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Q9BW92 (SYTM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Threonine--tRNA ligase, mitochondrial
EC=6.1.1.3
Alternative name(s):
Threonyl-tRNA synthetase
Short name=ThrRS
Threonyl-tRNA synthetase-like 1
Gene names
Name:TARS2
Synonyms:TARSL1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length718 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processProtein biosynthesis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processmitochondrial threonyl-tRNA aminoacylation

Traceable author statement Ref.4. Source: BHF-UCL

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 718Threonine--tRNA ligase, mitochondrialPRO_0000254586

Experimental info

Sequence conflict2691A → P in BAD96534. Ref.1
Sequence conflict5791E → G in BAD96534. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9BW92 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: A2F793A60483E7F9

FASTA71881,036
        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

« Hide

References

« Hide '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. expand/collapse author list , 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]"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: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

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.
IPIIPI00604527.
RefSeqNP_079426.2. NM_025150.3.
UniGeneHs.288974.

3D structure databases

HSSPHSSP built from PDB template 1WWT based on UniProtKB P26639.
ProteinModelPortalQ9BW92.
SMRQ9BW92. Positions 55-711.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9BW92.

Polymorphism databases

DMDM74752395.

Proteomic databases

PRIDEQ9BW92.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369064; ENSP00000358060; ENSG00000143374.
GeneID80222.
KEGGhsa:80222.
NMPDRfig|9606.3.peg.1960.
UCSCuc001euq.1. human.

Organism-specific databases

CTD80222.
GeneCardsGC01P150459.
H-InvDBHIX0001027.
HGNCHGNC:30740. TARS2.
HPAHPA028626.
MIM612805. gene.
neXtProtNX_Q9BW92.
PharmGKBPA162405200.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG06465.
HOGENOMHBG352811.
HOVERGENHBG059513.
InParanoidQ9BW92.
OMAVGSDALW.
PhylomeDBQ9BW92.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ9BW92.
BgeeQ9BW92.
CleanExHS_TARS2.
GenevestigatorQ9BW92.
GermOnlineENSG00000143374. Homo sapiens.

Family and domain databases

InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR012675. Beta-grasp_ferredoxin-type.
IPR004095. TGS.
IPR012676. TGS-like.
IPR002320. Thr-tRNA-synth_IIa.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
Gene3DG3DSA:3.40.50.800. Anticodon_bd. 1 hit.
G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
KOK01868.
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. Anticodon_bd. 1 hit.
SSF81271. TGS-like. 1 hit.
SSF55186. Thr/Ala-tRNA-synth_IIc_edit. 1 hit.
TIGRFAMsTIGR00418. ThrS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

DrugBankDB00156. L-Threonine.
NextBio70637.
SOURCESearch...

Entry information

Entry nameSYTM_HUMAN
AccessionPrimary (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: January 25, 2012
This is version 93 of the entry and version 1 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

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents