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Glycine--tRNA ligase (EC 3.6.1.17) (EC 6.1.1.14) (Diadenosine tetraphosphate synthetase) (AP-4-A synthetase) (Glycyl-tRNA synthetase) (GlyRS)

 GARS_HUMAN              Reviewed;         739 AA.
P41250; B3KQA2; B4DIA0; Q969Y1;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 3.
18-JUL-2018, entry version 193.
RecName: Full=Glycine--tRNA ligase;
EC=3.6.1.17 {ECO:0000269|PubMed:19710017};
EC=6.1.1.14 {ECO:0000269|PubMed:17544401};
AltName: Full=Diadenosine tetraphosphate synthetase;
Short=AP-4-A synthetase;
AltName: Full=Glycyl-tRNA synthetase;
Short=GlyRS;
Name=GARS;
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 VARIANT ALA-42.
PubMed=7962006;
Shiba K., Schimmel P., Motegi H., Noda T.;
"Human glycyl-tRNA synthetase. Wide divergence of primary structure
from bacterial counterpart and species-specific aminoacylation.";
J. Biol. Chem. 269:30049-30055(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-42.
PubMed=7753621; DOI=10.1093/nar/23.8.1307;
Williams J.H., Osvath S.R., Khong T.-F., Pearse M.J., Power D.A.;
"Cloning, sequencing and bacterial expression of human glycine tRNA
synthetase.";
Nucleic Acids Res. 23:1307-1310(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-42.
TISSUE=Embryo, and Hippocampus;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-42.
TISSUE=Eye, and Muscle;
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]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-739, AND VARIANT ALA-42.
PubMed=7961834;
Ge Q., Trieu E.P., Targoff I.N.;
"Primary structure and functional expression of human glycyl-tRNA
synthetase, an autoantigen in myositis.";
J. Biol. Chem. 269:28790-28797(1994).
[7]
SUBCELLULAR LOCATION, VARIANTS CMT2D GLY-125 AND ARG-294,
CHARACTERIZATION OF VARIANTS CMT2D GLY-125 AND ARG-294, VARIANTS HMN5A
PRO-183; ARG-472 AND ARG-580, AND CHARACTERIZATION OF VARIANTS HMN5A
PRO-183; ARG-472 AND ARG-580.
PubMed=17035524; DOI=10.1523/JNEUROSCI.1671-06.2006;
Antonellis A., Lee-Lin S.Q., Wasterlain A., Leo P., Quezado M.,
Goldfarb L.G., Myung K., Burgess S., Fischbeck K.H., Green E.D.;
"Functional analyses of glycyl-tRNA synthetase mutations suggest a key
role for tRNA-charging enzymes in peripheral axons.";
J. Neurosci. 26:10397-10406(2006).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-204 AND LYS-501, 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).
[9]
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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 AND THR-736, VARIANT
[LARGE SCALE ANALYSIS] ALA-42, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=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).
[11]
SUBCELLULAR LOCATION, VARIANTS CMT2D VAL-111; ASN-200; PHE-265;
ARG-294; LEU-298; PHE-334; ARG-472; ASN-554; ARG-580 AND ALA-652,
VARIANT LEU-635, CHARACTERIZATION OF VARIANTS CMT2D VAL-111; GLY-125;
PRO-183; ASN-200; PHE-265; ARG-294; LEU-298; PHE-334; ARG-472;
ASN-554; ARG-580 AND ALA-652, AND CHARACTERIZATION OF VARIANT LEU-635.
PubMed=25168514; DOI=10.1002/humu.22681;
Griffin L.B., Sakaguchi R., McGuigan D., Gonzalez M.A., Searby C.,
Zuchner S., Hou Y.M., Antonellis A.;
"Impaired function is a common feature of neuropathy-associated
glycyl-tRNA synthetase mutations.";
Hum. Mutat. 35:1363-1371(2014).
[12]
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).
[13]
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).
[14]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 55-739, FUNCTION, SUBUNIT,
CHARACTERIZATION OF VARIANT LEU-635, CATALYTIC ACTIVITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=17544401; DOI=10.1016/j.febslet.2007.05.046;
Cader M.Z., Ren J., James P.A., Bird L.E., Talbot K., Stammers D.K.;
"Crystal structure of human wildtype and S581L-mutant glycyl-tRNA
synthetase, an enzyme underlying distal spinal muscular atrophy.";
FEBS Lett. 581:2959-2964(2007).
[15]
X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 55-739, VARIANT ARG-580, AND
SUBUNIT.
PubMed=17545306; DOI=10.1073/pnas.0703908104;
Xie W., Nangle L.A., Zhang W., Schimmel P., Yang X.-L.;
"Long-range structural effects of a Charcot-Marie-Tooth disease-
causing mutation in human glycyl-tRNA synthetase.";
Proc. Natl. Acad. Sci. U.S.A. 104:9976-9981(2007).
[16]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 55-739 IN COMPLEX WITH ATP;
SUBSTRATE AND SUBSTRATE ANALOGS, AND FUNCTION.
PubMed=19710017; DOI=10.1074/jbc.M109.030692;
Guo R.-T., Chong Y.E., Guo M., Yang X.-L.;
"Crystal structures and biochemical analyses suggest a unique
mechanism and role for human glycyl-tRNA synthetase in Ap4A
homeostasis.";
J. Biol. Chem. 284:28968-28976(2009).
[17]
VARIANTS CMT2D GLY-125 AND ARG-294, VARIANTS HMN5A PRO-183 AND
ARG-580, AND TISSUE SPECIFICITY.
