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Q8BLY2 (SYTC2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Probable threonine--tRNA ligase 2, cytoplasmic
EC=6.1.1.3
Alternative name(s):
Threonyl-tRNA synthetase
Short name=ThrRS
Threonyl-tRNA synthetase-like protein 2
Gene names
Name:Tarsl2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length790 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

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

Subcellular location

Cytoplasm By similarity.

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processthreonyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

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

Initiator methionine11Removed By similarity
Chain2 – 790789Probable threonine--tRNA ligase 2, cytoplasmic
PRO_0000333829

Regions

Coiled coil13 – 6856 Potential

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Experimental info

Sequence conflict3811F → I in AAH39225. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8BLY2 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 50554D74CC75BB29

FASTA79091,318
        10         20         30         40         50         60 
MAAQALAAQA VASRLQRQEE DIRWLCAEVQ RLRDEQLRGP ERGQAEGPRL TREVAQLQAE 

        70         80         90        100        110        120 
NRDLHQRLCG LRLRLAEQRR TEAGRAAAHE PPTQNQEKDT KKKRLKQSEP GREVKQPNFI 

       130        140        150        160        170        180 
KERLQLFETL KTDHQLLPAT QEKKNTNNVI SVRVAGGKTV QGERWKTTPY QVAAGISKEL 

       190        200        210        220        230        240 
AEHTVIAKVN GVLWDLDRPL EGDSTVELLM FDNEEAQAVY WHSSAHILGE AMELYYGGHL 

       250        260        270        280        290        300 
CYGPPIENGF YYDMFIEDRV VSSTELSALE NICKTIIKEK QPFERLEVSK DTLLEMFKYN 

       310        320        330        340        350        360 
KFKCRILKEK VDTPTTTVYR CGPLIDLCKG PHVRHTGKIK AIKIFKNSST YWEGNPEMET 

       370        380        390        400        410        420 
LQRIYGISFP DSKMMKDWEK FQEEAKSRDH RKIGKEQELF FFHDLSPGSC FFLPRGAFIY 

       430        440        450        460        470        480 
NALMDFIREE YHKRNFTEVL SPNMYNSKLW ETSGHWQHYS NNMFTFDVEK DTFALKPMNC 

       490        500        510        520        530        540 
PGHCLMFAHR PRSWREMPVR FADFGVLHRN ELSGTLSGLT RVRRFQQDDA HIFCMVEQIE 

       550        560        570        580        590        600 
EEIKGCLHFL QSVYSTFGFS FQLNLSTRPE HFLGEIEIWD EAERQLQNSL VEFGKPWKIN 

       610        620        630        640        650        660 
PGDGAFYGPK IDIKIKDAIG RYHQCATIQL DFQLPIRFNL TYVSKDGDDK NRPVIIHRAI 

       670        680        690        700        710        720 
LGSVERMIAI LSENYGGKWP LWLSPRQVMV IPVGPACENY ALQVSKECFE EGFMADVDLD 

       730        740        750        760        770        780 
DSCTLNKKIR NAQLAQYNFI LVVGEKEKIN NAVNVRTRDN KIHGEISIAS VIEKLKNLKK 

       790 
SRTLNAEEDF

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
[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].
Strain: FVB/N.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK040927 mRNA. Translation: BAC30749.1.
BC039225 mRNA. Translation: AAH39225.1.
IPIIPI00229726.
RefSeqNP_758514.2. NM_172310.2.
UniGeneMm.35127.

3D structure databases

HSSPHSSP built from PDB template 1WWT based on UniProtKB P26639.
ProteinModelPortalQ8BLY2.
SMRQ8BLY2. Positions 149-789.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8BLY2.

PTM databases

PhosphoSiteQ8BLY2.

Proteomic databases

PRIDEQ8BLY2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032728; ENSMUSP00000032728; ENSMUSG00000030515.
GeneID272396.
KEGGmmu:272396.
NMPDRfig|10090.3.peg.16656.
UCSCuc009hgr.2. mouse.

Organism-specific databases

CTD123283.
MGIMGI:2444486. Tarsl2.

Phylogenomic databases

GeneTreeENSGT00390000002149.
HOGENOMHBG352811.
HOVERGENHBG059513.
InParanoidQ8BLY2.
OMAPRGAFLY.
OrthoDBEOG4DBTD5.
PhylomeDBQ8BLY2.

Gene expression databases

ArrayExpressQ8BLY2.
BgeeQ8BLY2.
GenevestigatorQ8BLY2.

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

NextBio393582.
SOURCESearch...

Entry information

Entry nameSYTC2_MOUSE
AccessionPrimary (citable) accession number: Q8BLY2
Secondary accession number(s): Q8CHT2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 1, 2003
Last modified: January 25, 2012
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

MGD cross-references

Mouse Genome Database (MGD) 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