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Q9UGM6

- SYWM_HUMAN

UniProt

Q9UGM6 - SYWM_HUMAN

Protein

Tryptophan--tRNA ligase, mitochondrial

Gene

WARS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    GO - Molecular functioni

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

    GO - Biological processi

    1. gene expression Source: Reactome
    2. tRNA aminoacylation for protein translation Source: Reactome
    3. tryptophanyl-tRNA aminoacylation Source: InterPro
    4. vasculogenesis Source: Ensembl

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi6.1.1.2. 2681.
    ReactomeiREACT_15302. Mitochondrial tRNA aminoacylation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tryptophan--tRNA ligase, mitochondrial (EC:6.1.1.2)
    Alternative name(s):
    (Mt)TrpRS
    Tryptophanyl-tRNA synthetase
    Short name:
    TrpRS
    Gene namesi
    Name:WARS2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:12730. WARS2.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: Reactome

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37341.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 1818MitochondrionAdd
    BLAST
    Chaini19 – 360342Tryptophan--tRNA ligase, mitochondrialPRO_0000035828Add
    BLAST

    Proteomic databases

    MaxQBiQ9UGM6.
    PaxDbiQ9UGM6.
    PRIDEiQ9UGM6.

    PTM databases

    PhosphoSiteiQ9UGM6.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UGM6.
    BgeeiQ9UGM6.
    CleanExiHS_WARS2.
    GenevestigatoriQ9UGM6.

    Interactioni

    Protein-protein interaction databases

    BioGridi115633. 3 interactions.
    STRINGi9606.ENSP00000235521.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UGM6.
    SMRiQ9UGM6. Positions 35-359.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0180.
    HOGENOMiHOG000059940.
    HOVERGENiHBG027444.
    InParanoidiQ9UGM6.
    KOiK01867.
    OMAiSHILHRP.
    OrthoDBiEOG7J447N.
    PhylomeDBiQ9UGM6.
    TreeFamiTF314321.

    Family and domain databases

    Gene3Di3.40.50.620. 1 hit.
    HAMAPiMF_00140_B. Trp_tRNA_synth_B.
    InterProiIPR001412. aa-tRNA-synth_I_CS.
    IPR002305. aa-tRNA-synth_Ic.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR002306. Trp-tRNA-ligase.
    IPR024109. Trp-tRNA-ligase_bac-type.
    [Graphical view]
    PANTHERiPTHR10055. PTHR10055. 1 hit.
    PfamiPF00579. tRNA-synt_1b. 1 hit.
    [Graphical view]
    PRINTSiPR01039. TRNASYNTHTRP.
    TIGRFAMsiTIGR00233. trpS. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 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: Q9UGM6-1) [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

    MALHSMRKAR ERWSFIRALH KGSAAAPALQ KDSKKRVFSG IQPTGILHLG    50
    NYLGAIESWV RLQDEYDSVL YSIVDLHSIT VPQDPAVLRQ SILDMTAVLL 100
    ACGINPEKSI LFQQSQVSEH TQLSWILSCM VRLPRLQHLH QWKAKTTKQK 150
    HDGTVGLLTY PVLQAADILL YKSTHVPVGE DQVQHMELVQ DLAQGFNKKY 200
    GEFFPVPESI LTSMKKVKSL RDPSAKMSKS DPDKLATVRI TDSPEEIVQK 250
    FRKAVTDFTS EVTYDPAGRA GVSNIVAVHA AVTGLSVEEV VRRSAGMNTA 300
    RYKLAVADAV IEKFAPIKRE IEKLKLDKDH LEKVLQIGSA KAKELAYTVC 350
    QEVKKLVGFL 360
    Length:360
    Mass (Da):40,147
    Last modified:May 1, 2000 - v1
    Checksum:i8C80DF6FCA214A91
    GO
    Isoform 2 (identifier: Q9UGM6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         212-220: TSMKKVKSL → SMCVLVFLT
         221-360: Missing.

    Show »
    Length:220
    Mass (Da):24,813
    Checksum:i2535F75EDCD833F5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti151 – 1511H → R in BAD96917. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti50 – 501G → S.1 Publication
    Corresponds to variant rs11552864 [ dbSNP | Ensembl ].
    VAR_028848
    Natural varianti267 – 2671A → P.
    Corresponds to variant rs3790549 [ dbSNP | Ensembl ].
    VAR_020217
    Natural varianti360 – 3601L → P.
    Corresponds to variant rs17023101 [ dbSNP | Ensembl ].
    VAR_052407

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei212 – 2209TSMKKVKSL → SMCVLVFLT in isoform 2. 1 PublicationVSP_041414
    Alternative sequencei221 – 360140Missing in isoform 2. 1 PublicationVSP_041415Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ242739 mRNA. Translation: CAB63107.1.
    AK223197 mRNA. Translation: BAD96917.1.
    AK313740 mRNA. Translation: BAG36481.1.
    AL359823, AL139420, AL590288 Genomic DNA. Translation: CAI21995.1.
    AL359823, AL139420, AL590288 Genomic DNA. Translation: CAI21996.1.
    AL139420, AL359823, AL590288 Genomic DNA. Translation: CAI22501.1.
    AL139420, AL359823, AL590288 Genomic DNA. Translation: CAI22502.1.
    AL590288, AL359823, AL139420 Genomic DNA. Translation: CAH71367.1.
    AL590288, AL139420, AL359823 Genomic DNA. Translation: CAH71368.1.
    CH471122 Genomic DNA. Translation: EAW56693.1.
    BC044575 mRNA. Translation: AAH44575.1.
    BC039889 mRNA. No translation available.
    CCDSiCCDS30817.1. [Q9UGM6-2]
    CCDS900.1. [Q9UGM6-1]
    RefSeqiNP_056651.1. NM_015836.3. [Q9UGM6-1]
    NP_957715.1. NM_201263.2. [Q9UGM6-2]
    UniGeneiHs.523506.

    Genome annotation databases

    EnsembliENST00000235521; ENSP00000235521; ENSG00000116874. [Q9UGM6-1]
    ENST00000369426; ENSP00000358434; ENSG00000116874. [Q9UGM6-2]
    GeneIDi10352.
    KEGGihsa:10352.
    UCSCiuc001ehm.3. human. [Q9UGM6-2]
    uc001ehn.3. human. [Q9UGM6-1]

    Polymorphism databases

    DMDMi21362967.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ242739 mRNA. Translation: CAB63107.1 .
    AK223197 mRNA. Translation: BAD96917.1 .
    AK313740 mRNA. Translation: BAG36481.1 .
    AL359823 , AL139420 , AL590288 Genomic DNA. Translation: CAI21995.1 .
    AL359823 , AL139420 , AL590288 Genomic DNA. Translation: CAI21996.1 .
    AL139420 , AL359823 , AL590288 Genomic DNA. Translation: CAI22501.1 .
    AL139420 , AL359823 , AL590288 Genomic DNA. Translation: CAI22502.1 .
    AL590288 , AL359823 , AL139420 Genomic DNA. Translation: CAH71367.1 .
    AL590288 , AL139420 , AL359823 Genomic DNA. Translation: CAH71368.1 .
    CH471122 Genomic DNA. Translation: EAW56693.1 .
    BC044575 mRNA. Translation: AAH44575.1 .
    BC039889 mRNA. No translation available.
    CCDSi CCDS30817.1. [Q9UGM6-2 ]
    CCDS900.1. [Q9UGM6-1 ]
    RefSeqi NP_056651.1. NM_015836.3. [Q9UGM6-1 ]
    NP_957715.1. NM_201263.2. [Q9UGM6-2 ]
    UniGenei Hs.523506.

    3D structure databases

    ProteinModelPortali Q9UGM6.
    SMRi Q9UGM6. Positions 35-359.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115633. 3 interactions.
    STRINGi 9606.ENSP00000235521.

    Chemistry

    DrugBanki DB00150. L-Tryptophan.

    PTM databases

    PhosphoSitei Q9UGM6.

    Polymorphism databases

    DMDMi 21362967.

    Proteomic databases

    MaxQBi Q9UGM6.
    PaxDbi Q9UGM6.
    PRIDEi Q9UGM6.

    Protocols and materials databases

    DNASUi 10352.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000235521 ; ENSP00000235521 ; ENSG00000116874 . [Q9UGM6-1 ]
    ENST00000369426 ; ENSP00000358434 ; ENSG00000116874 . [Q9UGM6-2 ]
    GeneIDi 10352.
    KEGGi hsa:10352.
    UCSCi uc001ehm.3. human. [Q9UGM6-2 ]
    uc001ehn.3. human. [Q9UGM6-1 ]

    Organism-specific databases

    CTDi 10352.
    GeneCardsi GC01M119573.
    H-InvDB HIX0023588.
    HGNCi HGNC:12730. WARS2.
    MIMi 604733. gene.
    neXtProti NX_Q9UGM6.
    PharmGKBi PA37341.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0180.
    HOGENOMi HOG000059940.
    HOVERGENi HBG027444.
    InParanoidi Q9UGM6.
    KOi K01867.
    OMAi SHILHRP.
    OrthoDBi EOG7J447N.
    PhylomeDBi Q9UGM6.
    TreeFami TF314321.

    Enzyme and pathway databases

    BRENDAi 6.1.1.2. 2681.
    Reactomei REACT_15302. Mitochondrial tRNA aminoacylation.

    Miscellaneous databases

    ChiTaRSi WARS2. human.
    GeneWikii WARS2.
    GenomeRNAii 10352.
    NextBioi 39255.
    PROi Q9UGM6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UGM6.
    Bgeei Q9UGM6.
    CleanExi HS_WARS2.
    Genevestigatori Q9UGM6.

    Family and domain databases

    Gene3Di 3.40.50.620. 1 hit.
    HAMAPi MF_00140_B. Trp_tRNA_synth_B.
    InterProi IPR001412. aa-tRNA-synth_I_CS.
    IPR002305. aa-tRNA-synth_Ic.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR002306. Trp-tRNA-ligase.
    IPR024109. Trp-tRNA-ligase_bac-type.
    [Graphical view ]
    PANTHERi PTHR10055. PTHR10055. 1 hit.
    Pfami PF00579. tRNA-synt_1b. 1 hit.
    [Graphical view ]
    PRINTSi PR01039. TRNASYNTHTRP.
    TIGRFAMsi TIGR00233. trpS. 1 hit.
    PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of human mitochondrial tryptophanyl-tRNA synthetase."
      Jorgensen R., Soegaard T.M.M., Rossing A.B., Martensen P.M., Justesen J.
      J. Biol. Chem. 275:16820-16826(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
    2. "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] (ISOFORM 1).
    3. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Kidney proximal tubule.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORMS 1 AND 2), VARIANT SER-50.
      Tissue: Brain.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSYWM_HUMAN
    AccessioniPrimary (citable) accession number: Q9UGM6
    Secondary accession number(s): B1ALR1
    , B2R9D4, Q53FT4, Q5VUD2, Q86TQ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 6, 2002
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 118 of the entry and version 1 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

    Complete proteome, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. Human chromosome 1
      Human chromosome 1: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3