Reviewed, UniProtKB/Swiss-Prot Q9BW92 (SYTM_HUMAN)

Names and origin

Protein names

Recommended name:
    Threonyl-tRNA synthetase, mitochondrial
    EC=6.1.1.3
Alternative name(s):
    Threonine--tRNA ligase
      Short name=ThrRS
    Threonyl-tRNA synthetase-like 1

Gene names

Name:	TARS2
Synonyms:	TARSL1

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

Protein attributes

Sequence length	718 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr).
Subcellular location	Mitochondrion matrix By similarity.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	threonyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW threonine-tRNA ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 718		Threonyl-tRNA synthetase, mitochondrial		PRO_0000254586
Experimental info
	Sequence conflict	269	1	A → P in BAD96534. Ref.1
	Sequence conflict	579	1	E → G in BAD96534. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9BW92-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: A2F793A60483E7F9	FASTA	718	81,036
	10 20 30 40 50 60 MALYQRWRCL RLQGLQACRL HTAVVSTPPR WLAERLGLFE ELWAAQVKRL ASMAQKEPRT 70 80 90 100 110 120 IKISLPGGQK IDAVAWNTTP YQLARQISST LADTAVAAQV NGEPYDLERP LETDSDLRFL 130 140 150 160 170 180 TFDSPEGKAV FWHSSTHVLG AAAEQFLGAV LCRGPSTEYG FYHDFFLGKE RTIRGSELPV 190 200 210 220 230 240 LERICQELTA AARPFRRLEA SRDQLRQLFK DNPFKLHLIE EKVTGPTATV YGCGTLVDLC 250 260 270 280 290 300 QGPHLRHTGQ IGGLKLLSNS SSLWRSSGAP ETLQRVSGIS FPTTELLRVW EAWREEAELR 310 320 330 340 350 360 DHRRIGKEQE LFFFHELSPG SCFFLPRGTR VYNALVAFIR AEYAHRGFSE VKTPTLFSTK 370 380 390 400 410 420 LWEQSGHWEH YQEDMFAVQP PGSDRPPSSQ SDDSTRHITD TLALKPMNCP AHCLMFAHRP 430 440 450 460 470 480 RSWRELPLRL ADFGALHRAE ASGGLGGLTR LRCFQQDDAH IFCTTDQLEA EIQSCLDFLR 490 500 510 520 530 540 SVYAVLGFSF RLALSTRPSG FLGDPCLWDQ AEQVLKQALK EFGEPWDLNS GDGAFYGPKI 550 560 570 580 590 600 DVHLHDALGR PHQCGTIQLD FQLPLRFDLQ YKGQAGALER PVLIHRAVLG SVERLLGVLA 610 620 630 640 650 660 ESCGGKWPLW LSPFQVVVIP VGSEQEEYAK EAQQSLRAAG LVSDLDADSG LTLSRRIRRA 670 680 690 700 710 QLAHYNFQFV VGQKEQSKRT VNIRTRDNRR LGEWDLPEAV QRLVELQNTR VPNAEEIF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	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]. Tissue: Liver.
[2]	"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: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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: Brain and Lung.
[4]	"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: 15779907] [Abstract] Cited for: IDENTIFICATION.
[5]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK222814 mRNA. Translation: BAD96534.1. AL356356 Genomic DNA. Translation: CAI15488.1. BC000541 mRNA. Translation: AAH00541.1. BC007824 mRNA. Translation: AAH07824.2. BC009997 mRNA. Translation: AAH09997.1.
IPI	IPI00604527.
RefSeq	NP_079426.2.
UniGene	Hs.288974
3D structure databases
HSSP	HSSP built from PDB template 1WWT based on UniProtKB P26639.
SMR	Q9BW92. Positions 300-715.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9BW92. 1 interaction.
STRING	Q9BW92.
Proteomic databases
PRIDE	Q9BW92.
Genome annotation databases
Ensembl	ENST00000369064; ENSP00000358060; ENSG00000143374; Homo sapiens. [Genome view]
GeneID	80222.
KEGG	hsa:80222.
NMPDR	fig|9606.3.peg.1960.
UCSC	uc001euq.1. human.
Organism-specific databases
CTD	80222.
GeneCards	GC01P148727.
HGNC	HGNC:30740. TARS2.
PharmGKB	PA134951561.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG06465.
HOGENOM	HBG352811.
HOVERGEN	Q9BW92.
InParanoid	Q9BW92.
OMA	ILIENHA.
OrthoDB	EOG9C5G53.
PhylomeDB	Q9BW92.
Enzyme and pathway databases
BRENDA	6.1.1.3. 247.
Reactome	REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	Q9BW92.
Bgee	Q9BW92.
CleanEx	HS_TARS2.
Genevestigator	Q9BW92.
GermOnline	ENSG00000143374. Homo sapiens.
Family and domain databases
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-dom. IPR006195. aa-tRNA-synth_II_cons-dom. IPR004154. Anticodon_bd. IPR012675. b-grasp_ferredoxin-like. IPR004095. TGS. IPR012676. TGS-like. IPR002320. Thr-tRNA-synth_IIa. IPR018158. Thr-tRNA-synth_IIa_cons-reg. IPR018163. Thr/Ala-tRNA-synth_IIc_edit. 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.
SMART	SM00863. tRNA_SAD. 1 hit. [Graphical view]
TIGRFAMs	TIGR00418. thrS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00156. L-Threonine.
NextBio	70637.

Entry information

Entry name

SYTM_HUMAN

Accession

Primary (citable) accession number: Q9BW92
Secondary accession number(s): Q53GW7, Q96I50

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	June 1, 2001
Last modified:	February 9, 2010
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.