVMALR REKMFVEEVS TGQECGVVLD KTCFYAEQGG
QIYDEGYLVK VDDSSEDKTE FTVKNAQVRG GYVLHIGTIY GDLKVGDQVW LFIDEPRRRP
IMSNHTATHI LNFALRSVLG EADQKGSLVA PDRLRFDFTA KGAMSTQQIK KAEEIANEMI
EAAKAVYTQD CPLAAAKAIQ GLRAVFDETY PDPVRVVSIG VPVSELLDDP SGPAGSLTSV
EFCGGTHLRN SSHAGAFVIV TEEAIAKGIR RIVAVTGAEA QKALRKAESL KKCLSVMEAK
VKAQTAPNKD VQREIADLGE ALATAVIPQW QKDELRETLK SLKKVMDDLD RASKADVQKR
VLEKTKQFID SNPNQPLVIL EMESGASAKA LNEALKLFKM HSPQTSAMLF TVDNEAGKIT
CLCQVPQNAA NRGLKASEWV QQVSGLMDGK GGGKDVSAQA TGKNVGCLQE ALQLATSFAQ
LRLGDVKN


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