PubMed=12690580; DOI=10.1086/375039;
Antonellis A., Ellsworth R.E., Sambuughin N., Puls I., Abel A.,
Lee-Lin S.Q., Jordanova A., Kremensky I., Christodoulou K.,
Middleton L.T., Sivakumar K., Ionasescu V., Funalot B., Vance J.M.,
Goldfarb L.G., Fischbeck K.H., Green E.D.;
"Glycyl tRNA synthetase mutations in Charcot-Marie-Tooth disease type
2D and distal spinal muscular atrophy type V.";
Am. J. Hum. Genet. 72:1293-1299(2003).
[18]
VARIANT LEU-635, AND VARIANTS CMT2D PHE-334 AND ALA-652.
PubMed=17101916; DOI=10.1212/01.wnl.0000242619.52335.bc;
James P.A., Cader M.Z., Muntoni F., Childs A.M., Crow Y.J., Talbot K.;
"Severe childhood SMA and axonal CMT due to anticodon binding domain
mutations in the GARS gene.";
Neurology 67:1710-1712(2006).
[19]
VARIANT CMT2D VAL-111.
PubMed=17663003; DOI=10.1016/j.jns.2007.06.047;
Rohkamm B., Reilly M.M., Lochmueller H., Schlotter-Weigel B.,
Barisic N., Schoels L., Nicholson G., Pareyson D., Laura M.,
Janecke A.R., Miltenberger-Miltenyi G., John E., Fischer C., Grill F.,
Wakeling W., Davis M., Pieber T.R., Auer-Grumbach M.;
"Further evidence for genetic heterogeneity of distal HMN type V, CMT2
with predominant hand involvement and Silver syndrome.";
J. Neurol. Sci. 263:100-106(2007).
[20]
VARIANT CMT2D LEU-298.
PubMed=20169446; DOI=10.1007/s00415-010-5491-x;
Hamaguchi A., Ishida C., Iwasa K., Abe A., Yamada M.;
"Charcot-Marie-Tooth disease type 2D with a novel glycyl-tRNA
synthetase gene (GARS) mutation.";
J. Neurol. 257:1202-1204(2010).
[21]
VARIANTS HMN5A ASN-200 AND PHE-265.
PubMed=23279345; DOI=10.1111/j.1529-8027.2012.00442.x;
Lee H.J., Park J., Nakhro K., Park J.M., Hur Y.M., Choi B.O.,
Chung K.W.;
"Two novel mutations of GARS in Korean families with distal hereditary
motor neuropathy type V.";
J. Peripher. Nerv. Syst. 17:418-421(2012).
[22]
VARIANT HMN5A ARG-472.
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).
[23]
VARIANT CMT2D PHE-334.
PubMed=24604904; DOI=10.1136/jnnp-2013-306740;
Klein C.J., Middha S., Duan X., Wu Y., Litchy W.J., Gu W., Dyck P.J.,
Gavrilova R.H., Smith D.I., Kocher J.P., Dyck P.J.;
"Application of whole exome sequencing in undiagnosed inherited
polyneuropathies.";
J. Neurol. Neurosurg. Psych. 85:1265-1272(2014).
[24]
VARIANTS CMT2D TYR-200 AND ARG-292.
PubMed=26244500; DOI=10.1371/journal.pone.0133423;
Liao Y.C., Liu Y.T., Tsai P.C., Chang C.C., Huang Y.H., Soong B.W.,
Lee Y.C.;
"Two novel de novo gars mutations cause early-onset axonal Charcot-
Marie-tooth disease.";
PLoS ONE 10:E0133423-E0133423(2015).
[25]
CHARACTERIZATION OF VARIANTS CMT2D GLY-125 AND ARG-294, AND
CHARACTERIZATION OF VARIANT HMN5A PRO-183.
PubMed=26503042; DOI=10.1038/nature15510;
He W., Bai G., Zhou H., Wei N., White N.M., Lauer J., Liu H., Shi Y.,
Dumitru C.D., Lettieri K., Shubayev V., Jordanova A.,
Guergueltcheva V., Griffin P.R., Burgess R.W., Pfaff S.L., Yang X.L.;
"CMT2D neuropathy is linked to the neomorphic binding activity of
glycyl-tRNA synthetase.";
Nature 526:710-714(2015).
[26]
ERRATUM.
PubMed=26789244; DOI=10.1038/nature16499;
He W., Bai G., Zhou H., Wei N., White N.M., Lauer J., Liu H., Shi Y.,
Dan Dumitru C., Lettieri K., Shubayev V., Jordanova A.,
Guergueltcheva V., Griffin P.R., Burgess R.W., Pfaff S.L., Yang X.L.;
"Corrigendum: CMT2D neuropathy is linked to the neomorphic binding
activity of glycyl-tRNA synthetase.";
Nature 532:402-402(2016).
