Threonyl-tRNA synthetase, cytoplasmic

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Reviewed, UniProtKB/Swiss-Prot P26639 (SYTC_HUMAN)

Last modified July 7, 2009. Version 102. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Threonyl-tRNA synthetase, cytoplasmic
    EC=6.1.1.3
Alternative name(s):
    Threonine--tRNA ligase
      Short name=ThrRS

Gene names

Name:

TARS

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	723 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr).
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family.

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Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	threonyl-tRNA aminoacylation Ref.1 Non-traceable author statement. Source: UniProtKB
Cellular component	cytoplasm Ref.1 Non-traceable author statement. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein homodimerization activity Ref.1 Non-traceable author statement. Source: UniProtKB threonine-tRNA ligase activity Ref.1 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
BCAR3	O75815	1	EBI-1042683,EBI-702336
ELF3	P78545	1	EBI-1042683,EBI-1057285
HLA-B	P30480	1	EBI-1042683,EBI-1054175
MCC	P23508	1	EBI-1042683,EBI-307531
NDRG1	Q92597	1	EBI-1042683,EBI-716486
TRAF6	Q9Y4K3	1	EBI-1042683,EBI-359276
VHL	P40337	1	EBI-1042683,EBI-301246

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 723

723

Threonyl-tRNA synthetase, cytoplasmic

PRO_0000101119

Amino acid modifications

Modified residue

298

Phosphotyrosine Ref.3

Cross-link

222

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.4

Natural variations

Natural variant

G → D: dbSNP rs34334786.

VAR_034533

Experimental info

Sequence conflict

164

A → G in AAB04939. Ref.1

Sequence conflict

350

A → V in AAB04939. Ref.1

Sequence conflict

417

C → S in AAB04939. Ref.1

Sequence conflict

439

V → G in AAB04939. Ref.1

Sequence conflict

453

T → I in AAH10578. Ref.2

Sequence conflict

581

D → E in AAB04939. Ref.1

Sequence conflict

612

W → LA in AAB04939. Ref.1

Sequence conflict

636

K → N in AAB04939. Ref.1

Sequence conflict

683

S → T in AAB04939. Ref.1

Secondary structure

723

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P26639-1 [UniParc].

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

723

83,435

        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

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References

	« Hide 'large scale' referencesShow '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: 2033077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cervix and Lung.
[3]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-298, MASS SPECTROMETRY.
[4]	"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: 17203973] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-222, MASS SPECTROMETRY. Tissue: Lung adenocarcinoma.
[5]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[6]	"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.

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Cross-references

Sequence databases

M63180 mRNA. Translation: AAB04939.1. Different initiation.
BC000517 mRNA. Translation: AAH00517.2.
BC010578 mRNA. Translation: AAH10578.2.

IPI

IPI00329633.

PIR

YSHUT. A38867.

RefSeq

NP_689508.3.

UniGene

Hs.481860

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WWT	NMR	-	A	79-153	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P26639. 10 interactions.

PTM databases

PhosphoSite

P26639.

Proteomic databases

PeptideAtlas

P26639.

PRIDE

P26639.

Genome annotation databases

Ensembl

ENSG00000113407. Homo sapiens. [Contig view]

GeneID

6897.

KEGG

hsa:6897.

NMPDR

fig|9606.3.peg.25109.

UCSC

uc003jhy.1. human.

Organism-specific databases

GeneCards

GC05P033476.

HGNC

HGNC:11572. TARS.

MIM

187790. gene.

PharmGKB

PA36337.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P26639.

HOVERGEN

P26639.

OMA

P26639. KLWQTSG.

Enzyme and pathway databases

BRENDA

6.1.1.3. 247.

Reactome

REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P26639.

Bgee

P26639.

CleanEx

HS_TARS.

GermOnline

ENSG00000113407. Homo sapiens.

Family and domain databases

InterPro

IPR002314. aa-tRNA-synt_IIb_cons-reg.
IPR006195. aa-tRNA-synth_II_cons-reg.
IPR004154. Anticodon_bd.
IPR012675. b-grasp_ferredoxin-like.
IPR004095. TGS.
IPR002320. Thr-tRNA-synth_IIa.
IPR018158. Thr-tRNA-synth_IIa_cons-reg.
IPR012947. tRNA_SAD.
[Graphical view]

Gene3D

G3DSA:3.40.50.800. Anticodon_bd. 1 hit.
G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.

Pfam

PF03129. HGTP_anticodon. 1 hit.
PF02824. TGS. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]

PRINTS

PR01047. TRNASYNTHTHR.

TIGRFAMs

TIGR00418. thrS. 1 hit.

PROSITE

PS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00156. L-Threonine.

NextBio

26959.

SOURCE

Search...

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Entry information

Entry name

SYTC_HUMAN

Accession

Primary (citable) accession number: P26639
Secondary accession number(s): Q96FP5, Q9BWA6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	February 15, 2005
Last modified:	July 7, 2009
This is version 102 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Human chromosome 5

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents