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P26639

- SYTC_HUMAN

UniProt

P26639 - SYTC_HUMAN

Protein

Threonine--tRNA ligase, cytoplasmic

Gene

TARS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 3 (15 Feb 2005)
      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. protein homodimerization activity Source: UniProtKB
    3. threonine-tRNA ligase activity Source: UniProtKB

    GO - Biological processi

    1. gene expression Source: Reactome
    2. threonyl-tRNA aminoacylation Source: UniProtKB
    3. translation Source: UniProtKB
    4. 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_15306. Cytosolic tRNA aminoacylation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Threonine--tRNA ligase, cytoplasmic (EC:6.1.1.3)
    Alternative name(s):
    Threonyl-tRNA synthetase
    Short name:
    ThrRS
    Gene namesi
    Name:TARS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:11572. TARS.

    Subcellular locationi

    GO - Cellular componenti

    1. actin cytoskeleton Source: HPA
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: Reactome
    4. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36337.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 723723Threonine--tRNA ligase, cytoplasmicPRO_0000101119Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki222 – 222Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei243 – 2431N6-acetyllysine1 Publication
    Modified residuei298 – 2981PhosphotyrosineBy similarity

    Post-translational modificationi

    ISGylated.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP26639.
    PaxDbiP26639.
    PeptideAtlasiP26639.
    PRIDEiP26639.

    PTM databases

    PhosphoSiteiP26639.

    Expressioni

    Gene expression databases

    ArrayExpressiP26639.
    BgeeiP26639.
    CleanExiHS_TARS.
    GenevestigatoriP26639.

    Organism-specific databases

    HPAiHPA037425.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi112760. 53 interactions.
    IntActiP26639. 12 interactions.
    MINTiMINT-3010570.
    STRINGi9606.ENSP00000265112.

    Structurei

    Secondary structure

    1
    723
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi82 – 865
    Beta strandi92 – 965
    Turni97 – 993
    Helixi102 – 1087
    Turni111 – 1133
    Helixi114 – 1163
    Beta strandi120 – 1278
    Beta strandi129 – 1313
    Beta strandi135 – 1417
    Helixi323 – 3297
    Beta strandi332 – 3343
    Helixi347 – 36620
    Beta strandi376 – 3794
    Helixi380 – 3856
    Helixi388 – 3914
    Helixi393 – 3953
    Beta strandi398 – 4014
    Beta strandi404 – 4085
    Helixi413 – 4219
    Helixi427 – 4293
    Beta strandi431 – 4366
    Beta strandi439 – 4413
    Helixi446 – 4483
    Turni451 – 4533
    Beta strandi456 – 4594
    Beta strandi462 – 4676
    Helixi469 – 4713
    Helixi472 – 49019
    Beta strandi493 – 4997
    Helixi509 – 52517
    Beta strandi530 – 5334
    Beta strandi543 – 5497
    Beta strandi555 – 56511
    Helixi566 – 5705
    Beta strandi587 – 5959
    Helixi597 – 60711
    Turni608 – 6103
    Helixi614 – 6163
    Beta strandi621 – 6277
    Helixi628 – 6303
    Helixi631 – 64212
    Turni643 – 6453
    Beta strandi648 – 6503
    Helixi658 – 66710
    Beta strandi671 – 6766
    Helixi678 – 6836
    Beta strandi685 – 6906
    Beta strandi695 – 7006
    Helixi701 – 71313

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WWTNMR-A79-153[»]
    4HWTX-ray2.30A/B321-723[»]
    ProteinModelPortaliP26639.
    SMRiP26639. Positions 81-722.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP26639.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0441.
    HOGENOMiHOG000003878.
    HOVERGENiHBG059513.
    InParanoidiP26639.
    KOiK01868.
    OMAiYNSKLWQ.
    OrthoDBiEOG7JDQX3.
    PhylomeDBiP26639.
    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.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P26639-1) [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

    MFEEKASSPS GKMGGEEKPI GAGEEKQKEG GKKKNKEGSG DGGRAELNPW    50
    PEYIYTRLEM YNILKAEHDS ILAEKAEKDS KPIKVTLPDG KQVDAESWKT 100
    TPYQIACGIS QGLADNTVIA KVNNVVWDLD RPLEEDCTLE LLKFEDEEAQ 150
    AVYWHSSAHI MGEAMERVYG GCLCYGPPIE NGFYYDMYLE EGGVSSNDFS 200
    SLEALCKKII KEKQAFERLE VKKETLLAMF KYNKFKCRIL NEKVNTPTTT 250
    VYRCGPLIDL CRGPHVRHTG KIKALKIHKN SSTYWEGKAD METLQRIYGI 300
    SFPDPKMLKE WEKFQEEAKN RDHRKIGRDQ ELYFFHELSP GSCFFLPKGA 350
    YIYNALIEFI RSEYRKRGFQ EVVTPNIFNS RLWMTSGHWQ HYSENMFSFE 400
    VEKELFALKP MNCPGHCLMF DHRPRSWREL PLRLADFGVL HRNELSGALT 450
    GLTRVRRFQQ DDAHIFCAME QIEDEIKGCL DFLRTVYSVF GFSFKLNLST 500
    RPEKFLGDIE VWDQAEKQLE NSLNEFGEKW ELNSGDGAFY GPKIDIQIKD 550
    AIGRYHQCAT IQLDFQLPIR FNLTYVSHDG DDKKRPVIVH RAILGSVERM 600
    IAILTENYGG KWPFWLSPRQ VMVVPVGPTC DEYAQKVRQQ FHDAKFMADI 650
    DLDPGCTLNK KIRNAQLAQY NFILVVGEKE KISGTVNIRT RDNKVHGERT 700
    ISETIERLQQ LKEFRSKQAE EEF 723
    Length:723
    Mass (Da):83,435
    Last modified:February 15, 2005 - v3
    Checksum:i885745118972C5A9
    GO
    Isoform 2 (identifier: P26639-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         110-110: S → SHTASCKNLSSLASLLASVAIPSSGMPWPPLFFL

    Show »
    Length:756
    Mass (Da):86,861
    Checksum:iE3516F3A14CBC746
    GO

    Sequence cautioni

    The sequence AAB04939.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti164 – 1641A → G in AAB04939. (PubMed:2033077)Curated
    Sequence conflicti350 – 3501A → V in AAB04939. (PubMed:2033077)Curated
    Sequence conflicti417 – 4171C → S in AAB04939. (PubMed:2033077)Curated
    Sequence conflicti439 – 4391V → G in AAB04939. (PubMed:2033077)Curated
    Sequence conflicti453 – 4531T → I in AAH10578. (PubMed:15489334)Curated
    Sequence conflicti581 – 5811D → E in AAB04939. (PubMed:2033077)Curated
    Sequence conflicti612 – 6121W → LA in AAB04939. (PubMed:2033077)Curated
    Sequence conflicti636 – 6361K → N in AAB04939. (PubMed:2033077)Curated
    Sequence conflicti683 – 6831S → T in AAB04939. (PubMed:2033077)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti21 – 211G → D.
    Corresponds to variant rs34334786 [ dbSNP | Ensembl ].
    VAR_034533

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei110 – 1101S → SHTASCKNLSSLASLLASVA IPSSGMPWPPLFFL in isoform 2. 1 PublicationVSP_045114

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63180 mRNA. Translation: AAB04939.1. Different initiation.
    AK292346 mRNA. Translation: BAF85035.1.
    AK293620 mRNA. Translation: BAG57079.1.
    AC025441 Genomic DNA. No translation available.
    AC034231 Genomic DNA. No translation available.
    CH471118 Genomic DNA. Translation: EAX10804.1.
    BC000517 mRNA. Translation: AAH00517.2.
    BC010578 mRNA. Translation: AAH10578.2.
    CCDSiCCDS3899.1. [P26639-1]
    CCDS58943.1. [P26639-2]
    PIRiA38867. YSHUT.
    RefSeqiNP_001245366.1. NM_001258437.1. [P26639-1]
    NP_001245367.1. NM_001258438.1. [P26639-2]
    NP_689508.3. NM_152295.4. [P26639-1]
    UniGeneiHs.481860.

    Genome annotation databases

    EnsembliENST00000265112; ENSP00000265112; ENSG00000113407. [P26639-1]
    ENST00000455217; ENSP00000387710; ENSG00000113407. [P26639-2]
    ENST00000502553; ENSP00000424387; ENSG00000113407. [P26639-1]
    GeneIDi6897.
    KEGGihsa:6897.
    UCSCiuc003jhy.4. human. [P26639-1]
    uc011coc.3. human.

    Polymorphism databases

    DMDMi60267755.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63180 mRNA. Translation: AAB04939.1 . Different initiation.
    AK292346 mRNA. Translation: BAF85035.1 .
    AK293620 mRNA. Translation: BAG57079.1 .
    AC025441 Genomic DNA. No translation available.
    AC034231 Genomic DNA. No translation available.
    CH471118 Genomic DNA. Translation: EAX10804.1 .
    BC000517 mRNA. Translation: AAH00517.2 .
    BC010578 mRNA. Translation: AAH10578.2 .
    CCDSi CCDS3899.1. [P26639-1 ]
    CCDS58943.1. [P26639-2 ]
    PIRi A38867. YSHUT.
    RefSeqi NP_001245366.1. NM_001258437.1. [P26639-1 ]
    NP_001245367.1. NM_001258438.1. [P26639-2 ]
    NP_689508.3. NM_152295.4. [P26639-1 ]
    UniGenei Hs.481860.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WWT NMR - A 79-153 [» ]
    4HWT X-ray 2.30 A/B 321-723 [» ]
    ProteinModelPortali P26639.
    SMRi P26639. Positions 81-722.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112760. 53 interactions.
    IntActi P26639. 12 interactions.
    MINTi MINT-3010570.
    STRINGi 9606.ENSP00000265112.

    Chemistry

    BindingDBi P26639.
    ChEMBLi CHEMBL3391.
    DrugBanki DB00156. L-Threonine.

    PTM databases

    PhosphoSitei P26639.

    Polymorphism databases

    DMDMi 60267755.

    Proteomic databases

    MaxQBi P26639.
    PaxDbi P26639.
    PeptideAtlasi P26639.
    PRIDEi P26639.

    Protocols and materials databases

    DNASUi 6897.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265112 ; ENSP00000265112 ; ENSG00000113407 . [P26639-1 ]
    ENST00000455217 ; ENSP00000387710 ; ENSG00000113407 . [P26639-2 ]
    ENST00000502553 ; ENSP00000424387 ; ENSG00000113407 . [P26639-1 ]
    GeneIDi 6897.
    KEGGi hsa:6897.
    UCSCi uc003jhy.4. human. [P26639-1 ]
    uc011coc.3. human.

    Organism-specific databases

    CTDi 6897.
    GeneCardsi GC05P033476.
    H-InvDB HIX0004790.
    HGNCi HGNC:11572. TARS.
    HPAi HPA037425.
    MIMi 187790. gene.
    neXtProti NX_P26639.
    PharmGKBi PA36337.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0441.
    HOGENOMi HOG000003878.
    HOVERGENi HBG059513.
    InParanoidi P26639.
    KOi K01868.
    OMAi YNSKLWQ.
    OrthoDBi EOG7JDQX3.
    PhylomeDBi P26639.
    TreeFami TF300858.

    Enzyme and pathway databases

    Reactomei REACT_15306. Cytosolic tRNA aminoacylation.

    Miscellaneous databases

    EvolutionaryTracei P26639.
    GeneWikii TARS_(gene).
    GenomeRNAii 6897.
    NextBioi 26959.
    PROi P26639.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P26639.
    Bgeei P26639.
    CleanExi HS_TARS.
    Genevestigatori P26639.

    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. "Nucleotide and deduced amino acid sequence of human threonyl-tRNA synthetase reveals extensive homology to the Escherichia coli and yeast enzymes."
      Cruzen M.E., Arfin S.M.
      J. Biol. Chem. 266:9919-9923(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] (ISOFORMS 1 AND 2).
      Tissue: Cerebellum and Testis.
    3. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [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: Cervix and Lung.
    6. Cited for: ISGYLATION.
    7. "The proteomic reactor facilitates the analysis of affinity-purified proteins by mass spectrometry: application for identifying ubiquitinated proteins in human cells."
      Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M., Haines D.S., Figeys D.
      J. Proteome Res. 6:298-305(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-222.
      Tissue: Lung adenocarcinoma.
    8. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Solution structure of the TGS domain from human threonyl-tRNA synthetase."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUL-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 79-153.

    Entry informationi

    Entry nameiSYTC_HUMAN
    AccessioniPrimary (citable) accession number: P26639
    Secondary accession number(s): A8K8I1
    , B4DEG8, Q96FP5, Q9BWA6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: February 15, 2005
    Last modified: October 1, 2014
    This is version 160 of the entry and version 3 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, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. Human chromosome 5
      Human chromosome 5: 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