[27]
VARIANT GLN-310, CHARACTERIZATION OF VARIANT GLN-310, CATALYTIC
ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=28675565; DOI=10.1002/humu.23287;
Oprescu S.N., Chepa-Lotrea X., Takase R., Golas G., Markello T.C.,
Adams D.R., Toro C., Gropman A.L., Hou Y.M., Malicdan M.C.V.,
Gahl W.A., Tifft C.J., Antonellis A.;
"Compound heterozygosity for loss-of-function GARS variants results in
a multisystem developmental syndrome that includes severe growth
retardation.";
Hum. Mutat. 38:1412-1420(2017).
[28]
VARIANTS ILE-268 AND CYS-412.
PubMed=28594869; DOI=10.1371/journal.pone.0178125;
Nafisinia M., Riley L.G., Gold W.A., Bhattacharya K., Broderick C.R.,
Thorburn D.R., Simons C., Christodoulou J.;
"Compound heterozygous mutations in glycyl-tRNA synthetase (GARS)
cause mitochondrial respiratory chain dysfunction.";
PLoS ONE 12:E0178125-E0178125(2017).
-!- FUNCTION: Catalyzes the ligation of glycine to the 3'-end of its
cognate tRNA. Also produces diadenosine tetraphosphate (Ap4A), a
universal pleiotropic signaling molecule needed for cell
regulation pathways, by direct condensation of 2 ATPs.
{ECO:0000269|PubMed:17544401, ECO:0000269|PubMed:19710017,
ECO:0000269|PubMed:28675565}.
-!- CATALYTIC ACTIVITY: ATP + glycine + tRNA(Gly) = AMP + diphosphate
+ glycyl-tRNA(Gly). {ECO:0000269|PubMed:17544401,
ECO:0000269|PubMed:28675565}.
-!- CATALYTIC ACTIVITY: P(1),P(4)-bis(5'-guanosyl) tetraphosphate +
H(2)O = GTP + GMP. {ECO:0000269|PubMed:19710017}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.3 uM for tRNA(Gly(GCC)) {ECO:0000269|PubMed:17544401};
KM=15 uM for glycine {ECO:0000269|PubMed:17544401};
KM=0.74 uM for tRNA(Gly) {ECO:0000269|PubMed:28675565};
Note=Kcat is 0.049 (sec-1) for aminoacylation for tRNA(Gly).
{ECO:0000269|PubMed:28675565};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17544401,
ECO:0000269|PubMed:17545306, ECO:0000269|PubMed:19710017}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-724143, EBI-724143;
Q9CZD3:Gars (xeno); NbExp=2; IntAct=EBI-724143, EBI-8321941;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17035524}.
Cell projection, axon {ECO:0000269|PubMed:17035524,
ECO:0000269|PubMed:25168514}. Secreted
{ECO:0000250|UniProtKB:Q9CZD3}. Secreted, exosome
{ECO:0000250|UniProtKB:Q9CZD3}. Note=Secreted by motor neuron,
possibly through the exosome pathway (By similarity). In
transfected COS7 cells, not detected in mitochondria, nor in Golgi
apparatus (PubMed:17035524). {ECO:0000250|UniProtKB:Q9CZD3,
ECO:0000269|PubMed:17035524}.
-!- TISSUE SPECIFICITY: Widely expressed, including in brain and
spinal cord. {ECO:0000269|PubMed:12690580}.
-!- DISEASE: Charcot-Marie-Tooth disease 2D (CMT2D) [MIM:601472]: A
dominant 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:12690580,
ECO:0000269|PubMed:17035524, ECO:0000269|PubMed:17101916,
ECO:0000269|PubMed:17663003, ECO:0000269|PubMed:20169446,
ECO:0000269|PubMed:24604904, ECO:0000269|PubMed:25168514,
ECO:0000269|PubMed:26244500, ECO:0000269|PubMed:26503042}.
Note=The disease is caused by mutations affecting the gene
represented in this entry. Contrary to the wild-type protein,
CMT2D variants Gly-125 and Arg-294 strongly interact with NRP1.
This interaction may compete out VEGFA binding and inhibits VEGFA-
NRP1 signling which is essential for motor neuron survival, as
suggested by experiments done in a mouse model.
{ECO:0000269|PubMed:26503042}.
-!- DISEASE: Neuronopathy, distal hereditary motor, 5A (HMN5A)
[MIM:600794]: A disorder characterized by distal muscular atrophy
mainly affecting the upper extremities, in contrast to other
distal motor neuronopathies. These constitute a heterogeneous
group of neuromuscular diseases caused by selective degeneration
of motor neurons in the anterior horn of the spinal cord, without
sensory deficit in the posterior horn. The overall clinical
picture consists of a classical distal muscular atrophy syndrome
in the legs without clinical sensory loss. The disease starts with
weakness and wasting of distal muscles of the anterior tibial and
peroneal compartments of the legs. Later on, weakness and atrophy
may expand to the proximal muscles of the lower limbs and/or to
the distal upper limbs. {ECO:0000269|PubMed:12690580,
ECO:0000269|PubMed:17035524, ECO:0000269|PubMed:23279345,
ECO:0000269|PubMed:24627108, ECO:0000269|PubMed:26503042}.
Note=The disease is caused by mutations affecting the gene
represented in this entry. Contrary to the wild-type protein,
HMN5A variant Pro-183 strongly interacts with NRP1. This
interaction may compete out VEGFA binding and inhibits VEGFA-NRP1
signling which is essential for motor neuron survival, as
suggested by experiments done in a mouse model.
{ECO:0000269|PubMed:26503042}.
-!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
family. {ECO:0000305}.
-!- CAUTION: According to a report, variant Leu-635 induces reduced
activity (PubMed:17544401). According to another report, it does
not affect function (PubMed:25168514).
{ECO:0000269|PubMed:17544401, ECO:0000269|PubMed:25168514}.
-!- SEQUENCE CAUTION:
Sequence=AAA57001.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAA86443.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Inherited peripheral neuropathies mutation db;
URL="http://www.molgen.ua.ac.be/CMTMutations/";
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EMBL; D30658; BAA06338.1; -; mRNA.
EMBL; U09510; AAA86443.1; ALT_INIT; mRNA.
EMBL; AK074524; BAG51964.1; -; mRNA.
EMBL; AK295490; BAG58412.1; -; mRNA.
EMBL; AC005154; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC006969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC004976; AAC71652.1; -; Genomic_DNA.
EMBL; BC007722; AAH07722.1; -; mRNA.
EMBL; BC007755; AAH07755.1; -; mRNA.
EMBL; U09587; AAA57001.1; ALT_INIT; mRNA.
CCDS; CCDS43564.1; -.
PIR; A55314; A55314.
RefSeq; NP_001303701.1; NM_001316772.1.
RefSeq; NP_002038.2; NM_002047.3.
UniGene; Hs.404321; -.
PDB; 2PME; X-ray; 2.90 A; A=55-739.
PDB; 2PMF; X-ray; 2.85 A; A=55-739.
PDB; 2Q5H; X-ray; 3.00 A; A=55-739.
PDB; 2Q5I; X-ray; 2.80 A; A=55-739.
PDB; 2ZT5; X-ray; 2.50 A; A=55-739.
PDB; 2ZT6; X-ray; 3.08 A; A=55-739.
PDB; 2ZT7; X-ray; 2.70 A; A=55-739.
PDB; 2ZT8; X-ray; 3.35 A; A=55-739.
PDB; 2ZXF; X-ray; 3.40 A; A=55-739.
PDB; 4KQE; X-ray; 2.74 A; A=55-739.
PDB; 4KR2; X-ray; 3.29 A; A=114-739.
PDB; 4KR3; X-ray; 3.24 A; A=114-739.
PDB; 4QEI; X-ray; 2.88 A; A=118-739.
PDB; 5E6M; X-ray; 2.93 A; A/B=55-739.
PDBsum; 2PME; -.
PDBsum; 2PMF; -.
PDBsum; 2Q5H; -.
PDBsum; 2Q5I; -.
PDBsum; 2ZT5; -.
PDBsum; 2ZT6; -.
PDBsum; 2ZT7; -.
PDBsum; 2ZT8; -.
PDBsum; 2ZXF; -.
PDBsum; 4KQE; -.
PDBsum; 4KR2; -.
PDBsum; 4KR3; -.
PDBsum; 4QEI; -.
PDBsum; 5E6M; -.
ProteinModelPortal; P41250; -.
SMR; P41250; -.
BioGrid; 108887; 91.
DIP; DIP-50471N; -.
IntAct; P41250; 26.
MINT; P41250; -.
STRING; 9606.ENSP00000373918; -.
DrugBank; DB00145; Glycine.
MoonProt; P41250; -.
iPTMnet; P41250; -.
PhosphoSitePlus; P41250; -.
SwissPalm; P41250; -.
BioMuta; GARS; -.
DMDM; 313104283; -.
EPD; P41250; -.
MaxQB; P41250; -.
PaxDb; P41250; -.
PeptideAtlas; P41250; -.
PRIDE; P41250; -.
ProteomicsDB; 55453; -.
DNASU; 2617; -.
Ensembl; ENST00000389266; ENSP00000373918; ENSG00000106105.
GeneID; 2617; -.
KEGG; hsa:2617; -.
UCSC; uc003tbm.4; human.
CTD; 2617; -.
DisGeNET; 2617; -.
EuPathDB; HostDB:ENSG00000106105.13; -.
GeneCards; GARS; -.
GeneReviews; GARS; -.
H-InvDB; HIX0006570; -.
HGNC; HGNC:4162; GARS.
HPA; HPA017896; -.
HPA; HPA019097; -.
MalaCards; GARS; -.
MIM; 600287; gene.
MIM; 600794; phenotype.
MIM; 601472; phenotype.
neXtProt; NX_P41250; -.
OpenTargets; ENSG00000106105; -.
Orphanet; 99938; Autosomal dominant Charcot-Marie-Tooth disease type 2D.
Orphanet; 139536; Distal hereditary motor neuropathy type 5.
PharmGKB; PA28575; -.
eggNOG; KOG2298; Eukaryota.
eggNOG; COG0423; LUCA.
GeneTree; ENSGT00390000016949; -.
HOGENOM; HOG000242015; -.
HOVERGEN; HBG036190; -.
InParanoid; P41250; -.
KO; K01880; -.
OMA; EPSYGID; -.
OrthoDB; EOG091G02U0; -.
PhylomeDB; P41250; -.
TreeFam; TF343504; -.
BRENDA; 6.1.1.14; 2681.
Reactome; R-HSA-379716; Cytosolic tRNA aminoacylation.
Reactome; R-HSA-379726; Mitochondrial tRNA aminoacylation.
ChiTaRS; GARS; human.
EvolutionaryTrace; P41250; -.
GeneWiki; Glycine%E2%80%94tRNA_ligase; -.
GenomeRNAi; 2617; -.
PMAP-CutDB; P41250; -.
PRO; PR:P41250; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000106105; -.
CleanEx; HS_GARS; -.
ExpressionAtlas; P41250; baseline and differential.
Genevisible; P41250; HS.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; ISS:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
GO; GO:0030141; C:secretory granule; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004081; F:bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity; IDA:UniProtKB.
GO; GO:0004820; F:glycine-tRNA ligase activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046983; F:protein dimerization activity; IDA:UniProtKB.
GO; GO:0015966; P:diadenosine tetraphosphate biosynthetic process; IDA:UniProtKB.
GO; GO:0070150; P:mitochondrial glycyl-tRNA aminoacylation; IBA:GO_Central.
GO; GO:0006418; P:tRNA aminoacylation for protein translation; IMP:UniProtKB.
CDD; cd00774; GlyRS-like_core; 1.
Gene3D; 3.40.50.800; -; 1.
InterPro; IPR002314; aa-tRNA-synt_IIb.
InterPro; IPR006195; aa-tRNA-synth_II.
InterPro; IPR004154; Anticodon-bd.
InterPro; IPR036621; Anticodon-bd_dom_sf.
InterPro; IPR027031; Gly-tRNA_synthase/POLG2.
InterPro; IPR033731; GlyRS-like_core.
InterPro; IPR009068; S15_NS1_RNA-bd.
InterPro; IPR002315; tRNA-synt_gly.
InterPro; IPR000738; WHEP-TRS_dom.
PANTHER; PTHR10745; PTHR10745; 1.
Pfam; PF03129; HGTP_anticodon; 1.
Pfam; PF00587; tRNA-synt_2b; 1.
Pfam; PF00458; WHEP-TRS; 1.
PRINTS; PR01043; TRNASYNTHGLY.
SMART; SM00991; WHEP-TRS; 1.
SUPFAM; SSF47060; SSF47060; 1.
TIGRFAMs; TIGR00389; glyS_dimeric; 1.
PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PROSITE; PS00762; WHEP_TRS_1; 1.
PROSITE; PS51185; WHEP_TRS_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding;
Cell projection; Charcot-Marie-Tooth disease; Complete proteome;
Cytoplasm; Disease mutation; Hydrolase; Ligase; Neurodegeneration;
Neuropathy; Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
Reference proteome; Secreted.
CHAIN 1 739 Glycine--tRNA ligase.
/FTId=PRO_0000072998.
DOMAIN 63 119 WHEP-TRS. {ECO:0000255|PROSITE-
ProRule:PRU00531}.
NP_BIND 331 333 ATP. {ECO:0000269|PubMed:19710017}.
NP_BIND 341 346 ATP. {ECO:0000269|PubMed:19710017}.
NP_BIND 457 458 ATP. {ECO:0000269|PubMed:19710017}.
NP_BIND 580 583 ATP. {ECO:0000269|PubMed:19710017}.
REGION 346 350 Substrate binding.
REGION 576 580 Substrate binding.
BINDING 213 213 Substrate. {ECO:0000269|PubMed:19710017}.
BINDING 299 299 Substrate. {ECO:0000269|PubMed:19710017}.
BINDING 435 435 Substrate; via carbonyl oxygen.
{ECO:0000269|PubMed:19710017}.
MOD_RES 35 35 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 204 204 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 453 453 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9CZD3}.
MOD_RES 501 501 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 700 700 Phosphoserine.
{ECO:0000250|UniProtKB:Q9CZD3}.
MOD_RES 736 736 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
VARIANT 42 42 P -> A (in dbSNP:rs1049402).
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7753621,
ECO:0000269|PubMed:7961834,
ECO:0000269|PubMed:7962006}.
/FTId=VAR_054865.
VARIANT 111 111 A -> V (in CMT2D; shows a reduction in
aminoacylation activity;
dbSNP:rs370531212).
{ECO:0000269|PubMed:17663003,
ECO:0000269|PubMed:25168514}.
/FTId=VAR_073187.
VARIANT 125 125 E -> G (in CMT2D; phenotype overlapping
with DSMA-V; complements the defect of
the wild-type gene in yeast; contrary to
the wild-type protein, strongly binds to
NRP1 and competes with VEGFA for NRP1-
binding; dbSNP:rs137852645).
{ECO:0000269|PubMed:12690580,
ECO:0000269|PubMed:17035524,
ECO:0000269|PubMed:25168514,
ECO:0000269|PubMed:26503042}.
/FTId=VAR_018718.
VARIANT 183 183 L -> P (in HMN5A; does not complement the
defect of the wild-type gene in yeast;
contrary to the wild-type protein,
strongly interacts with NRP1;
dbSNP:rs137852644).
{ECO:0000269|PubMed:12690580,
ECO:0000269|PubMed:17035524,
ECO:0000269|PubMed:25168514,
ECO:0000269|PubMed:26503042}.
/FTId=VAR_018719.
VARIANT 200 200 D -> N (in CMT2D and HMN5A; shows a large
reduction in aminoacylation activity).
{ECO:0000269|PubMed:23279345,
ECO:0000269|PubMed:25168514}.
/FTId=VAR_073188.
VARIANT 200 200 D -> Y (in CMT2D).
{ECO:0000269|PubMed:26244500}.
/FTId=VAR_074016.
VARIANT 265 265 S -> F (in CMT2D and HMN5A; shows a large
reduction in aminoacylation activity;
demonstrates a change in the subcellular
location pattern; does not associate with
granules). {ECO:0000269|PubMed:23279345,
ECO:0000269|PubMed:25168514}.
/FTId=VAR_073189.
VARIANT 268 268 T -> I (found in a patient with mild left
ventricular posterior wall hypertrophy,
exercise intolerance and lactic acidosis;
unknown pathological significance;
dbSNP:rs2230310).
{ECO:0000269|PubMed:28594869}.
/FTId=VAR_054866.
VARIANT 292 292 M -> R (in CMT2D).
{ECO:0000269|PubMed:26244500}.
/FTId=VAR_074017.
VARIANT 294 294 G -> R (in CMT2D; shows a large reduction
in aminoacylation activity; does not
impair transcription or translation or
protein stability; contrary to the wild-
type protein, strongly interacts with
NRP1; dbSNP:rs137852643).
{ECO:0000269|PubMed:12690580,
ECO:0000269|PubMed:17035524,
ECO:0000269|PubMed:25168514,
ECO:0000269|PubMed:26503042}.
/FTId=VAR_018720.
VARIANT 298 298 P -> L (in CMT2D; shows a large reduction
in aminoacylation activity; demonstrates
a change in subcellular location pattern;
does not associate with granules;
dbSNP:rs137852648).
{ECO:0000269|PubMed:20169446,
ECO:0000269|PubMed:25168514}.
/FTId=VAR_073190.
VARIANT 310 310 R -> Q (probable disease-associated
mutation found in a patient with growth
retardation, microcephaly, thinning of
the corpus callosum, decreased white
matter and brain stem involvement, as
well as large calvaria, cerebellar vermis
atrophy, dysmorphic features, prominent
epicanthal folds, hypotelorism, high-
arched palate, delayed motor milestones,
apnea and sparse thin scalp hair; reduces
to less than 1% aminoacylation activity;
dbSNP:rs1135401748).
{ECO:0000269|PubMed:28675565}.
/FTId=VAR_079827.
VARIANT 334 334 I -> F (in CMT2D; shows a large reduction
in aminoacylation activity; demonstrates
a change in subcellular location pattern;
does not associate with granules; unknown
pathological significance).
{ECO:0000269|PubMed:17101916,
ECO:0000269|PubMed:24604904,
ECO:0000269|PubMed:25168514}.
/FTId=VAR_073191.
VARIANT 388 388 R -> Q (in dbSNP:rs17159287).
/FTId=VAR_054867.
VARIANT 412 412 R -> C (found in a patient with mild left
ventricular posterior wall hypertrophy,
exercise intolerance and lactic acidosis;
unknown pathological significance;
dbSNP:rs770924455).
{ECO:0000269|PubMed:28594869}.
/FTId=VAR_079828.
VARIANT 472 472 H -> R (in HMN5A; shows a large reduction
in aminoacylation activity; does not
complement the defect of the wild-type
gene in yeast; dbSNP:rs1060502838).
{ECO:0000269|PubMed:17035524,
ECO:0000269|PubMed:24627108,
ECO:0000269|PubMed:25168514}.
/FTId=VAR_073192.
VARIANT 554 554 D -> N (in CMT2D; demonstrates no change
in subcellular location pattern;
dbSNP:rs137852647).
{ECO:0000269|PubMed:25168514}.
/FTId=VAR_073193.
VARIANT 580 580 G -> R (in HMN5A; higher dimerization
stability; loss of activity; shows a
large reduction in aminoacylation
activity; dbSNP:rs137852646).
{ECO:0000269|PubMed:12690580,
ECO:0000269|PubMed:17035524,
ECO:0000269|PubMed:17545306,
ECO:0000269|PubMed:25168514}.
/FTId=VAR_018721.
VARIANT 598 598 G -> A (in HMN5A; unknown pathological
significance; dbSNP:rs766280100).
{ECO:0000269|PubMed:17101916}.
/FTId=VAR_079829.
VARIANT 635 635 S -> L (polymorphism; has no effect on
subcellular localization; results in
reduced activity; dbSNP:rs201358272).
{ECO:0000269|PubMed:17101916,
ECO:0000269|PubMed:17544401,
ECO:0000269|PubMed:25168514}.
/FTId=VAR_073194.
VARIANT 652 652 G -> A (in CMT2D; shows a large reduction
in aminoacylation activity; demonstrates
a change in subcellular location pattern;
does not associate with granules).
{ECO:0000269|PubMed:17101916,
ECO:0000269|PubMed:25168514}.
/FTId=VAR_073195.
CONFLICT 9 18 Missing (in Ref. 3; BAG58412).
{ECO:0000305}.
CONFLICT 205 205 D -> G (in Ref. 3; BAG51964).
{ECO:0000305}.
CONFLICT 530 530 M -> I (in Ref. 2; AAA86443).
{ECO:0000305}.
CONFLICT 634 634 L -> S (in Ref. 3; BAG51964).
{ECO:0000305}.
TURN 62 64 {ECO:0000244|PDB:5E6M}.
HELIX 65 80 {ECO:0000244|PDB:5E6M}.
TURN 81 83 {ECO:0000244|PDB:5E6M}.
HELIX 95 112 {ECO:0000244|PDB:5E6M}.
HELIX 121 130 {ECO:0000244|PDB:2ZT5}.
STRAND 133 136 {ECO:0000244|PDB:2ZT5}.
HELIX 139 141 {ECO:0000244|PDB:2ZT5}.
STRAND 148 150 {ECO:0000244|PDB:2ZT5}.
HELIX 152 168 {ECO:0000244|PDB:2ZT5}.
HELIX 170 173 {ECO:0000244|PDB:2ZT5}.
STRAND 182 185 {ECO:0000244|PDB:2ZT5}.
HELIX 186 191 {ECO:0000244|PDB:2ZT5}.
HELIX 194 197 {ECO:0000244|PDB:2ZT5}.
STRAND 199 208 {ECO:0000244|PDB:2ZT5}.
STRAND 211 213 {ECO:0000244|PDB:2ZT5}.
HELIX 214 227 {ECO:0000244|PDB:2ZT5}.
STRAND 229 231 {ECO:0000244|PDB:2Q5I}.
HELIX 233 243 {ECO:0000244|PDB:2ZT5}.
TURN 244 248 {ECO:0000244|PDB:2ZT5}.
HELIX 251 260 {ECO:0000244|PDB:2ZT5}.
STRAND 266 268 {ECO:0000244|PDB:2ZT5}.
STRAND 276 279 {ECO:0000244|PDB:2ZT5}.
STRAND 283 285 {ECO:0000244|PDB:2ZT5}.
STRAND 287 296 {ECO:0000244|PDB:2ZT5}.
STRAND 298 300 {ECO:0000244|PDB:2ZXF}.
HELIX 301 305 {ECO:0000244|PDB:2ZT5}.
HELIX 308 314 {ECO:0000244|PDB:2ZT5}.
TURN 315 317 {ECO:0000244|PDB:2ZT5}.
STRAND 321 330 {ECO:0000244|PDB:2ZT5}.
HELIX 339 341 {ECO:0000244|PDB:2ZT5}.
STRAND 344 355 {ECO:0000244|PDB:2ZT5}.
HELIX 357 359 {ECO:0000244|PDB:4KQE}.
HELIX 365 367 {ECO:0000244|PDB:2ZT5}.
TURN 368 370 {ECO:0000244|PDB:2ZT5}.
STRAND 372 376 {ECO:0000244|PDB:2ZT5}.
HELIX 378 382 {ECO:0000244|PDB:2ZT5}.
STRAND 388 391 {ECO:0000244|PDB:2ZT5}.
HELIX 392 397 {ECO:0000244|PDB:2ZT5}.
STRAND 400 402 {ECO:0000244|PDB:2PME}.
HELIX 404 420 {ECO:0000244|PDB:2ZT5}.
HELIX 424 426 {ECO:0000244|PDB:2ZT5}.
STRAND 427 431 {ECO:0000244|PDB:2ZT5}.
HELIX 434 436 {ECO:0000244|PDB:2ZT5}.
STRAND 442 451 {ECO:0000244|PDB:2ZT5}.
STRAND 454 462 {ECO:0000244|PDB:2ZT5}.
HELIX 467 476 {ECO:0000244|PDB:2ZT5}.
STRAND 482 484 {ECO:0000244|PDB:2ZT5}.
HELIX 501 507 {ECO:0000244|PDB:4KQE}.
HELIX 512 519 {ECO:0000244|PDB:4KQE}.
HELIX 524 535 {ECO:0000244|PDB:4KQE}.
STRAND 541 544 {ECO:0000244|PDB:4KQE}.
STRAND 547 550 {ECO:0000244|PDB:4KQE}.
STRAND 552 554 {ECO:0000244|PDB:4KQE}.
STRAND 562 564 {ECO:0000244|PDB:2PMF}.
TURN 565 567 {ECO:0000244|PDB:2PMF}.
STRAND 568 570 {ECO:0000244|PDB:2ZT5}.
STRAND 573 580 {ECO:0000244|PDB:2ZT5}.
HELIX 581 592 {ECO:0000244|PDB:2ZT5}.
STRAND 593 595 {ECO:0000244|PDB:2ZT5}.
STRAND 597 600 {ECO:0000244|PDB:4KQE}.
STRAND 603 605 {ECO:0000244|PDB:2ZT5}.
TURN 609 611 {ECO:0000244|PDB:2ZT5}.
STRAND 615 621 {ECO:0000244|PDB:2ZT5}.
TURN 625 627 {ECO:0000244|PDB:2ZT5}.
HELIX 628 640 {ECO:0000244|PDB:2ZT5}.
STRAND 645 647 {ECO:0000244|PDB:2ZT5}.
STRAND 650 652 {ECO:0000244|PDB:5E6M}.
HELIX 654 663 {ECO:0000244|PDB:2ZT5}.
STRAND 668 672 {ECO:0000244|PDB:2ZT5}.
HELIX 674 677 {ECO:0000244|PDB:2ZT5}.
STRAND 679 681 {ECO:0000244|PDB:2ZT5}.
STRAND 683 688 {ECO:0000244|PDB:2ZT5}.
TURN 689 691 {ECO:0000244|PDB:2ZT5}.
STRAND 694 698 {ECO:0000244|PDB:2ZT5}.
TURN 699 701 {ECO:0000244|PDB:2ZT5}.
HELIX 702 710 {ECO:0000244|PDB:2ZT5}.
STRAND 712 714 {ECO:0000244|PDB:4KR3}.
HELIX 716 722 {ECO:0000244|PDB:2ZT5}.
SEQUENCE 739 AA; 83166 MW; E4C001CEBF985C59 CRC64;
MPSPRPVLLR GARAALLLLL PPRLLARPSL LLRRSLSAAS CPPISLPAAA SRSSMDGAGA
EEVLAPLRLA VRQQGDLVRK LKEDKAPQVD VDKAVAELKA RKRVLEAKEL ALQPKDDIVD
RAKMEDTLKR RFFYDQAFAI YGGVSGLYDF GPVGCALKNN IIQTWRQHFI QEEQILEIDC
TMLTPEPVLK TSGHVDKFAD FMVKDVKNGE CFRADHLLKA HLQKLMSDKK CSVEKKSEME
SVLAQLDNYG QQELADLFVN YNVKSPITGN DLSPPVSFNL MFKTFIGPGG NMPGYLRPET
AQGIFLNFKR LLEFNQGKLP FAAAQIGNSF RNEISPRSGL IRVREFTMAE IEHFVDPSEK
DHPKFQNVAD LHLYLYSAKA QVSGQSARKM RLGDAVEQGV INNTVLGYFI GRIYLYLTKV
GISPDKLRFR QHMENEMAHY ACDCWDAESK TSYGWIEIVG CADRSCYDLS CHARATKVPL
VAEKPLKEPK TVNVVQFEPS KGAIGKAYKK DAKLVMEYLA ICDECYITEM EMLLNEKGEF
TIETEGKTFQ LTKDMINVKR FQKTLYVEEV VPNVIEPSFG LGRIMYTVFE HTFHVREGDE
QRTFFSFPAV VAPFKCSVLP LSQNQEFMPF VKELSEALTR HGVSHKVDDS SGSIGRRYAR
TDEIGVAFGV TIDFDTVNKT PHTATLRDRD SMRQIRAEIS ELPSIVQDLA NGNITWADVE
ARYPLFEGQE TGKKETIEE


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EIAAB40852 62 kDa RNA-binding protein,Oryctolagus cuniculus,Rabbit,SARS,Serine--tRNA ligase,SerRS,SERS,Seryl-tRNA synthetase, cytoplasmic,Seryl-tRNA(Ser_Sec) synthetase
EIAAB40849 Bos taurus,Bovine,SARS,Serine--tRNA ligase,SerRS,SERS,Seryl-tRNA synthetase, cytoplasmic,Seryl-tRNA(Ser_Sec) synthetase
EIAAB40842 Arginine--tRNA ligase,Arginyl-tRNA synthetase-like,ArgRS,Mouse,Mus musculus,Probable arginyl-tRNA synthetase, mitochondrial,Rars2,Rarsl
EIAAB40928 Homo sapiens,Human,TARS2,TARSL1,Threonine--tRNA ligase,Threonyl-tRNA synthetase, mitochondrial,Threonyl-tRNA synthetase-like 1,ThrRS
EIAAB40910 Mouse,Mus musculus,Probable threonyl-tRNA synthetase 2, cytoplasmic,Tarsl2,Threonine--tRNA ligase,Threonyl-tRNA synthetase-like protein 2,ThrRS
EIAAB40911 Bos taurus,Bovine,Probable threonyl-tRNA synthetase 2, cytoplasmic,TARSL2,Threonine--tRNA ligase,Threonyl-tRNA synthetase-like protein 2,ThrRS
EIAAB40843 Arginine--tRNA ligase,Arginyl-tRNA synthetase-like,ArgRS,Bos taurus,Bovine,Probable arginyl-tRNA synthetase, mitochondrial,RARS2,RARSL
EIAAB40850 Rat,Rattus norvegicus,Sars,Sars1,Serine--tRNA ligase,SerRS,Seryl-tRNA synthetase, cytoplasmic,Seryl-tRNA(Ser_Sec) synthetase
EIAAB40926 Mouse,Mus musculus,Tars2,Tarsl1,Threonine--tRNA ligase,Threonyl-tRNA synthetase, mitochondrial,Threonyl-tRNA synthetase-like 1,ThrRS
EIAAB40927 Rat,Rattus norvegicus,Tars2,Tarsl1,Threonine--tRNA ligase,Threonyl-tRNA synthetase, mitochondrial,Threonyl-tRNA synthetase-like 1,ThrRS
18-003-44206 Seryl-tRNA synthetase. cytoplasmic - EC 6.1.1.11; Seryl-tRNA(Ser_Sec) synthetase; Serine--tRNA ligase; SerRS Polyclonal 0.1 mg Protein A
18-003-44205 Seryl-tRNA synthetase. cytoplasmic - EC 6.1.1.11; Seryl-tRNA(Ser_Sec) synthetase; Serine--tRNA ligase; SerRS Polyclonal 0.1 mg Protein A
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
29-249 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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