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Tryptophan--tRNA ligase, cytoplasmic (EC 6.1.1.2) (Interferon-induced protein 53) (IFP53) (Tryptophanyl-tRNA synthetase) (TrpRS) (hWRS) [Cleaved into: T1-TrpRS; T2-TrpRS]

 SYWC_HUMAN              Reviewed;         471 AA.
P23381; A6NGN1; A6NID3; P78535; Q502Y0; Q53XB6; Q9UDI5; Q9UDL3;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
01-DEC-1992, sequence version 2.
25-OCT-2017, entry version 181.
RecName: Full=Tryptophan--tRNA ligase, cytoplasmic;
EC=6.1.1.2;
AltName: Full=Interferon-induced protein 53;
Short=IFP53;
AltName: Full=Tryptophanyl-tRNA synthetase;
Short=TrpRS;
Short=hWRS;
Contains:
RecName: Full=T1-TrpRS;
Contains:
RecName: Full=T2-TrpRS;
Name=WARS; Synonyms=IFI53, WRS;
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=1761529;
Rubin B.Y., Anderson S.L., Xing L., Powell R.J., Tate W.P.;
"Interferon induces tryptophanyl-tRNA synthetase expression in human
fibroblasts.";
J. Biol. Chem. 266:24245-24248(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1763065; DOI=10.1073/pnas.88.24.11520;
Fleckner J., Rasmussen H.H., Justesen J.;
"Human interferon gamma potently induces the synthesis of a 55-kDa
protein (gamma 2) highly homologous to rabbit peptide chain release
factor and bovine tryptophanyl-tRNA synthetase.";
Proc. Natl. Acad. Sci. U.S.A. 88:11520-11524(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1765274; DOI=10.1016/0378-1119(91)90624-K;
Frolova L.Y., Sudomoina M.A., Grigorieva A.Y., Zinovieva O.L.,
Kisselev L.L.;
"Cloning and nucleotide sequence of the structural gene encoding for
human tryptophanyl-tRNA synthetase.";
Gene 109:291-296(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1537332;
Buwitt U., Flohr T., Boettger E.C.;
"Molecular cloning and characterization of an interferon induced human
cDNA with sequence homology to a mammalian peptide chain release
factor.";
EMBO J. 11:489-496(1992).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Fetal liver;
Li W.B., Gruber C., Jessee J., Polayes D.;
"Full-length cDNA libraries and normalization.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Teratocarcinoma;
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[8]
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.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Blood, and Lymph;
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).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
PubMed=8724762;
Sokolova I.V., Narovlianskii A.N., Amchenkova A.M., Turpaev K.T.;
"Alternative splicing of 5'-terminal exons of the human tryptophanyl-
tRNA synthetase gene.";
Mol. Biol. (Mosk.) 30:319-329(1996).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-141 AND 182-471.
TISSUE=Sperm;
PubMed=7685728; DOI=10.1016/0378-1119(93)90568-N;
Frolova L.Y., Grigorieva A.Y., Sudomoina M.A., Kisselev L.L.;
"The human gene encoding tryptophanyl-tRNA synthetase: interferon-
response elements and exon-intron organization.";
Gene 128:237-245(1993).
[12]
PROTEIN SEQUENCE OF 2-19; 142-162; 205-220; 278-298; 350-366 AND
433-448, AND INDUCTION.
TISSUE=Keratinocyte;
PubMed=8496617; DOI=10.1111/1523-1747.ep12476463;
Reano A., Richard M.H., Denoroy L., Viac J., Benedetto J.P.,
Schmitt D.;
"Gamma interferon potently induces tryptophanyl-tRNA synthetase
expression in human keratinocytes.";
J. Invest. Dermatol. 100:775-779(1993).
[13]
PROTEIN SEQUENCE OF 2-24; 97-106; 433-448 AND 465-471, CLEAVAGE OF
INITIATOR METHIONINE, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Colon carcinoma;
Bienvenut W.V., Heiserich L., Gottlieb E.;
Submitted (MAR-2008) to UniProtKB.
