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P26639 (SYTC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 155. 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:
Threonine--tRNA ligase, cytoplasmic

EC=6.1.1.3
Alternative name(s):
Threonyl-tRNA synthetase
Short name=ThrRS
Gene names
Name:TARS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length723 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr). HAMAP-Rule MF_00184

Subunit structure

Homodimer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00184.

Post-translational modification

ISGylated. Ref.6

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Sequence caution

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P26639-1)

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: P26639-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 723723Threonine--tRNA ligase, cytoplasmic HAMAP-Rule MF_00184
PRO_0000101119

Amino acid modifications

Modified residue2431N6-acetyllysine Ref.8
Modified residue2981Phosphotyrosine By similarity
Cross-link222Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7

Natural variations

Alternative sequence1101S → SHTASCKNLSSLASLLASVA IPSSGMPWPPLFFL in isoform 2.
VSP_045114
Natural variant211G → D.
Corresponds to variant rs34334786 [ dbSNP | Ensembl ].
VAR_034533

Experimental info

Sequence conflict1641A → G in AAB04939. Ref.1
Sequence conflict3501A → V in AAB04939. Ref.1
Sequence conflict4171C → S in AAB04939. Ref.1
Sequence conflict4391V → G in AAB04939. Ref.1
Sequence conflict4531T → I in AAH10578. Ref.5
Sequence conflict5811D → E in AAB04939. Ref.1
Sequence conflict6121W → LA in AAB04939. Ref.1
Sequence conflict6361K → N in AAB04939. Ref.1
Sequence conflict6831S → T in AAB04939. Ref.1

Secondary structure

......................................................................................... 723
Helix Strand Turn

Details...

Sequences

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

Last modified February 15, 2005. Version 3.
Checksum: 885745118972C5A9

FASTA72383,435
        10         20         30         40         50         60 
MFEEKASSPS GKMGGEEKPI GAGEEKQKEG GKKKNKEGSG DGGRAELNPW PEYIYTRLEM 

        70         80         90        100        110        120 
YNILKAEHDS ILAEKAEKDS KPIKVTLPDG KQVDAESWKT TPYQIACGIS QGLADNTVIA 

       130        140        150        160        170        180 
KVNNVVWDLD RPLEEDCTLE LLKFEDEEAQ AVYWHSSAHI MGEAMERVYG GCLCYGPPIE 

       190        200        210        220        230        240 
NGFYYDMYLE EGGVSSNDFS SLEALCKKII KEKQAFERLE VKKETLLAMF KYNKFKCRIL 

       250        260        270        280        290        300 
NEKVNTPTTT VYRCGPLIDL CRGPHVRHTG KIKALKIHKN SSTYWEGKAD METLQRIYGI 

       310        320        330        340        350        360 
SFPDPKMLKE WEKFQEEAKN RDHRKIGRDQ ELYFFHELSP GSCFFLPKGA YIYNALIEFI 

       370        380        390        400        410        420 
RSEYRKRGFQ EVVTPNIFNS RLWMTSGHWQ HYSENMFSFE VEKELFALKP MNCPGHCLMF 

       430        440        450        460        470        480 
DHRPRSWREL PLRLADFGVL HRNELSGALT GLTRVRRFQQ DDAHIFCAME QIEDEIKGCL 

       490        500        510        520        530        540 
DFLRTVYSVF GFSFKLNLST RPEKFLGDIE VWDQAEKQLE NSLNEFGEKW ELNSGDGAFY 

       550        560        570        580        590        600 
GPKIDIQIKD AIGRYHQCAT IQLDFQLPIR FNLTYVSHDG DDKKRPVIVH RAILGSVERM 

       610        620        630        640        650        660 
IAILTENYGG KWPFWLSPRQ VMVVPVGPTC DEYAQKVRQQ FHDAKFMADI DLDPGCTLNK 

       670        680        690        700        710        720 
KIRNAQLAQY NFILVVGEKE KISGTVNIRT RDNKVHGERT ISETIERLQQ LKEFRSKQAE 


EEF 

« Hide

Isoform 2 [UniParc].

Checksum: E3516F3A14CBC746
Show »

FASTA75686,861

References

« Hide 'large scale' references
[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. 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: 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. expand/collapse author list , 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]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].
[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]"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells."
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.
Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract]
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]"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].
[10]"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].
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRYSHUT. A38867.
RefSeqNP_001245366.1. NM_001258437.1.
NP_001245367.1. NM_001258438.1.
NP_689508.3. NM_152295.4.
UniGeneHs.481860.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WWTNMR-A79-153[»]
4HWTX-ray2.30A/B321-723[»]
ProteinModelPortalP26639.
SMRP26639. Positions 81-722.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112760. 50 interactions.
IntActP26639. 12 interactions.
MINTMINT-3010570.
STRING9606.ENSP00000265112.

Chemistry

BindingDBP26639.
ChEMBLCHEMBL3391.
DrugBankDB00156. L-Threonine.

PTM databases

PhosphoSiteP26639.

Polymorphism databases

DMDM60267755.

Proteomic databases

PaxDbP26639.
PeptideAtlasP26639.
PRIDEP26639.

Protocols and materials databases

DNASU6897.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265112; ENSP00000265112; ENSG00000113407. [P26639-1]
ENST00000455217; ENSP00000387710; ENSG00000113407. [P26639-2]
ENST00000502553; ENSP00000424387; ENSG00000113407. [P26639-1]
GeneID6897.
KEGGhsa:6897.
UCSCuc003jhy.4. human. [P26639-1]
uc011coc.3. human.

Organism-specific databases

CTD6897.
GeneCardsGC05P033476.
H-InvDBHIX0004790.
HGNCHGNC:11572. TARS.
HPAHPA037425.
MIM187790. gene.
neXtProtNX_P26639.
PharmGKBPA36337.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0441.
HOGENOMHOG000003878.
HOVERGENHBG059513.
InParanoidP26639.
KOK01868.
OMAGFFYDMS.
OrthoDBEOG7JDQX3.
PhylomeDBP26639.
TreeFamTF300858.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressP26639.
BgeeP26639.
CleanExHS_TARS.
GenevestigatorP26639.

Family and domain databases

Gene3D3.10.20.30. 1 hit.
3.40.50.800. 1 hit.
HAMAPMF_00184. Thr_tRNA_synth.
InterProIPR002314. 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]
PfamPF03129. HGTP_anticodon. 1 hit.
PF02824. TGS. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSPR01047. TRNASYNTHTHR.
SMARTSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMSSF52954. SSF52954. 1 hit.
SSF55186. SSF55186. 1 hit.
SSF81271. SSF81271. 1 hit.
TIGRFAMsTIGR00418. thrS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP26639.
GeneWikiTARS_(gene).
GenomeRNAi6897.
NextBio26959.
PROP26639.
SOURCESearch...

Entry information

Entry nameSYTC_HUMAN
AccessionPrimary (citable) accession number: P26639
Secondary accession number(s): A8K8I1 expand/collapse secondary AC list , B4DEG8, Q96FP5, Q9BWA6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: February 15, 2005
Last modified: April 16, 2014
This is version 155 of the entry and version 3 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 5

Human chromosome 5: entries, gene names and cross-references to MIM

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries