P23381 (SYWC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tryptophan--tRNA ligase, cytoplasmic
EC=6.1.1.2

Alternative name(s):
Interferon-induced protein 53
Short name=IFP53
Tryptophanyl-tRNA synthetase
Short name=TrpRS
Short name=hWRS

Cleaved into the following 2 chains:

1. T1-TrpRS
2. T2-TrpRS

Gene names

Name:	WARS
Synonyms:	IFI53, WRS

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	471 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.14 Ref.16 Ref.18 Ref.19
Catalytic activity	ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp).
Subunit structure	Homodimer. Isoform 1 and isoform 2 interact with an oxidized form of GAPDH. GAPDH stimulates the aminoacylation activity of isoform 2.
Subcellular location	Cytoplasm.
Induction	By IFNG/IFN-gamma. Ref.12
Post-translational modification	Proteolytic cleavage generates 2 forms; T1-TrpRS and T2-TrpRS.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family. Contains 1 WHEP-TRS domain.
Sequence caution	The sequence BAF83830.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Angiogenesis Protein biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	angiogenesis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of cell proliferation Traceable author statement. Source: ProtInc regulation of angiogenesis Inferred from direct assay Ref.18Ref.14. Source: UniProtKB tryptophanyl-tRNA aminoacylation Non-traceable author statement Ref.12. Source: UniProtKB
Cellular component	cytosol Traceable author statement. Source: Reactome soluble fraction Traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.20. Source: UniProtKB tryptophan-tRNA ligase activity Non-traceable author statement Ref.12. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P23381-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P23381-2)

Also known as: mini TrpRS;

The sequence of this isoform differs from the canonical sequence as follows:
     1-47: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.12 Ref.13

Chain

2 – 471

470

Tryptophan--tRNA ligase, cytoplasmic

PRO_0000136738

Chain

71 – 471

401

T1-TrpRS

PRO_0000386461

Chain

94 – 471

378

T2-TrpRS

PRO_0000386462

Regions

Domain

8 – 64

57

WHEP-TRS

Motif

164 – 173

10

"HIGH" region

Motif

349 – 353

5

"KMSKS" region

Amino acid modifications

Modified residue

467

1

Phosphoserine Ref.21 Ref.22

Natural variations

Alternative sequence

1 – 47

47

Missing in isoform 2.

VSP_038221

Natural variant

54

1

A → S.
Corresponds to variant rs2234521 [ dbSNP | Ensembl ].

VAR_052406

Natural variant

455

1

E → D in a breast cancer sample; somatic mutation. Ref.26

VAR_036466

Experimental info

Sequence conflict

213 – 214

2

SY → GD in AAA61298. Ref.3

Sequence conflict

310

1

A → V in AAH95453. Ref.9

Sequence conflict

424

1

A → R in CAA44450. Ref.4

Sequence conflict

439

1

Q → L in AAH95453. Ref.9

Secondary structure

1

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471

Helix Strand Turn

Details...

Helix

8 – 28

21

Helix

33 – 53

21

Beta strand

54 – 56

3

Beta strand

84 – 88

5

Helix

100 – 107

8

Helix

114 – 124

11

Helix

130 – 133

4

Beta strand

136 – 142

7

Helix

143 – 151

9

Beta strand

156 – 162

7

Helix

171 – 173

3

Helix

174 – 187

14

Beta strand

191 – 195

5

Helix

197 – 203

7

Helix

208 – 223

16

Beta strand

231 – 236

6

Helix

237 – 240

4

Helix

241 – 243

3

Helix

247 – 256

10

Helix

260 – 267

8

Helix

275 – 285

11

Helix

286 – 288

3

Helix

290 – 292

3

Helix

294 – 297

4

Beta strand

304 – 310

7

Helix

311 – 313

3

Helix

314 – 323

10

Helix

324 – 327

4

Beta strand

333 – 337

5

Beta strand

345 – 349

5

Helix

365 – 375

11

Helix

384 – 390

7

Turn

394 – 396

3

Helix

398 – 406

9

Helix

410 – 421

12

Helix

427 – 449

23

Helix

454 – 460

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 1992. Version 2. Checksum: E96344449053A0D0	FASTA	471	53,165
	10 20 30 40 50 60 MPNSEPASLL ELFNSIATQG ELVRSLKAGN ASKDEIDSAV KMLVSLKMSY KAAAGEDYKA 70 80 90 100 110 120 DCPPGNPAPT SNHGPDATEA EEDFVDPWTV QTSSAKGIDY DKLIVRFGSS KIDKELINRI 130 140 150 160 170 180 ERATGQRPHH FLRRGIFFSH RDMNQVLDAY ENKKPFYLYT GRGPSSEAMH VGHLIPFIFT 190 200 210 220 230 240 KWLQDVFNVP LVIQMTDDEK YLWKDLTLDQ AYSYAVENAK DIIACGFDIN KTFIFSDLDY 250 260 270 280 290 300 MGMSSGFYKN VVKIQKHVTF NQVKGIFGFT DSDCIGKISF PAIQAAPSFS NSFPQIFRDR 310 320 330 340 350 360 TDIQCLIPCA IDQDPYFRMT RDVAPRIGYP KPALLHSTFF PALQGAQTKM SASDPNSSIF 370 380 390 400 410 420 LTDTAKQIKT KVNKHAFSGG RDTIEEHRQF GGNCDVDVSF MYLTFFLEDD DKLEQIRKDY 430 440 450 460 470 TSGAMLTGEL KKALIEVLQP LIAEHQARRK EVTDEIVKEF MTPRKLSFDF Q
	Isoform 2 (mini TrpRS) [UniParc]. Checksum: 92A3AA78DAE9D0AF	FASTA	424	48,180
	10 20 30 40 50 60 MSYKAAAGED YKADCPPGNP APTSNHGPDA TEAEEDFVDP WTVQTSSAKG IDYDKLIVRF 70 80 90 100 110 120 GSSKIDKELI NRIERATGQR PHHFLRRGIF FSHRDMNQVL DAYENKKPFY LYTGRGPSSE 130 140 150 160 170 180 AMHVGHLIPF IFTKWLQDVF NVPLVIQMTD DEKYLWKDLT LDQAYSYAVE NAKDIIACGF 190 200 210 220 230 240 DINKTFIFSD LDYMGMSSGF YKNVVKIQKH VTFNQVKGIF GFTDSDCIGK ISFPAIQAAP 250 260 270 280 290 300 SFSNSFPQIF RDRTDIQCLI PCAIDQDPYF RMTRDVAPRI GYPKPALLHS TFFPALQGAQ 310 320 330 340 350 360 TKMSASDPNS SIFLTDTAKQ IKTKVNKHAF SGGRDTIEEH RQFGGNCDVD VSFMYLTFFL 370 380 390 400 410 420 EDDDKLEQIR KDYTSGAMLT GELKKALIEV LQPLIAEHQA RRKEVTDEIV KEFMTPRKLS FDFQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Interferon induces tryptophanyl-tRNA synthetase expression in human fibroblasts." Rubin B.Y., Anderson S.L., Xing L., Powell R.J., Tate W.P. J. Biol. Chem. 266:24245-24248(1991) [PubMed: 1761529] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"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." Fleckner J., Rasmussen H.H., Justesen J. Proc. Natl. Acad. Sci. U.S.A. 88:11520-11524(1991) [PubMed: 1763065] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Cloning and nucleotide sequence of the structural gene encoding for human tryptophanyl-tRNA synthetase." Frolova L.Y., Sudomoina M.A., Grigorieva A.Y., Zinovieva O.L., Kisselev L.L. Gene 109:291-296(1991) [PubMed: 1765274] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]	"Molecular cloning and characterization of an interferon induced human cDNA with sequence homology to a mammalian peptide chain release factor." Buwitt U., Flohr T., Boettger E.C. EMBO J. 11:489-496(1992) [PubMed: 1537332] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]	"Full-length cDNA libraries and normalization." Li W.B., Gruber C., Jessee J., Polayes D. Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Fetal liver.
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Teratocarcinoma.
[7]	"The DNA sequence and analysis of human chromosome 14." 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. Nature 421:601-607(2003) [PubMed: 12508121] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Blood and Lymph.
[10]	"Alternative splicing of 5'-terminal exons of the human tryptophanyl-tRNA synthetase gene." Sokolova I.V., Narovlianskii A.N., Amchenkova A.M., Turpaev K.T. Mol. Biol. (Mosk.) 30:319-329(1996) [PubMed: 8724762] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
[11]	"The human gene encoding tryptophanyl-tRNA synthetase: interferon-response elements and exon-intron organization." Frolova L.Y., Grigorieva A.Y., Sudomoina M.A., Kisselev L.L. Gene 128:237-245(1993) [PubMed: 7685728] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-141 AND 182-471. Tissue: Sperm.
[12]	"Gamma interferon potently induces tryptophanyl-tRNA synthetase expression in human keratinocytes." Reano A., Richard M.H., Denoroy L., Viac J., Benedetto J.P., Schmitt D. J. Invest. Dermatol. 100:775-779(1993) [PubMed: 8496617] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-19; 142-162; 205-220; 278-298; 350-366 AND 433-448, INDUCTION. Tissue: Keratinocyte.
[13]	Bienvenut W.V., Heiserich L., Gottlieb E. Submitted (MAR-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-24; 97-106; 433-448 AND 465-471, CLEAVAGE OF INITIATOR METHIONINE, MASS SPECTROMETRY. Tissue: Colon carcinoma.
[14]	"A human aminoacyl-tRNA synthetase as a regulator of angiogenesis." Wakasugi K., Slike B.M., Hood J., Otani A., Ewalt K.L., Friedlander M., Cheresh D.A., Schimmel P. Proc. Natl. Acad. Sci. U.S.A. 99:173-177(2002) [PubMed: 11773626] [Abstract] Cited for: PROTEIN SEQUENCE OF 71-75 AND 91-98, PROTEOLYTIC CLEAVAGE, FUNCTION.
[15]	"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes." Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J. Electrophoresis 13:960-969(1992) [PubMed: 1286667] [Abstract] Cited for: PROTEIN SEQUENCE OF 265-276; 278-296; 299-317 AND 350-365. Tissue: Keratinocyte.
[16]	"An interferon-induced protein with release factor activity is a tryptophanyl-tRNA synthetase." Bange F.-C., Flohr T., Buwitt U., Boettger E.C. FEBS Lett. 300:162-166(1992) [PubMed: 1373391] [Abstract] Cited for: FUNCTION.
[17]	"Transcriptional regulation of the interferon-gamma-inducible tryptophanyl-tRNA synthetase includes alternative splicing." Tolstrup A.B., Bejder A., Fleckner J., Justesen J. J. Biol. Chem. 270:397-403(1995) [PubMed: 7814400] [Abstract] Cited for: ALTERNATIVE SPLICING.
[18]	"A fragment of human TrpRS as a potent antagonist of ocular angiogenesis." Otani A., Slike B.M., Dorrell M.I., Hood J., Kinder K., Ewalt K.L., Cheresh D., Schimmel P., Friedlander M. Proc. Natl. Acad. Sci. U.S.A. 99:178-183(2002) [PubMed: 11773625] [Abstract] Cited for: FUNCTION.
[19]	"Biologically active fragment of a human tRNA synthetase inhibits fluid shear stress-activated responses of endothelial cells." Tzima E., Reader J.S., Irani-Tehrani M., Ewalt K.L., Schwartz M.A., Schimmel P. Proc. Natl. Acad. Sci. U.S.A. 100:14903-14907(2003) [PubMed: 14630953] [Abstract] Cited for: FUNCTION.
[20]	"Oxidative stress-responsive intracellular regulation specific for the angiostatic form of human tryptophanyl-tRNA synthetase." Wakasugi K., Nakano T., Morishima I. Biochemistry 44:225-232(2005) [PubMed: 15628863] [Abstract] Cited for: INTERACTION WITH GAPDH.
[21]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467, MASS SPECTROMETRY. Tissue: Colon adenocarcinoma.
[22]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]	"Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains." Yang X.-L., Otero F.J., Skene R.J., McRee D.E., Schimmel P., Ribas de Pouplana L. Proc. Natl. Acad. Sci. U.S.A. 100:15376-15380(2003) [PubMed: 14671330] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-466.
[25]	"Crystal structure of human tryptophanyl-tRNA synthetase catalytic fragment: insights into substrate recognition, tRNA binding, and angiogenesis activity." Yu Y., Liu Y., Shen N., Xu X., Xu F., Jia J., Jin Y., Arnold E., Ding J. J. Biol. Chem. 279:8378-8388(2004) [PubMed: 14660560] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 94-471.
[26]	"The consensus coding sequences of human breast and colorectal cancers." 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. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-455.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M77804 mRNA. Translation: AAA67324.1.
X59892 mRNA. Translation: CAA42545.1.
M61715 mRNA. Translation: AAA61298.1.
X62570 mRNA. Translation: CAA44450.1.
BX248006 mRNA. Translation: CAD62335.1.
AK056100 mRNA. Translation: BAG51626.1.
AK291141 mRNA. Translation: BAF83830.1. Different initiation.
AL157871 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW81700.1.
BC017489 mRNA. Translation: AAH17489.1.
BC095453 mRNA. Translation: AAH95453.1.
S82905 Genomic DNA. Translation: AAB39381.1.
X67920, X67921, X67922 Genomic DNA. Translation: CAB94198.1.
X67923 , X67924, X67925, X67926, X67927, X67928 Genomic DNA. Translation: CAB94199.1.

IPI

IPI00295400.
IPI00412737.

PIR

A41706. A41633.

RefSeq

NP_004175.2. NM_004184.3.
NP_776049.1. NM_173701.1.
NP_998810.1. NM_213645.1.
NP_998811.1. NM_213646.1.

UniGene

Hs.497599.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1O5T	X-ray	2.50	A	94-471	[»]
1R6T	X-ray	2.10	A/B	1-466	[»]
1R6U	X-ray	2.00	A/B	48-471	[»]
1ULH	X-ray	2.31	A/B	82-471	[»]
2AKE	X-ray	3.10	A	94-471	[»]
2AZX	X-ray	2.80	A/B	1-471	[»]
2DR2	X-ray	3.00	A	94-471	[»]
2QUH	X-ray	2.40	A/B	1-471	[»]
2QUI	X-ray	2.40	A/B	1-471	[»]
2QUJ	X-ray	2.42	A/B	1-471	[»]
2QUK	X-ray	2.80	A	1-471	[»]

ProteinModelPortal

P23381.

SMR

P23381. Positions 82-471.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29493N.

IntAct

P23381. 3 interactions.

MINT

MINT-1408962.

STRING

P23381.

PTM databases

PhosphoSite

P23381.

Polymorphism databases

DMDM

135191.

2D gel databases

Aarhus/Ghent-2DPAGE

3524. IEF.

OGP

P23381.

PHCI-2DPAGE

P23381.

Proteomic databases

PeptideAtlas

P23381.

PRIDE

P23381.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000355338; ENSP00000347495; ENSG00000140105.
ENST00000392882; ENSP00000376620; ENSG00000140105.

GeneID

7453.

KEGG

hsa:7453.

UCSC

uc001yhf.1. human.

Organism-specific databases

CTD

7453.

GeneCards

GC14M100800.

H-InvDB

HIX0011970.

HGNC

HGNC:12729. WARS.

MIM

191050. gene.

neXtProt

NX_P23381.

PharmGKB

PA37340.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG18493.

HOGENOM

HBG435805.

HOVERGEN

HBG002325.

InParanoid

P23381.

OMA

KFYLYTG.

OrthoDB

EOG4GQQ4S.

PhylomeDB

P23381.

Enzyme and pathway databases

Reactome

REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P23381.

Bgee

P23381.

CleanEx

HS_WARS.

Genevestigator

P23381.

GermOnline

ENSG00000140105. Homo sapiens.

Family and domain databases

InterPro

IPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009068. S15_NS1_RNA-bd.
IPR002306. Trp-tRNA-synth.
IPR000738. WHEP-TRS.
[Graphical view]

Gene3D

G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
G3DSA:1.10.287.10. S15_NS1_RNA_bd. 1 hit.

KO

K01867.

PANTHER

PTHR10055. Trp_tRNA-synt_1b. 1 hit.

Pfam

PF00579. tRNA-synt_1b. 1 hit.
PF00458. WHEP-TRS. 1 hit.
[Graphical view]

PRINTS

PR01039. TRNASYNTHTRP.

SMART

SM00991. WHEP-TRS. 1 hit.
[Graphical view]

SUPFAM

SSF47060. S15/NS1_bind. 1 hit.

TIGRFAMs

TIGR00233. TrpS. 1 hit.

PROSITE

PS00178. AA_TRNA_LIGASE_I. 1 hit.
PS00762. WHEP_TRS_1. 1 hit.
PS51185. WHEP_TRS_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00150. L-Tryptophan.

NextBio

29178.

SOURCE

Search...

Entry information

Entry name

SYWC_HUMAN

Accession

Primary (citable) accession number: P23381
Secondary accession number(s): A6NGN1 , A6NID3, P78535, Q502Y0, Q53XB6, Q9UDI5, Q9UDL3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	December 1, 1992
Last modified:	January 25, 2012
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.