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Q9BW92

- SYTM_HUMAN

UniProt

Q9BW92 - SYTM_HUMAN

Protein

Threonine--tRNA ligase, mitochondrial

Gene

TARS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr).

    GO - Molecular functioni

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

    GO - Biological processi

    1. gene expression Source: Reactome
    2. mitochondrial threonyl-tRNA aminoacylation Source: BHF-UCL
    3. tRNA aminoacylation for protein translation Source: Reactome

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_15302. Mitochondrial tRNA aminoacylation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Threonine--tRNA ligase, mitochondrial (EC:6.1.1.3)
    Alternative name(s):
    Threonyl-tRNA synthetase
    Short name:
    ThrRS
    Threonyl-tRNA synthetase-like 1
    Gene namesi
    Name:TARS2
    Synonyms:TARSL1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:30740. TARS2.

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162405200.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 718Threonine--tRNA ligase, mitochondrialPRO_0000254586
    Transit peptidei1 – ?MitochondrionSequence Analysis

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei52 – 521Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9BW92.
    PaxDbiQ9BW92.
    PRIDEiQ9BW92.

    PTM databases

    PhosphoSiteiQ9BW92.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9BW92.
    BgeeiQ9BW92.
    CleanExiHS_TARS2.
    GenevestigatoriQ9BW92.

    Organism-specific databases

    HPAiHPA028626.

    Interactioni

    Protein-protein interaction databases

    BioGridi123188. 5 interactions.
    IntActiQ9BW92. 6 interactions.
    MINTiMINT-8052579.
    STRINGi9606.ENSP00000358060.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BW92.
    SMRiQ9BW92. Positions 59-716.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0441.
    HOGENOMiHOG000003878.
    HOVERGENiHBG059513.
    InParanoidiQ9BW92.
    KOiK01868.
    OMAiTVYGCGM.
    PhylomeDBiQ9BW92.
    TreeFamiTF300858.

    Family and domain databases

    Gene3Di3.10.20.30. 1 hit.
    3.40.50.800. 1 hit.
    HAMAPiMF_00184. Thr_tRNA_synth.
    InterProiIPR002314. aa-tRNA-synt_IIb_cons-dom.
    IPR006195. aa-tRNA-synth_II.
    IPR004154. Anticodon-bd.
    IPR012675. Beta-grasp_dom.
    IPR004095. TGS.
    IPR012676. TGS-like.
    IPR002320. Thr-tRNA-ligase_IIa.
    IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
    IPR012947. tRNA_SAD.
    [Graphical view]
    PfamiPF03129. HGTP_anticodon. 1 hit.
    PF02824. TGS. 1 hit.
    PF00587. tRNA-synt_2b. 1 hit.
    PF07973. tRNA_SAD. 1 hit.
    [Graphical view]
    PRINTSiPR01047. TRNASYNTHTHR.
    SMARTiSM00863. tRNA_SAD. 1 hit.
    [Graphical view]
    SUPFAMiSSF52954. SSF52954. 1 hit.
    SSF55186. SSF55186. 1 hit.
    SSF81271. SSF81271. 1 hit.
    TIGRFAMsiTIGR00418. thrS. 1 hit.
    PROSITEiPS50862. AA_TRNA_LIGASE_II. 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: Q9BW92-1) [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

    MALYQRWRCL RLQGLQACRL HTAVVSTPPR WLAERLGLFE ELWAAQVKRL    50
    ASMAQKEPRT IKISLPGGQK IDAVAWNTTP YQLARQISST LADTAVAAQV 100
    NGEPYDLERP LETDSDLRFL TFDSPEGKAV FWHSSTHVLG AAAEQFLGAV 150
    LCRGPSTEYG FYHDFFLGKE RTIRGSELPV LERICQELTA AARPFRRLEA 200
    SRDQLRQLFK DNPFKLHLIE EKVTGPTATV YGCGTLVDLC QGPHLRHTGQ 250
    IGGLKLLSNS SSLWRSSGAP ETLQRVSGIS FPTTELLRVW EAWREEAELR 300
    DHRRIGKEQE LFFFHELSPG SCFFLPRGTR VYNALVAFIR AEYAHRGFSE 350
    VKTPTLFSTK LWEQSGHWEH YQEDMFAVQP PGSDRPPSSQ SDDSTRHITD 400
    TLALKPMNCP AHCLMFAHRP RSWRELPLRL ADFGALHRAE ASGGLGGLTR 450
    LRCFQQDDAH IFCTTDQLEA EIQSCLDFLR SVYAVLGFSF RLALSTRPSG 500
    FLGDPCLWDQ AEQVLKQALK EFGEPWDLNS GDGAFYGPKI DVHLHDALGR 550
    PHQCGTIQLD FQLPLRFDLQ YKGQAGALER PVLIHRAVLG SVERLLGVLA 600
    ESCGGKWPLW LSPFQVVVIP VGSEQEEYAK EAQQSLRAAG LVSDLDADSG 650
    LTLSRRIRRA QLAHYNFQFV VGQKEQSKRT VNIRTRDNRR LGEWDLPEAV 700
    QRLVELQNTR VPNAEEIF 718
    Length:718
    Mass (Da):81,036
    Last modified:June 1, 2001 - v1
    Checksum:iA2F793A60483E7F9
    GO
    Isoform 2 (identifier: Q9BW92-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         211-340: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:588
    Mass (Da):66,372
    Checksum:i19A2BD2A6BB8C400
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti269 – 2691A → P in BAD96534. 1 PublicationCurated
    Sequence conflicti579 – 5791E → G in BAD96534. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei211 – 340130Missing in isoform 2. 1 PublicationVSP_054537Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK022590 mRNA. Translation: BAB14117.1.
    AK222814 mRNA. Translation: BAD96534.1.
    AL356356 Genomic DNA. Translation: CAI15488.1.
    CH471121 Genomic DNA. Translation: EAW53549.1.
    BC000541 mRNA. Translation: AAH00541.1.
    BC007824 mRNA. Translation: AAH07824.2.
    BC009997 mRNA. Translation: AAH09997.1.
    CCDSiCCDS60252.1. [Q9BW92-2]
    CCDS952.1. [Q9BW92-1]
    RefSeqiNP_001258825.1. NM_001271896.1. [Q9BW92-2]
    NP_079426.2. NM_025150.4. [Q9BW92-1]
    UniGeneiHs.288974.

    Genome annotation databases

    EnsembliENST00000369054; ENSP00000358050; ENSG00000143374. [Q9BW92-2]
    ENST00000369064; ENSP00000358060; ENSG00000143374. [Q9BW92-1]
    GeneIDi80222.
    KEGGihsa:80222.
    UCSCiuc001euq.4. human. [Q9BW92-1]
    uc009wls.4. human.

    Polymorphism databases

    DMDMi74752395.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK022590 mRNA. Translation: BAB14117.1 .
    AK222814 mRNA. Translation: BAD96534.1 .
    AL356356 Genomic DNA. Translation: CAI15488.1 .
    CH471121 Genomic DNA. Translation: EAW53549.1 .
    BC000541 mRNA. Translation: AAH00541.1 .
    BC007824 mRNA. Translation: AAH07824.2 .
    BC009997 mRNA. Translation: AAH09997.1 .
    CCDSi CCDS60252.1. [Q9BW92-2 ]
    CCDS952.1. [Q9BW92-1 ]
    RefSeqi NP_001258825.1. NM_001271896.1. [Q9BW92-2 ]
    NP_079426.2. NM_025150.4. [Q9BW92-1 ]
    UniGenei Hs.288974.

    3D structure databases

    ProteinModelPortali Q9BW92.
    SMRi Q9BW92. Positions 59-716.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123188. 5 interactions.
    IntActi Q9BW92. 6 interactions.
    MINTi MINT-8052579.
    STRINGi 9606.ENSP00000358060.

    Chemistry

    DrugBanki DB00156. L-Threonine.

    PTM databases

    PhosphoSitei Q9BW92.

    Polymorphism databases

    DMDMi 74752395.

    Proteomic databases

    MaxQBi Q9BW92.
    PaxDbi Q9BW92.
    PRIDEi Q9BW92.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369054 ; ENSP00000358050 ; ENSG00000143374 . [Q9BW92-2 ]
    ENST00000369064 ; ENSP00000358060 ; ENSG00000143374 . [Q9BW92-1 ]
    GeneIDi 80222.
    KEGGi hsa:80222.
    UCSCi uc001euq.4. human. [Q9BW92-1 ]
    uc009wls.4. human.

    Organism-specific databases

    CTDi 80222.
    GeneCardsi GC01P150459.
    HGNCi HGNC:30740. TARS2.
    HPAi HPA028626.
    MIMi 612805. gene.
    neXtProti NX_Q9BW92.
    PharmGKBi PA162405200.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0441.
    HOGENOMi HOG000003878.
    HOVERGENi HBG059513.
    InParanoidi Q9BW92.
    KOi K01868.
    OMAi TVYGCGM.
    PhylomeDBi Q9BW92.
    TreeFami TF300858.

    Enzyme and pathway databases

    Reactomei REACT_15302. Mitochondrial tRNA aminoacylation.

    Miscellaneous databases

    ChiTaRSi TARS2. human.
    GenomeRNAii 80222.
    NextBioi 70637.
    PROi Q9BW92.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BW92.
    Bgeei Q9BW92.
    CleanExi HS_TARS2.
    Genevestigatori Q9BW92.

    Family and domain databases

    Gene3Di 3.10.20.30. 1 hit.
    3.40.50.800. 1 hit.
    HAMAPi MF_00184. Thr_tRNA_synth.
    InterProi IPR002314. aa-tRNA-synt_IIb_cons-dom.
    IPR006195. aa-tRNA-synth_II.
    IPR004154. Anticodon-bd.
    IPR012675. Beta-grasp_dom.
    IPR004095. TGS.
    IPR012676. TGS-like.
    IPR002320. Thr-tRNA-ligase_IIa.
    IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
    IPR012947. tRNA_SAD.
    [Graphical view ]
    Pfami PF03129. HGTP_anticodon. 1 hit.
    PF02824. TGS. 1 hit.
    PF00587. tRNA-synt_2b. 1 hit.
    PF07973. tRNA_SAD. 1 hit.
    [Graphical view ]
    PRINTSi PR01047. TRNASYNTHTHR.
    SMARTi SM00863. tRNA_SAD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52954. SSF52954. 1 hit.
    SSF55186. SSF55186. 1 hit.
    SSF81271. SSF81271. 1 hit.
    TIGRFAMsi TIGR00418. thrS. 1 hit.
    PROSITEi PS50862. AA_TRNA_LIGASE_II. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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 2).
    2. 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: Liver.
    3. "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].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Brain and Lung.
    6. "Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS."
      Bonnefond L., Fender A., Rudinger-Thirion J., Giege R., Florentz C., Sissler M.
      Biochemistry 44:4805-4816(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSYTM_HUMAN
    AccessioniPrimary (citable) accession number: Q9BW92
    Secondary accession number(s): Q53GW7, Q96I50, Q9H9V2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2006
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 120 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3