Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P23381 (SYWC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length471 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12 Ref.13
Chain2 – 471470Tryptophan--tRNA ligase, cytoplasmic
PRO_0000136738
Chain71 – 471401T1-TrpRS
PRO_0000386461
Chain94 – 471378T2-TrpRS
PRO_0000386462

Regions

Domain8 – 6457WHEP-TRS
Motif164 – 17310"HIGH" region
Motif349 – 3535"KMSKS" region

Amino acid modifications

Modified residue1541N6-succinyllysine By similarity

Natural variations

Alternative sequence1 – 4747Missing in isoform 2.
VSP_038221
Natural variant541A → S.
Corresponds to variant rs2234521 [ dbSNP | Ensembl ].
VAR_052406
Natural variant4551E → D in a breast cancer sample; somatic mutation. Ref.28
VAR_036466

Experimental info

Sequence conflict213 – 2142SY → GD in AAA61298. Ref.3
Sequence conflict3101A → V in AAH95453. Ref.9
Sequence conflict4241A → R in CAA44450. Ref.4
Sequence conflict4391Q → L in AAH95453. Ref.9

Secondary structure

............................................................................. 471
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 1992. Version 2.
Checksum: E96344449053A0D0

FASTA47153,165
        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 

« Hide

Isoform 2 (mini TrpRS) [UniParc].

Checksum: 92A3AA78DAE9D0AF
Show »

FASTA42448,180

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GAPDH.
[21]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-466.
[27]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 94-471.
[28]"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. expand/collapse author list , 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] [Europe PMC] [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 expand/collapse EMBL AC list , X67924, X67925, X67926, X67927, X67928 Genomic DNA. Translation: CAB94199.1.
PIRA41706. A41633.
RefSeqNP_004175.2. NM_004184.3.
NP_776049.1. NM_173701.1.
NP_998810.1. NM_213645.1.
NP_998811.1. NM_213646.1.
XP_005268101.1. XM_005268044.1.
UniGeneHs.497599.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1O5TX-ray2.50A94-471[»]
1R6TX-ray2.10A/B1-466[»]
1R6UX-ray2.00A/B48-471[»]
1ULHX-ray2.31A/B82-471[»]
2AKEX-ray3.10A94-471[»]
2AZXX-ray2.80A/B1-471[»]
2DR2X-ray3.00A94-471[»]
2QUHX-ray2.40A/B1-471[»]
2QUIX-ray2.40A/B1-471[»]
2QUJX-ray2.42A/B1-471[»]
2QUKX-ray2.80A1-471[»]
ProteinModelPortalP23381.
SMRP23381. Positions 82-471.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113292. 34 interactions.
DIPDIP-29493N.
IntActP23381. 5 interactions.
MINTMINT-1408962.
STRING9606.ENSP00000347495.

Chemistry

DrugBankDB00150. L-Tryptophan.

PTM databases

PhosphoSiteP23381.

Polymorphism databases

DMDM135191.

2D gel databases

OGPP23381.

Proteomic databases

PaxDbP23381.
PeptideAtlasP23381.
PRIDEP23381.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000344102; ENSP00000339485; ENSG00000140105.
ENST00000355338; ENSP00000347495; ENSG00000140105. [P23381-1]
ENST00000358655; ENSP00000351481; ENSG00000140105.
ENST00000392882; ENSP00000376620; ENSG00000140105. [P23381-1]
ENST00000556645; ENSP00000451887; ENSG00000140105.
ENST00000557135; ENSP00000451460; ENSG00000140105. [P23381-1]
GeneID7453.
KEGGhsa:7453.
UCSCuc001yhg.2. human. [P23381-1]

Organism-specific databases

CTD7453.
GeneCardsGC14M100800.
HGNCHGNC:12729. WARS.
HPAHPA018944.
MIM191050. gene.
neXtProtNX_P23381.
PharmGKBPA37340.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0180.
HOVERGENHBG002325.
InParanoidP23381.
KOK01867.
OMAKPETAIY.
OrthoDBEOG7T4MK3.
PhylomeDBP23381.
TreeFamTF105669.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressP23381.
BgeeP23381.
CleanExHS_WARS.
GenevestigatorP23381.

Family and domain databases

Gene3D1.10.287.10. 1 hit.
3.40.50.620. 1 hit.
InterProIPR001412. 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-ligase.
IPR000738. WHEP-TRS.
[Graphical view]
PANTHERPTHR10055. PTHR10055. 1 hit.
PfamPF00579. tRNA-synt_1b. 1 hit.
PF00458. WHEP-TRS. 1 hit.
[Graphical view]
PRINTSPR01039. TRNASYNTHTRP.
SMARTSM00991. WHEP-TRS. 1 hit.
[Graphical view]
SUPFAMSSF47060. SSF47060. 1 hit.
TIGRFAMsTIGR00233. trpS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
PS00762. WHEP_TRS_1. 1 hit.
PS51185. WHEP_TRS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSWARS. human.
EvolutionaryTraceP23381.
GeneWikiWARS_(gene).
GenomeRNAi7453.
NextBio29178.
PROP23381.
SOURCESearch...

Entry information

Entry nameSYWC_HUMAN
AccessionPrimary (citable) accession number: P23381
Secondary accession number(s): A6NGN1 expand/collapse secondary AC list , A6NID3, P78535, Q502Y0, Q53XB6, Q9UDI5, Q9UDL3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: December 1, 1992
Last modified: April 16, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries