TARS1

Protein identityUniProt · HPA

UniProt accession

P26639

Gene

TARS1

Ensembl

ENSG00000113407

Chromosome

5

Canonical length

723 aa

Protein class

Disease related genes, Enzymes, Human disease related genes, Metabolic proteins, Plasma proteins, Potential drug targets, Predicted intracellular proteins

Subcellular location

Actin filaments,Cytosol

Quaternary structure

Homodimer

OverviewNCBI Gene

Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. Threonyl-tRNA synthetase belongs to the class-II aminoacyl-tRNA synthetase family [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

723 residues, UniProt reviewed canonical sequence.

>P26639|TARS1
     1  MFEEKASSPS GKMGGEEKPI GAGEEKQKEG GKKKNKEGSG DGGRAELNPW PEYIYTRLEM
    61  YNILKAEHDS ILAEKAEKDS KPIKVTLPDG KQVDAESWKT TPYQIACGIS QGLADNTVIA
   121  KVNNVVWDLD RPLEEDCTLE LLKFEDEEAQ AVYWHSSAHI MGEAMERVYG GCLCYGPPIE
   181  NGFYYDMYLE EGGVSSNDFS SLEALCKKII KEKQAFERLE VKKETLLAMF KYNKFKCRIL
   241  NEKVNTPTTT VYRCGPLIDL CRGPHVRHTG KIKALKIHKN SSTYWEGKAD METLQRIYGI
   301  SFPDPKMLKE WEKFQEEAKN RDHRKIGRDQ ELYFFHELSP GSCFFLPKGA YIYNALIEFI
   361  RSEYRKRGFQ EVVTPNIFNS RLWMTSGHWQ HYSENMFSFE VEKELFALKP MNCPGHCLMF
   421  DHRPRSWREL PLRLADFGVL HRNELSGALT GLTRVRRFQQ DDAHIFCAME QIEDEIKGCL
   481  DFLRTVYSVF GFSFKLNLST RPEKFLGDIE VWDQAEKQLE NSLNEFGEKW ELNSGDGAFY
   541  GPKIDIQIKD AIGRYHQCAT IQLDFQLPIR FNLTYVSHDG DDKKRPVIVH RAILGSVERM
   601  IAILTENYGG KWPFWLSPRQ VMVVPVGPTC DEYAQKVRQQ FHDAKFMADI DLDPGCTLNK
   661  KIRNAQLAQY NFILVVGEKE KISGTVNIRT RDNKVHGERT ISETIERLQQ LKEFRSKQAE
   721  EEF

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against TARS1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Intracellular

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.27

Highest tissue expression

64 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about TARS1.

Disease | AllUniProt

Conditions TARS1 is implicated in, by any mechanism.

• Trichothiodystrophy 7, non-photosensitive (TTD7) MIM:618546

Disease | GeneticClinVar

5 pathogenic / likely-pathogenic of 186 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Trichothiodystrophy 7, nonphotosensitive

ReferencesPubMed · IEDB

Publications for TARS1 from three distinct lines of evidence, kept separate because they answer different questions: whether antibodies are directed at the protein, whether a B-cell epitope has been mapped on it, and whether a T-cell epitope has. Each is labelled with its source.

Sources: PubMed — antigen-level antibody evidence from a custom retrieval. Records matching a controlled set of autoantibody terms (the MeSH descriptors Autoantibodies and Autoantigens, with title and abstract term variants) were obtained through NCBI E-utilities, and their titles and abstracts parsed for constructions that direct an antibody at a named protein rather than for co-occurrence. Captured names were resolved against UniProt nomenclature and each antigen adjudicated individually against the source text. Bibliographic records from PubMed and MeSH, U.S. National Library of Medicine; citation metrics from NIH iCite (Hutchins et al., PLoS Biology 2016). Titles link to PubMed; abstracts are not reproduced here. The NLM does not endorse this analysis.

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.8

gnomAD pLI

0

DepMap mean gene effect

-1.9

DepMap dependency class

pan

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 12% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• threonyl-tRNA aminoacylation

Molecular functions

• ATP binding
• identical protein binding
• threonine-tRNA ligase activity
• tRNA binding
• zinc ion binding

Cellular components

• cytoplasm
• cytosol
• extracellular exosome

Protein domainsUniProt · Pfam · InterPro

• Aminoacyl-tRNA synthetase, class II (G/ P/ S/T)
• Threonine-tRNA ligase, class IIa
• TGS
• Anticodon-binding
• Aminoacyl-tRNA synthetase, class II
• Beta-grasp domain superfamily
• TGS-like
• Threonyl/alanyl tRNA synthetase, SAD
• Threonyl/alanyl tRNA synthetase, class II-like, putative editing domain superfamily
• Threonine-tRNA ligase catalytic core domain
• Anticodon-binding domain superfamily
• Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
• Threonine-tRNA ligase, class IIa, anticodon-binding domain
• tRNA synthetase class II core domain (G, H, P, S and T)
• TGS domain
• Anticodon binding domain
• Threonyl and Alanyl tRNA synthetase second additional domain

KeywordsUniProt

• Acetylation
• Aminoacyl-tRNA synthetase
• ATP-binding
• Cytoplasm
• Ligase
• Nucleotide-binding
• Phosphoprotein
• Protein biosynthesis
• RNA-binding
• tRNA-binding
• Ubl conjugation

InteractionsUniProt · HPA

Protein binding partners of TARS1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• TARS3