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P23381

- SYWC_HUMAN

UniProt

P23381 - SYWC_HUMAN

Protein

Tryptophan--tRNA ligase, cytoplasmic

Gene

WARS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 2 (01 Dec 1992)
      Previous versions | rss
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    Functioni

    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.4 Publications

    Catalytic activityi

    ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp).

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. tryptophan-tRNA ligase activity Source: UniProtKB

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. gene expression Source: Reactome
    3. negative regulation of cell proliferation Source: ProtInc
    4. regulation of angiogenesis Source: UniProtKB
    5. translation Source: ProtInc
    6. tRNA aminoacylation for protein translation Source: Reactome
    7. tryptophanyl-tRNA aminoacylation Source: UniProtKB

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Angiogenesis, Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_15306. Cytosolic tRNA aminoacylation.

    Names & Taxonomyi

    Protein namesi
    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:
    Gene namesi
    Name:WARS
    Synonyms:IFI53, WRS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:12729. WARS.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. nucleus Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37340.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 471470Tryptophan--tRNA ligase, cytoplasmicPRO_0000136738Add
    BLAST
    Chaini71 – 471401T1-TrpRSPRO_0000386461Add
    BLAST
    Chaini94 – 471378T2-TrpRSPRO_0000386462Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei154 – 1541N6-succinyllysineBy similarity

    Post-translational modificationi

    Proteolytic cleavage generates 2 forms; T1-TrpRS and T2-TrpRS.1 Publication

    Proteomic databases

    MaxQBiP23381.
    PaxDbiP23381.
    PeptideAtlasiP23381.
    PRIDEiP23381.

    2D gel databases

    OGPiP23381.

    PTM databases

    PhosphoSiteiP23381.

    Expressioni

    Inductioni

    By IFNG/IFN-gamma.1 Publication

    Gene expression databases

    ArrayExpressiP23381.
    BgeeiP23381.
    CleanExiHS_WARS.
    GenevestigatoriP23381.

    Organism-specific databases

    HPAiHPA018944.

    Interactioni

    Subunit structurei

    Homodimer. Isoform 1 and isoform 2 interact with an oxidized form of GAPDH. GAPDH stimulates the aminoacylation activity of isoform 2.

    Protein-protein interaction databases

    BioGridi113292. 34 interactions.
    DIPiDIP-29493N.
    IntActiP23381. 5 interactions.
    MINTiMINT-1408962.
    STRINGi9606.ENSP00000347495.

    Structurei

    Secondary structure

    1
    471
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 2821
    Helixi33 – 5321
    Beta strandi54 – 563
    Beta strandi84 – 863
    Beta strandi89 – 913
    Turni100 – 1023
    Helixi103 – 1064
    Helixi114 – 12411
    Helixi130 – 1334
    Beta strandi136 – 1427
    Helixi143 – 1508
    Turni151 – 1533
    Beta strandi156 – 1627
    Helixi171 – 18717
    Beta strandi191 – 1955
    Helixi197 – 2037
    Helixi208 – 22316
    Turni224 – 2263
    Helixi229 – 2313
    Beta strandi232 – 2365
    Helixi237 – 2404
    Helixi241 – 2433
    Helixi247 – 25610
    Helixi260 – 2678
    Beta strandi271 – 2744
    Helixi275 – 28511
    Helixi286 – 2883
    Helixi290 – 2923
    Helixi294 – 2974
    Beta strandi304 – 3107
    Helixi311 – 3133
    Helixi314 – 32310
    Helixi324 – 3274
    Beta strandi333 – 3375
    Beta strandi345 – 3495
    Beta strandi354 – 3574
    Beta strandi360 – 3623
    Helixi365 – 37410
    Helixi384 – 3907
    Turni394 – 3963
    Helixi398 – 4069
    Helixi410 – 42213
    Beta strandi423 – 4253
    Helixi430 – 45021
    Helixi454 – 4607

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP23381.
    SMRiP23381. Positions 82-471.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23381.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini8 – 6457WHEP-TRSPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi164 – 17310"HIGH" region
    Motifi349 – 3535"KMSKS" region

    Sequence similaritiesi

    Contains 1 WHEP-TRS domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0180.
    HOVERGENiHBG002325.
    InParanoidiP23381.
    KOiK01867.
    OMAiKTFIFNN.
    OrthoDBiEOG7T4MK3.
    PhylomeDBiP23381.
    TreeFamiTF105669.

    Family and domain databases

    Gene3Di1.10.287.10. 1 hit.
    3.40.50.620. 1 hit.
    InterProiIPR001412. 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]
    PANTHERiPTHR10055. PTHR10055. 1 hit.
    PfamiPF00579. tRNA-synt_1b. 1 hit.
    PF00458. WHEP-TRS. 1 hit.
    [Graphical view]
    PRINTSiPR01039. TRNASYNTHTRP.
    SMARTiSM00991. WHEP-TRS. 1 hit.
    [Graphical view]
    SUPFAMiSSF47060. SSF47060. 1 hit.
    TIGRFAMsiTIGR00233. trpS. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    PS00762. WHEP_TRS_1. 1 hit.
    PS51185. WHEP_TRS_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P23381-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MPNSEPASLL ELFNSIATQG ELVRSLKAGN ASKDEIDSAV KMLVSLKMSY    50
    KAAAGEDYKA DCPPGNPAPT SNHGPDATEA EEDFVDPWTV QTSSAKGIDY 100
    DKLIVRFGSS KIDKELINRI ERATGQRPHH FLRRGIFFSH RDMNQVLDAY 150
    ENKKPFYLYT GRGPSSEAMH VGHLIPFIFT KWLQDVFNVP LVIQMTDDEK 200
    YLWKDLTLDQ AYSYAVENAK DIIACGFDIN KTFIFSDLDY MGMSSGFYKN 250
    VVKIQKHVTF NQVKGIFGFT DSDCIGKISF PAIQAAPSFS NSFPQIFRDR 300
    TDIQCLIPCA IDQDPYFRMT RDVAPRIGYP KPALLHSTFF PALQGAQTKM 350
    SASDPNSSIF LTDTAKQIKT KVNKHAFSGG RDTIEEHRQF GGNCDVDVSF 400
    MYLTFFLEDD DKLEQIRKDY TSGAMLTGEL KKALIEVLQP LIAEHQARRK 450
    EVTDEIVKEF MTPRKLSFDF Q 471
    Length:471
    Mass (Da):53,165
    Last modified:December 1, 1992 - v2
    Checksum:iE96344449053A0D0
    GO
    Isoform 2 (identifier: P23381-2) [UniParc]FASTAAdd to Basket

    Also known as: mini TrpRS

    The sequence of this isoform differs from the canonical sequence as follows:
         1-41: Missing.

    Show »
    Length:430
    Mass (Da):48,852
    Checksum:i5FE1254E781221DD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti213 – 2142SY → GD in AAA61298. (PubMed:1765274)Curated
    Sequence conflicti310 – 3101A → V in AAH95453. (PubMed:15489334)Curated
    Sequence conflicti424 – 4241A → R in CAA44450. (PubMed:1537332)Curated
    Sequence conflicti439 – 4391Q → L in AAH95453. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti54 – 541A → S.
    Corresponds to variant rs2234521 [ dbSNP | Ensembl ].
    VAR_052406
    Natural varianti455 – 4551E → D in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036466

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4141Missing in isoform 2. 1 PublicationVSP_038221Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    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.
    CCDSiCCDS9960.1. [P23381-1]
    CCDS9961.1. [P23381-2]
    PIRiA41633. A41706.
    RefSeqiNP_004175.2. NM_004184.3. [P23381-1]
    NP_776049.1. NM_173701.1. [P23381-1]
    NP_998810.1. NM_213645.1.
    NP_998811.1. NM_213646.1.
    XP_005268101.1. XM_005268044.1. [P23381-1]
    XP_006720311.1. XM_006720248.1. [P23381-1]
    XP_006720312.1. XM_006720249.1. [P23381-1]
    UniGeneiHs.497599.

    Genome annotation databases

    EnsembliENST00000344102; ENSP00000339485; ENSG00000140105. [P23381-2]
    ENST00000355338; ENSP00000347495; ENSG00000140105. [P23381-1]
    ENST00000358655; ENSP00000351481; ENSG00000140105. [P23381-2]
    ENST00000392882; ENSP00000376620; ENSG00000140105. [P23381-1]
    ENST00000556645; ENSP00000451887; ENSG00000140105. [P23381-2]
    ENST00000557135; ENSP00000451460; ENSG00000140105. [P23381-1]
    GeneIDi7453.
    KEGGihsa:7453.
    UCSCiuc001yhg.2. human. [P23381-1]

    Polymorphism databases

    DMDMi135191.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    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 .
    CCDSi CCDS9960.1. [P23381-1 ]
    CCDS9961.1. [P23381-2 ]
    PIRi A41633. A41706.
    RefSeqi NP_004175.2. NM_004184.3. [P23381-1 ]
    NP_776049.1. NM_173701.1. [P23381-1 ]
    NP_998810.1. NM_213645.1.
    NP_998811.1. NM_213646.1.
    XP_005268101.1. XM_005268044.1. [P23381-1 ]
    XP_006720311.1. XM_006720248.1. [P23381-1 ]
    XP_006720312.1. XM_006720249.1. [P23381-1 ]
    UniGenei Hs.497599.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali P23381.
    SMRi P23381. Positions 82-471.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113292. 34 interactions.
    DIPi DIP-29493N.
    IntActi P23381. 5 interactions.
    MINTi MINT-1408962.
    STRINGi 9606.ENSP00000347495.

    Chemistry

    DrugBanki DB00150. L-Tryptophan.

    PTM databases

    PhosphoSitei P23381.

    Polymorphism databases

    DMDMi 135191.

    2D gel databases

    OGPi P23381.

    Proteomic databases

    MaxQBi P23381.
    PaxDbi P23381.
    PeptideAtlasi P23381.
    PRIDEi P23381.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000344102 ; ENSP00000339485 ; ENSG00000140105 . [P23381-2 ]
    ENST00000355338 ; ENSP00000347495 ; ENSG00000140105 . [P23381-1 ]
    ENST00000358655 ; ENSP00000351481 ; ENSG00000140105 . [P23381-2 ]
    ENST00000392882 ; ENSP00000376620 ; ENSG00000140105 . [P23381-1 ]
    ENST00000556645 ; ENSP00000451887 ; ENSG00000140105 . [P23381-2 ]
    ENST00000557135 ; ENSP00000451460 ; ENSG00000140105 . [P23381-1 ]
    GeneIDi 7453.
    KEGGi hsa:7453.
    UCSCi uc001yhg.2. human. [P23381-1 ]

    Organism-specific databases

    CTDi 7453.
    GeneCardsi GC14M100800.
    HGNCi HGNC:12729. WARS.
    HPAi HPA018944.
    MIMi 191050. gene.
    neXtProti NX_P23381.
    PharmGKBi PA37340.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0180.
    HOVERGENi HBG002325.
    InParanoidi P23381.
    KOi K01867.
    OMAi KTFIFNN.
    OrthoDBi EOG7T4MK3.
    PhylomeDBi P23381.
    TreeFami TF105669.

    Enzyme and pathway databases

    Reactomei REACT_15306. Cytosolic tRNA aminoacylation.

    Miscellaneous databases

    ChiTaRSi WARS. human.
    EvolutionaryTracei P23381.
    GeneWikii WARS_(gene).
    GenomeRNAii 7453.
    NextBioi 29178.
    PROi P23381.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P23381.
    Bgeei P23381.
    CleanExi HS_WARS.
    Genevestigatori P23381.

    Family and domain databases

    Gene3Di 1.10.287.10. 1 hit.
    3.40.50.620. 1 hit.
    InterProi 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-ligase.
    IPR000738. WHEP-TRS.
    [Graphical view ]
    PANTHERi PTHR10055. PTHR10055. 1 hit.
    Pfami PF00579. tRNA-synt_1b. 1 hit.
    PF00458. WHEP-TRS. 1 hit.
    [Graphical view ]
    PRINTSi PR01039. TRNASYNTHTRP.
    SMARTi SM00991. WHEP-TRS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47060. SSF47060. 1 hit.
    TIGRFAMsi TIGR00233. trpS. 1 hit.
    PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
    PS00762. WHEP_TRS_1. 1 hit.
    PS51185. WHEP_TRS_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-455.

    Entry informationi

    Entry nameiSYWC_HUMAN
    AccessioniPrimary (citable) accession number: P23381
    Secondary accession number(s): A6NGN1
    , A6NID3, P78535, Q502Y0, Q53XB6, Q9UDI5, Q9UDL3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 151 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3