[14]
PROTEIN SEQUENCE OF 71-75 AND 91-98, PROTEOLYTIC CLEAVAGE, AND
FUNCTION.
PubMed=11773626; DOI=10.1073/pnas.012602099;
Wakasugi K., Slike B.M., Hood J., Otani A., Ewalt K.L.,
Friedlander M., Cheresh D.A., Schimmel P.;
"A human aminoacyl-tRNA synthetase as a regulator of angiogenesis.";
Proc. Natl. Acad. Sci. U.S.A. 99:173-177(2002).
[15]
PROTEIN SEQUENCE OF 265-276; 278-296; 299-317 AND 350-365.
TISSUE=Keratinocyte;
PubMed=1286667; DOI=10.1002/elps.11501301199;
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel
protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[16]
FUNCTION.
PubMed=1373391; DOI=10.1016/0014-5793(92)80187-L;
Bange F.-C., Flohr T., Buwitt U., Boettger E.C.;
"An interferon-induced protein with release factor activity is a
tryptophanyl-tRNA synthetase.";
FEBS Lett. 300:162-166(1992).
[17]
ALTERNATIVE SPLICING.
PubMed=7814400; DOI=10.1074/jbc.270.1.397;
Tolstrup A.B., Bejder A., Fleckner J., Justesen J.;
"Transcriptional regulation of the interferon-gamma-inducible
tryptophanyl-tRNA synthetase includes alternative splicing.";
J. Biol. Chem. 270:397-403(1995).
[18]
FUNCTION.
PubMed=11773625; DOI=10.1073/pnas.012601899;
Otani A., Slike B.M., Dorrell M.I., Hood J., Kinder K., Ewalt K.L.,
Cheresh D., Schimmel P., Friedlander M.;
"A fragment of human TrpRS as a potent antagonist of ocular
angiogenesis.";
Proc. Natl. Acad. Sci. U.S.A. 99:178-183(2002).
[19]
FUNCTION.
PubMed=14630953; DOI=10.1073/pnas.2436330100;
Tzima E., Reader J.S., Irani-Tehrani M., Ewalt K.L., Schwartz M.A.,
Schimmel P.;
"Biologically active fragment of a human tRNA synthetase inhibits
fluid shear stress-activated responses of endothelial cells.";
Proc. Natl. Acad. Sci. U.S.A. 100:14903-14907(2003).
[20]
INTERACTION WITH GAPDH.
PubMed=15628863; DOI=10.1021/bi048313k;
Wakasugi K., Nakano T., Morishima I.;
"Oxidative stress-responsive intracellular regulation specific for the
angiostatic form of human tryptophanyl-tRNA synthetase.";
Biochemistry 44:225-232(2005).
[21]
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).
[22]
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).
[23]
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).
[24]
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).
[25]
CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], 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).
[26]
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).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, 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).
[28]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-466.
PubMed=14671330; DOI=10.1073/pnas.2136794100;
Yang X.-L., Otero F.J., Skene R.J., McRee D.E., Schimmel P.,
Ribas de Pouplana L.;
"Crystal structures that suggest late development of genetic code
components for differentiating aromatic side chains.";
Proc. Natl. Acad. Sci. U.S.A. 100:15376-15380(2003).
[29]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 94-471.
PubMed=14660560; DOI=10.1074/jbc.M311284200;
Yu Y., Liu Y., Shen N., Xu X., Xu F., Jia J., Jin Y., Arnold E.,
Ding J.;
"Crystal structure of human tryptophanyl-tRNA synthetase catalytic
fragment: insights into substrate recognition, tRNA binding, and
angiogenesis activity.";
J. Biol. Chem. 279:8378-8388(2004).
[30]
VARIANT [LARGE SCALE ANALYSIS] ASP-455.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Isoform 1, isoform 2 and T1-TrpRS have aminoacylation
activity while T2-TrpRS lacks it. Isoform 2, T1-TrpRS and T2-TrpRS
possess angiostatic activity whereas isoform 1 lacks it. T2-TrpRS
inhibits fluid shear stress-activated responses of endothelial
cells. Regulates ERK, Akt, and eNOS activation pathways that are
associated with angiogenesis, cytoskeletal reorganization and
shear stress-responsive gene expression.
{ECO:0000269|PubMed:11773625, ECO:0000269|PubMed:11773626,
ECO:0000269|PubMed:1373391, ECO:0000269|PubMed:14630953}.
-!- CATALYTIC ACTIVITY: ATP + L-tryptophan + tRNA(Trp) = AMP +
diphosphate + L-tryptophyl-tRNA(Trp).
-!- SUBUNIT: Homodimer. Isoform 1 and isoform 2 interact with an
oxidized form of GAPDH. GAPDH stimulates the aminoacylation
activity of isoform 2.
-!- INTERACTION:
P33151:CDH5; NbExp=4; IntAct=EBI-721244, EBI-2903122;
P54274:TERF1; NbExp=2; IntAct=EBI-721244, EBI-710997;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P23381-1; Sequence=Displayed;
Name=2; Synonyms=mini TrpRS;
IsoId=P23381-2; Sequence=VSP_038221;
-!- INDUCTION: By IFNG/IFN-gamma. {ECO:0000269|PubMed:8496617}.
-!- PTM: Proteolytic cleavage generates 2 forms; T1-TrpRS and T2-
TrpRS. {ECO:0000269|PubMed:11773626}.
-!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
family. {ECO:0000305}.
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EMBL; M77804; AAA67324.1; -; mRNA.
EMBL; X59892; CAA42545.1; -; mRNA.
EMBL; M61715; AAA61298.1; -; mRNA.
EMBL; X62570; CAA44450.1; -; mRNA.
EMBL; BX248006; CAD62335.1; -; mRNA.
EMBL; AK056100; BAG51626.1; -; mRNA.
EMBL; AK291141; BAF83830.1; -; mRNA.
EMBL; AL157871; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471061; EAW81700.1; -; Genomic_DNA.
EMBL; BC017489; AAH17489.1; -; mRNA.
EMBL; BC095453; AAH95453.1; -; mRNA.
EMBL; S82905; AAB39381.1; -; Genomic_DNA.
EMBL; X67920; CAB94198.1; -; Genomic_DNA.
EMBL; X67921; CAB94198.1; JOINED; Genomic_DNA.
EMBL; X67922; CAB94198.1; JOINED; Genomic_DNA.
EMBL; X67923; CAB94199.1; -; Genomic_DNA.
EMBL; X67924; CAB94199.1; JOINED; Genomic_DNA.
EMBL; X67925; CAB94199.1; JOINED; Genomic_DNA.
EMBL; X67926; CAB94199.1; JOINED; Genomic_DNA.
EMBL; X67927; CAB94199.1; JOINED; Genomic_DNA.
EMBL; X67928; CAB94199.1; JOINED; Genomic_DNA.
CCDS; CCDS9960.1; -. [P23381-1]
CCDS; CCDS9961.1; -. [P23381-2]
PIR; A41633; A41706.
RefSeq; NP_004175.2; NM_004184.3. [P23381-1]
RefSeq; NP_776049.1; NM_173701.1. [P23381-1]
RefSeq; NP_998810.1; NM_213645.1. [P23381-2]
RefSeq; NP_998811.1; NM_213646.1. [P23381-2]
RefSeq; XP_005268101.1; XM_005268044.3. [P23381-1]
RefSeq; XP_006720312.1; XM_006720249.3. [P23381-1]
RefSeq; XP_011535435.1; XM_011537133.2. [P23381-1]
RefSeq; XP_011535437.1; XM_011537135.2. [P23381-1]
RefSeq; XP_011535438.1; XM_011537136.2. [P23381-2]
RefSeq; XP_016877116.1; XM_017021627.1. [P23381-1]
RefSeq; XP_016877117.1; XM_017021628.1. [P23381-1]
RefSeq; XP_016877118.1; XM_017021629.1. [P23381-1]
UniGene; Hs.497599; -.
PDB; 1O5T; X-ray; 2.50 A; A=94-471.
PDB; 1R6T; X-ray; 2.10 A; A/B=1-466.
PDB; 1R6U; X-ray; 2.00 A; A/B=48-471.
PDB; 1ULH; X-ray; 2.31 A; A/B=82-471.
PDB; 2AKE; X-ray; 3.10 A; A=94-471.
PDB; 2AZX; X-ray; 2.80 A; A/B=1-471.
PDB; 2DR2; X-ray; 3.00 A; A=94-471.
PDB; 2QUH; X-ray; 2.40 A; A/B=1-471.
PDB; 2QUI; X-ray; 2.40 A; A/B=1-471.
PDB; 2QUJ; X-ray; 2.42 A; A/B=1-471.
PDB; 2QUK; X-ray; 2.80 A; A=1-471.
PDBsum; 1O5T; -.
PDBsum; 1R6T; -.
PDBsum; 1R6U; -.
PDBsum; 1ULH; -.
PDBsum; 2AKE; -.
PDBsum; 2AZX; -.
PDBsum; 2DR2; -.
PDBsum; 2QUH; -.
PDBsum; 2QUI; -.
PDBsum; 2QUJ; -.
PDBsum; 2QUK; -.
ProteinModelPortal; P23381; -.
SMR; P23381; -.
BioGrid; 113292; 64.
DIP; DIP-29493N; -.
IntAct; P23381; 10.
MINT; MINT-1408962; -.
STRING; 9606.ENSP00000347495; -.
DrugBank; DB00150; L-Tryptophan.
DrugBank; DB04537; L-Tryptophanamide.
DrugBank; DB01831; Tryptophanyl-5'amp.
MoonProt; P23381; -.
iPTMnet; P23381; -.
PhosphoSitePlus; P23381; -.
SwissPalm; P23381; -.
BioMuta; WARS; -.
DMDM; 135191; -.
OGP; P23381; -.
EPD; P23381; -.
MaxQB; P23381; -.
PaxDb; P23381; -.
PeptideAtlas; P23381; -.
PRIDE; P23381; -.
Ensembl; ENST00000344102; ENSP00000339485; ENSG00000140105. [P23381-2]
Ensembl; ENST00000355338; ENSP00000347495; ENSG00000140105. [P23381-1]
Ensembl; ENST00000358655; ENSP00000351481; ENSG00000140105. [P23381-2]
Ensembl; ENST00000392882; ENSP00000376620; ENSG00000140105. [P23381-1]
Ensembl; ENST00000556645; ENSP00000451887; ENSG00000140105. [P23381-2]
Ensembl; ENST00000557135; ENSP00000451460; ENSG00000140105. [P23381-1]
GeneID; 7453; -.
KEGG; hsa:7453; -.
UCSC; uc001yhg.3; human. [P23381-1]
CTD; 7453; -.
DisGeNET; 7453; -.
EuPathDB; HostDB:ENSG00000140105.17; -.
GeneCards; WARS; -.
HGNC; HGNC:12729; WARS.
HPA; HPA005573; -.
HPA; HPA018944; -.
MIM; 191050; gene.
neXtProt; NX_P23381; -.
OpenTargets; ENSG00000140105; -.
PharmGKB; PA37340; -.
eggNOG; KOG2145; Eukaryota.
eggNOG; COG0180; LUCA.
GeneTree; ENSGT00390000000666; -.
HOVERGEN; HBG002325; -.
InParanoid; P23381; -.
KO; K01867; -.
OMA; SIYHRFM; -.
OrthoDB; EOG091G09U9; -.
PhylomeDB; P23381; -.
TreeFam; TF105669; -.
BRENDA; 6.1.1.2; 2681.
Reactome; R-HSA-379716; Cytosolic tRNA aminoacylation.
ChiTaRS; WARS; human.
EvolutionaryTrace; P23381; -.
GeneWiki; WARS_(gene); -.
GenomeRNAi; 7453; -.
PRO; PR:P23381; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000140105; -.
CleanEx; HS_WARS; -.
ExpressionAtlas; P23381; baseline and differential.
Genevisible; P23381; HS.
GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IMP:CAFA.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019210; F:kinase inhibitor activity; IDA:CAFA.
GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
GO; GO:0019901; F:protein kinase binding; IPI:CAFA.
GO; GO:0004830; F:tryptophan-tRNA ligase activity; IBA:GO_Central.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:CAFA.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:CAFA.
GO; GO:0010628; P:positive regulation of gene expression; IDA:CAFA.
GO; GO:0031334; P:positive regulation of protein complex assembly; IMP:CAFA.
GO; GO:0045765; P:regulation of angiogenesis; IDA:UniProtKB.
GO; GO:0010835; P:regulation of protein ADP-ribosylation; IDA:CAFA.
GO; GO:0006412; P:translation; TAS:ProtInc.
GO; GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome.
GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IBA:GO_Central.
CDD; cd00806; TrpRS_core; 1.
Gene3D; 1.10.287.10; -; 1.
Gene3D; 3.40.50.620; -; 1.
InterPro; IPR001412; aa-tRNA-synth_I_CS.
InterPro; IPR002305; aa-tRNA-synth_Ic.
InterPro; IPR014729; Rossmann-like_a/b/a_fold.
InterPro; IPR009068; S15_NS1_RNA-bd.
InterPro; IPR002306; Trp-tRNA-ligase.
InterPro; IPR000738; WHEP-TRS_dom.
Pfam; PF00579; tRNA-synt_1b; 1.
Pfam; PF00458; WHEP-TRS; 1.
PRINTS; PR01039; TRNASYNTHTRP.
SMART; SM00991; WHEP-TRS; 1.
SUPFAM; SSF47060; SSF47060; 1.
TIGRFAMs; TIGR00233; trpS; 1.
PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PROSITE; PS00762; WHEP_TRS_1; 1.
PROSITE; PS51185; WHEP_TRS_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Aminoacyl-tRNA synthetase;
Angiogenesis; ATP-binding; Complete proteome; Cytoplasm;
Direct protein sequencing; Ligase; Nucleotide-binding; Phosphoprotein;
Polymorphism; Protein biosynthesis; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895,
ECO:0000269|PubMed:8496617,
ECO:0000269|Ref.13}.
CHAIN 2 471 Tryptophan--tRNA ligase, cytoplasmic.
/FTId=PRO_0000136738.
CHAIN 71 471 T1-TrpRS.
/FTId=PRO_0000386461.
CHAIN 94 471 T2-TrpRS.
/FTId=PRO_0000386462.
DOMAIN 8 64 WHEP-TRS. {ECO:0000255|PROSITE-
ProRule:PRU00531}.
MOTIF 164 173 "HIGH" region.
MOTIF 349 353 "KMSKS" region.
MOD_RES 154 154 N6-succinyllysine.
{ECO:0000250|UniProtKB:P32921}.
MOD_RES 351 351 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 41 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038221.
VARIANT 54 54 A -> S (in dbSNP:rs2234521).
/FTId=VAR_052406.
VARIANT 455 455 E -> D (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036466.
CONFLICT 213 214 SY -> GD (in Ref. 3; AAA61298).
{ECO:0000305}.
CONFLICT 310 310 A -> V (in Ref. 9; AAH95453).
{ECO:0000305}.
CONFLICT 424 424 A -> R (in Ref. 4; CAA44450).
{ECO:0000305}.
CONFLICT 439 439 Q -> L (in Ref. 9; AAH95453).
{ECO:0000305}.
HELIX 8 28 {ECO:0000244|PDB:1R6T}.
HELIX 33 53 {ECO:0000244|PDB:1R6T}.
STRAND 54 56 {ECO:0000244|PDB:1R6T}.
STRAND 84 86 {ECO:0000244|PDB:1R6U}.
STRAND 89 91 {ECO:0000244|PDB:1R6U}.
TURN 100 102 {ECO:0000244|PDB:1R6U}.
HELIX 103 106 {ECO:0000244|PDB:1R6U}.
HELIX 114 124 {ECO:0000244|PDB:1R6U}.
HELIX 130 133 {ECO:0000244|PDB:1R6U}.
STRAND 136 142 {ECO:0000244|PDB:1R6U}.
HELIX 143 150 {ECO:0000244|PDB:1R6U}.
TURN 151 153 {ECO:0000244|PDB:1R6U}.
STRAND 156 162 {ECO:0000244|PDB:1R6U}.
HELIX 171 187 {ECO:0000244|PDB:1R6U}.
STRAND 191 195 {ECO:0000244|PDB:1R6U}.
HELIX 197 203 {ECO:0000244|PDB:1R6U}.
HELIX 208 223 {ECO:0000244|PDB:1R6U}.
TURN 224 226 {ECO:0000244|PDB:1R6U}.
HELIX 229 231 {ECO:0000244|PDB:1R6U}.
STRAND 232 236 {ECO:0000244|PDB:1R6U}.
HELIX 237 240 {ECO:0000244|PDB:1R6U}.
HELIX 241 243 {ECO:0000244|PDB:1R6U}.
HELIX 247 256 {ECO:0000244|PDB:1R6U}.
HELIX 260 267 {ECO:0000244|PDB:1R6U}.
STRAND 271 274 {ECO:0000244|PDB:1ULH}.
HELIX 275 285 {ECO:0000244|PDB:1R6U}.
HELIX 286 288 {ECO:0000244|PDB:1R6U}.
HELIX 290 292 {ECO:0000244|PDB:1R6U}.
HELIX 294 297 {ECO:0000244|PDB:1R6U}.
STRAND 304 310 {ECO:0000244|PDB:1R6U}.
HELIX 311 313 {ECO:0000244|PDB:1R6U}.
HELIX 314 323 {ECO:0000244|PDB:1R6U}.
HELIX 324 327 {ECO:0000244|PDB:1R6U}.
STRAND 333 337 {ECO:0000244|PDB:1R6U}.
STRAND 345 349 {ECO:0000244|PDB:1R6U}.
STRAND 354 357 {ECO:0000244|PDB:1R6U}.
STRAND 360 362 {ECO:0000244|PDB:2AZX}.
HELIX 365 374 {ECO:0000244|PDB:1R6U}.
HELIX 384 390 {ECO:0000244|PDB:1R6U}.
TURN 394 396 {ECO:0000244|PDB:1R6U}.
HELIX 398 406 {ECO:0000244|PDB:1R6U}.
HELIX 410 422 {ECO:0000244|PDB:1R6U}.
STRAND 423 425 {ECO:0000244|PDB:1R6U}.
HELIX 430 450 {ECO:0000244|PDB:1R6U}.
HELIX 454 460 {ECO:0000244|PDB:1R6U}.
SEQUENCE 471 AA; 53165 MW; E96344449053A0D0 CRC64;
MPNSEPASLL ELFNSIATQG ELVRSLKAGN ASKDEIDSAV KMLVSLKMSY KAAAGEDYKA
DCPPGNPAPT SNHGPDATEA EEDFVDPWTV QTSSAKGIDY DKLIVRFGSS KIDKELINRI
ERATGQRPHH FLRRGIFFSH RDMNQVLDAY ENKKPFYLYT GRGPSSEAMH VGHLIPFIFT
KWLQDVFNVP LVIQMTDDEK YLWKDLTLDQ AYSYAVENAK DIIACGFDIN KTFIFSDLDY
MGMSSGFYKN VVKIQKHVTF NQVKGIFGFT DSDCIGKISF PAIQAAPSFS NSFPQIFRDR
TDIQCLIPCA IDQDPYFRMT RDVAPRIGYP KPALLHSTFF PALQGAQTKM SASDPNSSIF
LTDTAKQIKT KVNKHAFSGG RDTIEEHRQF GGNCDVDVSF MYLTFFLEDD DKLEQIRKDY
TSGAMLTGEL KKALIEVLQP LIAEHQARRK EVTDEIVKEF MTPRKLSFDF Q


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